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Database: UniProt
Entry: W5KB54_ASTMX
LinkDB: W5KB54_ASTMX
Original site: W5KB54_ASTMX 
ID   W5KB54_ASTMX            Unreviewed;       790 AA.
AC   W5KB54;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN   Name=ITGB8 {ECO:0000313|Ensembl:ENSAMXP00000004815.2};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000004815.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000004815.2}
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   AlphaFoldDB; W5KB54; -.
DR   STRING; 7994.ENSAMXP00000004815; -.
DR   Ensembl; ENSAMXT00000004815.2; ENSAMXP00000004815.2; ENSAMXG00000004704.2.
DR   eggNOG; KOG1226; Eukaryota.
DR   GeneTree; ENSGT01090000259987; -.
DR   HOGENOM; CLU_011772_3_1_1; -.
DR   InParanoid; W5KB54; -.
DR   OrthoDB; 5475862at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000004704; Expressed in brain and 10 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; 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; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
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; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR   PANTHER; PTHR10082:SF9; INTEGRIN BETA-8; 1.
DR   Pfam; PF07974; EGF_2; 2.
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; 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; PS00022; EGF_1; 1.
DR   PROSITE; PS00243; INTEGRIN_BETA; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell adhesion {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:UP000018467};
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..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..790
FT                   /note="Integrin beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017301053"
FT   TRANSMEM        703..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          559..570
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS00022"
FT   DISULFID        39..465
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        47..57
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        50..86
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        60..75
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        201..208
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        256..297
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        400..411
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        431..666
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        463..467
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        513..518
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        515..548
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        520..533
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        554..559
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        561..570
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        572..579
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        593..598
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        595..643
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        600..610
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        620..629
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        626..697
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        647..674
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ   SEQUENCE   790 AA;  87048 MW;  167A61685E24D443 CRC64;
     MTSWPREERN ITLRSALVFI ILIITLFAVA SCQLAEKRCA SPLVSSCEEC LSRGPECAWC
     FQKSFMDGAH VGERCGSAAR LLLKGCGEEF VENPSVKVEN TTLSSSQVTP RDISIQLRPG
     SEASFIVEVK QLERYPVDLY YLVDVSASMQ DNLDRLKTVG VTLSHRMKEH SSDFRVGFGS
     FVDKPVSPYI DVNPSKISNP CSDYDVHCRP AHGFIHVLPV TENMTDFKQV IQQQRISGNM
     DTPEGGFDAM LQAAVCQKDI GWRPEAKHLL LVMTDQPSHL ALDSKLAGIV VPHDGRCHLV
     DNMYSQSANM EHPTIGQLAE KLLENNIYSI FAVDQMQYKW YEDVVDFLPG TYLGKLLPKA
     SNLTNLVVDA YKKLLSEVGV EVGVEDSEAH RFWVRVSAIC PNGSTETNGR CSNVQPKQTV
     FFNITVGMRS CPAEGLRSGQ EVLLMVRPVG FNESVTVRVQ QACGCSCGEA GPYHEEPEPS
     SCMSGGGPAA ERGLMDGCRE ERSGLVCSGR GICSCGGCVC DQSSLGTIYG QFCEKDDFSC
     AYEGGLVCGG HGQCVSGECL CQPGWSGESC GCPMSSESCL SRDGSVCSGQ GKCVCGKCVC
     DDPRHSGAFC EKCPTCSNSC QSHWSCVSCH VSKGFGRDEA QQCNKSCTSL VAYVDDITEL
     VRGKYCLYHS REQCFFRFHM ELETHGPQLH ISRHAECVLS QRYFKTFLSI FLLTLVLGLG
     ILAVIRQLLR NKSWTLGEES SEQFDDSNKS PSYAPTTSEK TITYRRDHLH EHPVEMHVHV
     PKMPLSDIWP
//
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