Reviewed, UniProtKB/Swiss-Prot P09055 (ITB1_MOUSE)

Names and origin

Protein names

Recommended name:
    Integrin beta-1
Alternative name(s):
    Fibronectin receptor subunit beta
    Integrin VLA-4 subunit beta
    CD_antigen=CD29

Gene names

Name:

Itgb1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and GNB2L1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Ref.7 Ref.8 Ref.10
Subunit structure	Heterodimer of an alpha and a beta subunit. Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or alpha-V. Binds LGALS3BP and ITGB1BP3, when associated with alpha-7, but not with alpha-5. Interacts with FLNA, FLNB, FLNC and RANBP9. Interacts with KRT1 in the presence of GNB2L1 and SRC By similarity. Interacts with RAB21 By similarity.
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity. Melanosome By similarity.
Post-translational modification	The cysteine residues are involved in intrachain disulfide bonds By similarity.
Sequence similarities	Belongs to the integrin beta chain family. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Domain	Repeat Signal Transmembrane
Molecular function	Integrin Receptor
PTM	Acetylation Disulfide bond Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	G1/S transition of mitotic cell cycle Inferred from mutant phenotype. Source: MGI cardiac muscle cell differentiation Inferred from mutant phenotype. Source: MGI cell fate specification Inferred from mutant phenotype. Source: MGI cell-matrix adhesion Inferred from electronic annotation. Source: InterPro germ cell migration Inferred from mutant phenotype. Source: MGI in utero embryonic development Inferred from mutant phenotype. Source: MGI integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell differentiation Inferred from mutant phenotype. Source: MGI positive regulation of cell proliferation Inferred from mutant phenotype. Source: MGI regulation of cell cycle Inferred from mutant phenotype. Source: MGI sarcomere organization Inferred from mutant phenotype. Source: MGI
Cellular component	integrin complex Inferred from electronic annotation. Source: InterPro melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell neuromuscular junction Inferred from direct assay. Source: MGI sarcolemma Inferred from direct assay. Source: MGI synaptosome Inferred from direct assay. Source: MGI
Molecular function	integrin binding Inferred from physical interaction. Source: MGI receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Nme2	Q01768	2	EBI-644224,EBI-642573
Tmem158	Q6F5E0	2	EBI-644224,EBI-645317
Vegfb	P49766-1	2	EBI-644224,EBI-645309

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20
	Chain	21 – 798	778	Integrin beta-1		PRO_0000016335
Regions
	Topological domain	21 – 728	708	Extracellular Potential
	Transmembrane	729 – 751	23	Potential
	Topological domain	752 – 798	47	Cytoplasmic Potential
	Domain	140 – 378	239	VWFA
	Repeat	466 – 515	50	I
	Repeat	516 – 559	44	II
	Repeat	560 – 598	39	III
	Repeat	599 – 635	37	IV
	Region	466 – 635	170	Cysteine-rich tandem repeats
Amino acid modifications
	Modified residue	186	1	Phosphoserine Ref.11
	Modified residue	777	1	Phosphothreonine Ref.11
	Modified residue	783	1	Phosphotyrosine Ref.9
	Modified residue	794	1	N6-acetyllysine By similarity
	Modified residue	795	1	Phosphotyrosine By similarity
	Glycosylation	50	1	N-linked (GlcNAc...) Potential
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Glycosylation	212	1	N-linked (GlcNAc...) Potential
	Glycosylation	269	1	N-linked (GlcNAc...) Potential
	Glycosylation	363	1	N-linked (GlcNAc...) Ref.12
	Glycosylation	366	1	N-linked (GlcNAc...) Ref.12
	Glycosylation	376	1	N-linked (GlcNAc...) Ref.12
	Glycosylation	406	1	N-linked (GlcNAc...) Potential
	Glycosylation	417	1	N-linked (GlcNAc...) Potential
	Glycosylation	481	1	N-linked (GlcNAc...) Potential
	Glycosylation	520	1	N-linked (GlcNAc...) Potential
	Glycosylation	584	1	N-linked (GlcNAc...) Potential
	Glycosylation	669	1	N-linked (GlcNAc...) Ref.12
	Disulfide bond	27 ↔ 464		By similarity
	Disulfide bond	35 ↔ 45		By similarity
	Disulfide bond	38 ↔ 75		By similarity
	Disulfide bond	48 ↔ 64		By similarity
	Disulfide bond	207 ↔ 213		By similarity
	Disulfide bond	261 ↔ 301		By similarity
	Disulfide bond	401 ↔ 415		By similarity
	Disulfide bond	435 ↔ 691		By similarity
	Disulfide bond	462 ↔ 466		By similarity
	Disulfide bond	477 ↔ 489		By similarity
	Disulfide bond	486 ↔ 525		By similarity
	Disulfide bond	491 ↔ 500		By similarity
	Disulfide bond	502 ↔ 516		By similarity
	Disulfide bond	531 ↔ 536		By similarity
	Disulfide bond	533 ↔ 568		By similarity
	Disulfide bond	538 ↔ 553		By similarity
	Disulfide bond	555 ↔ 560		By similarity
	Disulfide bond	574 ↔ 579		By similarity
	Disulfide bond	576 ↔ 607		By similarity
	Disulfide bond	581 ↔ 590		By similarity
	Disulfide bond	592 ↔ 599		By similarity
	Disulfide bond	613 ↔ 618		By similarity
	Disulfide bond	615 ↔ 661		By similarity
	Disulfide bond	620 ↔ 630		By similarity
	Disulfide bond	633 ↔ 636		By similarity
	Disulfide bond	640 ↔ 649		By similarity
	Disulfide bond	646 ↔ 723		By similarity
	Disulfide bond	665 ↔ 699		By similarity
Experimental info
	Mutagenesis	783	1	Y → F: Reduced endocytosis; when associated with F-795. Ref.10
	Mutagenesis	795	1	Y → F: Reduced endocytosis; when associated with F-783. Ref.10
	Sequence conflict	5	1	L → Q in BAC40532. Ref.2
	Sequence conflict	72	1	K → E in BAE35290. Ref.2
	Sequence conflict	385	1	E → D in BAC36379. Ref.2
	Sequence conflict	385	1	E → P in CAA33272. Ref.5
	Sequence conflict	392	1	G → A in CAA33272. Ref.5
	Sequence conflict	407	1	G → E in BAC36379. Ref.2
	Sequence conflict	443 – 445	3	IKI → HSKL in CAA33272. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P09055-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 26788F7F0A168B56	FASTA	798	88,231
	10 20 30 40 50 60 MNLQLVSWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN TTFLQEGMPT 70 80 90 100 110 120 SARCDDLEAL KKKGCQPSDI ENPRGSQTIK KNKNVTNRSK GMAEKLRPED ITQIQPQQLL 130 140 150 160 170 180 LKLRSGEPQK FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF 190 200 210 220 230 240 RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTDRGE FFNELVGQQR 250 260 270 280 290 300 ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ 310 320 330 340 350 360 CHLENNVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL 370 380 390 400 410 420 SGNSSNVIQL IIDAYNSLSS EVILENSKLP DGVTINYKSY CKNGVNGTGE NGRKCSNISI 430 440 450 460 470 480 GDEVQFEISI TANKCPNKES ETIKIKPLGF TEEVEVVLQF ICKCNCQSHG IPASPKCHEG 490 500 510 520 530 540 NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK 550 560 570 580 590 600 RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCRCRVCE CYPNYTGSAC DCSLDTGPCL 610 620 630 640 650 660 ASNGQICNGR GICECGACKC TDPKFQGPTC ETCQTCLGVC AEHKECVQCR AFNKGEKKDT 670 680 690 700 710 720 CAQECSHFNL TKVESREKLP QPVQVDPVTH CKEKDIDDCW FYFTYSVNGN NEAIVHVVET 730 740 750 760 770 780 PDCPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN 790 PIYKSAVTTV VNPKYEGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Murine mRNA for the beta-subunit of integrin is increased in BALB/c-3T3 cells entering the G1 phase from the G0 state." Tominaga S. FEBS Lett. 238:315-319(1988) [PubMed: 3262537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Head, Osteoclast, Placenta and Thymocyte.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[5]	"Molecular cloning of a murine fibronectin receptor and its expression during inflammation. Expression of VLA-5 is increased in activated peritoneal macrophages in a manner discordant from major histocompatibility complex class II." Holers V.M., Ruff T.G., Parks D.L., McDonald J.A., Ballard L.L., Brown E.J. J. Exp. Med. 169:1589-1605(1989) [PubMed: 2523953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-798. Strain: BALB/c.
[6]	"Coordinate induction of fibronectin, fibronectin receptor, tropomyosin, and actin genes in serum-stimulated fibroblasts." Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R. Exp. Cell Res. 180:537-545(1989) [PubMed: 2521606] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 595-798.
[7]	"The muscle integrin binding protein (MIBP) interacts with alpha7beta1 integrin and regulates cell adhesion and laminin matrix deposition." Li J., Rao H., Burkin D., Kaufman S.J., Wu C. Dev. Biol. 261:209-219(2003) [PubMed: 12941630] [Abstract] Cited for: FUNCTION, INTERACTION WITH ITGB1BP3.
[8]	"NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin." Fukushi J., Makagiansar I.T., Stallcup W.B. Mol. Biol. Cell 15:3580-3590(2004) [PubMed: 15181153] [Abstract] Cited for: FUNCTION, INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
[9]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, MASS SPECTROMETRY. Tissue: Mast cell.
[10]	"Integrin trafficking regulated by Rab21 is necessary for cytokinesis." Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H., Grosse R., Kitzing T., Rantala J.K., Kallioniemi O., Faessler R., Kallio M., Ivaska J. Dev. Cell 15:371-385(2008) [PubMed: 18804435] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TYR-783 AND TYR-795.
[11]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND THR-777, MASS SPECTROMETRY. Tissue: Macrophage.
[12]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: Identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 0:0-0(2009) [PubMed: 19656770] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-363; ASN-366; ASN-376 AND ASN-669, MASS SPECTROMETRY. Tissue: Myoblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y00769 mRNA. Translation: CAA68738.1. AK076526 mRNA. Translation: BAC36379.1. Different initiation. AK088729 mRNA. Translation: BAC40532.1. AK159689 mRNA. Translation: BAE35290.1. AK167682 mRNA. Translation: BAE39731.1. CH466525 Genomic DNA. Translation: EDL11832.1. BC050906 mRNA. Translation: AAH50906.1. X15202 mRNA. Translation: CAA33272.1.
IPI	IPI00132474.
PIR	IJMSFB. PL0104. S01659.
RefSeq	NP_034708.1.
UniGene	Mm.263396
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P09055. 6 interactions.
STRING	P09055.
PTM databases
PhosphoSite	P09055.
Proteomic databases
PRIDE	P09055.
Genome annotation databases
Ensembl	ENSMUST00000090006; ENSMUSP00000087457; ENSMUSG00000025809; Mus musculus. [Genome view]
GeneID	16412.
KEGG	mmu:16412.
UCSC	uc009nzv.1. mouse.
Organism-specific databases
CTD	16412.
MGI	MGI:96610. Itgb1.
Phylogenomic databases
HOGENOM	P09055.
HOVERGEN	P09055.
OMA	VDPLSHC
OrthoDB	EOG9M3CVK
Gene expression databases
ArrayExpress	P09055.
Bgee	P09055.
CleanEx	MM_ITGB1.
Genevestigator	P09055.
GermOnline	ENSMUSG00000025809. Mus musculus.
Family and domain databases
InterPro	IPR013111. EGF_extracell. IPR015812. Integrin_bsu. IPR015438. Integrin_bsu-1_C. IPR001169. Integrin_bsu_C. IPR014836. Integrin_bsu_cyt. IPR002369. Integrin_bsu_N. IPR012012. Integrin_bsu_subgr. IPR012896. Integrin_bsu_tail. IPR003659. Plexin-like. IPR002035. VWF_A. [Graphical view]
Gene3D	G3DSA:1.20.5.630. Integrin_bsu_cyt. 1 hit.
PANTHER	PTHR10082. Integrin_beta_C. 1 hit. PTHR10082:SF14. Integrin_bsu-1_C. 1 hit.
Pfam	PF07974. EGF_2. 3 hits. PF08725. Integrin_b_cyt. 1 hit. PF07965. Integrin_B_tail. 1 hit. PF00362. Integrin_beta. 1 hit. [Graphical view]
PIRSF	PIRSF002512. Integrin_B. 1 hit.
PRINTS	PR01186. INTEGRINB.
SMART	SM00187. INB. 1 hit. SM00423. PSI. 1 hit. SM00327. VWA. 1 hit. [Graphical view]
PROSITE	PS00022. EGF_1. 2 hits. Uncertain. PS00243. INTEGRIN_BETA. 3 hits. PS50234. VWFA. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	289597.
SOURCE	Search...

Entry information

Entry name

ITB1_MOUSE

Accession

Primary (citable) accession number: P09055
Secondary accession number(s): Q3TIW5 , Q3TWH6, Q8BTU0, Q8BVU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	November 24, 2009
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)