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Conserved domains on  [gi|5902148|ref|NP_008931|]
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uroplakin-1a isoform 1 [Homo sapiens]

Protein Classification

tetraspanin family protein( domain architecture ID 13626501)

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:0005886
PubMed:  15763890|11756464|19709882|16024509
SCOP:  4001512

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
uroplakin_I_like_LEL cd03156
Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. ...
 112-230 1.62e-37

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: 128.03  E-value: 1.62e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148  112 ITSYTHRDYMVSNPSLITKQMLTFYSAdtdqGQELTRLWDRVMIEQECCGTSGPMDWVNFTSAFRaATPEVVFPWPPLCC 191
Cdd:cd03156   1 LALFFKKDLEDSFKNLLKNNYGNYNST----GDAITSTWNRVMIELKCCGVNGPTDFVDSTSFFR-QKNEPNSPYPESCC 75

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 5902148  192 RRTGNFIPLNEEGCRLGHMDYLFTKGCFEHIGHAIDSYT 230
Cdd:cd03156  76 KRNSNSQIVDLDCPKLGSPNSYNKKGCYEKLSNPIERYA 114
Tetraspanin pfam00335
Tetraspanin family;
24-162 6.55e-12

Tetraspanin family;


:

Pssm-ID: 459767  Cd Length: 183  Bit Score: 62.34  E-value: 6.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148     24 NIIILLSGLSLFAETIWVTADQYRVYplmgVSGKDDVFAGAWIAIFCGFSFFMVASFGVGAALCRRRSMVLTYLVLMLIV 103
Cdd:pfam00335   9 NLLFWLLGLLLLGVGVWLLSAFSLLL----LGLSEASAYIPILLIVLGAVIFLVGFLGCCGALKENRCLLLTYFVLLLLL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148    104 YIFECASCITSYTHRDYMVSN-PSLITKQMLTFYSADTDQGQELTRLWDRVMIEQECCGT 162
Cdd:pfam00335  85 FLAELAAGILAFVYRDKLSGLlSNWLKKSLEDGYRDWLDLYSCLNSALDSLQSEFGCCGG 144
 
Name Accession Description Interval E-value
uroplakin_I_like_LEL cd03156
Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. ...
 112-230 1.62e-37

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: 128.03  E-value: 1.62e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148  112 ITSYTHRDYMVSNPSLITKQMLTFYSAdtdqGQELTRLWDRVMIEQECCGTSGPMDWVNFTSAFRaATPEVVFPWPPLCC 191
Cdd:cd03156   1 LALFFKKDLEDSFKNLLKNNYGNYNST----GDAITSTWNRVMIELKCCGVNGPTDFVDSTSFFR-QKNEPNSPYPESCC 75

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 5902148  192 RRTGNFIPLNEEGCRLGHMDYLFTKGCFEHIGHAIDSYT 230
Cdd:cd03156  76 KRNSNSQIVDLDCPKLGSPNSYNKKGCYEKLSNPIERYA 114
Tetraspanin pfam00335
Tetraspanin family;
24-162 6.55e-12

Tetraspanin family;


Pssm-ID: 459767  Cd Length: 183  Bit Score: 62.34  E-value: 6.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148     24 NIIILLSGLSLFAETIWVTADQYRVYplmgVSGKDDVFAGAWIAIFCGFSFFMVASFGVGAALCRRRSMVLTYLVLMLIV 103
Cdd:pfam00335   9 NLLFWLLGLLLLGVGVWLLSAFSLLL----LGLSEASAYIPILLIVLGAVIFLVGFLGCCGALKENRCLLLTYFVLLLLL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148    104 YIFECASCITSYTHRDYMVSN-PSLITKQMLTFYSADTDQGQELTRLWDRVMIEQECCGT 162
Cdd:pfam00335  85 FLAELAAGILAFVYRDKLSGLlSNWLKKSLEDGYRDWLDLYSCLNSALDSLQSEFGCCGG 144
 
Name Accession Description Interval E-value
uroplakin_I_like_LEL cd03156
Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. ...
 112-230 1.62e-37

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: 128.03  E-value: 1.62e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148  112 ITSYTHRDYMVSNPSLITKQMLTFYSAdtdqGQELTRLWDRVMIEQECCGTSGPMDWVNFTSAFRaATPEVVFPWPPLCC 191
Cdd:cd03156   1 LALFFKKDLEDSFKNLLKNNYGNYNST----GDAITSTWNRVMIELKCCGVNGPTDFVDSTSFFR-QKNEPNSPYPESCC 75

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 5902148  192 RRTGNFIPLNEEGCRLGHMDYLFTKGCFEHIGHAIDSYT 230
Cdd:cd03156  76 KRNSNSQIVDLDCPKLGSPNSYNKKGCYEKLSNPIERYA 114
Tetraspanin pfam00335
Tetraspanin family;
24-162 6.55e-12

Tetraspanin family;


Pssm-ID: 459767  Cd Length: 183  Bit Score: 62.34  E-value: 6.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148     24 NIIILLSGLSLFAETIWVTADQYRVYplmgVSGKDDVFAGAWIAIFCGFSFFMVASFGVGAALCRRRSMVLTYLVLMLIV 103
Cdd:pfam00335   9 NLLFWLLGLLLLGVGVWLLSAFSLLL----LGLSEASAYIPILLIVLGAVIFLVGFLGCCGALKENRCLLLTYFVLLLLL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148    104 YIFECASCITSYTHRDYMVSN-PSLITKQMLTFYSADTDQGQELTRLWDRVMIEQECCGT 162
Cdd:pfam00335  85 FLAELAAGILAFVYRDKLSGLlSNWLKKSLEDGYRDWLDLYSCLNSALDSLQSEFGCCGG 144
tetraspanin_LEL cd03127
Tetraspanin, extracellular domain or large extracellular loop (LEL). Tetraspanins are ...
 115-206 2.79e-06

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: 44.42  E-value: 2.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148  115 YTHRDYMVSNPSLITKQMLTFYSADTDqgqeLTRLWDRVMIEQECCGTSGPMDWVNFTSAFraatpevvfpwPPLCCRRT 194
Cdd:cd03127   1 FVYRDQLESLVSDTLNDAWDEYYVDDD----FQEAMDALQSTFECCGVNGPTDYLDLRLLV-----------PSSCCKGT 65

                        90
                ....*....|....
gi 5902148  195 --GNFIPLNEEGCR 206
Cdd:cd03127  66 dgNCGLNLYTEGCL 79
CD151_like_LEL cd03155
Tetraspanin, extracellular domain or large extracellular loop (LEL), CD151_Like family. ...
 112-220 1.98e-05

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: 42.72  E-value: 1.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148  112 ITSYTHRDYMVSNpslITKQMLTFYSADTDQgqELTRLWDRVMIEQECCGTSGPMDWVNftSAF---RAATPEVVfpwPP 188
Cdd:cd03155   2 TYYQQLEDELKES---LKRTMQENYGQSGEE--ALTLTVDELQQEFKCCGSNNYTDWQD--SEWinsNEANGRLV---PD 71

                        90       100       110
                ....*....|....*....|....*....|....
gi 5902148  189 LCCRRtgnfiPLNEEGCRLGHMD--YLFTKGCFE 220
Cdd:cd03155  72 SCCKT-----VVDRCGCLRDHPSniYKVEGGCIP 100
NET-5_like_LEL cd03165
Tetraspanin, extracellular domain or large extracellular loop (LEL), NET-5_like family. ...
 139-220 3.03e-04

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: 38.89  E-value: 3.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902148  139 DTDQGQELTRLWDRVMIEQECCGTSGPMDWVNFTSAFRAatpevvfpwPPLCCRRtgnfiplNEEGCRLGHMDYLFTKGC 218
Cdd:cd03165  23 GTRNNRGLTNAWDITQTEFRCCGVTNYTDWYEVLGENRV---------PDSCCQE-------DSQDCGRNPTELWWKTGC 86


                ..
gi 5902148  219 FE 220
Cdd:cd03165  87 YE 88
 
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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