JAM1_RAT
ID JAM1_RAT Reviewed; 300 AA.
AC Q9JHY1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Junctional adhesion molecule A;
DE Short=JAM-A;
DE AltName: Full=Junctional adhesion molecule 1;
DE Short=JAM-1;
DE AltName: CD_antigen=CD321;
DE Flags: Precursor;
GN Name=F11r; Synonyms=Jam1;
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 [MRNA].
RC STRAIN=Sprague-Dawley;
RA Mashima H., Kojima I.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Seems to play a role in epithelial tight junction formation.
CC Appears early in primordial forms of cell junctions and recruits PARD3.
CC The association of the PARD6-PARD3 complex may prevent the interaction
CC of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a
CC role in regulating monocyte transmigration involved in integrity of
CC epithelial barrier. Ligand for integrin alpha-L/beta-2 involved in
CC memory T-cell and neutrophil transmigration.
CC {ECO:0000250|UniProtKB:O88792, ECO:0000250|UniProtKB:Q9Y624}.
CC -!- SUBUNIT: Interacts with the ninth PDZ domain of MPDZ. Interacts with
CC the first PDZ domain of PARD3. The association between PARD3 and PARD6B
CC probably disrupts this interaction. Interacts with ITGAL (via I-
CC domain). {ECO:0000250|UniProtKB:O88792, ECO:0000250|UniProtKB:Q9Y624}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q9Y624}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Y624}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9Y624}. Note=Localized at tight junctions of
CC both epithelial and endothelial cells. {ECO:0000250|UniProtKB:Q9Y624}.
CC -!- DOMAIN: The Ig-like V-type 2 domain is necessary and sufficient for
CC interaction with integrin alpha-L/beta-2.
CC {ECO:0000250|UniProtKB:Q9Y624}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF276998; AAF78250.1; -; mRNA.
DR EMBL; BC065309; AAH65309.1; -; mRNA.
DR RefSeq; NP_446248.1; NM_053796.1.
DR AlphaFoldDB; Q9JHY1; -.
DR SMR; Q9JHY1; -.
DR CORUM; Q9JHY1; -.
DR IntAct; Q9JHY1; 1.
DR MINT; Q9JHY1; -.
DR STRING; 10116.ENSRNOP00000006141; -.
DR GlyGen; Q9JHY1; 1 site.
DR iPTMnet; Q9JHY1; -.
DR PhosphoSitePlus; Q9JHY1; -.
DR PaxDb; Q9JHY1; -.
DR PRIDE; Q9JHY1; -.
DR GeneID; 116479; -.
DR KEGG; rno:116479; -.
DR UCSC; RGD:621842; rat.
DR CTD; 50848; -.
DR RGD; 621842; F11r.
DR VEuPathDB; HostDB:ENSRNOG00000004414; -.
DR eggNOG; ENOG502QWVN; Eukaryota.
DR HOGENOM; CLU_067351_0_0_1; -.
DR InParanoid; Q9JHY1; -.
DR OMA; YSRGYFE; -.
DR OrthoDB; 1122085at2759; -.
DR PhylomeDB; Q9JHY1; -.
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 Reactome; R-RNO-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-RNO-420029; Tight junction interactions.
DR PRO; PR:Q9JHY1; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000004414; Expressed in lung and 19 other tissues.
DR Genevisible; Q9JHY1; RN.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0036057; C:slit diaphragm; IDA:RGD.
DR GO; GO:0070160; C:tight junction; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEP:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:RGD.
DR GO; GO:0050892; P:intestinal absorption; ISO:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0035683; P:memory T cell extravasation; ISO:RGD.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:RGD.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; IDA:RGD.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; ISO:RGD.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISO:RGD.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0001817; P:regulation of cytokine production; ISO:RGD.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:RGD.
DR GO; GO:0090559; P:regulation of membrane permeability; ISO:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR042456; F11R.
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 PANTHER; PTHR45113; PTHR45113; 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 junction; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..300
FT /note="Junctional adhesion molecule A"
FT /id="PRO_0000015068"
FT TOPO_DOM 27..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..122
FT /note="Ig-like V-type 1"
FT DOMAIN 134..228
FT /note="Ig-like V-type 2"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y624"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y624"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 300 AA; 32370 MW; 45AE362A96158BFA CRC64;
MGTEGKAGSK LLFLFTSMIL GSLVQGKGSV YSPQTAVQVP ENDSVKLPCI YSGFSSPRVE
WKFVQGSTTA LVCYNNQITV PYADRVTFSS SGITFSSVTR KDNGEYTCMV SEDGGQNYGE
VSIHLTVLVP PSKPTVSIPS SVTIGNRAVL TCSEHDGSPP SEYSWFKDGV PMLTADAKKT
RAFINSSYTI DPKSGDLVFD PVSAFDSGEY YCEAQNGYGT AMRSEAVRME AVELNVGGIV
AAVLVTLILL GLLIFGIWFA YSRGYFERTK KGTAPGKKVI YSQPSARSEG EFKQTSSFLV
