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Database: UniProt
Entry: M3Y6D8_MUSPF
LinkDB: M3Y6D8_MUSPF
Original site: M3Y6D8_MUSPF 
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
//
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