HA1B_RABIT
ID HA1B_RABIT Reviewed; 361 AA.
AC P06140;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=RLA class I histocompatibility antigen, alpha chain 19-1;
DE Flags: Precursor;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3917974; DOI=10.1007/bf00372243;
RA Marche P.N., Tykocinski M.L., Max E.E., Kindt T.J.;
RT "Structure of a functional rabbit class I MHC gene: similarity to human
RT class I genes.";
RL Immunogenetics 21:71-82(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 -!- SIMILARITY: Belongs to the MHC class I family. {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; K02819; AAA98730.1; -; Genomic_DNA.
DR PIR; I46858; I46858.
DR PDB; 6M24; X-ray; 2.29 A; A=25-298.
DR PDB; 6M2J; X-ray; 2.20 A; A=25-298.
DR PDB; 6M2K; X-ray; 2.59 A; A=25-298.
DR PDBsum; 6M24; -.
DR PDBsum; 6M2J; -.
DR PDBsum; 6M2K; -.
DR AlphaFoldDB; P06140; -.
DR SMR; P06140; -.
DR PRIDE; P06140; -.
DR Proteomes; UP000001811; Unplaced.
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: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; Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..361
FT /note="RLA class I histocompatibility antigen, alpha chain
FT 19-1"
FT /id="PRO_0000018942"
FT TOPO_DOM 25..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..361
FT /note="Cytoplasmic"
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..308
FT /note="Connecting peptide"
FT REGION 335..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01901"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 125..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 227..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6M24"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:6M2K"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:6M2J"
FT HELIX 83..109
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:6M2J"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:6M2J"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:6M2J"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:6M2J"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 219..235
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:6M2J"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:6M2J"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:6M2J"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6M2J"
SQ SEQUENCE 361 AA; 40455 MW; C06FBD8B87ED0546 CRC64;
MGSIPPRTLL LLLAGALTLK DTQAGSHSMR YFYTSVSRPG LGEPRFIIVG YVDDTQFVRF
DSDAASPRME QRAPWMGQVE PEYWDQQTQI AKDTAQTFRV NLNTALRYYN QSAAGSHTFQ
TMFGCEVWAD GRFFHGYRQY AYDGADYIAL NEDLRSWTAA DTAAQNTQRK WEAAGEAERH
RAYLERECVE WLRRYLEMGK ETLQRADPPK AHVTHHPASD REATLRCWAL GFYPAEISLT
WQRDGEDQTQ DTELVETRPG GDGTFQKWAA VVVPSGEEQR YTCRVQHEGL PEPLTLTWEP
PAQPTALIVG IVAGVLGVLL ILGAVVAVVR RKKHSSDGKG GRYTPAAGGH RDQGSDDSLM
P
