CPD

Protein identityUniProt · HPA

UniProt accession

O75976

Gene

CPD

Ensembl

ENSG00000108582

Chromosome

17

Canonical length

1380 aa

Protein class

Enzymes, Predicted intracellular proteins, Predicted membrane proteins

Subcellular location

Cytosol

OverviewNCBI Gene

The metallocarboxypeptidase family of enzymes is divided into 2 subfamilies based on sequence similarities. The pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been identified as a regulatory B-type carboxypeptidase. CPD is a homolog of duck gp180, a hepatitis B virus-binding protein. Transcript variants utilizing alternative polyadenylation signals exist for this gene. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

1380 residues, UniProt reviewed canonical sequence.

>O75976|CPD
     1  MASGRDERPP WRLGRLLLLM CLLLLGSSAR AAHIKKAEAT TTTTSAGAEA AEGQFDRYYH
    61  EEELESALRE AAAAGLPGLA RLFSIGRSVE GRPLWVLRLT AGLGSLIPEG DAGPDAAGPD
   121  AAGPLLPGRP QVKLVGNMHG DETVSRQVLI YLARELAAGY RRGDPRLVRL LNTTDVYLLP
   181  SLNPDGFERA REGDCGFGDG GPSGASGRDN SRGRDLNRSF PDQFSTGEPP ALDEVPEVRA
   241  LIEWIRRNKF VLSGNLHGGS VVASYPFDDS PEHKATGIYS KTSDDEVFKY LAKAYASNHP
   301  IMKTGEPHCP GDEDETFKDG ITNGAHWYDV EGGMQDYNYV WANCFEITLE LSCCKYPPAS
   361  QLRQEWENNR ESLITLIEKV HIGVKGFVKD SITGSGLENA TISVAGINHN ITTGRFGDFY
   421  RLLVPGTYNL TVVLTGYMPL TVTNVVVKEG PATEVDFSLR PTVTSVIPDT TEAVSTASTV
   481  AIPNILSGTS SSYQPIQPKD FHHHHFPDME IFLRRFANEY PNITRLYSLG KSVESRELYV
   541  MEISDNPGVH EPGEPEFKYI GNMHGNEVVG RELLLNLIEY LCKNFGTDPE VTDLVHNTRI
   601  HLMPSMNPDG YEKSQEGDSI SVIGRNNSNN FDLNRNFPDQ FVQITDPTQP ETIAVMSWMK
   661  SYPFVLSANL HGGSLVVNYP FDDDEQGLAT YSKSPDDAVF QQIALSYSKE NSQMFQGRPC
   721  KNMYPNEYFP HGITNGASWY NVPGGMQDWN YLQTNCFEVT IELGCVKYPL EKELPNFWEQ
   781  NRRSLIQFMK QVHQGVRGFV LDATDGRGIL NATISVAEIN HPVTTYKTGD YWRLLVPGTY
   841  KITASARGYN PVTKNVTVKS EGAIQVNFTL VRSSTDSNNE SKKGKGASSS TNDASDPTTK
   901  EFETLIKDLS AENGLESLML RSSSNLALAL YRYHSYKDLS EFLRGLVMNY PHITNLTNLG
   961  QSTEYRHIWS LEISNKPNVS EPEEPKIRFV AGIHGNAPVG TELLLALAEF LCLNYKKNPA
  1021  VTQLVDRTRI VIVPSLNPDG RERAQEKDCT SKIGQTNARG KDLDTDFTNN ASQPETKAII
  1081  ENLIQKQDFS LSVALDGGSM LVTYPYDKPV QTVENKETLK HLASLYANNH PSMHMGQPSC
  1141  PNKSDENIPG GVMRGAEWHS HLGSMKDYSV TYGHCPEITV YTSCCYFPSA ARLPSLWADN
  1201  KRSLLSMLVE VHKGVHGFVK DKTGKPISKA VIVLNEGIKV QTKEGGYFHV LLAPGVHNII
  1261  AIADGYQQQH SQVFVHHDAA SSVVIVFDTD NRIFGLPREL VVTVSGATMS ALILTACIIW
  1321  CICSIKSNRH KDGFHRLRQH HDEYEDEIRM MSTGSKKSLL SHEFQDETDT EEETLYSSKH

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against CPD can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Cell surface

Secreted

No

Transmembrane segments

1

Mean surface accessibility (rSASA)

0.27

Highest tissue expression

54 nTPM

Expression across tissuesHPA

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.43

gnomAD pLI

0

gnomAD missense Z

2.59

DepMap mean gene effect

-0.24

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• peptide metabolic process
• protein processing

Molecular functions

• metallocarboxypeptidase activity
• serine-type carboxypeptidase activity
• zinc ion binding

Cellular components

• extracellular exosome
• extracellular space
• membrane
• plasma membrane

Protein domainsUniProt · Pfam · InterPro

• Peptidase M14, carboxypeptidase A
• Carboxypeptidase-like, regulatory domain superfamily
• Peptidase M14 domain-containing protein
• Zinc carboxypeptidases, zinc-binding region 1
• Zinc carboxypeptidases, zinc-binding region 2
• Zinc carboxypeptidase
• Carboxypeptidase regulatory-like domain
• Carboxypeptidase D, carboxypeptidase-like domain 3
• Carboxypeptidase D, carboxypeptidase-like domain 2

KeywordsUniProt

• Carboxypeptidase
• Cell membrane
• Glycoprotein
• Hydrolase
• Lipoprotein
• Membrane
• Metal-binding
• Metalloprotease
• Palmitate
• Phosphoprotein
• Protease
• Repeat
• Signal
• Transmembrane
• Transmembrane helix
• Zinc

InteractionsUniProt · HPA

Protein binding partners of CPD in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• CANX