CBPD_LOPSP
ID CBPD_LOPSP Reviewed; 380 AA.
AC P83852;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Carboxypeptidase D;
DE EC=3.4.17.22;
DE AltName: Full=CPD-2;
DE AltName: Full=Metallocarboxypeptidase D;
DE Flags: Fragment;
GN Name=CPD;
OS Lophonetta specularioides (Crested duck) (Anas specularioides).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Lophonetta.
OX NCBI_TaxID=75873;
RN [1] {ECO:0000305, ECO:0000312|PDB:1QMU}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), COFACTOR, METAL-BINDING, DISULFIDE
RP BOND, AND GLYCOSYLATION AT ASN-133; ASN-318 AND ASN-374.
RX PubMed=10545093; DOI=10.1093/emboj/18.21.5817;
RA Gomis-Rueth F.-X., Companys V., Qian Y., Fricker L.D., Vendrell J.,
RA Aviles F.X., Coll M.;
RT "Crystal structure of avian carboxypeptidase D domain II: a prototype for
RT the regulatory metallocarboxypeptidase subfamily.";
RL EMBO J. 18:5817-5826(1999).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=11278909; DOI=10.1074/jbc.m011457200;
RA Aloy P., Companys V., Vendrell J., Aviles F.X., Fricker L.D., Coll M.,
RA Gomis-Rueth F.-X.;
RT "The crystal structure of the inhibitor-complexed carboxypeptidase D domain
RT II and the modeling of regulatory carboxypeptidases.";
RL J. Biol. Chem. 276:16177-16184(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Releases C-terminal Arg and Lys from polypeptides.;
CC EC=3.4.17.22; Evidence={ECO:0000250|UniProtKB:Q90240};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10545093};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:10545093};
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000255}.
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DR PDB; 1H8L; X-ray; 2.60 A; A=1-380.
DR PDB; 1QMU; X-ray; 2.70 A; A=1-380.
DR PDBsum; 1H8L; -.
DR PDBsum; 1QMU; -.
DR AlphaFoldDB; P83852; -.
DR SMR; P83852; -.
DR iPTMnet; P83852; -.
DR EvolutionaryTrace; P83852; -.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR CDD; cd03863; M14_CPD_II; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR034224; M14_CPD_II.
DR InterPro; IPR015567; Pept_M14B_carboxypept_D2.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF73; PTHR11532:SF73; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Zinc.
FT CHAIN <1..>380
FT /note="Carboxypeptidase D"
FT /id="PRO_0000212786"
FT REGION 1..>380
FT /note="Carboxypeptidase 2"
FT REGION 112..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10545093"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10545093"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10545093"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10545093"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10545093"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10545093"
FT DISULFID 227..272
FT /evidence="ECO:0000269|PubMed:10545093"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:10545093"
FT NON_TER 380
FT /evidence="ECO:0000303|PubMed:10545093"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:1H8L"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:1H8L"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:1H8L"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1QMU"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:1H8L"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 281..297
FT /evidence="ECO:0007829|PDB:1H8L"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:1H8L"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 344..352
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:1H8L"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:1H8L"
SQ SEQUENCE 380 AA; 43292 MW; 536498919536E949 CRC64;
QAVQPVDFRH HHFSDMEIFL RRYANEYPSI TRLYSVGKSV ELRELYVMEI SDNPGIHEAG
EPEFKYIGNM HGNEVVGREL LLNLIEYLCK NFGTDPEVTD LVQSTRIHIM PSMNPDGYEK
SQEGDRGGTV GRNNSNNYDL NRNFPDQFFQ VTDPPQPETL AVMSWLKTYP FVLSANLHGG
SLVVNYPFDD DEQGIAIYSK SPDDAVFQQL ALSYSKENKK MYQGSPCKDL YPTEYFPHGI
TNGAQWYNVP GGMQDWNYLN TNCFEVTIEL GCVKYPKAEE LPKYWEQNRR SLLQFIKQVH
RGIWGFVLDA TDGRGILNAT ISVADINHPV TTYKDGDYWR LLVQGTYKVT ASARGYDPVT
KTVEVDSKGG VQVNFTLSRT
