ID   A0A1S3AS99_ERIEU        Unreviewed;      1190 AA.
AC   A0A1S3AS99;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=RC3H2 {ECO:0000313|RefSeq:XP_007540020.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007540020.1};
RN   [1] {ECO:0000313|RefSeq:XP_007540020.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}.
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DR   RefSeq; XP_007540020.1; XM_007539958.2.
DR   AlphaFoldDB; A0A1S3AS99; -.
DR   CTD; 54542; -.
DR   eggNOG; KOG3161; Eukaryota.
DR   InParanoid; A0A1S3AS99; -.
DR   OrthoDB; 2909513at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd16782; mRING-HC-C3HC3D_Roquin2; 1.
DR   Gene3D; 1.20.120.1790; -; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR041523; ROQ_II.
DR   InterPro; IPR048575; Roquin_1_2-like_ROQ.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13139; RING FINGER AND CCCH-TYPE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13139:SF2; ROQUIN-2; 1.
DR   Pfam; PF18386; ROQ_II; 1.
DR   Pfam; PF21206; Roquin_1_2-like_ROQ; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          14..54
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          410..438
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         410..438
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          527..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..684
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1190 AA;  131824 MW;  E0F4355A8874AAE0 CRC64;
     MPVQAAQWTE FLSCPICYNE FDENVHKPIS LGCSHTVCKT CLNKLHRKAC PFDQTAINTD
     IDVLPVNFAL LQLVGAQVPD HQSIKLSNLG ENKHYEVAKK CVEDLALYLK PLSGGKGVAS
     LNQSALSRPM QRKLVTLVNC QLVEEEGRVR AMRAARSLGE RTVTELILQH QNPQQLSANL
     WAAVRARGCQ FLGPAMQEEA LKLVLLALED GSALSRKVLV LFVVQRLEPR FPQASKTSIG
     HVVQLLYRAS CFKVTKRDED SSLMQLKEEF RSYEALRREH DAQIVHIAME AGLRISPEQW
     SSLLYGDLAH KSHMQSIIDK LQSPESFAKS VQELTIVLQR TGDPANLNRL RPHLELLANI
     DPNPDAVSPT WEQLENAMVA VKTVVHGLVD FIQNYSRKGH ETPQPQPNSK YKTSMCRDLR
     QQGGCPRGTN CTFAHSQEEL EKYRLRNKKI NATVRTFPLL NKVGVNNTVT TTAGNVISVI
     GSTETTGKIV PSSNGISNAE NSVSQLIPRS TDSTLRALET VKKVGKVGTN GQNASGPSAE
     SVAENKIGSP PKTPVSNVVA TSAGPSTVGT EINSVPPKSS PFITRVPVYP QHSENIQYFQ
     DPRTQIPFDV PQYPQTGYYP PPPTVPAGVA PCVPRFVRSS NVPESSLPPA SMPYADHYNT
     FSPRDRMSSS PYQPPPPQPY GPVPPVPSGM YAPVYDSRRI WRPPVYRDDI IRSNSLPPMD
     VMHSSVYQTS LRERYNSLDG YYSVACQPPS EPRTTVPLPR EPCGHLKTSC EEQIRRKPEQ
     WAQYHTQKAP LVSSTLPVAT QSPTPPSPLF SVDFRTDFSE NMSGTKFEED HLSHYSPWSC
     GTIGSCINAI DSEPRDVIAN SNAVLMDLDS GDVKRRVHLF ETQRRTKEED PIIPFSDGPI
     ISKWGAISRS SRTGYHTTDP VQATASQGST TKPISVSDYV PYANAVDSRW SSYGNEATSS
     AHYIERDRFI VTDLSGHRKH SSTGDLLTIE LQQAKSNSLL LQREANALAM QQKWNSLDEG
     RHLTLNLLSK EIELRNRELQ SDYTEDTADA KPDRDIELEL SALDTDEPDG QSEQIEEILD
     IQLGISSQND QLLNGTTVEN GHSVQPHQNE SLEQKRQRLG EDHVILEEQK TIMPVTSCFS
     QPLPVSVSNA SCLPITTSVS VGSLILKTHV MSEDKNDFLK PVANGKMVNS
//