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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012276  40 ISTQRAQLERSLRDVVEKTIQKYGTNPEETAAEESWDYVQFQLRCCGWHYPQDWFQvLILRGNGSEaHRVPCSCYNLSAT 119
Cdd:cd03160    1 IYFQRDKLKQEMGDIVEKVIQNYGGNPENKTAEEAWDYVQFQLQCCGWTGPQDWTD-NSLIKNSSE-PLYPCSCCNSSAT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768012276 120 NDStildkvilpqlsrlghlarSRHSADICAVPA--ESHIYREGCAQGLQKWLHNNLI 175
Cdd:cd03160   79 ADS-------------------PRPSKGFCEAPAslDWPVYQEGCMEKLQSWLNENLG 117

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012276  40 ISTQRAQLERSLRDVVEKTIQKYGTNPEETAAEESWDYVQFQLRCCGWHYPQDWFQvLILRGNGSEaHRVPCSCYNLSAT 119
Cdd:cd03160    1 IYFQRDKLKQEMGDIVEKVIQNYGGNPENKTAEEAWDYVQFQLQCCGWTGPQDWTD-NSLIKNSSE-PLYPCSCCNSSAT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768012276 120 NDStildkvilpqlsrlghlarSRHSADICAVPA--ESHIYREGCAQGLQKWLHNNLI 175
Cdd:cd03160   79 ADS-------------------PRPSKGFCEAPAslDWPVYQEGCMEKLQSWLNENLG 117

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012276  40 ISTQRAQLERSLRDVVEKTIQKYGTNPEETAAEESWDYVQFQLRCCGWHYPQDWFQvLILRGNGSEaHRVPCSCYNLSAT 119
Cdd:cd03160    1 IYFQRDKLKQEMGDIVEKVIQNYGGNPENKTAEEAWDYVQFQLQCCGWTGPQDWTD-NSLIKNSSE-PLYPCSCCNSSAT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768012276 120 NDStildkvilpqlsrlghlarSRHSADICAVPA--ESHIYREGCAQGLQKWLHNNLI 175
Cdd:cd03160   79 ADS-------------------PRPSKGFCEAPAslDWPVYQEGCMEKLQSWLNENLG 117

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012276  42 TQRAQLERSLRDVVEKTIQKYGTNPEETAAeesWDYVQFQLRCCGWHYPQDWfqvlilrgnGSEAHRVPCSCYNLSATND 121
Cdd:cd03127    2 VYRDQLESLVSDTLNDAWDEYYVDDDFQEA---MDALQSTFECCGVNGPTDY---------LDLRLLVPSSCCKGTDGNC 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768012276 122 StildkvilpqlsrlghlarsrhsadicavpaeSHIYREGCAQGLQKWLHNNL 174
Cdd:cd03127   70 G--------------------------------LNLYTEGCLEKLVDFLRSNL 90

Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF8_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 8 (TM4SF8) or Tspan-3 and related proteins. Tspan-3 has been reported to form a complex with integrin beta1 and OSP/claudin-11, which may be involved in oligodendrocyte proliferation and migration.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012276  51 LRDVVEKTIQKY-----GTNPEETAAeeswDYVQFQLRCCGWHYPQDWFQVLILrgNGSEAHRVPCSCYNLSATNDSTIL 125
Cdd:cd03163    8 VEDELNPSIDKVfnkynGTNAESRAV----DYLQRQLQCCGIHNYTDWENTPWF--KESKNNSVPLSCCKETFTSCTGSL 81

                 ..
gi 768012276 126 DK 127
Cdd:cd03163   82 TQ 83

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768012276  46 QLERSLRDVVEKTIQKYGTNPEETAAEESWDYVQFQLRCCGWHYPQDWFQVLILRGNGSEAHRVPCSC 113
Cdd:cd03155    6 QLEDELKESLKRTMQENYGQSGEEALTLTVDELQQEFKCCGSNNYTDWQDSEWINSNEANGRLVPDSC 73

Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_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". Peripherin, or RDS (retinal degradation slow) is a glycoprotein expressed in vertebrate photoreceptors, located at the rim of the disc membranes of the photoreceptor outer segments. RDS is thought to play a major role in folding and stacking of the discs. Mutations in RDS have been linked to hereditary retinal dystrophies, which typically exhibit a wide phenotypic spectrum.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768012276  44 RAQLERSLRDVVEKTIQKYG--TNPEETAAEESWDYVQFQLRCCGWHYPQDWFQV 96
Cdd:cd03162    4 RGSLEESLKTGLKNAMKFYKdtDTPGRCFLKKTIDMLQIEFQCCGNNGYRDWFEI 58

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012276  46 QLERSLRDVVEKTIQK-YGTNPEETAAeesWDYVQFQLRCCGWHYPQDWFQVL-ILRGNGSEAHRVPCSC 113
Cdd:cd03156    8 DLEDSFKNLLKNNYGNyNSTGDAITST---WNRVMIELKCCGVNGPTDFVDSTsFFRQKNEPNSPYPESC 74

Tetraspanin, extracellular domain or large extracellular loop (LEL), oculospanin_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 subfamily contains sequences similar to oculospanin, which is found to be expressed in retinal pigment epithelium, iris, ciliary body, and retinal ganglion cells.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012276  44 RAQLERSLRDVVEKTIQKYGTNPEetaAEESWDYVQFQLRCCGWHYPQDWFQVLILR--GNGSEAHRVPCSCYnLSATND 121
Cdd:cd03167    4 WGPLQDGLEHTLRLAIAHYQDDPD---LRFLIDQVQLGLQCCGASSYQDWQQNLYFNcsSPGVQACSLPASCC-IDPRED 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768012276 122 STILDKVILPQLSRLGHLArsrhsadicavpAESHIYREGCAQGLQKWLHNNL 174
Cdd:cd03167   80 GAVVNDQCGFGALGLDEDA------------AQRVVHLGGCGPPLRRWLRGNL 120