GEPH_DICDI
ID GEPH_DICDI Reviewed; 718 AA.
AC Q54KM0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Gephyrin;
DE AltName: Full=Putative glycine receptor-tubulin linker protein homolog;
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; Synonyms=gph; ORFNames=DDB_G0287261;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Microtubule-associated protein involved in membrane protein-
CC cytoskeleton interactions. {ECO:0000250|UniProtKB:Q03555}.
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:Q9NQX3}.
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 -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000250|UniProtKB:Q9NQX3}.
CC -!- SUBUNIT: Homotrimer, homodimer and homooligomer.
CC {ECO:0000250|UniProtKB:Q9NQX3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q03555};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q03555}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q03555}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9NQX3}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q03555}.
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; AAFI02000099; EAL63832.1; -; Genomic_DNA.
DR RefSeq; XP_637337.1; XM_632245.1.
DR AlphaFoldDB; Q54KM0; -.
DR SMR; Q54KM0; -.
DR STRING; 44689.DDB0266393; -.
DR PaxDb; Q54KM0; -.
DR EnsemblProtists; EAL63832; EAL63832; DDB_G0287261.
DR GeneID; 8626035; -.
DR KEGG; ddi:DDB_G0287261; -.
DR dictyBase; DDB_G0287261; gphn.
DR eggNOG; KOG2371; Eukaryota.
DR HOGENOM; CLU_010186_2_2_1; -.
DR InParanoid; Q54KM0; -.
DR OMA; RHRESPY; -.
DR PhylomeDB; Q54KM0; -.
DR Reactome; R-DDI-947581; Molybdenum cofactor biosynthesis.
DR UniPathway; UPA00344; -.
DR PRO; PR:Q54KM0; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IBA:GO_Central.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IBA:GO_Central.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central.
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; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton; Lipoprotein;
KW Magnesium; Membrane; Metal-binding; Molybdenum;
KW Molybdenum cofactor biosynthesis; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..718
FT /note="Gephyrin"
FT /id="PRO_0000327612"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..176
FT /note="MPT Mo-transferase"
FT REGION 222..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..718
FT /note="MPT adenylyltransferase"
FT REGION 344..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 78840 MW; 9E97D91ECE1D3636 CRC64;
MSNTLTTERN ITNSPTAAQL NEKESGKKEE EWIVGVLTTS DRVSQGIAID QSGPEIVAII
KNQLKQMMGE SCSINVITVY KVVPDEIEHI QQMITQWTHL KYKLILTTGG TGFTPRDVTP
EAIKPLLNRR TKGIEIAMLK TSLDITPHAM LSRPIAGIRD QTLIITLPGS VKAIRENLGV
VLPAIPHAIG LINSKPKSSL PESHRSKDYI KNSQIDSNLI INQNNQNNNN NNNNNNNNNN
NNNSHNHHHH HHHSCGGSGK RGSSYNMTPV DEAIKIILEQ CDNINNELEK VEITKSLGRI
LGEDISSVEP FPNFRASIKD GYAIRSKDGI GKYRLLGDSV AGNTGENLIP PQPQQPTNSI
NDDDNEKYCV RITTGAKIPD GYDSVVMIEE TEMIGENMVS IEVTCKPGQD IREIGSDIAS
GTIVLNKGDK IGCAEIGLLA TLGIQWVHCP KLPSISIIST GDELTDYQSK SDSMKSGIIR
DSNSPTLATI LQEISNHFGE CCSRDNINLV GIIPDKLENL KDTLLDCSKK SDIIITSGGV
SMGHLDLVKP LLEKIGTVHF GRVNMKPGKP LTFSTITTTT TDNNNQEEEK KKKTTLVFSL
PGNPVSTVVT FYLFVVPALR KLGGFGIKNN GSQLNLPCVE VKLLDRIQLD HERPEYHRCT
IEWDFQEHCF VSKSTGSQAS CRLLSLKQAN ALLVLPQKHG HLEKGSMVKA ILIGPINN
