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 17737893 132 FVFPQYMNSFLEyQFTDKIIHSYRDDSDLQNFIDFAQQEFNCCGLSNagYQDWSKNEYFNCSSPSVERCGVPYSCCINAT 211
Cdd:cd03158   1 FIFSNQTIDLLE-ENIRKAIVHYYDDLDLQNIIDFVQKEFKCCGGDD--YRDWSKNMYFNCSSPNPEACGVPYSCCIRAK 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17737893 212 DisSGLVNIMCGYGVQVRSVAAASKRIWTSGCIEIVRVWVERNL 255
Cdd:cd03158  78 D--QEVINTMCGYGVQNLERLEASKLIYTRGCIDAVVLWIEDNL 119

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 17737893 132 FVFPQYMNSFLEyQFTDKIIHSYRDDSDLQNFIDFAQQEFNCCGLSNagYQDWSKNEYFNCSSPSVERCGVPYSCCINAT 211
Cdd:cd03158   1 FIFSNQTIDLLE-ENIRKAIVHYYDDLDLQNIIDFVQKEFKCCGGDD--YRDWSKNMYFNCSSPNPEACGVPYSCCIRAK 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17737893 212 DisSGLVNIMCGYGVQVRSVAAASKRIWTSGCIEIVRVWVERNL 255
Cdd:cd03158  78 D--QEVINTMCGYGVQNLERLEASKLIYTRGCIDAVVLWIEDNL 119

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 17737893 132 FVFPQYMNSFLEyQFTDKIIHSYRDDSDLQNFIDFAQQEFNCCGLSNagYQDWSKNEYFNCSSPSVERCGVPYSCCINAT 211
Cdd:cd03158   1 FIFSNQTIDLLE-ENIRKAIVHYYDDLDLQNIIDFVQKEFKCCGGDD--YRDWSKNMYFNCSSPNPEACGVPYSCCIRAK 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17737893 212 DisSGLVNIMCGYGVQVRSVAAASKRIWTSGCIEIVRVWVERNL 255
Cdd:cd03158  78 D--QEVINTMCGYGVQNLERLEASKLIYTRGCIDAVVLWIEDNL 119

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 17737893 132 FVFPQYMNSFLEYQFTDKIIHsYRDDSDLQNFIDFAQQEFNCCGLSNagYQDWSKNEYFNCSSPSVERCGVPYSCCINAT 211
Cdd:cd03167   1 VALWGPLQDGLEHTLRLAIAH-YQDDPDLRFLIDQVQLGLQCCGASS--YQDWQQNLYFNCSSPGVQACSLPASCCIDPR 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17737893 212 DISSgLVNIMCGYGVQVRSVAAASKRIWTSGCIEIVRVWVERNL 255
Cdd:cd03167  78 EDGA-VVNDQCGFGALGLDEDAAQRVVHLGGCGPPLRRWLRGNL 120

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 17737893 132 FVFPQYMNSFLeYQFTDKIIHSYRDDSDLQNFIDFAQQEFNCCGLSnaGYQDWSKNeyfncsspsveRCGVPYSCCINat 211
Cdd:cd03127   1 FVYRDQLESLV-SDTLNDAWDEYYVDDDFQEAMDALQSTFECCGVN--GPTDYLDL-----------RLLVPSSCCKG-- 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17737893 212 dissglvnimcgygvqvrSVAAASKRIWTSGCIEIVRVWVERNL 255
Cdd:cd03127  65 ------------------TDGNCGLNLYTEGCLEKLVDFLRSNL 90

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        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737893 165 DFAQQEFNCCGLSNagYQDWskNEYFNCSSpsvercgVPYSCCINatdISSGlvnimCGYGvqvrsvaaASKRIWTSGCI 244
Cdd:cd03165  35 DITQTEFRCCGVTN--YTDW--YEVLGENR-------VPDSCCQE---DSQD-----CGRN--------PTELWWKTGCY 87

                        90
                ....*....|.
gi 17737893 245 EIVRVWVERNL 255
Cdd:cd03165  88 EKVQQWLVDNL 98

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 17737893 142 LEYQFTDKIIH----SYRDDSDLQNFIDFAQQEFNCCGLSNaGYQDWSKNEYFNCsspsveRCGVPYSCCinatdissgl 217
Cdd:cd03154  11 IENELKEKNTKllslLGQNAKSVKKSLEKFQKELKCCGLVN-GADDWGNDIPASC------NCTTTQSDC---------- 73

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17737893 218 VNIMCGygvqvrsvaaaSKRIWTSGCIEIVRVWVERNL 255
Cdd:cd03154  74 VVAYYG-----------GSNVYKEPCISKIKDFLKKNL 100

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 17737893 148 DKIIHSYR---DDSDLQNFIDFAQQEFNCCGLSnaGYQDWSKN-EYFNCSSPSvercgVPYSCCINATDISSGLVNI-MC 222
Cdd:cd03160  17 EKVIQNYGgnpENKTAEEAWDYVQFQLQCCGWT--GPQDWTDNsLIKNSSEPL-----YPCSCCNSSATADSPRPSKgFC 89

                        90       100       110
                ....*....|....*....|....*....|...
gi 17737893 223 GYGVQVRSvaaaskRIWTSGCIEIVRVWVERNL 255
Cdd:cd03160  90 EAPASLDW------PVYQEGCMEKLQSWLNENL 116

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 17737893 132 FVFPQYMNSFLEYQFTDKIIHsYRDDSD-----LQNFIDFAQQEFNCCGlsNAGYQDWSK-----NEYFNCSS-PSVERC 200
Cdd:cd03162   1 FIMRGSLEESLKTGLKNAMKF-YKDTDTpgrcfLKKTIDMLQIEFQCCG--NNGYRDWFEiqwisNRYLDFSSkEVKDRI 77

                        90
                ....*....|....*...
gi 17737893 201 -----------GVPYSCC 207
Cdd:cd03162  78 ksnvdgryltdGVPFSCC 95

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
                ....*....|....*....|....*....|....*....|....
gi 17737893 164 IDFAQQEFNCCGLSNagYQDWSKNEYFNCSSPSvercGVPYSCC 207
Cdd:cd03163  33 VDYLQRQLQCCGIHN--YTDWENTPWFKESKNN----SVPLSCC 70