YOP1_SCHPO
ID YOP1_SCHPO Reviewed; 182 AA.
AC Q9UU91;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Protein yop1;
GN Name=yop1; ORFNames=SPCC830.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION, INTERACTION WITH RTN1 AND TTS1, AND FUNCTION.
RX PubMed=20434336; DOI=10.1016/j.cub.2010.04.017;
RA Zhang D., Vjestica A., Oliferenko S.;
RT "The cortical ER network limits the permissive zone for actomyosin ring
RT assembly.";
RL Curr. Biol. 20:1029-1034(2010).
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 (By similarity). Required for the
CC correct positioning of the cellular division plane by delimiting the
CC actomyosin ring assembly at the cell equator (PubMed:20434336).
CC {ECO:0000250|UniProtKB:Q12402, ECO:0000269|PubMed:20434336}.
CC -!- SUBUNIT: Oligomer (By similarity). Interacts with RTN1 and TTS1.
CC {ECO:0000250|UniProtKB:Q12402, ECO:0000269|PubMed:20434336}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20434336}. Nucleus membrane
CC {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20434336}. Note=Enriched at the cell equator during
CC mitosis.
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; CU329672; CAB52881.1; -; Genomic_DNA.
DR PIR; T41634; T41634.
DR RefSeq; NP_588478.1; NM_001023469.2.
DR AlphaFoldDB; Q9UU91; -.
DR BioGRID; 275742; 18.
DR STRING; 4896.SPCC830.08c.1; -.
DR SwissPalm; Q9UU91; -.
DR MaxQB; Q9UU91; -.
DR PaxDb; Q9UU91; -.
DR EnsemblFungi; SPCC830.08c.1; SPCC830.08c.1:pep; SPCC830.08c.
DR GeneID; 2539171; -.
DR KEGG; spo:SPCC830.08c; -.
DR PomBase; SPCC830.08c; yop1.
DR VEuPathDB; FungiDB:SPCC830.08c; -.
DR eggNOG; KOG1725; Eukaryota.
DR HOGENOM; CLU_028431_2_1_1; -.
DR InParanoid; Q9UU91; -.
DR OMA; FILVLWM; -.
DR PhylomeDB; Q9UU91; -.
DR PRO; PR:Q9UU91; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; IMP:PomBase.
DR InterPro; IPR004345; TB2_DP1_HVA22.
DR PANTHER; PTHR12300; PTHR12300; 1.
DR Pfam; PF03134; TB2_DP1_HVA22; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Endoplasmic reticulum; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..182
FT /note="Protein yop1"
FT /id="PRO_0000101856"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 35..54
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 55..56
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 57..75
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 76..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 86..102
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 103..105
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TRANSMEM 106..124
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
FT TOPO_DOM 125..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12402"
SQ SEQUENCE 182 AA; 20782 MW; 95E8782B86182225 CRC64;
MSFQVRVKQN MQDLDNRLAA FPQLNSLEKN FGVSKLYVFL TAAGIYALFL FLNWGGFLLT
NLLAFAMPAF FSINAIETTN KADDTQWLTY YLVTSFLNVI EYWSQLILYY VPVYWLLKAI
FLIWLALPKF NGATIIYRHL IRPYITPHVI RICKSVSRQN AAPAPTASSF AHTTATDIPP
SI
