ID I3MKU4_ICTTR Unreviewed; 375 AA.
AC I3MKU4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Carboxypeptidase O {ECO:0000313|Ensembl:ENSSTOP00000011962.2};
GN Name=CPO {ECO:0000313|Ensembl:ENSSTOP00000011962.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000011962.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000011962.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; AGTP01081186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005335169.1; XM_005335112.1.
DR AlphaFoldDB; I3MKU4; -.
DR STRING; 43179.ENSSTOP00000011962; -.
DR MEROPS; M14.021; -.
DR Ensembl; ENSSTOT00000013348.3; ENSSTOP00000011962.2; ENSSTOG00000013351.3.
DR GeneID; 101963745; -.
DR CTD; 130749; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000161508; -.
DR HOGENOM; CLU_019326_4_1_1; -.
DR InParanoid; I3MKU4; -.
DR OMA; EEQWAGQ; -.
DR OrthoDB; 3540647at2759; -.
DR TreeFam; TF317197; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06247; M14_CPO; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR033850; Carboxypeptidase_O.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF19; CARBOXYPEPTIDASE O; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022645};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..375
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003677013"
FT DOMAIN 100..122
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
SQ SEQUENCE 375 AA; 43244 MW; 4409B73C87CB889B CRC64;
MKPLLGTLYL LGMLVPRGLG YDRSLVQHKN QVVDKTRSLW KNLETYSYNK YHPMEEIYLW
MSQISEKHAE VVTQHLLGMT FEKRPMYYLK ISQPSDNPKK IIWMDCGIHA REWIAPAFCQ
WFVKEILQNY KDNPRINRFL RNLDFYVLPV LNIDGYIYSW TTDRLWRKSR SSHNNGTCFG
SDLNRNFNVS WCSIGASKNC QDLTFCGTEP VSEPETKAVS SFVESKKEDI LCFLTIHSYG
QLILTPYGYT KNKPSNHEEL IQVGQKAANA LKAKHGTNYR VGSSADILYP TSGSSRDWAR
DIGIPYSYTF ELRDNGTEGF LLHETQIQPT CEEAMEAVLS ILDDVYAKYW LSNTATKVTS
TTVLLNLLWL FTSLL
//
