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

Glycerol-3-phosphate dehydrogenase 1-like protein

Gene

GPD1L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in regulating cardiac sodium current; decreased enzymatic activity with resulting increased levels of glycerol 3-phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway, may ultimately lead to decreased sodium current; cardiac sodium current may also be reduced due to alterations of NAD(H) balance induced by DPD1L.2 Publications

Catalytic activityi

sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43NADBy similarity1
Binding sitei99NADBy similarity1
Binding sitei122SubstrateBy similarity1
Binding sitei155NAD; via amide nitrogen1 Publication1
Active sitei206Proton acceptor1
Binding sitei271NADBy similarity1
Binding sitei298NAD; via amide nitrogen1 Publication1
Binding sitei300NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 17NAD1 Publication6

GO - Molecular functioni

  • glycerol-3-phosphate dehydrogenase [NAD+] activity Source: Reactome
  • ion channel binding Source: BHF-UCL
  • NAD binding Source: InterPro
  • sodium channel regulator activity Source: BHF-UCL

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • glycerol-3-phosphate catabolic process Source: InterPro
  • NADH metabolic process Source: Ensembl
  • NAD metabolic process Source: BHF-UCL
  • negative regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • negative regulation of protein kinase C signaling Source: BHF-UCL
  • phosphatidic acid biosynthetic process Source: Reactome
  • positive regulation of protein localization to cell surface Source: BHF-UCL
  • positive regulation of sodium ion transport Source: BHF-UCL
  • regulation of heart rate Source: BHF-UCL
  • regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
  • regulation of ventricular cardiac muscle cell membrane depolarization Source: BHF-UCL
  • triglyceride biosynthetic process Source: Reactome
  • ventricular cardiac muscle cell action potential Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-HSA-1483166. Synthesis of PA.
R-HSA-75109. Triglyceride Biosynthesis.

Chemistry databases

SwissLipidsiSLP:000000146.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase 1-like protein (EC:1.1.1.8)
Short name:
GPD1-L
Gene namesi
Name:GPD1L
Synonyms:KIAA0089
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:28956. GPD1L.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • glycerol-3-phosphate dehydrogenase complex Source: InterPro
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Brugada syndrome 2 (BRGDA2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset.
See also OMIM:611777
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_044047280A → V in BRGDA2; decreased enzymatic activity; affects SCN5A membrane expression; reduction of sodium current when coexpressed with SCN5A in HEK cells. 3 PublicationsCorresponds to variant rs72552291dbSNPEnsembl.1
Sudden infant death syndrome (SIDS)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionSIDS is the sudden death of an infant younger than 1 year that remains unexplained after a thorough case investigation, including performance of a complete autopsy, examination of the death scene, and review of clinical history. Pathophysiologic mechanisms for SIDS may include respiratory dysfunction, cardiac dysrhythmias, cardiorespiratory instability, and inborn errors of metabolism, but definitive pathogenic mechanisms precipitating an infant sudden death remain elusive.
See also OMIM:272120
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04404483E → K in SIDS; decreased enzymatic activity and significant reduction of sodium current when coexpressed with SCN5A in HEK cells. 2 PublicationsCorresponds to variant rs72552292dbSNPEnsembl.1
Natural variantiVAR_044045124I → V in SIDS; significant reduction of sodium current when coexpressed with SCN5A in HEK cells. 1 PublicationCorresponds to variant rs72552293dbSNPEnsembl.1
Natural variantiVAR_044046273R → C in SIDS; significant reduction of sodium current when coexpressed with SCN5A in HEK cells. 1 PublicationCorresponds to variant rs72552294dbSNPEnsembl.1

Keywords - Diseasei

Brugada syndrome, Disease mutation

Organism-specific databases

DisGeNETi23171.
MalaCardsiGPD1L.
MIMi272120. phenotype.
611777. phenotype.
OpenTargetsiENSG00000152642.
Orphaneti130. Brugada syndrome.
PharmGKBiPA134986345.

Polymorphism and mutation databases

BioMutaiGPD1L.
DMDMi74750945.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002865111 – 351Glycerol-3-phosphate dehydrogenase 1-like proteinAdd BLAST351

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei291N6-succinyllysineBy similarity1
Modified residuei328PhosphotyrosineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N335.
MaxQBiQ8N335.
PaxDbiQ8N335.
PeptideAtlasiQ8N335.
PRIDEiQ8N335.

PTM databases

iPTMnetiQ8N335.
PhosphoSitePlusiQ8N335.

Expressioni

Tissue specificityi

Most highly expressed in heart tissue, with lower levels in the skeletal muscle, kidney, lung and other organs.1 Publication

Gene expression databases

BgeeiENSG00000152642.
CleanExiHS_GPD1L.
ExpressionAtlasiQ8N335. baseline and differential.
GenevisibleiQ8N335. HS.

Organism-specific databases

HPAiHPA035284.

Interactioni

Subunit structurei

Interacts with SCN5A.2 Publications

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi116783. 29 interactors.
STRINGi9606.ENSP00000282541.

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 11Combined sources4
Helixi15 – 28Combined sources14
Beta strandi38 – 41Combined sources4
Helixi52 – 59Combined sources8
Turni63 – 65Combined sources3
Beta strandi75 – 79Combined sources5
Helixi81 – 85Combined sources5
Beta strandi89 – 93Combined sources5
Helixi97 – 99Combined sources3
Helixi100 – 107Combined sources8
Beta strandi116 – 119Combined sources4
Beta strandi124 – 127Combined sources4
Beta strandi130 – 133Combined sources4
Helixi134 – 142Combined sources9
Beta strandi144 – 152Combined sources9
Helixi155 – 159Combined sources5
Beta strandi164 – 169Combined sources6
Helixi173 – 183Combined sources11
Beta strandi188 – 194Combined sources7
Helixi196 – 218Combined sources23
Helixi223 – 244Combined sources22
Beta strandi245 – 247Combined sources3
Helixi251 – 254Combined sources4
Turni257 – 259Combined sources3
Helixi260 – 269Combined sources10
Helixi271 – 282Combined sources12
Helixi286 – 294Combined sources9
Helixi301 – 315Combined sources15
Helixi318 – 320Combined sources3
Helixi322 – 332Combined sources11
Helixi339 – 345Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PLAX-ray2.51A/B1-349[»]
ProteinModelPortaliQ8N335.
SMRiQ8N335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N335.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni271 – 272Substrate binding2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2711. Eukaryota.
COG0240. LUCA.
GeneTreeiENSGT00390000003114.
HOGENOMiHOG000246855.
HOVERGENiHBG003669.
InParanoidiQ8N335.
KOiK00006.
OMAiIINNEHE.
OrthoDBiEOG091G0DO6.
PhylomeDBiQ8N335.
TreeFamiTF300836.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8N335-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAPLKVCI VGSGNWGSAV AKIIGNNVKK LQKFASTVKM WVFEETVNGR
60 70 80 90 100
KLTDIINNDH ENVKYLPGHK LPENVVAMSN LSEAVQDADL LVFVIPHQFI
110 120 130 140 150
HRICDEITGR VPKKALGITL IKGIDEGPEG LKLISDIIRE KMGIDISVLM
160 170 180 190 200
GANIANEVAA EKFCETTIGS KVMENGLLFK ELLQTPNFRI TVVDDADTVE
210 220 230 240 250
LCGALKNIVA VGAGFCDGLR CGDNTKAAVI RLGLMEMIAF ARIFCKGQVS
260 270 280 290 300
TATFLESCGV ADLITTCYGG RNRRVAEAFA RTGKTIEELE KEMLNGQKLQ
310 320 330 340 350
GPQTSAEVYR ILKQKGLLDK FPLFTAVYQI CYESRPVQEM LSCLQSHPEH

T
Length:351
Mass (Da):38,419
Last modified:October 1, 2002 - v1
Checksum:i74C3B27EEB41DE89
GO

Sequence cautioni

The sequence BAA07648 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04404483E → K in SIDS; decreased enzymatic activity and significant reduction of sodium current when coexpressed with SCN5A in HEK cells. 2 PublicationsCorresponds to variant rs72552292dbSNPEnsembl.1
Natural variantiVAR_044045124I → V in SIDS; significant reduction of sodium current when coexpressed with SCN5A in HEK cells. 1 PublicationCorresponds to variant rs72552293dbSNPEnsembl.1
Natural variantiVAR_032114178L → F.Corresponds to variant rs35447795dbSNPEnsembl.1
Natural variantiVAR_044046273R → C in SIDS; significant reduction of sodium current when coexpressed with SCN5A in HEK cells. 1 PublicationCorresponds to variant rs72552294dbSNPEnsembl.1
Natural variantiVAR_044047280A → V in BRGDA2; decreased enzymatic activity; affects SCN5A membrane expression; reduction of sodium current when coexpressed with SCN5A in HEK cells. 3 PublicationsCorresponds to variant rs72552291dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D42047 mRNA. Translation: BAA07648.1. Different initiation.
AK292808 mRNA. Translation: BAF85497.1.
CH471055 Genomic DNA. Translation: EAW64422.1.
BC006168 mRNA. Translation: AAH06168.1.
BC028726 mRNA. Translation: AAH28726.1.
CCDSiCCDS33729.1.
RefSeqiNP_055956.1. NM_015141.3.
UniGeneiHs.82432.

Genome annotation databases

EnsembliENST00000282541; ENSP00000282541; ENSG00000152642.
GeneIDi23171.
KEGGihsa:23171.
UCSCiuc003cew.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D42047 mRNA. Translation: BAA07648.1. Different initiation.
AK292808 mRNA. Translation: BAF85497.1.
CH471055 Genomic DNA. Translation: EAW64422.1.
BC006168 mRNA. Translation: AAH06168.1.
BC028726 mRNA. Translation: AAH28726.1.
CCDSiCCDS33729.1.
RefSeqiNP_055956.1. NM_015141.3.
UniGeneiHs.82432.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PLAX-ray2.51A/B1-349[»]
ProteinModelPortaliQ8N335.
SMRiQ8N335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116783. 29 interactors.
STRINGi9606.ENSP00000282541.

Chemistry databases

SwissLipidsiSLP:000000146.

PTM databases

iPTMnetiQ8N335.
PhosphoSitePlusiQ8N335.

Polymorphism and mutation databases

BioMutaiGPD1L.
DMDMi74750945.

Proteomic databases

EPDiQ8N335.
MaxQBiQ8N335.
PaxDbiQ8N335.
PeptideAtlasiQ8N335.
PRIDEiQ8N335.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000282541; ENSP00000282541; ENSG00000152642.
GeneIDi23171.
KEGGihsa:23171.
UCSCiuc003cew.4. human.

Organism-specific databases

CTDi23171.
DisGeNETi23171.
GeneCardsiGPD1L.
GeneReviewsiGPD1L.
HGNCiHGNC:28956. GPD1L.
HPAiHPA035284.
MalaCardsiGPD1L.
MIMi272120. phenotype.
611777. phenotype.
611778. gene.
neXtProtiNX_Q8N335.
OpenTargetsiENSG00000152642.
Orphaneti130. Brugada syndrome.
PharmGKBiPA134986345.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2711. Eukaryota.
COG0240. LUCA.
GeneTreeiENSGT00390000003114.
HOGENOMiHOG000246855.
HOVERGENiHBG003669.
InParanoidiQ8N335.
KOiK00006.
OMAiIINNEHE.
OrthoDBiEOG091G0DO6.
PhylomeDBiQ8N335.
TreeFamiTF300836.

Enzyme and pathway databases

ReactomeiR-HSA-1483166. Synthesis of PA.
R-HSA-75109. Triglyceride Biosynthesis.

Miscellaneous databases

ChiTaRSiGPD1L. human.
EvolutionaryTraceiQ8N335.
GenomeRNAii23171.
PROiQ8N335.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000152642.
CleanExiHS_GPD1L.
ExpressionAtlasiQ8N335. baseline and differential.
GenevisibleiQ8N335. HS.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGPD1L_HUMAN
AccessioniPrimary (citable) accession number: Q8N335
Secondary accession number(s): A8K9U3, Q14702, Q9BRM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 131 of the entry and version 1 of the sequence. [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 3
    Human chromosome 3: 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. 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.