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Database: UniProt
Entry: F7BIL4_HORSE
LinkDB: F7BIL4_HORSE
Original site: F7BIL4_HORSE 
ID   F7BIL4_HORSE            Unreviewed;      1740 AA.
AC   F7BIL4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 2.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN   Name=ITGB4 {ECO:0000313|Ensembl:ENSECAP00000009107.2,
GN   ECO:0000313|VGNC:VGNC:19178};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000009107.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000009107.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000009107.2,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000009107.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000009107.2};
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   STRING; 9796.ENSECAP00000009107; -.
DR   PaxDb; 9796-ENSECAP00000009107; -.
DR   Ensembl; ENSECAT00000011628.4; ENSECAP00000009107.2; ENSECAG00000010178.4.
DR   VGNC; VGNC:19178; ITGB4.
DR   GeneTree; ENSGT01100000263555; -.
DR   InParanoid; F7BIL4; -.
DR   OMA; HTKFRQQ; -.
DR   TreeFam; TF105392; -.
DR   Proteomes; UP000002281; Chromosome 11.
DR   Bgee; ENSECAG00000010178; Expressed in oviduct epithelium and 20 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0048870; P:cell motility; IEA:InterPro.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   GO; GO:0031581; P:hemidesmosome assembly; IEA:InterPro.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   CDD; cd00063; FN3; 4.
DR   Gene3D; 2.60.40.2030; -; 1.
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; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
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; IPR012013; Integrin_bsu-4.
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; 1.
DR   Pfam; PF07974; EGF_2; 1.
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   PIRSF; PIRSF002513; Integrin_B4; 2.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00237; Calx_beta; 1.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SUPFAM; SSF141072; CalX-like; 1.
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; PS00022; EGF_1; 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS00243; INTEGRIN_BETA; 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell adhesion {ECO:0000256|RuleBase:RU000633};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1740
FT                   /note="Integrin beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040207333"
FT   TRANSMEM        712..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1211..1310
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1448..1543
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1561..1657
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          1113..1141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1740 AA;  193752 MW;  469281FD68D49D9F CRC64;
     MAGPHPSPWT RLLLAALLSV SFPGDMANRC KKAQVKSCTE CIRVDKDCAY CTDEMFKERR
     CNTQAELLAA GCRLESVVVM ERSFEITEAT QIDTTLRRSQ VSPQAMRVRL RPGEEQLFEL
     EVFEPLESPV DLYILMDFSN SMSDDLDNLK KMGQNLARVL SQLTSDYTIG FGKFVDKVSV
     PQTDMRPEKL KEPWPNSDPP FSFKNVISLT EDVNEFRSKL QGERISGNLD APEGGFDAIL
     QTAVCTRDIG WRPDSTHLLV FSTESAFHYE ADGANVLAGI MSRNDEECHL DATGTYTQYK
     TQDYPSVPTL VRLLGKHNII PIFAVTNYSY SYYEKLHTYF PVSSLGVLQE DSSNIVELLE
     EAFNRIRSNL DIRALESPRG LKTEITSKVF QKTKTGSFHI RRGEVGTYYV QLRAIEDVDG
     THVCQLPLED QKGNIHLKPS FSDGLRIDVG VICDVCSCEL QKEVRSAHCS FNGDFMCGHC
     MCNEGWSGKT CNCSTGSLSD TQPCLREDED KPCSGRGECQ CGRCVCYGEG RYEGQFCEYD
     NFQCPRTSGF LCNDRGRCSM GQCVCEPGWT GSSCDCPLSN ATCIDSNGGI CNGRGHCECG
     RCHCNQQSLY TDTICEINYS AIRLGLCEDL RSCVQCQAWG TGEKKGRTCE ECSFKVKMVD
     KLKKAEEVVE YCSFRDEDDD CTYSYTVEGD GAPGPNSTVL VHRKKDCPPT SFWWLIPLLI
     FLLLLLALLL LLCWKYCACC KACLALLPCC NRGHMVGFKE DHYMLRENLM ASDHLDTPML
     RSGNLKGRDT VRWKITNNVQ RPGFATRVAS TNPTELVPYG LSLRLARLCT ENLLKPDTRE
     CNQLRQEVEE NLNEVYRQIT GAYKLQQTKF RQQPNAGKKQ DHTIVDTVLM APRSAKQTLL
     KLTEKHVEQG AFHELKVAPG YYTLTADQDA RGMVEFQEGV ELVDVRVPLF IRPEDDDEKQ
     LLVEAIDVPV GTATLGRRLV NITIIKEQAS GIVSFEQPEY LVSGGEQVAR IPVVRRILDN
     GKSQVSYRTQ DNTAQGNRDY IPVEGELLFQ PGEMWKELQV KLLELQEMDS LLRGRQTRHF
     HIQLSNPKFG ARLGQPHSAT VIIGDPDELD RNLISQTVSS PPPPRGDLGA PQNPNAKAAG
     SRKIHFNWLP PPGKPTGYRV KYWIQGDSEL EAHLLDSKVP SVELTNLYPY CDYEMKVSLV
     SCRTHQEVPS EPGRLAFNVV SSTVTQLSWA EPAETNGEIT AYEVCYGLVN EDNRPIGPMK
     KVLVDSPKKR TLLIENLRES QPYRYTVKAR NGAGWGPERE AIINLATQPK RPMSIPIIPD
     IPIVDAQSGE DYESFLMYSD DVLRSPAGSQ RPSVSDDTEH LVNGRMDFAY PGSANSLHRM
     TVANAAYGTH LSPHLPHRVL STSSTLTRDY HSLTRTEHSH TATLPRDYST LTSLSSHSSR
     LAAGVPNTPT RLVFSALGPT SLKVSWQEPQ CDQALQGYSV EYQLLNGGEL HRLNIPNPSQ
     TSVVVEDLLP NHSYVFRVRA QSQEGWGPER EGVITIESQV HPQSPLCPLP GSTFTLSTPS
     APGPLVFTAL SPDSLQLSWE RPRRPDGDIL GYLVTCEMAH GGEPATTFLV DGDSPESRLT
     VPGLSENVPY KFKVQAKTTQ GFGPEREGII TIESQDGGPF PQLGSHSGLF QHPLPGEYSS
     ITTTHTSTIE PFLLDGLTLG SQHLEAGGSL TRHVTQEFVS RTLTTSGTLS TQVDQQFFQT
//
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