ID A0A452FQ10_CAPHI Unreviewed; 647 AA.
AC A0A452FQ10;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Carboxypeptidase Z {ECO:0000313|Ensembl:ENSCHIP00000026300.1};
GN Name=CPZ {ECO:0000313|Ensembl:ENSCHIP00000026300.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000026300.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000026300.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000026300.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR EMBL; LWLT01000006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452FQ10; -.
DR STRING; 9925.ENSCHIP00000026300; -.
DR Ensembl; ENSCHIT00000034162.1; ENSCHIP00000026300.1; ENSCHIG00000022665.1.
DR GeneTree; ENSGT00940000156391; -.
DR Proteomes; UP000291000; Chromosome 6.
DR Bgee; ENSCHIG00000022665; Expressed in skin of neck and 14 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:UP000291000}.
FT DOMAIN 40..162
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 590..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 124..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 647 AA; 72979 MW; AE4E42899922C684 CRC64;
WPSPSLPLLS QLRLNFLSTS APPSPLSSPT FYRKARGRAV CLATCVDLQL QTCSDVTYNR
TAFPTLLQHR TRAAVESSSE YILLSVLHHL LEGQCNPDLR LLGCAVLAPR CEGGRVRRPC
RHVCGALREA CQPAFDAIDM AWPYFLDCGR YFSGPEEGCY DPLEKLRGGL DIEEALPSGY
PPTFIQFTHH SYAQMVRVLR RTAARCAHIS KTYSIGRSFD GRDLLVIEFS SRPGQHELME
PEVKLIGNIH GNEVAGREML IYLAQYLCSE YLLGNPRIQR LLNTTRIHLL PSMNPDGYEV
AAAEGAGYNG WTSGRQNAQN LDLNRNFPDL TSEYYRLASV RGVRSDHIAI PQHYWWGKVA
PETKAVMKWM RAIPFVLSAS LHGGDLVVSY PFDFSKHPQE EKMFSPTPDE KMFKLLARAY
ADVHPMMMDR SENRCGGNFL KRGSIINGAD WYSFTGGMSD FNYLHSNCFE ITVELGCVKF
PPEEALYTIW QHNKEPLLNF VEMVHRGIKG MVMDKFGKPV KNARILVKGI RHAITTAPDG
DYWRLLPPGA HIVIAQAPGY SRVIKKVIIP SRMKRAGRVD FILQPLRTGP QKFLPGSRRG
GLGGEPQEPD QEPLGARRQP TTGGSKPWWW SYFTSLGQHQ PRWLLKY
//
