CBPD_RAT
ID CBPD_RAT Reviewed; 1378 AA.
AC Q9JHW1; O35850;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Carboxypeptidase D;
DE EC=3.4.17.22;
DE AltName: Full=Metallocarboxypeptidase D;
DE AltName: Full=gp180;
DE Flags: Precursor;
GN Name=Cpd {ECO:0000312|RGD:2393};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB70456.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAB70456.1};
RC TISSUE=Hippocampus {ECO:0000269|PubMed:9260933}, and
RC Testis {ECO:0000269|PubMed:9260933};
RX PubMed=9260933; DOI=10.1089/dna.1997.16.897;
RA Xin X., Varlamov O., Day R., Dong W., Bridgett M.M., Leiter E.H.,
RA Fricker L.D.;
RT "Cloning and sequence analysis of cDNA encoding rat carboxypeptidase D.";
RL DNA Cell Biol. 16:897-909(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF91481.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=11181555; DOI=10.1210/endo.142.3.8041;
RA Too C.K.L., Vickaryous N., Boudreau R.T.M., Sangster S.M.;
RT "Identification and nuclear localization of a novel prolactin and cytokine-
RT responsive carboxypeptidase D.";
RL Endocrinology 142:1357-1367(2001).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1366 AND THR-1368, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-811 AND ASN-1068, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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:0000250|UniProtKB:Q90240};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q90240};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000250|UniProtKB:Q90240}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:11181555}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:9260933};
CC IsoId=Q9JHW1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11181555}; Synonyms=CPD-N
CC {ECO:0000303|PubMed:11181555};
CC IsoId=Q9JHW1-2; Sequence=VSP_051712, VSP_051713;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed with highest levels
CC in the hippocampus, spinal cord, atrium, colon, testis and ovaries.
CC Detected in the liver of females but not males. Isoform 2 is not
CC detected in brain or lung. {ECO:0000269|PubMed:11181555,
CC ECO:0000269|PubMed:9260933}.
CC -!- INDUCTION: [Isoform 2]: Up-regulated by exposure to prolactin or
CC interleukin-2. {ECO:0000269|PubMed:11181555}.
CC -!- DOMAIN: There are 3 carboxypeptidase-like domains. Only the first two
CC domains seem to have kept a catalytic activity.
CC {ECO:0000303|PubMed:9260933}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000255}.
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 EMBL; U62897; AAB70456.1; -; mRNA.
DR EMBL; AF284830; AAF91481.1; -; mRNA.
DR RefSeq; NP_036968.1; NM_012836.2. [Q9JHW1-1]
DR AlphaFoldDB; Q9JHW1; -.
DR SMR; Q9JHW1; -.
DR IntAct; Q9JHW1; 3.
DR STRING; 10116.ENSRNOP00000005262; -.
DR MEROPS; M14.011; -.
DR MEROPS; M14.016; -.
DR MEROPS; M14.950; -.
DR GlyGen; Q9JHW1; 15 sites, 2 N-linked glycans (3 sites).
DR iPTMnet; Q9JHW1; -.
DR PhosphoSitePlus; Q9JHW1; -.
DR SwissPalm; Q9JHW1; -.
DR jPOST; Q9JHW1; -.
DR PaxDb; Q9JHW1; -.
DR PRIDE; Q9JHW1; -.
DR GeneID; 25306; -.
DR KEGG; rno:25306; -.
DR CTD; 1362; -.
DR RGD; 2393; Cpd.
DR eggNOG; KOG2649; Eukaryota.
DR InParanoid; Q9JHW1; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; Q9JHW1; -.
DR BRENDA; 3.4.17.22; 5301.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR PRO; PR:Q9JHW1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; ISS:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0071352; P:cellular response to interleukin-2; IEP:RGD.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISS: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; 3.
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 Alternative splicing; Carboxypeptidase; Cell membrane; Glycoprotein;
KW Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease; Nucleus;
KW Palmitate; Phosphoprotein; Protease; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..1378
FT /note="Carboxypeptidase D"
FT /evidence="ECO:0000255"
FT /id="PRO_0000004403"
FT TOPO_DOM 38..1297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1298..1318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1319..1378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 38..492
FT /note="Carboxypeptidase-like 1"
FT REGION 189..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..897
FT /note="Carboxypeptidase-like 2"
FT REGION 875..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..1297
FT /note="Carboxypeptidase-like 3"
FT REGION 1039..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 162..164
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 878..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 762
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
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:P19222"
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:P19222"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P19222"
FT BINDING 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P19222"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P19222"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P19222"
FT MOD_RES 265
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O89001"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O89001"
FT MOD_RES 1356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT MOD_RES 1366
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1368
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 1315
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT LIPID 1319
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT LIPID 1321
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 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 867
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 953
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:O75976"
FT CARBOHYD 976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1068
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 1140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..245
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11181555"
FT /id="VSP_051712"
FT VAR_SEQ 246..249
FT /note="RRNK -> MSQR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11181555"
FT /id="VSP_051713"
FT CONFLICT 455
FT /note="I -> M (in Ref. 2; AAF91481)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1378 AA; 152616 MW; 5F7A8DC267ED2DDD CRC64;
MASGWDERPP WRLESLRLLP PPPLLLLLLL LRSSAQAAHI KKAEATTTTV GGSEAAEGQF
DHYYHEAALG EALEAAAAAG PPGLARLFSI GNSVEGRPLW VLRLTAGLGP PPTPAAVGLD
AAGPLLPGRP QVKLVGNMHG DETVSRQVLV YLARELASGY RRGDPRLVRL LNTTDVYLLP
SLNPDGFERA REGDCGLGDS GPPGTSGRDN SRGRDLNRSF PDQFSTGEPP SLDEVPEVRA
LIDWIRRNKF VLSGNLHGGS VVASYPFDDS PEHKTTGIYS KTSDDEVFRY LAKAYASNHP
IMRTGEPHCP GDEEETFKDG ITNGAHWYDV EGGMQDYNYV WANCFEITLE LSCCKYPPAS
QLRQEWENNR ESLITLIEKV HIGIKGFVKD SVTGSGLENA TISVAGINHN ITTGRFGDFH
RLLIPGSYNL TAVSPGYMPL TINNIVVKEG PATEIDFSLQ PTVMSVVPDS TEAVTTPGTV
AVPNIPPGTP SSHQPIQPKD FHHHHFPDME IFLRRFANEY PNITRLYSLG KSVESRELYV
MEISDNPGVH EPGEPEFKYI GNMHGNEVVG RELLLNLIEY LCKNFGTDPE VTDLVRSTRI
HLMPSMNPDG YEKSQEGDSI SVVGRNNSNN FDLNRNFPDQ FVPITDPTQP ETIAVMSWVK
AYPFVLSANL HGGSLVVNYP YDDNEQGVAT YSKSPDDAVF QQIALSYSKE NSQMFQGRPC
KDMYLNEYFP HGITNGASWY NVPGGMQDWN YLQTNCFEVT IELGCVKYPF EKELPKYWEQ
NRRSLIQFMK QVHQGVKGFV LDATDGRGIL NATLSVAEIN HPVTTYKAGD YWRLLVPGTY
KITASARGYN PVTKNVTVRS EGAIQVNFTL VRSSTDANNE SKKGKGHSTS TDDTSDPTSK
EFEALIKHLS AENGLEGFML SSSSDLALYR YHSYKDLSEF LRGLVMNYPH ITNLTTLGQS
VEYRHIWSLE ISNKPNISEP EEPKIRFVAG IHGNAPVGTE LLLALAEFLC LNYKKNPVVT
QLVDRTRIVI VPSLNPDGRE RAQEKDCTSK TGHTNARGRD LDTDFTSNAS QPETKAIIEN
LIQKQDFSLS IALDGGSVLV TYPYDKPVQT VENKETLKHL ASLYANNHPS MHMGQPSCPN
NSDENIPGGV MRGAEWHSHL GSMKDYSVTY GHCPEITVYT SCCYFPSAAQ LPALWAENKK
SLLSMLVEVH KGVHGLVKDK TGKPISKAVI VLNEGIRVHT KEGGYFHVLL APGVHNINAI
ADGYQQQHSQ VFVHHDAASS VVIVFDTDNR IFGLPRELVV TVSGATMSAL ILTACIIWCI
CSIKSNRHKD GFHRLRQHHD EYEDEIRMMS TGSKKSLLSH EFQDETDTEE ETLYSSKH
