ID   A0A1S3APL9_ERIEU        Unreviewed;      1129 AA.
AC   A0A1S3APL9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=RC3H1 {ECO:0000313|RefSeq:XP_007538392.1};
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_007538392.1};
RN   [1] {ECO:0000313|RefSeq:XP_007538392.1}
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_007538392.1; XM_007538330.2.
DR   AlphaFoldDB; A0A1S3APL9; -.
DR   STRING; 9365.ENSEEUP00000013579; -.
DR   CTD; 149041; -.
DR   eggNOG; KOG3161; Eukaryota.
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; cd16781; mRING-HC-C3HC3D_Roquin1; 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:SF6; ROQUIN-1; 1.
DR   Pfam; PF18386; ROQ_II; 1.
DR   Pfam; PF21206; Roquin_1_2-like_ROQ; 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          413..441
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         413..441
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          509..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          997..1016
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1099..1129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1129 AA;  125399 MW;  50A1755D60754C77 CRC64;
     MPVQAPQWTD FLSCPICTQT FDETIRKPIS LGCGHTVCKM CLNKLHRKAC PFDQTTINTD
     IELLPVNSAL LQLVGAQVPE QQPITLCSGV EDTKHYEEAK KCVEELALYL KPLSSARGVG
     LNSTSQSVLS RPMQRKLVTL VHCQLVEEEG RIRAMRAARS LGERTVTELI LQHQNPQQLS
     SNLWAAVRAR GCQFLGPAMQ EEALKLVLLA LEDGSALSRK VLVLFVVQRL EPRFPQASKT
     SIGHVVQLLY RASCFKVTKR DEDSSLMQLK EEFRTYEALR REHDSQIVQI AMEAGLRIAP
     DQWSSLLYGD QSHKSHMQSI IDKLQTPASF AQSVQELTIA LQRTGDPANL NRLRPHLELL
     ANIDPSPDAP PPTWEQLENG LVAVRTVVHG LVDYIQNHSK KGADQQQPPQ HSKYKTYMCR
     DMKQRGGCPR GASCTFAHSQ EELEKFRKMN KRLVPRRPLS ASLGQLNEVG LPSSSILPDE
     GAVDLPNRKP PALPNGIVSA GNTVTKLIPR GTDTGYDSSL KPGKIDHLSS SAPGSPPDLL
     EPVPKNISAI PVNPHPVPPR GPTDLPPMPI TKPPQMVSRG SQLYPAQQAD VYYQDPRGAA
     PPFEPAPYQP GMYYTPPPQC VSRFVRPPPS APEPAPPYLD HYPPYLQDRV VNSQYGTQSQ
     QYPPMYPPHY DGRRLYPAQS YTREEMFRDS PIPIEIPPAA YVPESRERYP QVDGYYPVVP
     HPAQIRPYVR EPPYSRFPPP PPQPHPSLDE LHRRRKEIMA QLEERKVISP PPFAPSPTLP
     PAFHPEEFLD EDLKVAGKYK GNDYSQYSPW SCDTIGSYIG TKDAKPKDVV ASGSVEMMNL
     ESKGMRDQRL DLQRRAAETS DDDLIPFGDR PTVSRFGAIS RTSKTIYQGA GPMQAMAPQG
     ASTKSVNISD YSPYGPHSGW GGSSYSPHPN IPSQGHFSER DRLSMSEVAS HGKPLPSMER
     EQLRLELQQL NHQISQQTQL RGLEAVSNKL VLQRETNTLA GQPQPPPPPP KWPGMISSEQ
     LSLELHQVER EIGKRTRELN MENQCSLDIK SKLNTSKQAE NGQPEPQNKV PAEDLTLTFS
     DVPNGSALTQ ENISLLSNKT SSLTLSEDPE GGGDNNDCQR PSNTPSSAP
//