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P56199 (ITA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 alpha-1
Alternative name(s):
CD49 antigen-like family member A
Laminin and collagen receptor
VLA-1
CD_antigen=CD49a
Gene names
Name:ITGA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1179 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. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Ref.5

Subunit structure

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. Ref.5 Ref.6

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
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Magnesium
Metal-binding
   Molecular functionIntegrin
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cellular extravasation

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

muscle contraction

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

negative regulation of epidermal growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

neutrophil chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphoprotein phosphatase activity

Inferred from direct assay Ref.5. Source: UniProtKB

vasodilation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

basal part of cell

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integrin complex

Traceable author statement Ref.3. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

perikaryon

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncollagen binding

Traceable author statement Ref.3. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein phosphatase binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 11791151Integrin alpha-1
PRO_0000174215

Regions

Topological domain29 – 11411113Extracellular Potential
Transmembrane1142 – 116423Helical; Potential
Topological domain1165 – 117915Cytoplasmic Potential
Repeat30 – 9162FG-GAP 1
Repeat101 – 16060FG-GAP 2
Domain161 – 360200VWFA
Repeat365 – 41753FG-GAP 3
Repeat422 – 47554FG-GAP 4
Repeat476 – 53863FG-GAP 5
Repeat557 – 61559FG-GAP 6
Repeat619 – 67961FG-GAP 7
Calcium binding498 – 5069 Potential
Calcium binding580 – 5889 Potential
Calcium binding642 – 6509 Potential
Motif1167 – 11715GFFKR motif

Amino acid modifications

Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation1001N-linked (GlcNAc...) Ref.7
Glycosylation1051N-linked (GlcNAc...) Ref.7
Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Ref.7
Glycosylation3171N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Ref.7
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4181N-linked (GlcNAc...) Ref.7
Glycosylation4601N-linked (GlcNAc...) Ref.7
Glycosylation5321N-linked (GlcNAc...) Ref.4 Ref.7
Glycosylation6991N-linked (GlcNAc...) Potential
Glycosylation7481N-linked (GlcNAc...) Potential
Glycosylation7801N-linked (GlcNAc...) Ref.7
Glycosylation8401N-linked (GlcNAc...) Ref.7
Glycosylation8831N-linked (GlcNAc...) Potential
Glycosylation9081N-linked (GlcNAc...) Potential
Glycosylation9151N-linked (GlcNAc...) Potential
Glycosylation9391N-linked (GlcNAc...) Potential
Glycosylation9661N-linked (GlcNAc...) Ref.7
Glycosylation9741N-linked (GlcNAc...) Ref.7
Glycosylation10081N-linked (GlcNAc...) Ref.7
Glycosylation10731N-linked (GlcNAc...) Potential
Glycosylation10831N-linked (GlcNAc...) Potential
Glycosylation11021N-linked (GlcNAc...) Potential
Glycosylation11131N-linked (GlcNAc...) Potential
Disulfide bond82 ↔ 92 By similarity
Disulfide bond688 ↔ 697 By similarity
Disulfide bond703 ↔ 756 By similarity
Disulfide bond808 ↔ 814 By similarity
Disulfide bond878 ↔ 886 By similarity
Disulfide bond1030 ↔ 1062 By similarity
Disulfide bond1065 ↔ 1072 By similarity

Natural variations

Natural variant4801T → M.
Corresponds to variant rs4145748 [ dbSNP | Ensembl ].
VAR_034022
Natural variant6701V → I.
Corresponds to variant rs2279587 [ dbSNP | Ensembl ].
VAR_049630
Natural variant9611I → M.
Corresponds to variant rs12520591 [ dbSNP | Ensembl ].
VAR_034023
Natural variant11081E → G.
Corresponds to variant rs988574 [ dbSNP | Ensembl ].
VAR_034024

Experimental info

Sequence conflict1981E → K Ref.3
Sequence conflict2541I → T Ref.3
Sequence conflict7051D → E Ref.3

Secondary structure

................................. 1179
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56199 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1A86F30FD916C845

FASTA1,179130,848
        10         20         30         40         50         60 
MAPRPRARPG VAVACCWLLT VVLRCCVSFN VDVKNSMTFS GPVEDMFGYT VQQYENEEGK 

        70         80         90        100        110        120 
WVLIGSPLVG QPKNRTGDVY KCPVGRGESL PCVKLDLPVN TSIPNVTEVK ENMTFGSTLV 

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

       190        200        210        220        230        240 
NSIYPWDSVT AFLNDLLERM DIGPKQTQVG IVQYGENVTH EFNLNKYSST EEVLVAAKKI 

       250        260        270        280        290        300 
VQRGGRQTMT ALGIDTARKE AFTEARGARR GVKKVMVIVT DGESHDNHRL KKVIQDCEDE 

       310        320        330        340        350        360 
NIQRFSIAIL GSYNRGNLST EKFVEEIKSI ASEPTEKHFF NVSDELALVT IVKTLGERIF 

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

       430        440        450        460        470        480 
FNVESTKKNE PLASYLGYTV NSATASSGDV LYIAGQPRYN HTGQVIIYRM EDGNIKILQT 

       490        500        510        520        530        540 
LSGEQIGSYF GSILTTTDID KDSNTDILLV GAPMYMGTEK EEQGKVYVYA LNQTRFEYQM 

       550        560        570        580        590        600 
SLEPIKQTCC SSRQHNSCTT ENKNEPCGAR FGTAIAAVKD LNLDGFNDIV IGAPLEDDHG 

       610        620        630        640        650        660 
GAVYIYHGSG KTIRKEYAQR IPSGGDGKTL KFFGQSIHGE MDLNGDGLTD VTIGGLGGAA 

       670        680        690        700        710        720 
LFWSRDVAVV KVTMNFEPNK VNIQKKNCHM EGKETVCINA TVCFDVKLKS KEDTIYEADL 

       730        740        750        760        770        780 
QYRVTLDSLR QISRSFFSGT QERKVQRNIT VRKSECTKHS FYMLDKHDFQ DSVRITLDFN 

       790        800        810        820        830        840 
LTDPENGPVL DDSLPNSVHE YIPFAKDCGN KEKCISDLSL HVATTEKDLL IVRSQNDKFN 

       850        860        870        880        890        900 
VSLTVKNTKD SAYNTRTIVH YSPNLVFSGI EAIQKDSCES NHNITCKVGY PFLRRGEMVT 

       910        920        930        940        950        960 
FKILFQFNTS YLMENVTIYL SATSDSEEPP ETLSDNVVNI SIPVKYEVGL QFYSSASEYH 

       970        980        990       1000       1010       1020 
ISIAANETVP EVINSTEDIG NEINIFYLIR KSGSFPMPEL KLSISFPNMT SNGYPVLYPT 

      1030       1040       1050       1060       1070       1080 
GLSSSENANC RPHIFEDPFS INSGKKMTTS TDHLKRGTIL DCNTCKFATI TCNLTSSDIS 

      1090       1100       1110       1120       1130       1140 
QVNVSLILWK PTFIKSYFSS LNLTIRGELR SENASLVLSS SNQKRELAIQ ISKDGLPGRV 

      1150       1160       1170 
PLWVILLSAF AGLLLLMLLI LALWKIGFFK RPLKKKMEK 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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.
[3]"Expression of native and truncated forms of the human integrin alpha 1 subunit."
Briesewitz R., Epstein M.R., Marcantonio E.E.
J. Biol. Chem. 268:2989-2996(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-1179.
[4]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-532.
Tissue: Plasma.
[5]"Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP."
Mattila E., Pellinen T., Nevo J., Vuoriluoto K., Arjonen A., Ivaska J.
Nat. Cell Biol. 7:78-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EGFR SIGNALING, INTERACTION WITH PTPN2.
[6]"Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of beta1-integrins."
Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M., Ivaska J.
J. Cell Biol. 173:767-780(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB21.
[7]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-100; ASN-105; ASN-217; ASN-341; ASN-418; ASN-460; ASN-532; ASN-780; ASN-840; ASN-966; ASN-974 AND ASN-1008.
Tissue: Liver.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Trench-shaped binding sites promote multiple classes of interactions between collagen and the adherence receptors, alpha(1)beta(1) integrin and Staphylococcus aureus cna MSCRAMM."
Rich R.L., Deivanayagam C.C., Owens R.T., Carson M., Hook A., Moore D., Symersky J., Yang V.W., Narayana S.V., Hook M.
J. Biol. Chem. 274:24906-24913(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 168-359.
[10]"Jararhagin-derived RKKH peptides induce structural changes in alpha1I domain of human integrin alpha1beta1."
Nymalm Y., Puranen J.S., Nyholm T.K., Kapyla J., Kidron H., Pentikainen O.T., Airenne T.T., Heino J., Slotte J.P., Johnson M.S., Salminen T.A.
J. Biol. Chem. 279:7962-7970(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 166-356.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA45226.
RefSeqNP_852478.1. NM_181501.1.
UniGeneHs.644352.

3D structure databases

PDBe
RCSB PDB
PDBj
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/B168-366[»]
ProteinModelPortalP56199.
SMRP56199. Positions 29-1081, 1135-1179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109879. 8 interactions.
DIPDIP-206N.
IntActP56199. 6 interactions.
MINTMINT-7004837.
STRING9606.ENSP00000282588.

Chemistry

BindingDBP56199.
ChEMBLCHEMBL3682.

PTM databases

PhosphoSiteP56199.

Polymorphism databases

DMDM124056463.

Proteomic databases

PaxDbP56199.
PRIDEP56199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282588; ENSP00000282588; ENSG00000213949.
GeneID3672.
KEGGhsa:3672.
UCSCuc003jou.3. human.

Organism-specific databases

CTD3672.
GeneCardsGC05P052083.
HGNCHGNC:6134. ITGA1.
HPAHPA042555.
MIM192968. gene.
neXtProtNX_P56199.
PharmGKBPA29935.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322251.
HOGENOMHOG000059610.
HOVERGENHBG006185.
InParanoidP56199.
KOK06480.
OMAQRFSIAI.
OrthoDBEOG7GBFW6.
PhylomeDBP56199.
TreeFamTF105391.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_118779. Extracellular matrix organization.
REACT_17044. Muscle contraction.
REACT_604. Hemostasis.
SignaLinkP56199.

Gene expression databases

BgeeP56199.
GenevestigatorP56199.

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]
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]
SUPFAMSSF53300. SSF53300. 1 hit.
PROSITEPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP56199.
GeneWikiCD49a.
GenomeRNAi3672.
NextBio14373.
PROP56199.
SOURCESearch...

Entry information

Entry nameITA1_HUMAN
AccessionPrimary (citable) accession number: P56199
Secondary accession number(s): B2RNU0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries