ID   F7ILN0_CALJA            Unreviewed;       643 AA.
AC   F7ILN0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Carboxypeptidase Z {ECO:0000313|Ensembl:ENSCJAP00000040020.4};
GN   Name=CPZ {ECO:0000313|Ensembl:ENSCJAP00000040020.4};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000040020.4, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000040020.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000040020.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; F7ILN0; -.
DR   STRING; 9483.ENSCJAP00000040020; -.
DR   Ensembl; ENSCJAT00000042278.5; ENSCJAP00000040020.4; ENSCJAG00000021495.5.
DR   eggNOG; KOG2649; Eukaryota.
DR   GeneTree; ENSGT00940000156391; -.
DR   InParanoid; F7ILN0; -.
DR   TreeFam; TF315592; -.
DR   Proteomes; UP000008225; Chromosome 3.
DR   Bgee; ENSCJAG00000021495; Expressed in ovary and 3 other cell types or tissues.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd03867; M14_CPZ; 1.
DR   CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 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   PANTHER; PTHR11532:SF63; CARBOXYPEPTIDASE Z; 1.
DR   PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
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; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR   PROSITE; PS50038; FZ; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..643
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023855255"
FT   DOMAIN          27..149
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   REGION          584..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        111..135
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   643 AA;  72342 MW;  3E3C379719049C80 CRC64;
     MPPPPPLLLL AVLVAAAARP GCEFDGSLAA TCVDLQLRTC SDAAYNHTTF PTPLQHRSRE
     AVETSSEYIL LSVLHQLLEG QCNPDLRLLG CAVLAPRCEG GRVRRPCRHV CEGLREACQP
     AFDAIDMAWP YFLDCHRYFK REDEGCYDPL EKLRGGLEAD EVLPSGLPPT FIRFSHHSYA
     QMARVLRRTA ARCAHVARTY SIGRSFDGRD LLVIEFSSRP GQHELMEPEV KLIGNIHGNE
     VAGREMLIYL TQYLCSEYLL GNPRIQRLLN TTRIHLLPSM NPDGYEVAAA EGAGYNGWTS
     GRQNAQNLDL NRNFPDLTSE YYRLAGTRSV RSDHIPIPEH YWWGKVAPET KAIMKWMQTI
     PFVLSASLHG GDLVVSYPFD FSKHPQEEKM FSPTPDEKTF KLLSRAYAEV HPMMMDRSEN
     RCGGNFLKRG SIINGADWYS FTGGMSDFNY LHTNCFEITV ELGCVKFPPE EALYTIWQHN
     KESLLNFVET VHRGIKGVVM DKYGKPVKNA RILVKGIRHD ITTAPDGDYW RLLPPGTHIV
     IAQAPGYARL IKKVIIPARM KRAGRVDFIL QPLGVGPKNF LPGLRRTGPH DPLGGASPLG
     EGTEPNPDPL RARRQPSAGG SKPWWWSYFT SLSAHRPRWL LKY
//