JAM1_BOVIN
ID JAM1_BOVIN Reviewed; 298 AA.
AC Q9XT56; Q5E9V8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10395639;
RA Ozaki H., Ishii K., Horiuchi H., Arai H., Kawamoto T., Okawa K.,
RA Iwamatsu A., Kita T.;
RT "Combined treatment of TNF-alpha and IFN-gamma causes redistribution of
RT junctional adhesion molecule in human endothelial cells.";
RL J. Immunol. 163:553-557(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. Involved in platelet
CC activation. {ECO:0000250|UniProtKB:O88792,
CC 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 -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AF111714; AAD42051.1; -; mRNA.
DR EMBL; BT020812; AAX08829.1; -; mRNA.
DR EMBL; BC103325; AAI03326.1; -; mRNA.
DR RefSeq; NP_776520.1; NM_174095.5.
DR AlphaFoldDB; Q9XT56; -.
DR SMR; Q9XT56; -.
DR STRING; 9913.ENSBTAP00000023725; -.
DR PaxDb; Q9XT56; -.
DR PRIDE; Q9XT56; -.
DR Ensembl; ENSBTAT00000023725; ENSBTAP00000023725; ENSBTAG00000017846.
DR GeneID; 281258; -.
DR KEGG; bta:281258; -.
DR CTD; 50848; -.
DR VEuPathDB; HostDB:ENSBTAG00000017846; -.
DR VGNC; VGNC:50010; F11R.
DR eggNOG; ENOG502QWVN; Eukaryota.
DR GeneTree; ENSGT00940000159186; -.
DR HOGENOM; CLU_067351_0_0_1; -.
DR InParanoid; Q9XT56; -.
DR OrthoDB; 1122085at2759; -.
DR TreeFam; TF331459; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000017846; Expressed in mammary gland fat and 103 other tissues.
DR ExpressionAtlas; Q9XT56; baseline and differential.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
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:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IBA:GO_Central.
DR GO; GO:0050892; P:intestinal absorption; IBA:GO_Central.
DR GO; GO:0090559; P:regulation of membrane permeability; IBA:GO_Central.
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; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..298
FT /note="Junctional adhesion molecule A"
FT /id="PRO_0000015065"
FT TOPO_DOM 25..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..124
FT /note="Ig-like V-type 1"
FT DOMAIN 134..227
FT /note="Ig-like V-type 2"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y624"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y624"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 298 AA; 32456 MW; 714FE1C1714769A2 CRC64;
MGTKAKVGST ELLLFTSMIL CSLALGRGAV QTYEPVVRVP ENNPAKLSCS YSGFSSPRVE
WKFTHGDIRG LVCYNNKITA SYENRVTFSD TGITFHSVTR KDTGMYTCMV SDEGGNTYGE
VTVQLIVLVP PSKPTINVPS SVTIGTRAVL TCSERDGSPP SEYKWFKDGV EMPLEPKSNR
AFSNSSYTLN QKTGELIFDP VSASDTGDFT CQAQNGYASP VKSDTVHMDA VELNVGGIVA
AVFVTLILLG ALIFGIWFAY SRGYFDRAKK GTSNKKVIYS QPNARSDGEF RQTSSFLV
