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P40240 (CD9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
CD9 antigen
Alternative name(s):
CD_antigen=CD9
Gene names
Name:Cd9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length226 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 By similarity. Acts as a receptor for PSG17. Ref.4 Ref.6 Ref.7

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 By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed predominantly in the peripheral nervous system. Ref.7

Post-translational modification

Phosphorylated on tyrosine following B-cell activation By similarity.

Sequence similarities

Belongs to the tetraspanin (TM4SF) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 226225CD9 antigen
PRO_0000219206

Regions

Topological domain2 – 1211Cytoplasmic Potential
Transmembrane13 – 3321Helical; Potential
Topological domain34 – 5320Extracellular Potential
Transmembrane54 – 7421Helical; Potential
Topological domain75 – 8511Cytoplasmic Potential
Transmembrane86 – 10924Helical; Potential
Topological domain110 – 19384Extracellular Potential
Transmembrane194 – 21926Helical; Potential
Topological domain220 – 2267Cytoplasmic Potential

Amino acid modifications

Lipidation91S-palmitoyl cysteine By similarity
Lipidation761S-palmitoyl cysteine By similarity
Lipidation771S-palmitoyl cysteine By similarity
Lipidation851S-palmitoyl cysteine By similarity
Lipidation2161S-palmitoyl cysteine By similarity
Lipidation2171S-palmitoyl cysteine By similarity
Glycosylation501N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis173 – 1753SFQ → AAA: Sperm-egg fusion abolished. Ref.5
Mutagenesis1741F → A: 4-fold reduction of sperm-egg fusion. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P40240 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 06D24A878BF348C5

FASTA22625,258
        10         20         30         40         50         60 
MPVKGGSKCI KYLLFGFNFI FWLAGIAVLA IGLWLRFDSQ TKSIFEQENN HSSFYTGVYI 

        70         80         90        100        110        120 
LIGAGALMML VGFLGCCGAV QESQCMLGLF FGFLLVIFAI EIAAAVWGYT HKDEVIKELQ 

       130        140        150        160        170        180 
EFYKDTYQKL RSKDEPQRET LKAIHMALDC CGIAGPLEQF ISDTCPKKQL LESFQVKPCP 

       190        200        210        220 
EAISEVFNNK FHIIGAVGIG IAVVMIFGMI FSMILCCAIR RSREMV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the mouse equivalent of CD9 antigen."
Rubinstein E., Billard M., Plaisance S., Prenant M., Boucheix C.
Thromb. Res. 71:377-383(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Kidney.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Kidney.
[3]"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].
Strain: C57BL/6.
Tissue: Brain.
[4]"The gamete fusion process is defective in eggs of Cd9-deficient mice."
Kaji K., Oda S., Shikano T., Ohnuki T., Uematsu Y., Sakagami J., Tada N., Miyazaki S., Kudo A.
Nat. Genet. 24:279-282(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN GAMETE FUSION.
[5]"Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion."
Zhu G.-Z., Miller B.J., Boucheix C., Rubinstein E., Liu C.C., Hynes R.O., Myles D.G., Primakoff P.
Development 129:1995-2002(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PHE-174 AND 173-SER--GLN-175.
[6]"Murine CD9 is the receptor for pregnancy-specific glycoprotein 17."
Waterhouse R., Ha C., Dveksler G.S.
J. Exp. Med. 195:277-282(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RECEPTOR FOR PSG17.
[7]"Tetraspanin protein CD9 is a novel paranodal component regulating paranodal junctional formation."
Ishibashi T., Ding L., Ikenaka K., Inoue Y., Miyado K., Mekada E., Baba H.
J. Neurosci. 24:96-102(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN PARANODAL FORMATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08115 mRNA. Translation: AAA37405.1.
AK002251 mRNA. Translation: BAB21965.1.
AK012793 mRNA. Translation: BAB28473.1.
AK151443 mRNA. Translation: BAE30405.1.
AK151619 mRNA. Translation: BAE30556.1.
AK170310 mRNA. Translation: BAE41707.1.
BC070474 mRNA. Translation: AAH70474.1.
PIRI49589.
RefSeqNP_031683.1. NM_007657.3.
UniGeneMm.210676.
Mm.404614.

3D structure databases

ProteinModelPortalP40240.
SMRP40240. Positions 109-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP40240. 1 interaction.
MINTMINT-4090327.
STRING10090.ENSMUSP00000032492.

PTM databases

PhosphoSiteP40240.

Proteomic databases

PaxDbP40240.
PRIDEP40240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032492; ENSMUSP00000032492; ENSMUSG00000030342.
GeneID12527.
KEGGmmu:12527.
UCSCuc009dun.1. mouse.

Organism-specific databases

CTD928.
MGIMGI:88348. Cd9.

Phylogenomic databases

eggNOGNOG242618.
GeneTreeENSGT00680000099842.
HOGENOMHOG000230651.
HOVERGENHBG002324.
InParanoidP40240.
KOK06460.
OMALRFDTQT.
OrthoDBEOG7FBRJV.
PhylomeDBP40240.
TreeFamTF352895.

Gene expression databases

BgeeP40240.
CleanExMM_CD9.
GenevestigatorP40240.

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

NextBio281554.
PROP40240.
SOURCESearch...

Entry information

Entry nameCD9_MOUSE
AccessionPrimary (citable) accession number: P40240
Secondary accession number(s): Q3U9W0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot