YOR22_YEAST
ID YOR22_YEAST Reviewed; 715 AA.
AC Q12204; D6W289;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable phospholipase YOR022C, mitochondrial;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN OrderedLocusNames=YOR022C; ORFNames=OR26.12;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Probable phospholipase that hydrolyzes phosphatidic acid.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PA-PLA1 family. {ECO:0000305}.
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DR EMBL; X87331; CAA60771.1; -; Genomic_DNA.
DR EMBL; Z74930; CAA99212.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10805.1; -; Genomic_DNA.
DR PIR; S54628; S54628.
DR RefSeq; NP_014665.1; NM_001183441.1.
DR AlphaFoldDB; Q12204; -.
DR BioGRID; 34426; 61.
DR STRING; 4932.YOR022C; -.
DR iPTMnet; Q12204; -.
DR MaxQB; Q12204; -.
DR PaxDb; Q12204; -.
DR PRIDE; Q12204; -.
DR EnsemblFungi; YOR022C_mRNA; YOR022C; YOR022C.
DR GeneID; 854187; -.
DR KEGG; sce:YOR022C; -.
DR SGD; S000005548; YOR022C.
DR VEuPathDB; FungiDB:YOR022C; -.
DR eggNOG; KOG2308; Eukaryota.
DR GeneTree; ENSGT00940000169275; -.
DR HOGENOM; CLU_007365_0_0_1; -.
DR InParanoid; Q12204; -.
DR OMA; CGSPVGF; -.
DR BioCyc; YEAST:G3O-33570-MON; -.
DR Reactome; R-SCE-1483166; Synthesis of PA.
DR Reactome; R-SCE-1483226; Synthesis of PI.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR PRO; PR:Q12204; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12204; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:CACAO.
DR GO; GO:0004620; F:phospholipase activity; IDA:SGD.
DR GO; GO:0032048; P:cardiolipin metabolic process; IMP:SGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; IMP:SGD.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR004177; DDHD_dom.
DR Pfam; PF02862; DDHD; 2.
DR SMART; SM01127; DDHD; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS51043; DDHD; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid metabolism; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..715
FT /note="Probable phospholipase YOR022C, mitochondrial"
FT /id="PRO_0000237644"
FT DOMAIN 519..700
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 501
FT /evidence="ECO:0000250"
SQ SEQUENCE 715 AA; 81769 MW; DE3982A606E4BD9C CRC64;
MLRFTHRGLP SSTRFRNIFV RLNHIYVPWF YAIDVPNSKP YLPTYQTLHS PKKFKPFSVD
DSNRLEKASK RQERRPVLVN EDYLFKVDLS HMELSPTYWE GPTYQVRRGV WFDSSNQPLS
SDLTSEIEGL YKQLKFDDSN DDPTTTPPAE SQDIFRLKGK YPVDKENEGE QKNGSSNKDE
NESTFKFILF ANKQTAFLLS DLDGGKLQLA FLRSNLAQSL PINATMITRS YKYSSSATTK
QTSTSFKAAK TPQTEVADGS NSSKSRSIET KLEKKVSNLF NLSDFLQLFN GNASKDQDDA
QSLEKQMETD YNNADNSQGA NASSKIEDGK NSGASDRQIR SNRRDVDNLI LCVHGIGQTL
GKKYEYVNFA HTVNLLRSNM KKIYNNSEKL QSLNTAPDYK SNCNVQVLPI TWRHSISFQT
DAKEENIENP DLPTLSQVTV NGVLPLRKLL ADGLLDILLY VEPYYQDMIL QQVTSQLNKT
YRIFKEFNPE FDGKVHLVGH SLGSMILFDI LSKQKKYELE FQVDNLFFIG SPIGLLKLIQ
RTKIGDRPEF PNDLERKLTV QRPQCKDIYN VYHVCDPISY RMEPLVSKEM AHYEQTYLPH
CSEAYGLTSK VLEFGENIWK DLPGTDENNL QSKKTSPEKK EVKLSENLTR MLTGLNYTGR
LDYAMSPSLL EVDFISAIKS HVSYFEEPDI AAFILKEILS KHENASEIYV KRKTG