ID W5N0M8_LEPOC Unreviewed; 1893 AA.
AC W5N0M8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000014187.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000014187.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR EMBL; AHAT01000285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000014216.1; ENSLOCP00000014187.1; ENSLOCG00000011516.1.
DR GeneTree; ENSGT01100000263555; -.
DR HOGENOM; CLU_237558_0_0_1; -.
DR Proteomes; UP000018468; Linkage group LG10.
DR Bgee; ENSLOCG00000011516; Expressed in zone of skin and 10 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.2030; -; 2.
DR Gene3D; 4.10.1240.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF42; INTEGRIN BETA-4; 1.
DR Pfam; PF03160; Calx-beta; 2.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00237; Calx_beta; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00187; INB; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SUPFAM; SSF141072; CalX-like; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|RuleBase:RU000633};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1893
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004866990"
FT TRANSMEM 715..737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1239..1328
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1332..1431
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1601..1694
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1714..1810
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 1893 AA; 211002 MW; 5F5946207923C812 CRC64;
MERWVLHLSV GMVLLALLWT TTHASRVNHC LAARATTCTQ CIQSGKDCSY CADEEFKQPR
CDLYNNLDAA RCQMIMRAES EISVQRNMKI QTSLKQSQVA PQLMSMRLQP GEEQEVELHV
FEPLQAPLDL YILMDFSNSM SDDLDNLKKM GDSLANVVRN LSEDFTIGFG KFVDKVTEPQ
TDMRPQKLKE PWPNSDPPFS FKNVIRLTGS SETFRKELQK ERISGNLDAP EGGFDAILQT
AVCKNQIGWR DNSTHLLVFS TESAFHYEAD GGNVLAGILP RNDEACHLDR FGSYTHDTLQ
DYPSVPTLVR LLGKHNIIPI FAVTNYSYSY YDKLHRYFPV SEIGELKEDS SNILDLLRNA
FQNIRSKISI RAEDVPRALS TEILSQKAQI TETGTFRITP GEEGIFKVRV KAQKEVEGTH
VCQLSQQERE GSLRVKPTTF NTALNINAGI VCKKCNCEET PIKKAVRCNR NGDLVCGVCT
CNPGWKGPYC NCSESSTSDA SSCINPKTNR TCSDRGTCVC GVCICFNSEK NPLETYEGNF
CEFDSSQCPR FGGFLCNGLG RCFMGQCACD EGWEGSACEC PKSNETCIDS KGGICNGRGT
CQCGRCICDD PETFPGATCE ANFQARLGLC ENKRSCVQCQ AWKTGELKGK KCEGCPFKIT
MVDELKKKEE VIETCSFRDE DDDCTYEYTV DYLPNSKNLS DVQVLKKKEC PPGGFLWLIP
LIMFLMLLLG LLLLCCWKYC ACCKACLAML PCCGRGRMVG FKEDQYMLRQ SLLTSDHLDT
PLVRTGPPKS TDVVRWKIMD NVHRSATALT QTLNSKETIQ YPLSLRLTRL FTDSLSRPDA
RETDLLRREV EENLNDVYKQ IPGVQRVQKT KFRLQPNAGK RQDHTVVDTV LSAPRSAQPE
IVRLTERQVQ SGRFSDLKVV PNYYTVASDR DATGLVELQE GVESVDVRVP LFVKDEDDDK
KQLRVEALEV PLGIAEIGRR FVNITIIKEQ AKSIFTFLQP SYTYSRQDKV ANIPVSREII
EDGHTQVTYR TRDLTAKDQR DYVFTEGELT YRPGETQKTV PVKLLELTEA DSLLGEKQIK
QFVMDLSNPR QGAKLGRYPR TTVTISDDPE PSVMMFKKST QGFTTADQLY TIPVIRTRNQ
EGPATVYWRT RKASRFEMSS PLKFSPGETE KNIVIDPCMH PGPIKPEIFQ LELFDPSANA
VIGERKTTLV SVVEPSDGRP NEVQLFSQNL QSPGGRLGAP TKVTAKATSA KSIHLNWTPP
PGKPSGYKVK YWIEGDPESD AQVIDCKSPQ ADLTGLYPYC DYEMRVCSYN ALGEGRYSDV
VQCQTLEDVP SEPGRLAFNV INPTVTQLSW AEPAETNGDI TAYEVTYTPI NEDSKPMGPT
KKVKIDSPKK RMLLIENLQK CQTYCYTVKA RNKAGWGPTR EATINLATQP PRPLSIPIIP
DIPIVDAEAG EGYDSYLMYS SDVMRSPGGS KRPSVSDEEF VNGKWDQSFL YPGGAGSLTR
NISTTSYNQS SLSPSFRSPG GTMTMETTTT YLPGQGGSLT RRHDGMVHGG LRTEEVVLRK
RSETKGYYDN DGVRDSIVMV DEPGGFSDSL DSRLPPGVPD TPTRLVFSAL GPTALKVSWQ
EPHCEKEVLG YCVLYQLLNG GDVKRIDVPN PAENSVVVKD LLPNHSYIFK VKAHSEEGWG
PEREGVITIE SAVDPKSPLS PVPGSPFTLS TPSAPGPLVF TALSPESLQL SWEKPRKPNG
SILGYMVTCE QLNGGGDVRT FQVNGDTAET SLTVPNLSEN VPYKFKVQAR TTQGFGPERE
GIITIESQDG GNFSQFNSQQ VMRRDVFNMP GEVTTRTTHT MLNDPYFSDG MMMTTQRMET
SGTVTRQMTK EVVSRSMVSG TSMTKRVENF YEA
//
