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Database: UniProt
Entry: A0A2R9CD62_PANPA
LinkDB: A0A2R9CD62_PANPA
Original site: A0A2R9CD62_PANPA 
ID   A0A2R9CD62_PANPA        Unreviewed;       419 AA.
AC   A0A2R9CD62;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Carboxypeptidase A2 {ECO:0000313|Ensembl:ENSPPAP00000039881.1};
GN   Name=CPA2 {ECO:0000313|Ensembl:ENSPPAP00000039881.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000039881.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000039881.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000039881.1}
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; AJFE02042872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003813529.1; XM_003813481.2.
DR   AlphaFoldDB; A0A2R9CD62; -.
DR   STRING; 9597.ENSPPAP00000039881; -.
DR   Ensembl; ENSPPAT00000062793.1; ENSPPAP00000039881.1; ENSPPAG00000042610.1.
DR   GeneID; 100983954; -.
DR   KEGG; pps:100983954; -.
DR   CTD; 1358; -.
DR   GeneTree; ENSGT00940000160121; -.
DR   OMA; DTIYSWM; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000240080; Chromosome 7.
DR   Bgee; ENSPPAG00000042610; Expressed in testis.
DR   GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03870; M14_CPA; 1.
DR   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR034248; CPA_M14_CPD.
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   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 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:UP000240080};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..419
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015306507"
FT   DOMAIN          170..192
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
FT   DOMAIN          306..316
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   419 AA;  46984 MW;  4A5FE2BD6DEF1EFD CRC64;
     MAMRLILFFG ALFGHIYSLE TFVGDQVLEI VPSNEEQIKN LLQLEAQEHL QLDFWKSPTT
     PGETAHVRVP FVNVQAVKVF LESQGIAYSI MIEDVQVLLD KENEEMLFNR RRERSGNFNF
     GAYHTLEEIS QEMDNLVAEH PGLVSKVNIG SSFENRPMNV LKFSTGGDKP AIWLDAGIHA
     REWVTQATAL WTANKIVSDY GKDPSITSIL DTLDIFLLPV TNPDGYVFSQ TKNRMWRKTR
     SKVSGSLCVG VDPNRNWDAG FGGPGASSNP CSDSCHGPSA NSEVEVKSIV DFIKSHGKVK
     AFITLHSYSQ LLMFPYGYKC TKLDDFDELS EVAQKAAQSL RSLHGTKYKV GPICSVIYQA
     SGGSIDWSYD YGIKYSFAFE LRDTGRYGFL LPARQILPTA EETWLGLKAI MEHVRDHPY
//
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