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        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57529984 112 YIYYQQLSTELKENLKNTMTEKYRKEGEERVTSAVDKLQQEFKCCGSNNYTDWADSMWIKSPEASGRKVPDSCCKTITVL 191
Cdd:cd03155   1 YTYYQQLEDELKESLKRTMQENYGQSGEEALTLTVDELQQEFKCCGSNNYTDWQDSEWINSNEANGRLVPDSCCKTVVDR 80

                        90       100       110
                ....*....|....*....|....*....|
gi 57529984 192 CG-RRDHPSNIYK-ENGCITKLENFIQEHL 219
Cdd:cd03155  81 CGcLRDHPSNIYKvEGGCIPKLEDFLYDHL 110

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        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57529984 112 YIYYQQLSTELKENLKNTMTEKYRKEGEERVTSAVDKLQQEFKCCGSNNYTDWADSMWIKSPEASGRKVPDSCCKTITVL 191
Cdd:cd03155   1 YTYYQQLEDELKESLKRTMQENYGQSGEEALTLTVDELQQEFKCCGSNNYTDWQDSEWINSNEANGRLVPDSCCKTVVDR 80

                        90       100       110
                ....*....|....*....|....*....|
gi 57529984 192 CG-RRDHPSNIYK-ENGCITKLENFIQEHL 219
Cdd:cd03155  81 CGcLRDHPSNIYKvEGGCIPKLEDFLYDHL 110

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        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57529984 112 YIYYQQLSTELKENLKNTMTEKYRKEGEERVTSAVDKLQQEFKCCGSNNYTDWADSMWIKSPEASGRKVPDSCCKTITVL 191
Cdd:cd03155   1 YTYYQQLEDELKESLKRTMQENYGQSGEEALTLTVDELQQEFKCCGSNNYTDWQDSEWINSNEANGRLVPDSCCKTVVDR 80

                        90       100       110
                ....*....|....*....|....*....|
gi 57529984 192 CG-RRDHPSNIYK-ENGCITKLENFIQEHL 219
Cdd:cd03155  81 CGcLRDHPSNIYKvEGGCIPKLEDFLYDHL 110

Tetraspanin, extracellular domain or large extracellular loop (LEL), CD63 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". CD63 is present in platelets, neutrophils, and endothelial cells, amongst others. In platelets it associates with the integrin alphaIIBbeta3 and may modulate alphaIIbbeta3-dependent cytoskeletal reorganization.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57529984 112 YIYYQQLSTELKENLkNTMTEKYRKEGEerVTSAVDKLQQEFKCCGSNNYTDWAdsmwiKSPEASGRKVPDSCCKTITVL 191
Cdd:cd03166   1 YVFRDKVMSEFNDSF-NQMISNYNKTND--FRKILDRMQKDLKCCGANNYTDWE-----NIPSLDTDSVPDSCCINVTKG 72

                        90       100
                ....*....|....*....|....*.
gi 57529984 192 CGRRDHPSNIYKEnGCITKLENFIQE 217
Cdd:cd03166  73 CGINFDEKVIHLE-GCVTKIEGWLKK 97

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 57529984 112 YIYYQQLSTELKENLKNTMTEKYRKEGeerVTSAVDKLQQEFKCCGSNNYTDWADsmwikspeaSGRKVPDSCCKTITvl 191
Cdd:cd03127   1 FVYRDQLESLVSDTLNDAWDEYYVDDD---FQEAMDALQSTFECCGVNGPTDYLD---------LRLLVPSSCCKGTD-- 66

                        90       100
                ....*....|....*....|....*...
gi 57529984 192 cgrRDHPSNIYKEnGCITKLENFIQEHL 219
Cdd:cd03127  67 ---GNCGLNLYTE-GCLEKLVDFLRSNL 90

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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57529984 114 YYQQLSTELKENLKNTMTEKYrkEGEERVTSAVDKLQQEFKCCGSNNYTDWADSM-WIKSPEASGRKVPDSCCKT----- 187
Cdd:cd03156   5 FKKDLEDSFKNLLKNNYGNYN--STGDAITSTWNRVMIELKCCGVNGPTDFVDSTsFFRQKNEPNSPYPESCCKRnsnsq 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 57529984 188 ITVLCGRRDHPSNIYKENGCITKLENFIQEH 218
Cdd:cd03156  83 IVDLDCPKLGSPNSYNKKGCYEKLSNPIERY 113

Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF3_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 3 (TM4SF3) or D6.1a and related proteins. D6.1a associates with alpha6beta4 integrin and supports cell motility, it has been ascribed a role in tumor progression and metastasis.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57529984 108 GILAYIYYQQLSTELKENLKNTMTEKYrkEGEERVTSAVDKLQQEFKCCGSNNYTDWAdsmwikspeasGRKVPDSCCKT 187
Cdd:cd03154   1 GIVGAVYKPKIENELKEKNTKLLSLLG--QNAKSVKKSLEKFQKELKCCGLVNGADDW-----------GNDIPASCNCT 67

                        90       100       110
                ....*....|....*....|....*....|....
gi 57529984 188 ITVLCGR--RDHPSNIYKENgCITKLENFIQEHL 219
Cdd:cd03154  68 TTQSDCVvaYYGGSNVYKEP-CISKIKDFLKKNL 100

Tetraspanin, extracellular domain or large extracellular loop (LEL), penumbra_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". Human Penumbra exhibits growth-suppressive activity in vitro and has been associated with myeloid malignancies.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57529984 113 IYYQQLSTELKENLKNTMtEKYRKEGEerVTSAVDKLQQEFKCCGSNNYTDWADSMWI----KSPEASGrkVPDSCC--- 185
Cdd:cd03158   2 IFSNQTIDLLEENIRKAI-VHYYDDLD--LQNIIDFVQKEFKCCGGDDYRDWSKNMYFncssPNPEACG--VPYSCCira 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 57529984 186 KTITV---LCG----RRDHPSN---IYKeNGCITKLENFIQEHL 219
Cdd:cd03158  77 KDQEVintMCGygvqNLERLEAsklIYT-RGCIDAVVLWIEDNL 119

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        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57529984 112 YIYYQQLSTELKENLKNTMteKYRKE----GEERVTSAVDKLQQEFKCCGSNNYTDWADSMWI-------KSPEASGR-- 178
Cdd:cd03162   1 FIMRGSLEESLKTGLKNAM--KFYKDtdtpGRCFLKKTIDMLQIEFQCCGNNGYRDWFEIQWIsnryldfSSKEVKDRik 78

                        90
                ....*....|....*..
gi 57529984 179 ----------KVPDSCC 185
Cdd:cd03162  79 snvdgryltdGVPFSCC 95

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
                ....*....|....*....|....*....|....*....|..
gi 57529984 146 VDKLQQEFKCCGSNNYTDWADSMWIK--SPEASGRKVPDSCC 185
Cdd:cd03167  32 IDQVQLGLQCCGASSYQDWQQNLYFNcsSPGVQACSLPASCC 73