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Protein

Glycerophosphodiester phosphodiesterase domain-containing protein 5

Gene

Gdpd5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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
  • lipid metabolic process Source: InterPro
  • 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

Keywordsi

Molecular functionHydrolase
Biological processNeurogenesis

Enzyme and pathway databases

BRENDAi3.1.4.44 3474
3.1.4.46 3474

Chemistry databases

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2686926 Gdpd5

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 domaini1 – 42CytoplasmicSequence analysisAdd BLAST42
Transmembranei43 – 63HelicalSequence analysisAdd BLAST21
Topological domaini64 – 89ExtracellularSequence analysisAdd BLAST26
Transmembranei90 – 110HelicalSequence analysisAdd BLAST21
Topological domaini111 – 125CytoplasmicSequence analysisAdd BLAST15
Transmembranei126 – 146HelicalSequence analysisAdd BLAST21
Topological domaini147 – 160ExtracellularSequence analysisAdd BLAST14
Transmembranei161 – 181HelicalSequence analysisAdd BLAST21
Topological domaini182 – 192CytoplasmicSequence analysisAdd BLAST11
Transmembranei193 – 213HelicalSequence analysisAdd BLAST21
Topological domaini214 – 496ExtracellularSequence analysisAdd BLAST283
Transmembranei497 – 517HelicalSequence analysisAdd BLAST21
Topological domaini518 – 607CytoplasmicSequence analysisAdd BLAST90

Keywords - Cellular componenti

Cell projection, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002519421 – 607Glycerophosphodiester phosphodiesterase domain-containing protein 5Add BLAST607

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi15 ↔ 18Sequence analysis
Disulfide bondi25 ↔ 571By similarity
Glycosylationi301N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi336N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi352N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi374N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi448N-linked (GlcNAc...) asparagineSequence analysis1

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
PhosphoSitePlusiQ640M6

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
ExpressionAtlasiQ640M6 baseline and differential
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
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini228 – 485GP-PDEAdd BLAST258

Sequence similaritiesi

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
InterProiView protein in InterPro
IPR004129 GlyceroP-diester-Pdiesterase
IPR030395 GP_PDE_dom
IPR017946 PLC-like_Pdiesterase_TIM-brl
PANTHERiPTHR23344 PTHR23344, 1 hit
PfamiView protein in Pfam
PF03009 GDPD, 1 hit
SUPFAMiSSF51695 SSF51695, 1 hit
PROSITEiView protein in PROSITE
PS51704 GP_PDE, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti399P → L in AAH24955 (PubMed:15489334).Curated1
Sequence conflicti567E → G in AAH26428 (PubMed:15489334).Curated1

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
XP_017177670.1, XM_017322181.1
UniGeneiMm.286317

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiGDPD5_MOUSE
AccessioniPrimary (citable) accession number: Q640M6
Secondary accession number(s): Q8R0T5, Q8R3N5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 25, 2004
Last modified: April 25, 2018
This is version 104 of the entry and version 1 of the sequence. See 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
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