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Database: UniProt
Entry: E1B864_BOVIN
LinkDB: E1B864_BOVIN
Original site: E1B864_BOVIN 
ID   E1B864_BOVIN            Unreviewed;      1751 AA.
AC   E1B864;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 3.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN   Name=ITGB4 {ECO:0000313|Ensembl:ENSBTAP00000040201.4,
GN   ECO:0000313|VGNC:VGNC:30329};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000040201.4, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000040201.4, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000040201.4,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000040201.4}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000040201.4};
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   Ensembl; ENSBTAT00000042566.4; ENSBTAP00000040201.4; ENSBTAG00000018169.6.
DR   VEuPathDB; HostDB:ENSBTAG00000018169; -.
DR   VGNC; VGNC:30329; ITGB4.
DR   eggNOG; KOG1226; Eukaryota.
DR   GeneTree; ENSGT01100000263555; -.
DR   HOGENOM; CLU_237558_0_0_1; -.
DR   TreeFam; TF105392; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000018169; Expressed in placenta and 101 other cell types or tissues.
DR   ExpressionAtlas; E1B864; baseline.
DR   GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
DR   GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR   GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0030056; C:hemidesmosome; IEA:Ensembl.
DR   GO; GO:0008305; C:integrin complex; IEA:Ensembl.
DR   GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
DR   GO; GO:0031994; F:insulin-like growth factor I binding; IEA:Ensembl.
DR   GO; GO:0038132; F:neuregulin binding; IEA:Ensembl.
DR   GO; GO:0006914; P:autophagy; IEA:Ensembl.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
DR   GO; GO:0031581; P:hemidesmosome assembly; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0035878; P:nail development; IEA:Ensembl.
DR   GO; GO:0032290; P:peripheral nervous system myelin formation; IEA:Ensembl.
DR   GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR   GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
DR   GO; GO:0061450; P:trophoblast cell migration; IEA:Ensembl.
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; 4.
DR   PROSITE; PS00243; INTEGRIN_BETA; 2.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW   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   Proteomics identification {ECO:0007829|PeptideAtlas:E1B864};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
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..1751
FT                   /note="Integrin beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018688997"
FT   TRANSMEM        712..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1130..1219
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1223..1322
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1460..1555
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1573..1669
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          1114..1146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1751 AA;  194858 MW;  5023429399BA9771 CRC64;
     MAGPHPSPWT RLLLAALLSV SFPGHMANRC KKAQVKSCTE CIRVDKDCAY CTDEVFKERR
     CNTQAELLAA GCRLESVVVM ESSFEITEER QIDTTLRRSQ VSPQALRVRL RPGEERHFEL
     QVFEPLESPM DLYILMDFSN SMSDDLDNLK KMGQDLAQVL RQLTSDYTIG FGKFVDKVSV
     PQTDMRPEKL KEPWPNSDPP FSFKNVISLT EDVEEFRNKL KGERISGNLD APEGGFDAIL
     QTAVCTSDIG WRPDSTHLLV FSTESAFHYE ADGANVLAGI MRRNDEECHL DPTGTYTQYK
     MQDYPSVPTL VRLLGQHNII PIFAVTNYSY SYYERLSSYF PVSSLGVLQE DSSNIVDLLQ
     EAFNRIRSNL DIRALDSPRG LRTEVTSRMF QKTDTGSFFI RRGEVGTYQV QLRAIEDLDG
     AHVCQLLEAD QKGTIHLKPS FSNGLRMDVG VICDVCSCEL QKEERSSRCN FHGDFMCGHC
     VCHEGWSGKT CNCSTGSQSD LQPCRREGED KVCSGRGECQ CGHCVCYGEG RYEGQFCEYD
     NFQCPRTSGF LCNDRGRCSM GQCVCEPGWT GLSCDCPLSN ATCIDSNGGL CNGRGHCECG
     RCHCNQQSLY TDTVCEINYS AIHLGLCEDL RSCVQCQAWG TGEKKGRTCE ECSFKVKMVD
     ELKKAEEVVE HCSFRDEDDD CTYSYTVEGD SAPGPNSTVL VQRRKECPPG TFWWLIPLLI
     FLLLFPVLLL LLCWKYCACC KACLALLPCC NRGHMVGFKE DHYMLRENLM ASDHLDTPLL
     RSGNLKGRDT VRWKITNNVQ RPGFASHAAG INPSELVPYG LSLRLARLCT ENLLKPGTRE
     CDQLRQEVEE NLNEVYRQIT GAHNLQQTKF RQQPNAGKKQ DHTIVDTVLM APRSAKQALL
     KLTEKHVEQG AFHELKVAPG YYTLTADQDA RGMVEFQEGV ELVDVRVPLF IRPEDDDEKQ
     LLVEAIDVPV GTATLGRRLV NITIIKEQAS GIVSFEQPEY LVSSGEHVAR IPVVRRILDS
     GKSQVSYRTQ DNTAKANRDY IPMEGELLFQ PGETWKELQV KLLELQEMDS LLRGPQTRRF
     YIQLSNPKFG ARLGQPQCAT VITGDRDELD RNVMNQTVSS PPPPRGDLGA PQNPNAKAAG
     SRKIHFNWLP PPGKPTGYRV KYWIQGDSES EAHLLDSKVP SVELTNLYPY CDYEMKVCAY
     GAQGEGPYSS PVSCRTHQEV PSEPGRLAFN VVSSTVTQLS WAEPAETNGE ITAYEVCYGL
     VNEDNRPIGP MKKVLVDSPK KRTLLIENLR ESQPYRYTVK ARNGAGWGPE REAIINLATQ
     PKRPMSIPII PDIPIVDAQS GEDYESFLMY SDDVLRSPAG SQRPSVSDDT EHLVNGRMDF
     AFPGSANSLH RMTVSTAAHG AHLSPQLSHR VLSTSSTLTR DYHSLTRTEH SHSATLPRDY
     STLTSLSSQS SRLAAGVPNT PTRLVFSALG PTSLKVSWQE PQCERALQGY SVEYQLLNGG
     ELYRLNIPNP SQTSVVVEDL LPNHSYVFRV RAQSQEGWGP EREGVITIES QVHPQSPLCP
     LPGSAFTLST PSAPGPLVFT ALSPDSLQLS WERPRRPDGD ILGYLVTCEM AHGGEPATTF
     LVDGDSPESR LTVPGLSENV PYKFKVQAKT TQGFGPEREG IITIESQDGG PFPQLGGHLG
     LFQHPASGEY SSITTHSSTT EPFLLDGLTL GSQHLEASGS LTRHVTQEFV SRTLTTSGTL
     STHVDQQFFQ T
//
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