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 1622893032 120 LEHTIVTLRKNYRG--YNEPDDYSTQWNLVMEKLKCCGVNNYTDFSGSSF----EMTTGHTYPRGCCKSIGTVTCDGRN- 192
Cdd:cd03156     9 LEDSFKNLLKNNYGnyNSTGDAITSTWNRVMIELKCCGVNGPTDFVDSTSffrqKNEPNSPYPESCCKRNSNSQIVDLDc 88

                          90       100
                  ....*....|....*....|....*.
gi 1622893032 193 ---VSTNVIHQKGCFHKLLKITKTQS 215
Cdd:cd03156    89 pklGSPNSYNKKGCYEKLSNPIERYA 114

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 1622893032 120 LEHTIVTLRKNYRG--YNEPDDYSTQWNLVMEKLKCCGVNNYTDFSGSSF----EMTTGHTYPRGCCKSIGTVTCDGRN- 192
Cdd:cd03156     9 LEDSFKNLLKNNYGnyNSTGDAITSTWNRVMIELKCCGVNGPTDFVDSTSffrqKNEPNSPYPESCCKRNSNSQIVDLDc 88

                          90       100
                  ....*....|....*....|....*.
gi 1622893032 193 ---VSTNVIHQKGCFHKLLKITKTQS 215
Cdd:cd03156    89 pklGSPNSYNKKGCYEKLSNPIERYA 114

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 1622893032 120 LEHTIVTLRKNYRG--YNEPDDYSTQWNLVMEKLKCCGVNNYTDFSGSSF----EMTTGHTYPRGCCKSIGTVTCDGRN- 192
Cdd:cd03156     9 LEDSFKNLLKNNYGnyNSTGDAITSTWNRVMIELKCCGVNGPTDFVDSTSffrqKNEPNSPYPESCCKRNSNSQIVDLDc 88

                          90       100
                  ....*....|....*....|....*.
gi 1622893032 193 ---VSTNVIHQKGCFHKLLKITKTQS 215
Cdd:cd03156    89 pklGSPNSYNKKGCYEKLSNPIERYA 114

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 1622893032 116 RDVVLEHTIVTLRKNYRGYNEPDDYSTQWNLVMEKLKCCGVNNYTDFsgssfeMTTGHTYPRGCCKsiGTVTCDGRNvst 195
Cdd:cd03127     4 RDQLESLVSDTLNDAWDEYYVDDDFQEAMDALQSTFECCGVNGPTDY------LDLRLLVPSSCCK--GTDGNCGLN--- 72

                          90
                  ....*....|..
gi 1622893032 196 nvIHQKGCFHKL 207
Cdd:cd03127    73 --LYTEGCLEKL 82

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 1622893032 116 RDVVLEHTIVTLRKNYRGYNEPDdySTQ-WNLVMEKLKCCGVNNYTDFSGSSFE---MTTGHTYPRGCCKSIGTVTCDGR 191
Cdd:cd03155     8 EDELKESLKRTMQENYGQSGEEA--LTLtVDELQQEFKCCGSNNYTDWQDSEWInsnEANGRLVPDSCCKTVVDRCGCLR 85

                          90       100
                  ....*....|....*....|....*
gi 1622893032 192 NVSTNvIHQ--KGCFHKLLKITKTQ 214
Cdd:cd03155    86 DHPSN-IYKveGGCIPKLEDFLYDH 109

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 1622893032 122 HTIV-TLRKNYRGYNEPDDYSTQWNLVMEKLKCCGVNNYTDFSGSSFEMT-TGHTYPRGCCKSIGTVT--------CDGR 191
Cdd:cd03160    13 GDIVeKVIQNYGGNPENKTAEEAWDYVQFQLQCCGWTGPQDWTDNSLIKNsSEPLYPCSCCNSSATADsprpskgfCEAP 92

                          90
                  ....*....|....*.
gi 1622893032 192 NVSTNVIHQKGCFHKL 207
Cdd:cd03160    93 ASLDWPVYQEGCMEKL 108

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622893032 144 WNLVMEKLKCCGVNNYTDFsgssFEMTTGHTYPRGCCKSIgTVTCdGRNvSTNVIHQKGCFHKL 207
Cdd:cd03165    34 WDITQTEFRCCGVTNYTDW----YEVLGENRVPDSCCQED-SQDC-GRN-PTELWWKTGCYEKV 90