ID Q6PEB5_MOUSE Unreviewed; 338 AA. AC Q6PEB5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-SEP-2023, entry version 143. DE SubName: Full=H2-Bl protein {ECO:0000313|EMBL:AAH58170.1}; DE SubName: Full=Truncated MHC class I antigen splice variant Bl.1a {ECO:0000313|EMBL:AAY51868.1}; GN Name=H2-Bl {ECO:0000313|EMBL:AAH58170.1, ECO:0000313|MGI:MGI:892004}; 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:AAH58170.1}; RN [1] {ECO:0000313|EMBL:AAH58170.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Mix FVB/N {ECO:0000313|EMBL:AAH58170.1}; RC TISSUE=Mammary tumor. WAP-TGF alpha model. 7 months old RC {ECO:0000313|EMBL:AAH58170.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] {ECO:0000313|EMBL:AAY51868.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CD1 {ECO:0000313|EMBL:AAY51868.1}, and FVB/NJ RC {ECO:0000313|EMBL:AAY51869.1}; RC TISSUE=Small intestine {ECO:0000313|EMBL:AAY51868.1}; RX PubMed=16210630; RA Guidry P.A., Stroynowski I.; RT "The murine family of gut-restricted class Ib MHC includes alternatively RT spliced isoforms of the proposed HLA-G homolog, "blastocyst MHC"."; RL J. Immunol. 175:5248-5259(2005). 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; BC058170; AAH58170.1; -; mRNA. DR EMBL; AY989853; AAY51868.1; -; mRNA. DR EMBL; AY989854; AAY51869.1; -; mRNA. DR AlphaFoldDB; Q6PEB5; -. DR MGI; MGI:892004; H2-Bl. DR ChiTaRS; H2-Bl; mouse. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA: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; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0042824; C:MHC class I peptide loading complex; ISO:MGI. DR GO; GO:0042612; C:MHC class I protein complex; ISO:MGI. DR GO; GO:0032398; C:MHC class Ib 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:0042610; F:CD8 receptor binding; ISO:MGI. DR GO; GO:0042288; F:MHC class I protein binding; ISO:MGI. DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; ISO:MGI. DR GO; GO:0042605; F:peptide antigen binding; ISO:MGI. DR GO; GO:0042277; F:peptide binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI. DR GO; GO:0005102; F:signaling 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:0062061; F:TAP complex binding; ISO:MGI. DR GO; GO:0002250; P:adaptive immune response; ISO:MGI. DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI. DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IBA:GO_Central. DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; ISO:MGI. DR GO; GO:0002477; P:antigen processing and presentation of exogenous peptide antigen via MHC class Ib; ISO:MGI. DR GO; GO:0036037; P:CD8-positive, alpha-beta T cell activation; ISO:MGI. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0002519; P:natural killer cell tolerance induction; ISO:MGI. DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; ISO:MGI. DR GO; GO:0001815; P:positive regulation of antibody-dependent cellular cytotoxicity; ISO:MGI. DR GO; GO:2001187; P:positive regulation of CD8-positive, alpha-beta T cell activation; ISO:MGI. DR GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; ISO:MGI. DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:MGI. DR GO; GO:0032736; P:positive regulation of interleukin-13 production; ISO:MGI. DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:MGI. DR GO; GO:0002729; P:positive regulation of natural killer cell cytokine production; ISO:MGI. DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:MGI. DR GO; GO:0002717; P:positive regulation of natural killer cell mediated immunity; ISO:MGI. DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; ISO:MGI. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISO:MGI. DR GO; GO:0032759; P:positive regulation of TRAIL production; ISO:MGI. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI. DR GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; IDA:MGI. DR GO; GO:0002715; P:regulation of natural killer cell mediated immunity; ISO:MGI. DR CDD; cd21016; IgC1_MHC_Ib_T10_T22_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; 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 PANTHER; PTHR16675:SF251; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW 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..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..338 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014310596" FT TRANSMEM 297..317 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 195..283 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT REGION 47..66 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 338 AA; 38077 MW; AA892E687FCF61C0 CRC64; MAQRTLLLLL AAALTMIQTR AVFGPGLGEP RFISVGYVDN TQFVSFDSDA ENPRSEPRSP WMEQEGPEYW ERETQIAKDN EQSFGWSLRN LIHYYNQSKG GFHTFQRLSG CDMGLDGRLL RGYLQFAYDG RDYIALNEDL KTWMAADLVA LITRRKWEQA GAAELYKFYL EGECVEWLRR YLELGNETLL RTDPPKAHVT RHPRPAGDVT LRCWALGFYP ADITLTWQLN GEELTQDMEL VETRPAGDGT FQKWAAVVVP LGKEQNYTCR VHHEGLPEPL TLRWEPPPST GSNMVNIAVL VVLGAVIIIE AMVAFALKSR RKIAILPGPA GTRGSSAS //