Q9Y646 (CBPQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carboxypeptidase Q
EC=3.4.17.-

Alternative name(s):
Lysosomal dipeptidase
Plasma glutamate carboxypeptidase

Gene names

Name:	CPQ
Synonyms:	LCH1, PGCP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	Homodimer. The monomeric form is inactive while the homodimer is active. Ref.7 Ref.10
Subcellular location	Endoplasmic reticulum. Golgi apparatus. Lysosome By similarity. Secreted. Note: Secretion is stimulated by TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin By similarity. Ref.1
Tissue specificity	Mainly detected in blood plasma. Abundant in placenta and kidney. Present at low level in muscles, liver and skin fibroblasts. Not detected in brain or white blood cells (at protein level). Ref.1
Induction	Up-regulated in the majority of hepatitis C virus-associated hepatocellular carcinoma. Ref.8
Post-translational modification	N-glycosylated. The secreted form is modified by hybrid or complex type oligosaccharide chains By similarity. Ref.1
Sequence similarities	Belongs to the peptidase M28 family.
Sequence caution	The sequence AAD31418.1 differs from that shown. Reason: Frameshift at position 446.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Golgi apparatus Lysosome Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	peptide catabolic process Inferred from direct assay Ref.1. Source: UniProtKB proteolysis Inferred from direct assay Ref.1. Source: UniProtKB thyroid hormone generation Inferred from sequence or structural similarity. Source: UniProtKB tissue regeneration Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from direct assay Ref.1. Source: UniProtKB lysosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	carboxypeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallodipeptidase activity Inferred from direct assay Ref.1. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 44	24			PRO_5000055941
	Chain	45 – 472	428	Carboxypeptidase Q		PRO_5000055942
Sites
	Active site	336	1	Nucleophile By similarity
	Metal binding	290	1	Zinc 2 By similarity
	Metal binding	302	1	Zinc 1 By similarity
	Metal binding	302	1	Zinc 2 By similarity
	Metal binding	337	1	Zinc 1 By similarity
	Metal binding	364	1	Zinc 2 By similarity
	Metal binding	434	1	Zinc 1 By similarity
Amino acid modifications
	Glycosylation	61	1	N-linked (GlcNAc...) Potential
	Glycosylation	179	1	N-linked (GlcNAc...) Ref.9 Ref.11
	Glycosylation	353	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	356	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	396	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	138	1	S → N. Corresponds to variant rs34088584 [ dbSNP | Ensembl ].		VAR_037466
Experimental info
	Sequence conflict	37	1	K → E in BAC11423. Ref.4
	Sequence conflict	117	1	E → G in BAC11423. Ref.4
	Sequence conflict	385	1	M → V in BAC11423. Ref.4
	Sequence conflict	446	1	K → Q in AAD31418. Ref.1
	Sequence conflict	449	1	N → D in AAD31418. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9Y646 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: EB6CBD2149E042BF	FASTA	472	51,888
	10 20 30 40 50 60 MKFLIFAFFG GVHLLSLCSG KAICKNGISK RTFEEIKEEI ASCGDVAKAI INLAVYGKAQ 70 80 90 100 110 120 NRSYERLALL VDTVGPRLSG SKNLEKAIQI MYQNLQQDGL EKVHLEPVRI PHWERGEESA 130 140 150 160 170 180 VMLEPRIHKI AILGLGSSIG TPPEGITAEV LVVTSFDELQ RRASEARGKI VVYNQPYINY 190 200 210 220 230 240 SRTVQYRTQG AVEAAKVGAL ASLIRSVASF SIYSPHTGIQ EYQDGVPKIP TACITVEDAE 250 260 270 280 290 300 MMSRMASHGI KIVIQLKMGA KTYPDTDSFN TVAEITGSKY PEQVVLVSGH LDSWDVGQGA 310 320 330 340 350 360 MDDGGGAFIS WEALSLIKDL GLRPKRTLRL VLWTAEEQGG VGAFQYYQLH KVNISNYSLV 370 380 390 400 410 420 MESDAGTFLP TGLQFTGSEK ARAIMEEVMS LLQPLNITQV LSHGEGTDIN FWIQAGVPGA 430 440 450 460 470 SLLDDLYKYF FFHHSHGDTM TVMDPKQMNV AAAVWAVVSY VVADMEEMLP RS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification, cDNA cloning, and expression of a new human blood plasma glutamate carboxypeptidase homologous to N-acetyl-aspartyl-alpha-glutamate carboxypeptidase/prostate-specific membrane antigen." Gingras R., Richard C., El-Alfy M., Morales C.R., Potier M., Pshezhetsky A.V. J. Biol. Chem. 274:11742-11750(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-75, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
[2]	"Cloning of the human aminopeptidase gene." Liu C.H., Lin B.Y., Chang L.Y. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
[4]	"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries." Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T. DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[7]	"Purification and primary structure determination of human lysosomal dipeptidase." Dolenc I., Mihelic M. Biol. Chem. 384:317-320(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 45-74, HOMODIMERIZATION.
[8]	"Identification of novel tumor markers in hepatitis C virus-associated hepatocellular carcinoma." Smith M.W., Yue Z.N., Geiss G.K., Sadovnikova N.Y., Carter V.S., Boix L., Lazaro C.A., Rosenberg G.B., Bumgarner R.E., Fausto N., Bruix J., Katze M.G. Cancer Res. 63:859-864(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[9]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-179; ASN-353 AND ASN-356, MASS SPECTROMETRY. Tissue: Plasma.
[10]	"Presence of the propeptide on recombinant lysosomal dipeptidase controls both activation and dimerization." Dolenc I., Pain R., Turk V. Biol. Chem. 388:47-51(2007) [PubMed] [Europe PMC] [Abstract] Cited for: HOMODIMERIZATION.
[11]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-179, MASS SPECTROMETRY. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF119386 mRNA. Translation: AAD31418.1. Frameshift. AF107833 mRNA. Translation: AAD43213.1. AF107834 mRNA. Translation: AAD43214.1. AK075132 mRNA. Translation: BAC11423.1. AK315447 mRNA. Translation: BAG37835.1. CH471060 Genomic DNA. Translation: EAW91757.1. BC020689 mRNA. Translation: AAH20689.1.
IPI	IPI00005794.
RefSeq	NP_057218.1. NM_016134.2.
UniGene	Hs.156178.
3D structure databases
ProteinModelPortal	Q9Y646.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000220763.
Protein family/group databases
MEROPS	M28.014.
PTM databases
PhosphoSite	Q9Y646.
Polymorphism databases
DMDM	74735298.
Proteomic databases
PaxDb	Q9Y646.
PRIDE	Q9Y646.
Protocols and materials databases
DNASU	10404.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000220763; ENSP00000220763; ENSG00000104324.
GeneID	10404.
KEGG	hsa:10404.
UCSC	uc003yhw.3. human.
Organism-specific databases
CTD	10404.
GeneCards	GC08P097657.
HGNC	HGNC:16910. CPQ.
HPA	HPA023235. HPA024490.
neXtProt	NX_Q9Y646.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2234.
HOGENOM	HOG000295607.
HOVERGEN	HBG105014.
OMA	GGPDVSM.
Gene expression databases
ArrayExpress	Q9Y646.
Bgee	Q9Y646.
Genevestigator	Q9Y646.
Family and domain databases
InterPro	IPR007484. Peptidase_M28. [Graphical view]
Pfam	PF04389. Peptidase_M28. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10404.
NextBio	39428.

Entry information

Entry name

CBPQ_HUMAN

Accession

Primary (citable) accession number: Q9Y646
Secondary accession number(s): B2RD88 , Q8NBZ1, Q9UNM8, Q9Y5X6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.