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Reviewed, UniProtKB/Swiss-Prot P20702 (ITAX_HUMAN)

Last modified November 24, 2009. Version 107. 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-X
Alternative name(s):
    Leukocyte adhesion glycoprotein p150,95 alpha chain
    Leukocyte adhesion receptor p150,95
    Leu M5
    CD11 antigen-like family member C
    CD_antigen=CD11c
Gene names
Name: ITGAX
Synonyms: CD11C
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1163 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-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis.

Subunit structure

Heterodimer of an alpha and a beta subunit. Alpha-X associates with beta-2.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Predominantly expressed in monocytes and granulocytes.

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
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcell adhesion Ref.2

Traceable author statement. Source: ProtInc

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

organ morphogenesis Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentintegrin complex Ref.2

Traceable author statement. Source: ProtInc

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: UniProtKB

receptor activity Ref.2

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.5
Chain20 – 11631144Integrin alpha-X
PRO_0000016294

Regions

Topological domain20 – 11071088Extracellular Potential
Transmembrane1108 – 112821 Potential
Topological domain1129 – 116335Cytoplasmic Potential
Repeat34 – 8754FG-GAP 1
Repeat88 – ?FG-GAP 2
Domain165 – 351187VWFA
Repeat? – 401FG-GAP 3
Repeat402 – 45352FG-GAP 4
Repeat455 – 51763FG-GAP 5
Repeat518 – 57659FG-GAP 6
Repeat581 – 63353FG-GAP 7
Calcium binding466 – 4749 Potential
Calcium binding530 – 5389 Potential
Calcium binding593 – 6019 Potential
Motif1131 – 11355GFFKR motif

Amino acid modifications

Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation6971N-linked (GlcNAc...) Potential
Glycosylation7351N-linked (GlcNAc...) Potential
Glycosylation8991N-linked (GlcNAc...) Ref.6
Glycosylation9391N-linked (GlcNAc...) Potential
Glycosylation10501N-linked (GlcNAc...) Potential
Disulfide bond69 ↔ 76 By similarity
Disulfide bond108 ↔ 126 By similarity
Disulfide bond655 ↔ 712 By similarity
Disulfide bond771 ↔ 777 By similarity
Disulfide bond848 ↔ 863 By similarity
Disulfide bond998 ↔ 1022 By similarity
Disulfide bond1027 ↔ 1032 By similarity

Natural variations

Natural variant481W → R: dbSNP rs2230424.
VAR_018672
Natural variant2011F → L: dbSNP rs1574566. Ref.2
VAR_049632
Natural variant2511A → T: dbSNP rs2230428. Ref.2 Ref.1
VAR_031925
Natural variant5171P → R: dbSNP rs2230429.
VAR_031926
Natural variant5471E → K: dbSNP rs17853815. Ref.4
VAR_031927
Natural variant5641I → V: dbSNP rs2230430.
VAR_059363
Natural variant9711F → L: dbSNP rs2230427.
VAR_031928

Experimental info

Sequence conflict2091S → T in AAA59180. Ref.1
Sequence conflict2091S → T in AAA51620. Ref.2
Sequence conflict2661S → T in AAA51620. Ref.2
Sequence conflict3271N → T in AAA51620. Ref.2
Sequence conflict3301K → R in AAA51620. Ref.2
Sequence conflict3351A → P in AAA51620. Ref.2
Sequence conflict4601A → P in AAA51620. Ref.2
Sequence conflict4691S → T in AAA59180. Ref.1
Sequence conflict4801A → P in AAA51620. Ref.2
Sequence conflict4901G → A in AAA51620. Ref.2
Sequence conflict7561D → L in AAA59180. Ref.1
Sequence conflict8191I → V in AAH38237. Ref.4
Sequence conflict9901H → L in AAA51620. Ref.2
Sequence conflict10051P → G in AAA51620. Ref.2
Sequence conflict1161 – 11633SEK → TPHYPQDNV in AAH38237. Ref.4

Secondary structure

................................ 1163
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20702-1 [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: 8947288C43E76BE2

FASTA1,163127,829
        10         20         30         40         50         60 
MTRTRAALLL FTALATSLGF NLDTEELTAF RVDSAGFGDS VVQYANSWVV VGAPQKITAA 

        70         80         90        100        110        120 
NQTGGLYQCG YSTGACEPIG LQVPPEAVNM SLGLSLASTT SPSQLLACGP TVHHECGRNM 

       130        140        150        160        170        180 
YLTGLCFLLG PTQLTQRLPV SRQECPRQEQ DIVFLIDGSG SISSRNFATM MNFVRAVISQ 

       190        200        210        220        230        240 
FQRPSTQFSL MQFSNKFQTH FTFEEFRRSS NPLSLLASVH QLQGFTYTAT AIQNVVHRLF 

       250        260        270        280        290        300 
HASYGARRDA AKILIVITDG KKEGDSLDYK DVIPMADAAG IIRYAIGVGL AFQNRNSWKE 

       310        320        330        340        350        360 
LNDIASKPSQ EHIFKVEDFD ALKDIQNQLK EKIFAIEGTE TTSSSSFELE MAQEGFSAVF 

       370        380        390        400        410        420 
TPDGPVLGAV GSFTWSGGAF LYPPNMSPTF INMSQENVDM RDSYLGYSTE LALWKGVQSL 

       430        440        450        460        470        480 
VLGAPRYQHT GKAVIFTQVS RQWRMKAEVT GTQIGSYFGA SLCSVDVDSD GSTDLVLIGA 

       490        500        510        520        530        540 
PHYYEQTRGG QVSVCPLPRG WRRWWCDAVL YGEQGHPWGR FGAALTVLGD VNGDKLTDVV 

       550        560        570        580        590        600 
IGAPGEEENR GAVYLFHGVL GPSISPSHSQ RIAGSQLSSR LQYFGQALSG GQDLTQDGLV 

       610        620        630        640        650        660 
DLAVGARGQV LLLRTRPVLW VGVSMQFIPA EIPRSAFECR EQVVSEQTLV QSNICLYIDK 

       670        680        690        700        710        720 
RSKNLLGSRD LQSSVTLDLA LDPGRLSPRA TFQETKNRSL SRVRVLGLKA HCENFNLLLP 

       730        740        750        760        770        780 
SCVEDSVTPI TLRLNFTLVG KPLLAFRNLR PMLAADAQRY FTASLPFEKN CGADHICQDN 

       790        800        810        820        830        840 
LGISFSFPGL KSLLVGSNLE LNAEVMVWND GEDSYGTTIT FSHPAGLSYR YVAEGQKQGQ 

       850        860        870        880        890        900 
LRSLHLTCDS APVGSQGTWS TSCRINHLIF RGGAQITFLA TFDVSPKAVL GDRLLLTANV 

       910        920        930        940        950        960 
SSENNTPRTS KTTFQLELPV KYAVYTVVSS HEQFTKYLNF SESEEKESHV AMHRYQVNNL 

       970        980        990       1000       1010       1020 
GQRDLPVSIN FWVPVELNQE AVWMDVEVSH PQNPSLRCSS EKIAPPASDF LAHIQKNPVL 

      1030       1040       1050       1060       1070       1080 
DCSIAGCLRF RCDVPSFSVQ EELDFTLKGN LSFGWVRQIL QKKVSVVSVA EITFDTSVYS 

      1090       1100       1110       1120       1130       1140 
QLPGQEAFMR AQTTTVLEKY KVHNPTPLIV GSSIGGLLLL ALITAVLYKV GFFKRQYKEM 

      1150       1160 
MEEANGQIAP ENGTQTPSPP SEK 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and complete primary structure of the alpha subunit of a leukocyte adhesion glycoprotein, p150,95."
Corbi A.L., Miller L.J., O'Connor K., Larson R.S., Springer T.A.
EMBO J. 6:4023-4028(1987) [PubMed: 3327687] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-251.
[2]"Genomic structure of an integrin alpha subunit, the leukocyte p150,95 molecule."
Corbi A.L., Garcia-Aguilar J., Springer T.A.
J. Biol. Chem. 265:2782-2788(1990) [PubMed: 2303426] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-201 AND THR-251.
[3]Erratum
Corbi A.L., Garcia-Aguilar J., Springer T.A.
J. Biol. Chem. 265:12750-12751(1990)
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-547.
Tissue: Blood.
[5]"Purification and alpha subunit N-terminal sequences of human Mac-1 and p150,95 leukocyte adhesion proteins."
Miller L.J., Wiebe M., Springer T.A.
J. Immunol. 138:2381-2383(1987) [PubMed: 3549901] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-43.
[6]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-899, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

M81695 mRNA. Translation: AAA59180.1.
M29165 mRNA. No translation available.
M29487 expand/collapse EMBL AC list , M29482, M29483, M29484, M29485, M29486 Genomic DNA. Translation: AAA51620.1. Sequence problems.
BC038237 mRNA. Translation: AAH38237.1.
IPIIPI00302270.
PIRRWHU1C. A36584.
RefSeqNP_000878.2.
UniGeneHs.248472

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1N3YX-ray1.65A147-338[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP20702.

Proteomic databases

PRIDEP20702.

Genome annotation databases

EnsemblENST00000268296; ENSP00000268296; ENSG00000140678; Homo sapiens. [Genome view]
GeneID3687.
KEGGhsa:3687.
UCSCuc002ebu.1. human.

Organism-specific databases

CTD3687.
GeneCardsGC16P031274.
HGNCHGNC:6152. ITGAX.
HPACAB004458.
HPA004723.
MIM151510. gene.
PharmGKBPA29952.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP20702.
HOVERGENP20702.
OMAVMSQFQR
OrthoDBEOG9MD0JP

Enzyme and pathway databases

ReactomeREACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP20702.
BgeeP20702.
CleanExHS_ITGAX.
GenevestigatorP20702.
GermOnlineENSG00000140678. Homo sapiens.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR013513. Integrin_alpha_C.
IPR018184. Integrin_alpha_C_CS.
IPR002035. VWF_A.
[Graphical view]
PfamPF01839. FG-GAP. 3 hits.
PF00357. Integrin_alpha. 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]
PROSITEPS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio14429.
SOURCESearch...

Entry information

Entry nameITAX_HUMAN
AccessionPrimary (citable) accession number: P20702
Secondary accession number(s): Q8IVA6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 1, 2007
Last modified: November 24, 2009
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human cell differentiation molecules

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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents