ID   A0A3Q7SAV4_VULVU        Unreviewed;      1137 AA.
AC   A0A3Q7SAV4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
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_025857049.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025857049.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025857049.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025857049.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025857049.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_025857049.1; XM_026001264.1.
DR   AlphaFoldDB; A0A3Q7SAV4; -.
DR   STRING; 9627.ENSVVUP00000019398; -.
DR   KEGG; vvp:112921861; -.
DR   OrthoDB; 2909513at2759; -.
DR   Proteomes; UP000286640; 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:UP000286640};
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          508..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1137 AA;  126314 MW;  546C38546F965C8F CRC64;
     MPVQAPQWTD FLSCPICTQT FDETIRKPIS LGCGHTVCKM CLNKLHRKAC PFDQTTINTD
     IELLPVNSAL LQLVGAQVPE QQPITLCSGV EDTKHYEEAK KCVEELALYL KPLSSARGVG
     LNSTTQSVLS 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 LPSAAVLPDE
     GAVDLPSRKT PALPNGIVSA GTTVTQLIPR GTDPTYDSSL KPGKIDHLSS SAPGSPPDLL
     ESVPKSISAL PVNPHPVPPR GPTDLPPMPV TKPLQMVPRG SQLYPAQQAD VYYQDPRGAA
     PPFEPAPYQQ APYQQGMYYT TPPQCVSRFV RPPPSAPEPG PPYLDHYPPY LQDRVVNSQY
     GTQPQQYPPM YPPHYDGRRV YPAQSYTREE IFRESPIPIE IPPAAVPSYV PESRERYQQM
     EGYYPVAPHP TQIRPSYMRD PPYSRLPPPP QPHPSLDELH RRRKEIMAQL EERKVISPPP
     FAPSPTLPPT FHQEEFMDED LKVAGKYKGN DYSQYSPWSC DTIGSYIGTK DAKPKDVVAV
     GSVEMMNVES KGMRDQRLDL QRRAAETSDD DLIPFGDRPT VSRFGAISRT SKTIYQGAGP
     MQAMAPQGAP TKPINISDYT PYGTHGGWGG SPYSPHQNIP SQGHFSERER ISMSEVASHG
     KPLPSAEREQ LRLELQQLNH QISQQTQLRG LEAVSNRLLL QREVNTLAGQ SQPPPPPPKW
     PGMISSEQLS LELHQVEREI GKRTRELSLE NQCTLDMKSK LNTSKQAENG QPEPQNKVSA
     EDLTLTFSDV PNGSALTQEN ISLLSNKTSS LNLSEDPEGG GDNNDSQRAG VTSTSAP
//