ID T1WTJ2_MACAS Unreviewed; 365 AA. AC T1WTJ2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 19-JAN-2022, entry version 32. DE SubName: Full=MHC class I antigen A {ECO:0000313|EMBL:AGU42097.1}; OS Macaca assamensis (Assam macaque) (Assamese macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9551 {ECO:0000313|EMBL:AGU42097.1}; RN [1] {ECO:0000313|EMBL:AGU42097.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=X1-7 {ECO:0000313|EMBL:AGU42097.1}; RX PubMed=24045838; DOI=10.1007/s00251-013-0735-4; RA Yan X., Li A., Zeng L., Cao Y., He J., Lv L., Sui L., Ye H., Fan J., RA Cui X., Sun Z.; RT "Identification of MHC class I sequences in four species of Macaca of RT China."; RL Immunogenetics 65:851-859(2013). CC -!- SIMILARITY: Belongs to the MHC class I family. CC {ECO:0000256|RuleBase:RU004439}. 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; KF012906; AGU42097.1; -; mRNA. 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:0030670; C:phagocytic vesicle membrane; IEA:UniProt. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProt. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; IEA:UniProt. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IEA:UniProt. DR GO; GO:0045321; P:leukocyte activation; IEA:UniProt. 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..365 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004585643" FT TRANSMEM 308..332 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 209..297 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT REGION 338..365 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" SQ SEQUENCE 365 AA; 40871 MW; 70E61FA696CB0A28 CRC64; MAIMAPRTLL LVLSGALVLT QTRAGSHSMK YFYTSMSRPG RGQPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWVEQEG PEYWDRETQK MKTETQNAPV NLRNLLRYYN QSEAGSHTIQ KMYGCDLGPD ARLLRGYEQS AYDGKDYIAL NEDLRSWTAA DVAAQNTQRK WEAADVAESM RAYLEGECLE WLRRYLEDGK EMLQRTDPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPHTLKWEP SSQSTIPMVG IIAGLVLLGA VVTGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV //