ANY1_YEAST
ID ANY1_YEAST Reviewed; 405 AA.
AC Q03687; D6VZI4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Scramblase ANY1 {ECO:0000303|PubMed:27811238};
DE AltName: Full=Antagonizes NEO1 phospholipid flippase protein 1 {ECO:0000303|PubMed:27811238};
DE AltName: Full=CDC50 suppressor 1 {ECO:0000303|PubMed:28057802};
GN Name=ANY1 {ECO:0000303|PubMed:27811238};
GN Synonyms=CFS1 {ECO:0000303|PubMed:28057802}; OrderedLocusNames=YMR010W;
GN ORFNames=YM8270.13;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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 [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, TOPOLOGY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLY-80; ASP-84 AND 258-SER--LEU-405.
RX PubMed=27811238; DOI=10.1126/science.aag0839;
RA van Leeuwen J., Pons C., Mellor J.C., Yamaguchi T.N., Friesen H.,
RA Koschwanez J., Usaj M.M., Pechlaner M., Takar M., Usaj M., VanderSluis B.,
RA Andrusiak K., Bansal P., Baryshnikova A., Boone C.E., Cao J., Cote A.,
RA Gebbia M., Horecka G., Horecka I., Kuzmin E., Legro N., Liang W.,
RA van Lieshout N., McNee M., San Luis B.J., Shaeri F., Shuteriqi E., Sun S.,
RA Yang L., Youn J.Y., Yuen M., Costanzo M., Gingras A.C., Aloy P.,
RA Oostenbrink C., Murray A., Graham T.R., Myers C.L., Andrews B.J.,
RA Roth F.P., Boone C.;
RT "Exploring genetic suppression interactions on a global scale.";
RL Science 354:0-0(2016).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=28057802; DOI=10.1534/g3.116.035238;
RA Yamamoto T., Fujimura-Kamada K., Shioji E., Suzuki R., Tanaka K.;
RT "Cfs1p, a Novel Membrane Protein in the PQ-Loop Family, Is Involved in
RT Phospholipid Flippase Functions in Yeast.";
RL G3 (Bethesda) 7:179-192(2017).
CC -!- FUNCTION: Phospholipid scramblase that transports phosphatidylserine
CC (PS) and phosphatidylethalonamine (PE) bidirectionally from one leaflet
CC to the other of the phospholipid bilayer to at least partially collapse
CC the membrane asymmetry established by NEO1 and other flippases
CC (PubMed:27811238, PubMed:28057802). Functions in the trafficking
CC pathway from endosomes to the trans-Golgi network (TGN)
CC (PubMed:28057802). {ECO:0000269|PubMed:27811238,
CC ECO:0000269|PubMed:28057802}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:27811238, ECO:0000269|PubMed:28057802}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:27811238}. Late endosome membrane
CC {ECO:0000269|PubMed:27811238, ECO:0000269|PubMed:28057802}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:27811238}.
CC -!- DISRUPTION PHENOTYPE: Suppresses the growth defects caused by mutations
CC of flippases including NEO1, DRS2, DNF1, DNF2 and DNF3, as well as of
CC the DRS2 regulator CDC50. {ECO:0000269|PubMed:27811238,
CC ECO:0000269|PubMed:28057802}.
CC -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z48613; CAA88526.1; -; Genomic_DNA.
DR EMBL; AY558117; AAS56443.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09908.1; -; Genomic_DNA.
DR PIR; S53040; S53040.
DR RefSeq; NP_013723.1; NM_001182506.1.
DR AlphaFoldDB; Q03687; -.
DR BioGRID; 35179; 133.
DR DIP; DIP-4512N; -.
DR IntAct; Q03687; 26.
DR MINT; Q03687; -.
DR STRING; 4932.YMR010W; -.
DR TCDB; 2.A.43.2.13; the lysosomal cystine transporter (lct) family.
DR iPTMnet; Q03687; -.
DR MaxQB; Q03687; -.
DR PaxDb; Q03687; -.
DR PRIDE; Q03687; -.
DR EnsemblFungi; YMR010W_mRNA; YMR010W; YMR010W.
DR GeneID; 855022; -.
DR KEGG; sce:YMR010W; -.
DR SGD; S000004612; ANY1.
DR VEuPathDB; FungiDB:YMR010W; -.
DR eggNOG; KOG2913; Eukaryota.
DR GeneTree; ENSGT00390000002381; -.
DR HOGENOM; CLU_049047_1_1_1; -.
DR InParanoid; Q03687; -.
DR OMA; QMSLDIY; -.
DR BioCyc; YEAST:G3O-32718-MON; -.
DR PRO; PR:Q03687; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03687; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:SGD.
DR GO; GO:0045332; P:phospholipid translocation; IMP:SGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IGI:SGD.
DR InterPro; IPR006603; PQ-loop_rpt.
DR Pfam; PF04193; PQ-loop; 1.
PE 1: Evidence at protein level;
KW Endosome; Golgi apparatus; Lipid transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..405
FT /note="Scramblase ANY1"
FT /id="PRO_0000203270"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27811238"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..76
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27811238"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27811238"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..177
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27811238"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27811238"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..254
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27811238"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27811238"
FT TRANSMEM 284..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..312
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27811238"
FT TRANSMEM 313..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27811238"
FT DOMAIN 252..309
FT /note="PQ-loop"
FT /evidence="ECO:0000255"
FT REGION 379..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 80
FT /note="G->R: Suppresses the growth defects caused by
FT mutations of flippases."
FT /evidence="ECO:0000269|PubMed:27811238"
FT MUTAGEN 84
FT /note="D->G: Suppresses the growth defects caused by
FT mutations of flippases."
FT /evidence="ECO:0000269|PubMed:27811238"
FT MUTAGEN 258..405
FT /note="Missing: Suppresses the growth defects caused by
FT mutations of flippases."
FT /evidence="ECO:0000269|PubMed:27811238"
SQ SEQUENCE 405 AA; 46872 MW; AF019859073E134E CRC64;
MSTTGPLDAT LIRDVAVATA TKASYDMSDT LYSYLPKVDQ FYIPEWLTMQ FIANNLISFT
PLFSYGTTII SIEKCKTALG FSIDICATML IASILRISYY LITPYEITLL RQSLVMIFIQ
LILLRTSLKY RPDEYKYQNL TDVESLSHLI HDIWFEFFSC INRPKFLSED WKNLIKSLSF
TNLLKFSFKI FLAFFYKILK FFDPNFKRIG AFWQWDDDKN FWRFLALFAT VQILVTFFIS
NILNWDSLAQ GLGSIIGSLG LLVESLLPLP QIAILYKLKS VQGFKLILLV SWLCGDTLKI
TYLIFGAKNI SALFVIFALF QMSLDFYIGG QYIYYRYYYP KLRHQHHPND SNSPSDEDES
EMYELDLFNT LQKDVEKALK QDSNDTSDSP QDDQVGKSQA QAVTL
