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Protein

Integrin alpha-1

Gene

Itga1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi497 – 5059Sequence analysis
Calcium bindingi579 – 5879Sequence analysis
Calcium bindingi641 – 6499Sequence analysis

GO - Molecular functioni

  • collagen binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • receptor binding Source: RGD

GO - Biological processi

  • activation of MAPK activity Source: RGD
  • cell chemotaxis Source: RGD
  • cell-matrix adhesion Source: Ensembl
  • cellular extravasation Source: Ensembl
  • integrin-mediated signaling pathway Source: UniProtKB-KW
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  • neuron projection morphogenesis Source: RGD
  • neutrophil chemotaxis Source: Ensembl
  • positive regulation of neuron apoptotic process Source: RGD
  • positive regulation of phosphoprotein phosphatase activity Source: UniProtKB
  • vasodilation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-216083. Integrin cell surface interactions.
R-RNO-445355. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin alpha-1
Alternative name(s):
CD49 antigen-like family member A
Laminin and collagen receptor
VLA-1
CD_antigen: CD49a
Gene namesi
Name:Itga1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2923. Itga1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 11421114ExtracellularSequence analysisAdd
BLAST
Transmembranei1143 – 116523HelicalSequence analysisAdd
BLAST
Topological domaini1166 – 118015CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • acrosomal vesicle Source: RGD
  • basal part of cell Source: Ensembl
  • external side of plasma membrane Source: RGD
  • extracellular exosome Source: Ensembl
  • focal adhesion Source: Ensembl
  • integrin alpha1-beta1 complex Source: Ensembl
  • membrane Source: RGD
  • membrane raft Source: RGD
  • neuron projection Source: RGD
  • perikaryon Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Add
BLAST
Chaini29 – 11801152Integrin alpha-1PRO_0000016231Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi82 ↔ 92By similarity
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence analysis
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence analysis
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence analysis
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence analysis
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence analysis
Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence analysis
Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence analysis
Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence analysis
Glycosylationi531 – 5311N-linked (GlcNAc...)Sequence analysis
Disulfide bondi687 ↔ 696By similarity
Glycosylationi698 – 6981N-linked (GlcNAc...)Sequence analysis
Disulfide bondi702 ↔ 755By similarity
Glycosylationi747 – 7471N-linked (GlcNAc...)Sequence analysis
Glycosylationi779 – 7791N-linked (GlcNAc...)Sequence analysis
Disulfide bondi807 ↔ 813By similarity
Glycosylationi820 – 8201N-linked (GlcNAc...)Sequence analysis
Glycosylationi839 – 8391N-linked (GlcNAc...)Sequence analysis
Disulfide bondi877 ↔ 885By similarity
Glycosylationi882 – 8821N-linked (GlcNAc...)Sequence analysis
Glycosylationi907 – 9071N-linked (GlcNAc...)Sequence analysis
Glycosylationi938 – 9381N-linked (GlcNAc...)Sequence analysis
Glycosylationi965 – 9651N-linked (GlcNAc...)Sequence analysis
Glycosylationi973 – 9731N-linked (GlcNAc...)Sequence analysis
Glycosylationi1007 – 10071N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1029 ↔ 1062By similarity
Disulfide bondi1066 ↔ 1073By similarity
Glycosylationi1084 – 10841N-linked (GlcNAc...)Sequence analysis
Glycosylationi1103 – 11031N-linked (GlcNAc...)Sequence analysis
Glycosylationi1114 – 11141N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP18614.
PRIDEiP18614.

PTM databases

iPTMnetiP18614.
PhosphoSiteiP18614.
UniCarbKBiP18614.

Expressioni

Gene expression databases

GenevisibleiP18614. RN.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Alpha-1 associates with beta-1 (By similarity). Interacts with RAB21 (By similarity). Interacts (via cytoplasmic domain) with PTPN2; activates PTPN2 phosphatase activity towards EGFR and negatively regulates EGF signaling (By similarity).By similarity

GO - Molecular functioni

  • collagen binding Source: RGD
  • receptor binding Source: RGD

Protein-protein interaction databases

IntActiP18614. 1 interaction.
MINTiMINT-1889950.
STRINGi10116.ENSRNOP00000016353.

Structurei

Secondary structure

1
1180
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi171 – 1788Combined sources
Helixi186 – 19712Combined sources
Beta strandi208 – 22215Combined sources
Turni224 – 2263Combined sources
Helixi230 – 2389Combined sources
Helixi250 – 25910Combined sources
Turni260 – 2623Combined sources
Helixi264 – 2663Combined sources
Beta strandi273 – 28210Combined sources
Helixi287 – 2893Combined sources
Helixi290 – 29910Combined sources
Beta strandi302 – 3098Combined sources
Helixi311 – 3155Combined sources
Helixi321 – 3288Combined sources
Helixi335 – 3384Combined sources
Beta strandi339 – 3457Combined sources
Helixi346 – 3505Combined sources
Helixi352 – 3598Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CK4X-ray2.20A/B167-364[»]
1MHPX-ray2.80A/B169-360[»]
2B2XX-ray2.20A/B151-364[»]
ProteinModelPortaliP18614.
SMRiP18614. Positions 169-362, 1139-1173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18614.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati30 – 9162FG-GAP 1Add
BLAST
Repeati101 – 16060FG-GAP 2Add
BLAST
Domaini175 – 364190VWFAPROSITE-ProRule annotationAdd
BLAST
Repeati365 – 41753FG-GAP 3Add
BLAST
Repeati422 – 47453FG-GAP 4Add
BLAST
Repeati475 – 53763FG-GAP 5Add
BLAST
Repeati556 – 61459FG-GAP 6Add
BLAST
Repeati618 – 67861FG-GAP 7Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1168 – 11725GFFKR motif

Domaini

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

Sequence similaritiesi

Belongs to the integrin alpha chain family.Curated
Contains 7 FG-GAP repeats.Curated
Contains 1 VWFA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPB7. Eukaryota.
ENOG410YEM8. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000059610.
HOVERGENiHBG006185.
InParanoidiP18614.
KOiK06480.
OMAiQRFSIAI.
OrthoDBiEOG7GBFW6.
PhylomeDBiP18614.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18614-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPRRPASLE VTVACIWLLT VILGFCVSFN VDVKNSMSFS GPVEDMFGYT
60 70 80 90 100
VQQYENEEGK WVLIGSPLVG QPKARTGDVY KCPVGRERAM PCVKLDLPVN
110 120 130 140 150
TSIPNVTEIK ENMTFGSTLV TNPNGGFLAC GPLYAYRCGH LHYTTGICSD
160 170 180 190 200
VSPTFQVVNS FAPVQECSTQ LDIVIVLDGS NSIYPWESVI AFLNDLLKRM
210 220 230 240 250
DIGPKQTQVG IVQYGENVTH EFNLNKYSST EEVLVAANKI GRQGGLQTMT
260 270 280 290 300
ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNYRL KQVIQDCEDE
310 320 330 340 350
NIQRFSIAIL GHYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT
360 370 380 390 400
IVKALGERIF ALEATADQSA ASFEMEMSQT GFSAHYSQDW VMLGAVGAYD
410 420 430 440 450
WNGTVVMQKA NQMVIPHNTT FQTEPAKMNE PLASYLGYTV NSATIPGDVL
460 470 480 490 500
YIAGQPRYNH TGQVVIYKME DGNINILQTL GGEQIGSYFG SVLTTIDIDK
510 520 530 540 550
DSYTDLLLVG APMYMGTEKE EQGKVYVYAV NQTRFEYQMS LEPIRQTCCS
560 570 580 590 600
SLKDNSCTKE NKNEPCGARF GTAIAAVKDL NVDGFNDVVI GAPLEDDHAG
610 620 630 640 650
AVYIYHGSGK TIREAYAQRI PSGGDGKTLK FFGQSIHGEM DLNGDGLTDV
660 670 680 690 700
TIGGLGGAAL FWARDVAVVK VTMNFEPNKV NIQKKNCRVE GKETVCINAT
710 720 730 740 750
MCFHVKLKSK EDSIYEADLQ YRVTLDSLRQ ISRSFFSGTQ ERKIQRNITV
760 770 780 790 800
RESECIRHSF YMLDKHDFQD SVRVTLDFNL TDPENGPVLD DALPNSVHEH
810 820 830 840 850
IPFAKDCGNK ERCISDLTLN VSTTEKSLLI VKSQHDKFNV SLTVKNKGDS
860 870 880 890 900
AYNTRTVVQH SPNLIFSGIE EIQKDSCESN QNITCRVGYP FLRAGETVTF
910 920 930 940 950
KIIFQFNTSH LSENAIIHLS ATSDSEEPLE SLNDNEVNIS IPVKYEVGLQ
960 970 980 990 1000
FYSSASEHHI SVAANETIPE FINSTEDIGN EINVFYTIRK RGHFPMPELQ
1010 1020 1030 1040 1050
LSISFPNLTA DGYPVLYPIG WSSSDNVNCR PRSLEDPFGI NSGKKMTISK
1060 1070 1080 1090 1100
SEVLKRGTIQ DCSSTCGVAT ITCSLLPSDL SQVNVSLLLW KPTFIRAHFS
1110 1120 1130 1140 1150
SLNLTLRGEL KSENSSLTLS SSNRKRELAI QISKDGLPGR VPLWVILLSA
1160 1170 1180
FAGLLLLMLL ILALWKIGFF KRPLKKKMEK
Length:1,180
Mass (Da):130,809
Last modified:November 1, 1990 - v1
Checksum:i8E5DA2BE02362EE4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52140 mRNA. Translation: CAA36384.1.
PIRiA35854.
RefSeqiNP_112256.1. NM_030994.2.
UniGeneiRn.91044.

Genome annotation databases

EnsembliENSRNOT00000086114; ENSRNOP00000074337; ENSRNOG00000053550.
GeneIDi25118.
KEGGirno:25118.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52140 mRNA. Translation: CAA36384.1.
PIRiA35854.
RefSeqiNP_112256.1. NM_030994.2.
UniGeneiRn.91044.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CK4X-ray2.20A/B167-364[»]
1MHPX-ray2.80A/B169-360[»]
2B2XX-ray2.20A/B151-364[»]
ProteinModelPortaliP18614.
SMRiP18614. Positions 169-362, 1139-1173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18614. 1 interaction.
MINTiMINT-1889950.
STRINGi10116.ENSRNOP00000016353.

PTM databases

iPTMnetiP18614.
PhosphoSiteiP18614.
UniCarbKBiP18614.

Proteomic databases

PaxDbiP18614.
PRIDEiP18614.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000086114; ENSRNOP00000074337; ENSRNOG00000053550.
GeneIDi25118.
KEGGirno:25118.

Organism-specific databases

CTDi3672.
RGDi2923. Itga1.

Phylogenomic databases

eggNOGiENOG410IPB7. Eukaryota.
ENOG410YEM8. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000059610.
HOVERGENiHBG006185.
InParanoidiP18614.
KOiK06480.
OMAiQRFSIAI.
OrthoDBiEOG7GBFW6.
PhylomeDBiP18614.

Enzyme and pathway databases

ReactomeiR-RNO-216083. Integrin cell surface interactions.
R-RNO-445355. Smooth Muscle Contraction.

Miscellaneous databases

EvolutionaryTraceiP18614.
NextBioi605489.
PROiP18614.

Gene expression databases

GenevisibleiP18614. RN.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 151-364.

Entry informationi

Entry nameiITA1_RAT
AccessioniPrimary (citable) accession number: P18614
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: January 20, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.