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P21926 (CD9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CD9 antigen
Alternative name(s):
5H9 antigen
Cell growth-inhibiting gene 2 protein
Leukocyte antigen MIC3
Motility-related protein
Short name=MRP-1
Tetraspanin-29
Short name=Tspan-29
p24
CD_antigen=CD9
Gene names
Name:CD9
Synonyms:MIC3, TSPAN29
ORF Names:GIG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis. Required for sperm-egg fusion. Ref.11 Ref.12 Ref.13

Subunit structure

Forms both disulfide-linked homodimers and higher homooligomers as well as heterooligomers with other members of the tetraspanin family. Associates with CR2/CD21 and with PTGFRN/CD9P1. Interacts directly with IGSF8. Ref.14 Ref.16 Ref.17

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed by a variety of hematopoietic and epithelial cells.

Post-translational modification

Protein exists in three forms with molecular masses between 22 and 27 kDa, and is known to carry covalently linked fatty acids.

Sequence similarities

Belongs to the tetraspanin (TM4SF) family.

Ontologies

Keywords
   Biological processCell adhesion
Fertilization
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from direct assay Ref.12. Source: UniProtKB

cellular component movement

Inferred from direct assay Ref.11. Source: UniProtKB

fusion of sperm to egg plasma membrane

Inferred from direct assay Ref.13. Source: UniProtKB

multicellular organism reproduction

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

oligodendrocyte development

Inferred from electronic annotation. Source: Ensembl

paranodal junction assembly

Inferred from sequence or structural similarity. Source: UniProtKB

platelet activation

Non-traceable author statement Ref.2. Source: UniProtKB

platelet degranulation

Traceable author statement. Source: Reactome

response to water deprivation

Inferred from electronic annotation. Source: Ensembl

single fertilization

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

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 15326289PubMed 19056867PubMed 19199708. Source: UniProt

integral component of plasma membrane

Non-traceable author statement Ref.2. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule membrane

Traceable author statement. Source: Reactome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MMEP084736EBI-4280101,EBI-353759

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.10
Chain2 – 228227CD9 antigen
PRO_0000219205

Regions

Topological domain2 – 1211Cytoplasmic Potential
Transmembrane13 – 3321Helical; Potential
Topological domain34 – 5522Extracellular Potential
Transmembrane56 – 7621Helical; Potential
Topological domain77 – 8711Cytoplasmic Potential
Transmembrane88 – 11124Helical; Potential
Topological domain112 – 19584Extracellular Potential
Transmembrane196 – 22126Helical; Potential
Topological domain222 – 2287Cytoplasmic Potential

Amino acid modifications

Lipidation91S-palmitoyl cysteine Probable
Lipidation781S-palmitoyl cysteine Probable
Lipidation791S-palmitoyl cysteine Probable
Lipidation871S-palmitoyl cysteine Probable
Lipidation2181S-palmitoyl cysteine Probable
Lipidation2191S-palmitoyl cysteine Probable
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation531N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis91C → A: Loss of palmitoylation; when associated with A-78; A-79; A-87; A-218 and A-219. Ref.15
Mutagenesis781C → A: Loss of palmitoylation; when associated with A-9; A-79; A-87; A-218 and A-219. Ref.15
Mutagenesis791C → A: Loss of palmitoylation; when associated with A-9; A-78; A-87; A-218 and A-219. Ref.15
Mutagenesis871C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-218 and A-219. Ref.15
Mutagenesis2181C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-219. Ref.15
Mutagenesis2191C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-218. Ref.15
Sequence conflict2151M → T in AAH11988. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P21926 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: F68333E0C20611D8

FASTA22825,416
        10         20         30         40         50         60 
MPVKGGTKCI KYLLFGFNFI FWLAGIAVLA IGLWLRFDSQ TKSIFEQETN NNNSSFYTGV 

        70         80         90        100        110        120 
YILIGAGALM MLVGFLGCCG AVQESQCMLG LFFGFLLVIF AIEIAAAIWG YSHKDEVIKE 

       130        140        150        160        170        180 
VQEFYKDTYN KLKTKDEPQR ETLKAIHYAL NCCGLAGGVE QFISDICPKK DVLETFTVKS 

       190        200        210        220 
CPDAIKEVFD NKFHIIGAVG IGIAVVMIFG MIFSMILCCA IRRNREMV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the CD9 antigen. A new family of cell surface proteins."
Boucheix C., Benoit P., Frachet P., Billard M., Worthington R.E., Gagnon J., Uzan G.
J. Biol. Chem. 266:117-122(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-5.
[2]"cDNA cloning and expression of platelet p24/CD9. Evidence for a new family of multiple membrane-spanning proteins."
Lanza F., Wolf D., Fox C.F., Kieffer N., Seyer J.M., Fried V.A., Coughlin S.R., Phillips D.R., Jennings L.K.
J. Biol. Chem. 266:10638-10645(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]"Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility."
Miyake M., Koyama M., Seno M., Ikeyama S.
J. Exp. Med. 174:1347-1354(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Organization of the human CD9 gene."
Rubinstein E., Benoit P., Billard M., Plaisance S., Prenant M., Uzan G., Boucheix C.
Genomics 16:132-138(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leukocyte.
[5]"The tetraspanin CD9 is preferentially expressed on the human CD4(+)CD45RA+ naive T cell population and is involved in T cell activation."
Kobayashi H., Hosono O., Iwata S., Kawasaki H., Kuwana M., Tanaka H., Dang N.H., Morimoto C.
Clin. Exp. Immunol. 137:101-108(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Identification of a human growth inhibition gene 2 (GIG2)."
Kim J.W.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]SeattleSNPs variation discovery resource
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Ovary.
[10]"Purification and partial characterization of CD9 antigen of human platelets."
Higashihara M., Takahata K., Yatomi Y., Nakahara K., Kurokawa K.
FEBS Lett. 264:270-274(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Tissue: Platelet.
[11]"Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA."
Ikeyama S., Koyama M., Yamaoko M., Sasada R., Miyake M.
J. Exp. Med. 177:1231-1237(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN CELL MOTILITY AND METASTASIS.
[12]"CD9-regulated adhesion. Anti-CD9 monoclonal antibody induce pre-B cell adhesion to bone marrow fibroblasts through de novo recognition of fibronectin."
Masellis-Smith A., Shaw A.R.
J. Immunol. 152:2768-2777(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN CELL ADHESION.
[13]"Structural requirements for the inhibitory action of the CD9 large extracellular domain in sperm/oocyte binding and fusion."
Higginbottom A., Takahashi Y., Bolling L., Coonrod S.A., White J.M., Partridge L.J., Monk P.N.
Biochem. Biophys. Res. Commun. 311:208-214(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN SPERM-EGG FUSION.
[14]"Evidence for specific tetraspanin homodimers: inhibition of palmitoylation makes cysteine residues available for cross-linking."
Kovalenko O.V., Yang X., Kolesnikova T.V., Hemler M.E.
Biochem. J. 377:407-417(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[15]"Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation."
Charrin S., Manie S., Oualid M., Billard M., Boucheix C., Rubinstein E.
FEBS Lett. 516:139-144(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-9; CYS-78; CYS-79; CYS-87; CYS-218 AND CYS-219, MUTAGENESIS OF CYS-9; CYS-78; CYS-79; CYS-87; CYS-218 AND CYS-219.
[16]"The major CD9 and CD81 molecular partner. Identification and characterization of the complexes."
Charrin S., Le Naour F., Oualid M., Billard M., Faure G., Hanash S.M., Boucheix C., Rubinstein E.
J. Biol. Chem. 276:14329-14337(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTGFRN.
[17]"EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily."
Stipp C.S., Kolesnikova T.V., Hemler M.E.
J. Biol. Chem. 276:40545-40554(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGSF8.
[18]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M38690 mRNA. Translation: AAA80320.1.
L34068 mRNA. Translation: AAA59982.1.
X60111 mRNA. Translation: CAA42708.1.
S60489 expand/collapse EMBL AC list , S60462, S60463, S60464, S60700, S60699, S60465, S60472 Genomic DNA. Translation: AAC60586.1.
L08118 Genomic DNA. No translation available.
L08119 Genomic DNA. Translation: AAA51954.1. Sequence problems.
L08120 Genomic DNA. Translation: AAA51955.1. Sequence problems.
L08121 Genomic DNA. Translation: AAA51956.1.
L08122 Genomic DNA. Translation: AAA51957.1.
L08123 Genomic DNA. Translation: AAA51958.1.
L08124 Genomic DNA. Translation: AAA51959.1.
L08125 Genomic DNA. No translation available.
AB079244 mRNA. Translation: BAE71132.1.
AY423720 mRNA. Translation: AAS00483.1.
AY422198 Genomic DNA. Translation: AAQ87878.1.
CH471116 Genomic DNA. Translation: EAW88812.1.
CH471116 Genomic DNA. Translation: EAW88813.1.
BC011988 mRNA. Translation: AAH11988.1.
PIRA40402. A46123.
RefSeqNP_001760.1. NM_001769.3.
UniGeneHs.114286.
Hs.712104.

3D structure databases

ProteinModelPortalP21926.
SMRP21926. Positions 111-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107366. 22 interactions.
DIPDIP-1122N.
IntActP21926. 24 interactions.
MINTMINT-1527350.
STRING9606.ENSP00000009180.

Protein family/group databases

TCDB8.A.40.1.9. the tetraspanin (tetraspanin) family.

PTM databases

PhosphoSiteP21926.

Polymorphism databases

DMDM231724.

Proteomic databases

PaxDbP21926.
PRIDEP21926.

Protocols and materials databases

DNASU928.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000009180; ENSP00000009180; ENSG00000010278.
ENST00000382518; ENSP00000371958; ENSG00000010278.
GeneID928.
KEGGhsa:928.
UCSCuc001qnq.2. human.

Organism-specific databases

CTD928.
GeneCardsGC12P006308.
HGNCHGNC:1709. CD9.
HPACAB002490.
MIM143030. gene.
neXtProtNX_P21926.
PharmGKBPA26247.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242618.
HOGENOMHOG000230651.
HOVERGENHBG002324.
InParanoidP21926.
KOK06460.
OMALRFDTQT.
OrthoDBEOG7FBRJV.
PhylomeDBP21926.
TreeFamTF352895.

Enzyme and pathway databases

ReactomeREACT_163848. Reproduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP21926.
BgeeP21926.
CleanExHS_CD9.
GenevestigatorP21926.

Family and domain databases

InterProIPR000301. Tetraspanin.
IPR018499. Tetraspanin/Peripherin.
IPR018503. Tetraspanin_CS.
IPR008952. Tetraspanin_EC2.
[Graphical view]
PfamPF00335. Tetraspannin. 1 hit.
[Graphical view]
PIRSFPIRSF002419. Tetraspanin. 1 hit.
PRINTSPR00259. TMFOUR.
SUPFAMSSF48652. SSF48652. 1 hit.
PROSITEPS00421. TM4_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD9. human.
GeneWikiCD9.
GenomeRNAi928.
NextBio3846.
PROP21926.
SOURCESearch...

Entry information

Entry nameCD9_HUMAN
AccessionPrimary (citable) accession number: P21926
Secondary accession number(s): D3DUQ9, Q5J7W6, Q96ES4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 146 of the entry and version 4 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

MIM cross-references

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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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