CBPZ_CHICK
ID CBPZ_CHICK Reviewed; 647 AA.
AC Q8QGP3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Carboxypeptidase Z;
DE Short=CPZ;
DE Short=cCPZ;
DE EC=3.4.17.-;
DE Flags: Precursor;
GN Name=CPZ;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH WNT4.
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).
CC -!- FUNCTION: Cleaves substrates with C-terminal arginine residues.
CC Modulates the Wnt signaling pathway, probably by cleaving some
CC undefined protein. Regulates the development of skeletal elements
CC during development, probably by activating WNT4.
CC {ECO:0000269|PubMed:12944424}.
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 -!- SUBUNIT: Interacts with WNT4 vie its FZ domain.
CC {ECO:0000269|PubMed:12944424}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In the early embryo it is initially expressed
CC throughout the somites and subsequently becomes restricted to the
CC sclerotome. Expressed in somites, paraxial head mesoderm and apical
CC ectodermal ridge. {ECO:0000269|PubMed:12944424}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; AF351205; AAL84280.1; -; mRNA.
DR AlphaFoldDB; Q8QGP3; -.
DR SMR; Q8QGP3; -.
DR STRING; 9031.ENSGALP00000029089; -.
DR MEROPS; M14.012; -.
DR PaxDb; Q8QGP3; -.
DR PRIDE; Q8QGP3; -.
DR VEuPathDB; HostDB:geneid_395266; -.
DR eggNOG; KOG2649; Eukaryota.
DR InParanoid; Q8QGP3; -.
DR PhylomeDB; Q8QGP3; -.
DR Proteomes; UP000000539; 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; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS50038; FZ; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal;
KW Wnt signaling pathway; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..647
FT /note="Carboxypeptidase Z"
FT /id="PRO_0000252459"
FT DOMAIN 35..157
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT ACT_SITE 469
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 48..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 90..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 115..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 119..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 647 AA; 73919 MW; 8624E514B6E9F514 CRC64;
MVPSLLLLLT GLFRATEPAP RCETGQETLG QCQTAQKAKC VDISLSSCTD VTYTQTMYPN
FLDQKSREVI EYSSEYILIS VLHNLLQGEC NPDLRLLGCS VLAPQCEKDK VIKPCRHVCE
NLKKNCLSAF DAIDMAWPYF LDCDRFFAGE EEGCFDPLAK LRGEVAVEED LPSDFPATFI
QFKHHSYSQM VSTLKKTASR CSHIATTYSI GRSFEGKDLF VIEFSTKPGH HELLKPEFKY
IGNMHGNEVV GKELLYTLRS ICVQKYLLGN PRIQTLINNT RIHLLPSLNP DGYERAAEEG
AGYNGWVIGR QTAQNLDLNR NFPDLTSEAY RRAGIRGARL DHIPIPQSYW WGKVAPETKA
VMKWMRSIPF VLSASLHGGE LVVTYPYDYS RHPMEEKEFS PTPDEKMFKM LAKAYADAHP
VISDRSEHRC GGNFVKRGGI INGAEWYSFT GGMADFNYLH TNCFEVTVEV GCEKFPLEEE
LFTIWHENRD ALLNYMEMVH RGIKGIVSDK FGNPIKNARI SVRGIQHDIT TAADGDYWRL
LPPGTYIVTA QAMGYTKVMK RVTLPIKMKR AGRVDFVLRP IEIWPNKLLR RPMEDMYDQY
DPLELFDPHA QHAQARGGSQ QVREKPWWWS YFSSLDLHKP LWLLKQH
