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Database: UniProt
Entry: R9AF78_WALI9
LinkDB: R9AF78_WALI9
Original site: R9AF78_WALI9 
ID   R9AF78_WALI9            Unreviewed;       267 AA.
AC   R9AF78;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   03-MAY-2023, entry version 37.
DE   RecName: Full=ER membrane protein complex subunit 3 {ECO:0000256|ARBA:ARBA00020822, ECO:0000256|PIRNR:PIRNR010045};
GN   ORFNames=J056_000632 {ECO:0000313|EMBL:EOR00822.1};
OS   Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR00822.1, ECO:0000313|Proteomes:UP000014064};
RN   [1] {ECO:0000313|Proteomes:UP000014064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX   PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA   Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT   "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT   ichthyophaga: haloadaptations present and absent.";
RL   BMC Genomics 14:617-617(2013).
CC   -!- FUNCTION: The EMC seems to be required for efficient folding of
CC       proteins in the endoplasmic reticulum (ER).
CC       {ECO:0000256|PIRNR:PIRNR010045}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the EMC3 family. {ECO:0000256|ARBA:ARBA00005376,
CC       ECO:0000256|PIRNR:PIRNR010045}.
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DR   EMBL; KE007233; EOR00822.1; -; Genomic_DNA.
DR   RefSeq; XP_009268535.1; XM_009270260.1.
DR   AlphaFoldDB; R9AF78; -.
DR   STRING; 1299270.R9AF78; -.
DR   GeneID; 20373584; -.
DR   KEGG; wic:J056_000632; -.
DR   eggNOG; KOG3188; Eukaryota.
DR   HOGENOM; CLU_060791_0_0_1; -.
DR   OMA; KDMDPRW; -.
DR   OrthoDB; 167603at2759; -.
DR   Proteomes; UP000014064; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008568; EMC3.
DR   InterPro; IPR002809; EMC3/TMCO1.
DR   PANTHER; PTHR13116:SF5; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 3; 1.
DR   PANTHER; PTHR13116; UNCHARACTERIZED; 1.
DR   Pfam; PF01956; EMC3_TMCO1; 1.
DR   PIRSF; PIRSF010045; DUF850_TM_euk; 1.
DR   SMART; SM01415; DUF106; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          97..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   267 AA;  30201 MW;  47D9547268AB1FFE CRC64;
     MALTLNTPSL YIDDQIRDWV LFPITLVMIL VGLLRHYVVQ LLGGKGKKQE VKGIREQRAL
     MRSAMLRKNG GVLTPTAFFK RKQFLIEAFK QGSYLKQAPP KDGEQQHPPN PLNDPEQMDS
     MMDGMKKQMV MFIPQTVIMG WINSFFSGFI LIKLPFPLTR GFKSMLQRGI MTDDMPASYV
     SSISWYFLNL FGLNSVLRLI LGEGNHADGV RDMQTAAQLA GTSSQPNPMQ NQDMNKVFKA
     EIDNLELCEP KFMMSGVGNR VLEKYNG
//
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