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Junctional adhesion molecule-like (Adhesion molecule interacting with CXADR antigen 1) (Dendritic cell-specific protein CREA7-1)

 JAML_HUMAN              Reviewed;         394 AA.
Q86YT9; B0YIV1; B0YIV2; Q496M1; Q5DTC6; Q7Z499; Q8N9I7; Q8NF70;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
12-SEP-2018, entry version 133.
RecName: Full=Junctional adhesion molecule-like {ECO:0000312|HGNC:HGNC:19084};
AltName: Full=Adhesion molecule interacting with CXADR antigen 1;
AltName: Full=Dendritic cell-specific protein CREA7-1;
Flags: Precursor;
Name=JAML {ECO:0000312|HGNC:HGNC:19084}; Synonyms=AMICA1;
ORFNames=UNQ722/PRO1387;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN LEUKOCYTE
MIGRATION, INDUCTION, SUBCELLULAR LOCATION, DOMAIN, TISSUE
SPECIFICITY, MUTAGENESIS OF LYS-54, AND VARIANT ALA-193.
TISSUE=Bone marrow;
PubMed=12869515; DOI=10.1182/blood-2002-11-3462;
Moog-Lutz C., Cave-Riant F., Guibal F.C., Breau M.A., Di Gioia Y.,
Couraud P.O., Cayre Y.E., Bourdoulous S., Lutz P.G.;
"JAML, a novel protein with characteristics of a junctional adhesion
molecule, is induced during differentiation of myeloid leukemia
cells.";
Blood 102:3371-3378(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ASN-94 AND
ALA-193.
TISSUE=Dendritic cell;
Ahn J.H., Jung H.R., Lee B.-H., Jeon C.J., Bae Y.-S.;
"Dendritic cell specific protein Crea7-1.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
VARIANTS ASN-94 AND ALA-193.
TISSUE=Cerebellum, and Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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).
[8]
PROTEIN SEQUENCE OF 20-34.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[9]
FUNCTION IN LEUKOCYTE MIGRATION, INTERACTION WITH CXADR, SUBCELLULAR
LOCATION, AND DOMAIN.
PubMed=15800062; DOI=10.1091/mbc.E05-01-0036;
Zen K., Liu Y., McCall I.C., Wu T., Lee W., Babbin B.A., Nusrat A.,
Parkos C.A.;
"Neutrophil migration across tight junctions is mediated by adhesive
interactions between epithelial CAR and a JAM-like protein on
neutrophils.";
Mol. Biol. Cell 16:2694-2703(2005).
[10]
FUNCTION IN LEUKOCYTE MIGRATION, HOMODIMERIZATION, MUTAGENESIS OF
LYS-54, INTERACTION WITH CXADR, AND TISSUE SPECIFICITY.
PubMed=19064666; DOI=10.1083/jcb.200805061;
Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O.,
Bourdoulous S.;
"JAM-L-mediated leukocyte adhesion to endothelial cells is regulated
in cis by alpha4beta1 integrin activation.";
J. Cell Biol. 183:1159-1173(2008).
[11]
FUNCTION IN LEUKOCYTE MIGRATION, AND TISSUE SPECIFICITY.
PubMed=18948633; DOI=10.1161/ATVBAHA.108.177717;
Guo Y.L., Bai R., Chen C.X., Liu D.Q., Liu Y., Zhang C.Y., Zen K.;
"Role of junctional adhesion molecule-like protein in mediating
monocyte transendothelial migration.";
Arterioscler. Thromb. Vasc. Biol. 29:75-83(2009).
-!- FUNCTION: Transmembrane protein of the plasma membrane of
leukocytes that control their migration and activation through
interaction with CXADR, a plasma membrane receptor found on
adjacent epithelial and endothelial cells. The interaction between
both receptors mediates the activation of gamma-delta T-cells, a
subpopulation of T-cells residing in epithelia and involved in
tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML
induces downstream cell signaling events in gamma-delta T-cells
through PI3-kinase and MAP kinases. It results in proliferation
and production of cytokines and growth factors by T-cells that in
turn stimulate epithelial tissues repair. It also controls the
transmigration of leukocytes within epithelial and endothelial
tissues through adhesive interactions with epithelial and
endothelial CXADR. {ECO:0000269|PubMed:12869515,
ECO:0000269|PubMed:15800062, ECO:0000269|PubMed:18948633,
ECO:0000269|PubMed:19064666}.
-!- SUBUNIT: Homodimer; active form in leukocyte-endothelial cell
adhesion. Interacts (homodimeric form) with CXADR. Interacts (via
cytoplasmic domain) with the PI3 kinase; upon CXADR-binding.
Interacts with ITGA4 and ITGB1; integrin alpha-4/beta-1 may
regulate leukocyte to endothelial cells adhesion by controlling
JAML homodimerization. {ECO:0000269|PubMed:15800062,
ECO:0000269|PubMed:19064666}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12869515};
Single-pass type I membrane protein {ECO:0000269|PubMed:12869515}.
Cell junction {ECO:0000269|PubMed:12869515}. Note=Localized at the
plasma membrane and enriched in areas of cell-cell contacts
(PubMed:12869515).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q86YT9-1; Sequence=Displayed;
Name=2;
IsoId=Q86YT9-2; Sequence=VSP_014830;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q86YT9-3; Sequence=VSP_014831, VSP_014832;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q86YT9-4; Sequence=VSP_054911;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expression is restricted to the hematopoietic
tissues with the exception of liver. Expressed in fetal liver,
spleen and thymus. Preferentially expressed by mature leukocytes
(at protein level). {ECO:0000269|PubMed:12869515,
ECO:0000269|PubMed:18948633, ECO:0000269|PubMed:19064666}.
-!- INDUCTION: Up-regulated upon retinoic acid, Me2SO and PMA
treatment in differentiating myeloid leukemia cells.
{ECO:0000269|PubMed:12869515}.
-!- DOMAIN: The Ig-like V-type domain 1 mediates interaction with
CXADR (By similarity). The Ig-like V-type domain 2 may also play a
role in the interaction (PubMed:15800062). {ECO:0000250,
ECO:0000269|PubMed:12869515, ECO:0000269|PubMed:15800062}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC03390.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ515553; CAD56620.2; -; mRNA.
EMBL; AY093686; AAM15730.1; -; mRNA.
EMBL; AY138965; AAN52117.1; -; mRNA.
EMBL; AY358362; AAQ88728.1; -; mRNA.
EMBL; AK090409; BAC03390.1; ALT_INIT; mRNA.
EMBL; AK094399; BAC04347.1; -; mRNA.
EMBL; EF444945; ACA05929.1; -; Genomic_DNA.
EMBL; EF444945; ACA05930.1; -; Genomic_DNA.
EMBL; AP002800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC100797; AAI00798.1; -; mRNA.
CCDS; CCDS41723.1; -. [Q86YT9-1]
CCDS; CCDS66240.1; -. [Q86YT9-4]
CCDS; CCDS8391.1; -. [Q86YT9-2]
RefSeq; NP_001091996.1; NM_001098526.1. [Q86YT9-1]
RefSeq; NP_001273499.1; NM_001286570.1. [Q86YT9-4]
RefSeq; NP_001273500.1; NM_001286571.1. [Q86YT9-4]
RefSeq; NP_694938.2; NM_153206.2. [Q86YT9-2]
UniGene; Hs.16291; -.
ProteinModelPortal; Q86YT9; -.
SMR; Q86YT9; -.
BioGrid; 125686; 1.
IntAct; Q86YT9; 5.
STRING; 9606.ENSP00000348635; -.
iPTMnet; Q86YT9; -.
PhosphoSitePlus; Q86YT9; -.
SwissPalm; Q86YT9; -.
BioMuta; AMICA1; -.
DMDM; 71151910; -.
PaxDb; Q86YT9; -.
PeptideAtlas; Q86YT9; -.
PRIDE; Q86YT9; -.
ProteomicsDB; 70469; -.
ProteomicsDB; 70470; -. [Q86YT9-2]
ProteomicsDB; 70471; -. [Q86YT9-3]
Ensembl; ENST00000292067; ENSP00000292067; ENSG00000160593. [Q86YT9-2]
Ensembl; ENST00000356289; ENSP00000348635; ENSG00000160593. [Q86YT9-1]
Ensembl; ENST00000526620; ENSP00000431218; ENSG00000160593. [Q86YT9-4]
GeneID; 120425; -.
KEGG; hsa:120425; -.
UCSC; uc001psi.3; human. [Q86YT9-1]
CTD; 120425; -.
DisGeNET; 120425; -.
EuPathDB; HostDB:ENSG00000160593.17; -.
GeneCards; JAML; -.
HGNC; HGNC:19084; JAML.
HPA; HPA047919; -.
MIM; 609770; gene.
neXtProt; NX_Q86YT9; -.
OpenTargets; ENSG00000160593; -.
PharmGKB; PA38792; -.
eggNOG; ENOG410IKEA; Eukaryota.
eggNOG; ENOG4111DWB; LUCA.
GeneTree; ENSGT00440000034341; -.
HOGENOM; HOG000294145; -.
HOVERGEN; HBG055209; -.
InParanoid; Q86YT9; -.
OMA; YMTMHPV; -.
OrthoDB; EOG091G0KVU; -.
PhylomeDB; Q86YT9; -.
TreeFam; TF331728; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
ChiTaRS; JAML; human.
GeneWiki; AMICA1; -.
GenomeRNAi; 120425; -.
PRO; PR:Q86YT9; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000160593; Expressed in 170 organ(s), highest expression level in blood.
CleanEx; HS_AMICA1; -.
ExpressionAtlas; Q86YT9; baseline and differential.
Genevisible; Q86YT9; HS.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:UniProtKB.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0046629; P:gamma-delta T cell activation; ISS:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0035696; P:monocyte extravasation; IMP:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; IMP:UniProtKB.
GO; GO:0072672; P:neutrophil extravasation; IMP:UniProtKB.
GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; ISS:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
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; IPR013106; Ig_V-set.
InterPro; IPR029871; JAML.
InterPro; IPR000920; Myelin_P0-rel.
PANTHER; PTHR13869; PTHR13869; 1.
PANTHER; PTHR13869:SF22; PTHR13869:SF22; 1.
Pfam; PF07686; V-set; 2.
SMART; SM00409; IG; 2.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000269|PubMed:15340161}.
CHAIN 20 394 Junctional adhesion molecule-like.
/FTId=PRO_0000015074.
TOPO_DOM 20 275 Extracellular. {ECO:0000255}.
TRANSMEM 276 296 Helical. {ECO:0000255}.
TOPO_DOM 297 394 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 132 Ig-like V-type 1.
DOMAIN 137 250 Ig-like V-type 2.
CARBOHYD 76 76 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 116 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 155 234 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 39 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054911.
VAR_SEQ 1 14 MFCPLKLILLPVLL -> MVSG (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_014830.
VAR_SEQ 258 259 TL -> SI (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_014831.
VAR_SEQ 260 394 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_014832.
VARIANT 94 94 I -> N (in dbSNP:rs17121881).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.2}.
/FTId=VAR_049974.
VARIANT 193 193 V -> A (in dbSNP:rs1793174).
{ECO:0000269|PubMed:12869515,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.2}.
/FTId=VAR_049975.
VARIANT 322 322 I -> M (in dbSNP:rs2298831).
/FTId=VAR_049976.
MUTAGEN 54 54 K->E: Loss of the ability to
homodimerize, loss of interaction with
CXADR and loss of function in cell-cell
adhesion. {ECO:0000269|PubMed:12869515,
ECO:0000269|PubMed:19064666}.
CONFLICT 283 283 C -> G (in Ref. 2; AAM15730).
{ECO:0000305}.
SEQUENCE 394 AA; 44339 MW; 64B542F9384C7642 CRC64;
MFCPLKLILL PVLLDYSLGL NDLNVSPPEL TVHVGDSALM GCVFQSTEDK CIFKIDWTLS
PGEHAKDEYV LYYYSNLSVP IGRFQNRVHL MGDILCNDGS LLLQDVQEAD QGTYICEIRL
KGESQVFKKA VVLHVLPEEP KELMVHVGGL IQMGCVFQST EVKHVTKVEW IFSGRRAKEE
IVFRYYHKLR MSVEYSQSWG HFQNRVNLVG DIFRNDGSIM LQGVRESDGG NYTCSIHLGN
LVFKKTIVLH VSPEEPRTLV TPAALRPLVL GGNQLVIIVG IVCATILLLP VLILIVKKTC
GNKSSVNSTV LVKNTKKTNP EIKEKPCHFE RCEGEKHIYS PIIVREVIEE EEPSEKSEAT
YMTMHPVWPS LRSDRNNSLE KKSGGGMPKT QQAF


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