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Conserved domains on  [gi|568919495|ref|XP_006500575|]
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stAR-related lipid transfer protein 9 isoform X5 [Mus musculus]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
3707-3911 1.13e-104

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd08874:

Pssm-ID: 472699  Cd Length: 205  Bit Score: 334.19  E-value: 1.13e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919495 3707 MADVMAACSDNLHNLFIRQATDGWNYQGEEQEVQLYYKEFSSTRHGFLGASVVSQPLSQVWAAVSDPTLWPLYHKPIQTA 3786
Cdd:cd08874     1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919495 3787 RLHQRVTNSISLVYLVCNTTLCELKQLRDFCCVCVEAKEGCLSIMAAQSVYDASMPRPSRKMVRGEILPSAWVLQPVIIE 3866
Cdd:cd08874    81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKEGELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILEPVTVE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568919495 3867 GKEITRVISLVQVELGAPGFPPHLLNSCIKQQPLVVAKLASFLRS 3911
Cdd:cd08874   161 GNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205
 
Name Accession Description Interval E-value
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
3707-3911 1.13e-104

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.


Pssm-ID: 176883  Cd Length: 205  Bit Score: 334.19  E-value: 1.13e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919495 3707 MADVMAACSDNLHNLFIRQATDGWNYQGEEQEVQLYYKEFSSTRHGFLGASVVSQPLSQVWAAVSDPTLWPLYHKPIQTA 3786
Cdd:cd08874     1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919495 3787 RLHQRVTNSISLVYLVCNTTLCELKQLRDFCCVCVEAKEGCLSIMAAQSVYDASMPRPSRKMVRGEILPSAWVLQPVIIE 3866
Cdd:cd08874    81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKEGELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILEPVTVE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568919495 3867 GKEITRVISLVQVELGAPGFPPHLLNSCIKQQPLVVAKLASFLRS 3911
Cdd:cd08874   161 GNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205
 
Name Accession Description Interval E-value
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
3707-3911 1.13e-104

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.


Pssm-ID: 176883  Cd Length: 205  Bit Score: 334.19  E-value: 1.13e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919495 3707 MADVMAACSDNLHNLFIRQATDGWNYQGEEQEVQLYYKEFSSTRHGFLGASVVSQPLSQVWAAVSDPTLWPLYHKPIQTA 3786
Cdd:cd08874     1 ESIVMAACSVNLSNLDQCQATAGWSYQCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919495 3787 RLHQRVTNSISLVYLVCNTTLCELKQLRDFCCVCVEAKEGCLSIMAAQSVYDASMPRPSRKMVRGEILPSAWVLQPVIIE 3866
Cdd:cd08874    81 RIHKTFTEDICLVYLVHETPLCLLKQPRDFCCLQVEAKEGELSVVACQSVYDKSMPEPGRSLVRGEILPSAWILEPVTVE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568919495 3867 GKEITRVISLVQVELGAPGFPPHLLNSCIKQQPLVVAKLASFLRS 3911
Cdd:cd08874   161 GNQYTRVIYIAQVALCGPDVPAQLLSSLSKRQPLVIARLALFLEA 205
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
3723-3909 5.79e-20

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 90.48  E-value: 5.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919495 3723 IRQATDGWNYQGEEQEVQLYYKEF-SSTRHGFLGASVVSQPLSQVWAAVSDPTLWPLYHKPIQTARLHQRVTNSISLVYL 3801
Cdd:cd00177    10 LLEEPEGWKLVKEKDGVKIYTKPYeDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHTDIIYY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919495 3802 VcnttlceLKQL-----RDFCCVCVEAKEGC-LSIMAAQSVYDASMPrPSRKMVRGEILPSAWVLQPViieGKEITRVIS 3875
Cdd:cd00177    90 K-------TKPPwpvspRDFVYLRRRRKLDDgTYVIVSKSVDHDSHP-KEKGYVRAEIKLSGWIIEPL---DPGKTKVTY 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 568919495 3876 LVQVELGApGFPPHLLNSCIKQQPLVVAKLASFL 3909
Cdd:cd00177   159 VLQVDPKG-SIPKSLVNSAAKKQLASFLKDLRKA 191
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
3712-3882 9.45e-04

Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4, -5, and -6. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7a-hydroxycholesterol. STARD4 and STARD5 are ubiquitously expressed, with highest levels in liver and kidney. STRAD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176876  Cd Length: 206  Bit Score: 43.60  E-value: 9.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919495 3712 AACSDNLHN--LFIRQATDGWNYQGEEQEVQLYYKEfSSTRHGFL--GASVVSQPLSQVWAAV-SDPTLWPL-YHKPIQT 3785
Cdd:cd08867     4 KVIAEKLANeaLQYINDTDGWKVLKTVKNITVSWKP-STEFTGHLyrAEGIVDALPEKVIDVIiPPCGGLRLkWDKSLKH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568919495 3786 ARLHQRVTNSISLVYLVCNTTLCELKQLRDFC-CVCVEAKEGCLSIMAAQSVyDASMPRPSRKMVRGEILPSAWVLQPVI 3864
Cdd:cd08867    83 YEVLEKISEDLCVGRTITPSAAMGLISPRDFVdLVYVKRYEDNQWSSSGKSV-DIPERPPTPGFVRGYNHPCGYFCSPLK 161
                         170
                  ....*....|....*...
gi 568919495 3865 IEGKEiTRVISLVQVELG 3882
Cdd:cd08867   162 GSPDK-SFLVLYVQTDLR 178
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
3814-3863 4.86e-03

Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176877  Cd Length: 208  Bit Score: 41.57  E-value: 4.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568919495 3814 RDFCCV-CVEAKEGCLsIMAAQSVYDASMPrPSRKMVRGEILPSAWVLQPV 3863
Cdd:cd08868   112 RDFVSLrHWGIRENCY-LSSGVSVEHPAMP-PTKNYVRGENGPGCWILRPL 160
 
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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