ID Q6MGA2_RAT Unreviewed; 272 AA.
AC Q6MGA2; A6JJD8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 156.
DE SubName: Full=RT1 class II, DO beta {ECO:0000313|EMBL:CAE83944.1};
DE SubName: Full=RT1 class II, locus DOb {ECO:0000313|Ensembl:ENSRNOP00000082841.1};
DE SubName: Full=RT1-DOb {ECO:0000313|EMBL:AGV39012.1};
GN Name=RT1-DOb {ECO:0000313|EMBL:CAE83944.1,
GN ECO:0000313|Ensembl:ENSRNOP00000082841.1, ECO:0000313|RGD:1595814};
GN Synonyms=DOb {ECO:0000313|EMBL:AGV39012.1};
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|EMBL:AGV39012.1};
RN [1] {ECO:0000313|EMBL:CAE83944.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brown Norway {ECO:0000313|EMBL:CAE83944.1};
RA Boehm S., Borzym K., Gelling S., Gimmel V., Heitmann K., Kosiura A.,
RA Lang N., Lehrack S., Thiel J., Sontag M., Hurt P., Himmelbauer H.,
RA Sudbrak R., Reinhardt R.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAE83944.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brown Norway {ECO:0000313|EMBL:CAE83944.1};
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000082841.1, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000082841.1,
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 [4] {ECO:0000313|EMBL:AGV39012.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DA.1H {ECO:0000313|EMBL:AGV39012.1};
RX PubMed=24586191; DOI=10.1371/journal.pgen.1004151;
RG EURATRANS;
RA Tuncel J., Haag S., Yau A.C.Y., Norin U., Baud A., Lonnblom E., Maratou K.,
RA Ytterberg A.J., Ekman D., Thordardottir S., Johannesson M., Gillett A.,
RA Stridh P., Jagodic M., Olsson T., Fernandez-Teruel A., Zubarev R.A.,
RA Mott R., Aitman T.J., Flint J., Holmdahl R.;
RT "Natural polymorphisms in Tap2 influence negative selection and CD4?CD8
RT lineage commitment in the rat.";
RL PLoS Genet. 10:e1004151-e1004151(2014).
RN [5] {ECO:0000313|Ensembl:ENSRNOP00000082841.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000082841.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the MHC class II family.
CC {ECO:0000256|ARBA:ARBA00007394}.
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DR EMBL; KC222915; AGV39012.1; -; mRNA.
DR EMBL; BX883043; CAE83944.1; -; Genomic_DNA.
DR RefSeq; NP_001008846.1; NM_001008846.1.
DR STRING; 10116.ENSRNOP00000000526; -.
DR PaxDb; 10116-ENSRNOP00000000526; -.
DR Ensembl; ENSRNOT00000085724.2; ENSRNOP00000082841.1; ENSRNOG00000000454.6.
DR GeneID; 365542; -.
DR KEGG; rno:365542; -.
DR UCSC; RGD:1595814; rat.
DR AGR; RGD:1595814; -.
DR CTD; 365542; -.
DR RGD; 1595814; RT1-DOb.
DR eggNOG; ENOG502RWX2; Eukaryota.
DR GeneTree; ENSGT00940000162353; -.
DR HOGENOM; CLU_047501_13_1_1; -.
DR OMA; DIKITWF; -.
DR OrthoDB; 3785866at2759; -.
DR TreeFam; TF336626; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000454; Expressed in spleen and 18 other cell types or tissues.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0042613; C:MHC class II protein complex; ISO:RGD.
DR GO; GO:0023026; F:MHC class II protein complex binding; ISO:RGD.
DR GO; GO:0042605; F:peptide antigen binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IBA:GO_Central.
DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; ISO:RGD.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0050778; P:positive regulation of immune response; IBA:GO_Central.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR014745; MHC_II_a/b_N.
DR InterPro; IPR000353; MHC_II_b_N.
DR PANTHER; PTHR19944:SF43; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DO BETA CHAIN; 1.
DR PANTHER; PTHR19944; MHC CLASS II-RELATED; 1.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00969; MHC_II_beta; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00921; MHC_II_beta; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW MHC II {ECO:0000256|ARBA:ARBA00023182};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 225..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..213
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 272 AA; 30604 MW; 162F9B6BAEBC861B CRC64;
MGAGRAPWVV ALLVNLMRPD SFMVEGRDSP EDFVIQAKAE CYFTNGTEKV RFLVRFIFNL
EEYLHFDSDL GFFVALTELG EVDADQWNKR LDLLETSRAA VNMVCRQEYK LGAPFTVERN
VPPEVTVYPE RTPLLQQHNL LLCSVTDFYP GDISVRWFRN GQEERSGVMS TGLVRNGDWT
FQTTVMLEMI PELGDVYSCL VEHPGLLRPV SVAWVAQSEY SWEKILSGAA AFLLGLTVFL
VGAVIHLKAQ KASVETQPGN EASRALLPPH PY
//
