1A01_SAGOE
ID 1A01_SAGOE Reviewed; 365 AA.
AC P30515;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Saoe class I histocompatibility antigen, A alpha chain;
DE AltName: Full=Class I histocompatibility antigen, A alpha chain;
DE Flags: Precursor;
OS Saguinus oedipus (Cotton-top tamarin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Saguinus.
OX NCBI_TaxID=9490;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2104912;
RA Watkins D.I., Letvin N.L., Hughes A.L., Tedder T.F.;
RT "Molecular cloning of cDNA that encode MHC class I molecules from a New
RT World primate (Saguinus oedipus). Natural selection acts at positions that
RT may affect peptide presentation to T cells.";
RL J. Immunol. 144:1136-1143(1990).
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; M33475; AAA36951.1; -; mRNA.
DR PIR; I56053; I56053.
DR AlphaFoldDB; P30515; -.
DR SMR; P30515; -.
DR GO; GO:0009986; C:cell surface; IEA:UniProt.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProt.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProt.
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:0055038; C:recycling endosome 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I; Phosphoprotein;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..365
FT /note="Saoe class I histocompatibility antigen, A alpha
FT chain"
FT /id="PRO_0000018920"
FT TOPO_DOM 25..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..365
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 337..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18462"
FT MOD_RES 344
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18462"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18462"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04439"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30443"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30443"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30443"
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"
SQ SEQUENCE 365 AA; 40973 MW; B34B24FB6848E373 CRC64;
MTVMAPRTLL LLLSGALVLT ETWAGSHSMR YFETSVSRPG RGEPRYISVG YVDDTQFVRF
DSDAASPRME PRAPWMEQEG PEYWEEETRK GKADAQTFRV DLQTLLGYYN QSEAGSHTIQ
WMYGCDLGPD GRLLRGYDQH AYDGKDYIAL NEDLRSWTAT DVAAQITQRK WEAANEAERT
RAYLEGTCVE WLHRYLENGK ETLQRAEPPK THVTHHPVSD HEATLRCWAL GFYPAEITVT
WQRDGEDQTQ DMELVETRPA GDGTFQKWAA VVVLSGEEQR YTCHVQHEGL PEPLTLRWEP
PSQPTIPIMG IVAILAILGV VVTGAVVAAV MWRKKSSDKK GGSYSQAARS DSAQGSDVSL
TACKV
