HA12_RAT
ID HA12_RAT Reviewed; 371 AA.
AC P16391; O02940;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=RT1 class I histocompatibility antigen, AA alpha chain;
DE Flags: Precursor;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2315309; DOI=10.1073/pnas.87.6.2167;
RA Rada C., Lorenzi R., Powis S.J., van den Bogaerde J., Parham P.,
RA Howard J.C.;
RT "Concerted evolution of class I genes in the major histocompatibility
RT complex of murine rodents.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2167-2171(1990).
RN [2]
RP SEQUENCE REVISION.
RC STRAIN=DA; TISSUE=Lymph node, and Spleen;
RA Howard J.C.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 25-299.
RX PubMed=11163232; DOI=10.1016/s1074-7613(01)00091-7;
RA Speir J.A., Stevens J., Joly E., Butcher G.W., Wilson I.A.;
RT "Two different, highly exposed, bulged structures for an unusually long
RT peptide bound to rat MHC class I RT1-A(a).";
RL Immunity 14:81-92(2001).
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}.
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DR EMBL; M31018; AAB49324.1; -; mRNA.
DR PIR; A35090; A35090.
DR PDB; 1ED3; X-ray; 2.55 A; A/D=25-299.
DR PDB; 1KJM; X-ray; 2.35 A; A=25-300.
DR PDB; 6NF7; X-ray; 2.90 A; A/D/G/J/M=25-299.
DR PDBsum; 1ED3; -.
DR PDBsum; 1KJM; -.
DR PDBsum; 6NF7; -.
DR AlphaFoldDB; P16391; -.
DR SMR; P16391; -.
DR MINT; P16391; -.
DR GlyGen; P16391; 2 sites.
DR jPOST; P16391; -.
DR PRIDE; P16391; -.
DR EvolutionaryTrace; P16391; -.
DR Proteomes; UP000002494; Unplaced.
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:0071556; C:integral component of 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: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:0006955; P:immune response; IEA:InterPro.
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 InterPro; IPR010579; MHC_I_a_C.
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; 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; Glycoprotein; Immunity; Membrane; MHC I; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..371
FT /note="RT1 class I histocompatibility antigen, AA alpha
FT chain"
FT /id="PRO_0000018944"
FT TOPO_DOM 25..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..371
FT /note="Cytoplasmic"
FT DOMAIN 209..295
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..311
FT /note="Connecting peptide"
FT REGION 342..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 26..36
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1KJM"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1ED3"
FT HELIX 81..108
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1ED3"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1KJM"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:1KJM"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1KJM"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:1KJM"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 221..235
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1KJM"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:1ED3"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:1KJM"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6NF7"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1KJM"
SQ SEQUENCE 371 AA; 41830 MW; 79C162463E1746D8 CRC64;
MEAMAPRTLL LLLAAALAPT QTRAGSHSLR YFYTAVSRPG LGEPRFIAVG YVDDTEFVRF
DSDAENPRME PRARWMEREG PEYWEQQTRI AKEWEQIYRV DLRTLRGYYN QSEGGSHTIQ
EMYGCDVGSD GSLLRGYRQD AYDGRDYIAL NEDLKTWTAA DFAAQITRNK WERARYAERL
RAYLEGTCVE WLSRYLELGK ETLLRSDPPE AHVTLHPRPE GDVTLRCWAL GFYPADITLT
WQLNGEDLTQ DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCRVEHEGL PKPLSQRWEP
SPSTDSNMET TVIYVILGAV AMIGAVAIIG AMVAVVRRRK RNTGGKGGDY APAPGRDSSQ
SSDVSLPDCK A
