ID   A0A2K5EZE8_AOTNA        Unreviewed;      1133 AA.
AC   A0A2K5EZE8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-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|Ensembl:ENSANAP00000038612.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000038612.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000038612.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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_012299999.1; XM_012444576.1.
DR   RefSeq; XP_012300000.1; XM_012444577.1.
DR   RefSeq; XP_012300001.1; XM_012444578.1.
DR   AlphaFoldDB; A0A2K5EZE8; -.
DR   STRING; 37293.ENSANAP00000038612; -.
DR   Ensembl; ENSANAT00000056706.1; ENSANAP00000038612.1; ENSANAG00000036716.1.
DR   GeneID; 105711719; -.
DR   CTD; 149041; -.
DR   GeneTree; ENSGT00940000157143; -.
DR   OMA; WGSSPYS; -.
DR   OrthoDB; 2909513at2759; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:1905762; F:CCR4-NOT complex binding; IEA:Ensembl.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0035198; F:miRNA binding; IEA:Ensembl.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
DR   GO; GO:0035613; F:RNA stem-loop binding; IEA:Ensembl.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IEA:Ensembl.
DR   GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR   GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR   GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
DR   GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
DR   GO; GO:0002635; P:negative regulation of germinal center formation; IEA:Ensembl.
DR   GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IEA:Ensembl.
DR   GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
DR   GO; GO:0033962; P:P-body assembly; IEA:Ensembl.
DR   GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR   GO; GO:2000628; P:regulation of miRNA metabolic process; IEA:Ensembl.
DR   GO; GO:1900151; P:regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
DR   GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR   GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0061470; P:T follicular helper cell differentiation; IEA:Ensembl.
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:UP000233020};
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          1094..1133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1133 AA;  125835 MW;  DB915B7E37C863D9 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 LPSAAILPDE
     GAVDLPNRKP PALPNGIVSA GNTVTQLIPR GTDPSYDSSL KPGKIDHLSS SAPGSPPDLL
     ESVPKSISAL PVNPHPIPPR GPTDLPPMPV TKPLQMVPRG SQLYPAQQTD VYYQDPRGAA
     PPFEPAPYQQ GMYYTPPPQC VSRFIRPPPS APEPAPPYLD HYPPYLQDRV VNSQYGTQPQ
     QYPPIYPSHY DGRRVYPAQS YTREEIFRES PIPIEIPPAA VPSYVPESRE RYQQIESYYP
     VAPHPTQIRA SYLREPPYSR LPPPPQPHPS LDELHRRRKE IMAQLEERKV ISPPPFAPSP
     TLPPTFHPEE FLDEDLKVAG KYKGNDYSQY SPWSCDTIGS YIGTKDAKPK DVVAAGSVEM
     MNVESKGMRD QRLDLQRRAA ETSDDDLIPF GDRPTVSRFG AISRTSKTIY QGAGPMQAMA
     PQGAPTKPIN ISDYSPYGTH SGWGGSPYSP HQNIPSQGHF SERERISMSE VASHGKPLPS
     AEREQLRLEL QQLNHQISQQ TQLRGLEAVS NRLVLQREAN TLAGQSQPPP PQPPKWPGMI
     SSEQLSLELH QVEREIGKRT RELSMENQCS LDMKSKLNTS KQAENGQPEP QNKVPAEDLT
     LTFSDVPNGS ALTQENISLL SNKTSSLNLS EDPEGGGDNN DSQRSGVTPS SAP
//