ID A0A091DQP1_FUKDA Unreviewed; 378 AA.
AC A0A091DQP1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Mast cell carboxypeptidase A {ECO:0000313|EMBL:KFO32778.1};
GN ORFNames=H920_05800 {ECO:0000313|EMBL:KFO32778.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO32778.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO32778.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO32778.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN122131; KFO32778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DQP1; -.
DR STRING; 885580.ENSFDAP00000004300; -.
DR MEROPS; M14.010; -.
DR eggNOG; KOG2650; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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; 2.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF65; MAST CELL CARBOXYPEPTIDASE A; 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|EMBL:KFO32778.1};
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:UP000028990};
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..378
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012181319"
FT DOMAIN 165..187
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 265..275
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 378 AA; 43848 MW; BED9408D07E66CAB CRC64;
MKFILTLSLI TVALGIDPVR FDRDKVFRVK PQDEKQASII KDLAKTNELD FWYPDATHHV
AANMTVDFRV SEKEYQSVQS ALDENKMHYK ILVHDLQEEI EKQFDVDDIS GRHSYAKYNN
WDKIVAWTEK MVNKHPEMVS RIKIGSTVED NPLYVLKIGK DGRRKAIFMD CGIHAREWIS
PAFCQWFVYQ NRMWRKNRSK NKNSSCIGTD LNRNFDVSWK SSPSSNNPCS DIYRGPAPES
EKETKAVTDF IRRHLKSIKA YITFHSYSQM LLFPYGYTTK LPCNQEDLNK VAKIGTDVIS
TRYETHYIYG PIASTIYPTS GSSLDWAYDL GLKHTFAFEL RDRGKFGFLL PESLIKPTCK
ETMLAVKFIA KYILKHTS
//
