ID H2Q7J1_PANTR Unreviewed; 386 AA.
AC H2Q7J1; A0A2J8ML23;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Carboxypeptidase B2 {ECO:0000313|Ensembl:ENSPTRP00000009958.6};
GN Name=CPB2 {ECO:0000313|Ensembl:ENSPTRP00000009958.6,
GN ECO:0000313|VGNC:VGNC:14508};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000009958.6, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000009958.6, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000009958.6}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AACZ04066188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2Q7J1; -.
DR MEROPS; M14.009; -.
DR Ensembl; ENSPTRT00000010759.6; ENSPTRP00000009958.6; ENSPTRG00000005852.6.
DR VGNC; VGNC:14508; CPB2.
DR GeneTree; ENSGT00940000159160; -.
DR HOGENOM; CLU_019326_0_3_1; -.
DR Proteomes; UP000002277; Chromosome 13.
DR Bgee; ENSPTRG00000005852; Expressed in liver and 5 other cell types or tissues.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042730; P:fibrinolysis; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06246; M14_CPB2; 1.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR033849; CPB2.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF17; CARBOXYPEPTIDASE B2; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 2.
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.
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:UP000002277};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..386
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015092522"
FT DOMAIN 123..370
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 386 AA; 44000 MW; 9864E6B595AC3A2A CRC64;
MKLCSLAVLV PIVLFCEQHV FAFQSGQVLA ALPRTSRQVQ VLQNLTTTYE IVLWQPVTAD
LIVKKKQVHF FVNASDVDNV KAHLNVSGIP CSVLLADVED LIQQQISNDT VSPRASASYY
EQYHSLNEIY SWIEFITERH PDMLTKIHIG SSFEKNPLYV LKVSGKEQTA KNAIWIDCGI
HAREWISPAF CLWFIGHNRM WRKNRSFYAN NHCIGTDLNR NFASKHWCEE GASSSSCSET
YCGLYPESEP EVKAVASFLR RNINHIKAYI SMHSYSQHIV FPYSYTRSKS KDHEELSLVA
SEAVRAIEKT SKNTRYTHGH GSETLYLAPG GGDDWIYDLG IKYSFTIELR DTGTYGFLLP
ERYIKPTCRE AFAAVSKIAW HVIRNV
//
