ID   GEPH_MOUSE              Reviewed;         769 AA.
AC   Q8BUV3; E9QKJ1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Gephyrin;
DE   Includes:
DE     RecName: Full=Molybdopterin adenylyltransferase;
DE              Short=MPT adenylyltransferase;
DE              EC=2.7.7.75 {ECO:0000250|UniProtKB:Q9NQX3};
DE     AltName: Full=Domain G;
DE   Includes:
DE     RecName: Full=Molybdopterin molybdenumtransferase;
DE              Short=MPT Mo-transferase;
DE              EC=2.10.1.1 {ECO:0000250|UniProtKB:Q9NQX3};
DE     AltName: Full=Domain E;
GN   Name=Gphn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-194, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-194; SER-200;
RP   SER-262; THR-265; THR-266; SER-268; SER-270 AND SER-338, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   INTERACTION WITH SRGAP2.
RX   PubMed=22126966; DOI=10.1126/scisignal.2002189;
RA   Okada H., Uezu A., Mason F.M., Soderblom E.J., Moseley M.A. III,
RA   Soderling S.H.;
RT   "SH3 domain-based phototrapping in living cells reveals Rho family GAP
RT   signaling complexes.";
RL   Sci. Signal. 4:RS13-RS13(2011).
RN   [8]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND PALMITOYLATION.
RX   PubMed=25025157; DOI=10.1371/journal.pbio.1001908;
RA   Dejanovic B., Semtner M., Ebert S., Lamkemeyer T., Neuser F., Luescher B.,
RA   Meier J.C., Schwarz G.;
RT   "Palmitoylation of gephyrin controls receptor clustering and plasticity of
RT   GABAergic synapses.";
RL   PLoS Biol. 12:e1001908-e1001908(2014).
RN   [9]
RP   INTERACTION WITH SRGAP2.
RX   PubMed=27373832; DOI=10.1016/j.neuron.2016.06.013;
RA   Fossati M., Pizzarelli R., Schmidt E.R., Kupferman J.V., Stroebel D.,
RA   Polleux F., Charrier C.;
RT   "SRGAP2 and its human-specific paralog co-regulate the development of
RT   excitatory and inhibitory synapses.";
RL   Neuron 91:356-369(2016).
RN   [10]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH ARHGAP32; IQSEC3; INSYN1 AND
RP   INSYN2A.
RX   PubMed=27609886; DOI=10.1126/science.aag0821;
RA   Uezu A., Kanak D.J., Bradshaw T.W., Soderblom E.J., Catavero C.M.,
RA   Burette A.C., Weinberg R.J., Soderling S.H.;
RT   "Identification of an elaborate complex mediating postsynaptic
RT   inhibition.";
RL   Science 353:1123-1129(2016).
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 (By similarity).
CC       Acts as a major instructive molecule at inhibitory synapses, where it
CC       also clusters GABA type A receptors (PubMed:25025157).
CC       {ECO:0000250|UniProtKB:Q03555, ECO:0000269|PubMed:25025157}.
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:0000250|UniProtKB:Q03555}.
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:0000250|UniProtKB:Q9NQX3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31332;
CC         Evidence={ECO:0000250|UniProtKB:Q9NQX3};
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:0000250|UniProtKB:Q9NQX3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35048;
CC         Evidence={ECO:0000250|UniProtKB:Q9NQX3};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by copper and tungsten. {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000250|UniProtKB:Q9NQX3}.
CC   -!- SUBUNIT: Homotrimer, homodimer and homooligomer (PubMed:25025157).
CC       Interacts with SRGAP2 (via SH3 domain) (PubMed:22126966,
CC       PubMed:27373832). Interacts with GLRB (By similarity). Interacts with
CC       GABARAP (By similarity). Interacts with GABRA3 (By similarity). GABRA3
CC       and GLRB occupy overlapping binding sites (By similarity). Interacts
CC       with ARHGAP32; IQSEC3, INSYN1 and INSYN2A (PubMed:27609886).
CC       {ECO:0000250|UniProtKB:Q03555, ECO:0000250|UniProtKB:Q9NQX3,
CC       ECO:0000269|PubMed:22126966, ECO:0000269|PubMed:25025157,
CC       ECO:0000269|PubMed:27373832, ECO:0000269|PubMed:27609886}.
CC   -!- INTERACTION:
CC       Q8BUV3; P48168: Glrb; NbExp=4; IntAct=EBI-771218, EBI-7069198;
CC       Q8BUV3; Q9QUR7: Pin1; NbExp=6; IntAct=EBI-771218, EBI-2432975;
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q03555}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q03555}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q03555}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q03555}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q03555}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q03555}. Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:25025157}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q03555}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q9NQX3}. Postsynaptic density
CC       {ECO:0000269|PubMed:27609886}. Note=Cytoplasmic face of glycinergic
CC       postsynaptic membranes (By similarity). Forms clusters at synapses
CC       (PubMed:25025157). {ECO:0000250|UniProtKB:Q03555,
CC       ECO:0000269|PubMed:25025157}.
CC   -!- PTM: Palmitoylated (PubMed:25025157). Palmitoylation is stimulated by
CC       GABA type A receptors activity (PubMed:25025157). Palmitoylation by
CC       ZDHHC12 regulates clustering at synapses (PubMed:25025157).
CC       {ECO:0000269|PubMed:25025157}.
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; AK082353; BAC38476.1; -; mRNA.
DR   EMBL; AC124346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC125057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC148324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS26000.1; -.
DR   RefSeq; NP_766540.2; NM_172952.3.
DR   AlphaFoldDB; Q8BUV3; -.
DR   SMR; Q8BUV3; -.
DR   BioGRID; 234521; 69.
DR   CORUM; Q8BUV3; -.
DR   ELM; Q8BUV3; -.
DR   IntAct; Q8BUV3; 7.
DR   MINT; Q8BUV3; -.
DR   STRING; 10090.ENSMUSP00000106018; -.
DR   GlyGen; Q8BUV3; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; Q8BUV3; -.
DR   PhosphoSitePlus; Q8BUV3; -.
DR   SwissPalm; Q8BUV3; -.
DR   EPD; Q8BUV3; -.
DR   jPOST; Q8BUV3; -.
DR   MaxQB; Q8BUV3; -.
DR   PaxDb; 10090-ENSMUSP00000106018; -.
DR   PeptideAtlas; Q8BUV3; -.
DR   ProteomicsDB; 266793; -.
DR   Pumba; Q8BUV3; -.
DR   ABCD; Q8BUV3; 3 sequenced antibodies.
DR   Antibodypedia; 144; 490 antibodies from 38 providers.
DR   DNASU; 268566; -.
DR   Ensembl; ENSMUST00000052472.6; ENSMUSP00000054064.5; ENSMUSG00000047454.13.
DR   GeneID; 268566; -.
DR   KEGG; mmu:268566; -.
DR   UCSC; uc007nzc.2; mouse.
DR   AGR; MGI:109602; -.
DR   CTD; 10243; -.
DR   MGI; MGI:109602; Gphn.
DR   VEuPathDB; HostDB:ENSMUSG00000047454; -.
DR   eggNOG; KOG2371; Eukaryota.
DR   GeneTree; ENSGT00390000016577; -.
DR   HOGENOM; CLU_010186_2_2_1; -.
DR   InParanoid; Q8BUV3; -.
DR   OrthoDB; 275356at2759; -.
DR   Reactome; R-MMU-947581; Molybdenum cofactor biosynthesis.
DR   UniPathway; UPA00344; -.
DR   BioGRID-ORCS; 268566; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Gphn; mouse.
DR   PRO; PR:Q8BUV3; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8BUV3; Protein.
DR   Bgee; ENSMUSG00000047454; Expressed in spermatid and 265 other cell types or tissues.
DR   ExpressionAtlas; Q8BUV3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; TAS:MGI.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:MGI.
DR   GO; GO:0098690; C:glycinergic synapse; ISO:MGI.
DR   GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0098794; C:postsynapse; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR   GO; GO:0099572; C:postsynaptic specialization; ISS: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:0097060; C:synaptic membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008092; F:cytoskeletal protein binding; TAS:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR   GO; GO:0061598; F:molybdopterin adenylyltransferase activity; ISO:MGI.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; ISO:MGI.
DR   GO; GO:0061599; F:molybdopterin molybdotransferase activity; IMP:MGI.
DR   GO; GO:0008940; F:nitrate reductase activity; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0098879; F:structural constituent of postsynaptic specialization; IC:SynGO.
DR   GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR   GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; IMP:MGI.
DR   GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IGI:MGI.
DR   GO; GO:0072579; P:glycine receptor clustering; IMP:MGI.
DR   GO; GO:0098880; P:maintenance of postsynaptic specialization structure; IC:SynGO.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IMP:MGI.
DR   GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IMP:MGI.
DR   GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0098970; P:postsynaptic neurotransmitter receptor diffusion trapping; IEP:SynGO.
DR   GO; GO:0010038; P:response to metal ion; ISO:MGI.
DR   CDD; cd00887; MoeA; 1.
DR   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
DR   Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
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   NCBIfam; TIGR00177; molyb_syn; 2.
DR   PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR   PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
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; SSF63867; MoeA C-terminal domain-like; 1.
DR   SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 2.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
DR   Genevisible; Q8BUV3; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
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..769
FT                   /note="Gephyrin"
FT                   /id="PRO_0000269039"
FT   REGION          14..153
FT                   /note="MPT Mo-transferase"
FT   REGION          140..349
FT                   /note="Interaction with GABARAP"
FT                   /evidence="ECO:0000250"
FT   REGION          181..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..769
FT                   /note="MPT adenylyltransferase"
FT   COMPBIAS        206..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         198
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQX3"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         262
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         265
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         266
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         338
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18630941,
FT                   ECO:0007744|PubMed:21183079"
FT   LIPID           212
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQX3"
FT   LIPID           284
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQX3"
FT   CONFLICT        262
FT                   /note="S -> T (in Ref. 1; BAC38476)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        463
FT                   /note="T -> S (in Ref. 1; BAC38476)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   769 AA;  83282 MW;  D0EF325CC3CF87E9 CRC64;
     MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG GTISAYKIVP
     DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEAT KEVIEREAPG MALAMLMGSL
     NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAIVKVKEVH
     DELEDLPSPP PPLSPPPTTS PHKQTEDKGV QCEEEEEEKK DSGVASTEDS SSSHITAAAL
     AAKIPDSIIS RGVQVLPRDT ASLSTTPSES PRAQATSRLS TASCPTPKQI RRPDESKGVA
     SRVGSLKARL PSCSSTYSVS EVQSRCSSKE NILRASHSAV DITKVARRHR MSPFPLTSMD
     KAFITVLEMT PVLGTEIINY RDGMGRVLAQ DVYAKDNLPP FPASVKDGYA VRAADGPGDR
     FIIGESQAGE QPTQTVMPGQ VMRVTTGAPI PCGADAVVQV EDTELIRESD DGTEELEVRI
     LVQARPGQDI RPIGHDIKRG ECVLAKGTHM GPSEIGLLAT VGVTEVEVNK FPVVAVMSTG
     NELLNPEDDL LPGKIRDSNR STLLATIQEH GYPTINLGIV GDNPDDLLNA LNEGISRADV
     IITSGGVSMG EKDYLKQVLD IDLHAQIHFG RVFMKPGLPT TFATLDIDGV RKIIFALPGN
     PVSAVVTCNL FVVPALRKMQ GILDPRPTII KARLSCDVKL DPRPEYHRCI LTWHHQEPLP
     WAQSTGNQMS SRLMSMRSAN GLLMLPPKTE QYVELHKGEV VDVMVIGRL
//