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HLAF_MACMU
ID   HLAF_MACMU              Reviewed;         348 AA.
AC   P33617;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Mamu class I histocompatibility antigen, alpha chain F;
DE   AltName: Full=Leukocyte antigen F;
DE   AltName: Full=MHC class I antigen F;
DE   Flags: Precursor;
GN   Name=Mamu-F; Synonyms=HLAF;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8482576; DOI=10.1007/bf00190901;
RA   Otting N., Bontrop R.E.;
RT   "Characterization of the rhesus macaque (Macaca mulatta) equivalent of HLA-
RT   F.";
RL   Immunogenetics 38:141-145(1993).
RN   [2]
RP   SEQUENCE REVISION TO 39; 49; 212; 217; 234; 333 AND 346-347.
RA   Otting N.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; Z21819; CAA79885.2; -; mRNA.
DR   PIR; S29990; S29990.
DR   RefSeq; NP_001036235.2; NM_001042770.2.
DR   AlphaFoldDB; P33617; -.
DR   SMR; P33617; -.
DR   STRING; 9544.ENSMMUP00000011541; -.
DR   GeneID; 709076; -.
DR   KEGG; mcc:709076; -.
DR   CTD; 709076; -.
DR   eggNOG; ENOG502RQEK; Eukaryota.
DR   InParanoid; P33617; -.
DR   OrthoDB; 1390181at2759; -.
DR   Proteomes; UP000006718; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..348
FT                   /note="Mamu class I histocompatibility antigen, alpha chain
FT                   F"
FT                   /id="PRO_0000018885"
FT   TOPO_DOM        22..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        332..348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          208..296
FT                   /note="Ig-like C1-type"
FT   REGION          22..113
FT                   /note="Alpha-1"
FT   REGION          114..205
FT                   /note="Alpha-2"
FT   REGION          206..297
FT                   /note="Alpha-3"
FT   REGION          298..307
FT                   /note="Connecting peptide"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        124..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        226..282
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   348 AA;  39481 MW;  010108EA2FDE4EAD CRC64;
     MAPRTLLLVL SGALALTETW AGSHSLRYFS TAVSRPGRRE PQYRYIAVEY VDDTQFLRFD
     SDAAIPRMEP RAPWVEQEGP QYWERTTGYA KANARTDRVA LRKLLLRYNQ SEAGSHTLQG
     MNGCDMGPDG RLLRGYHQHA YDGKDYISLN EDLRSWTAAD TVARITQRFY EAEEYAEEFR
     TYLEGECLEL LRRYLENGKE TLQRADPPKA HVAHHPISDR EATLRCWALG FYPAEITLTW
     QRDGEEQTQD TELVETRPAG DGTFQKWAAV VVPSGEEQRY TCHVQHEGLP QPLTLRWESS
     SQPTIPIVGI VAGLAVLAVV VTGAVVAAVM WRRKSSDRNR GSYSQPTM
 
 
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