ID H2QEQ1_PANTR Unreviewed; 508 AA.
AC H2QEQ1; A0A2J8KWP2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Carnosine dipeptidase 1 {ECO:0000313|Ensembl:ENSPTRP00000017188.5};
GN Name=CNDP1 {ECO:0000313|Ensembl:ENSPTRP00000017188.5,
GN ECO:0000313|VGNC:VGNC:14787};
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:ENSPTRP00000017188.5, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000017188.5, 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:ENSPTRP00000017188.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR037242-3};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR037242-3};
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; AACZ04062348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001136945.1; XM_001136945.5.
DR AlphaFoldDB; H2QEQ1; -.
DR STRING; 9598.ENSPTRP00000062084; -.
DR MEROPS; M20.006; -.
DR PaxDb; 9598-ENSPTRP00000017188; -.
DR Ensembl; ENSPTRT00000018555.6; ENSPTRP00000017188.5; ENSPTRG00000010115.6.
DR GeneID; 455474; -.
DR KEGG; ptr:455474; -.
DR CTD; 84735; -.
DR VGNC; VGNC:14787; CNDP1.
DR eggNOG; KOG2276; Eukaryota.
DR GeneTree; ENSGT00940000160484; -.
DR HOGENOM; CLU_029469_3_1_1; -.
DR OrthoDB; 177966at2759; -.
DR TreeFam; TF300633; -.
DR Proteomes; UP000002277; Chromosome 18.
DR Bgee; ENSPTRG00000010115; Expressed in liver and 10 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05676; M20_dipept_like_CNDP; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR017153; CNDP/DUG1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF1; BETA-ALA-HIS DIPEPTIDASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|PIRSR:PIRSR037242-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037242-3};
KW Protease {ECO:0000256|ARBA:ARBA00022645};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..508
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015092671"
FT DOMAIN 251..400
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 135
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT BINDING 133
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 479
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT SITE 262
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-4"
SQ SEQUENCE 508 AA; 56909 MW; 8C6FBE91C5840ACC CRC64;
MDPKLGRMAA SLLAVLLLLL LERGMFSSPS PPPALLEKVF RYIDLHQDEF VQTLKEWVAI
ESDSVQPVPR FRQELFRMMA MAADMLQRLG ARVASVDMGL QQLPDGQSLP IPPIILAELG
SDPTKGTVCF YGHLDVQPAD QGDGWLTDPY VLTEVDGKLY GRGATDNKGP VLAWINAVSA
FRALEQDLPV NIKFIIEGME EAGSVALEEL VEKEKDRFFS GVDYIVISDN LWISQRKPAI
TYGTRGNSYF MVEVKCRDQD FHSGTFGGIL HEPMADLVAL LGSLVDSSGH ILVPGIYDEV
VRLTEEEINT YKAIHLDLEE YRNSSQIEKF LFDTKEEILM HLWRYPSLSI HGIEGAFDEP
GAKTVIPGRV IGKFSIRLVP HMNVSVVEKQ VTRHLEDVFS KRNSSNKMVV SMALGLHPWI
ANINDTQYLA AKRAIRTVFG TEPDMIRDGS TIPIAKMFQE IVHKSVVLIP LGAVDDGEHS
QNEKINRWNY IEGTKLFAAF FLEMAQLH
//