HA17_MOUSE
ID HA17_MOUSE Reviewed; 334 AA.
AC P14429;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=H-2 class I histocompatibility antigen, Q7 alpha chain;
DE AltName: Full=QA-2 antigen;
DE Flags: Precursor;
GN Name=H2-Q7;
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].
RC STRAIN=C57BL/10;
RX PubMed=3004940; DOI=10.1002/j.1460-2075.1985.tb04066.x;
RA Devlin J.J., Weiss E.H., Paulson M., Flavell R.A.;
RT "Duplicated gene pairs and alleles of class I genes in the Qa2 region of
RT the murine major histocompatibility complex: a comparison.";
RL EMBO J. 4:3203-3207(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10;
RX PubMed=3502706; DOI=10.1084/jem.165.5.1358;
RA Waneck G.L., Sherman D.H., Calvin S., Allen H., Flavell R.A.;
RT "Tissue-specific expression of cell-surface Qa-2 antigen from a transfected
RT Q7b gene of C57BL/10 mice.";
RL J. Exp. Med. 165:1358-1370(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=6895187; DOI=10.1016/0092-8674(81)90175-6;
RA Steinmetz M., Moore K.W., Frelinger J.G., Sher B.T., Shen F.W., Boyse E.A.,
RA Hood L.;
RT "A pseudogene homologous to mouse transplantation antigens: transplantation
RT antigens are encoded by eight exons that correlate with protein domains.";
RL Cell 25:683-692(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 292-334.
RX PubMed=2249652; DOI=10.1002/j.1460-2075.1990.tb07602.x;
RA Ulker N., Lewis K.D., Hood L.E., Stroynowski I.;
RT "Activated T cells transcribe an alternatively spliced mRNA encoding a
RT soluble form of Qa-2 antigen.";
RL EMBO J. 9:3839-3847(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 300-334.
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).
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=CAA28977.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X03210; CAA26954.1; -; Genomic_DNA.
DR EMBL; X03441; CAA26954.1; JOINED; Genomic_DNA.
DR EMBL; X05389; CAA28977.1; ALT_INIT; mRNA.
DR EMBL; X57330; CAA40606.1; -; mRNA.
DR CCDS; CCDS28697.1; -.
DR PIR; A24582; A24582.
DR RefSeq; NP_034524.3; NM_010394.4.
DR PDB; 1K8D; X-ray; 2.30 A; A=22-295.
DR PDBsum; 1K8D; -.
DR AlphaFoldDB; P14429; -.
DR SMR; P14429; -.
DR MINT; P14429; -.
DR STRING; 10090.ENSMUSP00000071843; -.
DR GlyGen; P14429; 2 sites.
DR iPTMnet; P14429; -.
DR PhosphoSitePlus; P14429; -.
DR EPD; P14429; -.
DR jPOST; P14429; -.
DR MaxQB; P14429; -.
DR PaxDb; P14429; -.
DR PRIDE; P14429; -.
DR ProteomicsDB; 269799; -.
DR DNASU; 15018; -.
DR Ensembl; ENSMUST00000071951; ENSMUSP00000071843; ENSMUSG00000060550.
DR GeneID; 15018; -.
DR KEGG; mmu:15018; -.
DR CTD; 15018; -.
DR MGI; MGI:95936; H2-Q7.
DR VEuPathDB; HostDB:ENSMUSG00000060550; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR GeneTree; ENSGT00980000198488; -.
DR HOGENOM; CLU_047501_1_1_1; -.
DR InParanoid; P14429; -.
DR OMA; DREQIYP; -.
DR OrthoDB; 1390181at2759; -.
DR PhylomeDB; P14429; -.
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; 15018; 3 hits in 73 CRISPR screens.
DR ChiTaRS; H2-Q7; mouse.
DR EvolutionaryTrace; P14429; -.
DR PRO; PR:P14429; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P14429; protein.
DR Bgee; ENSMUSG00000060550; Expressed in zone of skin and 55 other tissues.
DR ExpressionAtlas; P14429; baseline and differential.
DR Genevisible; P14429; 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; IBA:GO_Central.
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: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 GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0007566; P:embryo implantation; IDA:MGI.
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..21
FT /evidence="ECO:0000250"
FT CHAIN 22..334
FT /note="H-2 class I histocompatibility antigen, Q7 alpha
FT chain"
FT /id="PRO_0000018933"
FT TOPO_DOM 22..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 206..294
FT /note="Ig-like C1-type"
FT REGION 22..111
FT /note="Alpha-1"
FT REGION 112..203
FT /note="Alpha-2"
FT REGION 204..295
FT /note="Alpha-3"
FT REGION 296..310
FT /note="Connecting peptide"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 122..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 224..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 87
FT /note="I -> M (in Ref. 3)"
FT /evidence="ECO:0000305"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1K8D"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1K8D"
FT HELIX 77..105
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 128..139
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1K8D"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:1K8D"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:1K8D"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:1K8D"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 216..232
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:1K8D"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:1K8D"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1K8D"
SQ SEQUENCE 334 AA; 37924 MW; 1E63FAFCCBD6763B CRC64;
MALTMLLLLV AAALTLIETR AGQHSLQYFH TAVSRPGLGE PWFISVGYVD DTQFVRFDSD
AENPRMEPRA RWMEQEGPEY WERETQIAKG HEQSFRGSLR TAQSYYNQSK GGSHTLQWMY
GCDMGSDGRL LRGYLQFAYE GRDYIALNED LKTWTAVDMA AQITRRKWEQ AGIAEKDQAY
LEGTCMQSLR RYLQLGKETL LRTDPPKAHV THHPRSYGAV TLRCWALGFY PADITLTWQL
NGEELTQDME LVETRPAGDG TFQKWASVVV PLGKEQNYTC HVNHEGLPEP LTLRWGRWEP
PPYTVSNMAT IAVVVDLGAV AIIGAVVAFV MNRR
