YN8S_YEAST
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 03-AUG-2022, entry version 153.
DE RecName: Full=Probable phospholipid translocase non-catalytic 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}; 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;
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).
CC -!- FUNCTION: Potential non-catalytic subunit for a heteromeric
CC phospholipid translocase (PLT) CRF1-DNF3, implicated in the
CC translocation of phospholipids from the outer to the inner leaflet of
CC membrane bilayers. Shares an essential function for cell growth with
CC PLTs CDC50-DRS2 and LEM3-DNF1/2. May be involved in transport from
CC early endosomes to the trans-Golgi network (TGN).
CC {ECO:0000305|PubMed:15090616, ECO:0000305|PubMed:17093059}.
CC -!- SUBUNIT: Interacts with DNF3; interaction is required for proper
CC expression and endoplasmic reticulum (ER) export of either partner.
CC {ECO:0000269|PubMed:17093059, ECO:0000269|PubMed:19411703}.
CC -!- INTERACTION:
CC P53740; Q12674: DNF3; NbExp=3; 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; 54.
DR ComplexPortal; CPX-1026; DNF3-CRF1 P4-ATPase complex.
DR DIP; DIP-1250N; -.
DR IntAct; P53740; 3.
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 MaxQB; P53740; -.
DR PaxDb; P53740; -.
DR PRIDE; P53740; -.
DR EnsemblFungi; YNR048W_mRNA; YNR048W; YNR048W.
DR GeneID; 855784; -.
DR KEGG; sce:YNR048W; -.
DR SGD; S000005331; YNR048W.
DR VEuPathDB; FungiDB:YNR048W; -.
DR eggNOG; KOG2952; Eukaryota.
DR GeneTree; ENSGT00390000004660; -.
DR HOGENOM; CLU_025025_0_1_1; -.
DR InParanoid; P53740; -.
DR OMA; AWQPMLS; -.
DR BioCyc; YEAST:G3O-33355-MON; -.
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:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0045332; P:phospholipid translocation; IGI: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 Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..393
FT /note="Probable phospholipid translocase non-catalytic
FT subunit 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 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"
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
