YOP1_YEAST
ID YOP1_YEAST Reviewed; 180 AA.
AC Q12402; D6W438;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein YOP1;
DE AltName: Full=YIP1 partner protein 1;
DE AltName: Full=YPT-interacting protein 2;
GN Name=YOP1; Synonyms=YIP2; OrderedLocusNames=YPR028W; ORFNames=YP9367.08;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Matern H.T., Gallwitz D.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 2-13; 24-31 AND 143-150, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [5]
RP INTERACTION WITH YIP1, AND SUBCELLULAR LOCATION.
RX PubMed=11278413; DOI=10.1074/jbc.m008439200;
RA Calero M., Whittaker G.R., Collins R.N.;
RT "Yop1p, the yeast homolog of the polyposis locus protein 1, interacts with
RT Yip1p and negatively regulates cell growth.";
RL J. Biol. Chem. 276:12100-12112(2001).
RN [6]
RP FUNCTION.
RX PubMed=12427979; DOI=10.1104/pp.007716;
RA Brands A., Ho T.-H.D.;
RT "Function of a plant stress-induced gene, HVA22. Synthetic enhancement
RT screen with its yeast homolog reveals its role in vesicular traffic.";
RL Plant Physiol. 130:1121-1131(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18442980; DOI=10.1074/jbc.m800986200;
RA Shibata Y., Voss C., Rist J.M., Hu J., Rapoport T.A., Prinz W.A.,
RA Voeltz G.K.;
RT "The reticulon and DP1/Yop1p proteins form immobile oligomers in the
RT tubular endoplasmic reticulum.";
RL J. Biol. Chem. 283:18892-18904(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP FUNCTION, AND TOPOLOGY.
RX PubMed=25646439; DOI=10.1073/pnas.1415882112;
RA Brady J.P., Claridge J.K., Smith P.G., Schnell J.R.;
RT "A conserved amphipathic helix is required for membrane tubule formation by
RT Yop1p.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E639-E648(2015).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32432369; DOI=10.1111/mmi.14526;
RA Shi X., Hai L., Govindasamy K., Gao J., Coppens I., Hu J., Wang Q.,
RA Bhanot P.;
RT "A Plasmodium homolog of ER tubule-forming proteins is required for
RT parasite virulence.";
RL Mol. Microbiol. 114:454-467(2020).
CC -!- FUNCTION: Required to generate and maintain the structure of the
CC tubular endoplasmic reticulum network and the vacuole (PubMed:25646439,
CC PubMed:32432369). Induces high curvature in membranes and causes
CC membrane tubule formation (Probable). Involved in membrane/vesicle
CC trafficking (PubMed:12427979). {ECO:0000269|PubMed:12427979,
CC ECO:0000269|PubMed:25646439, ECO:0000269|PubMed:32432369,
CC ECO:0000305|PubMed:25646439}.
CC -!- SUBUNIT: Oligomer (PubMed:18442980). Interacts with YIP1
CC (PubMed:11278413). {ECO:0000269|PubMed:11278413,
CC ECO:0000269|PubMed:18442980}.
CC -!- INTERACTION:
CC Q12402; Q99287: SEY1; NbExp=2; IntAct=EBI-37092, EBI-37523;
CC Q12402; P03588: ORF1a; Xeno; NbExp=4; IntAct=EBI-37092, EBI-15874242;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11278413, ECO:0000269|PubMed:18442980}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:25646439}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:11278413}; 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. {ECO:0000305|PubMed:25646439}.
CC -!- DISRUPTION PHENOTYPE: Cells have more than three vacuoles with a grape-
CC like assembly. {ECO:0000269|PubMed:32432369}.
CC -!- MISCELLANEOUS: Present with 1759 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
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DR EMBL; AJ007902; CAA07720.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95024.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89282.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11454.1; -; Genomic_DNA.
DR PIR; S54502; S54502.
DR RefSeq; NP_015353.1; NM_001184125.1.
DR AlphaFoldDB; Q12402; -.
DR BioGRID; 36206; 119.
DR DIP; DIP-3914N; -.
DR IntAct; Q12402; 9.
DR MINT; Q12402; -.
DR STRING; 4932.YPR028W; -.
DR TCDB; 8.A.108.1.1; the curvature-stabilizing protein yop1 (yop1) family.
DR iPTMnet; Q12402; -.
DR MaxQB; Q12402; -.
DR PaxDb; Q12402; -.
DR PRIDE; Q12402; -.
DR TopDownProteomics; Q12402; -.
DR DNASU; 856140; -.
DR EnsemblFungi; YPR028W_mRNA; YPR028W; YPR028W.
DR GeneID; 856140; -.
DR KEGG; sce:YPR028W; -.
DR SGD; S000006232; YOP1.
DR VEuPathDB; FungiDB:YPR028W; -.
DR eggNOG; KOG1725; Eukaryota.
DR GeneTree; ENSGT00940000176263; -.
DR HOGENOM; CLU_028431_2_1_1; -.
DR InParanoid; Q12402; -.
DR OMA; WIPFYFF; -.
DR BioCyc; YEAST:G3O-34187-MON; -.
DR PRO; PR:Q12402; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12402; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IGI:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IGI:SGD.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR GO; GO:0032581; P:ER-dependent peroxisome organization; IGI:SGD.
DR GO; GO:0051292; P:nuclear pore complex assembly; IGI:SGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IGI:SGD.
DR GO; GO:0007033; P:vacuole organization; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
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 Acetylation; Direct protein sequencing; Endoplasmic reticulum;
KW Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:22814378"
FT CHAIN 2..180
FT /note="Protein YOP1"
FT /id="PRO_0000101859"
FT TOPO_DOM 2..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25646439"
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25646439"
FT TOPO_DOM 56..57
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:25646439"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25646439"
FT TOPO_DOM 79..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25646439"
FT TRANSMEM 89..105
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25646439"
FT TOPO_DOM 106..108
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:25646439"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25646439"
FT TOPO_DOM 128..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25646439"
FT REGION 2..17
FT /note="Interaction with YIP1"
FT /evidence="ECO:0000269|PubMed:11278413"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:22814378"
SQ SEQUENCE 180 AA; 20270 MW; 6F1073444B653CCF CRC64;
MSEYASSIHS QMKQFDTKYS GNRILQQLEN KTNLPKSYLV AGLGFAYLLL IFINVGGVGE
ILSNFAGFVL PAYLSLVALK TPTSTDDTQL LTYWIVFSFL SVIEFWSKAI LYLIPFYWFL
KTVFLIYIAL PQTGGARMIY QKIVAPLTDR YILRDVSKTE KDEIRASVNE ASKATGASVH
