YOP1_CANGA
ID YOP1_CANGA Reviewed; 177 AA.
AC Q6FMU3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Protein YOP1;
GN Name=YOP1; OrderedLocusNames=CAGL0K05203g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Required to generate and maintain the structure of the
CC tubular endoplasmic reticulum network and the vacuole. Induces high
CC curvature in membranes and causes membrane tubule formation. Involved
CC in membrane/vesicle trafficking. {ECO:0000250|UniProtKB:Q12402}.
CC -!- SUBUNIT: Oligomer. {ECO:0000250|UniProtKB:Q12402}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q12402}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12402}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q12402}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The short lumenal loops between transmembrane domains 1 and 2
CC and between transmembrane domains 3 and 4 may impart a wedge-like
CC configuration, thus deforming membranes.
CC {ECO:0000250|UniProtKB:Q12402}.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
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DR EMBL; CR380957; CAG61412.1; -; Genomic_DNA.
DR RefSeq; XP_448451.1; XM_448451.1.
DR AlphaFoldDB; Q6FMU3; -.
DR STRING; 5478.XP_448451.1; -.
DR EnsemblFungi; CAG61412; CAG61412; CAGL0K05203g.
DR GeneID; 2890509; -.
DR KEGG; cgr:CAGL0K05203g; -.
DR CGD; CAL0133823; CAGL0K05203g.
DR VEuPathDB; FungiDB:CAGL0K05203g; -.
DR eggNOG; KOG1725; Eukaryota.
DR HOGENOM; CLU_028431_2_1_1; -.
DR InParanoid; Q6FMU3; -.
DR OMA; FILVLWM; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IEA:EnsemblFungi.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; IEA:EnsemblFungi.
DR GO; GO:0032581; P:ER-dependent peroxisome organization; IEA:EnsemblFungi.
DR GO; GO:0051292; P:nuclear pore complex assembly; IEA:EnsemblFungi.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:EnsemblFungi.
DR GO; GO:0007033; P:vacuole organization; IEA:EnsemblFungi.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:EnsemblFungi.
DR InterPro; IPR004345; TB2_DP1_HVA22.
DR PANTHER; PTHR12300; PTHR12300; 1.
DR Pfam; PF03134; TB2_DP1_HVA22; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..177
FT /note="Protein YOP1"
FT /id="PRO_0000101849"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 56..57
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 79..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 89..103
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 104..108
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 128..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
SQ SEQUENCE 177 AA; 19867 MW; B2EBAA326935F2EB CRC64;
MADVISSLQT QLKELDTKFA GNNVLNQLEQ RTNLPKSYLV VGSTIFYLLL IFINVGGIGE
ILGNFAGFVI PAYYSILALK TTTTKDDTQL LTYWIVFSFL NVIEFWSKAL LYIIPFYWFL
KTIFLLYIAL PQTGGATMIY NRFISPLTDK YILGPKKTDG VQQSVKEASR ATGAATH
