Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carboxypeptidase Q

Gene

cpq

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Carboxypeptidase that may play an important role in the hydrolysis of circulating peptides. Catalyzes more efficiently the hydrolysis of dipeptides with unsubstituted terminals into amino acids (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi288Zinc 1By similarity1
Metal bindingi300Zinc 1By similarity1
Metal bindingi300Zinc 2; catalyticBy similarity1
Active sitei334NucleophileBy similarity1
Metal bindingi335Zinc 2; catalyticBy similarity1
Metal bindingi362Zinc 1By similarity1
Metal bindingi432Zinc 2; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionCarboxypeptidase, Hydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

Protein family/group databases

MEROPSiM28.014

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase Q (EC:3.4.17.-)
Alternative name(s):
Plasma glutamate carboxypeptidase
Gene namesi
Name:cpq
Synonyms:pgcp
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-5761579 cpq

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000031226620 – 42By similarityAdd BLAST23
ChainiPRO_000031226743 – 469Carboxypeptidase QAdd BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi59N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi159N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi351N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi394N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein, Zymogen

Interactioni

Subunit structurei

Homodimer. The monomeric form is inactive while the homodimer is active (By similarity).By similarity

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliQ6GQ29
SMRiQ6GQ29
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG105014
KOiK01302

Family and domain databases

InterProiView protein in InterPro
IPR007484 Peptidase_M28
PfamiView protein in Pfam
PF04389 Peptidase_M28, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6GQ29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLILTLLS LYELQLCCGA YNQNIRSQRK FEMIKTEISS YKDVAKSIID
60 70 80 90 100
LAVHGKAQNR SYERLALFVD TVGNRMSGSE NLKTAIAYMY KSLQEDDLDR
110 120 130 140 150
VYLEPVKVPH WERGEESAML LEPRKKSLAI LGLGGSIGTP VEGISAEVIV
160 170 180 190 200
VSSFAELHNR SKEAKGKIVV YNEPFVNYGE TVRYRGSGAV EAAKVGAVAS
210 220 230 240 250
LIRSVTPLSV YSPHTGWQWY ENDVPKIPTA SITVEDAEML SRMASRGLKI
260 270 280 290 300
VIQLKMGAVN HPDADSYNTV AEIVGSKYPE QVVIVSGHLD SWDVGQGAMD
310 320 330 340 350
DGGGAFISWE ALSLIKDLGL RPKRTLRLVL WTGEEQGGVG ASQYYELHKK
360 370 380 390 400
NISNIDLVME SDIGTFMPLG MQFTGKPEAR AIMTEVMQLL QPINITSLYD
410 420 430 440 450
YAEGTDINSW MQAGVPGASL FDDISKYFWF HHSQGDTMTV QDPVWMNLCA
460
AVWTVVSYVV ADMEEMLPR
Length:469
Mass (Da):52,016
Last modified:July 19, 2004 - v1
Checksum:i2F22FC1C09406E63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC072919 mRNA Translation: AAH72919.1
RefSeqiNP_001085551.1, NM_001092082.1
UniGeneiXl.14252

Genome annotation databases

GeneIDi443977
KEGGixla:443977

Similar proteinsi

Entry informationi

Entry nameiCBPQ_XENLA
AccessioniPrimary (citable) accession number: Q6GQ29
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: July 19, 2004
Last modified: May 10, 2017
This is version 50 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program