ID A0A2I3RUF3_PANTR Unreviewed; 182 AA.
AC A0A2I3RUF3; A0A2J8QT95;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Carboxypeptidase A2 {ECO:0000313|Ensembl:ENSPTRP00000067952.1};
GN Name=CPA2 {ECO:0000313|Ensembl:ENSPTRP00000067952.1,
GN ECO:0000313|VGNC:VGNC:4317};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000067952.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000067952.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000067952.1}
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; AACZ04061450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3RUF3; -.
DR SMR; A0A2I3RUF3; -.
DR Ensembl; ENSPTRT00000095903.1; ENSPTRP00000067952.1; ENSPTRG00000019693.5.
DR VGNC; VGNC:4317; CPA2.
DR GeneTree; ENSGT00940000160121; -.
DR Proteomes; UP000002277; Chromosome 7.
DR Bgee; ENSPTRG00000019693; Expressed in testis and 1 other cell type or tissue.
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:UniProtKB-KW.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF71; CARBOXYPEPTIDASE A2; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..182
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015081310"
FT DOMAIN 27..100
FT /note="Carboxypeptidase activation peptide"
FT /evidence="ECO:0000259|Pfam:PF02244"
FT DOMAIN 127..166
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 159..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 182 AA; 20832 MW; 6F707DB75CF57A7E CRC64;
MRLILFFGAL FGHIYCLETF VGDQVLEIVP SNEEQIKNLL QLEAQEHLQL DFWKSPTTPG
ETAHVRVPFV NVQAVKVFLE SQGIAYSIMI EDVQVLLDKE NEEMLFNRRR ERSGNFNFGA
YHTLEEISQE MDNLVAEHPG LVSKVNIGSS FENRPMNVLK KSSGRMQKDD GQLNPKPQRQ
TP
//
