CBPD_ANAPL
ID CBPD_ANAPL Reviewed; 1389 AA.
AC Q90240; O57512; Q9PXB2; Q9PXB3; Q9PXB4; Q9PXB5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Carboxypeptidase D;
DE EC=3.4.17.22;
DE AltName: Full=Metallocarboxypeptidase D;
DE AltName: Full=gp180;
DE AltName: Full=p170;
DE Flags: Precursor;
GN Name=CPD;
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA78903.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 420-424; 504-511; 551-564;
RP 843-850; 1065-1075 AND 1123-1231, AND BLOCKAGE OF N-TERMINUS.
RC STRAIN=Pekin breed {ECO:0000269|PubMed:7797483};
RC TISSUE=Liver {ECO:0000312|EMBL:AAA78903.1};
RX PubMed=7797483; DOI=10.1074/jbc.270.25.15022;
RA Kuroki K., Eng F., Ishikawa T., Turck C., Harada F., Ganem D.;
RT "gp180, a host cell glycoprotein that binds duck hepatitis B virus
RT particles, is encoded by a member of the carboxypeptidase gene family.";
RL J. Biol. Chem. 270:15022-15028(1995).
RN [2] {ECO:0000312|EMBL:AAB96915.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver {ECO:0000269|PubMed:10482623};
RX PubMed=10482623; DOI=10.1128/jvi.73.10.8696-8702.1999;
RA Tong S., Li J., Wands J.R.;
RT "Carboxypeptidase D is an avian hepatitis B virus receptor.";
RL J. Virol. 73:8696-8702(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAB96915.1}
RP PROTEIN SEQUENCE OF 541-567; 886-898; 1027-1047 AND 1367-1388, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Pekin breed {ECO:0000269|PubMed:7474130};
RX PubMed=7474130; DOI=10.1128/jvi.69.11.7106-7112.1995;
RA Tong S., Li J., Wands J.R.;
RT "Interaction between duck hepatitis B virus and a 170-kilodalton cellular
RT protein is mediated through a neutralizing epitope of the pre-S region and
RT occurs during viral infection.";
RL J. Virol. 69:7106-7112(1995).
RN [4] {ECO:0000305}
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Pekin breed {ECO:0000269|PubMed:8138993};
RX PubMed=8138993; DOI=10.1128/jvi.68.4.2091-2096.1994;
RA Kuroki K., Cheung R., Marion P.L., Ganem D.;
RT "A cell surface protein that binds avian hepatitis B virus particles.";
RL J. Virol. 68:2091-2096(1994).
RN [5] {ECO:0000305}
RP CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=9525948; DOI=10.1074/jbc.273.14.8382;
RA Eng F.J., Novikova E.G., Kuroki K., Ganem D., Fricker L.D.;
RT "gp180, a protein that binds duck hepatitis B virus particles, has
RT metallocarboxypeptidase D-like enzymatic activity.";
RL J. Biol. Chem. 273:8382-8388(1998).
RN [6] {ECO:0000305}
RP CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF GLU-353 AND GLU-771.
RX PubMed=10506132; DOI=10.1074/jbc.274.41.28887;
RA Novikova E.G., Eng F.J., Yan L., Qian Y., Fricker L.D.;
RT "Characterization of the enzymatic properties of the first and second
RT domains of metallocarboxypeptidase D.";
RL J. Biol. Chem. 274:28887-28892(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Releases C-terminal Arg and Lys from polypeptides.;
CC EC=3.4.17.22; Evidence={ECO:0000269|PubMed:10506132,
CC ECO:0000269|PubMed:9525948};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10506132, ECO:0000269|PubMed:9525948};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:10506132,
CC ECO:0000269|PubMed:9525948};
CC -!- SUBUNIT: Binds to pre-S, hepatitis B virus large envelope protein, via
CC the carboxypeptidase-like domain. {ECO:0000269|PubMed:7474130,
CC ECO:0000269|PubMed:8138993, ECO:0000269|PubMed:9525948}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8138993};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, lung, kidney, heart, stomach,
CC pancreas, spleen, gall bladder and intestine, but not in skeletal
CC muscle. {ECO:0000269|PubMed:7474130, ECO:0000269|PubMed:8138993}.
CC -!- DOMAIN: There are 3 carboxypeptidase domains. Only the first two
CC domains have any catalytic activity. The first domain preferentially
CC cleaves C-terminal Arg residues, whereas the second preferentially
CC cleaves C-terminal Lys residues. The third domain binds to pre-S,
CC hepatitis B virus large envelope protein. {ECO:0000269|PubMed:10506132,
CC ECO:0000269|PubMed:9525948}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7797483}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000255}.
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DR EMBL; U25126; AAA78903.1; -; mRNA.
DR EMBL; AF039749; AAB96915.1; -; mRNA.
DR PIR; I50090; I50090.
DR RefSeq; NP_001297311.1; NM_001310382.1.
DR AlphaFoldDB; Q90240; -.
DR SMR; Q90240; -.
DR MEROPS; M14.950; -.
DR SwissPalm; Q90240; -.
DR GeneID; 101802114; -.
DR KEGG; apla:101802114; -.
DR CTD; 1362; -.
DR OrthoDB; 101221at2759; -.
DR BRENDA; 3.4.17.22; 334.
DR SABIO-RK; Q90240; -.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA: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; IDA:UniProtKB.
DR CDD; cd03863; M14_CPD_II; 1.
DR CDD; cd06245; M14_CPD_III; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR034224; M14_CPD_II.
DR InterPro; IPR033848; M14_CPD_III.
DR InterPro; IPR015567; Pept_M14B_carboxypept_D2.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF73; PTHR11532:SF73; 4.
DR Pfam; PF00246; Peptidase_M14; 3.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 3.
DR SUPFAM; SSF49464; SSF49464; 3.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 2.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 2.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell membrane; Direct protein sequencing; Glycoprotein;
KW Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease;
KW Palmitate; Protease; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1389
FT /note="Carboxypeptidase D"
FT /evidence="ECO:0000255"
FT /id="PRO_0000004404"
FT TOPO_DOM 26..1308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1309..1329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1330..1389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 26..502
FT /note="Carboxypeptidase 1"
FT REGION 95..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..902
FT /note="Carboxypeptidase 2"
FT REGION 614..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..1308
FT /note="Carboxypeptidase-like"
FT REGION 1367..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 353
FT /note="Proton donor/acceptor 1"
FT /evidence="ECO:0000305|PubMed:10506132"
FT ACT_SITE 771
FT /note="Proton donor/acceptor 2"
FT /evidence="ECO:0000305|PubMed:10506132"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT BINDING 573
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P83852"
FT BINDING 576
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P83852"
FT BINDING 680
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P83852"
FT LIPID 1326
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT LIPID 1330
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT LIPID 1332
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P83852"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P83852"
FT CARBOHYD 876
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P83852"
FT CARBOHYD 958
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT CARBOHYD 981
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1073
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 353
FT /note="E->Q: Loss of catalytic activity in carboxypeptidase
FT domain 1. Total loss of catalytic activity; when associated
FT with Q-771."
FT /evidence="ECO:0000269|PubMed:10506132"
FT MUTAGEN 771
FT /note="E->Q: Loss of catalytic activity in carboxypeptidase
FT domain 2. Total loss of catalytic activity; when associated
FT with Q-535."
FT /evidence="ECO:0000269|PubMed:10506132"
FT CONFLICT 40
FT /note="G -> GG (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="Missing (in Ref. 2; AAB96915)"
FT /evidence="ECO:0000305"
FT CONFLICT 196..197
FT /note="Missing (in Ref. 2; AAB96915)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="F -> Y (in Ref. 2; AAB96915)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="A -> G (in Ref. 2; AAB96915)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="P -> L (in Ref. 2; AAB96915)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="V -> A (in Ref. 2; AAB96915)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="Q -> R (in Ref. 2; AAB96915)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="I -> V (in Ref. 2; AAB96915 and 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1076
FT /note="W -> R (in Ref. 2; AAB96915)"
FT /evidence="ECO:0000305"
FT CONFLICT 1126
FT /note="E -> D (in Ref. 2; AAB96915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1389 AA; 153506 MW; AD2604E157B058E9 CRC64;
MAGAARGLLW AALSLCLLPE PLRAAHIKKA EAAAAGGGGG VGGELRYLHA AELGQALRDL
VAEAPPGLAR LFSIGRSVEG RPLWVLRLTA GLPELPEARQ DGEKKKKEEE EEEEEEEGEE
GGGGALPGRP QVKLVGNMHG DEPLARPLLL RLAQELVRGW AGGDERLGRL LNTTDLYLLP
SLNPDGFERA REGDCGGGGG GGGEGGGEPG GRENSRGRDL NRSFPDQFGS AQPDLEPVPE
VRALIAWMRR NKFLLSGNLH GGSVVASYPY DDSPTHRPTG VYSKSADDEV FKYLAKAYAS
HHPIMRTGKP NCPGEEGETF QDGITNGAQW YDVEGGMQDY NYVWANCFEI TLELSCCKYP
PTSELQQEWE NNRESLLTFI EKVHIGVKGF VRDAITGAGL ENATIVVAGI AHNITAGKFG
DYHRLLVPGT YNVTAVVMGY APVTKENIEV KEADATVVDF SLQPTVVAPD PNLTQFTATP
APPSTLTPSV AQVEPPATTS LHQAVQPVDF RHHHFSDMEI FLRRYANEYP SITRLYSVGK
SVELRELYVM EISDNPGIHE AGEPEFKYIG NMHGNEVVGR ELLLNLIEYL CKNFGTDPEV
TDLVQSTRIH IMPSMNPDGY EKSQEGDRGG TVGRNNSNNY DLNRNFPDQF FQVTDPPQPE
TLAVMSWLKT YPFVLSANLH GGSLVVNYPF DDDEQGIAIY SKSPDDAVFQ QLALSYSKEN
KKMYQGSPCK DLYPTEYFPH GITNGAQWYN VPGGMQDWNY LNTNCFEVTI ELGCVKYPKA
EELPKYWEQN RRSLLQFIKQ VHRGIWGFVL DATDGRGILN ATISVADINH PVTTYKDGDY
WRLLVQGTYK VTASARGYDP VTKTVEVDSK GGVQVNFTLS RTDAKVEEGK VPVLNTPDTS
DPNEKEFETL IKDLSAENGL ERLLLASSGK VSPYRYRPYK DLSEFLRGLY LNYPHITNLT
SLGQSVEFRQ IWSLEISNKP NHSEPEEPKI RFVAGIHGNA PVGTELLLAL AEFLCMNYKK
NSAVTKLIDR TRIVIVPSLN PDGREIAQER GCTSKLGHAN AHGRDLDTDF TSNYSWYSGT
REPETKAIIE NLILKQDFSL SVALDGGSLL VTYPFDKPAQ TVENKETLKH LASVYANNHP
LMHLGQPGCP NKSDENIPGG VIRGSEWHSH LGSMKDFSVT FGHCPEITVY TSCCYFPSAG
QLPGLWADHR KSLLSMLVEV HKGVHGFVQD KSGKAISKAT IVLNEGLRVY TKEGGYFHVL
LAPGLHNINA IADGYQQKHM KVLVRHDAPS SVFIVFDMEN RIFGLPRELV VTVAGASMSA
LVLTACIIWC VCSIKSNRHK DGFPTLRQHH DDYEDEIRMM STGSKKSLLS HEFQDETDTE
EETLYSSKH
