ID   M3YUT0_MUSPF            Unreviewed;       838 AA.
AC   M3YUT0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   Name=RNF19A {ECO:0000313|Ensembl:ENSMPUP00000015090.1};
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:ENSMPUP00000015090.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000015090.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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DR   EMBL; AEYP01071310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01071311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004768951.1; XM_004768894.2.
DR   RefSeq; XP_004768952.1; XM_004768895.2.
DR   RefSeq; XP_012920213.1; XM_013064759.1.
DR   AlphaFoldDB; M3YUT0; -.
DR   STRING; 9669.ENSMPUP00000015090; -.
DR   Ensembl; ENSMPUT00000015328.1; ENSMPUP00000015090.1; ENSMPUG00000015199.1.
DR   GeneID; 101690798; -.
DR   KEGG; mpuf:101690798; -.
DR   CTD; 25897; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   GeneTree; ENSGT00940000158703; -.
DR   HOGENOM; CLU_016793_1_0_1; -.
DR   InParanoid; M3YUT0; -.
DR   OMA; HQCSISL; -.
DR   OrthoDB; 2943236at2759; -.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   GO; GO:0099576; P:regulation of protein catabolic process at postsynapse, modulating synaptic transmission; IEA:Ensembl.
DR   CDD; cd20362; BRcat_RBR_RNF19A; 1.
DR   CDD; cd20355; Rcat_RBR_RNF19; 1.
DR   CDD; cd16775; RING-HC_RBR_RNF19A; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 2.20.25.20; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685:SF111; E3 UBIQUITIN-PROTEIN LIGASE RNF19A; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   TRANSMEM        361..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        414..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          128..351
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          132..180
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          622..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..657
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  90804 MW;  ED919884E0A9BABB CRC64;
     MQEQEIGFIS KYNEGLCVNT DPESILMNIL DMSLHRQMGS DRDLQSSASS VSLPSVKKAP
     KKRRISIGSL FRRKKDNKRK SRELNGGVDG IASIESIHSE MCTDKNSIFS TNTSSDNGLT
     SISKQIGDFI ECPLCLLRHS KDRFPEIMTC HHRSCVDCLR QYLRIEISES RVNISCPECT
     ERFNPHDIRL ILSDDVLMEK YEEFMLRRWL VADPDCRWCP APDCGYAVIA FGCASCPKLT
     CGREGCGTEF CYHCKQIWHP NQTCDAARQE RAQSLRLRTI RSSSISYSQE SGAAADDIKP
     CPRCAAYIIK MNDGSCNHMT CAVCGCEFCW LCMKEISDLH YLSPSGCTFW GKKPWSRKKK
     ILWQLGTLVG APVGIALIAG IAIPAMIIGI PVYVGRKIHN RYEGKDVSKH KRNLAITGGV
     TLSVIVSPVV AAVTVGIGVP IMLAYVYGVV PISLCRSGGC GVSAGNGKGV RIEFDDENDI
     NVGGTNTAVD TTSVAEARHN PSIGEGSVGG LTGSLSASGS HMDRIGAIRD NLSETASTMA
     LAGASITGSL SGSAMVNCFN RLEVQADVQK ERYSLSGESG TVSLGTVSDN ASTKAMAGSI
     LNSYIPLDKE GNSMEVQVDI ESKPSKFRHN SGSSSVEDGS ATRSHAGASS SGLPEGKSGA
     TKWSKEATAG KKAKGGKLRK KSNMKINETR EDMDAQLLEQ QSTNSSEFEA PSLSDSMPSV
     ADSHSSHFSE FSCSDLESMK TSCSHGSNDY HARFATVNIL PEVENDRLEN SPHQCSISLL
     TKTASCSEVP QLNHIAEEHG NNGVKPSVDL YFGDALKETN NNHSHQTMEL KVAIQTEI
//