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
//