GenomeNet

Database: UniProt
Entry: D4A1C2_RAT
LinkDB: D4A1C2_RAT
Original site: D4A1C2_RAT 
ID   D4A1C2_RAT              Unreviewed;       379 AA.
AC   D4A1C2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 3.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Junction adhesion molecule like {ECO:0000313|Ensembl:ENSRNOP00000007588.5};
GN   Name=Jaml {ECO:0000313|Ensembl:ENSRNOP00000007588.5,
GN   ECO:0000313|RGD:1562572}; Synonyms=Amica1 {ECO:0000313|RGD:1562572};
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 {ECO:0000313|Ensembl:ENSRNOP00000007588.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000007588.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000007588.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000007588.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000007588.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_001067982.3; XM_001067982.6.
DR   RefSeq; XP_236198.6; XM_236198.9.
DR   AlphaFoldDB; D4A1C2; -.
DR   SMR; D4A1C2; -.
DR   STRING; 10116.ENSRNOP00000007588; -.
DR   PaxDb; 10116-ENSRNOP00000007588; -.
DR   Ensembl; ENSRNOT00000007588.6; ENSRNOP00000007588.5; ENSRNOG00000026702.7.
DR   UCSC; RGD:1562572; rat.
DR   AGR; RGD:1562572; -.
DR   RGD; 1562572; Jaml.
DR   eggNOG; ENOG502SVGE; Eukaryota.
DR   GeneTree; ENSGT00440000034341; -.
DR   HOGENOM; CLU_059564_0_0_1; -.
DR   InParanoid; D4A1C2; -.
DR   OrthoDB; 4354236at2759; -.
DR   TreeFam; TF331728; -.
DR   Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000026702; Expressed in spleen and 18 other cell types or tissues.
DR   GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR   GO; GO:0005178; F:integrin binding; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0046629; P:gamma-delta T cell activation; ISO:RGD.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR   GO; GO:0035696; P:monocyte extravasation; ISO:RGD.
DR   GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR   GO; GO:0072672; P:neutrophil extravasation; ISO:RGD.
DR   GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; ISO:RGD.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR013106; Ig_V-set.
DR   InterPro; IPR000920; Myelin_P0-rel.
DR   PANTHER; PTHR13869:SF22; JUNCTIONAL ADHESION MOLECULE-LIKE; 1.
DR   PANTHER; PTHR13869; MYELIN P0 RELATED; 1.
DR   Pfam; PF07686; V-set; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00406; IGv; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..379
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003053420"
FT   TRANSMEM        281..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..130
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          140..250
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
SQ   SEQUENCE   379 AA;  42185 MW;  2EC68F9A68C4D73C CRC64;
     MLCLLTLIVI PVVLVSVGYP QGLPDLTVSS LKLRVHVGES ALMGCVVQST EEKPVDKVDW
     VFSKGEHAEN EYVLYYYSSL SVPTGRFQNR SRLVGDLLRN DGSLLLQDVQ KADEGIYTCE
     IRLKNEGSVS KKFVLLHVLP EEPKELRVHV GDPIQMGCFF RSTEERRVTR VNWMFSSGKH
     AQEEIVLSYD FNMHSGTFQG QGRFRNRVDL TGDISRNDGS IMLQTVKKSD QGVYTCSIYL
     GKLESRKTIV LHVIQDESPR SISTTTETAG KQQGILDGNQ LVIIVGIVCA TLLLLPVLIL
     IVKKTKWNKS SVSSIASVKS LENKEKTSSE KHVYSSITTW ETAERGPSGE SEATYMTMHP
     VWRSSPKASS LALSSARIK
//
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