YOP1_KLULA
ID YOP1_KLULA Reviewed; 180 AA.
AC Q6CP93;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protein YOP1;
GN Name=YOP1; OrderedLocusNames=KLLA0E06578g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382125; CAG99333.1; -; Genomic_DNA.
DR RefSeq; XP_454246.1; XM_454246.1.
DR AlphaFoldDB; Q6CP93; -.
DR STRING; 28985.XP_454246.1; -.
DR PRIDE; Q6CP93; -.
DR EnsemblFungi; CAG99333; CAG99333; KLLA0_E06601g.
DR GeneID; 2893873; -.
DR KEGG; kla:KLLA0_E06601g; -.
DR eggNOG; KOG1725; Eukaryota.
DR HOGENOM; CLU_028431_2_1_1; -.
DR InParanoid; Q6CP93; -.
DR OMA; FILVLWM; -.
DR Proteomes; UP000000598; Chromosome E.
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..180
FT /note="Protein YOP1"
FT /id="PRO_0000101853"
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..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
SQ SEQUENCE 180 AA; 20257 MW; B93119CE1EB6E966 CRC64;
MADYLKLFQD SLKGLDTKFA GNQILSRIEA QTKLPRSYVI VGLVAVYFLL IFINVGGIGE
ILSNFVGFCI PTYYSLKALK TATSTDDTQL LTYWIVFSFL SVIEFWSKAI LYWVPFYWFF
KTVFLLYIAI PSFGGAQLVY TRLISPFSDK YLPIVEGKSG ELAQKVEAAA NNAKASGYSR
