YOP1_ASHGO
ID YOP1_ASHGO Reviewed; 188 AA.
AC Q75A56;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Protein YOP1;
GN Name=YOP1; OrderedLocusNames=ADR063W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 19.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS51983.2; -; Genomic_DNA.
DR RefSeq; NP_984159.2; NM_209512.2.
DR AlphaFoldDB; Q75A56; -.
DR STRING; 33169.AAS51983; -.
DR PRIDE; Q75A56; -.
DR EnsemblFungi; AAS51983; AAS51983; AGOS_ADR063W.
DR GeneID; 4620376; -.
DR KEGG; ago:AGOS_ADR063W; -.
DR eggNOG; KOG1725; Eukaryota.
DR HOGENOM; CLU_028431_2_1_1; -.
DR InParanoid; Q75A56; -.
DR OMA; FILVLWM; -.
DR Proteomes; UP000000591; Chromosome IV.
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..188
FT /note="Protein YOP1"
FT /id="PRO_0000101847"
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..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT REGION 163..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 188 AA; 20793 MW; 762E0B261ABA65A1 CRC64;
MAEIAGNLQR ILQSLDRQFA GNKYLQEFER KTGFPKSYAI AGAGVAYLFI IFINVGGVGE
ILSNFLGFVL PCYYSLHAIK TTTTADDTEL LTYWIVFAFF SVIEFWSKAI LYWVPFYWFF
KTIFLIFIAL PQLGGASLIY HRVIAPLTDP YIAAGSQRKA SGISSKMEQA AKGASARATG
AASHQSSD
