CBPQ_PONAB
ID CBPQ_PONAB Reviewed; 472 AA.
AC Q5RDN7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 57.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Carboxypeptidase that may play an important role in the
CC hydrolysis of circulating peptides. Catalyzes the hydrolysis of
CC dipeptides with unsubstituted terminals into amino acids. May play a
CC role in the liberation of thyroxine hormone from its thyroglobulin (Tg)
CC precursor (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}. Note=Secretion is stimulated by TSH/thyroid-stimulating
CC hormone, INS/insulin and SST/somatostatin. {ECO:0000250}.
CC -!- PTM: N-glycosylated. The secreted form is modified by hybrid or complex
CC type oligosaccharide chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
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DR EMBL; CR857867; CAH90120.1; -; mRNA.
DR RefSeq; NP_001127240.1; NM_001133768.1.
DR AlphaFoldDB; Q5RDN7; -.
DR SMR; Q5RDN7; -.
DR STRING; 9601.ENSPPYP00000021050; -.
DR MEROPS; M28.014; -.
DR GeneID; 100174295; -.
DR KEGG; pon:100174295; -.
DR CTD; 10404; -.
DR eggNOG; KOG2195; Eukaryota.
DR InParanoid; Q5RDN7; -.
DR OrthoDB; 792624at2759; -.
DR Proteomes; UP000001595; Unplaced.
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 GO; GO:0006590; P:thyroid hormone generation; ISS:UniProtKB.
DR GO; GO:0042246; P:tissue regeneration; 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..44
FT /evidence="ECO:0000250"
FT /id="PRO_0000312262"
FT CHAIN 45..472
FT /note="Carboxypeptidase Q"
FT /id="PRO_0000312263"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 472 AA; 52101 MW; 45CE13046C1AD467 CRC64;
MKFLIFAFFG GVHLLSLCSG KAIYKNGISK RTFEEIKEEI ASYGDVAKAI INLAVYGKAQ
NRSYERLALL VDTVGPRLSG SKNLEKAIQI MYQNLQQDEL ENVHLEPGRI PHWERGEESA
VMLEPRIHKI AILGLGSSIG TPPEGITAEV LVVTSFDELQ RRASEARGKI VVYNQPYINY
SRTVQYRTQG AVEAAKVGAL ASLIRSVASF SIYSPHTGIQ EYQDGVPRIP TACITVEDAE
MMSRMASRGI RIVIQLKMGA KTYPDTDSFN TVAEITGSKY PEQVVLVSGH LDSWDVGQGA
MDDGGGAFIS WEALSLIKDL GLRPKRTLRL VLWTAEEQGG VGAFQYYQLH KVNISNYSLV
MESDTGTFLP TGLQFTGSEK ARAVMEEVMS LLQPLNVTQV LSHGEGTDIN FWIKAGVPGA
SLLDDLYKYF FFHHSHGDTM TVMDPKQMNV AAAVWAVVSY VVADMEEMLP RS
