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Database: UniProt
Entry: Q9MX27_ONCMY
LinkDB: Q9MX27_ONCMY
Original site: Q9MX27_ONCMY 
ID   Q9MX27_ONCMY            Unreviewed;       219 AA.
AC   Q9MX27;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=MHC class II alpha {ECO:0000313|EMBL:CAB96450.1};
DE   Flags: Fragment;
GN   Name=onmy-DAA {ECO:0000313|EMBL:CAB96450.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022 {ECO:0000313|EMBL:CAB96450.1};
RN   [1] {ECO:0000313|EMBL:CAB96450.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10906388; DOI=10.1016/S0145-305X(00)00034-3;
RA   Grimholt U., Getahun A., Hermsen T., Stet R.J.;
RT   "The major histocompatibility class II alpha chain in salmonid fishes.";
RL   Dev. Comp. Immunol. 24:751-763(2000).
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DR   EMBL; AJ251431; CAB96450.1; -; mRNA.
DR   AlphaFoldDB; Q9MX27; -.
DR   GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW.
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; IPR001003; MHC_II_a_N.
DR   PANTHER; PTHR19944:SF86; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN; 1.
DR   PANTHER; PTHR19944; MHC CLASS II-RELATED; 1.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00993; MHC_II_alpha; 1.
DR   SMART; SM00407; IGc1; 1.
DR   SMART; SM00920; MHC_II_alpha; 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};
KW   MHC II {ECO:0000256|ARBA:ARBA00023182}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..219
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004330172"
FT   DOMAIN          98..192
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   NON_TER         219
FT                   /evidence="ECO:0000313|EMBL:CAB96450.1"
SQ   SEQUENCE   219 AA;  24208 MW;  EA676F3B07D0CA48 CRC64;
     MKTSMIVLIL CCQVYAEDKV LHTDIYINGC SDSDGVDMYG LDGEELWYAD FNKKEGVVAL
     PPFADQISFP GYYEQAVGNQ RTCKGDLGVD IKAYKNPPET IDPPHSSIYP RDDVELGVEN
     TLICHVSGFF PSPVRVRWTR NDQNVTEGGR ISTPYPNTDV TFNQFSSLSF TPEEGDIYGC
     TVEHKALTEP LTRIWEPEVS QPSVGPAVFC GVGLTLGLL
//
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