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Q9D8B7 (JAM3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. 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:
Junctional adhesion molecule C

Short name=JAM-C
Alternative name(s):
JAM-2
Junctional adhesion molecule 3
Short name=JAM-3
Gene names
Name:Jam3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in cell-cell adhesion. It is a counterreceptor for ITGAM mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN) By similarity. The soluble form is a mediator of angiogenesis. Ref.6 Ref.8 Ref.10

Subunit structure

Interacts with JAM2 By similarity. Interacts with ITGAM By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein Potential. Cell junctiondesmosome By similarity. Secretedextracellular space By similarity. Note: In epithelial cells, it is expressed at desmosomes but not at tight junctions. Localizes at the cell surface of endothelial cells. Treatment of endothelial cells with vascular endothelial growth factor stimulates recruitement of JAM3 to cell-cell contacts By similarity.

Tissue specificity

Endothelial cells. Ref.6

Post-translational modification

Proteolytically cleaved from endothelial cells surface into a soluble form by ADAM10 and ADAM17; the release of soluble JAM3 is increased by proinflammatory factors By similarity.

Sequence similarities

Belongs to the immunoglobulin superfamily.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Biological processAngiogenesis
Cell adhesion
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
   DomainImmunoglobulin domain
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processadaptive immune response

Inferred from mutant phenotype. Source: MGI

angiogenesis

Inferred from direct assay Ref.8. Source: UniProtKB

cell-matrix adhesion

Inferred from direct assay. Source: MGI

establishment of cell polarity

Inferred from direct assay. Source: MGI

leukocyte migration involved in inflammatory response

Inferred from mutant phenotype. Source: MGI

myelination

Inferred from mutant phenotype. Source: MGI

myeloid progenitor cell differentiation

Inferred from mutant phenotype. Source: MGI

neutrophil homeostasis

Inferred from mutant phenotype. Source: MGI

regulation of actin cytoskeleton organization by cell-cell adhesion

Inferred from mutant phenotype. Source: MGI

regulation of neutrophil chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

spermatid development

Inferred from mutant phenotype. Source: MGI

   Cellular componentdesmosome

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

paranodal junction

Inferred from direct assay. Source: MGI

tight junction

Inferred from direct assay. Source: MGI

   Molecular functionintegrin binding

Inferred from physical interaction. Source: MGI

protein heterodimerization activity

Inferred from physical interaction. Source: MGI

protein homodimerization activity

Inferred from physical interaction. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 310281Junctional adhesion molecule C
PRO_0000015072

Regions

Topological domain30 – 241212Extracellular Potential
Transmembrane242 – 26221Helical; Potential
Topological domain263 – 31048Cytoplasmic Potential
Domain35 – 12793Ig-like V-type
Domain139 – 23698Ig-like C2-type

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1921N-linked (GlcNAc...) Ref.9
Glycosylation1981N-linked (GlcNAc...) Ref.9
Disulfide bond53 ↔ 115 Potential
Disulfide bond160 ↔ 219 Potential

Experimental info

Sequence conflict441H → Q in BAB25519. Ref.3
Sequence conflict1721S → N in BAB25519. Ref.3
Sequence conflict3031R → K in BAB22715. Ref.3
Sequence conflict306 – 3072SS → IA in BAB22715. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9D8B7 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: 4B92BCB51D0A4B0A

FASTA31034,838
        10         20         30         40         50         60 
MALSRRLRLR LYARLPDFFL LLLFRGCMIE AVNLKSSNRN PVVHEFESVE LSCIITDSQT 

        70         80         90        100        110        120 
SDPRIEWKKI QDGQTTYVYF DNKIQGDLAG RTDVFGKTSL RIWNVTRSDS AIYRCEVVAL 

       130        140        150        160        170        180 
NDRKEVDEIT IELIVQVKPV TPVCRIPAAV PVGKTATLQC QESEGYPRPH YSWYRNDVPL 

       190        200        210        220        230        240 
PTDSRANPRF QNSSFHVNSE TGTLVFNAVH KDDSGQYYCI ASNDAGAARC EGQDMEVYDL 

       250        260        270        280        290        300 
NIAGIIGGVL VVLIVLAVIT MGICCAYRRG CFISSKQDGE SYKSPGKHDG VNYIRTSEEG 

       310 
DFRHKSSFVI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of JAM-2 and JAM-3: an emerging junctional adhesion molecular family?"
Aurrand-Lions M.A., Duncan L., Du Pasquier L., Imhof B.A.
Curr. Top. Microbiol. Immunol. 251:91-98(2000) [PubMed: 11036763] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"JAM-2, a novel immunoglobulin superfamily molecule, expressed by endothelial and lymphatic cells."
Aurrand-Lions M.A., Duncan L., Ballestrem C., Imhof B.A.
J. Biol. Chem. 276:2733-2741(2001) [PubMed: 11053409] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo, Small intestine and Wolffian duct.
[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].
Strain: FVB/N.
Tissue: Kidney.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 84-91 AND 146-154, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members."
Aurrand-Lions M.A., Johnson-Leger C., Wong C., Du Pasquier L., Imhof B.A.
Blood 98:3699-3707(2001) [PubMed: 11739175] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[7]"Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response."
Muller W.A.
Trends Immunol. 24:327-334(2003) [PubMed: 12810109] [Abstract]
Cited for: REVIEW, NOMENCLATURE.
[8]"Antibody against junctional adhesion molecule-C inhibits angiogenesis and tumor growth."
Lamagna C., Hodivala-Dilke K.M., Imhof B.A., Aurrand-Lions M.
Cancer Res. 65:5703-5710(2005) [PubMed: 15994945] [Abstract]
Cited for: FUNCTION IN ANGIOGENESIS.
[9]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed: 19656770] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192 AND ASN-198, MASS SPECTROMETRY.
Tissue: Myoblast.
[10]"Junctional adhesion molecule-C is a soluble mediator of angiogenesis."
Rabquer B.J., Amin M.A., Teegala N., Shaheen M.K., Tsou P.S., Ruth J.H., Lesch C.A., Imhof B.A., Koch A.E.
J. Immunol. 185:1777-1785(2010) [PubMed: 20592283] [Abstract]
Cited for: FUNCTION IN ANGIOGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ300304 mRNA. Translation: CAC20704.1.
AK008187 mRNA. Translation: BAB25519.1.
AK003326 mRNA. Translation: BAB22715.1.
AK013156 mRNA. Translation: BAB28683.1.
AK017692 mRNA. Translation: BAC25526.1.
AK032833 mRNA. Translation: BAC28049.1.
BC024357 mRNA. Translation: AAH24357.1.
IPIIPI00453847.
RefSeqNP_075766.1. NM_023277.4.
UniGeneMm.28770.

3D structure databases

ProteinModelPortalQ9D8B7.
SMRQ9D8B7. Positions 29-238.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1344650.
STRINGQ9D8B7.

Proteomic databases

PRIDEQ9D8B7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034472; ENSMUSP00000034472; ENSMUSG00000031990.
GeneID83964.
KEGGmmu:83964.
UCSCuc009oqj.1. mouse.

Organism-specific databases

CTD83700.
MGIMGI:1933825. Jam3.

Phylogenomic databases

eggNOGroNOG09320.
GeneTreeENSGT00600000084033.
HOGENOMHBG446408.
HOVERGENHBG000518.
InParanoidQ9D8B7.
OMAYSWYRND.
OrthoDBEOG4D26QH.
PhylomeDBQ9D8B7.

Gene expression databases

ArrayExpressQ9D8B7.
BgeeQ9D8B7.
CleanExMM_JAM3.
GenevestigatorQ9D8B7.
GermOnlineENSMUSG00000031990. Mus musculus.

Family and domain databases

InterProIPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 2 hits.
KOK06785.
PfamPF07679. I-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio350838.
SOURCESearch...

Entry information

Entry nameJAM3_MOUSE
AccessionPrimary (citable) accession number: Q9D8B7
Secondary accession number(s): Q8BT59, Q9D1M9, Q9EPK4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: January 25, 2012
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families