ID M3Y6D8_MUSPF Unreviewed; 805 AA.
AC M3Y6D8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Gephyrin {ECO:0000313|Ensembl:ENSMPUP00000006889.1};
GN Name=GPHN {ECO:0000313|Ensembl:ENSMPUP00000006889.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000006889.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000006889.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {ECO:0000256|ARBA:ARBA00008339}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
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DR EMBL; AEYP01004068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3Y6D8; -.
DR STRING; 9669.ENSMPUP00000006889; -.
DR Ensembl; ENSMPUT00000007003.1; ENSMPUP00000006889.1; ENSMPUG00000006944.1.
DR eggNOG; KOG2371; Eukaryota.
DR GeneTree; ENSGT00390000016577; -.
DR HOGENOM; CLU_010186_2_2_1; -.
DR InParanoid; M3Y6D8; -.
DR OMA; ESPYPMI; -.
DR UniPathway; UPA00344; -.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:Ensembl.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:Ensembl.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IEA:Ensembl.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010038; P:response to metal ion; IEA:Ensembl.
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.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150}.
FT DOMAIN 18..165
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT DOMAIN 571..714
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 181..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 87242 MW; 1AAB31F8873E2B34 CRC64;
MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG GTISAYKIVP
DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEAT KEVIEREAPG MALAMLMGSL
NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAIVKVKEVH
DELEDLPSPP PPLSPPPTTS PHKQTEDKGV QCEEEEEEKK DSGVASTEDS SSSHITAAAI
AAKKHPFYTS PAVIMAHGEQ PIPGLITYSH HATGSTDERI PDSIISRGVQ VLPRDTASLS
TTPSESPRAQ ATSRLSTASC PTPKQIRRPD ESKGVASRVG SLKAWLPSCS STYSVSEVQS
RCSSKENILR ASHSAVDITK VARRHRMSPF PLTSMDKAFI TVLEMTPVLG TEIINYRDGM
GRVLAQDVYA KDNLPPFPAS VKDGYAVRAA DGPGDRFIIG ESQAGEQPTQ TVMPGQVMRV
TTGAPIPCGA DAVVQVEDTE LIRESDDGTE ELEVRILVQA RPGQDIRPIG HDIKRGECVL
AKGTHMGPSE IGLLATVGVT EVEVNKFPVV AVMSTGNELL NPEDDLLPGK IRDSNRSTLL
ATIQEHGYPT INLGIVGDNP DDLLNALNEG ISRADVIITS GGVSMGEKDY LKQVLDIDLH
AQIHFGRVFM KPGLPTTFAT LDIDGVRKII FALPGNPVSA VVTCNLFVVP ALRKMQGILD
PRPTIIKARL SCDVKLDPRP EYHRCILTWH HQEPLPWAQS TGNQMSSRLM SMRSANGLLM
LPPKTEQYVE LHKGEVVDVM VIGRL
//