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Database: UniProt
Entry: Q64632
LinkDB: Q64632
Original site: Q64632 
ID   ITB4_RAT                Reviewed;        1807 AA.
AC   Q64632;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-FEB-2019, entry version 162.
DE   RecName: Full=Integrin beta-4;
DE   AltName: Full=GP150;
DE   AltName: CD_antigen=CD104;
DE   Flags: Precursor;
GN   Name=Itgb4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Sciatic nerve;
RX   PubMed=9074510; DOI=10.1016/S0378-1119(96)00725-1;
RA   Feltri M.L., Arona M., Scherer S.S., Wrabetz L.;
RT   "Cloning and sequence of the cDNA encoding the beta 4 integrin subunit
RT   in rat peripheral nerve.";
RL   Gene 186:299-304(1997).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773; SER-1071; SER-1121;
RP   SER-1386; SER-1389; SER-1425 AND SER-1776, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. It
CC       plays a critical structural role in the hemidesmosome of
CC       epithelial cells. Is required for the regulation of keratinocyte
CC       polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain)
CC       and this binding is essential for NRG1-ERBB signaling. ITGA6:ITGB4
CC       binds to IGF1 and this binding is essential for IGF1 signaling.
CC       ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2
CC       signaling. {ECO:0000250|UniProtKB:P16144}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-4
CC       associates with alpha-6. Interacts (via cytoplasmic region) with
CC       COL17A1 (via cytoplasmic region). Interacts (via cytoplasmic
CC       region) with DST isoform 3 (via N-terminus). Interacts (via
CC       cytoplasmic domain) with DST (via N-terminus). Interacts with
CC       RAC1. ITGA6:ITGB4 is found in a ternary complex with NRG1 and
CC       ERBB3. ITGA6:ITGB4 is found in a ternary complex with IGF1 and
CC       IGF1R. ITGA6:ITGB4 interacts with IGF2.
CC       {ECO:0000250|UniProtKB:P16144}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction,
CC       hemidesmosome {ECO:0000250}. Note=Colocalizes with DST at the
CC       leading edge of migrating keratinocytes. {ECO:0000250}.
CC   -!- DOMAIN: The fibronectin type-III-like domains bind BPAG1 and
CC       plectin and probably also recruit BP230.
CC   -!- PTM: Palmitoylated by DHHC3 at several cysteines of the membrane-
CC       proximal region, enhancing stability and cell surface expression.
CC       Palmitoylation also promotes secundary association with
CC       tertaspanins (By similarity). {ECO:0000250|UniProtKB:P16144}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; U60096; AAC53094.1; -; mRNA.
DR   PIR; JC6319; JC6319.
DR   RefSeq; NP_037312.1; NM_013180.1.
DR   UniGene; Rn.198908; -.
DR   ProteinModelPortal; Q64632; -.
DR   SMR; Q64632; -.
DR   STRING; 10116.ENSRNOP00000059783; -.
DR   iPTMnet; Q64632; -.
DR   PhosphoSitePlus; Q64632; -.
DR   PaxDb; Q64632; -.
DR   PRIDE; Q64632; -.
DR   GeneID; 25724; -.
DR   KEGG; rno:25724; -.
DR   CTD; 3691; -.
DR   RGD; 2928; Itgb4.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   HOGENOM; HOG000231105; -.
DR   HOVERGEN; HBG006189; -.
DR   InParanoid; Q64632; -.
DR   KO; K06525; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; Q64632; -.
DR   PRO; PR:Q64632; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005938; C:cell cortex; IDA:RGD.
DR   GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; TAS:RGD.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0030056; C:hemidesmosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0050839; F:cell adhesion molecule binding; TAS:RGD.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0031581; P:hemidesmosome assembly; IEA:InterPro.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR   CDD; cd00063; FN3; 4.
DR   Gene3D; 2.60.40.10; -; 4.
DR   Gene3D; 2.60.40.2030; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR038081; CalX-like_sf.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR013032; EGF-like_CS.
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; PTHR10082; 1.
DR   PANTHER; PTHR10082:SF42; PTHR10082:SF42; 1.
DR   Pfam; PF03160; Calx-beta; 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; SSF141072; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69687; SSF69687; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS00243; INTEGRIN_BETA; 2.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell junction; Cell membrane; Complete proteome;
KW   Disulfide bond; Glycoprotein; Integrin; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     27       {ECO:0000250}.
FT   CHAIN        28   1807       Integrin beta-4.
FT                                /FTId=PRO_0000016347.
FT   TOPO_DOM     28    713       Extracellular. {ECO:0000255}.
FT   TRANSMEM    714    734       Helical. {ECO:0000255}.
FT   TOPO_DOM    735   1807       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       29     73       PSI.
FT   DOMAIN      131    340       VWFA.
FT   REPEAT      457    503       I.
FT   REPEAT      504    543       II.
FT   REPEAT      544    582       III.
FT   REPEAT      583    621       IV.
FT   DOMAIN      981   1086       Calx-beta.
FT   DOMAIN     1131   1220       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1224   1323       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1514   1609       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1627   1723       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   REGION      194    199       Involved in NRG1- and IGF1-binding.
FT                                {ECO:0000250|UniProtKB:P16144}.
FT   REGION      457    621       Cysteine-rich tandem repeats.
FT   REGION      734    751       Palmitoylated on several cysteines.
FT                                {ECO:0000250}.
FT   MOD_RES     773    773       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1071   1071       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1121   1121       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1386   1386       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1389   1389       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1405   1405       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P16144}.
FT   MOD_RES    1418   1418       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P16144}.
FT   MOD_RES    1425   1425       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1514   1514       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P16144}.
FT   MOD_RES    1776   1776       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CARBOHYD    327    327       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    492    492       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    580    580       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    619    619       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    697    697       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     30    456       {ECO:0000250}.
FT   DISULFID     38     48       {ECO:0000250}.
FT   DISULFID     41     72       {ECO:0000250}.
FT   DISULFID     51     61       {ECO:0000250}.
FT   DISULFID    245    288       {ECO:0000250}.
FT   DISULFID    424    673       {ECO:0000250}.
FT   DISULFID    453    458       {ECO:0000250}.
FT   DISULFID    469    480       {ECO:0000250}.
FT   DISULFID    477    513       {ECO:0000250}.
FT   DISULFID    482    491       {ECO:0000250}.
FT   DISULFID    493    504       {ECO:0000250}.
FT   DISULFID    519    524       {ECO:0000250}.
FT   DISULFID    521    552       {ECO:0000250}.
FT   DISULFID    526    537       {ECO:0000250}.
FT   DISULFID    558    563       {ECO:0000250}.
FT   DISULFID    565    574       {ECO:0000250}.
FT   DISULFID    576    583       {ECO:0000250}.
FT   DISULFID    597    602       {ECO:0000250}.
FT   DISULFID    599    650       {ECO:0000250}.
FT   DISULFID    604    616       {ECO:0000250}.
FT   DISULFID    628    637       {ECO:0000250}.
FT   DISULFID    634    708       {ECO:0000250}.
FT   DISULFID    653    682       {ECO:0000250}.
SQ   SEQUENCE   1807 AA;  200589 MW;  2EF9BD4E345829A3 CRC64;
     MAGLCSSPWV KLLLAVVLSA GLPGNMANRC KKAQVKSCTE CIRVDKSCAY CTDELFKERR
     CNTQADVLAA GCRGESVLVM ESSLEITENI QIDTSLHRSQ VSPQGLQVRL RPGEERNFVF
     KVFEPLESPV DLYILMDFSN SMSDDLDNLK QMGQNLAKIL RQLTSDYTIG FGKFVDKVSV
     PQTDMRPEKL KEPWPNSDPP FSFKNVISLT ENVEEFWDKL QGERISGNLD APEGGFDAIL
     QTAVCTRDIG WRADSTHLLV FSTESAFHYE ADGANVLAGI MNRNDEKCHL DATGAYTQYK
     TQDYPSVPTL VRLLAKHNII PIFAVTNYSY SYYEKLHKYF PVSSLGVLQE DSSNIVELLE
     EAFYRIRSNL DIRALDSPRG LRTEVTSDTL QKTETGSFHI KRGEVGTYNV HLRAVEDIDG
     THVCQLAKED QRGNIHLKPS FSDGLRMDAS VICDMCACEL QKEVQSARCH YRGDFMCGHC
     VCNEGWSGKT CNCSTGSLSD TQPCLREGED KPCSGHGECQ CGRCVCYGEG RYEGHFCEYD
     NFQCPRTSGF LCNDRGRCSM GECVCEPGWT GRSCDCPLSN ATCIDSNGGI CNGLGFCECG
     RCHCNQRSSL YTDTTCEINY SAIRLGLCED LRSCVQCQAW GTGEKKGRTC EECNFKVKMV
     DELKKAEEVV EYCSFRDEDD DCTYSYTVEG DGSPGPNSTV LVHKKKDCLP APSWWLIPLL
     IFLLLLLVLL LLLCWKYCAC CKACLGLLPC CNQGHMVGFK EDHYMLRENL MASDHLDTPM
     LRSGNLKGRD TVRWKITNNV QRPGFATHAA SISPTELVPY GLSLRLGRLC TENLMKPGTR
     ECDQLRQEVE ENLNEVYRQV NGVHKLQQTK FRQQPNAGKK QDHTIVDTVL LAPRSAKQSL
     LKLTEKQVEQ GSFHELKVAP GYYTLTAEQD ARGMVEFQEG VELVDVRVPL FIRPEDDDEK
     QLLVEAIDVP VGTATLGRRL VNITIIKEQA SGIVSFEQPE YSVSRGDQVA RIPVIRHILD
     NGKSQVSYST QDNTAHGHRD YVPVEGELLF YPGETWKELQ VKLLELQEVD SLLRGRQVRR
     FQVQLSNPKF GARLGQPNTA TVIIGEQDET DRSLINEISA SPPLPRGDLG APQNPNAKAA
     GSRKIHFNWL PPPGKPMGYR VKYWVQGDSE SEAHLLDSKV PSVELTNLYP YCDYEMKVCA
     YGAHGEGPYS SLVSCRTHQE VPSEPGRLAF NVVSSTVTQL SWAEPAETNG EITAYEVCYG
     LVNEDNRPIG PMKKVLVDNP KNRMLLIENL RESQPYRYTV KARNGAGWGP EREAIINLAT
     QPKRPMSIPI IPDIPIVDAQ GGEDYENFLM YSDDVLRSPA SSQRPSVSDD TEHLVNGRMD
     FAYPGSANSL HRMTAANVAY GTHLSPHQTH RMLSTSSTLT RDYHSLTRTD HSQSGTLPRD
     YSTLTSLSSQ GLPPIWEDGR SRLPLSWTLG SWSRAQMKGV PASRGSPDSI ILAGQSAAPS
     WGTDSRGAMG VPDTPTRLVF SALGPTSLKV SWQEPQCDRA LLGYSVEYQL LNGGEMHRLN
     IPNPGQTSVV VEDLLPNHSY VFRVRAQSQE GWGREREGVI TIESQVHPQS PLCPLPGSAF
     TLSTPSAPGP LVFTALSPDS LQLSWERPRR PNGDILGYLV TCEMAQGGGP ARTFRVDGDN
     PESRLTVPGL SENVPYKFKV QARTTEGFGP EREGIITIES QDGGPFPQLG SHSGLFQNPL
     QSEYSTVTST HSTTTTEPFL IDGLTLGTQR LEAGGSLTRH VTQEFVSRTL TTSGSLSTHM
     DQQFFQT
//
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