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Protein

CD9 antigen

Gene

CD9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in platelet activation and aggregation. Regulates paranodal junction formation. Involved in cell adhesion, cell motility and tumor metastasis. Required for sperm-egg fusion.3 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCell adhesion, Fertilization

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1300652. Sperm:Oocyte Membrane Binding.
R-HSA-5336415. Uptake and function of diphtheria toxin.

Protein family/group databases

TCDBi8.A.40.1.9. the tetraspanin (tetraspanin) family.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CD9
Synonyms:MIC3, TSPAN29
ORF Names:GIG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000010278.11.
HGNCiHGNC:1709. CD9.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 12CytoplasmicSequence analysisAdd BLAST11
Transmembranei13 – 33HelicalSequence analysisAdd BLAST21
Topological domaini34 – 55ExtracellularSequence analysisAdd BLAST22
Transmembranei56 – 76HelicalSequence analysisAdd BLAST21
Topological domaini77 – 87CytoplasmicSequence analysisAdd BLAST11
Transmembranei88 – 111HelicalSequence analysisAdd BLAST24
Topological domaini112 – 195ExtracellularSequence analysisAdd BLAST84
Transmembranei196 – 221HelicalSequence analysisAdd BLAST26
Topological domaini222 – 228CytoplasmicSequence analysis7

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9C → A: Loss of palmitoylation; when associated with A-78; A-79; A-87; A-218 and A-219. 1 Publication1
Mutagenesisi78C → A: Loss of palmitoylation; when associated with A-9; A-79; A-87; A-218 and A-219. 1 Publication1
Mutagenesisi79C → A: Loss of palmitoylation; when associated with A-9; A-78; A-87; A-218 and A-219. 1 Publication1
Mutagenesisi87C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-218 and A-219. 1 Publication1
Mutagenesisi218C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-219. 1 Publication1
Mutagenesisi219C → A: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-218. 1 Publication1

Organism-specific databases

DisGeNETi928.
OpenTargetsiENSG00000010278.
PharmGKBiPA26247.

Chemistry databases

DrugBankiDB05398. C31G.

Polymorphism and mutation databases

BioMutaiCD9.
DMDMi231724.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002192052 – 228CD9 antigenAdd BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi9S-palmitoyl cysteine1 Publication1
Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi78S-palmitoyl cysteine1 Publication1
Lipidationi79S-palmitoyl cysteine1 Publication1
Lipidationi87S-palmitoyl cysteine1 Publication1
Lipidationi218S-palmitoyl cysteine1 Publication1
Lipidationi219S-palmitoyl cysteine1 Publication1

Post-translational modificationi

Palmitoylated at a low, basal level in unstimulated platelets. The level of palmitoylation increases when platelets are activated by thrombin (in vitro). The protein exists in three forms with molecular masses between 22 and 27 kDa, and is known to carry covalently linked fatty acids.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

EPDiP21926.
MaxQBiP21926.
PaxDbiP21926.
PeptideAtlasiP21926.
PRIDEiP21926.

PTM databases

iPTMnetiP21926.
PhosphoSitePlusiP21926.
SwissPalmiP21926.

Expressioni

Tissue specificityi

Detected in platelets (at protein level). Expressed by a variety of hematopoietic and epithelial cells.1 Publication

Gene expression databases

BgeeiENSG00000010278.
CleanExiHS_CD9.
ExpressionAtlasiP21926. baseline and differential.
GenevisibleiP21926. HS.

Organism-specific databases

HPAiCAB002490.

Interactioni

Subunit structurei

Forms both disulfide-linked homodimers and higher homooligomers as well as heterooligomers with other members of the tetraspanin family. Interacts with CD63. Identified in a complex with CD63 and ITGB3. Associates with CR2/CD21 and with PTGFRN/CD9P1. Interacts directly with IGSF8. Interacts with PDPN; this interaction is homophilic and attenuates platelet aggregation and pulmonary metastasis induced by PDPN (PubMed:18541721).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MMEP084736EBI-4280101,EBI-353759

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107366. 23 interactors.
CORUMiP21926.
DIPiDIP-1122N.
IntActiP21926. 24 interactors.
MINTiMINT-1527350.
STRINGi9606.ENSP00000009180.

Structurei

3D structure databases

ProteinModelPortaliP21926.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tetraspanin (TM4SF) family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3882. Eukaryota.
ENOG4111IRY. LUCA.
GeneTreeiENSGT00880000137858.
HOGENOMiHOG000230651.
HOVERGENiHBG002324.
InParanoidiP21926.
KOiK06460.
OMAiCCAIRKS.
OrthoDBiEOG091G0K9H.
PhylomeDBiP21926.
TreeFamiTF352895.

Family and domain databases

Gene3Di1.10.1450.10. 1 hit.
InterProiView protein in InterPro
IPR000301. Tetraspanin.
IPR018499. Tetraspanin/Peripherin.
IPR018503. Tetraspanin_CS.
IPR008952. Tetraspanin_EC2_sf.
PfamiView protein in Pfam
PF00335. Tetraspannin. 1 hit.
PIRSFiPIRSF002419. Tetraspanin. 1 hit.
PRINTSiPR00259. TMFOUR.
SUPFAMiSSF48652. SSF48652. 1 hit.
PROSITEiView protein in PROSITE
PS00421. TM4_1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21926-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVKGGTKCI KYLLFGFNFI FWLAGIAVLA IGLWLRFDSQ TKSIFEQETN
60 70 80 90 100
NNNSSFYTGV YILIGAGALM MLVGFLGCCG AVQESQCMLG LFFGFLLVIF
110 120 130 140 150
AIEIAAAIWG YSHKDEVIKE VQEFYKDTYN KLKTKDEPQR ETLKAIHYAL
160 170 180 190 200
NCCGLAGGVE QFISDICPKK DVLETFTVKS CPDAIKEVFD NKFHIIGAVG
210 220
IGIAVVMIFG MIFSMILCCA IRRNREMV
Length:228
Mass (Da):25,416
Last modified:January 23, 2007 - v4
Checksum:iF68333E0C20611D8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti215M → T in AAH11988 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38690 mRNA. Translation: AAA80320.1.
L34068 mRNA. Translation: AAA59982.1.
X60111 mRNA. Translation: CAA42708.1.
S60489
, 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.
CCDSiCCDS8540.1.
PIRiA46123. A40402.
RefSeqiNP_001317241.1. NM_001330312.1.
NP_001760.1. NM_001769.3.
UniGeneiHs.114286.
Hs.712104.

Genome annotation databases

EnsembliENST00000009180; ENSP00000009180; ENSG00000010278.
ENST00000382518; ENSP00000371958; ENSG00000010278.
GeneIDi928.
KEGGihsa:928.
UCSCiuc001qnq.3. human.

Similar proteinsi

Entry informationi

Entry nameiCD9_HUMAN
AccessioniPrimary (citable) accession number: P21926
Secondary accession number(s): D3DUQ9, Q5J7W6, Q96ES4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 181 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. SIMILARITY comments
    Index of protein domains and families