ID A0A3Q3AVM9_KRYMA Unreviewed; 416 AA.
AC A0A3Q3AVM9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Carboxypeptidase B {ECO:0000256|ARBA:ARBA00039334};
DE EC=3.4.17.2 {ECO:0000256|ARBA:ARBA00039143};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000015574.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000015574.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal lysine or arginine amino
CC acid.; EC=3.4.17.2; Evidence={ECO:0000256|ARBA:ARBA00036114};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Zymogen granule lumen
CC {ECO:0000256|ARBA:ARBA00037795}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR RefSeq; XP_017262312.1; XM_017406823.1.
DR AlphaFoldDB; A0A3Q3AVM9; -.
DR STRING; 37003.ENSKMAP00000015574; -.
DR Ensembl; ENSKMAT00000015799.1; ENSKMAP00000015574.1; ENSKMAG00000011653.1.
DR GeneID; 108230520; -.
DR KEGG; kmr:108230520; -.
DR CTD; 1360; -.
DR GeneTree; ENSGT00940000157819; -.
DR OMA; KYNTWSD; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
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:SF20; CARBOXYPEPTIDASE B; 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:UP000264800};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..416
FT /note="Carboxypeptidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018684028"
FT DOMAIN 166..188
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 303..313
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 416 AA; 46344 MW; 0FF12A417BC7E234 CRC64;
MKLLLVFGLV AVALADVTRF EGDKVLRLKP KLNEHVTFIK ELANSIEVDM WSPESSEQVT
TDIEVDIHIP AKYLDIVYTM LGQSDMEHQI LIEDVQAAIE GQADSGGSPR AHSYTKYNTW
SDIQNWMNSI SSSNPNLISK QVIGNTYEGR PMTVLKLGKA SSSAKPAIFM DCGIHAREWI
SPAFCQWFVK EALSTYGSDS QMTSLLNQMD VFVLPVFNID GYAYTHTNNR MWRKTRSSRS
GSSCVGADPN RNFDAGWCTL GASSNPCSDT FCGYSPESEI EVKNVADFIR RNKSVIKAYI
TMHSYSQLLL FPYSYKYGLA ADHSELLKVA QGASAALQSL YGTRYTSGPG ATTIYPAAGG
SDDWAYDLGV KYSYTFELRD TGRYGFLLPE SQIKPTCEET MLAFKYIAAY VQKNLY
//
