Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q3ULJ0

- GPD1L_MOUSE

UniProt

Q3ULJ0 - GPD1L_MOUSE

Protein

Glycerol-3-phosphate dehydrogenase 1-like protein

Gene

Gpd1l

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (15 May 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei43 – 431NADBy similarity
    Binding sitei99 – 991NADBy similarity
    Binding sitei122 – 1221SubstrateBy similarity
    Binding sitei155 – 1551NAD; via amide nitrogenBy similarity
    Active sitei206 – 2061Proton acceptorBy similarity
    Binding sitei271 – 2711NADBy similarity
    Binding sitei298 – 2981NAD; via amide nitrogenBy similarity
    Binding sitei300 – 3001NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 176NADBy similarity

    GO - Molecular functioni

    1. glycerol-3-phosphate dehydrogenase [NAD+] activity Source: UniProtKB-EC
    2. NAD binding Source: InterPro
    3. sodium channel regulator activity Source: Ensembl

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. glycerol-3-phosphate catabolic process Source: InterPro
    3. NADH metabolic process Source: MGI
    4. negative regulation of peptidyl-serine phosphorylation Source: Ensembl
    5. negative regulation of protein kinase C signaling Source: Ensembl
    6. positive regulation of protein localization to cell surface Source: Ensembl
    7. positive regulation of sodium ion transport Source: Ensembl
    8. regulation of heart rate Source: Ensembl
    9. regulation of sodium ion transmembrane transporter activity Source: Ensembl
    10. regulation of ventricular cardiac muscle cell membrane depolarization Source: Ensembl
    11. ventricular cardiac muscle cell action potential Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_188640. Synthesis of PA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycerol-3-phosphate dehydrogenase 1-like protein (EC:1.1.1.8)
    Gene namesi
    Name:Gpd1l
    Synonyms:Kiaa0089
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1289257. Gpd1l.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. glycerol-3-phosphate dehydrogenase complex Source: InterPro
    2. membrane Source: BHF-UCL
    3. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351Glycerol-3-phosphate dehydrogenase 1-like proteinPRO_0000286512Add
    BLAST

    Proteomic databases

    MaxQBiQ3ULJ0.
    PaxDbiQ3ULJ0.
    PRIDEiQ3ULJ0.

    PTM databases

    PhosphoSiteiQ3ULJ0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ3ULJ0.
    BgeeiQ3ULJ0.
    CleanExiMM_GPD1L.
    GenevestigatoriQ3ULJ0.

    Interactioni

    Subunit structurei

    Interacts with SCN5A.By similarity

    Protein-protein interaction databases

    IntActiQ3ULJ0. 1 interaction.
    MINTiMINT-4113076.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3ULJ0.
    SMRiQ3ULJ0. Positions 4-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni271 – 2722Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0240.
    GeneTreeiENSGT00390000003114.
    HOGENOMiHOG000246855.
    HOVERGENiHBG003669.
    InParanoidiQ3ULJ0.
    KOiK00006.
    OMAiKIFCKGQ.
    OrthoDBiEOG7ZKSBS.
    PhylomeDBiQ3ULJ0.
    TreeFamiTF300836.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    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]
    PANTHERiPTHR11728. PTHR11728. 1 hit.
    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.
    TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q3ULJ0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAAPLKVCI VGSGNWGSAV AKIIGSNVKT LQKFSSTVKM WVFEETVNGR    50
    KLTDIINNDH ENVKYLPGHK LPENVVAVPN LSEAVQDADL LVFVIPHQFI 100
    HKICDEITGR VPEKALGITL IKGIDEGPDG LKLISDIIRE KMGIDISVLM 150
    GANIASEVAA EKFCETTIGS KVMQNGLLFK ELLQTPNFRI TVVDDADTVE 200
    LCGALKNIVA VGAGFCDGLR CGDNTKAAVI RLGLMEMIAF AKIFCKGQVS 250
    TATFLESCGV ADLITTCYGG RNRRVAEAFA RTGKTIEELE KELLNGQKLQ 300
    GPQTSAEVYR ILRQKGLLDK FPLFTAVYQI CYEGRPVTQM LSCLQSHPEH 350
    I 351
    Length:351
    Mass (Da):38,226
    Last modified:May 15, 2007 - v2
    Checksum:iBE192D41F592E577
    GO
    Isoform 2 (identifier: Q3ULJ0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         321-351: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:320
    Mass (Da):34,634
    Checksum:i690C96D09F52BC54
    GO

    Sequence cautioni

    The sequence AAH37729.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD32164.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261S → G in BAC36001. (PubMed:16141072)Curated
    Sequence conflicti179 – 1791F → S in BAC36001. (PubMed:16141072)Curated
    Sequence conflicti202 – 2021C → W in BAC36001. (PubMed:16141072)Curated
    Sequence conflicti212 – 2121G → V in BAC36001. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei321 – 35131Missing in isoform 2. 1 PublicationVSP_025062Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK172886 mRNA. Translation: BAD32164.1. Different initiation.
    AK050572 mRNA. Translation: BAC34327.1.
    AK075845 mRNA. Translation: BAC36001.1.
    AK145475 mRNA. Translation: BAE26458.1.
    BC037729 mRNA. Translation: AAH37729.1. Different initiation.
    CCDSiCCDS23598.1. [Q3ULJ0-1]
    RefSeqiNP_780589.3. NM_175380.5. [Q3ULJ0-1]
    UniGeneiMm.38198.

    Genome annotation databases

    EnsembliENSMUST00000084853; ENSMUSP00000081913; ENSMUSG00000050627. [Q3ULJ0-2]
    ENSMUST00000146623; ENSMUSP00000117509; ENSMUSG00000050627. [Q3ULJ0-1]
    GeneIDi333433.
    KEGGimmu:333433.
    UCSCiuc009ryj.2. mouse. [Q3ULJ0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK172886 mRNA. Translation: BAD32164.1 . Different initiation.
    AK050572 mRNA. Translation: BAC34327.1 .
    AK075845 mRNA. Translation: BAC36001.1 .
    AK145475 mRNA. Translation: BAE26458.1 .
    BC037729 mRNA. Translation: AAH37729.1 . Different initiation.
    CCDSi CCDS23598.1. [Q3ULJ0-1 ]
    RefSeqi NP_780589.3. NM_175380.5. [Q3ULJ0-1 ]
    UniGenei Mm.38198.

    3D structure databases

    ProteinModelPortali Q3ULJ0.
    SMRi Q3ULJ0. Positions 4-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q3ULJ0. 1 interaction.
    MINTi MINT-4113076.

    PTM databases

    PhosphoSitei Q3ULJ0.

    Proteomic databases

    MaxQBi Q3ULJ0.
    PaxDbi Q3ULJ0.
    PRIDEi Q3ULJ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000084853 ; ENSMUSP00000081913 ; ENSMUSG00000050627 . [Q3ULJ0-2 ]
    ENSMUST00000146623 ; ENSMUSP00000117509 ; ENSMUSG00000050627 . [Q3ULJ0-1 ]
    GeneIDi 333433.
    KEGGi mmu:333433.
    UCSCi uc009ryj.2. mouse. [Q3ULJ0-1 ]

    Organism-specific databases

    CTDi 23171.
    MGIi MGI:1289257. Gpd1l.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0240.
    GeneTreei ENSGT00390000003114.
    HOGENOMi HOG000246855.
    HOVERGENi HBG003669.
    InParanoidi Q3ULJ0.
    KOi K00006.
    OMAi KIFCKGQ.
    OrthoDBi EOG7ZKSBS.
    PhylomeDBi Q3ULJ0.
    TreeFami TF300836.

    Enzyme and pathway databases

    Reactomei REACT_188640. Synthesis of PA.

    Miscellaneous databases

    NextBioi 399982.
    PROi Q3ULJ0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q3ULJ0.
    Bgeei Q3ULJ0.
    CleanExi MM_GPD1L.
    Genevestigatori Q3ULJ0.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    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 ]
    PANTHERi PTHR11728. PTHR11728. 1 hit.
    Pfami PF07479. NAD_Gly3P_dh_C. 1 hit.
    PF01210. NAD_Gly3P_dh_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000114. Glycerol-3-P_dh. 1 hit.
    PRINTSi PR00077. GPDHDRGNASE.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR03376. glycerol3P_DH. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Stomach and Thymus.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Eye.
    4. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 207-220, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.

    Entry informationi

    Entry nameiGPD1L_MOUSE
    AccessioniPrimary (citable) accession number: Q3ULJ0
    Secondary accession number(s): Q6A0D2
    , Q8BVZ7, Q8BWM5, Q8CFN6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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

    External Data

    Dasty 3