GEPH_CHICK
ID GEPH_CHICK Reviewed; 736 AA.
AC Q9PW38;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=10649567; DOI=10.1038/72066;
RA Tsen G., Williams B., Allaire P., Zhou Y.-D., Ikonomov O., Kondova I.,
RA Jacob M.H.;
RT "Receptors with opposing functions are in postsynaptic microdomains under
RT one presynaptic terminal.";
RL Nat. Neurosci. 3:126-132(2000).
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 (Probable). Acts as
CC a major instructive molecule at inhibitory synapses, where it also
CC clusters GABA type A receptors (By similarity).
CC {ECO:0000250|UniProtKB:Q9NQX3, ECO:0000305|PubMed:10649567}.
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 (By similarity).
CC Interacts with glycine receptors (PubMed:10649567).
CC {ECO:0000250|UniProtKB:Q9NQX3, ECO:0000269|PubMed:10649567}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:10649567}; 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:0000250|UniProtKB:Q9NQX3}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q03555}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9NQX3}. Postsynaptic density
CC {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; AF174130; AAD49748.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9PW38; -.
DR SMR; Q9PW38; -.
DR STRING; 9031.ENSGALP00000031974; -.
DR PaxDb; Q9PW38; -.
DR VEuPathDB; HostDB:geneid_428878; -.
DR eggNOG; KOG2371; Eukaryota.
DR InParanoid; Q9PW38; -.
DR OrthoDB; 1114121at2759; -.
DR PhylomeDB; Q9PW38; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000539; Unplaced.
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; IBA:GO_Central.
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:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
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:0007529; P:establishment of synaptic specificity at neuromuscular junction; IBA:GO_Central.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; ISS:UniProtKB.
DR GO; GO:0072579; P:glycine receptor clustering; 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 GO; GO:0098970; P:postsynaptic neurotransmitter receptor diffusion trapping; 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 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; Postsynaptic cell membrane; Reference proteome;
KW Synapse; Transferase.
FT CHAIN 1..736
FT /note="Gephyrin"
FT /id="PRO_0000269040"
FT REGION 14..153
FT /note="MPT Mo-transferase"
FT REGION 181..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..736
FT /note="MPT adenylyltransferase"
FT COMPBIAS 206..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 79721 MW; 6C94F6F1113CB2C8 CRC64;
MASEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG GTISAYKIVP
DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEAT KEVIEREAPG MALAMLMGSL
NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAIVKVKEVH
DELEDLPSPP PPLSPPPTTS PHKQTEDKGV QCEEEEEEKK DSGVASTEDS SSSHITAAAI
AAKIPDSIIS RGVQVLPRDT ASLSTTPSES PRAQATSRLS TASCPTPKVQ SRCSSKENIL
RASHSAVDIT KVARRHRMSP FPLTSMDKAF ITVLEMTPVL GTEIINYRDG MGRVLAQDVY
AKDNLPPFPA SVKDGYAVRA ADGPGDRFII GESQAGEQPT QTVMPGQVMR VTTGAPIPCG
ADAVVQVEDT ELIRESDDGT EELEVRILVQ ARPGQDIRPI GHDIKRGECV LAKGTHTGPS
EVGLLATVGV TEVEVNKFPV VAVMSTGNEL LNPEDDVLPG KIRDSNRSTL LATIQAHGYP
TINLGIVGDN PDDLLNALNE RISRADVIIT SGGVSMGGKY YLKQVLDIDL HAQIHFGRVF
MKPGLPTTFA TLDIDGVRKI IFALPGQSVS AVVTCNLFVV PALRKMQGIL DPRPTIIKAR
LSCDVKLDPR PEYHRCILTW HHQEPHPWAQ STGNQMSSRL MSMRSANGLL MLPPKTEQYV
ELHKGEVVDV MVIGRL
