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
Homo sapiens (Human)
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.

Cofactori

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

pH dependencei

Optimum pH is 6.0-6.5.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi139Zinc 1; catalyticBy similarity1
Metal bindingi142Zinc 1; catalyticBy similarity1
Metal bindingi257Zinc 1; catalyticBy similarity1
Metal bindingi564Zinc 2; catalyticBy similarity1
Metal bindingi567Zinc 2; catalyticBy similarity1
Metal bindingi671Zinc 2; catalyticBy similarity1
Active sitei762Proton donor/acceptorBy similarity1

GO - Molecular functioni

  • metallocarboxypeptidase activity Source: GO_Central
  • serine-type carboxypeptidase activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionCarboxypeptidase, Hydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.22. 2681.
ReactomeiR-HSA-432722. Golgi Associated Vesicle Biogenesis.

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:CPD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000108582.11.
HGNCiHGNC:2301. CPD.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini32 – 1299ExtracellularSequence analysisAdd BLAST1268
Transmembranei1300 – 1320HelicalSequence analysisAdd BLAST21
Topological domaini1321 – 1380CytoplasmicSequence analysisAdd BLAST60

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi1362.
OpenTargetsiENSG00000108582.
PharmGKBiPA26823.

Chemistry databases

DrugBankiDB04489. Guanidinoethylmercaptosuccinic acid.

Polymorphism and mutation databases

BioMutaiCPD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000000440132 – 1380Carboxypeptidase DAdd BLAST1349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi172N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi217N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei265PhosphotyrosineBy similarity1
Modified residuei270PhosphoserineBy similarity1
Glycosylationi399N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi410N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi429N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi522N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi626N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi811N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi855N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi867N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi879N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi955N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi978N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1070N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1142N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi1317S-palmitoyl cysteine1 Publication1
Lipidationi1321S-palmitoyl cysteine1 Publication1
Lipidationi1323S-palmitoyl cysteine1 Publication1
Modified residuei1358PhosphoserineCombined sources1
Modified residuei1361PhosphoserineCombined sources1
Modified residuei1368PhosphothreonineCombined sources1
Modified residuei1370PhosphothreonineCombined sources1

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiO75976.
MaxQBiO75976.
PaxDbiO75976.
PeptideAtlasiO75976.
PRIDEiO75976.

PTM databases

iPTMnetiO75976.
PhosphoSitePlusiO75976.
SwissPalmiO75976.

Expressioni

Tissue specificityi

Highly expressed in placenta, pancreas and hepatoma cells. Lower levels found in skeletal muscle, heart and colon carcinoma and melanoma cell lines.

Gene expression databases

BgeeiENSG00000108582.
CleanExiHS_CPD.
ExpressionAtlasiO75976. baseline and differential.
GenevisibleiO75976. HS.

Organism-specific databases

HPAiHPA052796.
HPA055465.

Interactioni

Protein-protein interaction databases

BioGridi107754. 20 interactors.
IntActiO75976. 6 interactors.
MINTiMINT-5003925.
STRINGi9606.ENSP00000225719.

Structurei

Secondary structure

11380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi383 – 390Combined sources8
Turni391 – 393Combined sources3
Beta strandi401 – 404Combined sources4
Beta strandi417 – 422Combined sources6
Beta strandi425 – 433Combined sources9
Beta strandi440 – 447Combined sources8
Beta strandi449 – 451Combined sources3
Beta strandi457 – 459Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AQ0X-ray0.95A/B383-461[»]
ProteinModelPortaliO75976.
SMRiO75976.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 493Carboxypeptidase-like 1Add BLAST462
Regioni494 – 897Carboxypeptidase-like 2Add BLAST404
Regioni898 – 1299Carboxypeptidase-like 3Add BLAST402

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi162 – 164Cell attachment siteSequence analysis3

Domaini

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

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
GeneTreeiENSGT00760000119124.
HOGENOMiHOG000046445.
HOVERGENiHBG006932.
InParanoidiO75976.
KOiK07752.
OMAiLTPPVKY.
OrthoDBiEOG091G06A9.
PhylomeDBiO75976.
TreeFamiTF315592.

Family and domain databases

CDDicd03868. M14_CPD_I. 1 hit.
cd03863. M14_CPD_II. 1 hit.
cd06245. M14_CPD_III. 1 hit.
InterProiView protein in InterPro
IPR008969. CarboxyPept-like_regulatory.
IPR034241. M14_CPD_I.
IPR034224. M14_CPD_II.
IPR033848. M14_CPD_III.
IPR015567. Pept_M14B_carboxypept_D2.
IPR000834. Peptidase_M14.
PANTHERiPTHR11532:SF73. PTHR11532:SF73. 4 hits.
PfamiView protein in Pfam
PF00246. Peptidase_M14. 3 hits.
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiView protein in SMART
SM00631. Zn_pept. 3 hits.
SUPFAMiSSF49464. SSF49464. 3 hits.
PROSITEiView protein in PROSITE
PS00132. CARBOXYPEPT_ZN_1. 2 hits.
PS00133. CARBOXYPEPT_ZN_2. 2 hits.

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 1 (identifier: O75976-1) [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
MASGRDERPP WRLGRLLLLM CLLLLGSSAR AAHIKKAEAT TTTTSAGAEA
60 70 80 90 100
AEGQFDRYYH EEELESALRE AAAAGLPGLA RLFSIGRSVE GRPLWVLRLT
110 120 130 140 150
AGLGSLIPEG DAGPDAAGPD AAGPLLPGRP QVKLVGNMHG DETVSRQVLI
160 170 180 190 200
YLARELAAGY RRGDPRLVRL LNTTDVYLLP SLNPDGFERA REGDCGFGDG
210 220 230 240 250
GPSGASGRDN SRGRDLNRSF PDQFSTGEPP ALDEVPEVRA LIEWIRRNKF
260 270 280 290 300
VLSGNLHGGS VVASYPFDDS PEHKATGIYS KTSDDEVFKY LAKAYASNHP
310 320 330 340 350
IMKTGEPHCP GDEDETFKDG ITNGAHWYDV EGGMQDYNYV WANCFEITLE
360 370 380 390 400
LSCCKYPPAS QLRQEWENNR ESLITLIEKV HIGVKGFVKD SITGSGLENA
410 420 430 440 450
TISVAGINHN ITTGRFGDFY RLLVPGTYNL TVVLTGYMPL TVTNVVVKEG
460 470 480 490 500
PATEVDFSLR PTVTSVIPDT TEAVSTASTV AIPNILSGTS SSYQPIQPKD
510 520 530 540 550
FHHHHFPDME IFLRRFANEY PNITRLYSLG KSVESRELYV MEISDNPGVH
560 570 580 590 600
EPGEPEFKYI GNMHGNEVVG RELLLNLIEY LCKNFGTDPE VTDLVHNTRI
610 620 630 640 650
HLMPSMNPDG YEKSQEGDSI SVIGRNNSNN FDLNRNFPDQ FVQITDPTQP
660 670 680 690 700
ETIAVMSWMK SYPFVLSANL HGGSLVVNYP FDDDEQGLAT YSKSPDDAVF
710 720 730 740 750
QQIALSYSKE NSQMFQGRPC KNMYPNEYFP HGITNGASWY NVPGGMQDWN
760 770 780 790 800
YLQTNCFEVT IELGCVKYPL EKELPNFWEQ NRRSLIQFMK QVHQGVRGFV
810 820 830 840 850
LDATDGRGIL NATISVAEIN HPVTTYKTGD YWRLLVPGTY KITASARGYN
860 870 880 890 900
PVTKNVTVKS EGAIQVNFTL VRSSTDSNNE SKKGKGASSS TNDASDPTTK
910 920 930 940 950
EFETLIKDLS AENGLESLML RSSSNLALAL YRYHSYKDLS EFLRGLVMNY
960 970 980 990 1000
PHITNLTNLG QSTEYRHIWS LEISNKPNVS EPEEPKIRFV AGIHGNAPVG
1010 1020 1030 1040 1050
TELLLALAEF LCLNYKKNPA VTQLVDRTRI VIVPSLNPDG RERAQEKDCT
1060 1070 1080 1090 1100
SKIGQTNARG KDLDTDFTNN ASQPETKAII ENLIQKQDFS LSVALDGGSM
1110 1120 1130 1140 1150
LVTYPYDKPV QTVENKETLK HLASLYANNH PSMHMGQPSC PNKSDENIPG
1160 1170 1180 1190 1200
GVMRGAEWHS HLGSMKDYSV TYGHCPEITV YTSCCYFPSA ARLPSLWADN
1210 1220 1230 1240 1250
KRSLLSMLVE VHKGVHGFVK DKTGKPISKA VIVLNEGIKV QTKEGGYFHV
1260 1270 1280 1290 1300
LLAPGVHNII AIADGYQQQH SQVFVHHDAA SSVVIVFDTD NRIFGLPREL
1310 1320 1330 1340 1350
VVTVSGATMS ALILTACIIW CICSIKSNRH KDGFHRLRQH HDEYEDEIRM
1360 1370 1380
MSTGSKKSLL SHEFQDETDT EEETLYSSKH
Length:1,380
Mass (Da):152,931
Last modified:October 3, 2006 - v2
Checksum:i567EC1F0B4B7A0C8
GO
Isoform 2 (identifier: O75976-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MA → MR
     3-249: Missing.

Note: No experimental confirmation available.
Show »
Length:1,133
Mass (Da):126,487
Checksum:iD253BDC1BA9B56B6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti863A → V in BAH14780 (PubMed:14702039).Curated1
Sequence conflicti896D → V (PubMed:9714835).Curated1
Sequence conflicti896D → V (PubMed:9355738).Curated1
Sequence conflicti948M → I in BAH14780 (PubMed:14702039).Curated1
Sequence conflicti1336R → W in BAH13725 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02777136K → E1 PublicationCorresponds to variant dbSNP:rs17857300Ensembl.1
Natural variantiVAR_027772454E → G1 PublicationCorresponds to variant dbSNP:rs17857301Ensembl.1
Natural variantiVAR_027773505H → N1 PublicationCorresponds to variant dbSNP:rs17854355Ensembl.1
Natural variantiVAR_027774899T → I. Corresponds to variant dbSNP:rs1860543Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0458331 – 2MA → MR in isoform 2. 1 Publication2
Alternative sequenceiVSP_0458343 – 249Missing in isoform 2. 1 PublicationAdd BLAST247

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85390 mRNA. Translation: BAA33370.1.
U65090 mRNA. Translation: AAC51775.2.
AK302497 mRNA. Translation: BAH13725.1.
AK316409 mRNA. Translation: BAH14780.1.
AC006050 Genomic DNA. No translation available.
AC090685 Genomic DNA. No translation available.
BC045549 mRNA. Translation: AAH45549.1.
BC045624 mRNA. Translation: AAH45624.1.
BC051702 mRNA. Translation: AAH51702.1.
CCDSiCCDS11257.1. [O75976-1]
CCDS56025.1. [O75976-2]
RefSeqiNP_001186704.1. NM_001199775.1. [O75976-2]
NP_001295.2. NM_001304.4. [O75976-1]
UniGeneiHs.446079.

Genome annotation databases

EnsembliENST00000225719; ENSP00000225719; ENSG00000108582. [O75976-1]
ENST00000543464; ENSP00000444443; ENSG00000108582. [O75976-2]
GeneIDi1362.
KEGGihsa:1362.
UCSCiuc002hfb.3. human. [O75976-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCBPD_HUMAN
AccessioniPrimary (citable) accession number: O75976
Secondary accession number(s): B7Z7T9
, B7ZAU4, F5GZH6, O15377, Q86SH9, Q86XE6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 3, 2006
Last modified: November 22, 2017
This is version 161 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families