JAM3_RAT
ID JAM3_RAT Reviewed; 310 AA.
AC Q68FQ2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Junctional adhesion molecule C;
DE Short=JAM-C;
DE AltName: Full=Junctional adhesion molecule 3;
DE Short=JAM-3;
DE Contains:
DE RecName: Full=Soluble form of JAM-C {ECO:0000250|UniProtKB:Q9BX67};
DE Short=sJAM-C {ECO:0000250|UniProtKB:Q9BX67};
DE Flags: Precursor;
GN Name=Jam3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 84-91; 115-123; 176-185 AND 288-303, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Junctional adhesion protein that mediates heterotypic cell-
CC cell interactions with its cognate receptor JAM2 to regulate different
CC cellular processes. Plays a role in homing and mobilization of
CC hematopoietic stem and progenitor cells within the bone marrow. At the
CC surface of bone marrow stromal cells, it contributes to the retention
CC of the hematopoietic stem and progenitor cells expressing JAM3 (By
CC similarity). Plays a central role in leukocytes extravasation by
CC facilitating transmigration through the endothelium (By similarity).
CC Plays a role in spermatogenesis where JAM2 and JAM3, which are
CC respectively expressed by Sertoli and germ cells, mediate an
CC interaction between both cell types and play an essential role in the
CC anchorage of germ cells onto Sertoli cells and the assembly of cell
CC polarity complexes during spermatid differentiation (By similarity).
CC Also functions as a counter-receptor for ITGAM, mediating leukocyte-
CC platelet interactions and is involved in the regulation of
CC transepithelial migration of polymorphonuclear neutrophils (PMN). Plays
CC a role in angiogenesis. Plays a role in the regulation of cell
CC migration (By similarity). During myogenesis, it is involved in myocyte
CC fusion (By similarity). {ECO:0000250|UniProtKB:A3KPA0,
CC ECO:0000250|UniProtKB:Q9BX67, ECO:0000250|UniProtKB:Q9D8B7}.
CC -!- FUNCTION: [Soluble form of JAM-C]: Promotes chemotaxis of vascular
CC endothelial cells and stimulates angiogenesis.
CC {ECO:0000250|UniProtKB:Q9BX67}.
CC -!- SUBUNIT: Interacts with ITGAM (By similarity). Interacts with GORASP2
CC (By similarity). {ECO:0000250|UniProtKB:Q9BX67,
CC ECO:0000250|UniProtKB:Q9D8B7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BX67};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BX67}.
CC Cell junction {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, desmosome
CC {ECO:0000250|UniProtKB:Q9BX67}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q9BX67}. Note=Detected in the acrosome region in
CC developing spermatids (By similarity). In epithelial cells, it is
CC expressed at desmosomes but not at tight junctions (By similarity).
CC Localizes at the cell surface of endothelial cells; treatment of
CC endothelial cells with vascular endothelial growth factor stimulates
CC recruitment of JAM3 to cell-cell contacts (By similarity).
CC {ECO:0000250|UniProtKB:Q9BX67, ECO:0000250|UniProtKB:Q9D8B7}.
CC -!- SUBCELLULAR LOCATION: [Soluble form of JAM-C]: Secreted
CC {ECO:0000250|UniProtKB:Q9BX67}.
CC -!- DOMAIN: The Ig-like V-type domain mediates interaction with JAM2.
CC {ECO:0000250|UniProtKB:Q9D8B7}.
CC -!- PTM: Proteolytically cleaved from endothelial cells surface into a
CC soluble form by ADAM10 and ADAM17; the release of soluble JAM3 is
CC increased by pro-inflammatory factors. {ECO:0000250|UniProtKB:Q9BX67}.
CC -!- PTM: S-palmitoylated by ZDHHC7. S-palmitoylation promotes expression at
CC tight junctions. {ECO:0000250|UniProtKB:Q9BX67}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; BC079429; AAH79429.1; -; mRNA.
DR RefSeq; NP_001004269.1; NM_001004269.1.
DR AlphaFoldDB; Q68FQ2; -.
DR SMR; Q68FQ2; -.
DR BioGRID; 261047; 1.
DR DIP; DIP-46159N; -.
DR IntAct; Q68FQ2; 1.
DR STRING; 10116.ENSRNOP00000012247; -.
DR GlyGen; Q68FQ2; 2 sites, 5 N-linked glycans (1 site).
DR iPTMnet; Q68FQ2; -.
DR SwissPalm; Q68FQ2; -.
DR PaxDb; Q68FQ2; -.
DR PRIDE; Q68FQ2; -.
DR Ensembl; ENSRNOT00000012247; ENSRNOP00000012247; ENSRNOG00000009149.
DR GeneID; 315509; -.
DR KEGG; rno:315509; -.
DR UCSC; RGD:1303248; rat.
DR CTD; 83700; -.
DR RGD; 1303248; Jam3.
DR eggNOG; ENOG502QTVP; Eukaryota.
DR GeneTree; ENSGT00940000156937; -.
DR HOGENOM; CLU_067351_2_0_1; -.
DR InParanoid; Q68FQ2; -.
DR OMA; PRPYYSW; -.
DR OrthoDB; 906664at2759; -.
DR PhylomeDB; Q68FQ2; -.
DR TreeFam; TF331459; -.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR PRO; PR:Q68FQ2; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000009149; Expressed in heart and 19 other tissues.
DR Genevisible; Q68FQ2; RN.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0030057; C:desmosome; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0031941; C:filamentous actin; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0033010; C:paranodal junction; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; ISS:UniProtKB.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:RGD.
DR GO; GO:0070160; C:tight junction; ISO:RGD.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; ISO:RGD.
DR GO; GO:0034333; P:adherens junction assembly; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0045176; P:apical protein localization; ISO:RGD.
DR GO; GO:0031103; P:axon regeneration; IEP:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:RGD.
DR GO; GO:0097530; P:granulocyte migration; ISO:RGD.
DR GO; GO:0097241; P:hematopoietic stem cell migration to bone marrow; ISO:RGD.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; ISO:RGD.
DR GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0033624; P:negative regulation of integrin activation; ISO:RGD.
DR GO; GO:0001780; P:neutrophil homeostasis; ISO:RGD.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:RGD.
DR GO; GO:1905710; P:positive regulation of membrane permeability; ISO:RGD.
DR GO; GO:1902414; P:protein localization to cell junction; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:RGD.
DR GO; GO:0090138; P:regulation of actin cytoskeleton organization by cell-cell adhesion; ISO:RGD.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR042974; JAM-C.
DR PANTHER; PTHR44598; PTHR44598; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Differentiation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Secreted; Signal; Spermatogenesis; Tight junction;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..310
FT /note="Junctional adhesion molecule C"
FT /id="PRO_0000015073"
FT CHAIN 32..?
FT /note="Soluble form of JAM-C"
FT /id="PRO_0000445338"
FT TOPO_DOM 32..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..127
FT /note="Ig-like V-type"
FT DOMAIN 139..236
FT /note="Ig-like C2-type"
FT LIPID 264
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX67"
FT LIPID 265
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX67"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT DISULFID 53..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 160..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ 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
