ID   YN8S_YEAST              Reviewed;         393 AA.
AC   P53740; D6W1M3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 168.
DE   RecName: Full=Phospholipid-transporting ATPase accessory subunit CRF1 {ECO:0000303|PubMed:17093059};
DE   AltName: Full=CDC50/ROS3 family protein 1 {ECO:0000303|PubMed:15090616};
DE            Short=CRF1;
GN   OrderedLocusNames=YNR048W {ECO:0000312|SGD:S000005331};
GN   ORFNames=N3453;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION.
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   [5]
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).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNF3.
RX   PubMed=17093059; DOI=10.1091/mbc.e06-05-0461;
RA   Furuta N., Fujimura-Kamada K., Saito K., Yamamoto T., Tanaka K.;
RT   "Endocytic recycling in yeast is regulated by putative phospholipid
RT   translocases and the Ypt31p/32p-Rcy1p pathway.";
RL   Mol. Biol. Cell 18:295-312(2007).
RN   [7]
RP   INTERACTION WITH DNF3.
RX   PubMed=19411703; DOI=10.1074/jbc.m109.013722;
RA   Lenoir G., Williamson P., Puts C.F., Holthuis J.C.;
RT   "Cdc50p plays a vital role in the ATPase reaction cycle of the putative
RT   aminophospholipid transporter Drs2p.";
RL   J. Biol. Chem. 284:17956-17967(2009).
RN   [8]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH DNF3, INTERACTION WITH DNF3,
RP   DISULFIDE BOND, AND MUTAGENESIS OF CYS-82 AND CYS-126.
RX   PubMed=22791719; DOI=10.1074/jbc.m112.371088;
RA   Puts C.F., Panatala R., Hennrich H., Tsareva A., Williamson P.,
RA   Holthuis J.C.;
RT   "Mapping functional interactions in a heterodimeric phospholipid pump.";
RL   J. Biol. Chem. 287:30529-30540(2012).
CC   -!- FUNCTION: Accessory component of a P4-ATPase flippase complex which
CC       catalyzes the hydrolysis of ATP coupled to the transport of
CC       phosphatidylcholine and small amounts of phosphatidylethanolamine from
CC       the lumen to the cytosolic leaflet of the trans-Golgi network and
CC       ensures the maintenance of asymmetric distribution of phospholipids
CC       (PubMed:22791719). May be involved in transport from early endosomes to
CC       the trans-Golgi network (TGN) (Probable). {ECO:0000269|PubMed:22791719,
CC       ECO:0000305|PubMed:15090616, ECO:0000305|PubMed:17093059}.
CC   -!- SUBUNIT: Component of a flippase complex consisting of DNF3 and
CC       YNR048W/CRF1 (PubMed:22791719). Interacts with DNF3; the interaction is
CC       direct and required for proper expression and endoplasmic reticulum
CC       (ER) export of either partner (PubMed:17093059, PubMed:19411703,
CC       PubMed:22791719). {ECO:0000269|PubMed:17093059,
CC       ECO:0000269|PubMed:19411703, ECO:0000269|PubMed:22791719}.
CC   -!- INTERACTION:
CC       P53740; Q12674: DNF3; NbExp=4; IntAct=EBI-28524, EBI-3142;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000269|PubMed:17093059}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- MISCELLANEOUS: Present with 4510 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; Z71663; CAA96329.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10589.1; -; Genomic_DNA.
DR   PIR; S63379; S63379.
DR   RefSeq; NP_014446.3; NM_001183225.3.
DR   AlphaFoldDB; P53740; -.
DR   SMR; P53740; -.
DR   BioGRID; 35873; 57.
DR   ComplexPortal; CPX-1026; DNF3-CRF1 P4-ATPase complex.
DR   DIP; DIP-1250N; -.
DR   FunCoup; P53740; 561.
DR   IntAct; P53740; 5.
DR   MINT; P53740; -.
DR   STRING; 4932.YNR048W; -.
DR   TCDB; 8.A.27.1.7; the cdc50 p-type atpase lipid flippase subunit (cdc50) family.
DR   GlyGen; P53740; 7 sites.
DR   PaxDb; 4932-YNR048W; -.
DR   PeptideAtlas; P53740; -.
DR   EnsemblFungi; YNR048W_mRNA; YNR048W; YNR048W.
DR   GeneID; 855784; -.
DR   KEGG; sce:YNR048W; -.
DR   AGR; SGD:S000005331; -.
DR   SGD; S000005331; YNR048W.
DR   VEuPathDB; FungiDB:YNR048W; -.
DR   eggNOG; KOG2952; Eukaryota.
DR   HOGENOM; CLU_025025_0_1_1; -.
DR   InParanoid; P53740; -.
DR   OMA; IPWSMFN; -.
DR   OrthoDB; 340608at2759; -.
DR   BioCyc; YEAST:G3O-33355-MONOMER; -.
DR   BioGRID-ORCS; 855784; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P53740; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53740; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005802; C:trans-Golgi network; IPI:SGD.
DR   GO; GO:0015247; F:aminophospholipid flippase activity; IBA:GO_Central.
DR   GO; GO:0045332; P:phospholipid translocation; IGI:SGD.
DR   InterPro; IPR005045; CDC50/LEM3_fam.
DR   PANTHER; PTHR10926:SF0; CDC50, ISOFORM A; 1.
DR   PANTHER; PTHR10926; CELL CYCLE CONTROL PROTEIN 50; 1.
DR   Pfam; PF03381; CDC50; 1.
DR   PIRSF; PIRSF015840; DUF284_TM_euk; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..393
FT                   /note="Phospholipid-transporting ATPase accessory subunit
FT                   CRF1"
FT                   /id="PRO_0000207672"
FT   TOPO_DOM        1..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..334
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        356..393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:16847258"
FT   REGION          70..332
FT                   /note="Confers specificity for binding DNF3"
FT                   /evidence="ECO:0000269|PubMed:22791719"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..126
FT                   /evidence="ECO:0000305|PubMed:22791719"
FT   DISULFID        179..193
FT                   /evidence="ECO:0000250|UniProtKB:P25656"
FT   MUTAGEN         82
FT                   /note="C->A: Reduces interaction with DNF3."
FT                   /evidence="ECO:0000269|PubMed:22791719"
FT   MUTAGEN         126
FT                   /note="C->A: Reduces interaction with DNF3."
FT                   /evidence="ECO:0000269|PubMed:22791719"
SQ   SEQUENCE   393 AA;  44542 MW;  9BCA199AA3D23969 CRC64;
     MGLILRWKEK KQLSSKQNAQ KSRKPANTSF RQQRLKAWQP ILSPQSVLPL LILMACVFAP
     IGIGLVVSTI SVQRLVVNYT ECDALAPAKH FETIPSEYVD YHFSKKVAVQ PQWMVLTDPE
     LGNQTCRIQF EVPNHIKKST YVYYRLTNFN QNYREYVQSL DLDQLKGKAL IGNDLDPNCD
     PLRTVENKTI FPCGLIANSM FNDTFGTTLT GVNDTADYLL TTKGIAWDTD SHRYGKTEYN
     ASDIVPPPNW AKLFPNGYTD DNIPDLQNWE QFKIWMRTAA LPNFYKLAMK NETNGLGKGI
     YIADIELNYP VRSFYGTKSF VLTTNSIIGA GNEALGIVYL IVAGIATLFA ILFLIKVIFK
     PRPMHDHSYL NFENSDTPFD ESSVVSIPLR EIL
//