ID A0A2Y9DQM6_TRIMA Unreviewed; 417 AA.
AC A0A2Y9DQM6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Carboxypeptidase B {ECO:0000256|ARBA:ARBA00039334};
DE EC=3.4.17.2 {ECO:0000256|ARBA:ARBA00039143};
GN Name=LOC101345894 {ECO:0000313|RefSeq:XP_004379261.1};
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_004379261.1};
RN [1] {ECO:0000313|RefSeq:XP_004379261.1}
RP IDENTIFICATION.
RG RefSeq;
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}.
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 RefSeq; XP_004379261.1; XM_004379204.1.
DR AlphaFoldDB; A0A2Y9DQM6; -.
DR STRING; 127582.A0A2Y9DQM6; -.
DR GeneID; 101345894; -.
DR KEGG; tmu:101345894; -.
DR InParanoid; A0A2Y9DQM6; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; cd03871; M14_CPB; 1.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR034253; CPB_M14_CPD.
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 ECO:0000313|RefSeq:XP_004379261.1};
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 /note="Carboxypeptidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015851099"
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; 47197 MW; 54C430AF952D5DC1 CRC64;
MLAFLVLVAV ALVSAHQSGE HFEGEKVFRV NVEDENHINL IQELASINQI DFWKPDSATQ
IKPHSTVDFR VKAEDIFTVE DFLEQNELQY EVLINNLRSV LEAQFDSHVR AAGHSYEKYN
NWETIEAWTQ QVATDNPDLI SRSVIGTTFQ GRSLYLLKVG KAGNKKPAIF IDCGFHAREW
ISPAFCQWFV REAVRTYGSE VDTTNLLNKL DFYVLPVFNI DGYVYSWTTN RMWRKTRSTN
SGSACIGTDP NRNFDAGWCQ IGASRSPCAE TYCGSAAESE KETKALTNFI RKNLSSIKAY
LTIHSYSQLL LYPYSYAYKL PENNDELNAL AKAAVAELAT LYNTKYTYGP GATAIYPAAG
GSDDWAFDQG IKYSFTFELR DTGRYGFALP ESQIQPTCKE TLLAVKYIAN YILKHLY
//
