P49134 (ITB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Integrin beta-1

Alternative name(s):
Beta oligodendroglia
Short name=Beta OL
Fibronectin receptor subunit beta
VLA-4 subunit beta
CD_antigen=CD29

Gene names

Name:

Itgb1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	799 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis By similarity.
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 NMRK2, 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. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with FGR and HCK. Interacts with MYO10. Interacts with DAB2. Interacts with ITGB1BP1 By similarity.
Subcellular location	Cell membrane; Single-pass type I membrane protein. 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.
Sequence caution	The sequence AAI31846.1 differs from that shown. Reason: Frameshift at positions 442, 443 and 447.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Magnesium Metal-binding
Molecular function	Integrin Receptor
PTM	Acetylation Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara calcium-independent cell-matrix adhesion Inferred from electronic annotation. Source: Compara cardiac muscle cell differentiation Inferred from electronic annotation. Source: Compara cell adhesion Inferred from direct assay PubMed 12639933. Source: RGD cell fate specification Inferred from electronic annotation. Source: Compara cell migration involved in sprouting angiogenesis Inferred from electronic annotation. Source: Compara cell-cell adhesion mediated by integrin Inferred from electronic annotation. Source: Compara cellular calcium ion homeostasis Inferred from direct assay PubMed 12639933. Source: RGD cellular response to ionizing radiation Inferred from expression pattern PubMed 19714308. Source: RGD cellular response to mechanical stimulus Inferred from expression pattern PubMed 19720043. Source: RGD cellular response to vitamin D Inferred from expression pattern PubMed 20304064. Source: RGD germ cell migration Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Inferred from direct assay PubMed 12639933. Source: RGD leukocyte cell-cell adhesion Inferred from electronic annotation. Source: Compara maternal process involved in female pregnancy Inferred from expression pattern PubMed 20353731. Source: RGD negative regulation of anoikis Inferred from electronic annotation. Source: Compara negative regulation of cell projection organization Inferred from mutant phenotype PubMed 20039268. Source: RGD negative regulation of cell proliferation Inferred from mutant phenotype PubMed 18658130. Source: RGD negative regulation of neuron differentiation Inferred from mutant phenotype PubMed 18658130. Source: RGD neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of MAPK cascade Inferred from direct assay PubMed 12639933. Source: RGD positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from mutant phenotype PubMed 18167060PubMed 19686792PubMed 19705458. Source: RGD positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of cell-substrate adhesion Inferred from mutant phenotype PubMed 18167060PubMed 19705458. Source: RGD positive regulation of endocytosis Inferred from mutant phenotype PubMed 18577581. Source: RGD positive regulation of neuron differentiation Inferred from mutant phenotype PubMed 18658130. Source: RGD positive regulation of neuron projection development Inferred from mutant phenotype PubMed 14564503PubMed 19118221. Source: RGD positive regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype PubMed 18465789. Source: RGD protein transport within lipid bilayer Inferred from mutant phenotype PubMed 19420267. Source: RGD regulation of G-protein coupled receptor protein signaling pathway Inferred from mutant phenotype PubMed 17157995. Source: RGD regulation of cell cycle Inferred from electronic annotation. Source: Compara response to activity Inferred from expression pattern PubMed 18378961. Source: RGD response to drug Inferred from expression pattern PubMed 20368265. Source: RGD response to gonadotropin stimulus Inferred from expression pattern PubMed 20189708. Source: RGD response to transforming growth factor beta stimulus Inferred from expression pattern PubMed 18378961. Source: RGD sarcomere organization Inferred from electronic annotation. Source: Compara tight junction assembly Inferred from mutant phenotype PubMed 18579774. Source: RGD tissue homeostasis Inferred from mutant phenotype PubMed 17118629. Source: RGD
Cellular_component	acrosomal vesicle Inferred from direct assay PubMed 9202984. Source: RGD alpha3-beta1 integrin complex Inferred from direct assay PubMed 1835909. Source: RGD alpha9-beta1 integrin complex Inferred from direct assay PubMed 8020590. Source: RGD basement membrane Inferred from direct assay PubMed 18596883PubMed 9202984. Source: RGD cell surface Inferred from direct assay PubMed 19705458. Source: RGD cell-cell junction Inferred from direct assay PubMed 11133699. Source: RGD external side of plasma membrane Inferred from electronic annotation. Source: Compara focal adhesion Inferred from direct assay PubMed 17157995PubMed 19027888. Source: RGD hemidesmosome Inferred from direct assay PubMed 18579774. Source: RGD intercalated disc Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane raft Inferred from direct assay PubMed 17157995PubMed 19118221. Source: RGD myelin sheath abaxonal region Inferred from electronic annotation. Source: Compara neuromuscular junction Inferred from electronic annotation. Source: Compara ruffle membrane Inferred from electronic annotation. Source: Compara sarcolemma Inferred from electronic annotation. Source: Compara
Molecular_function	actin binding Inferred from direct assay PubMed 16935300. Source: RGD alpha-actinin binding Inferred from direct assay PubMed 16935300. Source: RGD collagen binding Inferred from direct assay PubMed 1835909. Source: RGD fibronectin binding Inferred from direct assay PubMed 1835909. Source: RGD integrin binding Inferred from mutant phenotype PubMed 17118629. Source: RGD laminin binding Inferred from direct assay PubMed 1835909. Source: RGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptide binding Inferred from direct assay PubMed 12639933. Source: RGD protein domain specific binding Inferred from direct assay PubMed 18658130. Source: RGD protein heterodimerization activity Inferred from mutant phenotype PubMed 17118629. Source: RGD receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	By similarity
	Chain	21 – 798	778	Integrin beta-1		PRO_0000016336
Regions
	Topological domain	21 – 729	709	Extracellular Potential
	Transmembrane	730 – 752	23	Helical; Potential
	Topological domain	753 – 799	47	Cytoplasmic Potential
	Domain	140 – 378	239	VWFA
	Repeat	467 – 516	50	I
	Repeat	517 – 560	44	II
	Repeat	561 – 599	39	III
	Repeat	600 – 636	37	IV
	Region	467 – 636	170	Cysteine-rich tandem repeats
	Region	786 – 793	8	Interaction with ITGB1BP1 By similarity
Sites
	Metal binding	152	1	Magnesium By similarity
	Metal binding	154	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	156	1	Calcium 1 By similarity
	Metal binding	157	1	Calcium 1 By similarity
	Metal binding	189	1	Calcium 2 By similarity
	Metal binding	244	1	Calcium 2 By similarity
	Metal binding	246	1	Calcium 2 By similarity
	Metal binding	248	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	249	1	Calcium 2 By similarity
	Metal binding	249	1	Magnesium By similarity
Amino acid modifications
	Modified residue	186	1	Phosphoserine By similarity
	Modified residue	778	1	Phosphothreonine By similarity
	Modified residue	784	1	Phosphotyrosine By similarity
	Modified residue	795	1	N6-acetyllysine 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...) Potential
	Glycosylation	406	1	N-linked (GlcNAc...) Potential
	Glycosylation	417	1	N-linked (GlcNAc...) Potential
	Glycosylation	482	1	N-linked (GlcNAc...) Potential
	Glycosylation	521	1	N-linked (GlcNAc...) Potential
	Glycosylation	585	1	N-linked (GlcNAc...) Potential
	Glycosylation	670	1	N-linked (GlcNAc...) Potential
	Disulfide bond	27 ↔ 45		By similarity
	Disulfide bond	35 ↔ 465		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 ↔ 463		By similarity
	Disulfide bond	467 ↔ 692		By similarity
	Disulfide bond	478 ↔ 490		By similarity
	Disulfide bond	487 ↔ 526		By similarity
	Disulfide bond	492 ↔ 501		By similarity
	Disulfide bond	503 ↔ 517		By similarity
	Disulfide bond	532 ↔ 537		By similarity
	Disulfide bond	534 ↔ 569		By similarity
	Disulfide bond	539 ↔ 554		By similarity
	Disulfide bond	556 ↔ 561		By similarity
	Disulfide bond	575 ↔ 580		By similarity
	Disulfide bond	577 ↔ 608		By similarity
	Disulfide bond	582 ↔ 591		By similarity
	Disulfide bond	593 ↔ 600		By similarity
	Disulfide bond	614 ↔ 619		By similarity
	Disulfide bond	616 ↔ 662		By similarity
	Disulfide bond	621 ↔ 631		By similarity
	Disulfide bond	634 ↔ 637		By similarity
	Disulfide bond	641 ↔ 650		By similarity
	Disulfide bond	647 ↔ 724		By similarity
	Disulfide bond	666 ↔ 700		By similarity
Experimental info
	Sequence conflict	76	1	H → Q in AAI31846. Ref.2
	Sequence conflict	711	1	K → N in AAI31846. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P49134 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: F4475202EB8A3EA6	FASTA	799	88,495
	10 20 30 40 50 60 MNLQLVFWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN TTFLQEGMPT 70 80 90 100 110 120 SARCDDLEAL KKKGCHPSDI 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 ENQLKLNPLG FTEEVEVVLQ FICKCNCQSH GIPASPKCHE 490 500 510 520 530 540 GNGTFECGAC RCNEGRVGRH CECSTDEVNS EDMDAYCRKE NSSEICSNNG ECVCGQCVCR 550 560 570 580 590 600 KRENTNEIYS GKFCECDNFN CDRSNGLICG GNGVCRCRVC ECYPNYTGSA CDCSLDTVPC 610 620 630 640 650 660 VATNGQICNG RGICECGACK CTDPKFQGPT CETCQTCLGV CAEHKECVQC RAFNKGEKKD 670 680 690 700 710 720 TCAQECSHFN LTKVESREKL PQPVQVDPVT HCKEKDIDDC WFYFTYSVNS KGEAHVHVVE 730 740 750 760 770 780 TPDCPTGPDI IPIVAGVVAG IVLIGLALLL IWKLLMIIHD RREFAKFEKE KMNAKWDTGE 790 NPIYKSAVTT VVNPKYEGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence of the cDNA encoding the rat oligodendrocyte integrin beta 1 subunit." Malek-Hedayat S., Rome L.H. Gene 158:287-290(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Oligodendrocyte.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U12309 mRNA. Translation: AAA86669.1. BC131845 mRNA. Translation: AAI31846.1. Frameshift.
IPI	IPI00191681.
PIR	JC4126.
RefSeq	NP_058718.2. NM_017022.2.
UniGene	Rn.25733.
3D structure databases
ProteinModelPortal	P49134.
SMR	P49134. Positions 722-798.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49134. 1 interaction.
PTM databases
PhosphoSite	P49134.
Proteomic databases
PaxDb	P49134.
PRIDE	P49134.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000014785; ENSRNOP00000014785; ENSRNOG00000010966.
GeneID	24511.
KEGG	rno:24511.
UCSC	RGD:2927. rat.
Organism-specific databases
CTD	3688.
RGD	2927. Itgb1.
Phylogenomic databases
eggNOG	NOG287997.
GeneTree	ENSGT00700000104375.
HOGENOM	HOG000252936.
HOVERGEN	HBG006190.
InParanoid	A2RRT8.
KO	K05719.
OrthoDB	EOG4K9BBM.
Gene expression databases
ArrayExpress	P49134.
Genevestigator	P49134.
GermOnline	ENSRNOG00000010966. Rattus norvegicus.
Family and domain databases
Gene3D	1.20.5.630. 1 hit.
InterPro	IPR013111. EGF_extracell. IPR027071. Integrin_beta-1. IPR015812. Integrin_bsu. IPR014836. Integrin_bsu_cyt_dom. IPR002369. Integrin_bsu_N. IPR012896. Integrin_bsu_tail. IPR003659. Plexin-like. IPR016201. Plexin-like_fold. IPR002035. VWF_A. [Graphical view]
PANTHER	PTHR10082. PTHR10082. 1 hit. PTHR10082:SF28. PTHR10082:SF28. 1 hit.
Pfam	PF07974. EGF_2. 1 hit. 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]
SUPFAM	SSF69687. Integrin_bsu_tail. 1 hit. SSF103575. Plexin-like_fold. 1 hit.
PROSITE	PS00022. EGF_1. 2 hits. Uncertain. PS00243. INTEGRIN_BETA. 3 hits. PS50234. VWFA. False negative. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P49134.
ChEMBL	CHEMBL2989.
NextBio	603533.

Entry information

Entry name

ITB1_RAT

Accession

Primary (citable) accession number: P49134
Secondary accession number(s): A2RRT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program