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Junctional adhesion molecule C (JAM-C) (Junctional adhesion molecule 3) (JAM-3)

 JAM3_RAT                Reviewed;         310 AA.
Q68FQ2;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
05-DEC-2018, entry version 114.
RecName: Full=Junctional adhesion molecule C;
Short=JAM-C;
AltName: Full=Junctional adhesion molecule 3;
Short=JAM-3;
Contains:
RecName: Full=Soluble form of JAM-C {ECO:0000250|UniProtKB:Q9BX67};
Short=sJAM-C {ECO:0000250|UniProtKB:Q9BX67};
Flags: Precursor;
Name=Jam3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
PROTEIN SEQUENCE OF 84-91; 115-123; 176-185 AND 288-303, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[3]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24090084; DOI=10.1021/pr400783j;
Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
Graham M.E., Packer N.H., Cordwell S.J.;
"Site-specific glycan-peptide analysis for determination of N-
glycoproteome heterogeneity.";
J. Proteome Res. 12:5791-5800(2013).
-!- FUNCTION: Mediates cell-cell adhesion. Functions as counter-
receptor for JAM2. Functions as a counter-receptor for ITGAM,
mediating leukocyte-platelet interactions and is involved in the
regulation of transepithelial migration of polymorphonuclear
neutrophils (PMN). Plays a role in angiogenesis. May play a role
in the regulation of cell migration (By similarity). Required for
normal polarization and acrosome formation in developing
spermatids, and for normal male fertility (By similarity).
{ECO:0000250|UniProtKB:Q9BX67, ECO:0000250|UniProtKB:Q9D8B7}.
-!- FUNCTION: Soluble form of JAM-C: Promotes chemotaxis of vascular
endothelial cells and stimulates angiogenesis.
{ECO:0000250|UniProtKB:Q9BX67}.
-!- SUBUNIT: Interacts with GORASP2 (By similarity). Interacts with
JAM2. Interacts with ITGAM (By similarity).
{ECO:0000250|UniProtKB:Q9BX67, ECO:0000250|UniProtKB:Q9D8B7}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q9D8B7}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q9BX67}. Cell junction
{ECO:0000250|UniProtKB:Q9D8B7}. Cell junction, desmosome
{ECO:0000250|UniProtKB:Q9BX67}. Cell junction, tight junction
{ECO:0000250|UniProtKB:Q9D8B7}. Note=Detected in the acrosome
region in developing spermatids (By similarity). 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 recruitment of JAM3 to cell-cell contacts (By
similarity). {ECO:0000250|UniProtKB:Q9BX67,
ECO:0000250|UniProtKB:Q9D8B7}.
-!- SUBCELLULAR LOCATION: Soluble form of JAM-C: Secreted
{ECO:0000250|UniProtKB:Q9BX67}.
-!- PTM: Proteolytically cleaved from endothelial cells surface into a
soluble form by ADAM10 and ADAM17; the release of soluble JAM3 is
increased by proinflammatory factors.
{ECO:0000250|UniProtKB:Q9BX67}.
-!- PTM: S-palmitoylated by ZDHHC7. S-palmitoylation promotes
expression at tight junctions. {ECO:0000250|UniProtKB:Q9BX67}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC079429; AAH79429.1; -; mRNA.
RefSeq; NP_001004269.1; NM_001004269.1.
UniGene; Rn.104684; -.
ProteinModelPortal; Q68FQ2; -.
SMR; Q68FQ2; -.
BioGrid; 261047; 1.
DIP; DIP-46159N; -.
IntAct; Q68FQ2; 1.
STRING; 10116.ENSRNOP00000012247; -.
SwissPalm; Q68FQ2; -.
UniCarbKB; Q68FQ2; -.
PaxDb; Q68FQ2; -.
PRIDE; Q68FQ2; -.
Ensembl; ENSRNOT00000012247; ENSRNOP00000012247; ENSRNOG00000009149.
GeneID; 315509; -.
KEGG; rno:315509; -.
UCSC; RGD:1303248; rat.
CTD; 83700; -.
RGD; 1303248; Jam3.
eggNOG; ENOG410IGQI; Eukaryota.
eggNOG; ENOG41100KX; LUCA.
GeneTree; ENSGT00940000156937; -.
HOGENOM; HOG000247041; -.
HOVERGEN; HBG000518; -.
InParanoid; Q68FQ2; -.
KO; K06785; -.
OMA; QTNDPRI; -.
OrthoDB; EOG091G0DWZ; -.
PhylomeDB; Q68FQ2; -.
TreeFam; TF331459; -.
Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
Reactome; R-RNO-216083; Integrin cell surface interactions.
PRO; PR:Q68FQ2; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000009149; Expressed in 9 organ(s), highest expression level in heart.
Genevisible; Q68FQ2; RN.
GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl.
GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0033010; C:paranodal junction; IEA:Ensembl.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0002250; P:adaptive immune response; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0031103; P:axon regeneration; IEP:RGD.
GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEA:Ensembl.
GO; GO:0042552; P:myelination; IEA:Ensembl.
GO; GO:0002318; P:myeloid progenitor cell differentiation; IEA:Ensembl.
GO; GO:0001780; P:neutrophil homeostasis; IEA:Ensembl.
GO; GO:0090138; P:regulation of actin cytoskeleton organization by cell-cell adhesion; IEA:Ensembl.
GO; GO:0090022; P:regulation of neutrophil chemotaxis; IEA:Ensembl.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SMART; SM00406; IGv; 2.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
Cell adhesion; Cell junction; Cell membrane; Complete proteome;
Differentiation; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
Reference proteome; Secreted; Signal; Spermatogenesis; Tight junction;
Transmembrane; Transmembrane helix.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 310 Junctional adhesion molecule C.
/FTId=PRO_0000015073.
CHAIN 32 ? Soluble form of JAM-C.
/FTId=PRO_0000445338.
TOPO_DOM 32 241 Extracellular. {ECO:0000255}.
TRANSMEM 242 262 Helical. {ECO:0000255}.
TOPO_DOM 263 310 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 127 Ig-like V-type.
DOMAIN 139 236 Ig-like C2-type.
LIPID 264 264 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q9BX67}.
LIPID 265 265 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q9BX67}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
DISULFID 53 115 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 160 219 {ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 310 AA; 34783 MW; BB0CAD5EE41D383B CRC64;
MALSRRLRLR LCARLPDFFL LLLFRGCVIE AVNLKSSNRN PVVHEFESVE LSCIITDSQT
NDPRIEWKKI QDGQTTYVYF DNKIQGDLAG RTDVFGKTSL RIWNVTRSDS AIYRCEVVAL
NDRKEVDELT IELIVQVKPV APVCRVPKAV PVGKAATLQC QESEGYPRPY YSWYRNDVPL
PTDSRANPRF QNSSFHVNSE TGTLVFSAVH KEDSGQYYCI ASNDAGAARC EGQDMEVYDL
NIAGIIGGVL VVLIVLAVIT MGICCAYRRG CFISSKQDGE SYKSPGKHEG VNYIRTSEEG
DFRHKSSFVI


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