Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carboxypeptidase D

Gene

Cpd

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Releases C-terminal Arg and Lys from polypeptides.By similarity

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Zinc 1; catalyticBy similarity
Metal bindingi142 – 1421Zinc 1; catalyticBy similarity
Metal bindingi257 – 2571Zinc 1; catalyticBy similarity
Metal bindingi564 – 5641Zinc 2; catalyticBy similarity
Metal bindingi567 – 5671Zinc 2; catalyticBy similarity
Metal bindingi671 – 6711Zinc 2; catalyticBy similarity
Active sitei762 – 7621Proton donor/acceptorBy similarity

GO - Molecular functioni

  • metallocarboxypeptidase activity Source: UniProtKB
  • protein complex binding Source: RGD
  • protein phosphatase 2A binding Source: RGD
  • serine-type carboxypeptidase activity Source: InterPro
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cellular response to interleukin-2 Source: RGD
  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.22. 5301.

Protein family/group databases

MEROPSiM14.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase D (EC:3.4.17.22)
Alternative name(s):
Metallocarboxypeptidase D
gp180
Gene namesi
Name:CpdImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2393. Cpd.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini38 – 12971260ExtracellularSequence analysisAdd
BLAST
Transmembranei1298 – 131821HelicalSequence analysisAdd
BLAST
Topological domaini1319 – 137860CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB
  • intracellular membrane-bounded organelle Source: RGD
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
  • trans-Golgi network Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3737Sequence analysisAdd
BLAST
Chaini38 – 13781341Carboxypeptidase DSequence analysisPRO_0000004403Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi172 – 1721N-linked (GlcNAc...)By similarity
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence analysis
Modified residuei265 – 2651PhosphotyrosineBy similarity
Modified residuei270 – 2701PhosphoserineBy similarity
Glycosylationi399 – 3991N-linked (GlcNAc...)Sequence analysis
Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence analysis
Glycosylationi429 – 4291N-linked (GlcNAc...)Sequence analysis
Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence analysis
Glycosylationi626 – 6261N-linked (GlcNAc...)Sequence analysis
Glycosylationi811 – 8111N-linked (GlcNAc...)By similarity
Glycosylationi855 – 8551N-linked (GlcNAc...)Sequence analysis
Glycosylationi867 – 8671N-linked (GlcNAc...)Sequence analysis
Glycosylationi879 – 8791N-linked (GlcNAc...)Sequence analysis
Glycosylationi953 – 9531N-linked (GlcNAc...)By similarity
Glycosylationi976 – 9761N-linked (GlcNAc...)Sequence analysis
Glycosylationi1068 – 10681N-linked (GlcNAc...)Sequence analysis
Glycosylationi1140 – 11401N-linked (GlcNAc...)Sequence analysis
Lipidationi1315 – 13151S-palmitoyl cysteineBy similarity
Lipidationi1319 – 13191S-palmitoyl cysteineBy similarity
Lipidationi1321 – 13211S-palmitoyl cysteineBy similarity
Modified residuei1356 – 13561PhosphoserineBy similarity
Modified residuei1359 – 13591PhosphoserineBy similarity
Modified residuei1366 – 13661PhosphothreonineCombined sources
Modified residuei1368 – 13681PhosphothreonineCombined sources

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ9JHW1.
PRIDEiQ9JHW1.

PTM databases

iPTMnetiQ9JHW1.
SwissPalmiQ9JHW1.
UniCarbKBiQ9JHW1.

Expressioni

Tissue specificityi

Isoform 1 is widely expressed with highest levels in the hippocampus, spinal cord, atrium, colon, testis and ovaries. Detected in the liver of females but not males. Isoform 2 is not detected in brain or lung.2 Publications

Inductioni

Isoform 2 is up-regulated by exposure to prolactin or interleukin-2.1 Publication

Interactioni

GO - Molecular functioni

  • protein complex binding Source: RGD
  • protein phosphatase 2A binding Source: RGD

Protein-protein interaction databases

MINTiMINT-4567762.
STRINGi10116.ENSRNOP00000005262.

Structurei

3D structure databases

ProteinModelPortaliQ9JHW1.
SMRiQ9JHW1. Positions 494-873.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 492455Carboxypeptidase-like 1Add
BLAST
Regioni494 – 897404Carboxypeptidase-like 2Add
BLAST
Regioni898 – 1297400Carboxypeptidase-like 3Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi162 – 1643Cell attachment siteSequence analysis

Domaini

There are 3 carboxypeptidase-like domains. Only the first two domains seem to have kept a catalytic activity.1 Publication

Sequence similaritiesi

Belongs to the peptidase M14 family.Sequence analysis

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
HOGENOMiHOG000046445.
HOVERGENiHBG006932.
InParanoidiQ9JHW1.
KOiK07752.
PhylomeDBiQ9JHW1.

Family and domain databases

Gene3Di2.60.40.1120. 3 hits.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR015567. Pept_M14B_carboxypept_D2.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF50. PTHR11532:SF50. 3 hits.
PfamiPF00246. Peptidase_M14. 3 hits.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 3 hits.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 3 hits.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 2 hits.
PS00133. CARBOXYPEPT_ZN_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q9JHW1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASGWDERPP WRLESLRLLP PPPLLLLLLL LRSSAQAAHI KKAEATTTTV
60 70 80 90 100
GGSEAAEGQF DHYYHEAALG EALEAAAAAG PPGLARLFSI GNSVEGRPLW
110 120 130 140 150
VLRLTAGLGP PPTPAAVGLD AAGPLLPGRP QVKLVGNMHG DETVSRQVLV
160 170 180 190 200
YLARELASGY RRGDPRLVRL LNTTDVYLLP SLNPDGFERA REGDCGLGDS
210 220 230 240 250
GPPGTSGRDN SRGRDLNRSF PDQFSTGEPP SLDEVPEVRA LIDWIRRNKF
260 270 280 290 300
VLSGNLHGGS VVASYPFDDS PEHKTTGIYS KTSDDEVFRY LAKAYASNHP
310 320 330 340 350
IMRTGEPHCP GDEEETFKDG ITNGAHWYDV EGGMQDYNYV WANCFEITLE
360 370 380 390 400
LSCCKYPPAS QLRQEWENNR ESLITLIEKV HIGIKGFVKD SVTGSGLENA
410 420 430 440 450
TISVAGINHN ITTGRFGDFH RLLIPGSYNL TAVSPGYMPL TINNIVVKEG
460 470 480 490 500
PATEIDFSLQ PTVMSVVPDS TEAVTTPGTV AVPNIPPGTP SSHQPIQPKD
510 520 530 540 550
FHHHHFPDME IFLRRFANEY PNITRLYSLG KSVESRELYV MEISDNPGVH
560 570 580 590 600
EPGEPEFKYI GNMHGNEVVG RELLLNLIEY LCKNFGTDPE VTDLVRSTRI
610 620 630 640 650
HLMPSMNPDG YEKSQEGDSI SVVGRNNSNN FDLNRNFPDQ FVPITDPTQP
660 670 680 690 700
ETIAVMSWVK AYPFVLSANL HGGSLVVNYP YDDNEQGVAT YSKSPDDAVF
710 720 730 740 750
QQIALSYSKE NSQMFQGRPC KDMYLNEYFP HGITNGASWY NVPGGMQDWN
760 770 780 790 800
YLQTNCFEVT IELGCVKYPF EKELPKYWEQ NRRSLIQFMK QVHQGVKGFV
810 820 830 840 850
LDATDGRGIL NATLSVAEIN HPVTTYKAGD YWRLLVPGTY KITASARGYN
860 870 880 890 900
PVTKNVTVRS EGAIQVNFTL VRSSTDANNE SKKGKGHSTS TDDTSDPTSK
910 920 930 940 950
EFEALIKHLS AENGLEGFML SSSSDLALYR YHSYKDLSEF LRGLVMNYPH
960 970 980 990 1000
ITNLTTLGQS VEYRHIWSLE ISNKPNISEP EEPKIRFVAG IHGNAPVGTE
1010 1020 1030 1040 1050
LLLALAEFLC LNYKKNPVVT QLVDRTRIVI VPSLNPDGRE RAQEKDCTSK
1060 1070 1080 1090 1100
TGHTNARGRD LDTDFTSNAS QPETKAIIEN LIQKQDFSLS IALDGGSVLV
1110 1120 1130 1140 1150
TYPYDKPVQT VENKETLKHL ASLYANNHPS MHMGQPSCPN NSDENIPGGV
1160 1170 1180 1190 1200
MRGAEWHSHL GSMKDYSVTY GHCPEITVYT SCCYFPSAAQ LPALWAENKK
1210 1220 1230 1240 1250
SLLSMLVEVH KGVHGLVKDK TGKPISKAVI VLNEGIRVHT KEGGYFHVLL
1260 1270 1280 1290 1300
APGVHNINAI ADGYQQQHSQ VFVHHDAASS VVIVFDTDNR IFGLPRELVV
1310 1320 1330 1340 1350
TVSGATMSAL ILTACIIWCI CSIKSNRHKD GFHRLRQHHD EYEDEIRMMS
1360 1370
TGSKKSLLSH EFQDETDTEE ETLYSSKH
Length:1,378
Mass (Da):152,616
Last modified:April 12, 2005 - v2
Checksum:i5F7A8DC267ED2DDD
GO
Isoform 21 Publication (identifier: Q9JHW1-2) [UniParc]FASTAAdd to basket

Also known as: CPD-N1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-245: Missing.
     246-249: RRNK → MSQR

Show »
Length:1,133
Mass (Da):126,436
Checksum:i7CE78DCF627F95BA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti455 – 4551I → M in AAF91481 (PubMed:11181555).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 245245Missing in isoform 2. 1 PublicationVSP_051712Add
BLAST
Alternative sequencei246 – 2494RRNK → MSQR in isoform 2. 1 PublicationVSP_051713

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62897 mRNA. Translation: AAB70456.1.
AF284830 mRNA. Translation: AAF91481.1.
RefSeqiNP_036968.1. NM_012836.2. [Q9JHW1-1]
UniGeneiRn.25905.

Genome annotation databases

GeneIDi25306.
KEGGirno:25306.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62897 mRNA. Translation: AAB70456.1.
AF284830 mRNA. Translation: AAF91481.1.
RefSeqiNP_036968.1. NM_012836.2. [Q9JHW1-1]
UniGeneiRn.25905.

3D structure databases

ProteinModelPortaliQ9JHW1.
SMRiQ9JHW1. Positions 494-873.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4567762.
STRINGi10116.ENSRNOP00000005262.

Protein family/group databases

MEROPSiM14.011.

PTM databases

iPTMnetiQ9JHW1.
SwissPalmiQ9JHW1.
UniCarbKBiQ9JHW1.

Proteomic databases

PaxDbiQ9JHW1.
PRIDEiQ9JHW1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25306.
KEGGirno:25306.

Organism-specific databases

CTDi1362.
RGDi2393. Cpd.

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
HOGENOMiHOG000046445.
HOVERGENiHBG006932.
InParanoidiQ9JHW1.
KOiK07752.
PhylomeDBiQ9JHW1.

Enzyme and pathway databases

BRENDAi3.4.17.22. 5301.

Miscellaneous databases

PROiQ9JHW1.

Family and domain databases

Gene3Di2.60.40.1120. 3 hits.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR015567. Pept_M14B_carboxypept_D2.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF50. PTHR11532:SF50. 3 hits.
PfamiPF00246. Peptidase_M14. 3 hits.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 3 hits.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 3 hits.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 2 hits.
PS00133. CARBOXYPEPT_ZN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of cDNA encoding rat carboxypeptidase D."
    Xin X., Varlamov O., Day R., Dong W., Bridgett M.M., Leiter E.H., Fricker L.D.
    DNA Cell Biol. 16:897-909(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Strain: Sprague-DawleyImported.
    Tissue: Hippocampus1 Publication and Testis1 Publication.
  2. "Identification and nuclear localization of a novel prolactin and cytokine-responsive carboxypeptidase D."
    Too C.K.L., Vickaryous N., Boudreau R.T.M., Sangster S.M.
    Endocrinology 142:1357-1367(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1366 AND THR-1368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCBPD_RAT
AccessioniPrimary (citable) accession number: Q9JHW1
Secondary accession number(s): O35850
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: June 8, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.