JAML_MOUSE
ID JAML_MOUSE Reviewed; 379 AA.
AC Q80UL9; E9QNV7; Q5DTC4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Junctional adhesion molecule-like {ECO:0000250|UniProtKB:Q86YT9};
DE AltName: Full=Dendritic cell-specific protein CREA7;
DE Short=mCrea7;
DE Flags: Precursor;
GN Name=Jaml {ECO:0000250|UniProtKB:Q86YT9}; Synonyms=Amica1, Gm638;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Ahn J.H., Jung H.R., Lee B.-H., Jeon C.J., Bae Y.-S.;
RT "mCrea7, mouse ortholog of human dendritic cell specific protein Crea7.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=B5/EGFP; TISSUE=Trophoblast;
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 [4]
RP FUNCTION IN GAMMA-DELTA T-CELL ACTIVATION, INTERACTION WITH CXADR,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20813954; DOI=10.1126/science.1192698;
RA Witherden D.A., Verdino P., Rieder S.E., Garijo O., Mills R.E., Teyton L.,
RA Fischer W.H., Wilson I.A., Havran W.L.;
RT "The junctional adhesion molecule JAML is a costimulatory receptor for
RT epithelial gammadelta T cell activation.";
RL Science 329:1205-1210(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 21-280 ALONE AND IN COMPLEX WITH
RP CXADR, DOMAIN, HOMODIMERIZATION, INTERACTION WITH PI3 KINASE, GLYCOSYLATION
RP AT ASN-79; ASN-89 AND ASN-125, DISULFIDE BONDS, AND MUTAGENESIS OF ASP-59;
RP TYR-72; PHE-75; TYR-77; ARG-122; TYR-334; TYR-355 AND 360-PRO--PRO-366.
RX PubMed=20813955; DOI=10.1126/science.1187996;
RA Verdino P., Witherden D.A., Havran W.L., Wilson I.A.;
RT "The molecular interaction of CAR and JAML recruits the central cell signal
RT transducer PI3K.";
RL Science 329:1210-1214(2010).
CC -!- FUNCTION: Transmembrane protein of the plasma membrane of leukocytes
CC that control their migration and activation through interaction with
CC CXADR, a plasma membrane receptor found on adjacent epithelial and
CC endothelial cells. The interaction between both receptors mediates the
CC activation of gamma-delta T-cells, a subpopulation of T-cells residing
CC in epithelia and involved in tissue homeostasis and repair. Upon
CC epithelial CXADR-binding, JAML induces downstream cell signaling events
CC in gamma-delta T-cells through PI3-kinase and MAP kinases. It results
CC in proliferation and production of cytokines and growth factors by T-
CC cells that in turn stimulate epithelial tissues repair. It also
CC controls the transmigration of leukocytes within epithelial and
CC endothelial tissues through adhesive interactions with epithelial and
CC endothelial CXADR. {ECO:0000269|PubMed:20813954}.
CC -!- SUBUNIT: Homodimer; active form in leukocyte-endothelial cell adhesion.
CC Interacts (homodimeric form) with CXADR. Interacts (via cytoplasmic
CC domain) with the PI3 kinase; upon CXADR-binding. Interacts with ITGA4
CC and ITGB1; integrin alpha-4/beta-1 may regulate leukocyte to
CC endothelial cells adhesion by controlling JAML homodimerization.
CC {ECO:0000269|PubMed:20813954, ECO:0000269|PubMed:20813955}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20813954};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:20813954}. Cell
CC junction {ECO:0000250|UniProtKB:Q86YT9}. Note=Localized at the plasma
CC membrane and enriched in areas of cell-cell contacts.
CC {ECO:0000250|UniProtKB:Q86YT9}.
CC -!- TISSUE SPECIFICITY: Expressed by gamma-delta intraepithelial T cells
CC (at protein level). {ECO:0000269|PubMed:20813954}.
CC -!- DOMAIN: The Ig-like V-type domain 1 mediates interaction with CXADR
CC (PubMed:20813954). The Ig-like V-type domain 2 may also play a role in
CC the interaction (PubMed:20813955). {ECO:0000269|PubMed:20813954,
CC ECO:0000269|PubMed:20813955}.
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; AY093688; AAM15732.1; -; mRNA.
DR EMBL; AC122305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050133; AAH50133.1; -; mRNA.
DR CCDS; CCDS23128.1; -.
DR RefSeq; NP_001005421.3; NM_001005421.4.
DR RefSeq; XP_006510446.1; XM_006510383.3.
DR PDB; 3MJ6; X-ray; 2.19 A; A=21-280.
DR PDB; 3MJ7; X-ray; 2.80 A; A=21-280.
DR PDB; 3MJ9; X-ray; 2.95 A; A=21-280.
DR PDBsum; 3MJ6; -.
DR PDBsum; 3MJ7; -.
DR PDBsum; 3MJ9; -.
DR AlphaFoldDB; Q80UL9; -.
DR SMR; Q80UL9; -.
DR BioGRID; 234770; 1.
DR DIP; DIP-59107N; -.
DR IntAct; Q80UL9; 2.
DR MINT; Q80UL9; -.
DR STRING; 10090.ENSMUSP00000052033; -.
DR GlyGen; Q80UL9; 3 sites.
DR iPTMnet; Q80UL9; -.
DR PhosphoSitePlus; Q80UL9; -.
DR EPD; Q80UL9; -.
DR PaxDb; Q80UL9; -.
DR PRIDE; Q80UL9; -.
DR ProteomicsDB; 269419; -.
DR ABCD; Q80UL9; 1 sequenced antibody.
DR DNASU; 270152; -.
DR Ensembl; ENSMUST00000050020; ENSMUSP00000052033; ENSMUSG00000048534.
DR Ensembl; ENSMUST00000215880; ENSMUSP00000150697; ENSMUSG00000048534.
DR GeneID; 270152; -.
DR KEGG; mmu:270152; -.
DR UCSC; uc009pfd.2; mouse.
DR CTD; 120425; -.
DR MGI; MGI:2685484; Jaml.
DR VEuPathDB; HostDB:ENSMUSG00000048534; -.
DR eggNOG; ENOG502SVGE; Eukaryota.
DR GeneTree; ENSGT00440000034341; -.
DR HOGENOM; CLU_059564_0_0_1; -.
DR InParanoid; Q80UL9; -.
DR OMA; PVWPSLK; -.
DR OrthoDB; 1154501at2759; -.
DR PhylomeDB; Q80UL9; -.
DR TreeFam; TF331728; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 270152; 1 hit in 72 CRISPR screens.
DR EvolutionaryTrace; Q80UL9; -.
DR PRO; PR:Q80UL9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80UL9; protein.
DR Bgee; ENSMUSG00000048534; Expressed in granulocyte and 42 other tissues.
DR ExpressionAtlas; Q80UL9; baseline and differential.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0046629; P:gamma-delta T cell activation; IDA:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0035696; P:monocyte extravasation; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0072672; P:neutrophil extravasation; ISO:MGI.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IDA:UniProtKB.
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; IPR029871; JAML.
DR InterPro; IPR000920; Myelin_P0-rel.
DR PANTHER; PTHR13869; PTHR13869; 1.
DR PANTHER; PTHR13869:SF22; PTHR13869:SF22; 1.
DR Pfam; PF07686; V-set; 2.
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 3D-structure; Cell adhesion; Cell junction; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..379
FT /note="Junctional adhesion molecule-like"
FT /id="PRO_0000015075"
FT TOPO_DOM 21..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..135
FT /note="Ig-like V-type 1"
FT DOMAIN 140..250
FT /note="Ig-like V-type 2"
FT MOD_RES 355
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20813955"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20813955"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20813955"
FT DISULFID 45..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20813955"
FT DISULFID 158..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20813955"
FT MUTAGEN 59
FT /note="D->A,K,N: Loss of interaction with CXADR."
FT /evidence="ECO:0000269|PubMed:20813955"
FT MUTAGEN 72
FT /note="Y->A: Loss of interaction with CXADR."
FT /evidence="ECO:0000269|PubMed:20813955"
FT MUTAGEN 75
FT /note="F->A,W: Loss of interaction with CXADR."
FT /evidence="ECO:0000269|PubMed:20813955"
FT MUTAGEN 77
FT /note="Y->A,F: Loss of interaction with CXADR."
FT /evidence="ECO:0000269|PubMed:20813955"
FT MUTAGEN 122
FT /note="R->A: Loss of interaction with CXADR."
FT /evidence="ECO:0000269|PubMed:20813955"
FT MUTAGEN 334
FT /note="Y->F: No effect on interaction with PI3 kinase."
FT /evidence="ECO:0000269|PubMed:20813955"
FT MUTAGEN 355
FT /note="Y->F: Loss of interaction with PI3 kinase."
FT /evidence="ECO:0000269|PubMed:20813955"
FT MUTAGEN 360..366
FT /note="PVWPSSP->AVWASSA: Loss of interaction with PI3
FT kinase."
FT /evidence="ECO:0000269|PubMed:20813955"
FT CONFLICT 231
FT /note="Q -> R (in Ref. 3; AAH50133)"
FT /evidence="ECO:0000305"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 55..66
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3MJ6"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3MJ6"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3MJ6"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3MJ6"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3MJ6"
FT TURN 203..207
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3MJ6"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3MJ6"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:3MJ6"
FT STRAND 243..254
FT /evidence="ECO:0007829|PDB:3MJ6"
SQ SEQUENCE 379 AA; 42533 MW; EFC0F1A84EEC8A12 CRC64;
MLCLLKLIVI PVILAPVGYP QGLPGLTVSS PQLRVHVGES VLMGCVVQRT EEKHVDRVDW
LFSKDKDDAS EYVLFYYSNL SVPTGRFQNR SHLVGDTFHN DGSLLLQDVQ KADEGIYTCE
IRLKNESMVM KKPVELWVLP EEPKDLRVRV GDTTQMRCSI QSTEEKRVTK VNWMFSSGSH
TEEETVLSYD SNMRSGKFQS LGRFRNRVDL TGDISRNDGS IKLQTVKESD QGIYTCSIYV
GKLESRKTIV LHVVQDEFQR TISPTPPTDK GQQGILNGNQ LVIIVGIVCA TFLLLPVLIL
IVKKAKWNKS SVSSMASVKS LENKEKINPE KHIYSSITTW ETTERGISGE SEGTYMTMNP
VWPSSPKASS LVRSSVRSK
