CBPYA_ASPOR
ID CBPYA_ASPOR Reviewed; 542 AA.
AC Q2TYA1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=cpyA; ORFNames=AO090103000332;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=12223187; DOI=10.1016/s1087-1845(02)00033-6;
RA Ohneda M., Arioka M., Nakajima H., Kitamoto K.;
RT "Visualization of vacuoles in Aspergillus oryzae by expression of CPY-
RT EGFP.";
RL Fungal Genet. Biol. 37:29-38(2002).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=16085884; DOI=10.1128/aem.71.8.4856-4861.2005;
RA Ohneda M., Arioka M., Kitamoto K.;
RT "Isolation and characterization of Aspergillus oryzae vacuolar protein
RT sorting mutants.";
RL Appl. Environ. Microbiol. 71:4856-4861(2005).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=20622126; DOI=10.1128/aem.03087-09;
RA Yoon J., Aishan T., Maruyama J., Kitamoto K.;
RT "Enhanced production and secretion of heterologous proteins by the
RT filamentous fungus Aspergillus oryzae via disruption of vacuolar protein
RT sorting receptor gene Aovps10.";
RL Appl. Environ. Microbiol. 76:5718-5727(2010).
CC -!- FUNCTION: Vacuolar carboxypeptidase involved in degradation of small
CC peptides. Digests preferentially peptides containing an aliphatic or
CC hydrophobic residue in P1' position, as well as methionine, leucine or
CC phenylalanine in P1 position of ester substrate (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity.;
CC EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:12223187,
CC ECO:0000269|PubMed:16085884, ECO:0000269|PubMed:20622126}.
CC Note=Requires vps10 for correct vacuolar localization.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007174; BAE65772.1; -; Genomic_DNA.
DR RefSeq; XP_001826905.1; XM_001826853.2.
DR AlphaFoldDB; Q2TYA1; -.
DR SMR; Q2TYA1; -.
DR STRING; 510516.Q2TYA1; -.
DR ESTHER; aspor-q2tya1; Carboxypeptidase_S10.
DR MEROPS; S10.001; -.
DR EnsemblFungi; BAE65772; BAE65772; AO090103000332.
DR GeneID; 5999027; -.
DR KEGG; aor:AO090103000332; -.
DR VEuPathDB; FungiDB:AO090103000332; -.
DR HOGENOM; CLU_008523_10_4_1; -.
DR OMA; GDWMKPF; -.
DR Proteomes; UP000006564; Chromosome 8.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA:UniProtKB.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR008442; Propeptide_carboxypepY.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF05388; Carbpep_Y_N; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Vacuole; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..123
FT /evidence="ECO:0000250"
FT /id="PRO_0000407437"
FT CHAIN 124..542
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407438"
FT ACT_SITE 265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 178..418
FT /evidence="ECO:0000250"
FT DISULFID 312..326
FT /evidence="ECO:0000250"
FT DISULFID 336..359
FT /evidence="ECO:0000250"
FT DISULFID 343..352
FT /evidence="ECO:0000250"
FT DISULFID 381..388
FT /evidence="ECO:0000250"
SQ SEQUENCE 542 AA; 60892 MW; BD339D3954E9EB3A CRC64;
MRVLPATLLV GAASAAVPPL QQVLGRPEEG MSFSKPLHAF QEQLKTLSED ARKLWDEVAN
YFPDSMDHSP IFSLPKKHTR RPDSHWDHIV RGSDVQKIWV NNADGEKERE IDGKLEAYDL
RIKKADPSAL GIDPNVKQYT GYLDDNGNDK HLFYWFFESR NDPKNDPVVL WLNGGPGCSS
LTGLFMELGP SSIDENIKPV YNDFSWNSNA SVIFLDQPVN VGYSYSGSAV SDTVAAGKDV
YALLSLFFKQ FPEYAEQDFH IAGESYAGHY IPVFASEILA HKNRNINLKS VLIGNGLTDG
LTQYGYYRPM GCGEGGYKAV LDEATCESMD NALPRCRSMI ESCYNSESAW VCVPASIYCN
NALIGPYQRT GQNVYDVRSK CEDESNLCYK GMGYVSEYLN KAEVREAVGA EVGGYDSCNF
DINRNFLFHG DWMKPYHRLV PGLLEQIPVL IYAGDADYIC NWLGNKAWTE ALEWPGQKEY
ASAELEDLKI EQNEHTGKKI GQVKSHGNFT FMRLYGGGHM VPMDQPEASL EFFNRWLGGE
WF
