ID A0A3B4FYG9_9CICH Unreviewed; 419 AA.
AC A0A3B4FYG9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carboxypeptidase A2-like {ECO:0000313|Ensembl:ENSPNYP00000015647.1, ECO:0000313|RefSeq:XP_005731590.1};
GN Name=LOC102199360 {ECO:0000313|RefSeq:XP_005731590.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000015647.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000015647.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005731590.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_005731590.1; XM_005731533.2.
DR AlphaFoldDB; A0A3B4FYG9; -.
DR STRING; 303518.ENSPNYP00000015647; -.
DR Ensembl; ENSPNYT00000016048.1; ENSPNYP00000015647.1; ENSPNYG00000011831.1.
DR GeneID; 102199360; -.
DR CTD; 51200; -.
DR GeneTree; ENSGT00940000160121; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; Unplaced.
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 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:SF155; CARBOXYPEPTIDASE A4-RELATED; 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 ECO:0000313|RefSeq:XP_005731590.1};
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:UP000695023};
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..419
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041073622"
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; 47233 MW; CB2FC82A0B68FB00 CRC64;
MKGFWLLLVL VAAAKAEKGF TGDQVIRVNV KSEEQIHLLQ ALETAQEWEV DFWLDPVSTE
LPVDIRVPRF SLIPVKEHLT FHNIPFTVMI ENVQELLDKE KAEMEANQMK ERSTRSLNFG
AYHDLNTIYS WMDTLVADYP NLITKQHIGV SYENRPMYVL KFSTGGYNRP AIWVDTGIHA
REWVTQATGV WTANKIATDY GTDASLTSLL NTMDLYMLIV ANPDGYVFSH TNDRMWRKTR
SVNPGYACRG VDPNRNWDAG FGGPGASSYP CSDSYHGPSA NSEIEVKNVV NLIQSHGNFK
AFISVHSYSQ LLMYPYGYVC SSANHQAELH SVGRAAAQKL TSLYGTAYQV GSICNIIYQA
SGGSIDWSYN SGIKYSFAFE LRDTGRYGFI LPADQIIPTA SETWLALKHI MEYVRDHPY
//