ATG42_YEAST
ID ATG42_YEAST Reviewed; 508 AA.
AC P38109; D6VQD5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Vacuolar serine-type carboxypeptidase ATG42 {ECO:0000303|PubMed:29514932};
DE EC=3.4.16.5 {ECO:0000269|PubMed:29514932};
DE AltName: Full=Carboxypeptidase C {ECO:0000303|PubMed:17408619};
DE Short=CPC {ECO:0000303|PubMed:17408619};
DE Flags: Precursor;
GN Name=ATG42 {ECO:0000303|PubMed:29514932}; OrderedLocusNames=YBR139W;
GN ORFNames=YBR1015;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091856; DOI=10.1002/yea.320100002;
RA Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F.,
RA Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M.,
RA Herbert C.J.;
RT "The sequence of 29.7 kb from the right arm of chromosome II reveals 13
RT complete open reading frames, of which ten correspond to new genes.";
RL Yeast 10:S1-S11(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 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 [5]
RP DISCUSSION OF SEQUENCE.
RX PubMed=7954890; DOI=10.1007/bf00326297;
RA Nasr F., Becam A.-M., Grzybowska E., Zagulski M., Slonimski P.P.,
RA Herbert C.J.;
RT "An analysis of the sequence of part of the right arm of chromosome II of
RT S. cerevisiae reveals new genes encoding an amino-acid permease and a
RT carboxypeptidase.";
RL Curr. Genet. 26:1-7(1994).
RN [6]
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 [7]
RP INDUCTION.
RX PubMed=16879428; DOI=10.1111/j.1567-1364.2006.00060.x;
RA Scherens B., Feller A., Vierendeels F., Messenguy F., Dubois E.;
RT "Identification of direct and indirect targets of the Gln3 and Gat1
RT activators by transcriptional profiling in response to nitrogen
RT availability in the short and long term.";
RL FEMS Yeast Res. 6:777-791(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17408619; DOI=10.1016/j.febslet.2007.03.039;
RA Wuenschmann J., Beck A., Meyer L., Letzel T., Grill E., Lendzian K.J.;
RT "Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 581:1681-1687(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19897216; DOI=10.1016/j.phytochem.2009.09.034;
RA Wuenschmann J., Krajewski M., Letzel T., Huber E.M., Ehrmann A., Grill E.,
RA Lendzian K.J.;
RT "Dissection of glutathione conjugate turnover in yeast.";
RL Phytochemistry 71:54-61(2010).
RN [10]
RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-163 AND ASN-242, FUNCTION,
RP DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF
RP ASN-163; SER-219; ASN-242; ASP-415 AND HIS-474.
RX PubMed=29514932; DOI=10.1091/mbc.e17-08-0516;
RA Parzych K.R., Ariosa A., Mari M., Klionsky D.J.;
RT "A newly characterized vacuolar serine carboxypeptidase, Atg42/Ybr139w, is
RT required for normal vacuole function and the terminal steps of autophagy in
RT the yeast Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 29:1089-1099(2018).
CC -!- FUNCTION: Vacuolar serine-type carboxypeptidase involved in vacuolar
CC zymogen activation, breakdown of the autophagic body, and
CC autophagosome-dependent protein synthesis (PubMed:29514932). Plays a
CC key role in phytochelatin (PC) synthesis from glutathione (GSH) by
CC cleaving the Gly from GSH and form the PC-peptides of the structure
CC (gamma-Glu-Cys)2-Gly (PubMed:17408619). Also involved in resistance to
CC xenobiotics via the degradation of glutathione-S-conjugates
CC (PubMed:19897216). {ECO:0000269|PubMed:17408619,
CC ECO:0000269|PubMed:19897216, ECO:0000269|PubMed:29514932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity.;
CC EC=3.4.16.5; Evidence={ECO:0000269|PubMed:29514932};
CC -!- SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:29514932}.
CC Note=The vacuolar sorting receptor VPS10 is required for the delivery
CC of ATG42 to the vacuole lumen. {ECO:0000269|PubMed:29514932}.
CC -!- INDUCTION: Expression is induced by nitrogen limitation in a GLN3 and
CC GAT1-independent manner. {ECO:0000269|PubMed:16879428}.
CC -!- DISRUPTION PHENOTYPE: Leads to vacuolar defects as well as defects in
CC the terminal steps of autophagy, when PCR1 is also deleted
CC (PubMed:29514932). The PCR1/ATG42 double deletion abrogates also the
CC production ofphytochelatin and the degradation of glutathione-S-
CC conjugates (PubMed:17408619, PubMed:19897216).
CC {ECO:0000269|PubMed:17408619, ECO:0000269|PubMed:19897216,
CC ECO:0000269|PubMed:29514932}.
CC -!- MISCELLANEOUS: Present with 1420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; X75891; CAA53497.1; -; Genomic_DNA.
DR EMBL; Z36008; CAA85097.1; -; Genomic_DNA.
DR EMBL; AY692681; AAT92700.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07255.1; -; Genomic_DNA.
DR PIR; S46008; S46008.
DR RefSeq; NP_009697.3; NM_001178487.3.
DR AlphaFoldDB; P38109; -.
DR SMR; P38109; -.
DR BioGRID; 32839; 133.
DR DIP; DIP-4923N; -.
DR IntAct; P38109; 7.
DR MINT; P38109; -.
DR STRING; 4932.YBR139W; -.
DR ESTHER; yeast-yby9; Carboxypeptidase_S10.
DR MEROPS; S10.A49; -.
DR iPTMnet; P38109; -.
DR MaxQB; P38109; -.
DR PaxDb; P38109; -.
DR PRIDE; P38109; -.
DR EnsemblFungi; YBR139W_mRNA; YBR139W; YBR139W.
DR GeneID; 852436; -.
DR KEGG; sce:YBR139W; -.
DR SGD; S000000343; YBR139W.
DR VEuPathDB; FungiDB:YBR139W; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; P38109; -.
DR OMA; NCYVEMD; -.
DR BioCyc; MetaCyc:G3O-29093-MON; -.
DR BioCyc; YEAST:G3O-29093-MON; -.
DR PRO; PR:P38109; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38109; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA:SGD.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:SGD.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IGI:SGD.
DR GO; GO:0016236; P:macroautophagy; IGI:SGD.
DR GO; GO:0046938; P:phytochelatin biosynthetic process; IGI:SGD.
DR GO; GO:0031638; P:zymogen activation; IGI:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 1: Evidence at protein level;
KW Autophagy; Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Signal; Vacuole.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..508
FT /note="Vacuolar serine-type carboxypeptidase ATG42"
FT /id="PRO_0000120563"
FT ACT_SITE 219
FT /evidence="ECO:0000269|PubMed:29514932"
FT ACT_SITE 415
FT /evidence="ECO:0000269|PubMed:29514932"
FT ACT_SITE 474
FT /evidence="ECO:0000269|PubMed:29514932"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT BINDING 475
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:29514932"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:29514932"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 132..375
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT DISULFID 267..281
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT DISULFID 291..314
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT DISULFID 298..307
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT DISULFID 336..345
FT /evidence="ECO:0000250|UniProtKB:P00729"
FT MUTAGEN 163
FT /note="N->Q: Reduces the glycolation level."
FT /evidence="ECO:0000269|PubMed:29514932"
FT MUTAGEN 219
FT /note="S->A: Leads to partial block in enzymatic activity."
FT /evidence="ECO:0000269|PubMed:29514932"
FT MUTAGEN 242
FT /note="N->Q: Reduces the glycolation level."
FT /evidence="ECO:0000269|PubMed:29514932"
FT MUTAGEN 415
FT /note="D->A: Leads to partial block in enzymatic activity."
FT /evidence="ECO:0000269|PubMed:29514932"
FT MUTAGEN 474
FT /note="H->A: Leads to partial block in enzymatic activity."
FT /evidence="ECO:0000269|PubMed:29514932"
SQ SEQUENCE 508 AA; 57639 MW; AAB2806C8EE2EDE1 CRC64;
MKYLNLVFVL QLLISIKYAS FGRAFSLFED DTTFANLDKQ LKLPQNTQQT LKLDRLNHDD
PLFTTFISSV DTDYSLRLRT VDPSKLGIDT VKQWSGYMDY KDSKHFFYWF FESRNDPAND
PIILWLNGGP GCSSFTGLLF ELGPSSIGAD MKPIHNPYSW NNNASMIFLE QPLGVGFSYG
DEKVSSTKLA GKDAYIFLEL FFEAFPHLRS NDFHIAGESY AGHYIPQIAH EIVVKNPERT
FNLTSVMIGN GITDPLIQAD YYEPMACGKG GYHPVLSSEE CEKMSKAAGR CRRLNKLCYA
SKSSLPCIVA TAYCDSALLE PYINTGLNVY DIRGPCEDNS TDGMCYTGLR YVDQYMNFPE
VQETLGSDVH NYSGCDNDVF TGFLFTGDGS KPFQQYIAEL LNHNIPVLIY AGDKDYICNW
LGNHAWSNEL EWINKRRYQR RMLRPWVSKE TGEELGQVKN YGPFTFLRIY DAGHMVPYDQ
PEASLEMVNS WISGNRAFSD LSTLENAS
