ID C5MFK2_CANTT Unreviewed; 304 AA.
AC C5MFK2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=ER membrane protein complex subunit 3 {ECO:0000256|ARBA:ARBA00020822, ECO:0000256|PIRNR:PIRNR010045};
GN ORFNames=CTRG_04845 {ECO:0000313|EMBL:EER31115.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER31115.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER31115.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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: Endoplasmic reticulum membrane
CC {ECO:0000256|PIRNR:PIRNR010045}; Multi-pass membrane protein
CC {ECO:0000256|PIRNR:PIRNR010045}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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; GG692401; EER31115.1; -; Genomic_DNA.
DR RefSeq; XP_002550547.1; XM_002550501.1.
DR AlphaFoldDB; C5MFK2; -.
DR STRING; 294747.C5MFK2; -.
DR EnsemblFungi; CTRG_04845-t43_1; CTRG_04845-t43_1-p1; CTRG_04845.
DR GeneID; 8296557; -.
DR KEGG; ctp:CTRG_04845; -.
DR VEuPathDB; FungiDB:CTRG_04845; -.
DR eggNOG; KOG3188; Eukaryota.
DR HOGENOM; CLU_060791_0_0_1; -.
DR OrthoDB; 167603at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0072546; C:EMC complex; IEA:EnsemblFungi.
DR GO; GO:0032977; F:membrane insertase activity; IEA:EnsemblFungi.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:EnsemblFungi.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:EnsemblFungi.
DR GO; GO:0015914; P:phospholipid transport; IEA:EnsemblFungi.
DR GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; IEA:EnsemblFungi.
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|PIRNR:PIRNR010045};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR010045};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR010045}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR010045"
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR010045"
FT TRANSMEM 173..197
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR010045"
SQ SEQUENCE 304 AA; 34697 MW; 30C7A44795DA1C0E CRC64;
MLFIKLIISH VLLILFFFFL VVDFQDLFFF KQRKFSTTKQ PSNQQRTMIT PDLLLDPQLK
YWVLLPISVA MVLVGLLRSN ATFLLQTQPK LEAYKTVREG QFLHRARCFR ENNSVLNDSD
FEIRKKYFID KLNSDEFIAK KPAANGAEDP MAALNPGSNE ALMQMAKGNL MSYIPQTVIM
AWVNYFFAGF VVMKLPFPLT DGFKNMLQSG VNTPDLNVRY VSSISWYFVN LFGLKPIYSL
LMGSDEAAEL MQQQGQQQPQ MPNLGGPGAP QADKVFKGEA ENIQILSHKS VFDGVVDRFI
ERYS
//
