ID   CBPQ_XENLA              Reviewed;         469 AA.
AC   Q6GQ29;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Carboxypeptidase Q;
DE            EC=3.4.17.-;
DE   AltName: Full=Plasma glutamate carboxypeptidase;
DE   Flags: Precursor;
GN   Name=cpq; Synonyms=pgcp;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Carboxypeptidase that may play an important role in the
CC       hydrolysis of circulating peptides. Catalyzes more efficiently the
CC       hydrolysis of dipeptides with unsubstituted terminals into amino acids
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. The monomeric form is inactive while the homodimer
CC       is active (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi
CC       apparatus {ECO:0000250}. Lysosome {ECO:0000250}. Secreted
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
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DR   EMBL; BC072919; AAH72919.1; -; mRNA.
DR   RefSeq; NP_001085551.1; NM_001092082.1.
DR   AlphaFoldDB; Q6GQ29; -.
DR   SMR; Q6GQ29; -.
DR   MEROPS; M28.014; -.
DR   GeneID; 443977; -.
DR   KEGG; xla:443977; -.
DR   CTD; 443977; -.
DR   Xenbase; XB-GENE-5761579; cpq.L.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 443977; Expressed in internal ear and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   InterPro; IPR039866; CPQ.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12053; PTHR12053; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   Hydrolase; Lysosome; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..42
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000312266"
FT   CHAIN           43..469
FT                   /note="Carboxypeptidase Q"
FT                   /id="PRO_0000312267"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         432
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   469 AA;  52016 MW;  2F22FC1C09406E63 CRC64;
     MKTLILTLLS LYELQLCCGA YNQNIRSQRK FEMIKTEISS YKDVAKSIID LAVHGKAQNR
     SYERLALFVD TVGNRMSGSE NLKTAIAYMY KSLQEDDLDR VYLEPVKVPH WERGEESAML
     LEPRKKSLAI LGLGGSIGTP VEGISAEVIV VSSFAELHNR SKEAKGKIVV YNEPFVNYGE
     TVRYRGSGAV EAAKVGAVAS LIRSVTPLSV YSPHTGWQWY ENDVPKIPTA SITVEDAEML
     SRMASRGLKI VIQLKMGAVN HPDADSYNTV AEIVGSKYPE QVVIVSGHLD SWDVGQGAMD
     DGGGAFISWE ALSLIKDLGL RPKRTLRLVL WTGEEQGGVG ASQYYELHKK NISNIDLVME
     SDIGTFMPLG MQFTGKPEAR AIMTEVMQLL QPINITSLYD YAEGTDINSW MQAGVPGASL
     FDDISKYFWF HHSQGDTMTV QDPVWMNLCA AVWTVVSYVV ADMEEMLPR