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Protein

Carboxypeptidase Z

Gene

Cpz

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing (By similarity).By similarity

Cofactori

Zn2+By similarity

Enzyme regulationi

Inhibited by 2-mercaptomethyl-3-guanidinoethylthiopropanoic acid (MGTA) and guanidinoethylmercaptosuccinic acid (GEMSA). Inhibited by chelating agents such as EDTA and EGTA (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi251 – 2511Zinc; catalyticBy similarity
Metal bindingi254 – 2541Zinc; catalyticBy similarity
Metal bindingi383 – 3831Zinc; catalyticBy similarity
Active sitei475 – 4751Proton donor/acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM14.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase Z (EC:3.4.17.-)
Short name:
CPZ
Gene namesi
Name:Cpz
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620496. Cpz.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 652632Carboxypeptidase ZPRO_0000252458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 112PROSITE-ProRule annotation
Disulfide bondi54 ↔ 105PROSITE-ProRule annotation
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi96 ↔ 132PROSITE-ProRule annotation
Disulfide bondi121 ↔ 160PROSITE-ProRule annotation
Disulfide bondi125 ↔ 149PROSITE-ProRule annotation
Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO54858.

Expressioni

Tissue specificityi

Abundantly expressed in the placenta, with low to moderate levels in the brain, lung, thymus and kidney.

Inductioni

By Alachlor.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012109.

Structurei

3D structure databases

ProteinModelPortaliO54858.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 163123FZPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated
Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
HOGENOMiHOG000232185.
HOVERGENiHBG003410.
InParanoidiO54858.
KOiK13022.
OrthoDBiEOG7B8S32.
PhylomeDBiO54858.
TreeFamiTF315592.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR020067. Frizzled_dom.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF01392. Fz. 1 hit.
PF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00063. FRI. 1 hit.
SM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
SSF63501. SSF63501. 1 hit.
PROSITEiPS00133. CARBOXYPEPT_ZN_2. 1 hit.
PS50038. FZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O54858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTTPLLLAA LAALAALAVA AYPSCSPGPD PSGKCQRLAS THSATCVDLH
60 70 80 90 100
LRTCADAAYN HTSFPTPLEH RSWEAVEASP EYTLLGVLHF LLEGQCNPDL
110 120 130 140 150
RLLGCSVLAP RCQGGHTQRP CRRVCEGLRE ACQPAFDAID MAWPYFLDCT
160 170 180 190 200
QYFAPEEEGC YDPLEQLRGE LDVEEALPSG LPPTFIRFAH HSYAQMVRVL
210 220 230 240 250
KRTAARCSQV AKTYSIGRSF EGKDLVVIEF SSRPGQHELM EPEVKLIGNI
260 270 280 290 300
HGNEVAGREI LIYLAQYLCS EYLLGNPRIQ RLLNTTRIHL LPSMNPDGYE
310 320 330 340 350
VAAAEGAGYN GWTSGRQNAQ NLDLNRNFPD LTSEYYRLAS TRGVRTDHIP
360 370 380 390 400
ISQYYWWGKV APETKAIMKW IQTIPFVLSA SLHGGDLVVS YPFDFSKHPH
410 420 430 440 450
EEKMFSPTPD EKMFKLLARA YADVHPMMMD RSENRCGGNF LKRGSIINGA
460 470 480 490 500
DWYSFTGGMS DFNYLHTNCF EITVELGCVK FPPEEALYGL WQHNKEPLLN
510 520 530 540 550
FLEMVHRGIK GVVTDKYGKP VKNARILVKG IRHDVTTAPD GDYWRLLPPG
560 570 580 590 600
SHIVIAQAPG YSKVMKRVTI PLRMKRAGRV DFILQPLGTG PKNFLPGPSR
610 620 630 640 650
ALPRSLDPQG APAQLDFEPP RARRQPASGS KPWWWAYFTS LSPHKPRWLL

KY
Length:652
Mass (Da):73,082
Last modified:June 1, 1998 - v1
Checksum:iBE085394B91A978C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231P → S in AAC04669 (PubMed:9570147).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017637 mRNA. Translation: AAC04668.1.
AF017638 mRNA. Translation: AAC04669.1.
RefSeqiNP_113954.1. NM_031766.1.
UniGeneiRn.11056.

Genome annotation databases

GeneIDi83575.
KEGGirno:83575.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017637 mRNA. Translation: AAC04668.1.
AF017638 mRNA. Translation: AAC04669.1.
RefSeqiNP_113954.1. NM_031766.1.
UniGeneiRn.11056.

3D structure databases

ProteinModelPortaliO54858.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012109.

Protein family/group databases

MEROPSiM14.012.

Proteomic databases

PaxDbiO54858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi83575.
KEGGirno:83575.

Organism-specific databases

CTDi8532.
RGDi620496. Cpz.

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
HOGENOMiHOG000232185.
HOVERGENiHBG003410.
InParanoidiO54858.
KOiK13022.
OrthoDBiEOG7B8S32.
PhylomeDBiO54858.
TreeFamiTF315592.

Miscellaneous databases

NextBioi616081.
PROiO54858.

Family and domain databases

Gene3Di1.10.2000.10. 1 hit.
2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR020067. Frizzled_dom.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF01392. Fz. 1 hit.
PF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00063. FRI. 1 hit.
SM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
SSF63501. SSF63501. 1 hit.
PROSITEiPS00133. CARBOXYPEPT_ZN_2. 1 hit.
PS50038. FZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequence analysis, and distribution of rat metallocarboxypeptidase Z."
    Xin X., Day R., Dong W., Lei Y., Fricker L.D.
    DNA Cell Biol. 17:311-319(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Buffalo.
  2. "Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues."
    Novikova E.G., Reznik S.E., Varlamov O., Fricker L.D.
    J. Biol. Chem. 275:4865-4870(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  3. "Genomic analysis of alachlor-induced oncogenesis in rat olfactory mucosa."
    Genter M.B., Burman D.M., Vijayakumar S., Ebert C.L., Aronow B.J.
    Physiol. Genomics 12:35-45(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiCBPZ_RAT
AccessioniPrimary (citable) accession number: O54858
Secondary accession number(s): O54859
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.