CBPZ_RAT
ID CBPZ_RAT Reviewed; 652 AA.
AC O54858; O54859;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Carboxypeptidase Z;
DE Short=CPZ;
DE EC=3.4.17.-;
DE Flags: Precursor;
GN Name=Cpz;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Buffalo;
RX PubMed=9570147; DOI=10.1089/dna.1998.17.311;
RA Xin X., Day R., Dong W., Lei Y., Fricker L.D.;
RT "Cloning, sequence analysis, and distribution of rat
RT metallocarboxypeptidase Z.";
RL DNA Cell Biol. 17:311-319(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=10671522; DOI=10.1074/jbc.275.7.4865;
RA Novikova E.G., Reznik S.E., Varlamov O., Fricker L.D.;
RT "Carboxypeptidase Z is present in the regulated secretory pathway and
RT extracellular matrix in cultured cells and in human tissues.";
RL J. Biol. Chem. 275:4865-4870(2000).
RN [3]
RP INDUCTION.
RX PubMed=12419858; DOI=10.1152/physiolgenomics.00120.2002;
RA Genter M.B., Burman D.M., Vijayakumar S., Ebert C.L., Aronow B.J.;
RT "Genomic analysis of alachlor-induced oncogenesis in rat olfactory
RT mucosa.";
RL Physiol. Genomics 12:35-45(2002).
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:0000269|PubMed:10671522}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the placenta, with low to
CC moderate levels in the brain, lung, thymus and kidney.
CC -!- INDUCTION: By Alachlor. {ECO:0000269|PubMed:12419858}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; AF017637; AAC04668.1; -; mRNA.
DR EMBL; AF017638; AAC04669.1; -; mRNA.
DR RefSeq; NP_113954.1; NM_031766.1.
DR AlphaFoldDB; O54858; -.
DR SMR; O54858; -.
DR STRING; 10116.ENSRNOP00000012109; -.
DR MEROPS; M14.012; -.
DR GlyGen; O54858; 2 sites.
DR PhosphoSitePlus; O54858; -.
DR jPOST; O54858; -.
DR PaxDb; O54858; -.
DR GeneID; 83575; -.
DR KEGG; rno:83575; -.
DR CTD; 8532; -.
DR RGD; 620496; Cpz.
DR eggNOG; KOG2649; Eukaryota.
DR InParanoid; O54858; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; O54858; -.
DR TreeFam; TF315592; -.
DR PRO; PR:O54858; -.
DR Proteomes; UP000002494; Unplaced.
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..652
FT /note="Carboxypeptidase Z"
FT /id="PRO_0000252458"
FT DOMAIN 41..163
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 594..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 475
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 54..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 96..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 121..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 125..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CONFLICT 23
FT /note="P -> S (in Ref. 1; AAC04669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 652 AA; 73082 MW; BE085394B91A978C CRC64;
MPTTPLLLAA LAALAALAVA AYPSCSPGPD PSGKCQRLAS THSATCVDLH LRTCADAAYN
HTSFPTPLEH RSWEAVEASP EYTLLGVLHF LLEGQCNPDL RLLGCSVLAP RCQGGHTQRP
CRRVCEGLRE ACQPAFDAID MAWPYFLDCT QYFAPEEEGC YDPLEQLRGE LDVEEALPSG
LPPTFIRFAH HSYAQMVRVL KRTAARCSQV AKTYSIGRSF EGKDLVVIEF SSRPGQHELM
EPEVKLIGNI HGNEVAGREI LIYLAQYLCS EYLLGNPRIQ RLLNTTRIHL LPSMNPDGYE
VAAAEGAGYN GWTSGRQNAQ NLDLNRNFPD LTSEYYRLAS TRGVRTDHIP ISQYYWWGKV
APETKAIMKW IQTIPFVLSA SLHGGDLVVS YPFDFSKHPH EEKMFSPTPD EKMFKLLARA
YADVHPMMMD RSENRCGGNF LKRGSIINGA DWYSFTGGMS DFNYLHTNCF EITVELGCVK
FPPEEALYGL WQHNKEPLLN FLEMVHRGIK GVVTDKYGKP VKNARILVKG IRHDVTTAPD
GDYWRLLPPG SHIVIAQAPG YSKVMKRVTI PLRMKRAGRV DFILQPLGTG PKNFLPGPSR
ALPRSLDPQG APAQLDFEPP RARRQPASGS KPWWWAYFTS LSPHKPRWLL KY
