GEPH_MOUSE
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 03-AUG-2022, entry version 156.
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, Pancreas,
RC 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; 23.
DR CORUM; Q8BUV3; -.
DR ELM; Q8BUV3; -.
DR IntAct; Q8BUV3; 7.
DR MINT; Q8BUV3; -.
DR STRING; 10090.ENSMUSP00000106018; -.
DR iPTMnet; Q8BUV3; -.
DR PhosphoSitePlus; Q8BUV3; -.
DR SwissPalm; Q8BUV3; -.
DR EPD; Q8BUV3; -.
DR jPOST; Q8BUV3; -.
DR MaxQB; Q8BUV3; -.
DR PeptideAtlas; Q8BUV3; -.
DR PRIDE; Q8BUV3; -.
DR ProteomicsDB; 266793; -.
DR ABCD; Q8BUV3; 3 sequenced antibodies.
DR Antibodypedia; 144; 416 antibodies from 38 providers.
DR DNASU; 268566; -.
DR Ensembl; ENSMUST00000052472; ENSMUSP00000054064; ENSMUSG00000047454.
DR GeneID; 268566; -.
DR KEGG; mmu:268566; -.
DR UCSC; uc007nzc.2; mouse.
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; 1114121at2759; -.
DR Reactome; R-MMU-947581; Molybdenum cofactor biosynthesis.
DR UniPathway; UPA00344; -.
DR BioGRID-ORCS; 268566; 1 hit in 74 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 262 other tissues.
DR ExpressionAtlas; Q8BUV3; baseline and differential.
DR Genevisible; Q8BUV3; MM.
DR GO; GO:0099144; C:anchored component of synaptic membrane; IDA:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; 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:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO: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:0045202; C:synapse; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
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; ISO: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:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IBA:GO_Central.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
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; 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 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
