CDC50_YEAST
ID CDC50_YEAST Reviewed; 391 AA.
AC P25656; D6VR94;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cell division control protein 50;
GN Name=CDC50; OrderedLocusNames=YCR094W; ORFNames=YCR94W;
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].
RX PubMed=11180453;
RX DOI=10.1002/1097-0061(200102)18:3<195::aid-yea660>3.0.co;2-l;
RA Radji M., Kim J.-M., Togan T., Yoshikawa H., Shirahige K.;
RT "The cloning and characterization of the CDC50 gene family in Saccharomyces
RT cerevisiae.";
RL Yeast 18:195-205(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 SUBCELLULAR LOCATION.
RX PubMed=12589066; DOI=10.1091/mbc.e02-06-0314;
RA Misu K., Fujimura-Kamada K., Ueda T., Nakano A., Katoh H., Tanaka K.;
RT "Cdc50p, a conserved endosomal membrane protein, controls polarized growth
RT in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:730-747(2003).
RN [5]
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 [6]
RP INTERACTION WITH DRS2.
RX PubMed=15090616; DOI=10.1091/mbc.e03-11-0829;
RA Saito K., Fujimura-Kamada K., Furuta N., Kato U., Umeda M., Tanaka K.;
RT "Cdc50p, a protein required for polarized growth, associates with the Drs2p
RT P-type ATPase implicated in phospholipid translocation in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 15:3418-3432(2004).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Required for polarized cell growth.
CC -!- SUBUNIT: Interacts with DRS2. Might function as an essential subunit
CC for this protein. {ECO:0000269|PubMed:15090616}.
CC -!- INTERACTION:
CC P25656; P39524: DRS2; NbExp=10; IntAct=EBI-22014, EBI-3106;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:12589066}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12589066}.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR EMBL; X59720; CAA42249.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07563.1; -; Genomic_DNA.
DR PIR; S19510; S19510.
DR RefSeq; NP_010018.1; NM_001178800.1.
DR PDB; 6PSX; EM; 3.30 A; E=1-391.
DR PDB; 6PSY; EM; 2.80 A; E=1-391.
DR PDB; 6ROH; EM; 2.80 A; C=1-391.
DR PDB; 6ROI; EM; 3.70 A; C=1-391.
DR PDB; 6ROJ; EM; 2.90 A; C=1-391.
DR PDB; 7OH4; EM; 3.00 A; C=1-391.
DR PDB; 7OH5; EM; 2.90 A; C=1-391.
DR PDB; 7OH6; EM; 3.00 A; C=1-391.
DR PDB; 7OH7; EM; 3.80 A; C=1-391.
DR PDBsum; 6PSX; -.
DR PDBsum; 6PSY; -.
DR PDBsum; 6ROH; -.
DR PDBsum; 6ROI; -.
DR PDBsum; 6ROJ; -.
DR PDBsum; 7OH4; -.
DR PDBsum; 7OH5; -.
DR PDBsum; 7OH6; -.
DR PDBsum; 7OH7; -.
DR AlphaFoldDB; P25656; -.
DR SMR; P25656; -.
DR BioGRID; 31066; 434.
DR ComplexPortal; CPX-1018; DRS2-CDC50 P4-ATPase complex.
DR DIP; DIP-5138N; -.
DR IntAct; P25656; 7.
DR MINT; P25656; -.
DR STRING; 4932.YCR094W; -.
DR TCDB; 8.A.27.1.2; the cdc50 p-type atpase lipid flippase subunit (cdc50) family.
DR MaxQB; P25656; -.
DR PaxDb; P25656; -.
DR PRIDE; P25656; -.
DR EnsemblFungi; YCR094W_mRNA; YCR094W; YCR094W.
DR GeneID; 850456; -.
DR KEGG; sce:YCR094W; -.
DR SGD; S000000690; CDC50.
DR VEuPathDB; FungiDB:YCR094W; -.
DR eggNOG; KOG2952; Eukaryota.
DR GeneTree; ENSGT00390000004660; -.
DR HOGENOM; CLU_025025_0_1_1; -.
DR InParanoid; P25656; -.
DR OMA; TWNNDQP; -.
DR BioCyc; YEAST:G3O-29388-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P25656; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25656; protein.
DR GO; GO:1990530; C:Cdc50p-Drs2p complex; IPI:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IDA:SGD.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0051666; P:actin cortical patch localization; IGI:SGD.
DR GO; GO:0140331; P:aminophospholipid translocation; IEA:GOC.
DR GO; GO:0006897; P:endocytosis; IGI:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IMP:SGD.
DR GO; GO:0045332; P:phospholipid translocation; IGI:SGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
DR InterPro; IPR005045; CDC50/LEM3_fam.
DR PANTHER; PTHR10926; PTHR10926; 1.
DR Pfam; PF03381; CDC50; 1.
DR PIRSF; PIRSF015840; DUF284_TM_euk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endosome; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..391
FT /note="Cell division control protein 50"
FT /id="PRO_0000207670"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..331
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT TURN 27..31
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 45..65
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6PSX"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6ROH"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:6ROH"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:7OH4"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6ROJ"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 277..288
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 331..356
FT /evidence="ECO:0007829|PDB:6PSY"
SQ SEQUENCE 391 AA; 44982 MW; 565575CA402C0C91 CRC64;
MVSLFKRGKA PPLTKEGPTS KKPPNTAFRQ QRLKAWQPIL SPQSVLPLLI FVACIFTPIG
IGLIVSATKV QDLTIDYSHC DTKASTTAFE DIPKKYIKYH FKSKVENKPQ WRLTENENGE
QSCELQFEIP NDIKKSIFIY YKITNFYQNH RRYVQSFDTK QILGEPIKKD DLDTSCSPIR
SREDKIIYPC GLIANSMFND TFSQVLSGID DTEDYNLTNK HISWSIDRHR FKTTKYNASD
IVPPPNWMKK YPDGYTDENL PDIHTWEEFQ VWMRTAAFPK FYKLTLKNES ASLPKGKYQM
NIELNYPISL FGGTKSFVLT TNGAIGGRNM SLGVLYLIVA GLCALFGIIF LVKLIFQPRA
MGDHTYLNFD DEENEDYEDV HAENTTLREI L
