ID H0WJM6_OTOGA Unreviewed; 1835 AA.
AC H0WJM6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB4 {ECO:0000313|Ensembl:ENSOGAP00000001708.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000001708.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000001708.2}
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 EMBL; AAQR03041477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03041478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03041479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03041480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03041481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03041482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03041483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03041484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03041485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03041486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 30611.ENSOGAP00000001708; -.
DR Ensembl; ENSOGAT00000001917.2; ENSOGAP00000001708.2; ENSOGAG00000001913.2.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01100000263555; -.
DR HOGENOM; CLU_237558_0_0_1; -.
DR InParanoid; H0WJM6; -.
DR OMA; HTKFRQQ; -.
DR TreeFam; TF105392; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
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; 1.
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; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|RuleBase:RU000633};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000005225};
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..1835
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003544271"
FT TRANSMEM 320..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1136..1225
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1229..1328
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1543..1638
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1656..1752
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1119..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1835 AA; 203849 MW; 63FFFF56BC50101F CRC64;
MAGPHPRLWT RLLLAALLST SLPGAMANLC KKAQVKSCTE CIRVDKDCAY CTDEMFKERR
CNTQAELLAA GCRQGSVVVM ESSFQIIEET QIDTTLRRSQ VSPQSLRVRL RPGEEQHFEL
EVFEPLESPV DLYILMDFSN SMSDDLDNLK QMGQNLARVL SQLTSDYTIG FGKFVDKVTV
PQTDMRPEKL KEPWPNSDPP FSFKNVISLT EDVEEFRNKL QGERISGNLD APEGGFDAIL
QTAVCTRGHE QPAMGSEALE RISRSLQLSF LKTSLDFLNG PQKTKNQNCP YFHHHQIAGH
LISNQRILFP FPYLRSLESV YLYIMLKFCF FFTYHYHKHF LSCTYFNCHF LYILAEAWCL
WLKQLRASHI HLSWRVQIQP RPTKQQRRLQ QVMAHAVNKL SPGSAPVAQA AKGTYQVHLR
AIEDIDGTPV CQLPVEDQKG NIHLKPSFSD GLRMDVGIIC DMCACELQKE VQSARCNFQG
DFTCGHCVCS EGWSGKTCNC STGSLSDMQP CLQEGDDKPC SGRGECQCGH CVCYGEGRYE
GQFCEYDNFQ CPRTSGFLCN DRGRCSMGQC VCEPGWTGPS CDCPLSNATC IDSNGGICNG
RGHCECGRCH CNQQSLYTDT TCEINYSAIR LGLCEDLRSC VQCQAWGTGE KKGRTCEECS
FKVKMVDELK KAVGAAEEVV EFCSFRDEDD DCTYSYTVEG DGTPGPNSTV LVHRKKDCPP
GSFWWLIPLL LFLLLLLALL LLLCWKYCAC CRACLALLPC CNRGHMVGFK EDHYMLRENL
MASDHLDTPM LRSGNLKGRD TVRWKVTNNM QRPGFATHAA STNPTELGEG WGWVLGLLPV
SLGPLGPPDP SFAWQLNEVY RHISGVHKLQ QTKFRQQPNA GKKQDHTIVD TVLTAPRSAK
QALLKLTEKH VEQGSFHELK VAPGYYTLTT DQDARGMVEF QEGVELVDVR VPLFIRPEDD
DEKQLLVEAI DVPVGTATLG RRLVNITIIK EQASGMVFFE QPEYSVTRGE KVARIPVVRR
ILDSGKSQVS YRTQDNTAQG NRDYVPVEGE LLFHPGETWK ELQVKLLELQ EVDSLLRGRQ
TRRFNIQLSN PKFGARLGQP HLATIIIGDR DEDELDQNFV SQTSSSPSPL HGNLGAPQNP
NAKAAGSRKI HFNWLPPSGK PMGYRVKYWI QGDSESDAHL LDSKVPSVEL TNLYPYCDYE
MKVCAYGAQG EGPYSSLVSC RTHQEVPSEP GRLAFNVVSS TVTQVSWAEP AETNGEITAY
EVCYGLVNED NRPIGPMKKV LVDNPKNRML LIENLRESQP YRYTVKARNG AGWGPEREAI
INLATQPKRP MSIPIIPDIP IVDAQGGEDY ENFLMYSDDV LRSPASSQRP SVSDDTGGSW
KFEPLLGEEL DLRRVTWRLP PELIPRLSAS SGRSSDAAEA PLGPPDDGAH PGAGNTGGEG
GSLPRSATPR PPGEHLVNGR MDFAFPGSAN SLHRMTVANT AYGTHLSPHL PHRGLSTSST
LTRDYHSLTR TEHSHSASLP RDYSTLTSLS SHDSRLISGV PDTPTRLVFS ALGPTSLKVS
WQEPQCDHTL QGYSVEYQLL NGGELHHLNI PNPNQTSVVV EDLLPNHSYV FRVRAQSQEG
WGREREGVIT IESQVHPQSP LCPLPGSTFT LSTPSAPGPL VFTALSPESL QLSWERPRRP
NGDILGYLVT CEMAQGGGTA TTFRVDGDNP ESRLTVPGLS ENVPYKFKVQ ARTTEGFGPE
REGIITIESQ DGGPFPQLGS HPGLFQHPLQ GEYSSVTTTH TSTTEPFLMD GLTLGSQRLE
AGGSLTRHVT QEFVSRTLTT SGTLSTQMDQ QFFQT
//
