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Carboxypeptidase Q (EC 3.4.17.-) (Hematopoietic lineage switch 2 related protein) (Hls2-rp) (Liver annexin-like protein 1) (LAL-1) (Plasma glutamate carboxypeptidase)

 CBPQ_RAT                Reviewed;         472 AA.
Q6IRK9; Q9JLV0; Q9Z1Y1;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
23-MAY-2018, entry version 86.
RecName: Full=Carboxypeptidase Q;
EC=3.4.17.-;
AltName: Full=Hematopoietic lineage switch 2 related protein;
Short=Hls2-rp;
AltName: Full=Liver annexin-like protein 1;
Short=LAL-1;
AltName: Full=Plasma glutamate carboxypeptidase;
Flags: Precursor;
Name=Cpq; Synonyms=Pgcp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=12390252; DOI=10.1046/j.1365-2443.2002.00593.x;
Della Fazia M.A., Piobbico D., Bartoli D., Castelli M.,
Brancorsini S., Viola Magni M., Servillo G.;
"lal-1: a differentially expressed novel gene during proliferation in
liver regeneration and in hepatoma cells.";
Genes Cells 7:1183-1190(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Fischer;
Chen Y., Talmage D.;
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 170-182 AND 262-279, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=22127294; DOI=10.1016/j.biochi.2011.10.018;
Suban D., Zajc T., Renko M., Turk B., Turk V., Dolenc I.;
"Cathepsin C and plasma glutamate carboxypeptidase secreted from
Fischer rat thyroid cells liberate thyroxin from the N-terminus of
thyroglobulin.";
Biochimie 94:719-726(2012).
-!- FUNCTION: Carboxypeptidase that may play an important role in the
hydrolysis of circulating peptides. Catalyzes the hydrolysis of
dipeptides with unsubstituted terminals into amino acids. May play
a role in the liberation of thyroxine hormone from its
thyroglobulin (Tg) precursor. {ECO:0000269|PubMed:22127294}.
-!- SUBUNIT: Homodimer. The monomeric form is inactive while the
homodimer is active (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:22127294}. Golgi apparatus
{ECO:0000269|PubMed:22127294}. Lysosome
{ECO:0000269|PubMed:22127294}. Secreted
{ECO:0000269|PubMed:22127294}. Note=Secretion is stimulated by
TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin.
-!- INDUCTION: During regeneration of liver.
{ECO:0000269|PubMed:12390252}.
-!- PTM: N-glycosylated. The secreted form is modified by hybrid or
complex type oligosaccharide chains.
{ECO:0000269|PubMed:22127294}.
-!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
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EMBL; AF131077; AAF36518.1; -; mRNA.
EMBL; AF097723; AAC72384.1; -; mRNA.
EMBL; BC070884; AAH70884.1; -; mRNA.
RefSeq; NP_113828.1; NM_031640.1.
RefSeq; XP_008763639.1; XM_008765417.2.
UniGene; Rn.17112; -.
ProteinModelPortal; Q6IRK9; -.
SMR; Q6IRK9; -.
IntAct; Q6IRK9; 1.
STRING; 10116.ENSRNOP00000008211; -.
iPTMnet; Q6IRK9; -.
PhosphoSitePlus; Q6IRK9; -.
PaxDb; Q6IRK9; -.
PRIDE; Q6IRK9; -.
Ensembl; ENSRNOT00000008211; ENSRNOP00000008211; ENSRNOG00000005931.
GeneID; 58952; -.
KEGG; rno:58952; -.
UCSC; RGD:628610; rat.
CTD; 10404; -.
RGD; 628610; Cpq.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
GeneTree; ENSGT00390000018110; -.
HOGENOM; HOG000295607; -.
HOVERGEN; HBG105014; -.
InParanoid; Q6IRK9; -.
KO; K01302; -.
OMA; FMNEENG; -.
OrthoDB; EOG091G08CB; -.
PhylomeDB; Q6IRK9; -.
TreeFam; TF323248; -.
PRO; PR:Q6IRK9; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000005931; -.
Genevisible; Q6IRK9; RN.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070573; F:metallodipeptidase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0006590; P:thyroid hormone generation; IDA:UniProtKB.
GO; GO:0042246; P:tissue regeneration; IEP:RGD.
InterPro; IPR007484; Peptidase_M28.
Pfam; PF04389; Peptidase_M28; 1.
1: Evidence at protein level;
Carboxypeptidase; Complete proteome; Direct protein sequencing;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase;
Lysosome; Metal-binding; Metalloprotease; Protease;
Reference proteome; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 44 {ECO:0000250}.
/FTId=PRO_0000312264.
CHAIN 45 472 Carboxypeptidase Q.
/FTId=PRO_0000312265.
ACT_SITE 336 336 Nucleophile. {ECO:0000250}.
METAL 290 290 Zinc 1. {ECO:0000250}.
METAL 302 302 Zinc 1. {ECO:0000250}.
METAL 302 302 Zinc 2; catalytic. {ECO:0000250}.
METAL 337 337 Zinc 2; catalytic. {ECO:0000250}.
METAL 364 364 Zinc 1. {ECO:0000250}.
METAL 434 434 Zinc 2; catalytic. {ECO:0000250}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 114 114 E -> G (in Ref. 2; AAC72384).
{ECO:0000305}.
CONFLICT 245 245 M -> T (in Ref. 1; AAF36518).
{ECO:0000305}.
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


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