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
//