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 04-NOV-2026, entry version 183. DE RecName: Full=Phospholipid-transporting ATPase accessory subunit CDC50 {ECO:0000305}; DE AltName: Full=Cell division control protein 50 {ECO:0000305}; GN Name=CDC50 {ECO:0000303|PubMed:11180453}; GN Synonyms=SWA4 {ECO:0000303|PubMed:16956384}; GN 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). RN [8] RP FUNCTION, INTERACTION WITH DRS2, SUBCELLULAR LOCATION, AND DISRUPTION RP PHENOTYPE. RX PubMed=16956384; DOI=10.1111/j.1600-0854.2006.00485.x; RA Chen S., Wang J., Muthusamy B.P., Liu K., Zare S., Andersen R.J., RA Graham T.R.; RT "Roles for the Drs2p-Cdc50p complex in protein transport and RT phosphatidylserine asymmetry of the yeast plasma membrane."; RL Traffic 7:1503-1517(2006). RN [9] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DRS2, INTERACTION WITH DRS2, AND RP DISRUPTION PHENOTYPE. 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 [10] RP FUNCTION, INTERACTION WITH DRS2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP PRO-23; GLN-71 AND THR-320. RX PubMed=21212072; DOI=10.1093/jb/mvq155; RA Takahashi Y., Fujimura-Kamada K., Kondo S., Tanaka K.; RT "Isolation and characterization of novel mutations in CDC50, the non- RT catalytic subunit of the Drs2p phospholipid flippase."; RL J. Biochem. 149:423-432(2011). RN [11] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DRS2, INTERACTION WITH DRS2, RP DISRUPTION PHENOTYPE, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-80 AND RP CYS-123. 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). RN [12] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DRS2, INTERACTION WITH DRS2, RP IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE. RX PubMed=25393116; DOI=10.1371/journal.pone.0112176; RA Azouaoui H., Montigny C., Ash M.R., Fijalkowski F., Jacquot A., RA Groenberg C., Lopez-Marques R.L., Palmgren M.G., Garrigos M., le Maire M., RA Decottignies P., Gourdon P., Nissen P., Champeil P., Lenoir G.; RT "A high-yield co-expression system for the purification of an intact Drs2p- RT Cdc50p lipid flippase complex, critically dependent on and stabilized by RT phosphatidylinositol-4-phosphate."; RL PLoS ONE 9:e112176-e112176(2014). RN [13] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DRS2, INTERACTION WITH DRS2, AND RP MASS SPECTROMETRY. RX PubMed=28302728; DOI=10.1074/jbc.m116.751487; RA Azouaoui H., Montigny C., Dieudonne T., Champeil P., Jacquot A., RA Vazquez-Ibar J.L., Le Marechal P., Ulstrup J., Ash M.R., Lyons J.A., RA Nissen P., Lenoir G.; RT "High phosphatidylinositol 4-phosphate (PI4P)-dependent ATPase activity for RT the Drs2p-Cdc50p flippase after removal of its N- and C-terminal RT extensions."; RL J. Biol. Chem. 292:7954-7970(2017). RN [14] {ECO:0007744|PDB:6ROH, ECO:0007744|PDB:6ROI, ECO:0007744|PDB:6ROJ} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH DRS2 AND MAGNESIUM, RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH DRS2, INTERACTION WITH DRS2, RP GLYCOSYLATION AT ASN-199; ASN-216; ASN-237 AND ASN-288, AND DISULFIDE RP BONDS. RX PubMed=31243363; DOI=10.1038/s41586-019-1344-7; RA Timcenko M., Lyons J.A., Januliene D., Ulstrup J.J., Dieudonne T., RA Montigny C., Ash M.R., Karlsen J.L., Boesen T., Kuhlbrandt W., Lenoir G., RA Moeller A., Nissen P.; RT "Structure and autoregulation of a P4-ATPase lipid flippase."; RL Nature 571:366-370(2019). RN [15] {ECO:0007744|PDB:6PSX, ECO:0007744|PDB:6PSY} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH DRS2, FUNCTION, RP IDENTIFICATION IN A COMPLEX WITH DRS2, INTERACTION WITH DRS2, GLYCOSYLATION RP AT ASN-199; ASN-216 AND ASN-288, AND DISULFIDE BONDS. RX PubMed=31515475; DOI=10.1038/s41467-019-12191-9; RA Bai L., Kovach A., You Q., Hsu H.C., Zhao G., Li H.; RT "Autoinhibition and activation mechanisms of the eukaryotic lipid flippase RT Drs2p-Cdc50p."; RL Nat. Commun. 10:4142-4142(2019). RN [16] {ECO:0007744|PDB:7OH4, ECO:0007744|PDB:7OH5, ECO:0007744|PDB:7OH6, ECO:0007744|PDB:7OH7} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH DRS2 AND RP PHOSPHATIDYLINOSITOL 4-PHOSPHATE, FUNCTION, IDENTIFICATION IN A COMPLEX RP WITH DRS2, INTERACTION WITH DRS2, AND DISULFIDE BONDS. RX PubMed=34023399; DOI=10.1016/j.jmb.2021.167062; RA Timcenko M., Dieudonne T., Montigny C., Boesen T., Lyons J.A., Lenoir G., RA Nissen P.; RT "Structural Basis of Substrate-Independent Phosphorylation in a P4-ATPase RT Lipid Flippase."; RL J. Mol. Biol. 433:167062-167062(2021). RN [17] {ECO:0007744|PDB:7PEM} RP STRUCTURE BY ELECTRON MICROSCOPY, IDENTIFICATION IN A COMPLEX WITH DRS2, RP INTERACTION WITH DRS2, AND DISULFIDE BONDS. RA Wang Y., Lyons J.A., Timcenko M., Kummerer F., de Groot B.L., Nissen P., RA Gapsys V., Lindorff-Larsen K.; RT "Substrate Transport and Specificity in a Phospholipid Flippase."; RL Submitted (AUG-2021) to the PDB data bank. CC -!- FUNCTION: Accessory component of a P4-ATPase flippase complex which CC catalyzes the hydrolysis of ATP coupled to the transport of CC phosphatidylserine and small amounts of ethanolamine from the lumen to CC the cytosolic leaflet of the trans-Golgi network and ensures the CC maintenance of asymmetric distribution of phospholipids CC (PubMed:16956384, PubMed:19411703, PubMed:22791719, PubMed:25393116, CC PubMed:28302728, PubMed:31243363, PubMed:31515475, PubMed:34023399). CC Required for the formation of transport vesicles from endosomes CC (PubMed:21212072). {ECO:0000269|PubMed:16956384, CC ECO:0000269|PubMed:19411703, ECO:0000269|PubMed:21212072, CC ECO:0000269|PubMed:22791719, ECO:0000269|PubMed:25393116, CC ECO:0000269|PubMed:28302728, ECO:0000269|PubMed:31243363, CC ECO:0000269|PubMed:31515475, ECO:0000269|PubMed:34023399}. CC -!- SUBUNIT: Component of a flippase complex consisting of DRS2 and CDC50 CC (PubMed:19411703, PubMed:22791719, PubMed:25393116, PubMed:28302728, CC PubMed:31243363, PubMed:31515475, PubMed:34023399, Ref.17). Interacts CC with DRS2; the interaction is direct, is required for their mutual CC export from the endoplasmic reticulum, and preferentially occurs when CC DRS2 is in the E2P state (PubMed:15090616, PubMed:16956384, CC PubMed:19411703, PubMed:21212072, PubMed:22791719, PubMed:25393116, CC PubMed:28302728, PubMed:31243363, PubMed:31515475, PubMed:34023399, CC Ref.17). {ECO:0000269|PubMed:15090616, ECO:0000269|PubMed:16956384, CC ECO:0000269|PubMed:19411703, ECO:0000269|PubMed:21212072, CC ECO:0000269|PubMed:22791719, ECO:0000269|PubMed:25393116, CC ECO:0000269|PubMed:28302728, ECO:0000269|PubMed:31243363, CC ECO:0000269|PubMed:31515475, ECO:0000269|PubMed:34023399, CC ECO:0000269|Ref.17}. CC -!- INTERACTION: CC P25656; P39524: DRS2; NbExp=11; IntAct=EBI-22014, EBI-3106; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:21212072, ECO:0000305|PubMed:16956384}; Multi-pass CC membrane protein {ECO:0000255}. Late endosome membrane CC {ECO:0000269|PubMed:12589066}; Multi-pass membrane protein CC {ECO:0000269|PubMed:12589066}. CC -!- MASS SPECTROMETRY: Mass=52300; Method=MALDI; CC Evidence={ECO:0000269|PubMed:28302728}; CC -!- DISRUPTION PHENOTYPE: Leads to abnormal trafficking of DRS2 from the CC endoplasmic reticulum to the Golgi, and decreases DRS2 protein level CC (PubMed:16956384, PubMed:19411703). Abnormal processing and CC modification of proteins in the trans-Golgi network (PubMed:16956384). CC Accumulation of aberrant membranous material probably derived from the CC Golgi (PubMed:16956384). Sensitive to cold, papuamide B (lipopeptide CC that permeabilizes phosphatidylserine-containing membranes), and Ro09- CC 0198 (antifungal peptide that targets phosphatidylethanolamine in the CC outer leaflet of the cell membrane) (PubMed:16956384, PubMed:22791719, CC PubMed:25393116). {ECO:0000269|PubMed:16956384, CC ECO:0000269|PubMed:19411703, ECO:0000269|PubMed:22791719, CC ECO:0000269|PubMed:25393116}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7PEM; EM; 3.10 A; C=1-391. DR AlphaFoldDB; P25656; -. DR EMDB; EMD-12893; -. DR EMDB; EMD-12895; -. DR EMDB; EMD-12896; -. DR EMDB; EMD-13353; -. DR EMDB; EMD-20467; -. DR EMDB; EMD-20468; -. DR EMDB; EMD-4972; -. DR EMDB; EMD-4973; -. DR EMDB; EMD-4974; -. DR SMR; P25656; -. DR BioGRID; 31066; 439. DR ComplexPortal; CPX-1018; DRS2-CDC50 P4-ATPase complex. DR DIP; DIP-5138N; -. DR FunCoup; P25656; 481. DR IntAct; P25656; 8. DR STRING; 4932.YCR094W; -. DR TCDB; 8.A.27.1.2; the cdc50 p-type atpase lipid flippase subunit (cdc50) family. DR GlyCosmos; P25656; 5 sites, No reported glycans. DR GlyGen; P25656; 5 sites. DR iPTMnet; P25656; -. DR PaxDb; 4932-YCR094W; -. DR PeptideAtlas; P25656; -. DR EnsemblFungi; YCR094W_mRNA; YCR094W; YCR094W. DR GeneID; 850456; -. DR KEGG; sce:YCR094W; -. DR AGR; SGD:S000000690; -. DR SGD; S000000690; CDC50. DR VEuPathDB; FungiDB:YCR094W; -. DR eggNOG; KOG2952; Eukaryota. DR HOGENOM; CLU_025025_0_1_1; -. DR InParanoid; P25656; -. DR OMA; ACENQLH; -. DR OrthoDB; 340608at2759; -. DR BioCyc; YEAST:G3O-29388-MONOMER; -. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 850456; 1 hit in 10 CRISPR screens. 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:0031902; C:late endosome membrane; IDA:SGD. DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; NAS:ComplexPortal. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD. DR GO; GO:0140767; F:enzyme-substrate adaptor activity; IBA:GO_Central. 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: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 3D-structure; Disulfide bond; Endosome; Glycoprotein; Golgi apparatus; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..391 FT /note="Phospholipid-transporting ATPase accessory subunit FT CDC50" 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 REGION 68..329 FT /note="Confers specificity for binding DRS2" FT /evidence="ECO:0000269|PubMed:22791719" FT CARBOHYD 199 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:31243363, FT ECO:0000269|PubMed:31515475" FT CARBOHYD 216 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:31243363, FT ECO:0000269|PubMed:31515475, ECO:0007744|PDB:7OH6, FT ECO:0007744|PDB:7OH7" FT CARBOHYD 237 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:31243363" FT CARBOHYD 288 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:31243363, FT ECO:0000269|PubMed:31515475" FT CARBOHYD 329 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 80..123 FT /evidence="ECO:0000269|PubMed:31243363, FT ECO:0000269|PubMed:31515475, ECO:0000269|Ref.17, FT ECO:0000305|PubMed:22791719, ECO:0007744|PDB:6PSX, FT ECO:0007744|PDB:6PSY, ECO:0007744|PDB:6ROH, FT ECO:0007744|PDB:6ROI, ECO:0007744|PDB:6ROJ, FT ECO:0007744|PDB:7OH4, ECO:0007744|PDB:7OH5, FT ECO:0007744|PDB:7OH6, ECO:0007744|PDB:7OH7, FT ECO:0007744|PDB:7PEM" FT DISULFID 176..190 FT /evidence="ECO:0000269|PubMed:31243363, FT ECO:0000269|PubMed:31515475, ECO:0000269|Ref.17, FT ECO:0000305|PubMed:22791719, ECO:0007744|PDB:6PSX, FT ECO:0007744|PDB:6PSY, ECO:0007744|PDB:6ROH, FT ECO:0007744|PDB:6ROI, ECO:0007744|PDB:6ROJ, FT ECO:0007744|PDB:7OH4, ECO:0007744|PDB:7OH5, FT ECO:0007744|PDB:7OH6, ECO:0007744|PDB:7OH7, FT ECO:0007744|PDB:7PEM" FT MUTAGEN 23 FT /note="P->H: Abnormal endocytic recycling, but interaction FT with DRS2 appears normal; when associated with A-320." FT /evidence="ECO:0000269|PubMed:21212072" FT MUTAGEN 71 FT /note="Q->H: Abnormal endocytic recycling, but interaction FT with DRS2 appears normal." FT /evidence="ECO:0000269|PubMed:21212072" FT MUTAGEN 80 FT /note="C->A: Reduces interaction with DRS2." FT /evidence="ECO:0000269|PubMed:22791719" FT MUTAGEN 123 FT /note="C->A: Reduces interaction with DRS2." FT /evidence="ECO:0000269|PubMed:22791719" FT MUTAGEN 320 FT /note="T->A: Abnormal endocytic recycling, but interaction FT with DRS2 appears normal; when associated with H-23." FT /evidence="ECO:0000269|PubMed:21212072" 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 //