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Conserved domains on  [gi|15228268|ref|NP_190370|]
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chloroplastic lipocalin [Arabidopsis thaliana]

Protein Classification

lipocalin/fatty acid-binding family protein( domain architecture ID 3669)

lipocalin/fatty acid-binding family protein contains a large beta-barrel cavity that binds hydrophobic ligands

CATH:  2.40.128.20
Gene Ontology:  GO:0036094
PubMed:  11058745|11058743
SCOP:  3001332

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
lipocalin_FABP super family cl10502
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
126-266 3.14e-88

lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They have a large beta-barrel ligand-binding cavity. Members include retinol-binding protein, retinoic acid-binding protein, complement protein C8 gamma, Can f 2, apolipoprotein D, extracellular fatty acid-binding protein, beta-lactoglobulin, oderant-binding protein, and bacterial lipocalin Blc. Lipocalins are involved in many important processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty acid-binding proteins also bind hydrophobic ligands in a non-covalent, reversible manner, and are involved in protection and shuttling of fatty acids within the cell, and in acquisition and removal of fatty acids from intracellular sites.


The actual alignment was detected with superfamily member cd19851:

Pssm-ID: 471979  Cd Length: 141  Bit Score: 261.59  E-value: 3.14e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 126 MRGMTAKNFDPVRYSGRWFEVASLKRGFAGQGQEDCHCTQGVYTFDMKESAIRVDTFCVHGSPDGYITGIRGKVQCVGAE 205
Cdd:cd19851   1 MRGMTAKNFDPVRYSGRWFEVASLKRGFAGQGQEDCHCTQGVYTFDMKESAIRVDTFCVHGSPDGYITGIRGKVQCVGAE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228268 206 DLEKSETDLEKQEMIKEKCFLRFPTIPFIPKLPYDVIATDYDNYALVSGAKDKGFVQVYSR 266
Cdd:cd19851  81 DLEKSETDLEKQEMIKEKCFLRFPTIPFIPKLPYDVIATDYDNYALVSGAKDKGFVQVYSR 141
 
Name Accession Description Interval E-value
lipocalin_CHL cd19851
chloroplastic lipocalin(CHL) similar to Arabidopsis CHL; Chloroplastic lipocalin (CHL) ...
126-266 3.14e-88

chloroplastic lipocalin(CHL) similar to Arabidopsis CHL; Chloroplastic lipocalin (CHL) prevents thylakoidal membrane lipids peroxidation and is protective against oxidative stress, especially mediated by singlet oxygen in response to excess light and other stress (e.g. heat shocks). CHL is required for seed longevity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381251  Cd Length: 141  Bit Score: 261.59  E-value: 3.14e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 126 MRGMTAKNFDPVRYSGRWFEVASLKRGFAGQGQEDCHCTQGVYTFDMKESAIRVDTFCVHGSPDGYITGIRGKVQCVGAE 205
Cdd:cd19851   1 MRGMTAKNFDPVRYSGRWFEVASLKRGFAGQGQEDCHCTQGVYTFDMKESAIRVDTFCVHGSPDGYITGIRGKVQCVGAE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228268 206 DLEKSETDLEKQEMIKEKCFLRFPTIPFIPKLPYDVIATDYDNYALVSGAKDKGFVQVYSR 266
Cdd:cd19851  81 DLEKSETDLEKQEMIKEKCFLRFPTIPFIPKLPYDVIATDYDNYALVSGAKDKGFVQVYSR 141
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
130-300 3.53e-13

Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442274  Cd Length: 178  Bit Score: 66.80  E-value: 3.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 130 TAKNFDPVRYSGRWFEVASLKRGFagqgQEDCHCTQGVYTFDmKESAIRVDTFCVHGsPDGYITGIRGKVQCVGAED--- 206
Cdd:COG3040  29 PVPPVDLDRYLGTWYEIARLPHRF----ERGCVNVTAEYSLR-EDGTIKVINRGRKG-FDGEWKEAEGKARVVDDPTnak 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 207 LEKSetdlekqemikekcFlrFPtiPFipKLPYDVIATDYD-NYALVSGaKDKGFVQVYSRTPNPGPEFIAKYKNYLAQF 285
Cdd:COG3040 103 LKVS--------------F--FG--PF--YGDYWILALDPDyQYALVGG-PDRDYLWILSRTPTLPDAVYQELLARARAL 161
                       170
                ....*....|....*
gi 15228268 286 GYDPEKIKDTPQDCE 300
Cdd:COG3040 162 GYDTSKLIRVPQTPP 176
Lipocalin_2 pfam08212
Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as ...
138-297 2.44e-10

Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The structure is an eight-stranded beta barrel.


Pssm-ID: 400495  Cd Length: 143  Bit Score: 58.11  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268   138 RYSGRWFEVASLKRGFagqgQEDCHCTQGVYTFdMKESAIRVDTFCvhGSPDGYITGIRGKVQCVGaedlEKSETDLEkq 217
Cdd:pfam08212   5 RYMGTWYEIARLPMRF----QRGCVDVTATYTL-RDDGTIAVTNRC--RTFDGKLKTAEGVAKVAD----PGSNAKLK-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268   218 emikekcfLRFPTIPFIPKLPYDVIATDYD-NYALVsGAKDKGFVQVYSRTPNPGPEFIAKYKNYLAQFGYDPEKIKDTP 296
Cdd:pfam08212  72 --------VSFLGWFFPVKGDYWVLYIDPDySWAIV-GSPSRKYLWILSRTPQLSDAQYEQLLEKARDQGYDTSKLIRVP 142

                  .
gi 15228268   297 Q 297
Cdd:pfam08212 143 Q 143
 
Name Accession Description Interval E-value
lipocalin_CHL cd19851
chloroplastic lipocalin(CHL) similar to Arabidopsis CHL; Chloroplastic lipocalin (CHL) ...
126-266 3.14e-88

chloroplastic lipocalin(CHL) similar to Arabidopsis CHL; Chloroplastic lipocalin (CHL) prevents thylakoidal membrane lipids peroxidation and is protective against oxidative stress, especially mediated by singlet oxygen in response to excess light and other stress (e.g. heat shocks). CHL is required for seed longevity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381251  Cd Length: 141  Bit Score: 261.59  E-value: 3.14e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 126 MRGMTAKNFDPVRYSGRWFEVASLKRGFAGQGQEDCHCTQGVYTFDMKESAIRVDTFCVHGSPDGYITGIRGKVQCVGAE 205
Cdd:cd19851   1 MRGMTAKNFDPVRYSGRWFEVASLKRGFAGQGQEDCHCTQGVYTFDMKESAIRVDTFCVHGSPDGYITGIRGKVQCVGAE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228268 206 DLEKSETDLEKQEMIKEKCFLRFPTIPFIPKLPYDVIATDYDNYALVSGAKDKGFVQVYSR 266
Cdd:cd19851  81 DLEKSETDLEKQEMIKEKCFLRFPTIPFIPKLPYDVIATDYDNYALVSGAKDKGFVQVYSR 141
lipocalin_apoD-like cd19437
apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein ...
133-297 1.58e-19

apolipoprotein D and similar proteins; Human apolipoprotein D (ApoD) is a small glycoprotein associated with high density lipoproteins (HDL) in plasma. It appears promiscuous since it can bind hydrophobic ligands belonging to different lipid groups, with different shapes and biochemical properties; however, it exhibits specificity between very similar lipidic species. Some ligands, such as progesterone and arachidonic acid, bind to the ligand-binding pocket with high affinity, while others may interact with ApoD via its region of surface hydrophobicity. This hydrophobic surface cluster may facilitate its association with HDL particles and facilitate its insertion into cellular lipid membranes. Drosophila NLaz and Schistocerca Laz belong to this group, and share functional properties with human ApoD, including regulation of lifespan, lipid and carbohydrate metabolism control, and protection against oxidative stress or starvation. This group also includes Sandercyanin, a blue protein secreted in the skin mucus of blue forms of walleye, Sander vitreus. Walleye is an important golden yellow commercial and sport fish; the findings of blue walleye are recent. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381212 [Multi-domain]  Cd Length: 160  Bit Score: 84.22  E-value: 1.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 133 NFDPVRYSGRWFEVASLKRGFagqgQEDCHCTQGVYTFDmKESAIRVDTFCVHgSPDGYITGIRGKVQCVGAEDlekset 212
Cdd:cd19437  12 DFDVDKYLGRWYEIERYPAPF----EKGGDCVTANYSLN-DDGTVRVVNSGIN-LTDGSINTIEGSARCPDPNE------ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 213 dlekqemiKEKCFLRFPtiPFIPKLPYDVIATDYDNYALVSGAKDKG------FVQVYSRTPNPGPEFIAKYKNYLAQFG 286
Cdd:cd19437  80 --------PAKLGVSFP--GFPPAGPYWVLDTDYDNYAIVYSCTDVLglfkveYAWILSRQRTLSAETLTKAKEILTSYG 149
                       170
                ....*....|.
gi 15228268 287 YDPEKIKDTPQ 297
Cdd:cd19437 150 IDVSKLKKTDQ 160
lipocalin_Blc-like cd19438
bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar ...
131-292 2.09e-15

bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar proteins; Escherichia coli bacterial lipocalin (Blc, also known as YjeL) is an outer membrane lipoprotein involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Blc has a binding preference for lysophospholipids. This group includes eukaryotic lipocalins such as Arabidopsis thaliana temperature-induced lipocalin-1 (TIL) which is involved in thermotolerance, oxidative, salt, drought and high light stress tolerance, and is needed for seed longevity by ensuring polyunsaturated lipids integrity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381213  Cd Length: 143  Bit Score: 72.21  E-value: 2.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 131 AKNFDPVRYSGRWFEVASLKRGFagqgQEDCHCTQGVYTFDmKESAIRVDTFCVHGSpDGYITGIRGKVQCVGAEDLEKs 210
Cdd:cd19438   1 VPNVDLDRYMGTWYEIARLPNRF----EKGCVNVTATYTLN-DDGTISVVNRCRDGD-EGKWKEAEGKARVVDPSDNAK- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 211 etdLEkqemikekcfLRFPTIPFIPklPYDVIATDYD-NYALVSGAkDKGFVQVYSRTPNPGPEFIAKYKNYLAQFGYDP 289
Cdd:cd19438  74 ---LK----------VSFFGPPFYG--DYWVLALDPDyQWALVGGP-SRDYLWILSRTPQLSEETLQRLLEKARELGYDT 137

                ...
gi 15228268 290 EKI 292
Cdd:cd19438 138 DKL 140
Blc COG3040
Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];
130-300 3.53e-13

Bacterial lipocalin Blc [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442274  Cd Length: 178  Bit Score: 66.80  E-value: 3.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 130 TAKNFDPVRYSGRWFEVASLKRGFagqgQEDCHCTQGVYTFDmKESAIRVDTFCVHGsPDGYITGIRGKVQCVGAED--- 206
Cdd:COG3040  29 PVPPVDLDRYLGTWYEIARLPHRF----ERGCVNVTAEYSLR-EDGTIKVINRGRKG-FDGEWKEAEGKARVVDDPTnak 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 207 LEKSetdlekqemikekcFlrFPtiPFipKLPYDVIATDYD-NYALVSGaKDKGFVQVYSRTPNPGPEFIAKYKNYLAQF 285
Cdd:COG3040 103 LKVS--------------F--FG--PF--YGDYWILALDPDyQYALVGG-PDRDYLWILSRTPTLPDAVYQELLARARAL 161
                       170
                ....*....|....*
gi 15228268 286 GYDPEKIKDTPQDCE 300
Cdd:COG3040 162 GYDTSKLIRVPQTPP 176
lipocalin_FABP cd00301
lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low ...
138-266 8.12e-13

lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They have a large beta-barrel ligand-binding cavity. Members include retinol-binding protein, retinoic acid-binding protein, complement protein C8 gamma, Can f 2, apolipoprotein D, extracellular fatty acid-binding protein, beta-lactoglobulin, oderant-binding protein, and bacterial lipocalin Blc. Lipocalins are involved in many important processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty acid-binding proteins also bind hydrophobic ligands in a non-covalent, reversible manner, and are involved in protection and shuttling of fatty acids within the cell, and in acquisition and removal of fatty acids from intracellular sites.


Pssm-ID: 381182  Cd Length: 109  Bit Score: 64.10  E-value: 8.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 138 RYSGRWFEVASLKRGFAGQgqeDCHCTQGVYTFDmKESAIRVDTFCVHgspDGYITGIRGKVQCVGaedleksetdlekq 217
Cdd:cd00301   1 KFSGKWYEVASASNAPEED---EGKCTTAEYTLE-GNGNLKVTNSFVR---DGVCKSITGTLKKTD-------------- 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15228268 218 emIKEKCFLRFPTIPFipKLPYDVIATDYDNYALVSGAKDKG-----FVQVYSR 266
Cdd:cd00301  60 --GPGKFTVTYPGYTG--KNELYVLSTDYDNYAIVYSCKNLDgghtvVAWLLSR 109
Lipocalin_2 pfam08212
Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as ...
138-297 2.44e-10

Lipocalin-like domain; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The structure is an eight-stranded beta barrel.


Pssm-ID: 400495  Cd Length: 143  Bit Score: 58.11  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268   138 RYSGRWFEVASLKRGFagqgQEDCHCTQGVYTFdMKESAIRVDTFCvhGSPDGYITGIRGKVQCVGaedlEKSETDLEkq 217
Cdd:pfam08212   5 RYMGTWYEIARLPMRF----QRGCVDVTATYTL-RDDGTIAVTNRC--RTFDGKLKTAEGVAKVAD----PGSNAKLK-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268   218 emikekcfLRFPTIPFIPKLPYDVIATDYD-NYALVsGAKDKGFVQVYSRTPNPGPEFIAKYKNYLAQFGYDPEKIKDTP 296
Cdd:pfam08212  72 --------VSFLGWFFPVKGDYWVLYIDPDySWAIV-GSPSRKYLWILSRTPQLSDAQYEQLLEKARDQGYDTSKLIRVP 142

                  .
gi 15228268   297 Q 297
Cdd:pfam08212 143 Q 143
Lipocalin pfam00061
Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small ...
140-297 8.24e-09

Lipocalin / cytosolic fatty-acid binding protein family; Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2). Alignment subsumes both the lipocalin and fatty acid binding protein signatures from PROSITE. This is supported on structural and functional grounds. The structure is an eight-stranded beta barrel.


Pssm-ID: 395015  Cd Length: 143  Bit Score: 53.60  E-value: 8.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268   140 SGRWFEVASLKRGFagqgqedchctqgvytFDMKESAIRVDTFcvhgspdgyitgirgKVQCVGAEDLEKSETDLEKQEM 219
Cdd:pfam00061   1 SGKWYLIASANFNE----------------LEEEMKALGVGFA---------------TIKVLENGNLPVTEITKEGGKC 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268   220 IKEKCFLRFPTIPFIPKLPYD---------VIATDYDNYALV-----SGAKDKGFVQVYSRTPNPGPEFIAKYKNYLAQF 285
Cdd:pfam00061  50 KTVSVTFKKTEEPGKLGVEFDeyaggrkvkVLTTDYDNYLIFyqkgdKDGKTTIVRELYGRDPELSPELLEKFKKFLKEL 129
                         170
                  ....*....|..
gi 15228268   286 GYDPEKIKDTPQ 297
Cdd:pfam00061 130 GIDEENIVRLYQ 141
lipocalin_crustacyanin cd19436
crustacyanin Type I CRTC and Type II CRTA subunits; Alpha crustacyanin bound with the ...
132-299 1.66e-05

crustacyanin Type I CRTC and Type II CRTA subunits; Alpha crustacyanin bound with the carotenoid astaxanthisn (AXT) is the predominant cartenoprotein generating the slate-grey/blue color of the lobster carapace. Crustacyanin forms heterodimers (beta-crustacyanin) or complexes of 16 subunits (alpha-crustacyanin) assembled from beta-crustacyanin. Beta-crustacyanin is formed from one type I CRTC lipocalin subunit, and one type II CRTA lipocalin subunit (and two bound astaxanthin molecules). Homarus gammarus (European lobster) crustacyanin has of five distinct subunits evident on 6 M urea-PAGE gels: type I CRTC ( A1, C1, C2) and type II CRTA ( A2, A3). Homarus americanus crustacyanin consists of only two major subunits, namely type I CRTC (H1) and type II CRTA (H2), both of which behave like Ax subunits on a 6 M urea-PAGE gel. This family includes both type I CRTC subunit and type II CRTA subunits and belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381211  Cd Length: 169  Bit Score: 44.77  E-value: 1.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 132 KNFDPVRYSGRWFEVASLKRGFagqgQEDCHCTQGVYTFDMKESAIRVDTFCVhgSPDGYITGIRGKVqcvgaedlekse 211
Cdd:cd19436  17 DNFDLRRYAGRWYQTHLINNPY----QPVTRCVHSNYSYSGSDYGFKVTSAGF--NPDNNYLKRNGKV------------ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 212 tdLEKQEMIKEKCFLRFPTIpFIPklPYDVIATDYDNYALVSGAKDKG-----FVQVYSRTPNPGPEFIAKYKNYLAQFG 286
Cdd:cd19436  79 --YPTKEFPAAHMLIDYPSV-FAA--PYEVIETDYENYSCVYSCIDTDgykseFGFVFSRSPQLAGPAVEKCAAVFKKNG 153
                       170
                ....*....|....*
gi 15228268 287 YDPEKIKDTPQ--DC 299
Cdd:cd19436 154 VDFSRFVPVVHtsDC 168
lipocalin_L-PGDS cd19419
lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5. ...
132-297 3.43e-05

lipocalin-type prostaglandin D synthase; Lipocalin-type prostaglandin D synthase (L-PGDS; EC:5.3.99.2) is a secreted enzyme and the second most abundant protein in human cerebrospinal fluid. L-PGDS acts as both, an enzyme and as a lipid transporter, converting prostaglandin H2 to prostaglandin D2 and serving as a carrier for hydrophobic ligands including retinoids, hemoglobin metabolites, thyroid hormones, gangliosides, and fatty acids. L-PGDS belongs to the lipocalin/cytosolic fatty-acid binding protein family which has a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381194  Cd Length: 158  Bit Score: 43.50  E-value: 3.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 132 KNFDPVRYSGRWFEVaslkrGFAGQGQedchctqgvyTFDMKESAIRVDTFCVHGSPDGyitgirgkvqcvgaeDLEKSE 211
Cdd:cd19419   3 PDFDLDKFAGRWYSV-----GLASNSN----------WFVEKKAKLKMCTTVVAPTTDG---------------NLNLTM 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 212 TDL-----EKQEMIKEKCFL--RFPTipFIPKLPYD----VIATDYDNYALVSGAKDKG---FVQV--YSRTPNPGPEFI 275
Cdd:cd19419  53 TFLkkngcETRTYLYEKTEQpgRFTY--KSPRWGSDhdvrVVETNYDEYALVHTIKTKGneeFTMVtlYSRTQTLRPELK 130
                       170       180
                ....*....|....*....|..
gi 15228268 276 AKYKNYLAQFGYDPEKIKDTPQ 297
Cdd:cd19419 131 EKFRQFAKAQGFTEENIVTLPQ 152
lipocalin_15-like cd19422
lipocalin 15 and similar proteins, such as chicken CALbeta; This subfamily includes ...
230-286 1.43e-03

lipocalin 15 and similar proteins, such as chicken CALbeta; This subfamily includes uncharacterized human lipocalin 15, and chicken chondrogenesis-associated lipocalin (CAL) beta which is associated with chondrogenesis and inflammation. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381197  Cd Length: 143  Bit Score: 38.69  E-value: 1.43e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228268 230 TIPFIPKLPYDVIATDYDNYALVSGAKDKG-----FVQVYSRTPNPGPEFIAKYKNYLAQFG 286
Cdd:cd19422  69 RVPELGKRDLRVMDTDYSSYAILYIYKELEgesstMVQLYTRNQDVSPQLLQKFKELYPTLG 130
lipocalin_LTBP1-like cd19423
Triatominae salivary lipocalins such as Rhodnius prolixus LTBP1 and Meccus pallidipennis ...
130-252 8.09e-03

Triatominae salivary lipocalins such as Rhodnius prolixus LTBP1 and Meccus pallidipennis triabin, and similar proteins; This subfamily includes various insect proteins found in the saliva of Triatominae (kissing bugs), including Rhodnius prolixus leukotriene-binding LTBP1. Rhodnius prolixus, a vector of the pathogen Trypanosoma cruzi, sequesters cysteinyl leukotrienes during feeding to inhibit immediate inflammatory responses; LTBP1 binds leukotrienes C4 (LTC4), D4 (LTD4), and E4 (LTE4). Meccus pallidipennis (syn Triatoma pallidipennis) triabin is a potent and selective thrombin inhibitor. It also includes Triatoma protracta procalin, a major salivary allergen which causes an allergic reaction in humans. It belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.


Pssm-ID: 381198  Cd Length: 132  Bit Score: 36.18  E-value: 8.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228268 130 TAKNFDPVRY-SGRWFEVASLKrgfaGQGQEDCHctqgVYTFDMKESAIRVDTfcvhgSPDGYITGIRGKVQCVGAEDLE 208
Cdd:cd19423   8 PMSNFDSTKFfSGTWYVTHAKN----GTNSTVCR----KYKTSKNDGKITINY-----GGYYGGKGKNYEVRCSGTKKSK 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15228268 209 KSETDLekqemikeKCFLRFPTIPFIP-KLPYDVIATDYDNYALV 252
Cdd:cd19423  75 KGQFSF--------DCKQKNDRKENTNfQVEFSVIDTDYDNYALV 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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