ID   Q61892_MOUSE            Unreviewed;       365 AA.
AC   Q61892;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   24-JUL-2024, entry version 157.
DE   SubName: Full=mRNA {ECO:0000313|EMBL:AAA39739.1};
GN   Name=H2-D1 {ECO:0000313|MGI:MGI:95896};
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 {ECO:0000313|EMBL:AAA39739.1};
RN   [1] {ECO:0000313|EMBL:AAA39739.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B10.SM {ECO:0000313|EMBL:AAA39739.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:AAA39739.1};
RX   PubMed=1370689; DOI=10.1084/jem.175.2.583;
RA   Cai Z., Pease L.R.;
RT   "Structural and functional analysis of three D/L-like class I molecules
RT   from H-2v: indications of an ancestral family of D/L genes.";
RL   J. Exp. Med. 175:583-596(1992).
RN   [2] {ECO:0000313|EMBL:AAA39739.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B10.SM {ECO:0000313|EMBL:AAA39739.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:AAA39739.1};
RX   PubMed=1730883;
RA   Pullen J.K., Horton R.M., Cai Z., Pease L.R.;
RT   "Structural diversity of the classical H-2 genes: K, D, and L.";
RL   J. Immunol. 148:953-967(1992).
CC   -!- FUNCTION: Involved in the presentation of foreign antigens to the
CC       immune system. {ECO:0000256|ARBA:ARBA00002297}.
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 I family.
CC       {ECO:0000256|ARBA:ARBA00006909, ECO:0000256|RuleBase:RU004439}.
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DR   EMBL; M69067; AAA39739.1; -; mRNA.
DR   AlphaFoldDB; Q61892; -.
DR   PeptideAtlas; Q61892; -.
DR   AGR; MGI:95896; -.
DR   MGI; MGI:95896; H2-D1.
DR   ChiTaRS; H2-D1; mouse.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; IEA:UniProt.
DR   GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProt.
DR   GO; GO:0042605; F:peptide antigen binding; IEA:TreeGrafter.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:TreeGrafter.
DR   GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IEA:TreeGrafter.
DR   GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IEA:TreeGrafter.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:TreeGrafter.
DR   CDD; cd12087; TM_EGFR-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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; IPR050208; MHC_class-I_related.
DR   InterPro; IPR011161; MHC_I-like_Ag-recog.
DR   InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR   InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR   InterPro; IPR001039; MHC_I_a_a1/a2.
DR   InterPro; IPR010579; MHC_I_a_C.
DR   PANTHER; PTHR16675:SF242; CLASS IB MHC ANTIGEN QA-2-RELATED; 1.
DR   PANTHER; PTHR16675; MHC CLASS I-RELATED; 1.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00129; MHC_I; 1.
DR   Pfam; PF06623; MHC_I_C; 1.
DR   PRINTS; PR01638; MHCCLASSI.
DR   SMART; SM00407; IGc1; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunity {ECO:0000256|ARBA:ARBA00022451};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   MHC I {ECO:0000256|ARBA:ARBA00022451}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..365
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004265582"
FT   TRANSMEM        310..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          209..297
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          343..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  40910 MW;  2A995EE6384EE480 CRC64;
     MGAMAPRTLL LLLAAALAPT QTRAGPHSLR YFTTAVSRPG LGEPRFISVG YVDNTEFVRF
     DSDAENPRDE PRARWMEQVE PEYWERNTRR AKGHEQWFRV SLRNLLGYYN QSAGGSHTLQ
     WMSGCDVGSD GRLLRGYEQY AYDGCDYIAL NEDLKTWTAA DMAALITKHK WEQAGAAEYY
     RAYLEGECVE WLLRHLKNGN ATLLRTDSPK AHVTHHPRSK GEVTLKCWAL GFYPADITLT
     WQLNGEELTQ DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCHVHHEGL PEPLTLRWGR
     WEPPPSTDSY MVIVAVLGVL GAMAIIGAVV AFVMKRRRNT GGKGGDYALA PGSQSSEMSL
     RDCKA
//