CBPQ_BOVIN
ID CBPQ_BOVIN Reviewed; 472 AA.
AC Q17QK3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) 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; BC118309; AAI18310.1; -; mRNA.
DR RefSeq; NP_001069716.1; NM_001076248.1.
DR AlphaFoldDB; Q17QK3; -.
DR SMR; Q17QK3; -.
DR STRING; 9913.ENSBTAP00000015799; -.
DR MEROPS; M28.014; -.
DR PaxDb; Q17QK3; -.
DR Ensembl; ENSBTAT00000015799; ENSBTAP00000015799; ENSBTAG00000011908.
DR GeneID; 540923; -.
DR KEGG; bta:540923; -.
DR CTD; 10404; -.
DR VEuPathDB; HostDB:ENSBTAG00000011908; -.
DR VGNC; VGNC:27668; CPQ.
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT00390000018110; -.
DR HOGENOM; CLU_033697_1_1_1; -.
DR InParanoid; Q17QK3; -.
DR OMA; LFMNEEN; -.
DR OrthoDB; 792624at2759; -.
DR TreeFam; TF323248; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000011908; Expressed in thyroid gland and 100 other tissues.
DR ExpressionAtlas; Q17QK3; baseline and differential.
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_0000312258"
FT CHAIN 45..472
FT /note="Carboxypeptidase Q"
FT /id="PRO_0000312259"
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 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 51679 MW; AC781B707B3FB9FC CRC64;
MKFLLFMFVG VVHLLPLASG KAIYGNGPSQ RTFQEIKEEI AHYGDVAKSI INLTVYGKAQ
NRSYERLALL VDTVGPRLSG SKNLERAIEI MQQNLKGDGL ENVHLEPVKI PHWERGEESA
VMLEPRIHKM AILGLGSSIG TPPEGITAEV LVVTSFDELQ RRGPDAEGKI VVYNQPYTNY
SAAVQYRMEG AVEAAKVGAL ASLIRSVASF SIYSPHTGIQ EYQKGVPKIP TACITVEDAE
MMSRMASRGN RIVVQLKMGA KSYPDADSFN TVAEITGSKY PEQVVLVSGH LDSWDVGQGA
MDDGGGAFIS WEALSLIKDL GLRPKRTLRL VLWTAEEQGG VGSSQYYQLH KANSSNYSLV
MESDLGTFLP SGLKFTGSDK ARVIMEEVMS LLQPINITQV LKAGDGTDIN FWIQDGVPGA
SLLDDLYKYF SFHHSHGDTM TVMDPKQMNV AAAVWAVVSY VVADLEEMLP RS
