ID Q5HYL2_HUMAN Unreviewed; 362 AA. AC Q5HYL2; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 24-JUL-2024, entry version 128. DE SubName: Full=Uncharacterized protein DKFZp686N10220 {ECO:0000313|EMBL:CAI46008.1}; GN Name=DKFZp686N10220 {ECO:0000313|EMBL:CAI46008.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CAI46008.1}; RN [1] {ECO:0000313|EMBL:CAI46008.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Rectum tumor {ECO:0000313|EMBL:CAI46008.1}; RG The German cDNA Consortium; RA Wambutt R., Heubner D., Mewes H.W., Weil B., Amid C., Osanger A., Fobo G., RA Han M., Wiemann S.; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. 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}. 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; BX647315; CAI46008.1; -; mRNA. DR AlphaFoldDB; Q5HYL2; -. DR PeptideAtlas; Q5HYL2; -. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProt. 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:0055038; C:recycling endosome 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; cd21026; IgC1_MHC_Ia_HLA-B; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; 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}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..362 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004257364" FT TRANSMEM 306..330 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 209..295 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT REGION 335..362 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 339..362 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 362 AA; 40538 MW; DC9703B049418C82 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAAG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE NLRIALRYYN QSEAGSHTWQ TMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRHLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA //