CBPS2_YEAST
ID CBPS2_YEAST Reviewed; 581 AA.
AC P0C155;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Putative carboxypeptidase YOL153C;
DE EC=3.4.17.-;
GN OrderedLocusNames=YOL153C; ORFNames=O0435/O0437/O0440;
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], AND IDENTIFICATION OF GLU-132 AND
RP GLU-432 IN STRAIN W303-1A.
RC STRAIN=ATCC 208353 / W303-1A, and ATCC 96604 / S288c / FY1679;
RX PubMed=8810044;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<709::aid-yea957>3.0.co;2-1;
RA Gamo F.-J., Lafuente M.J., Casamayor A., Arino J., Aldea M., Casas C.,
RA Herrero E., Gancedo C.;
RT "Analysis of the DNA sequence of a 15,500 bp fragment near the left
RT telomere of chromosome XV from Saccharomyces cerevisiae reveals a putative
RT sugar transporter, a carboxypeptidase homologue and two new open reading
RT frames.";
RL Yeast 12:709-714(1996).
RN [2]
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 [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).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene unlikely to encode a
CC functional protein. Strain S288c has two stop codons in position 132
CC and 432, which disrupt the gene coding for this protein and produce
CC three ORFs. Because of that it is not part of the S.cerevisiae S288c
CC complete/reference proteome set. {ECO:0000305|PubMed:24374639,
CC ECO:0000305|PubMed:8810044}.
CC -!- SEQUENCE CAUTION:
CC Sequence=X89715; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=Z74895; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; X89715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z74895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C155; -.
DR PRIDE; P0C155; -.
DR SGD; S000005513; YOL153C.
DR InParanoid; P0C155; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017141; Pept_M20_carboxypep.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 5: Uncertain;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Isopeptide bond; Membrane;
KW Metal-binding; Protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Zinc.
FT CHAIN 1..581
FT /note="Putative carboxypeptidase YOL153C"
FT /id="PRO_0000226147"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..46
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 172
FT /evidence="ECO:0000250"
FT ACT_SITE 241
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P27614"
SQ SEQUENCE 581 AA; 65093 MW; D6A7D7BBCA0F7FA3 CRC64;
MTETHHAPLP DVYPSSKQPT SSTYSKCKKF GLPLIGLLTL LLAYISSFTK PVPNSTFDVP
ASPQCKKPQV YRPSFNKSVN LILNDKQFKI DSIRKLSGAI QIPTEISDTN PLPNDDPEYY
SEFFKLHKYF EETFPLVHSH LKVEKVNQLG LLYTWEGTDP SLKPILFMAH QDVVPVNREI
WDSWQYPPLS GHYDQETDYV WGRGSNDCKN LMLAELEGIE QLLADGYQTE RTVILSLGFD
EESSGFMGAK VLAPFLLERY GPDSMFSIID EGAGLLRLDK NLYIAAAVNA EKGYVDVRIS
IHGHGGHSSV QPDHTTIGVA SELIYMMENH PFDYNFSLDN PIYDVLQCAA EHSGFLPPHV
REAILKAPVD EGKRKVLTEF AASHPDIRDL IRTTRAVDVI NGGVKANALP GLTSFIVNHR
VDIHSSVNET VENDLYWARV IAEKHGYGLT FHDEIIIPET KLGHISLASE KMLEPAPVSP
TSGHVWEIFA GTVQNLFQNE ILAEQKDADV YVTGGLFSGN TDTKYYWGLS KNIYRFVAGI
FPFDQLRTIH SVNEHISASS HVSAVAFVYE YIVNVNEYGH D
