CBPQ_MOUSE
ID CBPQ_MOUSE Reviewed; 470 AA.
AC Q9WVJ3; O70216; Q3U8N9;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Carboxypeptidase Q;
DE EC=3.4.17.-;
DE AltName: Full=Hematopoietic lineage switch 2;
DE AltName: Full=Plasma glutamate carboxypeptidase;
DE Flags: Precursor;
GN Name=Cpq; Synonyms=Hls2, Pgcp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Williams J.H., Chan C.-Y., Klinken S.P.;
RT "Hematopoietic lineage switch 2 (HLS2), a novel mRNA species induced during
RT an erythroid to myeloid lineage switch.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Liu C.H., Lin B.Y., Chang L.Y.;
RT "Cloning of the mouse aminopeptidase gene.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Olfactory bulb, Urinary bladder, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17945.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC17945.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF009513; AAC17945.1; ALT_SEQ; mRNA.
DR EMBL; AF107835; AAD43215.1; -; mRNA.
DR EMBL; AK032972; BAC28105.1; -; mRNA.
DR EMBL; AK075686; BAC35891.1; -; mRNA.
DR EMBL; AK135096; BAE22419.1; -; mRNA.
DR EMBL; AK137164; BAE23259.1; -; mRNA.
DR EMBL; AK152139; BAE30978.1; -; mRNA.
DR EMBL; AK152145; BAE30982.1; -; mRNA.
DR EMBL; BC037067; AAH37067.1; -; mRNA.
DR CCDS; CCDS27414.1; -.
DR RefSeq; NP_061225.2; NM_018755.2.
DR RefSeq; NP_788262.1; NM_176073.4.
DR AlphaFoldDB; Q9WVJ3; -.
DR SMR; Q9WVJ3; -.
DR STRING; 10090.ENSMUSP00000039046; -.
DR MEROPS; M28.014; -.
DR GlyConnect; 2187; 4 N-Linked glycans (1 site).
DR GlyGen; Q9WVJ3; 3 sites, 4 N-linked glycans (1 site).
DR PhosphoSitePlus; Q9WVJ3; -.
DR CPTAC; non-CPTAC-5580; -.
DR jPOST; Q9WVJ3; -.
DR MaxQB; Q9WVJ3; -.
DR PaxDb; Q9WVJ3; -.
DR PeptideAtlas; Q9WVJ3; -.
DR PRIDE; Q9WVJ3; -.
DR ProteomicsDB; 281231; -.
DR Antibodypedia; 12985; 121 antibodies from 26 providers.
DR DNASU; 54381; -.
DR Ensembl; ENSMUST00000042167; ENSMUSP00000039046; ENSMUSG00000039007.
DR Ensembl; ENSMUST00000228916; ENSMUSP00000154400; ENSMUSG00000039007.
DR GeneID; 54381; -.
DR KEGG; mmu:54381; -.
DR UCSC; uc007vla.1; mouse.
DR CTD; 10404; -.
DR MGI; MGI:1889205; Cpq.
DR VEuPathDB; HostDB:ENSMUSG00000039007; -.
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT00390000018110; -.
DR HOGENOM; CLU_033697_1_1_1; -.
DR InParanoid; Q9WVJ3; -.
DR OMA; LFMNEEN; -.
DR OrthoDB; 792624at2759; -.
DR PhylomeDB; Q9WVJ3; -.
DR TreeFam; TF323248; -.
DR BioGRID-ORCS; 54381; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cpq; mouse.
DR PRO; PR:Q9WVJ3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9WVJ3; protein.
DR Bgee; ENSMUSG00000039007; Expressed in epithelium of lens and 222 other tissues.
DR ExpressionAtlas; Q9WVJ3; baseline and differential.
DR Genevisible; Q9WVJ3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
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 1: Evidence at protein 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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..42
FT /evidence="ECO:0000250"
FT /id="PRO_0000312260"
FT CHAIN 43..470
FT /note="Carboxypeptidase Q"
FT /id="PRO_0000312261"
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 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 167
FT /note="K -> E (in Ref. 3; BAE30978)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..292
FT /note="Missing (in Ref. 1; AAC17945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 51813 MW; 0F3490681691866A CRC64;
MRSLFFLFIV HLLALGSGKA VFKNGVSQRT FREIKEEIAN YEDVAKAIIN LAVYGKYQNR
SYERLGLLVD TVGPRLSGSK NLEKAIQIMY QNLQQDGLEN VHLEQVRIPH WERGEESAVM
LEPRIHKMAI LGLGSSIGTP PGGITAEVLV VASFDELQRR ASEARGKIIV YNQPYTGYEK
TVQYRVQGAV EAAKVGAVAS LIQSVASFSI YSPHTGIQKY QDGVPKIPTA CITVEDAEMM
SRMASRGNKI VIHLEMGAKT YPDTDSFNTV AEITGSMYPE EVVLVSGHLD SWDVGQGALD
DGGGAFISWE ALSLVKDLGL RPKRTLRLVL WTAEEQGGIG ASQYYELHKA NISKYSLVME
ADSGTFLPTG LQFTGSDKAR AIMKEVMNLL QPLNVTKVFS NGEGTDINFW IQAGVPGASL
RDDLYKYFFF HHSHGDTMTV MDPKQMNVAA AVWAVVAYVV ADMDEMLPRS
