Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Calcium bindingi497 – 505Sequence analysis9
Calcium bindingi579 – 587Sequence analysis9
Calcium bindingi641 – 649Sequence analysis9

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)DescriptionActionsGraphical viewLength
Topological domaini29 – 1142ExtracellularSequence analysisAdd BLAST1114
Transmembranei1143 – 1165HelicalSequence analysisAdd BLAST23
Topological domaini1166 – 1180CytoplasmicSequence analysisAdd BLAST15

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Add BLAST28
ChainiPRO_000001623129 – 1180Integrin alpha-1Add BLAST1152

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi82 ↔ 92By similarity
Glycosylationi100N-linked (GlcNAc...)Sequence analysis1
Glycosylationi105N-linked (GlcNAc...)Sequence analysis1
Glycosylationi112N-linked (GlcNAc...)Sequence analysis1
Glycosylationi217N-linked (GlcNAc...)Sequence analysis1
Glycosylationi317N-linked (GlcNAc...)Sequence analysis1
Glycosylationi341N-linked (GlcNAc...)Sequence analysis1
Glycosylationi402N-linked (GlcNAc...)Sequence analysis1
Glycosylationi418N-linked (GlcNAc...)Sequence analysis1
Glycosylationi459N-linked (GlcNAc...)Sequence analysis1
Glycosylationi531N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi687 ↔ 696By similarity
Glycosylationi698N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi702 ↔ 755By similarity
Glycosylationi747N-linked (GlcNAc...)Sequence analysis1
Glycosylationi779N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi807 ↔ 813By similarity
Glycosylationi820N-linked (GlcNAc...)Sequence analysis1
Glycosylationi839N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi877 ↔ 885By similarity
Glycosylationi882N-linked (GlcNAc...)Sequence analysis1
Glycosylationi907N-linked (GlcNAc...)Sequence analysis1
Glycosylationi938N-linked (GlcNAc...)Sequence analysis1
Glycosylationi965N-linked (GlcNAc...)Sequence analysis1
Glycosylationi973N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1007N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1029 ↔ 1062By similarity
Disulfide bondi1066 ↔ 1073By similarity
Glycosylationi1084N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1103N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1114N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP18614.
PRIDEiP18614.

PTM databases

iPTMnetiP18614.
PhosphoSitePlusiP18614.
UniCarbKBiP18614.

Expressioni

Gene expression databases

BgeeiENSRNOG00000012080.
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 interactor.
MINTiMINT-1889950.
STRINGi10116.ENSRNOP00000016353.

Structurei

Secondary structure

11180
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi171 – 178Combined sources8
Helixi186 – 197Combined sources12
Beta strandi208 – 222Combined sources15
Turni224 – 226Combined sources3
Helixi230 – 238Combined sources9
Helixi250 – 259Combined sources10
Turni260 – 262Combined sources3
Helixi264 – 266Combined sources3
Beta strandi273 – 282Combined sources10
Helixi287 – 289Combined sources3
Helixi290 – 299Combined sources10
Beta strandi302 – 309Combined sources8
Helixi311 – 315Combined sources5
Helixi321 – 328Combined sources8
Helixi335 – 338Combined sources4
Beta strandi339 – 345Combined sources7
Helixi346 – 350Combined sources5
Helixi352 – 359Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP18614.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati30 – 91FG-GAP 1PROSITE-ProRule annotationAdd BLAST62
Repeati101 – 160FG-GAP 2PROSITE-ProRule annotationAdd BLAST60
Domaini175 – 364VWFAPROSITE-ProRule annotationAdd BLAST190
Repeati365 – 417FG-GAP 3PROSITE-ProRule annotationAdd BLAST53
Repeati422 – 474FG-GAP 4PROSITE-ProRule annotationAdd BLAST53
Repeati475 – 537FG-GAP 5PROSITE-ProRule annotationAdd BLAST63
Repeati556 – 614FG-GAP 6PROSITE-ProRule annotationAdd BLAST59
Repeati618 – 678FG-GAP 7PROSITE-ProRule annotationAdd BLAST61

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1168 – 1172GFFKR motif5

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.PROSITE-ProRule annotation
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.
OrthoDBiEOG091G00TK.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CK4X-ray2.20A/B167-364[»]
1MHPX-ray2.80A/B169-360[»]
2B2XX-ray2.20A/B151-364[»]
ProteinModelPortaliP18614.
SMRiP18614.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP18614.
PhosphoSitePlusiP18614.
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.
OrthoDBiEOG091G00TK.
PhylomeDBiP18614.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP18614.
PROiP18614.

Gene expression databases

BgeeiENSRNOG00000012080.
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...

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: November 2, 2016
This is version 150 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.