HA1T_MOUSE
ID HA1T_MOUSE Reviewed; 384 AA.
AC P14432; P14433; Q31194; Q31203;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=H-2 class I histocompatibility antigen, TLA(B) alpha chain;
DE AltName: Full=MHC thymus leukemia antigen;
DE Flags: Precursor;
GN Name=H2-T3;
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=BALB/cJ;
RX PubMed=3894562; DOI=10.1084/jem.162.2.528;
RA Fisher D.A., Hunt S.W. III, Hood L.E.;
RT "Structure of a gene encoding a murine thymus leukemia antigen, and
RT organization of Tla genes in the BALB/c mouse.";
RL J. Exp. Med. 162:528-545(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3456611; DOI=10.1073/pnas.83.6.1782;
RA Pontarotti P.A., Mashimo H., Zeff R.A., Fisher D.A., Hood L., Mellor A.,
RA Flavell R.A., Nathenson S.G.;
RT "Conservation and diversity in the class I genes of the major
RT histocompatibility complex: sequence analysis of a Tlab gene and comparison
RT with a Tlac gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1782-1786(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1339405; DOI=10.1007/bf00215662;
RA Mashimo H., Chorney M.J., Pontarotti P., Fisher D.A., Hood L.,
RA Nathenson S.G.;
RT "Nucleotide sequence of the BALB/c H-2T region gene, T3d.";
RL Immunogenetics 36:326-332(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-384.
RX PubMed=2410925; DOI=10.1073/pnas.82.16.5475;
RA Obata Y., Chen Y.-T., Stockert E., Old L.J.;
RT "Structural analysis of TL genes of the mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5475-5479(1985).
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 -!- TISSUE SPECIFICITY: TL antigens are only expressed on thymocytes,
CC activated T-lymphocytes and on some thymic leukemias.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26586.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X02817; CAA26586.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M13285; AAA39687.1; -; Genomic_DNA.
DR EMBL; M75875; AAA39658.1; -; Genomic_DNA.
DR EMBL; M11741; AAA39692.1; -; Genomic_DNA.
DR EMBL; M11742; AAA39692.1; JOINED; Genomic_DNA.
DR CCDS; CCDS28718.1; -.
DR PIR; A25132; A25132.
DR PIR; A25148; A25148.
DR PIR; I48851; I48851.
DR PIR; I54499; I54499.
DR PDB; 1NEZ; X-ray; 2.10 A; A=27-300.
DR PDBsum; 1NEZ; -.
DR AlphaFoldDB; P14432; -.
DR SMR; P14432; -.
DR STRING; 10090.ENSMUSP00000099736; -.
DR GlyGen; P14432; 4 sites.
DR jPOST; P14432; -.
DR MaxQB; P14432; -.
DR PaxDb; P14432; -.
DR PeptideAtlas; P14432; -.
DR PRIDE; P14432; -.
DR ProteomicsDB; 271383; -.
DR MGI; MGI:95959; H2-T3.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR InParanoid; P14432; -.
DR PhylomeDB; P14432; -.
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 EvolutionaryTrace; P14432; -.
DR PRO; PR:P14432; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P14432; protein.
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: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: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: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: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:0046977; F:TAP binding; ISO:MGI.
DR GO; GO:0062061; F:TAP complex 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..384
FT /note="H-2 class I histocompatibility antigen, TLA(B) alpha
FT chain"
FT /id="PRO_0000018937"
FT TOPO_DOM 27..314
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 211..299
FT /note="Ig-like C1-type"
FT REGION 27..116
FT /note="Alpha-1"
FT REGION 117..208
FT /note="Alpha-2"
FT REGION 209..300
FT /note="Alpha-3"
FT REGION 301..314
FT /note="Connecting peptide"
FT REGION 354..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 127..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 229..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 147
FT /note="P -> R (in haplotype T3B)"
FT VARIANT 365
FT /note="E -> D (in haplotype T3B)"
FT VARIANT 381
FT /note="P -> H (in haplotype T3B)"
FT CONFLICT 6
FT /note="P -> Q (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="G -> S (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="G -> V (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="V -> A (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="N -> D (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="S -> A (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="A -> G (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="P -> Q (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="T -> M (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="P -> A (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="Y -> D (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="R -> G (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="D -> H (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="L -> S (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="K -> E (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="P -> L (in Ref. 4; AAA39692)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="T -> S (in Ref. 1; CAA26586)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="D -> T (in Ref. 4; AAA39692)"
FT /evidence="ECO:0000305"
FT STRAND 28..39
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1NEZ"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1NEZ"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1NEZ"
FT HELIX 83..102
FT /evidence="ECO:0007829|PDB:1NEZ"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 119..130
FT /evidence="ECO:0007829|PDB:1NEZ"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1NEZ"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:1NEZ"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:1NEZ"
FT HELIX 189..204
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 223..237
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:1NEZ"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1NEZ"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1NEZ"
SQ SEQUENCE 384 AA; 43479 MW; 305891FC35F41E76 CRC64;
MRMGTPVPGT LLILLAASQG QTQTCPGSHS LRYFYTALSR PAISEPWYIA VGYLDDTQFV
RFNSSGETAT YKLSAPWVEQ EGPEYWARET EIVTSNAQFF RENLQTMLDY YNLSQNGSHT
IQVMYGCEVE FFGSLFRAYE QHGYDGPDYI ALNEDLKTWT AADTAAEITR SKWEQAGYTE
LRRTYLEGPC KDSLLRYLEN RKKTQECTDP PKTHVTHHPR PEGYVTLRCW ALRFYPADIT
LTWQLNGEEL IQDTELVETR PAGDGTFQKW AAVVVPLGKE QKYTCHVYHE GLPEPLTLRW
EPPQTSMPNR TTVRALLGAM IILGFMSGSV MMWMRKNNGG NGDDNTAAYQ NEREHLSLDP
RAESEALGVE AGMKDLPSAP PLVS
