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Database: UniProt
Entry: H2ASD0_KAZAF
LinkDB: H2ASD0_KAZAF
Original site: H2ASD0_KAZAF 
ID   H2ASD0_KAZAF            Unreviewed;       202 AA.
AC   H2ASD0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=GOLD domain-containing protein {ECO:0000259|PROSITE:PS50866};
GN   Name=KAFR0C02870 {ECO:0000313|EMBL:CCF57280.1};
GN   ORFNames=KAFR_0C02870 {ECO:0000313|EMBL:CCF57280.1};
OS   Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS   1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF57280.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF57280.1, ECO:0000313|Proteomes:UP000005220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC   NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003827}; Single-
CC       pass type I membrane protein {ECO:0000256|RuleBase:RU003827}.
CC   -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC       {ECO:0000256|ARBA:ARBA00007104, ECO:0000256|RuleBase:RU003827}.
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DR   EMBL; HE650823; CCF57280.1; -; Genomic_DNA.
DR   RefSeq; XP_003956415.1; XM_003956366.1.
DR   AlphaFoldDB; H2ASD0; -.
DR   STRING; 1071382.H2ASD0; -.
DR   GeneID; 13885603; -.
DR   KEGG; kaf:KAFR_0C02870; -.
DR   eggNOG; KOG1692; Eukaryota.
DR   HOGENOM; CLU_066963_4_0_1; -.
DR   InParanoid; H2ASD0; -.
DR   OrthoDB; 601480at2759; -.
DR   Proteomes; UP000005220; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:GOC.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProt.
DR   InterPro; IPR015720; Emp24-like.
DR   InterPro; IPR009038; GOLD_dom.
DR   InterPro; IPR036598; GOLD_dom_sf.
DR   PANTHER; PTHR22811:SF50; RE49489P; 1.
DR   PANTHER; PTHR22811; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01105; EMP24_GP25L; 1.
DR   SMART; SM01190; EMP24_GP25L; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR   PROSITE; PS50866; GOLD; 1.
PE   3: Inferred from homology;
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003827};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022892}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..202
FT                   /note="GOLD domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003559630"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..119
FT                   /note="GOLD"
FT                   /evidence="ECO:0000259|PROSITE:PS50866"
SQ   SEQUENCE   202 AA;  23029 MW;  3C4478005CDF3981 CRC64;
     MRFSIIATFV VSTLLTSVAT AHNVLLPPYG RRCFFEELNQ NDELAITYQF GDRNPQSSSQ
     LSGDFVIYSV ERNEVIRTVS DASHGEVTVV VPYKGKYQYC FGNEKSGIDT KDVTFNIHGV
     VYIDEDDSKT LGGAIKKLSK LVREVKDEQS YIVIRERTHR NTAESTNDRV KWWSVFQVGV
     VVANSVFQIY YLKRFFEVTS LV
//
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