CBPQ_RAT
ID CBPQ_RAT Reviewed; 472 AA.
AC Q6IRK9; Q9JLV0; Q9Z1Y1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Carboxypeptidase Q;
DE EC=3.4.17.-;
DE AltName: Full=Hematopoietic lineage switch 2 related protein;
DE Short=Hls2-rp;
DE AltName: Full=Liver annexin-like protein 1;
DE Short=LAL-1;
DE AltName: Full=Plasma glutamate carboxypeptidase;
DE Flags: Precursor;
GN Name=Cpq; Synonyms=Pgcp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=12390252; DOI=10.1046/j.1365-2443.2002.00593.x;
RA Della Fazia M.A., Piobbico D., Bartoli D., Castelli M., Brancorsini S.,
RA Viola Magni M., Servillo G.;
RT "lal-1: a differentially expressed novel gene during proliferation in liver
RT regeneration and in hepatoma cells.";
RL Genes Cells 7:1183-1190(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer;
RA Chen Y., Talmage D.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 170-182 AND 262-279, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=22127294; DOI=10.1016/j.biochi.2011.10.018;
RA Suban D., Zajc T., Renko M., Turk B., Turk V., Dolenc I.;
RT "Cathepsin C and plasma glutamate carboxypeptidase secreted from Fischer
RT rat thyroid cells liberate thyroxin from the N-terminus of thyroglobulin.";
RL Biochimie 94:719-726(2012).
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. {ECO:0000269|PubMed:22127294}.
CC -!- SUBUNIT: Homodimer. The monomeric form is inactive while the homodimer
CC is active (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:22127294}. Golgi apparatus
CC {ECO:0000269|PubMed:22127294}. Lysosome {ECO:0000269|PubMed:22127294}.
CC Secreted {ECO:0000269|PubMed:22127294}. Note=Secretion is stimulated by
CC TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin.
CC -!- INDUCTION: During regeneration of liver. {ECO:0000269|PubMed:12390252}.
CC -!- PTM: N-glycosylated. The secreted form is modified by hybrid or complex
CC type oligosaccharide chains. {ECO:0000269|PubMed:22127294}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
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DR EMBL; AF131077; AAF36518.1; -; mRNA.
DR EMBL; AF097723; AAC72384.1; -; mRNA.
DR EMBL; BC070884; AAH70884.1; -; mRNA.
DR RefSeq; NP_113828.1; NM_031640.1.
DR RefSeq; XP_008763639.1; XM_008765417.2.
DR AlphaFoldDB; Q6IRK9; -.
DR SMR; Q6IRK9; -.
DR IntAct; Q6IRK9; 1.
DR STRING; 10116.ENSRNOP00000008211; -.
DR MEROPS; M28.014; -.
DR GlyGen; Q6IRK9; 3 sites.
DR iPTMnet; Q6IRK9; -.
DR PhosphoSitePlus; Q6IRK9; -.
DR PaxDb; Q6IRK9; -.
DR PRIDE; Q6IRK9; -.
DR Ensembl; ENSRNOT00000008211; ENSRNOP00000008211; ENSRNOG00000005931.
DR GeneID; 58952; -.
DR KEGG; rno:58952; -.
DR UCSC; RGD:628610; rat.
DR CTD; 10404; -.
DR RGD; 628610; Cpq.
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT00390000018110; -.
DR HOGENOM; CLU_033697_1_1_1; -.
DR InParanoid; Q6IRK9; -.
DR OMA; LFMNEEN; -.
DR OrthoDB; 792624at2759; -.
DR PhylomeDB; Q6IRK9; -.
DR TreeFam; TF323248; -.
DR PRO; PR:Q6IRK9; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000005931; Expressed in liver and 19 other tissues.
DR Genevisible; Q6IRK9; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA: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; IDA:UniProtKB.
DR GO; GO:0006590; P:thyroid hormone generation; IDA:UniProtKB.
DR GO; GO:0042246; P:tissue regeneration; IEP:RGD.
DR InterPro; IPR039866; CPQ.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12053; PTHR12053; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Hydrolase; Lysosome; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..44
FT /evidence="ECO:0000250"
FT /id="PRO_0000312264"
FT CHAIN 45..472
FT /note="Carboxypeptidase Q"
FT /id="PRO_0000312265"
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 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 114
FT /note="E -> G (in Ref. 2; AAC72384)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="M -> T (in Ref. 1; AAF36518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52042 MW; 1ABB7863A99CD8CA CRC64;
MRFLFFLFVA VVHLFSLGSG KAIYKSGVSQ RTFQEIKEEI ANYEDVAKAI INLAVYGKYQ
NRSYERLGLL VDTVGPRLSG SKNLEKAIQI MYQNLQQDGL ENVHLEQVRI PHWERGEESA
VMVVPRIHKL AILGLGGSIG TPPEGITAEV LVVASFVELQ RRASEARGKI VVYNQPYTDY
GKTVQYRERG AVEAAKVGAV ASLIRSVASF SIYSPHTGHQ GYQDGVPKIP TACITIEDAE
MMSRMASRGD KIVIHLKMGA KTYPDTDSFN TVAEITGSKY PEEVVLVSGH LDSWDVGQGA
LDDGGGAFIS WEALSLVKDL GLRPKRTLRL VLWTAEEQGG VGASQYYELH KANISKYSLV
MEADSGTFLP TGLQFTGSDK ARAIMKEVMS LLQPLNITKV FNDAEGTDIN FWIQAGVPGA
SLRDDLYKYF FFHHSHGDTM TAMDPKQMNV AAAVWAVVAY VVADMEEMLP RS
