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P20702 (ITAX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. 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-X
Alternative name(s):
CD11 antigen-like family member C
Leu M5
Leukocyte adhesion glycoprotein p150,95 alpha chain
Leukocyte adhesion receptor p150,95
CD_antigen=CD11c
Gene names
Name:ITGAX
Synonyms:CD11C
OrganismHomo sapiens (Human) [Reference 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. Ref.7

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.

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 – 112821Helical; Potential
Topological domain1129 – 116335Cytoplasmic Potential
Repeat23 – 7856FG-GAP 1
Repeat79 – 13860FG-GAP 2
Domain165 – 339175VWFA
Repeat340 – 39152FG-GAP 3
Repeat392 – 44554FG-GAP 4
Repeat446 – 50459FG-GAP 5
Repeat507 – 56559FG-GAP 6
Repeat570 – 63061FG-GAP 7
Calcium binding466 – 4749
Calcium binding530 – 5389
Calcium binding593 – 6019
Motif1131 – 11355GFFKR motif

Sites

Metal binding1571Magnesium
Metal binding1591Magnesium
Metal binding1611Magnesium
Metal binding2591Magnesium
Metal binding4661Calcium 2
Metal binding4681Calcium 2
Metal binding4701Calcium 2
Metal binding4721Calcium 2; via carbonyl oxygen
Metal binding5321Calcium 3
Metal binding5341Calcium 3
Metal binding5361Calcium 3; via carbonyl oxygen
Metal binding5931Calcium 1
Metal binding5951Calcium 1
Metal binding5971Calcium 1
Metal binding5991Calcium 1; via carbonyl oxygen
Metal binding6011Calcium 1

Amino acid modifications

Glycosylation611N-linked (GlcNAc...) Ref.7
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Ref.7
Glycosylation6971N-linked (GlcNAc...) Ref.7
Glycosylation7351N-linked (GlcNAc...) Ref.7
Glycosylation8991N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation9391N-linked (GlcNAc...) Potential
Glycosylation10501N-linked (GlcNAc...) Potential
Disulfide bond69 ↔ 76 Ref.7
Disulfide bond108 ↔ 126 Ref.7
Disulfide bond116 ↔ 145 Ref.7
Disulfide bond495 ↔ 506 Ref.7
Disulfide bond639 ↔ 722 Ref.7
Disulfide bond655 ↔ 712 Ref.7
Disulfide bond771 ↔ 777 Ref.7
Disulfide bond848 ↔ 863 Ref.7
Disulfide bond998 ↔ 1022 Ref.7
Disulfide bond1027 ↔ 1032 Ref.7

Natural variations

Natural variant481W → R.
Corresponds to variant rs2230424 [ dbSNP | Ensembl ].
VAR_018672
Natural variant2011F → L. Ref.2
Corresponds to variant rs1574566 [ dbSNP | Ensembl ].
VAR_049632
Natural variant2511A → T. Ref.1 Ref.2
Corresponds to variant rs2230428 [ dbSNP | Ensembl ].
VAR_031925
Natural variant5171P → R.
Corresponds to variant rs2230429 [ dbSNP | Ensembl ].
VAR_031926
Natural variant5471E → K. Ref.4
Corresponds to variant rs17853815 [ dbSNP | Ensembl ].
VAR_031927
Natural variant5641I → V.
Corresponds to variant rs2230430 [ dbSNP | Ensembl ].
VAR_059363
Natural variant9711F → L.
Corresponds to variant rs2230427 [ dbSNP | Ensembl ].
VAR_031928
Natural variant10121A → V. Ref.9
Corresponds to variant rs181404376 [ dbSNP | Ensembl ].
VAR_066662

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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-899.
Tissue: Liver.
[7]"Structure of an integrin with an alphaI domain, complement receptor type 4."
Xie C., Zhu J., Chen X., Mi L., Nishida N., Springer T.A.
EMBO J. 29:666-679(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 20-1103 IN COMPLEX WITH ITGB2, GLYCOSYLATION AT ASN-61; ASN-392; ASN-697; ASN-735 AND ASN-899, DISULFIDE BONDS, METAL-BINDING SITES, SUBUNIT.
[8]"Structure and binding interface of the cytosolic tails of alphaXbeta2 integrin."
Chua G.L., Tang X.Y., Patra A.T., Tan S.M., Bhattacharjya S.
PLoS ONE 7:E41924-E41924(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1129-1163.
[9]"VPS35 mutations in Parkinson disease."
Vilarino-Guell C., Wider C., Ross O.A., Dachsel J.C., Kachergus J.M., Lincoln S.J., Soto-Ortolaza A.I., Cobb S.A., Wilhoite G.J., Bacon J.A., Behrouz B., Melrose H.L., Hentati E., Puschmann A., Evans D.M., Conibear E., Wasserman W.W., Aasly J.O. expand/collapse author list , Burkhard P.R., Djaldetti R., Ghika J., Hentati F., Krygowska-Wajs A., Lynch T., Melamed E., Rajput A., Rajput A.H., Solida A., Wu R.M., Uitti R.J., Wszolek Z.K., Vingerhoets F., Farrer M.J.
Am. J. Hum. Genet. 89:162-167(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-1012.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRRWHU1C. A36584.
RefSeqNP_000878.2. NM_000887.4.
NP_001273304.1. NM_001286375.1.
UniGeneHs.248472.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N3YX-ray1.65A147-338[»]
2LUVNMR-A1129-1163[»]
3K6SX-ray3.50A/C/E/G20-1103[»]
3K71X-ray3.95A/C/E/G20-1103[»]
3K72X-ray3.70A/C20-1103[»]
4NEHX-ray2.75A20-1101[»]
4NENX-ray2.90A20-1101[»]
ProteinModelPortalP20702.
SMRP20702. Positions 20-1101, 1129-1163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109893. 1 interaction.
DIPDIP-59369N.
IntActP20702. 1 interaction.
STRING9606.ENSP00000268296.

PTM databases

PhosphoSiteP20702.

Polymorphism databases

DMDM146345441.

Proteomic databases

PaxDbP20702.
PRIDEP20702.

Protocols and materials databases

DNASU3687.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268296; ENSP00000268296; ENSG00000140678.
GeneID3687.
KEGGhsa:3687.
UCSCuc002ebu.1. human.

Organism-specific databases

CTD3687.
GeneCardsGC16P031366.
H-InvDBHIX0012988.
HGNCHGNC:6152. ITGAX.
HPACAB004458.
HPA004723.
MIM151510. gene.
neXtProtNX_P20702.
PharmGKBPA29952.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301393.
HOGENOMHOG000113114.
HOVERGENHBG100530.
InParanoidP20702.
KOK06462.
OrthoDBEOG7353W1.
PhylomeDBP20702.
TreeFamTF105391.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
SignaLinkP20702.

Gene expression databases

ArrayExpressP20702.
BgeeP20702.
CleanExHS_ITGAX.
GenevestigatorP20702.

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

Other

ChiTaRSITGAX. human.
EvolutionaryTraceP20702.
GeneWikiCD11c.
GenomeRNAi3687.
NextBio14429.
PROP20702.
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: April 16, 2014
This is version 149 of the entry and version 3 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 16

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

Human cell differentiation molecules

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