GenomeNet

Database: UniProt
Entry: P09055
LinkDB: P09055
Original site: P09055 
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   10-APR-2019, entry version 207.
DE   RecName: Full=Integrin beta-1;
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;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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-
RT   3T3 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;
RC   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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
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   [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
RT   project: 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
RT   histocompatibility 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,
RT   tropomyosin, 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,
RP   INTERACTION WITH ITGA7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL 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.,
RA   Maier A., 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
RT   nonmuscle 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;
RA   Baudoin C., Van der Flier A., Borradori L., Sonnenberg A.;
RT   "Genomic organization of the mouse beta 1 gene: conservation of the
RT   beta 1D 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
RT   development.";
RL   Genes Dev. 12:1202-1216(1998).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH CD9.
RX   PubMed=10634791;
RA   Miyado K., Yamada G., Yamada S., Hasuwa H., Nakamura Y., Ryu F.,
RA   Suzuki K., 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.,
RA   Minamisawa S., Cheng C.F., Kobuke K., Dalton N., Takada Y.,
RA   Tashiro K., Ross J., Honjo T., 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
RT   beta1 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   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
RT   via engagement of galectin-3 and alpha3beta1 integrin.";
RL   Mol. Biol. Cell 15:3580-3590(2004).
RN   [16]
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-
RT   induced epithelial to mesenchymal transition (EMT).";
RL   J. Biol. Chem. 280:17540-17548(2005).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, AND IDENTIFICATION
RP   BY 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   [18]
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.,
RA   Grosse R., Kitzing T., Rantala J.K., Kallioniemi O., Faessler R.,
RA   Kallio M., Ivaska J.;
RT   "Integrin trafficking regulated by Rab21 is necessary for
RT   cytokinesis.";
RL   Dev. Cell 15:371-385(2008).
RN   [19]
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   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, AND IDENTIFICATION
RP   BY 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   [21]
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.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   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   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [23]
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   [24]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21768292; DOI=10.1083/jcb.201007108;
RA   Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A.,
RA   Mosher D., 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).
CC   -!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-
CC       1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-
CC       1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated
CC       sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-
CC       3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-
CC       10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for
CC       fibronectin. Alpha-4/beta-1 recognizes one or more domains within
CC       the alternatively spliced CS-1 and CS-5 regions of fibronectin.
CC       Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin
CC       alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1
CC       are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1)
CC       is present in oocytes and is involved in sperm-egg fusion
CC       (PubMed:10634791). Integrin alpha-4/beta-1 is a receptor for VCAM1
CC       and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-
CC       9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It
CC       recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin
CC       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
CC       invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation
CC       by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1
CC       is a receptor for vitronectin. Beta-1 integrins recognize the
CC       sequence R-G-D in a wide array of ligands. When associated with
CC       alpha-7/beta-1 integrin, regulates cell adhesion and laminin
CC       matrix deposition (PubMed:12941630). Involved in promoting
CC       endothelial cell motility and angiogenesis (PubMed:15181153).
CC       Involved in osteoblast compaction through the fibronectin
CC       fibrillogenesis cell-mediated matrix assembly process and the
CC       formation of mineralized bone nodules (PubMed:21768292). May be
CC       involved in up-regulation of the activity of kinases such as PKC
CC       via binding to KRT1. Together with KRT1 and RACK1, serves as a
CC       platform for SRC activation or inactivation. Plays a mechanistic
CC       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-
CC       dependent fractalkine signaling (By similarity). ITGA4:ITGB1 and
CC       ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct
CC       from the classical ligand-binding site (site 1) and this induces
CC       integrin conformational changes and enhanced ligand binding to
CC       site 1 (By similarity). ITGA5:ITGB1 acts as a receptor for
CC       fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to
CC       FBN1 (By similarity). ITGA5:ITGB1 is a receptor for IL1B and
CC       binding is essential for IL1B signaling (By similarity).
CC       {ECO:0000250|UniProtKB:P05556, 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
CC       occurs at the cell surface of invadopodia membrane in a collagen-
CC       dependent manner (By similarity). Heterodimer of an alpha and a
CC       beta subunit. Beta-1 associates with either alpha-1, alpha-2,
CC       alpha-3, alpha-4, alpha-5, alpha-6, alpha-7, alpha-8, alpha-9,
CC       alpha-10, alpha-11 or alpha-V. ITGA6:ITGB1 is found in a complex
CC       with CD9; interaction takes place in oocytes and is involved in
CC       sperm-egg fusion (PubMed:10634791). Binds LGALS3BP and NMRK2, when
CC       associated with alpha-7, but not with alpha-5. Interacts with
CC       FLNA, FLNB, FLNC and RANBP9. Interacts with KRT1 in the presence
CC       of RACK1 and SRC. Interacts with JAML; integrin alpha-4/beta-1 may
CC       regulate leukocyte to endothelial cells adhesion by controlling
CC       JAML homodimerization. Interacts with RAB21. Interacts (via the
CC       cytoplasmic region) with RAB25 (via the hypervariable C-terminal
CC       region). Interacts with MYO10. Interacts with ITGB1BP1 (via C-
CC       terminal region); the interaction is a prerequisite for focal
CC       adhesion disassembly. Interacts with TLN1; the interaction is
CC       prevented by competitive binding of ITGB1BP1. Interacts with
CC       ACAP1; required for ITGB1 recycling. Interacts with ASAP3.
CC       Interacts with FERMT2; the interaction is inhibited in presence of
CC       ITGB1BP1. Interacts with DAB2. Interacts with FGR and HCK. Isoform
CC       2 interacts with alpha-7A and alpha-7B in adult skeletal muscle.
CC       Isoform 2 interacts with alpha-7B in cardiomyocytes of adult
CC       heart. Interacts with EMP2; the interaction may be direct or
CC       indirect and ITGB1 has an heterodimer form (PubMed:12189152).
CC       ITGA5:ITGB1 interacts with CCN3 (By similarity). ITGA4:ITGB1 is
CC       found in a ternary complex with CX3CR1 and CX3CL1 (By similarity).
CC       ITGA5:ITGB1 interacts with FBN1 (By similarity). ITGA5:ITGB1
CC       interacts with IL1B. {ECO:0000250|UniProtKB:P05556,
CC       ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:12189152,
CC       ECO:0000269|PubMed:12941630, ECO:0000269|PubMed:15181153,
CC       ECO:0000269|PubMed:15734730, ECO:0000269|PubMed:18483218,
CC       ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:8567725}.
CC   -!- INTERACTION:
CC       P26955:Csf2rb; NbExp=2; IntAct=EBI-644224, EBI-1810026;
CC       Q01768:Nme2; NbExp=3; IntAct=EBI-644224, EBI-642573;
CC       Q6F5E0:Tmem158; NbExp=3; IntAct=EBI-644224, EBI-645317;
CC       Q91YD9:Wasl; NbExp=2; IntAct=EBI-644224, EBI-642417;
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Cell projection, invadopodium membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Cell projection, ruffle membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Recycling endosome
CC       {ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:8567725}.
CC       Melanosome {ECO:0000250|UniProtKB:P05556}. Cell projection,
CC       lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell projection,
CC       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
CC       ruffles and lamellipodia during the early stages of cell spreading
CC       on fibronectin or collagen. Translocates from peripheral focal
CC       adhesions to fibrillar adhesions in an ITGB1BP1-dependent manner.
CC       Enriched preferentially at invadopodia, cell membrane protrusions
CC       that correspond to sites of cell invasion, in a collagen-dependent
CC       manner. Localized at plasma and ruffle membranes in a collagen-
CC       independent 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
CC       and intercalated disks.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Beta-1A;
CC         IsoId=P09055-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta-1D;
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
CC       expressed in striated muscles and not detected in adult skeletal
CC       muscle fibers and 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
CC       its amount continues to rise during myotube growth and maturation
CC       reaching its highest level at day 9 through day 10, when mature
CC       differentiated myotubes appear in cell culture. Isoform 1
CC       expression is down-regulated during myodifferentiation in culture
CC       and it is completely displaced by isoform 2 in mature
CC       differentiated myotubes. {ECO:0000269|PubMed:8567725}.
CC   -!- PTM: The cysteine residues are involved in intrachain disulfide
CC       bonds. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Isoform 2 knockout mice are viable and
CC       fertile, but male mice display a mild abnormality of cardiac
CC       function reflected by an increased expression of atrial
CC       natriuretic peptide and beta myosin heavy chain. Muscles do not
CC       show any histological or ultrastructural alterations. Replacement
CC       of isoform 1 by isoform 2 results in embryonic lethality before
CC       16.5 dpc with a plethora of developmental defects including open
CC       neural tube, which is abnormally waved both rostrally and
CC       caudally. Some embryos lack part of the hindbrain and in most
CC       embryos the first branchial arch is shortened, which in some of
CC       the embryos leaves the tongue exposed. Abnormally strong
CC       fibronectin staining is seen in the mesenchyme under the open
CC       neural tube. Extravasation of red blood cells is evident in
CC       various tissues and they are also found in the pericardial cavity.
CC       Choroid plexus is virtually absent correlating with the presence
CC       of an abnormally smooth head and small brain cavities. At later
CC       developmental stages, a striking feature is the lack of a lower
CC       jaw and a dysmorphic lower face. These defects are in part caused
CC       by the abnormal migration of neuroepithelial cells.
CC       {ECO:0000269|PubMed:9553049}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC36379.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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   UniGene; Mm.263396; -.
DR   PDB; 5XQ0; X-ray; 2.75 A; A/B=784-798.
DR   PDBsum; 5XQ0; -.
DR   ProteinModelPortal; P09055; -.
DR   SMR; P09055; -.
DR   BioGrid; 200826; 49.
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; 62.
DR   MINT; P09055; -.
DR   STRING; 10090.ENSMUSP00000087457; -.
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   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   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P09055; -.
DR   KO; K05719; -.
DR   OMA; VVETPEC; -.
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-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   ChiTaRS; Itgb1; mouse.
DR   PRO; PR:P09055; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000025809; Expressed in 327 organ(s), highest expression level in trachea.
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: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:0071438; C:invadopodium membrane; ISS:UniProtKB.
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; IEA:Ensembl.
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; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
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; ISO: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: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:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR   GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; 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: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:2000811; P:negative regulation of anoikis; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IMP: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; ISO:MGI.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IGI: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; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
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:0043547; P:positive regulation of GTPase activity; ISO: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:0032594; P:protein transport within lipid bilayer; ISO:MGI.
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: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; Complete proteome;
KW   Disulfide bond; Endosome; Glycoprotein; Integrin; Isopeptide bond;
KW   Magnesium; Membrane; Metal-binding; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     20
FT   CHAIN        21    798       Integrin beta-1.
FT                                /FTId=PRO_0000016335.
FT   TOPO_DOM     21    728       Extracellular. {ECO:0000255}.
FT   TRANSMEM    729    751       Helical. {ECO:0000255}.
FT   TOPO_DOM    752    798       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      140    378       VWFA.
FT   REPEAT      466    515       I.
FT   REPEAT      516    559       II.
FT   REPEAT      560    598       III.
FT   REPEAT      599    635       IV.
FT   REGION      207    213       CX3CL1-binding.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   REGION      295    314       CX3CL1-binding.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   REGION      466    635       Cysteine-rich tandem repeats.
FT   REGION      762    767       Signal for sorting from recycling
FT                                endosomes; interaction with ACAP1.
FT                                {ECO:0000250}.
FT   REGION      785    792       Interaction with ITGB1BP1. {ECO:0000250}.
FT   METAL       152    152       Magnesium. {ECO:0000250}.
FT   METAL       154    154       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       156    156       Calcium 1. {ECO:0000250}.
FT   METAL       157    157       Calcium 1. {ECO:0000250}.
FT   METAL       189    189       Calcium 2. {ECO:0000250}.
FT   METAL       244    244       Calcium 2. {ECO:0000250}.
FT   METAL       246    246       Calcium 2. {ECO:0000250}.
FT   METAL       248    248       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       249    249       Calcium 2. {ECO:0000250}.
FT   METAL       249    249       Magnesium. {ECO:0000250}.
FT   MOD_RES     777    777       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19144319}.
FT   MOD_RES     783    783       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:17947660}.
FT   MOD_RES     785    785       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   MOD_RES     789    789       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   MOD_RES     794    794       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   CARBOHYD     50     50       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     94     94       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     97     97       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    212    212       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    269    269       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    363    363       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19656770}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    417    417       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    481    481       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    520    520       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    584    584       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    669    669       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19656770}.
FT   DISULFID     27     45       {ECO:0000250}.
FT   DISULFID     35    464       {ECO:0000250}.
FT   DISULFID     38     75       {ECO:0000250}.
FT   DISULFID     48     64       {ECO:0000250}.
FT   DISULFID    207    213       {ECO:0000250}.
FT   DISULFID    261    301       {ECO:0000250}.
FT   DISULFID    401    415       {ECO:0000250}.
FT   DISULFID    435    462       {ECO:0000250}.
FT   DISULFID    466    691       {ECO:0000250}.
FT   DISULFID    477    489       {ECO:0000250}.
FT   DISULFID    486    525       {ECO:0000250}.
FT   DISULFID    491    500       {ECO:0000250}.
FT   DISULFID    502    516       {ECO:0000250}.
FT   DISULFID    531    536       {ECO:0000250}.
FT   DISULFID    533    568       {ECO:0000250}.
FT   DISULFID    538    553       {ECO:0000250}.
FT   DISULFID    555    560       {ECO:0000250}.
FT   DISULFID    574    579       {ECO:0000250}.
FT   DISULFID    576    607       {ECO:0000250}.
FT   DISULFID    581    590       {ECO:0000250}.
FT   DISULFID    592    599       {ECO:0000250}.
FT   DISULFID    613    618       {ECO:0000250}.
FT   DISULFID    615    661       {ECO:0000250}.
FT   DISULFID    620    630       {ECO:0000250}.
FT   DISULFID    633    636       {ECO:0000250}.
FT   DISULFID    640    649       {ECO:0000250}.
FT   DISULFID    646    723       {ECO:0000250}.
FT   DISULFID    665    699       {ECO:0000250}.
FT   CROSSLNK    794    794       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   VAR_SEQ     778    778       G -> Q (in isoform 2).
FT                                {ECO:0000303|PubMed:8567725}.
FT                                /FTId=VSP_053581.
FT   VAR_SEQ     786    798       AVTTVVNPKYEGK -> PINNFKNPNYGRKAGL (in
FT                                isoform 2). {ECO:0000303|PubMed:8567725}.
FT                                /FTId=VSP_053582.
FT   MUTAGEN     783    783       Y->F: Reduced endocytosis; when
FT                                associated with F-795.
FT                                {ECO:0000269|PubMed:18804435}.
FT   MUTAGEN     795    795       Y->F: Reduced endocytosis; when
FT                                associated with F-783.
FT                                {ECO:0000269|PubMed:18804435}.
FT   CONFLICT      5      5       L -> Q (in Ref. 2; BAC40532).
FT                                {ECO:0000305}.
FT   CONFLICT     72     72       K -> E (in Ref. 2; BAE35290).
FT                                {ECO:0000305}.
FT   CONFLICT    385    385       E -> D (in Ref. 2; BAC36379).
FT                                {ECO:0000305}.
FT   CONFLICT    385    385       E -> P (in Ref. 6; CAA33272).
FT                                {ECO:0000305}.
FT   CONFLICT    392    392       G -> A (in Ref. 6; CAA33272).
FT                                {ECO:0000305}.
FT   CONFLICT    407    407       G -> E (in Ref. 2; BAC36379).
FT                                {ECO:0000305}.
FT   CONFLICT    443    445       IKI -> HSKL (in Ref. 6; CAA33272).
FT                                {ECO:0000305}.
FT   STRAND      788    791       {ECO:0000244|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
//
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