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P18614 (ITA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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 alpha-1
Alternative name(s):
CD49 antigen-like family member A
Laminin and collagen receptor
VLA-1
CD_antigen=CD49a
Gene names
Name:Itga1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen.

Subunit structure

Heterodimer of an alpha and a beta subunit. Alpha-1 associates with beta-1. Interacts with RAB21 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Domain

The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage.

Sequence similarities

Belongs to the integrin alpha chain family.

Contains 7 FG-GAP repeats.

Contains 1 VWFA domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Magnesium
   Molecular functionIntegrin
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processactivation of MAPK activity

Inferred from mutant phenotype. Source: RGD

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell chemotaxis

Inferred from mutant phenotype. Source: RGD

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection morphogenesis

Inferred from mutant phenotype. Source: RGD

positive regulation of neuron apoptosis

Inferred from mutant phenotype. Source: RGD

vasodilation

Inferred from mutant phenotype. Source: RGD

   Cellular componentacrosomal vesicle

Inferred from direct assay. Source: RGD

external side of plasma membrane

Inferred from direct assay. Source: RGD

integrin complex

Inferred from electronic annotation. Source: InterPro

membrane fraction

Inferred from direct assay. Source: RGD

membrane raft

Inferred from direct assay. Source: RGD

neuron projection

Inferred from direct assay. Source: RGD

perikaryon

Inferred from direct assay. Source: RGD

   Molecular functioncollagen binding

Inferred from mutant phenotype. Source: RGD

integrin binding

Inferred from mutant phenotype. Source: RGD

protein heterodimerization activity

Inferred from mutant phenotype. Source: RGD

receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828
Chain29 – 11801152Integrin alpha-1
PRO_0000016231

Regions

Topological domain29 – 11421114Extracellular Potential
Transmembrane1143 – 116523Helical; Potential
Topological domain1166 – 118015Cytoplasmic Potential
Repeat30 – 9162FG-GAP 1
Repeat101 – 16060FG-GAP 2
Domain175 – 364190VWFA
Repeat365 – 41753FG-GAP 3
Repeat422 – 47453FG-GAP 4
Repeat475 – 53763FG-GAP 5
Repeat556 – 61459FG-GAP 6
Repeat618 – 67861FG-GAP 7
Calcium binding497 – 5059 Potential
Calcium binding579 – 5879 Potential
Calcium binding641 – 6499 Potential
Motif1168 – 11725GFFKR motif

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation3171N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4181N-linked (GlcNAc...) Potential
Glycosylation4591N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential
Glycosylation6981N-linked (GlcNAc...) Potential
Glycosylation7471N-linked (GlcNAc...) Potential
Glycosylation7791N-linked (GlcNAc...) Potential
Glycosylation8201N-linked (GlcNAc...) Potential
Glycosylation8391N-linked (GlcNAc...) Potential
Glycosylation8821N-linked (GlcNAc...) Potential
Glycosylation9071N-linked (GlcNAc...) Potential
Glycosylation9381N-linked (GlcNAc...) Potential
Glycosylation9651N-linked (GlcNAc...) Potential
Glycosylation9731N-linked (GlcNAc...) Potential
Glycosylation10071N-linked (GlcNAc...) Potential
Glycosylation10841N-linked (GlcNAc...) Potential
Glycosylation11031N-linked (GlcNAc...) Potential
Glycosylation11141N-linked (GlcNAc...) Potential
Disulfide bond82 ↔ 92 By similarity
Disulfide bond687 ↔ 696 By similarity
Disulfide bond702 ↔ 755 By similarity
Disulfide bond807 ↔ 813 By similarity
Disulfide bond877 ↔ 885 By similarity
Disulfide bond1029 ↔ 1062 By similarity
Disulfide bond1066 ↔ 1073 By similarity

Secondary structure

1 ................................ 1180
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18614 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 8E5DA2BE02362EE4

FASTA1,180130,809
        10         20         30         40         50         60 
MVPRRPASLE VTVACIWLLT VILGFCVSFN VDVKNSMSFS GPVEDMFGYT VQQYENEEGK 

        70         80         90        100        110        120 
WVLIGSPLVG QPKARTGDVY KCPVGRERAM PCVKLDLPVN TSIPNVTEIK ENMTFGSTLV 

       130        140        150        160        170        180 
TNPNGGFLAC GPLYAYRCGH LHYTTGICSD VSPTFQVVNS FAPVQECSTQ LDIVIVLDGS 

       190        200        210        220        230        240 
NSIYPWESVI AFLNDLLKRM DIGPKQTQVG IVQYGENVTH EFNLNKYSST EEVLVAANKI 

       250        260        270        280        290        300 
GRQGGLQTMT ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNYRL KQVIQDCEDE 

       310        320        330        340        350        360 
NIQRFSIAIL GHYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT IVKALGERIF 

       370        380        390        400        410        420 
ALEATADQSA ASFEMEMSQT GFSAHYSQDW VMLGAVGAYD WNGTVVMQKA NQMVIPHNTT 

       430        440        450        460        470        480 
FQTEPAKMNE PLASYLGYTV NSATIPGDVL YIAGQPRYNH TGQVVIYKME DGNINILQTL 

       490        500        510        520        530        540 
GGEQIGSYFG SVLTTIDIDK DSYTDLLLVG APMYMGTEKE EQGKVYVYAV NQTRFEYQMS 

       550        560        570        580        590        600 
LEPIRQTCCS SLKDNSCTKE NKNEPCGARF GTAIAAVKDL NVDGFNDVVI GAPLEDDHAG 

       610        620        630        640        650        660 
AVYIYHGSGK TIREAYAQRI PSGGDGKTLK FFGQSIHGEM DLNGDGLTDV TIGGLGGAAL 

       670        680        690        700        710        720 
FWARDVAVVK VTMNFEPNKV NIQKKNCRVE GKETVCINAT MCFHVKLKSK EDSIYEADLQ 

       730        740        750        760        770        780 
YRVTLDSLRQ ISRSFFSGTQ ERKIQRNITV RESECIRHSF YMLDKHDFQD SVRVTLDFNL 

       790        800        810        820        830        840 
TDPENGPVLD DALPNSVHEH IPFAKDCGNK ERCISDLTLN VSTTEKSLLI VKSQHDKFNV 

       850        860        870        880        890        900 
SLTVKNKGDS AYNTRTVVQH SPNLIFSGIE EIQKDSCESN QNITCRVGYP FLRAGETVTF 

       910        920        930        940        950        960 
KIIFQFNTSH LSENAIIHLS ATSDSEEPLE SLNDNEVNIS IPVKYEVGLQ FYSSASEHHI 

       970        980        990       1000       1010       1020 
SVAANETIPE FINSTEDIGN EINVFYTIRK RGHFPMPELQ LSISFPNLTA DGYPVLYPIG 

      1030       1040       1050       1060       1070       1080 
WSSSDNVNCR PRSLEDPFGI NSGKKMTISK SEVLKRGTIQ DCSSTCGVAT ITCSLLPSDL 

      1090       1100       1110       1120       1130       1140 
SQVNVSLLLW KPTFIRAHFS SLNLTLRGEL KSENSSLTLS SSNRKRELAI QISKDGLPGR 

      1150       1160       1170       1180 
VPLWVILLSA FAGLLLLMLL ILALWKIGFF KRPLKKKMEK

« Hide

References

[1]"Molecular cloning of the rat integrin alpha 1-subunit: a receptor for laminin and collagen."
Ignatius M.J., Large T.H., Houde M., Tawil J.W., Barton A., Esch F., Carbonetto S., Reichardt L.F.
J. Cell Biol. 111:709-720(1990) [PubMed: 2380249] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Crystal structure of the alpha1beta1 integrin I-domain: insights into integrin I-domain function."
Nolte M., Pepinsky R.B., Venyaminov S.Y., Koteliansky V., Gotwals P.J., Karpusas M.
FEBS Lett. 452:379-385(1999) [PubMed: 10386626] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 151-364.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52140 mRNA. Translation: CAA36384.1.
IPIIPI00324585.
PIRA35854.
RefSeqNP_112256.1. NM_030994.2.
UniGeneRn.91044.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CK4X-ray2.20A/B167-364[»]
1MHPX-ray2.80A/B169-360[»]
2B2XX-ray2.20A/B151-364[»]
ProteinModelPortalP18614.
SMRP18614. Positions 169-362, 1139-1173.
ModBaseSearch...

Protein-protein interaction databases

IntActP18614. 1 interaction.
MINTMINT-1889950.
STRINGP18614.

PTM databases

PhosphoSiteP18614.

Proteomic databases

PRIDEP18614.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25118.
KEGGrno:25118.

Organism-specific databases

CTD3672.
RGD2923. Itga1.

Phylogenomic databases

eggNOGmaNOG13530.
GeneTreeENSGT00600000084333.
HOVERGENHBG006185.
InParanoidP18614.
OrthoDBEOG4THVS7.

Gene expression databases

ArrayExpressP18614.
GenevestigatorP18614.
GermOnlineENSRNOG00000012080. Rattus norvegicus.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR002035. VWF_A.
[Graphical view]
KOK06480.
PfamPF01839. FG-GAP. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PRINTSPR01185. INTEGRINA.
SMARTSM00191. Int_alpha. 5 hits.
SM00327. VWA. 1 hit.
[Graphical view]
PROSITEPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio605489.

Entry information

Entry nameITA1_RAT
AccessionPrimary (citable) accession number: P18614
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 16, 2011
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents