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Database: UniProt
Entry: A0A1V9ZFD1_9STRA
LinkDB: A0A1V9ZFD1_9STRA
Original site: A0A1V9ZFD1_9STRA 
ID   A0A1V9ZFD1_9STRA        Unreviewed;       214 AA.
AC   A0A1V9ZFD1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=GOLD domain-containing protein {ECO:0000259|PROSITE:PS50866};
GN   ORFNames=ACHHYP_14627 {ECO:0000313|EMBL:OQR96601.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR96601.1, ECO:0000313|Proteomes:UP000243579};
RN   [1] {ECO:0000313|EMBL:OQR96601.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR96601.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU003827}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003827}.
CC   -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC       {ECO:0000256|ARBA:ARBA00007104, ECO:0000256|RuleBase:RU003827}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQR96601.1}.
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DR   EMBL; JNBR01000138; OQR96601.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9ZFD1; -.
DR   STRING; 1202772.A0A1V9ZFD1; -.
DR   OrthoDB; 886406at2759; -.
DR   Proteomes; UP000243579; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR015720; Emp24-like.
DR   InterPro; IPR009038; GOLD_dom.
DR   PANTHER; PTHR22811; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22811:SF159; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN 4; 1.
DR   Pfam; PF01105; EMP24_GP25L; 1.
DR   SMART; SM01190; EMP24_GP25L; 1.
DR   PROSITE; PS50866; GOLD; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243579};
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}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..214
FT                   /note="GOLD domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012912831"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..147
FT                   /note="GOLD"
FT                   /evidence="ECO:0000259|PROSITE:PS50866"
FT   COILED          133..160
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   214 AA;  24339 MW;  3D06BF6D73575B38 CRC64;
     MFRPLLVVVA AVAGTASGLR FFVTPEEHRC FFLDIPDATT FRAEYESPDT TDLLKSEIKI
     YGPSTSGDDE PNQVPSVTHT LGDKGSITYT STLAGGHWTC VSIDTNKYVV PSTTKMRFLL
     KLKFGTSNEE YANLAKREQM NELELEVMKL RDRVRAIQKQ QDYAQEKDEK FRSTSESNNS
     RAMWVSVIQI VILVITGVWQ VHHLQTYFHK KKLV
//
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