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P49134 (ITB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length799 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. 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. Interacts with AMICA1; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling AMICA1 homodimerization. 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 (via C-terminal region); the interaction is a prerequisite for focal adhesion disassembly. Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1. Interacts with TLN1; the interaction is prevented by competitive binding of ITGB1BP1. Interacts with ACAP1; required for ITGB1 recycling. Interacts with ASAP3 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Recycling endosome By similarity. Melanosome By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity. Note: Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions to fibrillar adhesions in an ITGB1BP1-dependent manner 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 processCell adhesion
   Cellular componentCell membrane
Cell projection
Endosome
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandMagnesium
Metal-binding
   Molecular functionIntegrin
Receptor
   PTMAcetylation
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

calcium-independent cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

cardiac muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from direct assay PubMed 12639933. Source: RGD

cell fate specification

Inferred from electronic annotation. Source: Ensembl

cell migration involved in sprouting angiogenesis

Inferred from electronic annotation. Source: Ensembl

cell-cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

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

formation of radial glial scaffolds

Inferred from electronic annotation. Source: Ensembl

germ cell migration

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

integrin-mediated signaling pathway

Inferred from direct assay PubMed 12639933. Source: RGD

leukocyte cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

maternal process involved in female pregnancy

Inferred from expression pattern PubMed 20353731. Source: RGD

negative regulation of anoikis

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of MAPK cascade

Inferred from direct assay PubMed 12639933. Source: RGD

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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: Ensembl

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

Inferred from expression pattern PubMed 20189708. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 20200130. Source: RGD

response to transforming growth factor beta

Inferred from expression pattern PubMed 18378961. Source: RGD

sarcomere organization

Inferred from electronic annotation. Source: Ensembl

tight junction assembly

Inferred from mutant phenotype PubMed 18579774. Source: RGD

tissue homeostasis

Inferred from mutant phenotype PubMed 17118629. Source: RGD

   Cellular_componentacrosomal vesicle

Inferred from direct assay PubMed 9202984. Source: RGD

adherens junction

Inferred from direct assay PubMed 18579774. Source: RGD

alpha3-beta1 integrin complex

Inferred from direct assay PubMed 1835909. Source: RGD

alpha7-beta1 integrin complex

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

filopodium

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from direct assay PubMed 17157995PubMed 19027888. Source: RGD

hemidesmosome

Inferred from direct assay PubMed 18579774. Source: RGD

integrin complex

Inferred from direct assay PubMed 17157995. Source: RGD

intercalated disc

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 17157995PubMed 9202984. Source: RGD

membrane raft

Inferred from direct assay PubMed 17157995PubMed 19118221. Source: RGD

myelin sheath abaxonal region

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

recycling endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle membrane

Inferred from electronic annotation. Source: Ensembl

sarcolemma

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactin 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

glycoprotein binding

Inferred from physical interaction PubMed 18658130. Source: RGD

integrin binding

Inferred from mutant phenotype PubMed 17118629. Source: RGD

kinase binding

Inferred from physical interaction PubMed 16935300PubMed 18677563. 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

protease binding

Inferred from physical interaction PubMed 19027888. Source: RGD

protein binding

Inferred from physical interaction PubMed 16935300PubMed 18677563PubMed 8020590PubMed 9858254. Source: RGD

protein complex binding

Inferred from physical interaction PubMed 16935300. 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

protein kinase binding

Inferred from physical interaction PubMed 11133699PubMed 18465789. Source: RGD

receptor activity

Inferred from electronic annotation. Source: InterPro

receptor binding

Inferred from physical interaction PubMed 18465789PubMed 21969374. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 798778Integrin beta-1
PRO_0000016336

Regions

Topological domain21 – 729709Extracellular Potential
Transmembrane730 – 75223Helical; Potential
Topological domain753 – 79947Cytoplasmic Potential
Domain140 – 378239VWFA
Repeat467 – 51650I
Repeat517 – 56044II
Repeat561 – 59939III
Repeat600 – 63637IV
Region467 – 636170Cysteine-rich tandem repeats
Region763 – 7686Signal for sorting from recycling endosomes; interaction with ACAP1 By similarity
Region786 – 7938Interaction with ITGB1BP1 By similarity

Sites

Metal binding1521Magnesium By similarity
Metal binding1541Calcium 1; via carbonyl oxygen By similarity
Metal binding1561Calcium 1 By similarity
Metal binding1571Calcium 1 By similarity
Metal binding1891Calcium 2 By similarity
Metal binding2441Calcium 2 By similarity
Metal binding2461Calcium 2 By similarity
Metal binding2481Calcium 2; via carbonyl oxygen By similarity
Metal binding2491Calcium 2 By similarity
Metal binding2491Magnesium By similarity

Amino acid modifications

Modified residue7781Phosphothreonine By similarity
Modified residue7841Phosphotyrosine By similarity
Modified residue7951N6-acetyllysine By similarity
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4821N-linked (GlcNAc...) Potential
Glycosylation5211N-linked (GlcNAc...) Potential
Glycosylation5851N-linked (GlcNAc...) Potential
Glycosylation6701N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 45 By similarity
Disulfide bond35 ↔ 465 By similarity
Disulfide bond38 ↔ 75 By similarity
Disulfide bond48 ↔ 64 By similarity
Disulfide bond207 ↔ 213 By similarity
Disulfide bond261 ↔ 301 By similarity
Disulfide bond401 ↔ 415 By similarity
Disulfide bond435 ↔ 463 By similarity
Disulfide bond467 ↔ 692 By similarity
Disulfide bond478 ↔ 490 By similarity
Disulfide bond487 ↔ 526 By similarity
Disulfide bond492 ↔ 501 By similarity
Disulfide bond503 ↔ 517 By similarity
Disulfide bond532 ↔ 537 By similarity
Disulfide bond534 ↔ 569 By similarity
Disulfide bond539 ↔ 554 By similarity
Disulfide bond556 ↔ 561 By similarity
Disulfide bond575 ↔ 580 By similarity
Disulfide bond577 ↔ 608 By similarity
Disulfide bond582 ↔ 591 By similarity
Disulfide bond593 ↔ 600 By similarity
Disulfide bond614 ↔ 619 By similarity
Disulfide bond616 ↔ 662 By similarity
Disulfide bond621 ↔ 631 By similarity
Disulfide bond634 ↔ 637 By similarity
Disulfide bond641 ↔ 650 By similarity
Disulfide bond647 ↔ 724 By similarity
Disulfide bond666 ↔ 700 By similarity

Experimental info

Sequence conflict761H → Q in AAI31846. Ref.2
Sequence conflict7111K → N in AAI31846. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P49134 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: F4475202EB8A3EA6

FASTA79988,495
        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 

« Hide

References

« Hide '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.
PIRJC4126.
RefSeqNP_058718.2. NM_017022.2.
UniGeneRn.25733.

3D structure databases

ProteinModelPortalP49134.
SMRP49134. Positions 722-798.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246668. 6 interactions.
IntActP49134. 2 interactions.
MINTMINT-122445.

Chemistry

BindingDBP49134.

PTM databases

PhosphoSiteP49134.

Proteomic databases

PaxDbP49134.
PRIDEP49134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014785; ENSRNOP00000014785; ENSRNOG00000010966.
GeneID24511.
KEGGrno:24511.
UCSCRGD:2927. rat.

Organism-specific databases

CTD3688.
RGD2927. Itgb1.

Phylogenomic databases

eggNOGNOG287997.
GeneTreeENSGT00730000110513.
HOGENOMHOG000252936.
HOVERGENHBG006190.
InParanoidA2RRT8.
KOK05719.
OrthoDBEOG7T7GSB.
PhylomeDBP49134.
TreeFamTF105392.

Gene expression databases

GenevestigatorP49134.

Family and domain databases

Gene3D1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProIPR013111. EGF_extracell.
IPR027071. Integrin_beta-1.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]
PANTHERPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF28. PTHR10082:SF28. 1 hit.
PfamPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFPIRSF002512. Integrin_B. 1 hit.
PRINTSPR01186. INTEGRINB.
SMARTSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEPS00022. EGF_1. 2 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio603533.
PROP49134.

Entry information

Entry nameITB1_RAT
AccessionPrimary (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: June 11, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families