GEPH_RAT
ID GEPH_RAT Reviewed; 768 AA.
AC Q03555;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Gephyrin;
DE AltName: Full=Putative glycine receptor-tubulin linker protein;
DE Includes:
DE RecName: Full=Molybdopterin adenylyltransferase;
DE Short=MPT adenylyltransferase;
DE EC=2.7.7.75 {ECO:0000305|PubMed:9990024};
DE AltName: Full=Domain G;
DE Includes:
DE RecName: Full=Molybdopterin molybdenumtransferase;
DE Short=MPT Mo-transferase;
DE EC=2.10.1.1 {ECO:0000305|PubMed:9990024};
DE AltName: Full=Domain E;
GN Name=Gphn; Synonyms=Gph;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=1319186; DOI=10.1016/0896-6273(92)90136-2;
RA Prior P., Schmitt B., Grenningloh G., Pribilla I., Multhaup G.,
RA Beyreuther K., Maulet Y., Werner P., Langosch D., Kirsch J., Betz H.;
RT "Primary structure and alternative splice variants of gephyrin, a putative
RT glycine receptor-tubulin linker protein.";
RL Neuron 8:1161-1170(1992).
RN [2]
RP SEQUENCE REVISION TO 255.
RA Schmitt B.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND INTERACTION
RP WITH GLRB.
RX PubMed=11083919; DOI=10.1006/mcne.2000.0899;
RA Meier J., De Chaldee M., Triller A., Vannier C.;
RT "Functional heterogeneity of gephyrins.";
RL Mol. Cell. Neurosci. 16:566-577(2000).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, X-RAY
RP CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 348-768 IN COMPLEX WITH GLRB, AND
RP SUBUNIT.
RX PubMed=15201864; DOI=10.1038/sj.emboj.7600256;
RA Sola M., Bavro V.N., Timmins J., Franz T., Ricard-Blum S., Schoehn G.,
RA Ruigrok R.W.H., Paarmann I., Saiyed T., O'Sullivan G.A., Schmitt B.,
RA Betz H., Weissenhorn W.;
RT "Structural basis of dynamic glycine receptor clustering by gephyrin.";
RL EMBO J. 23:2510-2519(2004).
RN [5]
RP FUNCTION.
RX PubMed=8264797; DOI=10.1038/366745a0;
RA Kirsch J., Wolters I., Triller A., Betz H.;
RT "Gephyrin antisense oligonucleotides prevent glycine receptor clustering in
RT spinal neurons.";
RL Nature 366:745-748(1993).
RN [6]
RP INTERACTION WITH GABARAP.
RX PubMed=10900017; DOI=10.1073/pnas.97.15.8594;
RA Kneussel M., Haverkamp S., Fuhrmann J.C., Wang H., Waessle H., Olsen R.W.,
RA Betz H.;
RT "The gamma-aminobutyric acid type A receptor (GABAAR)-associated protein
RT GABARAP interacts with gephyrin but is not involved in receptor anchoring
RT at the synapse.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8594-8599(2000).
RN [7]
RP FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=9990024; DOI=10.1073/pnas.96.4.1333;
RA Stallmeyer B., Schwarz G., Schulze J., Nerlich A., Reiss J., Kirsch J.,
RA Mendel R.R.;
RT "The neurotransmitter receptor-anchoring protein gephyrin reconstitutes
RT molybdenum cofactor biosynthesis in bacteria, plants, and mammalian
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1333-1338(1999).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12684523; DOI=10.1074/jbc.m301070200;
RA Rees M.I., Harvey K., Ward H., White J.H., Evans L., Duguid I.C.,
RA Hsu C.-C., Coleman S.L., Miller J., Baer K., Waldvogel H.J., Gibbon F.,
RA Smart T.G., Owen M.J., Harvey R.J., Snell R.G.;
RT "Isoform heterogeneity of the human gephyrin gene (GPHN), binding domains
RT to the glycine receptor, and mutation analysis in hyperekplexia.";
RL J. Biol. Chem. 278:24688-24696(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201; SER-207 AND SER-283, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-201, AND SUBUNIT.
RX PubMed=11325967; DOI=10.1074/jbc.m101923200;
RA Sola M., Kneussel M., Heck I.S., Betz H., Weissenhorn W.;
RT "X-ray crystal structure of the trimeric N-terminal domain of gephyrin.";
RL J. Biol. Chem. 276:25294-25301(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 350-768 IN COMPLEX WITH GLRB,
RP SUBCELLULAR LOCATION, INTERACTION WITH GLRB, AND MUTAGENESIS OF PHE-362;
RP PRO-745 AND 745-PRO-PRO-746.
RX PubMed=16511563; DOI=10.1038/sj.emboj.7601029;
RA Kim E.Y., Schrader N., Smolinsky B., Bedet C., Vannier C., Schwarz G.,
RA Schindelin H.;
RT "Deciphering the structural framework of glycine receptor anchoring by
RT gephyrin.";
RL EMBO J. 25:1385-1395(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 350-768, INTERACTION WITH GLRB,
RP AND SUBUNIT.
RX PubMed=25137389; DOI=10.1021/cb500303a;
RA Maric H.M., Kasaragod V.B., Schindelin H.;
RT "Modulation of gephyrin-glycine receptor affinity by multivalency.";
RL ACS Chem. Biol. 9:2554-2562(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 350-768 IN COMPLEX WITH GABRA3,
RP INTERACTION WITH GABRA3 AND GLRB, AND SUBUNIT.
RX PubMed=25531214; DOI=10.1038/ncomms6767;
RA Maric H.M., Kasaragod V.B., Hausrat T.J., Kneussel M., Tretter V.,
RA Stromgaard K., Schindelin H.;
RT "Molecular basis of the alternative recruitment of GABA(A) versus glycine
RT receptors through gephyrin.";
RL Nat. Commun. 5:5767-5767(2014).
CC -!- FUNCTION: Microtubule-associated protein involved in membrane protein-
CC cytoskeleton interactions. It is thought to anchor the inhibitory
CC glycine receptor (GLYR) to subsynaptic microtubules (PubMed:8264797).
CC Acts as a major instructive molecule at inhibitory synapses, where it
CC also clusters GABA type A receptors (By similarity).
CC {ECO:0000250|UniProtKB:Q8BUV3, ECO:0000269|PubMed:8264797}.
CC -!- FUNCTION: Has also a catalytic activity and catalyzes two steps in the
CC biosynthesis of the molybdenum cofactor. In the first step,
CC molybdopterin is adenylated. Subsequently, molybdate is inserted into
CC adenylated molybdopterin and AMP is released.
CC {ECO:0000269|PubMed:9990024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC ChEBI:CHEBI:62727; EC=2.7.7.75;
CC Evidence={ECO:0000305|PubMed:9990024};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31332;
CC Evidence={ECO:0000305|PubMed:9990024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; EC=2.10.1.1;
CC Evidence={ECO:0000305|PubMed:9990024};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35048;
CC Evidence={ECO:0000305|PubMed:9990024};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Inhibited by copper and tungsten. {ECO:0000250}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000305|PubMed:9990024}.
CC -!- SUBUNIT: Homotrimer, homodimer and homooligomer (PubMed:11325967,
CC PubMed:25137389, PubMed:25531214). Interacts with SRGAP2 (via SH3
CC domain) (By similarity). Interacts with GLRB (PubMed:15201864,
CC PubMed:16511563, PubMed:25137389, PubMed:25531214). Interacts with
CC GABARAP (PubMed:10900017). Interacts with GABRA3 (PubMed:25531214).
CC GABRA3 and GLRB occupy overlapping binding sites (PubMed:25531214).
CC Interacts with ARHGAP32; IQSEC3, INSYN1 and INSYN2A (By similarity).
CC {ECO:0000250|UniProtKB:Q8BUV3, ECO:0000269|PubMed:10900017,
CC ECO:0000269|PubMed:11325967, ECO:0000269|PubMed:15201864,
CC ECO:0000269|PubMed:16511563}.
CC -!- INTERACTION:
CC Q03555; P48168: Glrb; Xeno; NbExp=4; IntAct=EBI-349317, EBI-7069198;
CC Q03555-6; P20236: Gabra3; NbExp=5; IntAct=EBI-5273276, EBI-5273284;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:16511563}; Lipid-anchor
CC {ECO:0000305|PubMed:16511563}; Cytoplasmic side
CC {ECO:0000269|PubMed:16511563}. Cell membrane
CC {ECO:0000269|PubMed:12684523}; Lipid-anchor
CC {ECO:0000305|PubMed:12684523}; Cytoplasmic side
CC {ECO:0000305|PubMed:12684523}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9NQX3}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16511563}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9NQX3}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q8BUV3}. Note=Cytoplasmic face of glycinergic
CC postsynaptic membranes (PubMed:16511563). Forms clusters at synapses
CC (By similarity). {ECO:0000250|UniProtKB:Q8BUV3,
CC ECO:0000269|PubMed:16511563}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=6;
CC IsoId=Q03555-1; Sequence=Displayed;
CC Name=1; Synonyms=GE124'56;
CC IsoId=Q03555-2; Sequence=VSP_003238;
CC Name=2; Synonyms=GE236;
CC IsoId=Q03555-3; Sequence=VSP_003239, VSP_003240, VSP_003243;
CC Name=3; Synonyms=GE24'6;
CC IsoId=Q03555-4; Sequence=VSP_003239;
CC Name=4; Synonyms=GE245;
CC IsoId=Q03555-5; Sequence=VSP_003241, VSP_003242;
CC Name=5; Synonyms=GE26;
CC IsoId=Q03555-6; Sequence=VSP_003239, VSP_003243;
CC -!- TISSUE SPECIFICITY: Expressed in tissues including spinal cord, brain,
CC liver, kidney and lung.
CC -!- PTM: Phosphorylated.
CC -!- PTM: Palmitoylated. Palmitoylation is stimulated by GABA type A
CC receptors activity. Palmitoylation by ZDHHC12 regulates clustering at
CC synapses. {ECO:0000250|UniProtKB:Q8BUV3}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {ECO:0000305}.
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DR EMBL; X66366; CAA47009.2; -; mRNA.
DR PIR; JH0681; JH0681.
DR RefSeq; NP_074056.2; NM_022865.3. [Q03555-6]
DR PDB; 1IHC; X-ray; 1.90 A; A=1-201.
DR PDB; 1T3E; X-ray; 3.25 A; A/B=348-768.
DR PDB; 2FTS; X-ray; 2.41 A; A=350-768.
DR PDB; 2FU3; X-ray; 2.70 A; A/B=350-768.
DR PDB; 4PD0; X-ray; 1.70 A; A=350-768.
DR PDB; 4PD1; X-ray; 1.98 A; A=350-768.
DR PDB; 4TK1; X-ray; 2.70 A; A/B=350-768.
DR PDB; 4TK2; X-ray; 4.10 A; A/B=350-768.
DR PDB; 4TK3; X-ray; 2.70 A; A/B=350-768.
DR PDB; 4TK4; X-ray; 3.60 A; A/B=350-768.
DR PDB; 4U90; X-ray; 2.00 A; A=350-768.
DR PDB; 4U91; X-ray; 2.00 A; A=350-768.
DR PDB; 5ERQ; X-ray; 1.55 A; A=350-768.
DR PDB; 5ERR; X-ray; 1.65 A; A=350-768.
DR PDB; 5ERS; X-ray; 1.70 A; A=350-768.
DR PDB; 5ERT; X-ray; 2.00 A; A=350-768.
DR PDB; 5ERU; X-ray; 1.60 A; A=350-768.
DR PDB; 5ERV; X-ray; 1.80 A; A=350-768.
DR PDB; 6FGC; X-ray; 1.50 A; A=350-768.
DR PDB; 6FGD; X-ray; 1.50 A; A=350-768.
DR PDB; 6HSN; X-ray; 1.55 A; A=350-768.
DR PDB; 6HSO; X-ray; 1.95 A; A=350-768.
DR PDBsum; 1IHC; -.
DR PDBsum; 1T3E; -.
DR PDBsum; 2FTS; -.
DR PDBsum; 2FU3; -.
DR PDBsum; 4PD0; -.
DR PDBsum; 4PD1; -.
DR PDBsum; 4TK1; -.
DR PDBsum; 4TK2; -.
DR PDBsum; 4TK3; -.
DR PDBsum; 4TK4; -.
DR PDBsum; 4U90; -.
DR PDBsum; 4U91; -.
DR PDBsum; 5ERQ; -.
DR PDBsum; 5ERR; -.
DR PDBsum; 5ERS; -.
DR PDBsum; 5ERT; -.
DR PDBsum; 5ERU; -.
DR PDBsum; 5ERV; -.
DR PDBsum; 6FGC; -.
DR PDBsum; 6FGD; -.
DR PDBsum; 6HSN; -.
DR PDBsum; 6HSO; -.
DR AlphaFoldDB; Q03555; -.
DR SMR; Q03555; -.
DR BioGRID; 249211; 10.
DR DIP; DIP-33263N; -.
DR IntAct; Q03555; 9.
DR MINT; Q03555; -.
DR STRING; 10116.ENSRNOP00000064099; -.
DR iPTMnet; Q03555; -.
DR PhosphoSitePlus; Q03555; -.
DR SwissPalm; Q03555; -.
DR jPOST; Q03555; -.
DR PRIDE; Q03555; -.
DR ABCD; Q03555; 3 sequenced antibodies.
DR Ensembl; ENSRNOT00000100642; ENSRNOP00000091082; ENSRNOG00000064046. [Q03555-1]
DR Ensembl; ENSRNOT00000101616; ENSRNOP00000083857; ENSRNOG00000064630. [Q03555-3]
DR Ensembl; ENSRNOT00000104959; ENSRNOP00000097129; ENSRNOG00000064630. [Q03555-5]
DR Ensembl; ENSRNOT00000106781; ENSRNOP00000082928; ENSRNOG00000064046. [Q03555-5]
DR Ensembl; ENSRNOT00000107245; ENSRNOP00000082164; ENSRNOG00000064630. [Q03555-1]
DR Ensembl; ENSRNOT00000108357; ENSRNOP00000093484; ENSRNOG00000064046. [Q03555-3]
DR GeneID; 64845; -.
DR KEGG; rno:64845; -.
DR UCSC; RGD:69194; rat. [Q03555-1]
DR CTD; 10243; -.
DR RGD; 69194; Gphn.
DR eggNOG; KOG2371; Eukaryota.
DR GeneTree; ENSGT00390000016577; -.
DR InParanoid; Q03555; -.
DR OrthoDB; 1114121at2759; -.
DR PhylomeDB; Q03555; -.
DR Reactome; R-RNO-947581; Molybdenum cofactor biosynthesis.
DR UniPathway; UPA00344; -.
DR EvolutionaryTrace; Q03555; -.
DR PRO; PR:Q03555; -.
DR Proteomes; UP000002494; Chromosome 6.
DR GO; GO:0099144; C:anchored component of synaptic membrane; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0099572; C:postsynaptic specialization; IDA:SynGO.
DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:GOC.
DR GO; GO:0099091; C:postsynaptic specialization, intracellular component; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0097060; C:synaptic membrane; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:RGD.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IDA:MGI.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISO:RGD.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IDA:MGI.
DR GO; GO:0008940; F:nitrate reductase activity; ISO:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; TAS:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0015631; F:tubulin binding; TAS:RGD.
DR GO; GO:0045184; P:establishment of protein localization; IMP:BHF-UCL.
DR GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; ISO:RGD.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; ISS:UniProtKB.
DR GO; GO:0072579; P:glycine receptor clustering; ISO:RGD.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:MGI.
DR GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IBA:GO_Central.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; ISO:RGD.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0098970; P:postsynaptic neurotransmitter receptor diffusion trapping; ISO:RGD.
DR GO; GO:0006605; P:protein targeting; TAS:RGD.
DR GO; GO:0010038; P:response to metal ion; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; IEP:RGD.
DR CDD; cd00887; MoeA; 1.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 2.40.340.10; -; 1.
DR Gene3D; 3.40.980.10; -; 2.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR PANTHER; PTHR10192; PTHR10192; 2.
DR Pfam; PF00994; MoCF_biosynth; 2.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 2.
DR SUPFAM; SSF53218; SSF53218; 2.
DR SUPFAM; SSF63867; SSF63867; 1.
DR SUPFAM; SSF63882; SSF63882; 1.
DR TIGRFAMs; TIGR00177; molyb_syn; 2.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Molybdenum;
KW Molybdenum cofactor biosynthesis; Multifunctional enzyme;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Synapse; Transferase.
FT CHAIN 1..768
FT /note="Gephyrin"
FT /id="PRO_0000170965"
FT REGION 14..166
FT /note="MPT Mo-transferase"
FT REGION 153..348
FT /note="Interaction with GABARAP"
FT /evidence="ECO:0000269|PubMed:10900017"
FT REGION 194..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..768
FT /note="MPT adenylyltransferase"
FT COMPBIAS 219..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQX3"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUV3"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUV3"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUV3"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQX3"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUV3"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQX3"
FT LIPID 225
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQX3"
FT LIPID 297
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQX3"
FT VAR_SEQ 1..22
FT /note="MATEGMILTNHDHQIRVGVLTV -> MSFPLSPAFTLLHILV (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:11083919"
FT /id="VSP_003238"
FT VAR_SEQ 99..111
FT /note="Missing (in isoform 5, isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11083919,
FT ECO:0000303|PubMed:1319186"
FT /id="VSP_003239"
FT VAR_SEQ 256
FT /note="K -> KNHPFYTSPAVFMANHGQPIPGLISYSHHATGSADKR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11083919"
FT /id="VSP_003240"
FT VAR_SEQ 302..320
FT /note="Missing (in isoform 5 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:11083919,
FT ECO:0000303|PubMed:1319186"
FT /id="VSP_003243"
FT VAR_SEQ 302..315
FT /note="QIRRPDESKGVASR -> ARLPSCSSTYSVSE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11083919"
FT /id="VSP_003241"
FT VAR_SEQ 316..320
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11083919"
FT /id="VSP_003242"
FT MUTAGEN 362
FT /note="F->A: Reduced GLRB binding."
FT /evidence="ECO:0000269|PubMed:16511563"
FT MUTAGEN 745..746
FT /note="PP->AA: Reduced GLRB binding."
FT /evidence="ECO:0000269|PubMed:16511563"
FT MUTAGEN 745
FT /note="P->A: Loss of GLRB binding."
FT /evidence="ECO:0000269|PubMed:16511563"
FT CONFLICT 255
FT /note="A -> R (in Ref. 3)"
FT /evidence="ECO:0000305"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:1IHC"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:1IHC"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1IHC"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:1IHC"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1IHC"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:1IHC"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:1IHC"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1IHC"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:1IHC"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1IHC"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:1IHC"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:1IHC"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1IHC"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:1IHC"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:1IHC"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1IHC"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:1IHC"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:1IHC"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:6HSN"
FT HELIX 358..368
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:6FGC"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 402..410
FT /evidence="ECO:0007829|PDB:6FGC"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 416..425
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:6FGC"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 462..467
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 471..479
FT /evidence="ECO:0007829|PDB:6FGC"
FT TURN 485..488
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:6FGC"
FT HELIX 511..520
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 524..528
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:6FGC"
FT HELIX 558..568
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 573..579
FT /evidence="ECO:0007829|PDB:6FGC"
FT HELIX 583..596
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 598..604
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:5ERQ"
FT TURN 610..613
FT /evidence="ECO:0007829|PDB:5ERQ"
FT HELIX 614..620
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 625..632
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 640..646
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 649..656
FT /evidence="ECO:0007829|PDB:6FGC"
FT HELIX 660..678
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 688..695
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 704..711
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:1T3E"
FT STRAND 720..723
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 728..730
FT /evidence="ECO:0007829|PDB:2FTS"
FT HELIX 733..735
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 740..744
FT /evidence="ECO:0007829|PDB:6FGC"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:6HSN"
FT STRAND 759..764
FT /evidence="ECO:0007829|PDB:6FGC"
SQ SEQUENCE 768 AA; 83266 MW; FAD1B6DD76ED79EA CRC64;
MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG GTISAYKIVP
DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEKF PTFPFCGLQK GATKEVIERE
APGMALAMLM GSLNVTPLGM LSRPVCGIRG KTLIINLPGS KKGSQECFQF ILPALPHAID
LLRDAIVKVK EVHDELEDLP SPPPPLSPPP TTSPHKQTED KGVQCEEEEE EKKDSGVAST
EDSSSSHITA AALAAKIPDS IISRGVQVLP RDTASLSTTP SESPRAQATS RLSTASCPTP
KQIRRPDESK GVASRVGSLK VQSRCSSKEN ILRASHSAVD ITKVARRHRM SPFPLTSMDK
AFITVLEMTP VLGTEIINYR DGMGRVLAQD VYAKDNLPPF PASVKDGYAV RAADGPGDRF
IIGESQAGEQ PTQTVMPGQV MRVTTGAPIP CGADAVVQVE DTELIRESDD GTEELEVRIL
VQARPGQDIR PIGHDIKRGE CVLAKGTHMG PSEIGLLATV GVTEVEVNKF PVVAVMSTGN
ELLNPEDDLL PGKIRDSNRS TLLATIQEHG YPTINLGIVG DNPDDLLNAL NEGISRADVI
ITSGGVSMGE KDYLKQVLDI DLHAQIHFGR VFMKPGLPTT FATLDIDGVR KIIFALPGNP
VSAVVTCNLF VVPALRKMQG ILDPRPTIIK ARLSCDVKLD PRPEYHRCIL TWHHQEPLPW
AQSTGNQMSS RLMSMRSANG LLMLPPKTEQ YVELHKGEVV DVMVIGRL
