ID ITB4_MOUSE Reviewed; 1818 AA.
AC A2A863; A2A865; A2A866; Q6PCS0; Q8R3J1; Q91W15;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 01-MAY-2013, entry version 65.
DE RecName: Full=Integrin beta-4;
DE AltName: CD_antigen=CD104;
DE Flags: Precursor;
GN Name=Itgb4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8359687; DOI=10.1016/0378-1119(93)90421-X;
RA Kennel S.J., Foote L.J., Cimino L., Rizzo M.G., Chang L.Y., Sacchi A.;
RT "Sequence of a cDNA encoding the beta 4 subunit of murine integrin.";
RL Gene 130:209-216(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-1818 (ISOFORM 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 (By similarity).
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 RAC1
CC (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein (By similarity). Cell junction, hemidesmosome (By
CC similarity). Note=Colocalizes with DST at the leading edge of
CC migrating keratinocytes (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2A863-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A863-2; Sequence=VSP_037636;
CC Name=3;
CC IsoId=A2A863-3; Sequence=VSP_037636, VSP_037637;
CC -!- DOMAIN: The fibronectin type-III-like domains bind BPAG1 and
CC plectin and probably also recruit BP230 (By similarity).
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC -!- SIMILARITY: Contains 1 Calx-beta domain.
CC -!- SIMILARITY: Contains 4 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 1 PSI domain.
CC -!- SIMILARITY: Contains 1 VWFA domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL607108; CAM24050.1; -; Genomic_DNA.
DR EMBL; AL645647; CAM24050.1; JOINED; Genomic_DNA.
DR EMBL; AL607108; CAM24052.1; -; Genomic_DNA.
DR EMBL; AL645647; CAM24052.1; JOINED; Genomic_DNA.
DR EMBL; AL607108; CAM24053.1; -; Genomic_DNA.
DR EMBL; AL645647; CAM24053.1; JOINED; Genomic_DNA.
DR EMBL; BC006632; AAH06632.1; -; mRNA.
DR EMBL; BC025194; AAH25194.1; -; mRNA.
DR EMBL; BC059192; AAH59192.1; -; mRNA.
DR IPI; IPI00313479; -.
DR IPI; IPI00480458; -.
DR IPI; IPI00649251; -.
DR PIR; JN0786; JN0786.
DR UniGene; Mm.213873; -.
DR ProteinModelPortal; A2A863; -.
DR SMR; A2A863; 29-711, 933-1111, 1128-1340, 1515-1737.
DR PhosphoSite; A2A863; -.
DR PaxDb; A2A863; -.
DR PRIDE; A2A863; -.
DR Ensembl; ENSMUST00000068981; ENSMUSP00000070811; ENSMUSG00000020758.
DR Ensembl; ENSMUST00000106458; ENSMUSP00000102066; ENSMUSG00000020758.
DR Ensembl; ENSMUST00000106460; ENSMUSP00000102068; ENSMUSG00000020758.
DR Ensembl; ENSMUST00000106461; ENSMUSP00000102069; ENSMUSG00000020758.
DR UCSC; uc007mji.1; mouse.
DR MGI; MGI:96613; Itgb4.
DR eggNOG; NOG303049; -.
DR GeneTree; ENSGT00700000104058; -.
DR HOGENOM; HOG000231105; -.
DR InParanoid; A2A863; -.
DR OMA; EDDDCTY; -.
DR ChiTaRS; ITGB4; mouse.
DR ArrayExpress; A2A863; -.
DR Bgee; A2A863; -.
DR Genevestigator; A2A863; -.
DR GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0030056; C:hemidesmosome; IDA:MGI.
DR GO; GO:0008305; C:integrin complex; IDA:MGI.
DR GO; GO:0004872; F:receptor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0046847; P:filopodium assembly; IMP:MGI.
DR GO; GO:0031581; P:hemidesmosome assembly; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007275; P:multicellular organismal development; IEA:InterPro.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR012013; Integrin_bsu-4.
DR InterPro; IPR002369; Integrin_bsu_N.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR003659; Plexin-like.
DR InterPro; IPR016201; Plexin-like_fold.
DR InterPro; IPR002035; VWF_A.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF6; PTHR10082:SF6; 1.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 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; SM00423; PSI; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49265; FN_III-like; 4.
DR SUPFAM; SSF69687; Integrin_bsu_tail; 1.
DR SUPFAM; SSF103575; Plexin-like_fold; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; UNKNOWN_2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
DR PROSITE; PS50234; VWFA; FALSE_NEG.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell junction; Complete proteome;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 28 By similarity.
FT CHAIN 29 1818 Integrin beta-4.
FT /FTId=PRO_0000379078.
FT TOPO_DOM 29 712 Extracellular (Potential).
FT TRANSMEM 713 733 Helical; (Potential).
FT TOPO_DOM 734 1818 Cytoplasmic (Potential).
FT DOMAIN 30 74 PSI.
FT DOMAIN 132 310 VWFA.
FT REPEAT 458 504 I.
FT REPEAT 505 544 II.
FT REPEAT 545 583 III.
FT REPEAT 584 621 IV.
FT DOMAIN 981 1086 Calx-beta.
FT DOMAIN 1128 1217 Fibronectin type-III 1.
FT DOMAIN 1222 1320 Fibronectin type-III 2.
FT DOMAIN 1524 1614 Fibronectin type-III 3.
FT DOMAIN 1637 1730 Fibronectin type-III 4.
FT REGION 458 621 Cysteine-rich tandem repeats.
FT MOTIF 473 475 Cell attachment site (Potential).
FT MOTIF 1005 1007 Cell attachment site (Potential).
FT MOD_RES 1526 1526 Phosphothreonine (By similarity).
FT CARBOHYD 328 328 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 493 493 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 581 581 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 619 619 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 697 697 N-linked (GlcNAc...) (Potential).
FT DISULFID 31 457 By similarity.
FT DISULFID 39 49 By similarity.
FT DISULFID 42 73 By similarity.
FT DISULFID 52 62 By similarity.
FT DISULFID 246 289 By similarity.
FT DISULFID 425 673 By similarity.
FT DISULFID 454 459 By similarity.
FT DISULFID 470 481 By similarity.
FT DISULFID 478 514 By similarity.
FT DISULFID 483 492 By similarity.
FT DISULFID 494 505 By similarity.
FT DISULFID 520 525 By similarity.
FT DISULFID 522 553 By similarity.
FT DISULFID 527 538 By similarity.
FT DISULFID 559 564 By similarity.
FT DISULFID 566 575 By similarity.
FT DISULFID 577 584 By similarity.
FT DISULFID 598 603 By similarity.
FT DISULFID 600 650 By similarity.
FT DISULFID 605 616 By similarity.
FT DISULFID 628 637 By similarity.
FT DISULFID 634 708 By similarity.
FT DISULFID 653 682 By similarity.
FT VAR_SEQ 1372 1436 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_037636.
FT VAR_SEQ 1515 1515 Q -> QGLPPIWEDGRSRLPLSWTLGSLSRAHMKGVPASRG
FT SPDSIILAGQSAAPSWGT (in isoform 3).
FT /FTId=VSP_037637.
FT CONFLICT 17 17 A -> R (in Ref. 1).
FT CONFLICT 67 68 EL -> DV (in Ref. 1).
FT CONFLICT 94 94 D -> V (in Ref. 1).
FT CONFLICT 113 113 P -> R (in Ref. 1).
FT CONFLICT 118 118 S -> T (in Ref. 1).
FT CONFLICT 624 624 Missing (in Ref. 1).
FT CONFLICT 666 666 Missing (in Ref. 1).
FT CONFLICT 709 713 PPGSF -> LPAPS (in Ref. 1).
FT CONFLICT 851 851 E -> K (in Ref. 3; AAH59192).
FT CONFLICT 877 877 T -> A (in Ref. 1 and 3; AAH06632/
FT AAH59192).
FT CONFLICT 972 972 G -> S (in Ref. 1).
FT CONFLICT 1105 1107 Missing (in Ref. 1).
FT CONFLICT 1204 1204 Q -> K (in Ref. 1).
FT CONFLICT 1292 1292 E -> D (in Ref. 1).
FT CONFLICT 1537 1537 P -> R (in Ref. 1).
FT CONFLICT 1552 1552 M -> T (in Ref. 1 and 3; AAH06632/
FT AAH25194/AAH59192).
FT CONFLICT 1564 1566 NGG -> TCV (in Ref. 1).
FT CONFLICT 1590 1592 HSY -> YSH (in Ref. 1).
FT CONFLICT 1653 1653 L -> P (in Ref. 1).
FT CONFLICT 1662 1663 RP -> SR (in Ref. 1).
FT CONFLICT 1744 1744 H -> N (in Ref. 1).
FT CONFLICT 1759 1759 V -> M (in Ref. 3; AAH25194).
SQ SEQUENCE 1818 AA; 201650 MW; CA41A7E6B4E20B59 CRC64;
MAGPCCSPWV KLLLLAAMLS ASLPGDLANR CKKAQVKSCT ECIRVDKSCA YCTDELFKER
RCNTQAELLA AGCRGESILV MESSLEITEN TQIDTSLHRS QVSPQGLQVR LRPGEERSFV
FQVFEPLESP VDLYILMDFS NSMSDDLDNL KQMGQNLAKI LRQLTSDYTI GFGKFVDKVS
VPQTDMRPEK LKEPWPNSDP PFSFKNVISL TENVEEFWNK LQGERISGNL DAPEGGFDAI
LQTAVCTRDI GWRADSTHLL VFSTESAFHY EADGANVLAG IMNRNDEKCH LDASGAYTQY
KTQDYPSVPT LVRLLAKHNI IPIFAVTNYS YSYYEKLHKY FPVSSLGVLQ EDSSNIVELL
EEAFYRIRSN LDIRALDSPR GLRTEVTSDT LQKTETGSFH IKRGEVGTYN VHLRAVEDID
GTHVCQLAKE DQGGNIHLKP SFSDGLRMDA SVICDVCPCE LQKEVRSARC HFRGDFMCGH
CVCNEGWSGK TCNCSTGSLS DTQPCLREGE DKPCSGHGEC QCGRCVCYGE GRYEGHFCEY
DNFQCPRTSG FLCNDRGRCS MGECVCEPGW TGRSCDCPLS NATCIDSNGG ICNGRGYCEC
GRCHCNQQSL YTDTTCEINY SAIRLGLCED LRSCVQCQAW GTGEKKGRAC DDCPFKVKMV
DELKKAEEVV EYCSFRDEDD DCTYSYNVEG DGSPGPNSTV LVHKKKDCPP GSFWWLIPLL
IFLLLLLALL LLLCWKYCAC CKACLGLLPC CNRGHMVGFK EDHYMLRENL MASDHLDTPM
LRSGNLKGRD TVRWKITNNV QRPGFATHAA STSPTELVPY GLSLRLGRLC TENLMKPGTR
ECDQLRQEVE ENLNEVYRQV SGAHKLQQTK FRQQPNTGKK QDHTIVDTVL LAPRSAKQML
LKLTEKQVEQ GSFHELKVAP GYYTVTAEQD ARGMVEFQEG VELVDVRVPL FIRPEDDDEK
QLLVEAIDVP VGTATLGRRL VNITIIKEQA SGVVSFEQPE YSVSRGDQVA RIPVIRHILD
NGKSQVSYST QDNTAHGHRD YVPVEGELLF HPGETWKELQ VKLLELQEVD SLLRGRQVRR
FQVQLSNPKF GARLGQPSTT TVILGEHDET DRSLINQTLS SPPPPHGDLG APQNPNAKAA
GSRKIHFNWL PPPGKPMGYR VKYWIQGDSE SEAHLLDSKV PSVELTNLYP YCDYEMKVCA
YGAQGEGPYS SLVSCRTHQE VPSEPGRLAF NVVSSTVTQL SWAEPAETNG EITAYEVCYG
LVNEDNRPIG PMKKVLVDNP KNRMLLIENL RESQPYRYTV KARNGAGWGP EREAIINLAT
QPKRPMSIPI IPDIPIVDAQ GGEDYENFLM YSDDVLRSPA SSQRPSVSDD TGCGWKFEPL
LGEELDLRRV TWRLPPELIP RLSASSGRSD EDGSVAGGVE GEGSGWIRGA TPRPPGEHLV
NGRMDFAYPG SANSLHRMTA ANVAYGTHLS PHLSHRVLST SSTLTRDYHS LTRTEHSHSG
TLPRDYSTLT SLSSQDSRGA VGVPDTPTRL VFSALGPTSL KVSWQEPQCD RMLLGYSVEY
QLLNGGEMHR LNIPNPGQTS VVVEDLLPNH SYVFRVRAQS QEGWGREREG VITIESQVHP
QSPLCPLPGS AFTLSTPSAP GPLVFTALSP DSLQLSWERP RRPNGDILGY LVTCEMAQGG
APARTFRVDG DNPESRLTVP GLSENVPYKF KVQARTTEGF GPEREGIITI ESQVGGPFPQ
LGSHSGLFQN PVQSEFSSVT STHSTTTEPF LMDGLTLGTQ RLEAGGSLTR HVTQEFVTRT
LTASGSLSTH MDQQFFQT
//
