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Conserved domains on  [gi|17137362|ref|NP_477248|]
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transmembrane 4 superfamily, isoform A [Drosophila melanogaster]

Protein Classification

tetraspanin family protein( domain architecture ID 11992908)

tetraspanin family protein is a transmembrane (TM) glycoprotein with four TM segments that facilitates the interaction of membrane and intracellular signaling molecules (such as integrins, pro-growth factors and their receptors, protein kinase-C) in the formation of membrane signaling microdomains (also referred to as the tetraspanin web)

Gene Ontology:  GO:0016020
PubMed:  15763890|11756464|19709882|16024509|32974937
SCOP:  4001512

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tetraspanin pfam00335
Tetraspanin family;
10-224 1.07e-29

Tetraspanin family;


:

Pssm-ID: 459767  Cd Length: 183  Bit Score: 110.87  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137362    10 FKYLVYSYVVLLALTGAAQIFLGTSLLWGHSVYYGIVQNKLWAPAAILLCLGPVTFILCWMGCQATNQRKRCLLGMFAAL 89
Cdd:pfam00335   1 LKYLLFLFNLLFWLLGLLLLGVGVWLLSAFSLLLLGLSEASAYIPILLIVLGAVIFLVGFLGCCGALKENRCLLLTYFVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137362    90 LVACICVQFIICGWSLAMRENLPTSVEIFIDDSFVEFLDKFSRTKVDNLHLWNRMQSQLQCCGvdgpldyrrlslpwscc 169
Cdd:pfam00335  81 LLLLFLAELAAGILAFVYRDKLSGLLSNWLKKSLEDGYRDWLDLYSCLNSALDSLQSEFGCCG----------------- 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17137362   170 srpehayesacdthykrGCLAVVSEQIRNRLLITAFGAAIIAIFQSLGIFCAVHL 224
Cdd:pfam00335 144 -----------------GCKEKLLEWLRKNLKIIGAGVIALGVIQLLGIILACCL 181
 
Name Accession Description Interval E-value
Tetraspanin pfam00335
Tetraspanin family;
10-224 1.07e-29

Tetraspanin family;


Pssm-ID: 459767  Cd Length: 183  Bit Score: 110.87  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137362    10 FKYLVYSYVVLLALTGAAQIFLGTSLLWGHSVYYGIVQNKLWAPAAILLCLGPVTFILCWMGCQATNQRKRCLLGMFAAL 89
Cdd:pfam00335   1 LKYLLFLFNLLFWLLGLLLLGVGVWLLSAFSLLLLGLSEASAYIPILLIVLGAVIFLVGFLGCCGALKENRCLLLTYFVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137362    90 LVACICVQFIICGWSLAMRENLPTSVEIFIDDSFVEFLDKFSRTKVDNLHLWNRMQSQLQCCGvdgpldyrrlslpwscc 169
Cdd:pfam00335  81 LLLLFLAELAAGILAFVYRDKLSGLLSNWLKKSLEDGYRDWLDLYSCLNSALDSLQSEFGCCG----------------- 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17137362   170 srpehayesacdthykrGCLAVVSEQIRNRLLITAFGAAIIAIFQSLGIFCAVHL 224
Cdd:pfam00335 144 -----------------GCKEKLLEWLRKNLKIIGAGVIALGVIQLLGIILACCL 181
uroplakin_I_like_LEL cd03156
Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. ...
 111-197 4.41e-16

Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Uroplakin Ia and Ib are components of the 16nm protein particles, which are packed hexagonally to form 2D crystals of asymmetric unit membranes, and cover the apical surface of mammalian urothelium, contributing to the urinay bladder's permeability barrier function. Uroplakins Ia and Ib are maturation facilitators. They trigger conformational changes in their single-transmembrane-domain binding partner proteins uroplakin II and IIIa, which in turn may lead to ER-exit, stabilization, and cell-surface expression.


Pssm-ID: 239409  Cd Length: 114  Bit Score: 72.57  E-value: 4.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137362 111 LPTSVEIFIDDSFVEFLDKFSRTK----VDNLHLWNRMQSQLQCCGVDGPLDYR------------RLSLPWSCCSRPEH 174
Cdd:cd03156   1 LALFFKKDLEDSFKNLLKNNYGNYnstgDAITSTWNRVMIELKCCGVNGPTDFVdstsffrqknepNSPYPESCCKRNSN 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 17137362 175 AYES--------ACDTHYKRGCLAVVSEQIR 197
Cdd:cd03156  81 SQIVdldcpklgSPNSYNKKGCYEKLSNPIE 111
 
Name Accession Description Interval E-value
Tetraspanin pfam00335
Tetraspanin family;
10-224 1.07e-29

Tetraspanin family;


Pssm-ID: 459767  Cd Length: 183  Bit Score: 110.87  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137362    10 FKYLVYSYVVLLALTGAAQIFLGTSLLWGHSVYYGIVQNKLWAPAAILLCLGPVTFILCWMGCQATNQRKRCLLGMFAAL 89
Cdd:pfam00335   1 LKYLLFLFNLLFWLLGLLLLGVGVWLLSAFSLLLLGLSEASAYIPILLIVLGAVIFLVGFLGCCGALKENRCLLLTYFVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137362    90 LVACICVQFIICGWSLAMRENLPTSVEIFIDDSFVEFLDKFSRTKVDNLHLWNRMQSQLQCCGvdgpldyrrlslpwscc 169
Cdd:pfam00335  81 LLLLFLAELAAGILAFVYRDKLSGLLSNWLKKSLEDGYRDWLDLYSCLNSALDSLQSEFGCCG----------------- 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17137362   170 srpehayesacdthykrGCLAVVSEQIRNRLLITAFGAAIIAIFQSLGIFCAVHL 224
Cdd:pfam00335 144 -----------------GCKEKLLEWLRKNLKIIGAGVIALGVIQLLGIILACCL 181
uroplakin_I_like_LEL cd03156
Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. ...
 111-197 4.41e-16

Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Uroplakin Ia and Ib are components of the 16nm protein particles, which are packed hexagonally to form 2D crystals of asymmetric unit membranes, and cover the apical surface of mammalian urothelium, contributing to the urinay bladder's permeability barrier function. Uroplakins Ia and Ib are maturation facilitators. They trigger conformational changes in their single-transmembrane-domain binding partner proteins uroplakin II and IIIa, which in turn may lead to ER-exit, stabilization, and cell-surface expression.


Pssm-ID: 239409  Cd Length: 114  Bit Score: 72.57  E-value: 4.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137362 111 LPTSVEIFIDDSFVEFLDKFSRTK----VDNLHLWNRMQSQLQCCGVDGPLDYR------------RLSLPWSCCSRPEH 174
Cdd:cd03156   1 LALFFKKDLEDSFKNLLKNNYGNYnstgDAITSTWNRVMIELKCCGVNGPTDFVdstsffrqknepNSPYPESCCKRNSN 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 17137362 175 AYES--------ACDTHYKRGCLAVVSEQIR 197
Cdd:cd03156  81 SQIVdldcpklgSPNSYNKKGCYEKLSNPIE 111
tetraspanin_LEL cd03127
Tetraspanin, extracellular domain or large extracellular loop (LEL). Tetraspanins are ...
 105-197 1.13e-13

Tetraspanin, extracellular domain or large extracellular loop (LEL). Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. The tetraspanin family contains CD9, CD63, CD37, CD53, CD82, CD151, and CD81, amongst others. Tetraspanins are involved in diverse processes such as cell activation and proliferation, adhesion and motility, differentiation, cancer, and others. Their various functions may relate to their ability to act as molecular facilitators, grouping specific cell-surface proteins and affecting formation and stability of signaling complexes. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web", which may also include integrins.


Pssm-ID: 239401 [Multi-domain]  Cd Length: 90  Bit Score: 65.22  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137362 105 LAMRENLPTSVEIFIDDSFVEFLDKFSRTKvdnlhLWNRMQSQLQCCGVDGPLDY--RRLSLPWSCCSRPEhayESACDT 182
Cdd:cd03127   1 FVYRDQLESLVSDTLNDAWDEYYVDDDFQE-----AMDALQSTFECCGVNGPTDYldLRLLVPSSCCKGTD---GNCGLN 72

                        90
                ....*....|....*
gi 17137362 183 HYKRGCLAVVSEQIR 197
Cdd:cd03127  73 LYTEGCLEKLVDFLR 87
CD53_like_LEL cd03164
Tetraspanin, extracellular domain or large extracellular loop (LEL), CD53_Like family. ...
 141-203 6.77e-06

Tetraspanin, extracellular domain or large extracellular loop (LEL), CD53_Like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD53 is a tetraspanin of the lymphoid-myeloid lineage and has been implicated in apoptosis protection. It associates with integrin alpha4beta1. Some of the cellular responses modulated by CD53 may be mediated by JNK activation and/or via the AKT pathway.


Pssm-ID: 239417 [Multi-domain]  Cd Length: 86  Bit Score: 43.62  E-value: 6.77e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17137362 141 WNRMQSQLQCCGVDGPLDYRRLsLPWSCCSrpehayeSACDtHYKRGCLAVVSEQIRNRLLIT 203
Cdd:cd03164  32 WDMIQSNLQCCGINGTTDWGSG-VPSSCCS-------SDTE-YKVEGCYKKLKNWFESNFLYT 85
NET-5_like_LEL cd03165
Tetraspanin, extracellular domain or large extracellular loop (LEL), NET-5_like family. ...
 141-200 3.54e-05

Tetraspanin, extracellular domain or large extracellular loop (LEL), NET-5_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This sub-family contains proteins similar to human tetraspan NET-5.


Pssm-ID: 239418 [Multi-domain]  Cd Length: 98  Bit Score: 41.97  E-value: 3.54e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17137362 141 WNRMQSQLQCCGVDGPLDYRRL----SLPWSCCSRpehaYESAC-----DTHYKRGCLAVVSEQIRNRL 200
Cdd:cd03165  34 WDITQTEFRCCGVTNYTDWYEVlgenRVPDSCCQE----DSQDCgrnptELWWKTGCYEKVQQWLVDNL 98
CD151_like_LEL cd03155
Tetraspanin, extracellular domain or large extracellular loop (LEL), CD151_Like family. ...
 140-200 1.62e-03

Tetraspanin, extracellular domain or large extracellular loop (LEL), CD151_Like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD151strongly associates with integrins, especially alpha3beta1, alpha6beta1, alpha7beta1, and alpha6beta4; it may play roles in cell-cell adhesion, cell migration, platelet aggregation, and angiogenesis. For example, CD151 is is involved in regulation of migration of neutrophils, endothelial cells, and various tumor cell lines; it associates specifically with laminin-binding integrins and strengthens alpha6beta1 integrin-mediated adhesion to laminin-1; CD151 also specifically attenuates adhesion-dependent activation of Ras and correspdonding downstream effects, and is involved in epithelial cell-cell adhesion as a modulator of PKC- and Cdc42-dependent actin cytoskeletal reorganization.


Pssm-ID: 239408 [Multi-domain]  Cd Length: 110  Bit Score: 37.33  E-value: 1.62e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17137362 140 LWNRMQSQLQCCGVDGPLDYR-----------RLSLPWSCCsRPEHAYESACDTH----YK--RGCLAVVSEQIRNRL 200
Cdd:cd03155  34 TVDELQQEFKCCGSNNYTDWQdsewinsneanGRLVPDSCC-KTVVDRCGCLRDHpsniYKveGGCIPKLEDFLYDHL 110
TM4SF9_like_LEL cd03159
Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF9_like subfamily. ...
 119-171 5.90e-03

Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF9_like subfamily. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contaions transmembrane 4 superfamily 9 (TM4SF9) or Tetraspanin-5 and related proteins. TM4SF9 is strongly expressed witin the central nervous system, and expression levels appear to correlate with differentiation status of particular neurons, hinting at a role in neuronal maturation.


Pssm-ID: 239412 [Multi-domain]  Cd Length: 121  Bit Score: 35.86  E-value: 5.90e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137362 119 IDDSFVEFLDKFSRTKVDNLHLWNRM---QSQLQCCGVDGPLDY---------------RRLSLPWSCCSR 171
Cdd:cd03159   7 IKDQLTEFLNNNIRAYRDDIDLQNLIdflQEYWQCCGARGPDDWnlniyfnctdsnpsrERCGVPFSCCVK 77
CD37_CD82_like_LEL cd03160
Tetraspanin, extracellular domain or large extracellular loop (LEL), CD37_CD82_Like family. ...
 141-169 8.54e-03

Tetraspanin, extracellular domain or large extracellular loop (LEL), CD37_CD82_Like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD37 is a leukocyte-specific protein, and its restricted expression pattern suggests a role in the immune system. A regulatory role in T-cell proliferation has been suggested. CD82 is a metastasis suppressor implicated in biological processes ranging from fusion, adhesion, and migration to apoptosis and alterations of cell morphology.


Pssm-ID: 239413  Cd Length: 117  Bit Score: 35.44  E-value: 8.54e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 17137362 141 WNRMQSQLQCCGVDGPLDYRRLSL---------PWSCC 169
Cdd:cd03160  36 WDYVQFQLQCCGWTGPQDWTDNSLiknsseplyPCSCC 73
 
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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