ITB1_MOUSE
ID ITB1_MOUSE Reviewed; 798 AA.
AC P09055; F6R105; Q3TIW5; Q3TWH6; Q60993; Q61126; Q8BTU0; Q8BVU1;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Integrin beta-1 {ECO:0000305};
DE AltName: Full=Fibronectin receptor subunit beta;
DE AltName: Full=VLA-4 subunit beta;
DE AltName: CD_antigen=CD29;
DE Flags: Precursor;
GN Name=Itgb1 {ECO:0000312|MGI:MGI:96610};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=3262537; DOI=10.1016/0014-5793(88)80503-9;
RA Tominaga S.;
RT "Murine mRNA for the beta-subunit of integrin is increased in BALB/c-3T3
RT cells entering the G1 phase from the G0 state.";
RL FEBS Lett. 238:315-319(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Osteoclast, Placenta, and Thymocyte;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-798 (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=2523953; DOI=10.1084/jem.169.5.1589;
RA Holers V.M., Ruff T.G., Parks D.L., McDonald J.A., Ballard L.L.,
RA Brown E.J.;
RT "Molecular cloning of a murine fibronectin receptor and its expression
RT during inflammation. Expression of VLA-5 is increased in activated
RT peritoneal macrophages in a manner discordant from major histocompatibility
RT complex class II.";
RL J. Exp. Med. 169:1589-1605(1989).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 595-798 (ISOFORM 1).
RX PubMed=2521606; DOI=10.1016/0014-4827(89)90080-3;
RA Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.;
RT "Coordinate induction of fibronectin, fibronectin receptor, tropomyosin,
RT and actin genes in serum-stimulated fibroblasts.";
RL Exp. Cell Res. 180:537-545(1989).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 718-798 (ISOFORM 2), FUNCTION, INTERACTION
RP WITH ITGA7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Myoblast;
RX PubMed=8567725; DOI=10.1083/jcb.132.1.211;
RA Belkin A.M., Zhidkova N.I., Balzac F., Altruda F., Tomatis D., Maier A.,
RA Tarone G., Koteliansky V.E., Burridge K.;
RT "Beta 1D integrin displaces the beta 1A isoform in striated muscles:
RT localization at junctional structures and signaling potential in nonmuscle
RT cells.";
RL J. Cell Biol. 132:211-226(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 723-798.
RC TISSUE=Skeletal muscle;
RX PubMed=8870969; DOI=10.3109/15419069609010759;
RA Baudoin C., Van der Flier A., Borradori L., Sonnenberg A.;
RT "Genomic organization of the mouse beta 1 gene: conservation of the beta 1D
RT but not of the beta 1B and beta 1C integrin splice variants.";
RL Cell Adhes. Commun. 4:1-11(1996).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=9553049; DOI=10.1101/gad.12.8.1202;
RA Baudoin C., Goumans M.J., Mummery C., Sonnenberg A.;
RT "Knockout and knockin of the beta1 exon D define distinct roles for
RT integrin splice variants in heart function and embryonic development.";
RL Genes Dev. 12:1202-1216(1998).
RN [11]
RP FUNCTION, AND INTERACTION WITH CD9.
RX PubMed=10634791; DOI=10.1126/science.287.5451.321;
RA Miyado K., Yamada G., Yamada S., Hasuwa H., Nakamura Y., Ryu F., Suzuki K.,
RA Kosai K., Inoue K., Ogura A., Okabe M., Mekada E.;
RT "Requirement of CD9 on the egg plasma membrane for fertilization.";
RL Science 287:321-324(2000).
RN [12]
RP INTERACTION WITH FBLN5.
RX PubMed=11805835; DOI=10.1038/415171a;
RA Nakamura T., Lozano P.R., Ikeda Y., Iwanaga Y., Hinek A., Minamisawa S.,
RA Cheng C.F., Kobuke K., Dalton N., Takada Y., Tashiro K., Ross J., Honjo T.,
RA Chien K.R.;
RT "Fibulin-5/DANCE is essential for elastogenesis in vivo.";
RL Nature 415:171-175(2002).
RN [13]
RP INTERACTION WITH EMP2.
RX PubMed=12189152; DOI=10.1074/jbc.m206868200;
RA Wadehra M., Iyer R., Goodglick L., Braun J.;
RT "The tetraspan protein epithelial membrane protein-2 interacts with beta1
RT integrins and regulates adhesion.";
RL J. Biol. Chem. 277:41094-41100(2002).
RN [14]
RP FUNCTION, AND INTERACTION WITH NMRK2.
RX PubMed=12941630; DOI=10.1016/s0012-1606(03)00304-x;
RA Li J., Rao H., Burkin D., Kaufman S.J., Wu C.;
RT "The muscle integrin binding protein (MIBP) interacts with alpha7beta1
RT integrin and regulates cell adhesion and laminin matrix deposition.";
RL Dev. Biol. 261:209-219(2003).
RN [15]
RP INTERACTION WITH MDK.
RX PubMed=15466886; DOI=10.1242/jcs.01423;
RA Muramatsu H., Zou P., Suzuki H., Oda Y., Chen G.Y., Sakaguchi N.,
RA Sakuma S., Maeda N., Noda M., Takada Y., Muramatsu T.;
RT "alpha4beta1- and alpha6beta1-integrins are functional receptors for
RT midkine, a heparin-binding growth factor.";
RL J. Cell Sci. 117:5405-5415(2004).
RN [16]
RP FUNCTION, AND INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
RX PubMed=15181153; DOI=10.1091/mbc.e04-03-0236;
RA Fukushi J., Makagiansar I.T., Stallcup W.B.;
RT "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via
RT engagement of galectin-3 and alpha3beta1 integrin.";
RL Mol. Biol. Cell 15:3580-3590(2004).
RN [17]
RP INTERACTION WITH DAB2.
RX PubMed=15734730; DOI=10.1074/jbc.m500974200;
RA Prunier C., Howe P.H.;
RT "Disabled-2 (Dab2) is required for transforming growth factor beta-induced
RT epithelial to mesenchymal transition (EMT).";
RL J. Biol. Chem. 280:17540-17548(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [19]
RP FUNCTION, AND MUTAGENESIS OF TYR-783 AND TYR-795.
RX PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
RA Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H., Grosse R.,
RA Kitzing T., Rantala J.K., Kallioniemi O., Faessler R., Kallio M.,
RA Ivaska J.;
RT "Integrin trafficking regulated by Rab21 is necessary for cytokinesis.";
RL Dev. Cell 15:371-385(2008).
RN [20]
RP INTERACTION WITH FERMT2.
RX PubMed=18483218; DOI=10.1101/gad.469408;
RA Montanez E., Ussar S., Schifferer M., Bosl M., Zent R., Moser M.,
RA Fassler R.;
RT "Kindlin-2 controls bidirectional signaling of integrins.";
RL Genes Dev. 22:1325-1330(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [22]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-363 AND ASN-669.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [24]
RP FUNCTION, AND INTERACTION WITH FGR AND HCK.
RX PubMed=19903482; DOI=10.1016/j.febslet.2009.11.009;
RA Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G.,
RA Berton G.;
RT "c-Abl and Src-family kinases cross-talk in regulation of myeloid cell
RT migration.";
RL FEBS Lett. 584:15-21(2010).
RN [25]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21768292; DOI=10.1083/jcb.201007108;
RA Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D.,
RA Block M.R., Albiges-Rizo C., Bouvard D.;
RT "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT fibronectin deposition.";
RL J. Cell Biol. 194:307-322(2011).
RN [26]
RP INTERACTION WITH LAMB1.
RX PubMed=34427057; DOI=10.1002/jcsm.12767;
RA Luo W., Lin Z., Chen J., Chen G., Zhang S., Liu M., Li H., He D., Liang S.,
RA Luo Q., Zhang D., Nie Q., Zhang X.;
RT "TMEM182 interacts with integrin beta 1 and regulates myoblast
RT differentiation and muscle regeneration.";
RL J. Cachexia Sarcopenia Muscle 12:1704-1723(2021).
CC -!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and
CC alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1
CC and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-
CC E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-
CC 4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-
CC 11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-
CC 4/beta-1 recognizes one or more domains within the alternatively
CC spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1
CC is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1,
CC alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin
CC alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in
CC sperm-egg fusion (PubMed:10634791). Integrin alpha-4/beta-1 is a
CC receptor for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1.
CC Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and
CC osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin.
CC Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and
CC CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP
CC (seprase) at invadopodia plasma membranes in a collagen-dependent
CC manner and hence may participate in the adhesion, formation of
CC invadopodia and matrix degradation processes, promoting cell invasion.
CC Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of
CC endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for
CC vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide
CC array of ligands. When associated with alpha-7/beta-1 integrin,
CC regulates cell adhesion and laminin matrix deposition
CC (PubMed:12941630). Involved in promoting endothelial cell motility and
CC angiogenesis (PubMed:15181153). Involved in osteoblast compaction
CC through the fibronectin fibrillogenesis cell-mediated matrix assembly
CC process and the formation of mineralized bone nodules
CC (PubMed:21768292). May be involved in up-regulation of the activity of
CC kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1,
CC serves as a platform for SRC activation or inactivation. Plays a
CC mechanistic adhesive role during telophase, required for the successful
CC completion of cytokinesis (PubMed:18804435). ITGA4:ITGB1 binds to
CC fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent
CC fractalkine signaling (By similarity). ITGA4:ITGB1 and ITGA5:ITGB1 bind
CC to PLA2G2A via a site (site 2) which is distinct from the classical
CC ligand-binding site (site 1) and this induces integrin conformational
CC changes and enhanced ligand binding to site 1 (By similarity).
CC ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-
CC D-dependent cell adhesion to FBN1 (By similarity). ITGA5:ITGB1 is a
CC receptor for IL1B and binding is essential for IL1B signaling (By
CC similarity). ITGA5:ITGB3 is a receptor for soluble CD40LG and is
CC required for CD40/CD40LG signaling (By similarity). Plays an important
CC role in myoblast differentiation and fusion during skeletal myogenesis
CC (By similarity). {ECO:0000250|UniProtKB:P05556,
CC ECO:0000250|UniProtKB:P07228, ECO:0000269|PubMed:10634791,
CC ECO:0000269|PubMed:12941630, ECO:0000269|PubMed:15181153,
CC ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19903482,
CC ECO:0000269|PubMed:21768292}.
CC -!- FUNCTION: [Isoform 2]: Isoform 2 displaces isoform 1 in striated
CC muscles. {ECO:0000269|PubMed:8567725}.
CC -!- SUBUNIT: Interacts with seprase FAP (seprase); the interaction occurs
CC at the cell surface of invadopodia membrane in a collagen-dependent
CC manner (By similarity). Heterodimer of an alpha and a beta subunit.
CC Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4,
CC alpha-5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or
CC alpha-V. ITGA6:ITGB1 is found in a complex with CD9; interaction takes
CC place in oocytes and is involved in sperm-egg fusion (PubMed:10634791).
CC Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with
CC alpha-5. Interacts with FLNA, FLNB, FLNC and RANBP9. Interacts with
CC KRT1 in the presence of RACK1 and SRC. Interacts with JAML; integrin
CC alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by
CC controlling JAML homodimerization. Interacts with RAB21. Interacts (via
CC the cytoplasmic region) with RAB25 (via the hypervariable C-terminal
CC region). Interacts with MYO10. Interacts with ITGB1BP1 (via C-terminal
CC region); the interaction is a prerequisite for focal adhesion
CC disassembly. Interacts with TLN1; the interaction is prevented by
CC competitive binding of ITGB1BP1. Interacts with ACAP1; required for
CC ITGB1 recycling. Interacts with ASAP3. Interacts with FERMT2; the
CC interaction is inhibited in presence of ITGB1BP1. Interacts with DAB2.
CC Interacts with FGR and HCK. Isoform 2 interacts with alpha-7A and
CC alpha-7B in adult skeletal muscle. Isoform 2 interacts with alpha-7B in
CC cardiomyocytes of adult heart. Interacts with EMP2; the interaction may
CC be direct or indirect and ITGB1 has a heterodimer form
CC (PubMed:12189152). ITGA5:ITGB1 interacts with CCN3 (By similarity).
CC ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and CX3CL1 (By
CC similarity). ITGA5:ITGB1 interacts with FBN1 (By similarity).
CC ITGA5:ITGB1 interacts with IL1B. Interacts with MDK (PubMed:15466886).
CC ITGA4:ITGB1 interacts with MDK; this interaction mediates MDK-induced
CC osteoblast cells migration through PXN phosphorylation
CC (PubMed:15466886). ITGA6:ITGB1 interacts with MDK; this interaction
CC mediates MDK-induced neurite-outgrowth (PubMed:15466886). ITGA5:ITGB1
CC interacts with ACE2 (By similarity). Interacts with TMEM182 (By
CC similarity). Interacts with LAMB1 (PubMed:34427057).
CC {ECO:0000250|UniProtKB:P05556, ECO:0000250|UniProtKB:P07228,
CC ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:12189152,
CC ECO:0000269|PubMed:12941630, ECO:0000269|PubMed:15181153,
CC ECO:0000269|PubMed:15466886, ECO:0000269|PubMed:15734730,
CC ECO:0000269|PubMed:18483218, ECO:0000269|PubMed:19903482,
CC ECO:0000269|PubMed:34427057, ECO:0000269|PubMed:8567725}.
CC -!- INTERACTION:
CC P09055; P26955: Csf2rb; NbExp=2; IntAct=EBI-644224, EBI-1810026;
CC P09055; Q01768: Nme2; NbExp=3; IntAct=EBI-644224, EBI-642573;
CC P09055; Q6F5E0: Tmem158; NbExp=3; IntAct=EBI-644224, EBI-645317;
CC P09055; Q91YD9: Wasl; NbExp=2; IntAct=EBI-644224, EBI-642417;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556};
CC Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type
CC I membrane protein {ECO:0000255}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein
CC {ECO:0000255}. Recycling endosome {ECO:0000269|PubMed:21768292,
CC ECO:0000269|PubMed:8567725}. Melanosome {ECO:0000250|UniProtKB:P05556}.
CC Cell projection, lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell
CC projection, ruffle {ECO:0000250|UniProtKB:P05556}. Cell junction, focal
CC adhesion {ECO:0000250|UniProtKB:P05556}. Cell surface
CC {ECO:0000250|UniProtKB:P05556}. Note=Colocalizes with ITGB1BP1 and
CC metastatic suppressor protein NME2 at the edge or peripheral ruffles
CC and lamellipodia during the early stages of cell spreading on
CC fibronectin or collagen. Translocates from peripheral focal adhesions
CC to fibrillar adhesions in an ITGB1BP1-dependent manner. Enriched
CC preferentially at invadopodia, cell membrane protrusions that
CC correspond to sites of cell invasion, in a collagen-dependent manner.
CC Localized at plasma and ruffle membranes in a collagen-independent
CC manner. {ECO:0000250|UniProtKB:P05556}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane, sarcolemma. Cell
CC junction. Note=In cardiac muscle, isoform 2 is found in costameres and
CC intercalated disks.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Beta-1A {ECO:0000303|PubMed:8567725};
CC IsoId=P09055-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta-1D {ECO:0000303|PubMed:8567725};
CC IsoId=P09055-2; Sequence=VSP_053581, VSP_053582;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in skeletal and cardiac
CC muscles only (at protein level). Isoform 1 is very weakly expressed in
CC striated muscles and not detected in adult skeletal muscle fibers and
CC cardiomyocytes. {ECO:0000269|PubMed:8567725}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is not detected in proliferating
CC myoblasts, but it appears immediately after myoblast fusion and its
CC amount continues to rise during myotube growth and maturation reaching
CC its highest level at day 9 through day 10, when mature differentiated
CC myotubes appear in cell culture. Isoform 1 expression is down-regulated
CC during myodifferentiation in culture and it is completely displaced by
CC isoform 2 in mature differentiated myotubes.
CC {ECO:0000269|PubMed:8567725}.
CC -!- PTM: The cysteine residues are involved in intrachain disulfide bonds.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Isoform 2 knockout mice are viable and fertile,
CC but male mice display a mild abnormality of cardiac function reflected
CC by an increased expression of atrial natriuretic peptide and beta
CC myosin heavy chain. Muscles do not show any histological or
CC ultrastructural alterations. Replacement of isoform 1 by isoform 2
CC results in embryonic lethality before 16.5 dpc with a plethora of
CC developmental defects including open neural tube, which is abnormally
CC waved both rostrally and caudally. Some embryos lack part of the
CC hindbrain and in most embryos the first branchial arch is shortened,
CC which in some of the embryos leaves the tongue exposed. Abnormally
CC strong fibronectin staining is seen in the mesenchyme under the open
CC neural tube. Extravasation of red blood cells is evident in various
CC tissues and they are also found in the pericardial cavity. Choroid
CC plexus is virtually absent correlating with the presence of an
CC abnormally smooth head and small brain cavities. At later developmental
CC stages, a striking feature is the lack of a lower jaw and a dysmorphic
CC lower face. These defects are in part caused by the abnormal migration
CC of neuroepithelial cells. {ECO:0000269|PubMed:9553049}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36379.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y00769; CAA68738.1; -; mRNA.
DR EMBL; AK076526; BAC36379.1; ALT_INIT; mRNA.
DR EMBL; AK088729; BAC40532.1; -; mRNA.
DR EMBL; AK159689; BAE35290.1; -; mRNA.
DR EMBL; AK167682; BAE39731.1; -; mRNA.
DR EMBL; AC156608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11832.1; -; Genomic_DNA.
DR EMBL; BC050906; AAH50906.1; -; mRNA.
DR EMBL; X15202; CAA33272.1; -; mRNA.
DR EMBL; U37029; AAA80243.1; -; mRNA.
DR EMBL; U47283; AAA88821.1; -; Genomic_DNA.
DR CCDS; CCDS22791.1; -. [P09055-1]
DR PIR; PL0104; IJMSFB.
DR PIR; S01659; S01659.
DR RefSeq; NP_034708.1; NM_010578.2. [P09055-1]
DR PDB; 5XQ0; X-ray; 2.75 A; A/B=784-798.
DR PDBsum; 5XQ0; -.
DR AlphaFoldDB; P09055; -.
DR BMRB; P09055; -.
DR SMR; P09055; -.
DR BioGRID; 200826; 122.
DR ComplexPortal; CPX-3027; Integrin alpha5-beta1 complex.
DR ComplexPortal; CPX-3114; Integrin alpha1-beta1 complex.
DR ComplexPortal; CPX-3115; Integrin alpha2-beta1 complex.
DR ComplexPortal; CPX-3117; Integrin alpha3-beta1 complex.
DR ComplexPortal; CPX-3118; integrin alpha4-beta1 complex.
DR ComplexPortal; CPX-3119; Integrin alpha6-beta1 complex.
DR ComplexPortal; CPX-3121; Integrin alpha7-beta1 complex.
DR ComplexPortal; CPX-3122; Integrin alpha8-beta1 complex.
DR ComplexPortal; CPX-3123; Integrin alpha9-beta1 complex.
DR ComplexPortal; CPX-3124; Integrin alpha10-beta1 complex.
DR ComplexPortal; CPX-3125; Integrin alpha11-beta1 complex.
DR ComplexPortal; CPX-3130; Integrin alphav-beta1 complex.
DR CORUM; P09055; -.
DR DIP; DIP-46247N; -.
DR IntAct; P09055; 58.
DR MINT; P09055; -.
DR STRING; 10090.ENSMUSP00000087457; -.
DR GlyConnect; 2403; 8 N-Linked glycans (3 sites).
DR GlyGen; P09055; 12 sites, 8 N-linked glycans (3 sites).
DR iPTMnet; P09055; -.
DR PhosphoSitePlus; P09055; -.
DR SwissPalm; P09055; -.
DR EPD; P09055; -.
DR jPOST; P09055; -.
DR MaxQB; P09055; -.
DR PaxDb; P09055; -.
DR PeptideAtlas; P09055; -.
DR PRIDE; P09055; -.
DR ProteomicsDB; 268897; -. [P09055-1]
DR ProteomicsDB; 268898; -. [P09055-2]
DR Antibodypedia; 3126; 2934 antibodies from 52 providers.
DR DNASU; 16412; -.
DR Ensembl; ENSMUST00000090006; ENSMUSP00000087457; ENSMUSG00000025809. [P09055-1]
DR GeneID; 16412; -.
DR KEGG; mmu:16412; -.
DR UCSC; uc009nzv.2; mouse. [P09055-1]
DR CTD; 3688; -.
DR MGI; MGI:96610; Itgb1.
DR VEuPathDB; HostDB:ENSMUSG00000025809; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01030000234611; -.
DR HOGENOM; CLU_011772_2_1_1; -.
DR InParanoid; P09055; -.
DR OMA; NCVCGAC; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; P09055; -.
DR TreeFam; TF105392; -.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-1566977; Fibronectin matrix formation.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-3000170; Syndecan interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR Reactome; R-MMU-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8875513; MET interacts with TNS proteins.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9634597; GPER1 signaling.
DR BioGRID-ORCS; 16412; 10 hits in 77 CRISPR screens.
DR ChiTaRS; Itgb1; mouse.
DR PRO; PR:P09055; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P09055; protein.
DR Bgee; ENSMUSG00000025809; Expressed in ileal epithelium and 285 other tissues.
DR ExpressionAtlas; P09055; baseline and differential.
DR Genevisible; P09055; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0097386; C:glial cell projection; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030056; C:hemidesmosome; ISO:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099699; C:integral component of synaptic membrane; IDA:SynGO.
DR GO; GO:0034665; C:integrin alpha1-beta1 complex; ISO:MGI.
DR GO; GO:0034680; C:integrin alpha10-beta1 complex; ISO:MGI.
DR GO; GO:0034681; C:integrin alpha11-beta1 complex; ISO:MGI.
DR GO; GO:0034666; C:integrin alpha2-beta1 complex; ISO:MGI.
DR GO; GO:0034667; C:integrin alpha3-beta1 complex; ISO:MGI.
DR GO; GO:0034674; C:integrin alpha5-beta1 complex; ISO:MGI.
DR GO; GO:0034677; C:integrin alpha7-beta1 complex; IDA:MGI.
DR GO; GO:0034679; C:integrin alpha9-beta1 complex; ISO:MGI.
DR GO; GO:0008305; C:integrin complex; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0035748; C:myelin sheath abaxonal region; IDA:BHF-UCL.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0097060; C:synaptic membrane; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0019960; F:C-X3-C chemokine binding; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IPI:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0043236; F:laminin binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0048675; P:axon extension; IMP:MGI.
DR GO; GO:0071711; P:basement membrane organization; IMP:CAFA.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0007161; P:calcium-independent cell-matrix adhesion; ISO:MGI.
DR GO; GO:0060912; P:cardiac cell fate specification; IMP:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IMP:MGI.
DR GO; GO:0023035; P:CD40 signaling pathway; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0030030; P:cell projection organization; ISO:MGI.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:MGI.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR GO; GO:0021943; P:formation of radial glial scaffolds; IMP:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0008354; P:germ cell migration; IMP:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0048626; P:myoblast fate specification; IMP:MGI.
DR GO; GO:0007520; P:myoblast fusion; ISS:UniProtKB.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0031345; P:negative regulation of cell projection organization; ISO:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IGI:MGI.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:MGI.
DR GO; GO:0051951; P:positive regulation of glutamate uptake involved in transmission of nerve impulse; IMP:ARUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; ISO:MGI.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
DR GO; GO:0032594; P:protein transport within lipid bilayer; ISO:MGI.
DR GO; GO:0150103; P:reactive gliosis; IMP:ARUK-UCL.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:0010710; P:regulation of collagen catabolic process; ISS:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:1901979; P:regulation of inward rectifier potassium channel activity; IMP:ARUK-UCL.
DR GO; GO:0150003; P:regulation of spontaneous synaptic transmission; IMP:ARUK-UCL.
DR GO; GO:0045214; P:sarcomere organization; IMP:MGI.
DR GO; GO:0001894; P:tissue homeostasis; ISO:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR027071; Integrin_beta-1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF28; PTHR10082:SF28; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell adhesion;
KW Cell junction; Cell membrane; Cell projection; Disulfide bond; Endosome;
KW Glycoprotein; Integrin; Isopeptide bond; Magnesium; Membrane;
KW Metal-binding; Myogenesis; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..20
FT CHAIN 21..798
FT /note="Integrin beta-1"
FT /id="PRO_0000016335"
FT TOPO_DOM 21..728
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 729..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 140..378
FT /note="VWFA"
FT REPEAT 466..515
FT /note="I"
FT REPEAT 516..559
FT /note="II"
FT REPEAT 560..598
FT /note="III"
FT REPEAT 599..635
FT /note="IV"
FT REGION 76..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..213
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT REGION 295..314
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT REGION 383..465
FT /note="Interaction with TMEM182"
FT /evidence="ECO:0000250|UniProtKB:P07228"
FT REGION 466..635
FT /note="Cysteine-rich tandem repeats"
FT REGION 762..767
FT /note="Signal for sorting from recycling endosomes;
FT interaction with ACAP1"
FT /evidence="ECO:0000250"
FT REGION 785..792
FT /note="Interaction with ITGB1BP1"
FT /evidence="ECO:0000250"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 777
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 783
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 789
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 794
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT DISULFID 27..45
FT /evidence="ECO:0000250"
FT DISULFID 35..464
FT /evidence="ECO:0000250"
FT DISULFID 38..75
FT /evidence="ECO:0000250"
FT DISULFID 48..64
FT /evidence="ECO:0000250"
FT DISULFID 207..213
FT /evidence="ECO:0000250"
FT DISULFID 261..301
FT /evidence="ECO:0000250"
FT DISULFID 401..415
FT /evidence="ECO:0000250"
FT DISULFID 435..462
FT /evidence="ECO:0000250"
FT DISULFID 466..691
FT /evidence="ECO:0000250"
FT DISULFID 477..489
FT /evidence="ECO:0000250"
FT DISULFID 486..525
FT /evidence="ECO:0000250"
FT DISULFID 491..500
FT /evidence="ECO:0000250"
FT DISULFID 502..516
FT /evidence="ECO:0000250"
FT DISULFID 531..536
FT /evidence="ECO:0000250"
FT DISULFID 533..568
FT /evidence="ECO:0000250"
FT DISULFID 538..553
FT /evidence="ECO:0000250"
FT DISULFID 555..560
FT /evidence="ECO:0000250"
FT DISULFID 574..579
FT /evidence="ECO:0000250"
FT DISULFID 576..607
FT /evidence="ECO:0000250"
FT DISULFID 581..590
FT /evidence="ECO:0000250"
FT DISULFID 592..599
FT /evidence="ECO:0000250"
FT DISULFID 613..618
FT /evidence="ECO:0000250"
FT DISULFID 615..661
FT /evidence="ECO:0000250"
FT DISULFID 620..630
FT /evidence="ECO:0000250"
FT DISULFID 633..636
FT /evidence="ECO:0000250"
FT DISULFID 640..649
FT /evidence="ECO:0000250"
FT DISULFID 646..723
FT /evidence="ECO:0000250"
FT DISULFID 665..699
FT /evidence="ECO:0000250"
FT CROSSLNK 794
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT VAR_SEQ 778
FT /note="G -> Q (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8567725"
FT /id="VSP_053581"
FT VAR_SEQ 786..798
FT /note="AVTTVVNPKYEGK -> PINNFKNPNYGRKAGL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8567725"
FT /id="VSP_053582"
FT MUTAGEN 783
FT /note="Y->F: Reduced endocytosis; when associated with F-
FT 795."
FT /evidence="ECO:0000269|PubMed:18804435"
FT MUTAGEN 795
FT /note="Y->F: Reduced endocytosis; when associated with F-
FT 783."
FT /evidence="ECO:0000269|PubMed:18804435"
FT CONFLICT 5
FT /note="L -> Q (in Ref. 2; BAC40532)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="K -> E (in Ref. 2; BAE35290)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="E -> D (in Ref. 2; BAC36379)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="E -> P (in Ref. 6; CAA33272)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="G -> A (in Ref. 6; CAA33272)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="G -> E (in Ref. 2; BAC36379)"
FT /evidence="ECO:0000305"
FT CONFLICT 443..445
FT /note="IKI -> HSKL (in Ref. 6; CAA33272)"
FT /evidence="ECO:0000305"
FT STRAND 788..791
FT /evidence="ECO:0007829|PDB:5XQ0"
SQ SEQUENCE 798 AA; 88231 MW; 26788F7F0A168B56 CRC64;
MNLQLVSWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN TTFLQEGMPT
SARCDDLEAL KKKGCQPSDI ENPRGSQTIK KNKNVTNRSK GMAEKLRPED ITQIQPQQLL
LKLRSGEPQK FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTDRGE FFNELVGQQR
ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
CHLENNVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
SGNSSNVIQL IIDAYNSLSS EVILENSKLP DGVTINYKSY CKNGVNGTGE NGRKCSNISI
GDEVQFEISI TANKCPNKES ETIKIKPLGF TEEVEVVLQF ICKCNCQSHG IPASPKCHEG
NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK
RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCRCRVCE CYPNYTGSAC DCSLDTGPCL
ASNGQICNGR GICECGACKC TDPKFQGPTC ETCQTCLGVC AEHKECVQCR AFNKGEKKDT
CAQECSHFNL TKVESREKLP QPVQVDPVTH CKEKDIDDCW FYFTYSVNGN NEAIVHVVET
PDCPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN
PIYKSAVTTV VNPKYEGK
