ID M4A2K3_XIPMA Unreviewed; 790 AA.
AC M4A2K3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000008697.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000008697.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000008697.1};
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 RefSeq; XP_014330685.1; XM_014475199.1.
DR AlphaFoldDB; M4A2K3; -.
DR Ensembl; ENSXMAT00000008710.2; ENSXMAP00000008697.1; ENSXMAG00000008649.2.
DR GeneID; 102221802; -.
DR KEGG; xma:102221802; -.
DR CTD; 564266; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01090000259987; -.
DR HOGENOM; CLU_011772_0_1_1; -.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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 Gene3D; 4.10.1240.30; -; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
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; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF25; INTEGRIN BETA-3; 1.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU000633};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1};
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:UP000002852};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..790
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004047310"
FT TRANSMEM 721..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..72
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 31..456
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 629..720
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 744..790
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 24..456
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 32..42
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 35..71
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 45..60
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 198..205
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 253..294
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 395..407
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 454..458
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 469..481
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 478..516
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 483..492
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 494..507
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 522..527
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 524..557
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 529..542
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 544..549
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 563..568
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 565..596
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 570..579
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 581..588
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 602..607
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 604..652
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 609..619
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 622..625
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 629..638
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 635..715
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 656..691
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 790 AA; 86600 MW; 3F13EB2E74F45D72 CRC64;
MGSLLPYLVY LFLFASNVCG SNICTSRGVT TCRECLVVHP SCAWCSDEVF GKGRSTLSRC
DLKENLVKEG CSAAAIEFPT SKLEIQQNNP LSDRASSTAD VTQIRPQKLQ LTLRIGDTKR
FTVSVKQVED YPVDLYYLMD LSYSMKDDLL KLQTLGNKLA ETMGKTTSKL HMGFGAFVDK
TTYPYLITYP KGAIQNPCVG INDQCQAQFG FKNVLSLTEK VSRFTEEVQK QKVSRNRDSP
EGGFDAIIQA MVCKDKIGWR PDASHLLVLT TDAKTHLALD GRIAGIVQPN DGECHLDDNN
NFNKSTVLDY PSLGLITDKM SENNINLIFA VTSYVVPLYQ EYSQLIPGTT VGTLSDDSGN
VIQLIKEAYE KIRSKMELEL LGVPEELNLS FNASCLNGEV IRGLRSCSGL KIGDTVSFTV
DAQLRSCPKE KSRTFTIKPL GFKDSLEVTV NFACGCDCEA KAVPNSPVCS NGNGTYECGV
CQCHPGRLGS LCECSQEDYR PSDDANCLPS SNSLICSGRG DCLCGQCSCH STGFGQVWGK
YCECDDFNCL HFKGALCSDH GKCNCGFCQC DAGWKGDNCN CTTRTDTCVS SSGLLCSGRG
NCECGVCQCT QPGAFGDTCD RCPTCPDACT IKTQCVECQH FKRGQYINDS SCNRICKNEI
QIVDQLSKKM NGNGEFQQGI AVNCSYKDEN CIVHFQYYED KTGTSILYVV KEPECPEGPD
ILVVLLAVAG AILLLGLVGL LIWKLLVTIH DRKEYSKFEE EKAKAKWDTA NNPLYKGATS
TFTNVAYKGN
//
