CBPZ_MOUSE
ID CBPZ_MOUSE Reviewed; 654 AA.
AC Q8R4V4; G3X945;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Carboxypeptidase Z;
DE Short=CPZ;
DE EC=3.4.17.-;
DE Flags: Precursor;
GN Name=Cpz;
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].
RC STRAIN=NMRI;
RX PubMed=12944424; DOI=10.1242/dev.00686;
RA Moeller C., Swindell E.C., Kispert A., Eichele G.;
RT "Carboxypeptidase Z (CPZ) modulates Wnt signaling and regulates the
RT development of skeletal elements in the chicken.";
RL Development 130:5103-5111(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves substrates with C-terminal arginine residues.
CC Probably modulates the Wnt signaling pathway, by cleaving some
CC undefined protein. May play a role in cleavage during prohormone
CC processing (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC -!- ACTIVITY REGULATION: Inhibited by 2-mercaptomethyl-3-
CC guanidinoethylthiopropanoic acid (MGTA) and
CC guanidinoethylmercaptosuccinic acid (GEMSA). Inhibited by chelating
CC agents such as EDTA and EGTA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; AF356844; AAM00219.1; -; mRNA.
DR EMBL; AC116705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466524; EDL37485.1; -; Genomic_DNA.
DR CCDS; CCDS19229.1; -.
DR RefSeq; NP_694747.2; NM_153107.2.
DR AlphaFoldDB; Q8R4V4; -.
DR SMR; Q8R4V4; -.
DR STRING; 10090.ENSMUSP00000039804; -.
DR MEROPS; M14.012; -.
DR GlyGen; Q8R4V4; 2 sites.
DR PhosphoSitePlus; Q8R4V4; -.
DR MaxQB; Q8R4V4; -.
DR PaxDb; Q8R4V4; -.
DR PRIDE; Q8R4V4; -.
DR ProteomicsDB; 281410; -.
DR Antibodypedia; 22804; 64 antibodies from 22 providers.
DR DNASU; 242939; -.
DR Ensembl; ENSMUST00000038676; ENSMUSP00000039804; ENSMUSG00000036596.
DR GeneID; 242939; -.
DR KEGG; mmu:242939; -.
DR UCSC; uc008xdt.1; mouse.
DR CTD; 8532; -.
DR MGI; MGI:88487; Cpz.
DR VEuPathDB; HostDB:ENSMUSG00000036596; -.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000156391; -.
DR HOGENOM; CLU_006722_5_1_1; -.
DR InParanoid; Q8R4V4; -.
DR OMA; RCAHIAK; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; Q8R4V4; -.
DR TreeFam; TF315592; -.
DR BioGRID-ORCS; 242939; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8R4V4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R4V4; protein.
DR Bgee; ENSMUSG00000036596; Expressed in diaphysis of femur and 94 other tissues.
DR ExpressionAtlas; Q8R4V4; baseline and differential.
DR Genevisible; Q8R4V4; MM.
DR GO; GO:0031012; C:extracellular matrix; TAS:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd03867; M14_CPZ; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR034239; M14_CPZ_CPD.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS50038; FZ; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Secreted; Signal; Wnt signaling pathway; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..654
FT /note="Carboxypeptidase Z"
FT /id="PRO_0000252457"
FT DOMAIN 43..165
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 596..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 477
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 56..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 98..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 123..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 127..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 180
FT /note="P -> A (in Ref. 1; AAM00219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 654 AA; 73721 MW; F437569D31BE47C4 CRC64;
MPTMPLLLAA LAALAVLALA ARPSPSCSPG PDPSGKCQRL VYTHSATCVD LHLRTCADAA
YNHTSFPTPL EHRSWEAVES SPEYMLLGVI HFLLEGQCNP DLRLLGCSVL APRCEGGHTQ
RPCRHVCEGL REACQPAFDA IDMAWPYFLD CAQYFAPEEE GCYDPLEELR GELDVEEALP
SGLPPTFIRF AHHSYAQMVR VLKRTAARCS QVAKTYSIGR SFEGKDLVVI EFSSRPGQHE
LMEPEVKLIG NIHGNEVAGR EVLIYLAQYL CSEYLLGNPR IQRLLNTTRI HLLPSMNPDG
YEVAAAEGAG YNGWTSGRQN AQNLDLNRNF PDLTSEYYRL ASTRGVRTDH IPISQYYWWG
KVAPETKAIM KWIQTIPFVL SASLHGGDLV VSYPFDFSKN PHEKKMFSPT PDEKMFKLLA
RAYADVHPMM MDRSENRCGG NFLKRGSIIN GADWYSFTGG MSDFNYLHTN CFEITVELGC
VKFPPEEALY GLWQQNKEPL LNFLEMVHRG IKGMVTDKYG KPVKNARILV KGIRHDVTTA
PDGDYWRLLP PGSHIVIAQA PGYSKVMKRV TIPLRMKKAG RVDFILHPLA TGPKNFLPGP
SRALPRFQDP QREPTQMDFE PPRARRQPAS GSKPWWWAYF TSLSPYKPRW LLKY
