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Q03555

- GEPH_RAT

UniProt

Q03555 - GEPH_RAT

Protein

Gephyrin

Gene

Gphn

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (16 May 2006)
      Previous versions | rss
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    Functioni

    Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules By similarity. Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.By similarity2 Publications

    Catalytic activityi

    ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.
    Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Inhibited by copper and tungsten.By similarity

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. molybdopterin adenylyltransferase activity Source: MGI
    4. molybdopterin molybdotransferase activity Source: MGI
    5. protein binding Source: UniProtKB
    6. protein binding, bridging Source: RGD
    7. protein complex scaffold Source: RGD
    8. protein homodimerization activity Source: RGD
    9. receptor binding Source: RGD
    10. tubulin binding Source: RGD

    GO - Biological processi

    1. establishment of protein localization Source: BHF-UCL
    2. Mo-molybdopterin cofactor biosynthetic process Source: MGI
    3. protein homooligomerization Source: RGD
    4. protein targeting Source: RGD
    5. synapse assembly Source: RGD

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Molybdenum, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00344.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gephyrin
    Alternative name(s):
    Putative glycine receptor-tubulin linker protein
    Including the following 2 domains:
    Molybdopterin adenylyltransferase (EC:2.7.7.75)
    Short name:
    MPT adenylyltransferase
    Alternative name(s):
    Domain G
    Molybdopterin molybdenumtransferase (EC:2.10.1.1)
    Short name:
    MPT Mo-transferase
    Alternative name(s):
    Domain E
    Gene namesi
    Name:Gphn
    Synonyms:Gph
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi69194. Gphn.

    Subcellular locationi

    Cell junctionsynapse 1 Publication. Cell junctionsynapsepostsynaptic cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Cytoplasmic face of glycinergic postsynaptic membranes.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: RGD
    3. cytoskeleton Source: UniProtKB-SubCell
    4. inhibitory synapse Source: BHF-UCL
    5. postsynaptic membrane Source: UniProtKB-SubCell
    6. synapse Source: RGD

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi362 – 3621F → A: Reduced GLRB binding. 1 Publication
    Mutagenesisi745 – 7462PP → AA: Reduced GLRB binding. 1 Publication
    Mutagenesisi745 – 7451P → A: Loss of GLRB binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 768768GephyrinPRO_0000170965Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei201 – 2011PhosphoserineBy similarity
    Modified residuei207 – 2071PhosphoserineBy similarity
    Modified residuei279 – 2791PhosphothreonineBy similarity
    Modified residuei337 – 3371PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ03555.
    PRIDEiQ03555.

    PTM databases

    PhosphoSiteiQ03555.

    Expressioni

    Tissue specificityi

    Expressed in tissues including spinal cord, brain, liver, kidney and lung.

    Gene expression databases

    GenevestigatoriQ03555.

    Interactioni

    Subunit structurei

    Homotrimer, homodimer and homooligomer. Interacts with SRGAP2 (via SH3 domain) By similarity. Interacts with GLRB and GABARAP.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Gabra3P202365EBI-5273276,EBI-5273284
    GlrbP481684EBI-349317,EBI-7069198From a different organism.

    Protein-protein interaction databases

    BioGridi249211. 8 interactions.
    DIPiDIP-33263N.
    IntActiQ03555. 5 interactions.
    MINTiMINT-241818.

    Structurei

    Secondary structure

    1
    768
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 227
    Helixi24 – 274
    Helixi34 – 4411
    Turni46 – 494
    Beta strandi52 – 598
    Helixi63 – 7513
    Beta strandi80 – 867
    Beta strandi89 – 913
    Helixi112 – 1165
    Beta strandi118 – 1203
    Helixi122 – 13514
    Helixi137 – 1415
    Beta strandi146 – 1494
    Beta strandi152 – 1576
    Helixi161 – 17111
    Helixi172 – 1743
    Helixi175 – 1828
    Helixi188 – 1936
    Beta strandi355 – 3573
    Helixi358 – 36811
    Beta strandi374 – 3785
    Helixi379 – 3813
    Beta strandi386 – 3894
    Beta strandi397 – 4004
    Beta strandi402 – 4109
    Helixi412 – 4143
    Beta strandi418 – 4247
    Beta strandi439 – 4435
    Beta strandi455 – 4584
    Helixi459 – 4613
    Beta strandi462 – 4687
    Beta strandi469 – 4724
    Beta strandi474 – 4796
    Turni485 – 4884
    Beta strandi494 – 4963
    Beta strandi501 – 5033
    Helixi511 – 52010
    Beta strandi524 – 5285
    Beta strandi533 – 5386
    Helixi558 – 56710
    Turni568 – 5703
    Beta strandi573 – 5797
    Helixi583 – 59614
    Beta strandi598 – 6047
    Beta strandi607 – 6093
    Helixi612 – 6198
    Turni620 – 6223
    Beta strandi625 – 6328
    Beta strandi640 – 6467
    Beta strandi649 – 6568
    Helixi660 – 67819
    Beta strandi688 – 6958
    Beta strandi704 – 7118
    Beta strandi716 – 7183
    Beta strandi720 – 7234
    Beta strandi728 – 7303
    Beta strandi740 – 7445
    Beta strandi752 – 7543
    Beta strandi759 – 7646

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IHCX-ray1.90A1-201[»]
    1T3EX-ray3.25A/B348-768[»]
    2FTSX-ray2.41A350-768[»]
    2FU3X-ray2.70A/B350-768[»]
    ProteinModelPortaliQ03555.
    SMRiQ03555. Positions 13-194, 350-768.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03555.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 166153MPT Mo-transferaseAdd
    BLAST
    Regioni153 – 348196Interaction with GABARAPAdd
    BLAST
    Regioni326 – 768443MPT adenylyltransferaseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi213 – 2186Glu-rich (acidic)

    Sequence similaritiesi

    In the N-terminal section; belongs to the MoaB/Mog family.Curated
    In the C-terminal section; belongs to the MoeA family.Curated

    Phylogenomic databases

    eggNOGiCOG0303.
    HOGENOMiHOG000280651.
    HOVERGENiHBG005828.
    InParanoidiQ03555.
    KOiK15376.
    PhylomeDBiQ03555.

    Family and domain databases

    Gene3Di2.40.340.10. 1 hit.
    3.40.980.10. 2 hits.
    InterProiIPR020817. Mo_cofactor_synthesis.
    IPR008284. MoCF_biosynth_CS.
    IPR005111. MoeA_C_domain_IV.
    IPR005110. MoeA_linker/N.
    IPR001453. Mopterin-bd_dom.
    [Graphical view]
    PfamiPF00994. MoCF_biosynth. 2 hits.
    PF03454. MoeA_C. 1 hit.
    PF03453. MoeA_N. 1 hit.
    [Graphical view]
    SMARTiSM00852. MoCF_biosynth. 2 hits.
    [Graphical view]
    SUPFAMiSSF53218. SSF53218. 2 hits.
    SSF63867. SSF63867. 1 hit.
    SSF63882. SSF63882. 1 hit.
    TIGRFAMsiTIGR00177. molyb_syn. 2 hits.
    PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
    PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 6 (identifier: Q03555-1) [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

    MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG    50
    GTISAYKIVP DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEKF 100
    PTFPFCGLQK GATKEVIERE APGMALAMLM GSLNVTPLGM LSRPVCGIRG 150
    KTLIINLPGS KKGSQECFQF ILPALPHAID LLRDAIVKVK EVHDELEDLP 200
    SPPPPLSPPP TTSPHKQTED KGVQCEEEEE EKKDSGVAST EDSSSSHITA 250
    AALAAKIPDS IISRGVQVLP RDTASLSTTP SESPRAQATS RLSTASCPTP 300
    KQIRRPDESK GVASRVGSLK VQSRCSSKEN ILRASHSAVD ITKVARRHRM 350
    SPFPLTSMDK AFITVLEMTP VLGTEIINYR DGMGRVLAQD VYAKDNLPPF 400
    PASVKDGYAV RAADGPGDRF IIGESQAGEQ PTQTVMPGQV MRVTTGAPIP 450
    CGADAVVQVE DTELIRESDD GTEELEVRIL VQARPGQDIR PIGHDIKRGE 500
    CVLAKGTHMG PSEIGLLATV GVTEVEVNKF PVVAVMSTGN ELLNPEDDLL 550
    PGKIRDSNRS TLLATIQEHG YPTINLGIVG DNPDDLLNAL NEGISRADVI 600
    ITSGGVSMGE KDYLKQVLDI DLHAQIHFGR VFMKPGLPTT FATLDIDGVR 650
    KIIFALPGNP VSAVVTCNLF VVPALRKMQG ILDPRPTIIK ARLSCDVKLD 700
    PRPEYHRCIL TWHHQEPLPW AQSTGNQMSS RLMSMRSANG LLMLPPKTEQ 750
    YVELHKGEVV DVMVIGRL 768
    Length:768
    Mass (Da):83,266
    Last modified:May 16, 2006 - v3
    Checksum:iFAD1B6DD76ED79EA
    GO
    Isoform 1 (identifier: Q03555-2) [UniParc]FASTAAdd to Basket

    Also known as: GE124'56

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: MATEGMILTNHDHQIRVGVLTV → MSFPLSPAFTLLHILV

    Show »
    Length:762
    Mass (Da):82,616
    Checksum:iCF467AB5D3BE99BE
    GO
    Isoform 2 (identifier: Q03555-3) [UniParc]FASTAAdd to Basket

    Also known as: GE236

    The sequence of this isoform differs from the canonical sequence as follows:
         99-111: Missing.
         256-256: K → KNHPFYTSPAVFMANHGQPIPGLISYSHHATGSADKR
         302-320: Missing.

    Show »
    Length:772
    Mass (Da):83,638
    Checksum:iD25D2294184BE3D4
    GO
    Isoform 3 (identifier: Q03555-4) [UniParc]FASTAAdd to Basket

    Also known as: GE24'6

    The sequence of this isoform differs from the canonical sequence as follows:
         99-111: Missing.

    Show »
    Length:755
    Mass (Da):81,814
    Checksum:i219EC28CC2910AC1
    GO
    Isoform 4 (identifier: Q03555-5) [UniParc]FASTAAdd to Basket

    Also known as: GE245

    The sequence of this isoform differs from the canonical sequence as follows:
         302-315: QIRRPDESKGVASR → ARLPSCSSTYSVSE
         316-320: Missing.

    Show »
    Length:763
    Mass (Da):82,669
    Checksum:i5E6039E40BDA68ED
    GO
    Isoform 5 (identifier: Q03555-6) [UniParc]FASTAAdd to Basket

    Also known as: GE26

    The sequence of this isoform differs from the canonical sequence as follows:
         99-111: Missing.
         302-320: Missing.

    Show »
    Length:736
    Mass (Da):79,748
    Checksum:iB3817E1BE1D4D41B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti255 – 2551A → R(PubMed:11083919)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2222MATEG…GVLTV → MSFPLSPAFTLLHILV in isoform 1. 1 PublicationVSP_003238Add
    BLAST
    Alternative sequencei99 – 11113Missing in isoform 5, isoform 2 and isoform 3. 2 PublicationsVSP_003239Add
    BLAST
    Alternative sequencei256 – 2561K → KNHPFYTSPAVFMANHGQPI PGLISYSHHATGSADKR in isoform 2. 1 PublicationVSP_003240
    Alternative sequencei302 – 32019Missing in isoform 5 and isoform 2. 2 PublicationsVSP_003243Add
    BLAST
    Alternative sequencei302 – 31514QIRRP…GVASR → ARLPSCSSTYSVSE in isoform 4. 1 PublicationVSP_003241Add
    BLAST
    Alternative sequencei316 – 3205Missing in isoform 4. 1 PublicationVSP_003242

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66366 mRNA. Translation: CAA47009.2.
    PIRiJH0681.
    RefSeqiNP_074056.2. NM_022865.3. [Q03555-6]
    UniGeneiRn.11032.

    Genome annotation databases

    GeneIDi64845.
    KEGGirno:64845.
    UCSCiRGD:69194. rat. [Q03555-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66366 mRNA. Translation: CAA47009.2 .
    PIRi JH0681.
    RefSeqi NP_074056.2. NM_022865.3. [Q03555-6 ]
    UniGenei Rn.11032.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IHC X-ray 1.90 A 1-201 [» ]
    1T3E X-ray 3.25 A/B 348-768 [» ]
    2FTS X-ray 2.41 A 350-768 [» ]
    2FU3 X-ray 2.70 A/B 350-768 [» ]
    ProteinModelPortali Q03555.
    SMRi Q03555. Positions 13-194, 350-768.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249211. 8 interactions.
    DIPi DIP-33263N.
    IntActi Q03555. 5 interactions.
    MINTi MINT-241818.

    PTM databases

    PhosphoSitei Q03555.

    Proteomic databases

    PaxDbi Q03555.
    PRIDEi Q03555.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 64845.
    KEGGi rno:64845.
    UCSCi RGD:69194. rat. [Q03555-1 ]

    Organism-specific databases

    CTDi 10243.
    RGDi 69194. Gphn.

    Phylogenomic databases

    eggNOGi COG0303.
    HOGENOMi HOG000280651.
    HOVERGENi HBG005828.
    InParanoidi Q03555.
    KOi K15376.
    PhylomeDBi Q03555.

    Enzyme and pathway databases

    UniPathwayi UPA00344 .

    Miscellaneous databases

    EvolutionaryTracei Q03555.
    NextBioi 613764.
    PROi Q03555.

    Gene expression databases

    Genevestigatori Q03555.

    Family and domain databases

    Gene3Di 2.40.340.10. 1 hit.
    3.40.980.10. 2 hits.
    InterProi IPR020817. Mo_cofactor_synthesis.
    IPR008284. MoCF_biosynth_CS.
    IPR005111. MoeA_C_domain_IV.
    IPR005110. MoeA_linker/N.
    IPR001453. Mopterin-bd_dom.
    [Graphical view ]
    Pfami PF00994. MoCF_biosynth. 2 hits.
    PF03454. MoeA_C. 1 hit.
    PF03453. MoeA_N. 1 hit.
    [Graphical view ]
    SMARTi SM00852. MoCF_biosynth. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53218. SSF53218. 2 hits.
    SSF63867. SSF63867. 1 hit.
    SSF63882. SSF63882. 1 hit.
    TIGRFAMsi TIGR00177. molyb_syn. 2 hits.
    PROSITEi PS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
    PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and alternative splice variants of gephyrin, a putative glycine receptor-tubulin linker protein."
      Prior P., Schmitt B., Grenningloh G., Pribilla I., Multhaup G., Beyreuther K., Maulet Y., Werner P., Langosch D., Kirsch J., Betz H.
      Neuron 8:1161-1170(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PARTIAL PROTEIN SEQUENCE.
      Strain: Wistar.
      Tissue: Brain.
    2. Schmitt B.
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 255.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
    4. Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 348-768 IN COMPLEX WITH GLRB, SUBUNIT.
    5. "Gephyrin antisense oligonucleotides prevent glycine receptor clustering in spinal neurons."
      Kirsch J., Wolters I., Triller A., Betz H.
      Nature 366:745-748(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The gamma-aminobutyric acid type A receptor (GABAAR)-associated protein GABARAP interacts with gephyrin but is not involved in receptor anchoring at the synapse."
      Kneussel M., Haverkamp S., Fuhrmann J.C., Wang H., Waessle H., Olsen R.W., Betz H.
      Proc. Natl. Acad. Sci. U.S.A. 97:8594-8599(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GABARAP.
    7. "The neurotransmitter receptor-anchoring protein gephyrin reconstitutes molybdenum cofactor biosynthesis in bacteria, plants, and mammalian cells."
      Stallmeyer B., Schwarz G., Schulze J., Nerlich A., Reiss J., Kirsch J., Mendel R.R.
      Proc. Natl. Acad. Sci. U.S.A. 96:1333-1338(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "X-ray crystal structure of the trimeric N-terminal domain of gephyrin."
      Sola M., Kneussel M., Heck I.S., Betz H., Weissenhorn W.
      J. Biol. Chem. 276:25294-25301(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-201, SUBUNIT.
    9. "Deciphering the structural framework of glycine receptor anchoring by gephyrin."
      Kim E.Y., Schrader N., Smolinsky B., Bedet C., Vannier C., Schwarz G., Schindelin H.
      EMBO J. 25:1385-1395(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 350-768 IN COMPLEX WITH GLRB, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-362; PRO-745 AND 745-PRO-PRO-746.

    Entry informationi

    Entry nameiGEPH_RAT
    AccessioniPrimary (citable) accession number: Q03555
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 148 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3