LipidDB-9606-00639

Lipid Modification Database

Tag

Content

LipidDB ID

LipidDB-9606-00639

Entry Name

UniProt Accession

O75976; B7Z7T9; B7ZAU4; F5GZH6; O15377; Q86SH9; Q86XE6;

Theoretical PI

5.68

Molecular Weight

152931.06

Genbank Protein ID

BAA33370.1; AAC51775.2; BAH13725.1; BAH14780.1; AAH45549.1; AAH45624.1; AAH51702.1;

Genbank Nucleotide ID

D85390; U65090; AK302497; AK316409; AC006050; AC090685; BC045549; BC045624; BC051702;

Protein Name

Carboxypeptidase D

Protein Synonyms/Alias

3.4.17.22; Metallocarboxypeptidase D; gp180;

Gene Name

CPD

Gene Synonyms/Alias

Created Date

15-NOV-2002

Lipid Modification Sites
Position	Sequence Form	Peptide	References	Modification Type
1317	Canonical	SALILTACIIWCICS	[1]	S-Palmitoylation
1321	Canonical	LTACIIWCICSIKSN	[1]	S-Palmitoylation
1323	Canonical	ACIIWCICSIKSNRH	[1]	S-Palmitoylation

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Kalinina EV, Fricker LD. Palmitoylation of carboxypeptidase D. Implicationsfor intracellular trafficking. J Biol Chem. 2003 Mar 14;278(11):9244-9. PubMedPMID: 12643288.[PMID:12643288]

Functional Description

Sequence Annotation

Topological domain: 32 1299 Extracellular.
Transmembrane: 1300 1320 Helical.
Topological domain: 1321 1380 Cytoplasmic.
Region: 32 493 Carboxypeptidase-like 1.
Region: 494 897 Carboxypeptidase-like 2.
Region: 898 1299 Carboxypeptidase-like 3.
Motif: 162 164 Cell attachment site.
Active site: 350 350 Nucleophile 1.
Active site: 762 762 Nucleophile 2.
Metal binding site: 139 139 Zinc 1.
Metal binding site: 142 142 Zinc 1.
Metal binding site: 257 257 Zinc 1.
Metal binding site: 564 564 Zinc 2.
Metal binding site: 567 567 Zinc 2.
Metal binding site: 671 671 Zinc 2.
Modified residue: 1358 1358 Phosphoserine.
Modified residue: 1361 1361 Phosphoserine.
Modified residue: 1368 1368 Phosphothreonine.
Modified residue: 1370 1370 Phosphothreonine.

Protein Length

1380 AA.

Protein Sequence
(Canonical)

MASGRDERPP WRLGRLLLLM CLLLLGSSAR AAHIKKAEAT TTTTSAGAEA AEGQFDRYYH  60
EEELESALRE AAAAGLPGLA RLFSIGRSVE GRPLWVLRLT AGLGSLIPEG DAGPDAAGPD  120
AAGPLLPGRP QVKLVGNMHG DETVSRQVLI YLARELAAGY RRGDPRLVRL LNTTDVYLLP  180
SLNPDGFERA REGDCGFGDG GPSGASGRDN SRGRDLNRSF PDQFSTGEPP ALDEVPEVRA  240
LIEWIRRNKF VLSGNLHGGS VVASYPFDDS PEHKATGIYS KTSDDEVFKY LAKAYASNHP  300
IMKTGEPHCP GDEDETFKDG ITNGAHWYDV EGGMQDYNYV WANCFEITLE LSCCKYPPAS  360
QLRQEWENNR ESLITLIEKV HIGVKGFVKD SITGSGLENA TISVAGINHN ITTGRFGDFY  420
RLLVPGTYNL TVVLTGYMPL TVTNVVVKEG PATEVDFSLR PTVTSVIPDT TEAVSTASTV  480
AIPNILSGTS SSYQPIQPKD FHHHHFPDME IFLRRFANEY PNITRLYSLG KSVESRELYV  540
MEISDNPGVH EPGEPEFKYI GNMHGNEVVG RELLLNLIEY LCKNFGTDPE VTDLVHNTRI  600
HLMPSMNPDG YEKSQEGDSI SVIGRNNSNN FDLNRNFPDQ FVQITDPTQP ETIAVMSWMK  660
SYPFVLSANL HGGSLVVNYP FDDDEQGLAT YSKSPDDAVF QQIALSYSKE NSQMFQGRPC  720
KNMYPNEYFP HGITNGASWY NVPGGMQDWN YLQTNCFEVT IELGCVKYPL EKELPNFWEQ  780
NRRSLIQFMK QVHQGVRGFV LDATDGRGIL NATISVAEIN HPVTTYKTGD YWRLLVPGTY  840
KITASARGYN PVTKNVTVKS EGAIQVNFTL VRSSTDSNNE SKKGKGASSS TNDASDPTTK  900
EFETLIKDLS AENGLESLML RSSSNLALAL YRYHSYKDLS EFLRGLVMNY PHITNLTNLG  960
QSTEYRHIWS LEISNKPNVS EPEEPKIRFV AGIHGNAPVG TELLLALAEF LCLNYKKNPA  1020
VTQLVDRTRI VIVPSLNPDG RERAQEKDCT SKIGQTNARG KDLDTDFTNN ASQPETKAII  1080
ENLIQKQDFS LSVALDGGSM LVTYPYDKPV QTVENKETLK HLASLYANNH PSMHMGQPSC  1140
PNKSDENIPG GVMRGAEWHS HLGSMKDYSV TYGHCPEITV YTSCCYFPSA ARLPSLWADN  1200
KRSLLSMLVE VHKGVHGFVK DKTGKPISKA VIVLNEGIKV QTKEGGYFHV LLAPGVHNII  1260
AIADGYQQQH SQVFVHHDAA SSVVIVFDTD NRIFGLPREL VVTVSGATMS ALILTACIIW  1320
CICSIKSNRH KDGFHRLRQH HDEYEDEIRM MSTGSKKSLL SHEFQDETDT EEETLYSSKH  1380

FASTA
(Canonical)

>LipidDB-9606-00639|O75976
MASGRDERPPWRLGRLLLLMCLLLLGSSARAAHIKKAEATTTTTSAGAEAAEGQFDRYYH
EEELESALREAAAAGLPGLARLFSIGRSVEGRPLWVLRLTAGLGSLIPEGDAGPDAAGPD
AAGPLLPGRPQVKLVGNMHGDETVSRQVLIYLARELAAGYRRGDPRLVRLLNTTDVYLLP
SLNPDGFERAREGDCGFGDGGPSGASGRDNSRGRDLNRSFPDQFSTGEPPALDEVPEVRA
LIEWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKATGIYSKTSDDEVFKYLAKAYASNHP
IMKTGEPHCPGDEDETFKDGITNGAHWYDVEGGMQDYNYVWANCFEITLELSCCKYPPAS
QLRQEWENNRESLITLIEKVHIGVKGFVKDSITGSGLENATISVAGINHNITTGRFGDFY
RLLVPGTYNLTVVLTGYMPLTVTNVVVKEGPATEVDFSLRPTVTSVIPDTTEAVSTASTV
AIPNILSGTSSSYQPIQPKDFHHHHFPDMEIFLRRFANEYPNITRLYSLGKSVESRELYV
MEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVHNTRI
HLMPSMNPDGYEKSQEGDSISVIGRNNSNNFDLNRNFPDQFVQITDPTQPETIAVMSWMK
SYPFVLSANLHGGSLVVNYPFDDDEQGLATYSKSPDDAVFQQIALSYSKENSQMFQGRPC
KNMYPNEYFPHGITNGASWYNVPGGMQDWNYLQTNCFEVTIELGCVKYPLEKELPNFWEQ
NRRSLIQFMKQVHQGVRGFVLDATDGRGILNATISVAEINHPVTTYKTGDYWRLLVPGTY
KITASARGYNPVTKNVTVKSEGAIQVNFTLVRSSTDSNNESKKGKGASSSTNDASDPTTK
EFETLIKDLSAENGLESLMLRSSSNLALALYRYHSYKDLSEFLRGLVMNYPHITNLTNLG
QSTEYRHIWSLEISNKPNVSEPEEPKIRFVAGIHGNAPVGTELLLALAEFLCLNYKKNPA
VTQLVDRTRIVIVPSLNPDGRERAQEKDCTSKIGQTNARGKDLDTDFTNNASQPETKAII
ENLIQKQDFSLSVALDGGSMLVTYPYDKPVQTVENKETLKHLASLYANNHPSMHMGQPSC
PNKSDENIPGGVMRGAEWHSHLGSMKDYSVTYGHCPEITVYTSCCYFPSAARLPSLWADN
KRSLLSMLVEVHKGVHGFVKDKTGKPISKAVIVLNEGIKVQTKEGGYFHVLLAPGVHNII
AIADGYQQQHSQVFVHHDAASSVVIVFDTDNRIFGLPRELVVTVSGATMSALILTACIIW
CICSIKSNRHKDGFHRLRQHHDEYEDEIRMMSTGSKKSLLSHEFQDETDTEEETLYSSKH

Gene Ontology

GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IDA:UniProtKB
GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro
GO:0004185; F:serine-type carboxypeptidase activity; TAS:ProtInc
GO:0008270; F:zinc ion binding; IEA:InterPro

Interpro

InterPro; IPR008969; CarboxyPept-like_regulatory
InterPro; IPR014766; CarboxyPept_regulatory_dom
InterPro; IPR015567; Pept_M14B_carboxypept_D2
InterPro; IPR000834; Peptidase_M14

Pfam

Pfam; PF00246; Peptidase_M14;

SMART

SMART; SM00631; Zn_pept;

PROSITE

PROSITE; PS00132; CARBOXYPEPT_ZN_1;
PROSITE; PS00133; CARBOXYPEPT_ZN_2;

PRINTS

PRINTS; PR00765; CRBOXYPTASEA;