ID Q61892_MOUSE Unreviewed; 365 AA. AC Q61892; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 125. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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 RT molecules from H-2v: indications of an ancestral family of D/L RT 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|SAAS:SAAS00339060}. CC -!- SIMILARITY: Belongs to the MHC class I family. CC {ECO:0000256|RuleBase:RU004439}. CC -!- SIMILARITY: Contains Ig-like C1-type (immunoglobulin-like) domain. CC {ECO:0000256|SAAS:SAAS00368946}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M69067; AAA39739.1; -; mRNA. DR ProteinModelPortal; Q61892; -. DR MGI; MGI:95896; H2-D1. DR HOVERGEN; HBG016709; -. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISO:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0042612; C:MHC class I protein complex; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0030881; F:beta-2-microglobulin binding; ISO:MGI. DR GO; GO:0042605; F:peptide antigen binding; ISO:MGI. DR GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI. DR GO; GO:0005102; F:receptor binding; ISO:MGI. DR GO; GO:0042608; F:T cell receptor binding; ISO:MGI. DR GO; GO:0046977; F:TAP binding; ISO:MGI. DR GO; GO:0002485; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent; IDA:MGI. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:MGI. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:MGI. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. 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; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|SAAS:SAAS00281758}; KW Immunity {ECO:0000256|SAAS:SAAS00281824}; KW Membrane {ECO:0000256|SAAS:SAAS00281753, ECO:0000256|SAM:Phobius}; KW MHC I {ECO:0000256|SAAS:SAAS00281777}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00281848, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00281807, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 365 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004265582. FT TRANSMEM 310 333 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 209 297 Ig-like (immunoglobulin-like). FT {ECO:0000259|PROSITE:PS50835}. 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 //