YP097_YEAST
ID YP097_YEAST Reviewed; 1073 AA.
AC Q06839; D6W496;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=PX domain-containing protein YPR097W;
GN OrderedLocusNames=YPR097W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 848.
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 DOMAIN.
RX PubMed=11557775; DOI=10.1074/jbc.m108811200;
RA Yu J.W., Lemmon M.A.;
RT "All phox homology (PX) domains from Saccharomyces cerevisiae specifically
RT recognize phosphatidylinositol 3-phosphate.";
RL J. Biol. Chem. 276:44179-44184(2001).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-451, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization.
CC {ECO:0000269|PubMed:11557775}.
CC -!- MISCELLANEOUS: Present with 3080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U51033; AAB68142.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11512.2; -; Genomic_DNA.
DR PIR; S69079; S69079.
DR RefSeq; NP_015422.2; NM_001184194.2.
DR AlphaFoldDB; Q06839; -.
DR BioGRID; 36264; 55.
DR DIP; DIP-49374N; -.
DR IntAct; Q06839; 4.
DR MINT; Q06839; -.
DR STRING; 4932.YPR097W; -.
DR CarbonylDB; Q06839; -.
DR iPTMnet; Q06839; -.
DR MaxQB; Q06839; -.
DR PaxDb; Q06839; -.
DR PRIDE; Q06839; -.
DR EnsemblFungi; YPR097W_mRNA; YPR097W; YPR097W.
DR GeneID; 856212; -.
DR KEGG; sce:YPR097W; -.
DR SGD; S000006301; YPR097W.
DR VEuPathDB; FungiDB:YPR097W; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_007739_1_0_1; -.
DR InParanoid; Q06839; -.
DR OMA; QLWQDPE; -.
DR BioCyc; YEAST:G3O-34238-MON; -.
DR PRO; PR:Q06839; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06839; protein.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:SGD.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR024554; DUF3818_PX-associated.
DR InterPro; IPR024555; PX-associated.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR Pfam; PF12825; DUF3818; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF12828; PXB; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Phosphoprotein; Reference proteome.
FT CHAIN 1..1073
FT /note="PX domain-containing protein YPR097W"
FT /id="PRO_0000257826"
FT DOMAIN 273..506
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 218..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 848
FT /note="S -> G (in Ref. 1; AAB68142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1073 AA; 123084 MW; 3D5B831A7E9B3334 CRC64;
MITQDTPALN PTEEHYLKRE LLRCQLDYEI GKLNDQFALR KFGYPFSPND PTAPQPISNN
DSSPVLGGKG HFSVNYPMLS YVLQEFISTF PLLSTNLLVD EKFWQSKVQV FFEHFMSLGF
SESYDREEAS KRKKVSKKLS KVILLLFNSG VGSFQEQAYY NEDKFVLQSG QARKRSNIEK
FAMPTRENLE NLLTNESVFI NGWDVNIISV FNKNSRKCTE SVDNDKSSKS TPTSSPKSHA
IKSFASTSKW MKNAFNNTIN STINSMPESS ASLFSKLSLG VPSTKSKQSR KHHYFLIKIK
KQDDDDQDNS NEENSNLDHH AGYFYVTRTY SDFKKLSHDL KSEFPGKKCP RLPHRNKKVT
SMITKTEVLH NGQTKSAARE KIVNTFDTDL QSASESDNSS FLQTTNELSA TETVLTEKET
ETLRKNILNE IKEEDNIDED EYEEEGEGEE SDFDEYKDAS DSKINTLVGE KMRTSLRQYL
RTLCKDAEVS QSSSIRRFFL SGPNLDIKDI NPKIADDIRN RALIDVSNLE NQIRFQQMAL
EKSLKLQDSM KDFKTSLLKD EKYLMSLLVE IKDNTKVEDL SPLLQDFVEW CKIYISSMIY
QMFLGNDNSY ELYTQIRRLH KLMPYTVMGQ IMKFTNPIAI MRGMIELFMA QPFGGHSLLQ
TMFSTILTDD LKTQKVAIKE LERKIAEMDP GASVVTKCLK DFVFNNDTKD EHDTKLFTMD
AVNAESESMN MPVPLIVLMK SAAANLIPDE VVAGLIESYS SWKLQKEDTD ALNVTSEDQS
GIYFTHVKDL WQLYIKEHDK QLMRQLWQDP ELTQMLKAIV TMIYEPMVKI FKVARMDVAL
KNFEKFMSDL IRLVDDVING QLGVSTQFDV VEEIHNLVTK HQDAFFEFIH DVYLNDSEGI
FEGFITWITT IVKFLQKSKF GGPSERIDFN KLICRDDIDI DVKLLKVQVN NVLNKKIGAR
KIYKKLLDLK VKQGTKQNNK HAAGILQKNW SDINSLVMPS SSGSFGLGDG DLVDLDLDTG
DYDFLHKENE VELEKQYKDL LNLVVDESEI DKLRSQVFAQ ELKNYLEAQI AKK
