YOP1_YARLI
ID YOP1_YARLI Reviewed; 189 AA.
AC Q6CE07;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein YOP1;
GN Name=YOP1; OrderedLocusNames=YALI0B19668g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382128; CAG83358.2; -; Genomic_DNA.
DR RefSeq; XP_501105.2; XM_501105.2.
DR AlphaFoldDB; Q6CE07; -.
DR STRING; 4952.CAG83358; -.
DR EnsemblFungi; CAG83358; CAG83358; YALI0_B19668g.
DR GeneID; 2907149; -.
DR KEGG; yli:YALI0B19668g; -.
DR VEuPathDB; FungiDB:YALI0_B19668g; -.
DR HOGENOM; CLU_028431_2_1_1; -.
DR InParanoid; Q6CE07; -.
DR OMA; WIPFYFF; -.
DR Proteomes; UP000001300; Chromosome B.
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..189
FT /note="Protein YOP1"
FT /id="PRO_0000101858"
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..105
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 106..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..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
SQ SEQUENCE 189 AA; 20958 MW; B546FC578E26786C CRC64;
MSQIIDQVQA ALQNIDKELE KYPALKELEK QIPVPKSYIL LGFVGFYFIL IFLNIGGIGQ
LLSNIAGLVI PGYYSLLALE TPGKADDTQY LTYWVVFATL NVFEFWSKAI LYWVPFYYLF
KTAFLLYIGL PQYGGAELVY KAIVKPLAQK LVNIQPHGGP SDSLKAQAQS AVDAAESHVP
QGHSTGVSH
