HA10_MOUSE
ID HA10_MOUSE Reviewed; 325 AA.
AC P01898; O19475; Q31214; Q95HC3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=H-2 class I histocompatibility antigen, Q10 alpha chain;
DE Flags: Precursor;
GN Name=H2-Q10;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6420070; DOI=10.1016/0092-8674(84)90082-5;
RA Mellor A.L., Weiss E.H., Kress M., Jay G., Flavell R.A.;
RT "A nonpolymorphic class I gene in the murine major histocompatibility
RT complex.";
RL Cell 36:139-144(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C3H/HeJ;
RX PubMed=2767053; DOI=10.1002/j.1460-2075.1989.tb03568.x;
RA Watts S., Davis A.C., Gaut B., Wheeler C., Hill L., Goodenow R.S.;
RT "Organization and structure of the Qa genes of the major histocompatibility
RT complex of the C3H mouse: implications for Qa function and class I
RT evolution.";
RL EMBO J. 8:1749-1759(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RX PubMed=3510743; DOI=10.1016/0092-8674(86)90760-9;
RA Kimura A., Israel A., le Bail O., Kourilsky P.;
RT "Detailed analysis of the mouse H-2Kb promoter: enhancer-like sequences and
RT their role in the regulation of class I gene expression.";
RL Cell 44:261-272(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-325 (CLONE PH16).
RX PubMed=6411351; DOI=10.1016/0092-8674(83)90149-6;
RA Kress M., Cosman D., Khoury G., Jay G.;
RT "Secretion of a transplantation-related antigen.";
RL Cell 34:189-196(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 300-325.
RX PubMed=2584927; DOI=10.1084/jem.170.6.1837;
RA Brorson K.A., Hunt S.W. III, Hunkapiller T., Sun Y.H., Cheroutre H.,
RA Nickerson D.A., Hood L.;
RT "Comparison of exon 5 sequences from 35 class I genes of the BALB/c
RT mouse.";
RL J. Exp. Med. 170:1837-1858(1989).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110 AND ASN-280.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the presentation of foreign antigens to the
CC immune system.
CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
CC microglobulin).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39574.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA39676.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; K01207; AAA39574.1; ALT_INIT; Genomic_DNA.
DR EMBL; K01205; AAA39574.1; JOINED; Genomic_DNA.
DR EMBL; X16426; CAA34449.1; -; Genomic_DNA.
DR EMBL; AK131620; BAE20725.1; -; mRNA.
DR EMBL; BC011215; AAH11215.1; -; mRNA.
DR EMBL; M12484; AAA39676.1; ALT_INIT; Genomic_DNA.
DR EMBL; K00614; AAA39681.1; -; mRNA.
DR EMBL; X16206; CAA34326.1; -; Genomic_DNA.
DR CCDS; CCDS37599.1; -.
DR PIR; A02199; HLMSTR.
DR PIR; A21125; A21125.
DR PIR; S20045; S20045.
DR RefSeq; NP_034521.1; NM_010391.4.
DR PDB; 5J6G; X-ray; 3.30 A; A/C=25-280.
DR PDB; 5J6H; X-ray; 2.30 A; A=25-325.
DR PDBsum; 5J6G; -.
DR PDBsum; 5J6H; -.
DR AlphaFoldDB; P01898; -.
DR SMR; P01898; -.
DR BioGRID; 200177; 1.
DR STRING; 10090.ENSMUSP00000134163; -.
DR GlyGen; P01898; 2 sites.
DR iPTMnet; P01898; -.
DR PhosphoSitePlus; P01898; -.
DR CPTAC; non-CPTAC-5600; -.
DR EPD; P01898; -.
DR jPOST; P01898; -.
DR MaxQB; P01898; -.
DR PaxDb; P01898; -.
DR PeptideAtlas; P01898; -.
DR PRIDE; P01898; -.
DR ProteomicsDB; 270920; -.
DR DNASU; 15007; -.
DR Ensembl; ENSMUST00000068291; ENSMUSP00000066419; ENSMUSG00000067235.
DR Ensembl; ENSMUST00000174525; ENSMUSP00000134163; ENSMUSG00000067235.
DR GeneID; 15007; -.
DR KEGG; mmu:15007; -.
DR UCSC; uc008cht.1; mouse.
DR CTD; 15007; -.
DR MGI; MGI:95929; H2-Q10.
DR VEuPathDB; HostDB:ENSMUSG00000067235; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR GeneTree; ENSGT00980000198488; -.
DR HOGENOM; CLU_047501_0_1_1; -.
DR InParanoid; P01898; -.
DR OMA; EREDQEY; -.
DR OrthoDB; 1390181at2759; -.
DR PhylomeDB; P01898; -.
DR TreeFam; TF336617; -.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-1236977; Endosomal/Vacuolar pathway.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2172127; DAP12 interactions.
DR Reactome; R-MMU-2424491; DAP12 signaling.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 15007; 2 hits in 75 CRISPR screens.
DR ChiTaRS; H2-Q10; mouse.
DR PRO; PR:P01898; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P01898; protein.
DR Bgee; ENSMUSG00000067235; Expressed in left lobe of liver and 94 other tissues.
DR Genevisible; P01898; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0033106; C:cis-Golgi network membrane; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; 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:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO: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:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein 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:0042803; F:protein homodimerization activity; 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:0046978; F:TAP1 binding; ISO:MGI.
DR GO; GO:0046979; F:TAP2 binding; ISO:MGI.
DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 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 Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..325
FT /note="H-2 class I histocompatibility antigen, Q10 alpha
FT chain"
FT /id="PRO_0000018936"
FT TOPO_DOM 25..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 209..297
FT /note="Ig-like C1-type"
FT REGION 25..114
FT /note="Alpha-1"
FT REGION 115..206
FT /note="Alpha-2"
FT REGION 207..298
FT /note="Alpha-3"
FT REGION 299..310
FT /note="Connecting peptide"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT DISULFID 125..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 227..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 99
FT /note="H -> R (in Ref. 4; AAH11215)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="Y -> H (in Ref. 1; AAA39574)"
FT /evidence="ECO:0000305"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:5J6H"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:5J6H"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:5J6H"
FT HELIX 81..108
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5J6H"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:5J6H"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:5J6H"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:5J6H"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 222..235
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5J6G"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:5J6H"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:5J6H"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:5J6H"
SQ SEQUENCE 325 AA; 37251 MW; 82B8B7B9140CD72A CRC64;
MGAMAPRTLL LLLAAALAPT QTQAGSHSMR YFETSVSRPG LGEPRFIIVG YVDDTQFVRF
DSDAETPRME PRAPWMEQEG PEYWERETQR AKGNEQSFHV SLRTLLGYYN QSESGSHTIQ
WMYGCKVGSD GRFLRGYLQY AYDGRDYIAL NEDLKTWTAA DVAAIITRRK WEQAGAAEYY
RAYLEAECVE WLLRYLELGK ETLLRTDPPK THVTHHPGSE GDVTLRCWAL GFYPADITLT
WQLNGEELTQ DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCHVYHEGL PEPLTLRWEP
PPSTDSIMSH IADLLWPSLK LWWYL
