ECM18_YEAST
ID ECM18_YEAST Reviewed; 453 AA.
AC Q04623; D6VSB1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein ECM18;
DE EC=2.3.1.-;
DE AltName: Full=Extracellular mutant protein 18;
GN Name=ECM18; OrderedLocusNames=YDR125C; ORFNames=YD9727.20C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
RN [4]
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 [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).
CC -!- FUNCTION: May be involved in cell wall organization and biogenesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 143 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z48758; CAA88678.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11971.1; -; Genomic_DNA.
DR PIR; S52690; S52690.
DR RefSeq; NP_010410.3; NM_001180433.3.
DR AlphaFoldDB; Q04623; -.
DR SMR; Q04623; -.
DR BioGRID; 32181; 31.
DR STRING; 4932.YDR125C; -.
DR ESTHER; yeast-ECM18; CGI-58_ABHD5_ABHD4.
DR MEROPS; S33.A42; -.
DR PaxDb; Q04623; -.
DR PRIDE; Q04623; -.
DR EnsemblFungi; YDR125C_mRNA; YDR125C; YDR125C.
DR GeneID; 851703; -.
DR KEGG; sce:YDR125C; -.
DR SGD; S000002532; ECM18.
DR VEuPathDB; FungiDB:YDR125C; -.
DR eggNOG; KOG4409; Eukaryota.
DR GeneTree; ENSGT00940000170137; -.
DR HOGENOM; CLU_017361_1_1_1; -.
DR InParanoid; Q04623; -.
DR OMA; EQWRIDN; -.
DR BioCyc; YEAST:G3O-29725-MON; -.
DR Reactome; R-SCE-1482839; Acyl chain remodelling of PE.
DR PRO; PR:Q04623; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04623; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell wall biogenesis/degradation; Mitochondrion;
KW Reference proteome; Transferase.
FT CHAIN 1..453
FT /note="Protein ECM18"
FT /id="PRO_0000086914"
FT DOMAIN 130..435
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT MOTIF 428..433
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250"
SQ SEQUENCE 453 AA; 53185 MW; A927A846375B10CF CRC64;
MLLIKRYLMD PESLRRQIMN VYKCYMWKRA FHSNRSLLEV KRREKSLQRK ILERILRPKE
ENAVKKSGFK LWSSHLNNPH KTYMRLEELQ RRIMEEVHVE GIKKNDKLFN EINQWHFQNE
NTSTVRTPTL LIHGYAASSM SFFRNYPGLS KHIRNLYSID MPASGLSSVP SLEINTTTPL
PLDIKFIGEN KFKVPYTINA NHNKFVIQMY EDFYLDRIEQ WRIDNKLGKM NVVGHSFGGY
LSFKYAVKYP NSVNKLCLVS PLGVERNIWS VNNNFHSNTL YTIDFKNPNS KFYSKRNMIP
KYLFEQQFHI LRMMGPLGAK LCWNYIMAAY SRVPSLAYKE YIFELFYGKG GIPEVTTDIF
KALFSRCILA KDPLMDSLQY LNVKKLLIVY GQYDWMNKKA GMFMVKELNN LKNCLEGASY
LEIPSSGHNL FLDNPESFNQ SIVSFLSDET KSP
