ID A0A2Y9DQR4_TRIMA Unreviewed; 417 AA.
AC A0A2Y9DQR4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Mast cell carboxypeptidase A {ECO:0000313|RefSeq:XP_004379260.1};
GN Name=LOC101345637 {ECO:0000313|RefSeq:XP_004379260.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004379260.1};
RN [1] {ECO:0000313|RefSeq:XP_004379260.1}
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_004379260.1; XM_004379203.2.
DR AlphaFoldDB; A0A2Y9DQR4; -.
DR STRING; 127582.A0A2Y9DQR4; -.
DR GeneID; 101345637; -.
DR KEGG; tmu:101345637; -.
DR InParanoid; A0A2Y9DQR4; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000248480; 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 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: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|RefSeq:XP_004379260.1};
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:UP000248480};
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..417
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015904605"
FT DOMAIN 167..189
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 304..314
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 417 AA; 48570 MW; 27A5FF003857B62F CRC64;
MRFILLVGLI ATTLAIAPLR FDREKVFRVK PQDEKQANII KDLAKTKELD FWYPDATHHV
TANKMVDFRV SENNSQSIQS ALEQNQMHYE ILIHDLQKEI EKQFDVKEAI PGRHSYAKYN
NWDKIVVWTE KMMNKHPEMV SRIKIGMTVE DNPLYVLQVG KQDERKKSVF MNCGIHAREW
ISPAFCQWFV YQATKSYGKN KIMTKLLDQM NFYVLPVFNV DGYIWSWTQN RMWRKNRSKN
PNSRCIGTDL NRNFNASWNS LPNTNNPCSD TYHGTAPESE RETKAVTQFI RSHLNSIKAY
ITFHSYSQML LFPYGYTSEL TPNHEDLAKV AKIGTDALAT HYETRYIYDP MASITYPTTG
SSLDWAYDLG IKHTFAFELR DKGKFGFLLP ESQIKSTCKE TMLAVKFIAK YILKHAS
//
