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Reviewed, UniProtKB/Swiss-Prot P56199 (ITA1_HUMAN)

Last modified November 25, 2008. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Integrin alpha-1
Alternative name(s):
    Laminin and collagen receptor
    VLA-1
    CD49 antigen-like family member A
    CD_antigen=CD49a
Gene names
Name: ITGA1
OrganismHomo sapiens (Human)
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.

Subunit structure

Heterodimer of an alpha and a beta subunit. Alpha-1 associates with beta-1.

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
   LigandCalcium
Magnesium
   Molecular functionIntegrin
Receptor
   PTMGlycoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processcell-matrix adhesion

Non-traceable author statement. Source: UniProtKB

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegrin complex Ref.2

Traceable author statement. Source: UniProtKB

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

collagen binding Ref.2

Traceable author statement. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 Potential
Chain29 – 11791151Integrin alpha-1
PRO_0000174215

Regions

Topological domain29 – 11411113Extracellular Potential
Transmembrane1142 – 116423 Potential
Topological domain1165 – 117915Cytoplasmic Potential
Repeat44 – 10360FG-GAP 1
Repeat104 – ?FG-GAP 2
Domain147 – 360214VWFA
Repeat349 – 40456FG-GAP 3
Repeat405 – 45753FG-GAP 4
Repeat459 – 52062FG-GAP 5
Repeat540 – 59960FG-GAP 6
Repeat602 – 65453FG-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...) 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
Glycosylation4601N-linked (GlcNAc...) Potential
Glycosylation5321N-linked (GlcNAc...)
Glycosylation6991N-linked (GlcNAc...) Potential
Glycosylation7481N-linked (GlcNAc...) Potential
Glycosylation7801N-linked (GlcNAc...) Potential
Glycosylation8401N-linked (GlcNAc...) Potential
Glycosylation8831N-linked (GlcNAc...) Potential
Glycosylation9081N-linked (GlcNAc...) Potential
Glycosylation9151N-linked (GlcNAc...) Potential
Glycosylation9391N-linked (GlcNAc...) Potential
Glycosylation9661N-linked (GlcNAc...) Potential
Glycosylation9741N-linked (GlcNAc...) Potential
Glycosylation10081N-linked (GlcNAc...) Potential
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: dbSNP rs4145748.
VAR_034022
Natural variant9611I → M: dbSNP rs12520591.
VAR_034023
Natural variant11081E → G: dbSNP rs988574.
VAR_034024

Experimental info

Sequence conflict1981E → K Ref.2
Sequence conflict2541I → T Ref.2
Sequence conflict7051D → E Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P56199-1 [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: 15372022] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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: 8428973] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-1179.
[3]"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: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-532, MASS SPECTROMETRY.
Tissue: Plasma.
[4]"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: 10455165] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 168-359.
[5]"Jararhagin-derived RKKH peptides induce structural changes in alpha1I domain of human integrin alpha1beta1."
Nymalm Y., Puranen J.S., Nyholm T.K., K