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Protein

Integrin alpha-1

Gene

ITGA1

Organism
Homo sapiens (Human)
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.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi498 – 506Sequence analysis9
Calcium bindingi580 – 588Sequence analysis9
Calcium bindingi642 – 650Sequence analysis9

GO - Molecular functioni

  • collagen binding Source: UniProtKB
  • collagen binding involved in cell-matrix adhesion Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein phosphatase binding Source: UniProtKB
  • receptor binding Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionIntegrin, Receptor
Biological processCell adhesion
LigandCalcium, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-216083. Integrin cell surface interactions.
R-HSA-3000157. Laminin interactions.
R-HSA-416700. Other semaphorin interactions.
R-HSA-445355. Smooth Muscle Contraction.
R-HSA-447041. CHL1 interactions.
R-HSA-75892. Platelet Adhesion to exposed collagen.
SignaLinkiP56199.
SIGNORiP56199.

Protein family/group databases

TCDBi8.A.54.1.1. the integrin (integrin) family.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000213949.8.
HGNCiHGNC:6134. ITGA1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini29 – 1141ExtracellularSequence analysisAdd BLAST1113
Transmembranei1142 – 1164HelicalSequence analysisAdd BLAST23
Topological domaini1165 – 1179CytoplasmicSequence analysisAdd BLAST15

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi3672.
OpenTargetsiENSG00000213949.
PharmGKBiPA29935.

Chemistry databases

ChEMBLiCHEMBL3682.
GuidetoPHARMACOLOGYi2437.

Polymorphism and mutation databases

BioMutaiITGA1.
DMDMi124056463.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000017421529 – 1179Integrin alpha-1Add BLAST1151

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi74N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi82 ↔ 92By similarity
Glycosylationi100N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi105N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi112N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi217N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi317N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi341N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi402N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi418N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi460N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi532N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi688 ↔ 697By similarity
Glycosylationi699N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi703 ↔ 756By similarity
Glycosylationi748N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi780N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi808 ↔ 814By similarity
Glycosylationi840N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi878 ↔ 886By similarity
Glycosylationi883N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi908N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi915N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi939N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi966N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi974N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1008N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi1030 ↔ 1062By similarity
Disulfide bondi1065 ↔ 1072By similarity
Glycosylationi1073N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1083N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1102N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1113N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP56199.
MaxQBiP56199.
PaxDbiP56199.
PeptideAtlasiP56199.
PRIDEiP56199.

PTM databases

iPTMnetiP56199.
PhosphoSitePlusiP56199.

Expressioni

Gene expression databases

BgeeiENSG00000213949.
GenevisibleiP56199. HS.

Organism-specific databases

HPAiHPA042555.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Alpha-1 associates with beta-1. Interacts with RAB21. Interacts (via cytoplasmic domain) with PTPN2; activates PTPN2 phosphatase activity towards EGFR and negatively regulates EGF signaling.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P045122EBI-2554465,EBI-15711650From Rotavirus A (strain RVA/SA11-Both/G3P5B[2]).

GO - Molecular functioni

  • collagen binding Source: UniProtKB
  • collagen binding involved in cell-matrix adhesion Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • receptor binding Source: Ensembl

Protein-protein interaction databases

BioGridi109879. 18 interactors.
CORUMiP56199.
DIPiDIP-206N.
IntActiP56199. 15 interactors.
MINTiMINT-7004837.
STRINGi9606.ENSP00000282588.

Chemistry databases

BindingDBiP56199.

Structurei

Secondary structure

11179
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi171 – 178Combined sources8
Helixi187 – 197Combined sources11
Beta strandi206 – 222Combined sources17
Turni224 – 226Combined sources3
Helixi230 – 238Combined sources9
Helixi250 – 259Combined sources10
Turni260 – 262Combined sources3
Helixi264 – 266Combined sources3
Beta strandi272 – 282Combined sources11
Helixi287 – 289Combined sources3
Helixi290 – 299Combined sources10
Beta strandi302 – 309Combined sources8
Helixi311 – 315Combined sources5
Helixi321 – 330Combined sources10
Helixi335 – 338Combined sources4
Beta strandi339 – 344Combined sources6
Helixi345 – 351Combined sources7
Helixi352 – 359Combined sources8
Helixi1143 – 1168Combined sources26

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PT6X-ray1.87A/B166-366[»]
1QC5X-ray2.00A/B168-359[»]
1QCYX-ray2.30A169-361[»]
2L8SNMR-A1135-1179[»]
2M32NMR-A168-359[»]
4A0QX-ray1.90A/B166-366[»]
5HGJX-ray1.40A/B170-364[»]
ProteinModelPortaliP56199.
SMRiP56199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56199.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati30 – 91FG-GAP 1PROSITE-ProRule annotationAdd BLAST62
Repeati101 – 160FG-GAP 2PROSITE-ProRule annotationAdd BLAST60
Domaini161 – 360VWFAPROSITE-ProRule annotationAdd BLAST200
Repeati365 – 417FG-GAP 3PROSITE-ProRule annotationAdd BLAST53
Repeati422 – 475FG-GAP 4PROSITE-ProRule annotationAdd BLAST54
Repeati476 – 538FG-GAP 5PROSITE-ProRule annotationAdd BLAST63
Repeati557 – 615FG-GAP 6PROSITE-ProRule annotationAdd BLAST59
Repeati619 – 679FG-GAP 7PROSITE-ProRule annotationAdd BLAST61

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1167 – 1171GFFKR 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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPB7. Eukaryota.
ENOG410YEM8. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000059610.
HOVERGENiHBG006185.
InParanoidiP56199.
KOiK06480.
OMAiQRFSIAI.
OrthoDBiEOG091G00TK.
PhylomeDBiP56199.
TreeFamiTF105391.

Family and domain databases

InterProiView protein in InterPro
IPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom_sf.
IPR002035. VWF_A.
IPR036465. vWFA_dom_sf.
PfamiView protein in Pfam
PF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
PF00092. VWA. 1 hit.
PRINTSiPR01185. INTEGRINA.
SMARTiView protein in SMART
SM00191. Int_alpha. 5 hits.
SM00327. VWA. 1 hit.
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 3 hits.
PROSITEiView protein in PROSITE
PS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P56199-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPRPRARPG VAVACCWLLT VVLRCCVSFN VDVKNSMTFS GPVEDMFGYT
60 70 80 90 100
VQQYENEEGK WVLIGSPLVG QPKNRTGDVY KCPVGRGESL PCVKLDLPVN
110 120 130 140 150
TSIPNVTEVK ENMTFGSTLV TNPNGGFLAC GPLYAYRCGH LHYTTGICSD
160 170 180 190 200
VSPTFQVVNS IAPVQECSTQ LDIVIVLDGS NSIYPWDSVT AFLNDLLERM
210 220 230 240 250
DIGPKQTQVG IVQYGENVTH EFNLNKYSST EEVLVAAKKI VQRGGRQTMT
260 270 280 290 300
ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNHRL KKVIQDCEDE
310 320 330 340 350
NIQRFSIAIL GSYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT
360 370 380 390 400
IVKTLGERIF ALEATADQSA ASFEMEMSQT GFSAHYSQDW VMLGAVGAYD
410 420 430 440 450
WNGTVVMQKA SQIIIPRNTT FNVESTKKNE PLASYLGYTV NSATASSGDV
460 470 480 490 500
LYIAGQPRYN HTGQVIIYRM EDGNIKILQT LSGEQIGSYF GSILTTTDID
510 520 530 540 550
KDSNTDILLV GAPMYMGTEK EEQGKVYVYA LNQTRFEYQM SLEPIKQTCC
560 570 580 590 600
SSRQHNSCTT ENKNEPCGAR FGTAIAAVKD LNLDGFNDIV IGAPLEDDHG
610 620 630 640 650
GAVYIYHGSG KTIRKEYAQR IPSGGDGKTL KFFGQSIHGE MDLNGDGLTD
660 670 680 690 700
VTIGGLGGAA LFWSRDVAVV KVTMNFEPNK VNIQKKNCHM EGKETVCINA
710 720 730 740 750
TVCFDVKLKS KEDTIYEADL QYRVTLDSLR QISRSFFSGT QERKVQRNIT
760 770 780 790 800
VRKSECTKHS FYMLDKHDFQ DSVRITLDFN LTDPENGPVL DDSLPNSVHE
810 820 830 840 850
YIPFAKDCGN KEKCISDLSL HVATTEKDLL IVRSQNDKFN VSLTVKNTKD
860 870 880 890 900
SAYNTRTIVH YSPNLVFSGI EAIQKDSCES NHNITCKVGY PFLRRGEMVT
910 920 930 940 950
FKILFQFNTS YLMENVTIYL SATSDSEEPP ETLSDNVVNI SIPVKYEVGL
960 970 980 990 1000
QFYSSASEYH ISIAANETVP EVINSTEDIG NEINIFYLIR KSGSFPMPEL
1010 1020 1030 1040 1050
KLSISFPNMT SNGYPVLYPT GLSSSENANC RPHIFEDPFS INSGKKMTTS
1060 1070 1080 1090 1100
TDHLKRGTIL DCNTCKFATI TCNLTSSDIS QVNVSLILWK PTFIKSYFSS
1110 1120 1130 1140 1150
LNLTIRGELR SENASLVLSS SNQKRELAIQ ISKDGLPGRV PLWVILLSAF
1160 1170
AGLLLLMLLI LALWKIGFFK RPLKKKMEK
Length:1,179
Mass (Da):130,848
Last modified:January 23, 2007 - v2
Checksum:i1A86F30FD916C845
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti198E → K (PubMed:8428973).Curated1
Sequence conflicti254I → T (PubMed:8428973).Curated1
Sequence conflicti705D → E (PubMed:8428973).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034022480T → M. Corresponds to variant dbSNP:rs4145748Ensembl.1
Natural variantiVAR_049630670V → I. Corresponds to variant dbSNP:rs2279587Ensembl.1
Natural variantiVAR_034023961I → M. Corresponds to variant dbSNP:rs12520591Ensembl.1
Natural variantiVAR_0340241108E → G. Corresponds to variant dbSNP:rs988574Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC027326 Genomic DNA. No translation available.
AC022133 Genomic DNA. No translation available.
AC025180 Genomic DNA. No translation available.
BC137121 mRNA. Translation: AAI37122.1.
BC137122 mRNA. Translation: AAI37123.1.
X68742 mRNA. No translation available.
CCDSiCCDS3955.1.
PIRiA45226.
RefSeqiNP_852478.1. NM_181501.1.
UniGeneiHs.644352.

Genome annotation databases

EnsembliENST00000282588; ENSP00000282588; ENSG00000213949.
GeneIDi3672.
KEGGihsa:3672.
UCSCiuc003jou.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiITA1_HUMAN
AccessioniPrimary (citable) accession number: P56199
Secondary accession number(s): B2RNU0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 177 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families