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

Glycerophosphodiester phosphodiesterase domain-containing protein 5

Gene

Gdpd5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Promotes neurite formation. Cooperates with PRDX1 to drive postmitotic motor neuron differentiation. The glycerophosphodiester phosphodiesterase activity may be required for its role in neuronal differentiation. May contribute to the osmotic regulation of cellular glycerophosphocholine.2 Publications

GO - Molecular functioni

GO - Biological processi

  • cerebral cortex neuron differentiation Source: MGI
  • glycerophospholipid catabolic process Source: Reactome
  • negative regulation of Notch signaling pathway Source: CACAO
  • neuron projection development Source: MGI
  • positive regulation of cell cycle Source: CACAO
  • positive regulation of neuron differentiation Source: CACAO
  • regulation of timing of cell differentiation Source: MGI
  • spinal cord motor neuron differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Neurogenesis

Enzyme and pathway databases

BRENDAi3.1.4.44. 3474.
3.1.4.46. 3474.
ReactomeiR-MMU-6814848. Glycerophospholipid catabolism.

Chemistry

SwissLipidsiSLP:000000668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerophosphodiester phosphodiesterase domain-containing protein 5 (EC:3.1.-.-)
Alternative name(s):
Glycerophosphodiester phosphodiesterase 2
Gene namesi
Name:Gdpd5
Synonyms:Gde2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2686926. Gdpd5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4242CytoplasmicSequence analysisAdd
BLAST
Transmembranei43 – 6321HelicalSequence analysisAdd
BLAST
Topological domaini64 – 8926ExtracellularSequence analysisAdd
BLAST
Transmembranei90 – 11021HelicalSequence analysisAdd
BLAST
Topological domaini111 – 12515CytoplasmicSequence analysisAdd
BLAST
Transmembranei126 – 14621HelicalSequence analysisAdd
BLAST
Topological domaini147 – 16014ExtracellularSequence analysisAdd
BLAST
Transmembranei161 – 18121HelicalSequence analysisAdd
BLAST
Topological domaini182 – 19211CytoplasmicSequence analysisAdd
BLAST
Transmembranei193 – 21321HelicalSequence analysisAdd
BLAST
Topological domaini214 – 496283ExtracellularSequence analysisAdd
BLAST
Transmembranei497 – 51721HelicalSequence analysisAdd
BLAST
Topological domaini518 – 60790CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: CACAO
  • endoplasmic reticulum membrane Source: Reactome
  • growth cone Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • neuronal cell body Source: CACAO
  • perinuclear endoplasmic reticulum Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 607607Glycerophosphodiester phosphodiesterase domain-containing protein 5PRO_0000251942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi15 ↔ 18Sequence analysis
Disulfide bondi25 ↔ 571By similarity
Glycosylationi301 – 3011N-linked (GlcNAc...)Sequence analysis
Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence analysis
Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence analysis
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence analysis
Glycosylationi448 – 4481N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Intramolecular disulfide bond between Cys-25 and Cys-571 is reduced by PRDX1.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ640M6.
PaxDbiQ640M6.
PeptideAtlasiQ640M6.
PRIDEiQ640M6.

PTM databases

iPTMnetiQ640M6.
PhosphoSiteiQ640M6.

Expressioni

Tissue specificityi

Detected in brain, lung, heart, kidney and testis.1 Publication

Inductioni

Up-regulated during neuronal differentiation by retinoic acid.1 Publication

Gene expression databases

BgeeiENSMUSG00000035314.
GenevisibleiQ640M6. MM.

Interactioni

Subunit structurei

Interacts with PRDX1; forms a mixed-disulfide with PRDX1, leading to disrupt intramolecular disulfide bond between Cys-25 and Cys-571.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000036175.

Structurei

3D structure databases

ProteinModelPortaliQ640M6.
SMRiQ640M6. Positions 228-476.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini228 – 485258GP-PDEAdd
BLAST

Sequence similaritiesi

Contains 1 GP-PDE domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2258. Eukaryota.
COG0584. LUCA.
GeneTreeiENSGT00510000046457.
HOGENOMiHOG000232101.
HOVERGENiHBG081551.
InParanoidiQ640M6.
OMAiWEVHNDY.
OrthoDBiEOG091G043H.
PhylomeDBiQ640M6.
TreeFamiTF313692.

Family and domain databases

Gene3Di3.20.20.190. 1 hit.
InterProiIPR004129. GlyceroP-diester-Pdiesterase.
IPR030395. GP_PDE_dom.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
[Graphical view]
PANTHERiPTHR23344. PTHR23344. 1 hit.
PfamiPF03009. GDPD. 1 hit.
[Graphical view]
SUPFAMiSSF51695. SSF51695. 1 hit.
PROSITEiPS51704. GP_PDE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q640M6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRHQPLQYY EPQLCLSCLT GIYGCRWKRY QRSHDDTTPW ERLWFLLLVC
60 70 80 90 100
TFSLTLTWLY FWWGVHNDYD EFNWYLYNRM GYWSDWSVPI LVTSAAAFTY
110 120 130 140 150
IAGLLVLALC HIAVGQQLNL HWIHKMGLVV ILASTVVAMS AVAQLWEDEW
160 170 180 190 200
EVLLISLQGT APFLHIGALV AITALSWIVA GQFARAERSS SQLTILCTFF
210 220 230 240 250
AVVFTFYLIP LTISSPCIME KKDLGPKPAL IGHRGAPMLA PEHTVMSFRK
260 270 280 290 300
ALEQRLYGLQ ADITISLDGV PFLMHDTTLR RTTNVEHLFP ELARRPAAML
310 320 330 340 350
NWTVLQRLNA GQWFLKTDPF WTASSLSPSD HREVQNQSIC SLAELLELAK
360 370 380 390 400
GNASLLLNLR DPPRDHPYRG SFLNVTLEAV LRSGFPQHQV MWLFNRQRPL
410 420 430 440 450
VRKMAPGFQQ TSGSKEAIAN LRKGHIQKLN LRYTQVSHQE LRDYASWNLS
460 470 480 490 500
VNLYTVNAPW LFSLLWCAGV PSVTSDNSHT LSRVPSPLWI MPPDEYCLMW
510 520 530 540 550
VTADLISFSL IIGIFVLQKW RLGGIRSYNP EQIMLSAAVR RTSRDVSIMK
560 570 580 590 600
EKLIFSEISD GVEVSDELSV CSDSSYDTYA NANSTATPVG PRNAGSRAKT

VTEQSGH
Length:607
Mass (Da):68,890
Last modified:October 25, 2004 - v1
Checksum:i3FF90C40A866E992
GO

Sequence cautioni

The sequence AAH26428 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti399 – 3991P → L in AAH24955 (PubMed:15489334).Curated
Sequence conflicti567 – 5671E → G in AAH26428 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK141189 mRNA. Translation: BAE24577.1.
AK154771 mRNA. Translation: BAE32819.1.
BC024955 mRNA. Translation: AAH24955.1.
BC026428 mRNA. Translation: AAH26428.1. Different initiation.
BC082585 mRNA. Translation: AAH82585.1.
CCDSiCCDS21481.1.
RefSeqiNP_958740.2. NM_201352.2.
UniGeneiMm.286317.

Genome annotation databases

EnsembliENSMUST00000037528; ENSMUSP00000036175; ENSMUSG00000035314.
GeneIDi233552.
KEGGimmu:233552.
UCSCiuc009ilo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK141189 mRNA. Translation: BAE24577.1.
AK154771 mRNA. Translation: BAE32819.1.
BC024955 mRNA. Translation: AAH24955.1.
BC026428 mRNA. Translation: AAH26428.1. Different initiation.
BC082585 mRNA. Translation: AAH82585.1.
CCDSiCCDS21481.1.
RefSeqiNP_958740.2. NM_201352.2.
UniGeneiMm.286317.

3D structure databases

ProteinModelPortaliQ640M6.
SMRiQ640M6. Positions 228-476.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000036175.

Chemistry

SwissLipidsiSLP:000000668.

PTM databases

iPTMnetiQ640M6.
PhosphoSiteiQ640M6.

Proteomic databases

MaxQBiQ640M6.
PaxDbiQ640M6.
PeptideAtlasiQ640M6.
PRIDEiQ640M6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037528; ENSMUSP00000036175; ENSMUSG00000035314.
GeneIDi233552.
KEGGimmu:233552.
UCSCiuc009ilo.1. mouse.

Organism-specific databases

CTDi81544.
MGIiMGI:2686926. Gdpd5.

Phylogenomic databases

eggNOGiKOG2258. Eukaryota.
COG0584. LUCA.
GeneTreeiENSGT00510000046457.
HOGENOMiHOG000232101.
HOVERGENiHBG081551.
InParanoidiQ640M6.
OMAiWEVHNDY.
OrthoDBiEOG091G043H.
PhylomeDBiQ640M6.
TreeFamiTF313692.

Enzyme and pathway databases

BRENDAi3.1.4.44. 3474.
3.1.4.46. 3474.
ReactomeiR-MMU-6814848. Glycerophospholipid catabolism.

Miscellaneous databases

ChiTaRSiGdpd5. mouse.
PROiQ640M6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000035314.
GenevisibleiQ640M6. MM.

Family and domain databases

Gene3Di3.20.20.190. 1 hit.
InterProiIPR004129. GlyceroP-diester-Pdiesterase.
IPR030395. GP_PDE_dom.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
[Graphical view]
PANTHERiPTHR23344. PTHR23344. 1 hit.
PfamiPF03009. GDPD. 1 hit.
[Graphical view]
SUPFAMiSSF51695. SSF51695. 1 hit.
PROSITEiPS51704. GP_PDE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGDPD5_MOUSE
AccessioniPrimary (citable) accession number: Q640M6
Secondary accession number(s): Q8R0T5, Q8R3N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 25, 2004
Last modified: September 7, 2016
This is version 95 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.