ID   U3JJY9_FICAL            Unreviewed;      1125 AA.
AC   U3JJY9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 61.
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:ENSFALP00000003093.2};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000003093.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000003093.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000003093.2}
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_016155738.1; XM_016300252.1.
DR   AlphaFoldDB; U3JJY9; -.
DR   STRING; 59894.ENSFALP00000003093; -.
DR   Ensembl; ENSFALT00000003106.2; ENSFALP00000003093.2; ENSFALG00000002947.2.
DR   GeneID; 101809134; -.
DR   CTD; 149041; -.
DR   eggNOG; KOG3161; Eukaryota.
DR   GeneTree; ENSGT00940000157143; -.
DR   HOGENOM; CLU_004948_0_0_1; -.
DR   Proteomes; UP000016665; Chromosome 8.
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:UP000016665};
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          516..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1095..1125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1125 AA;  124435 MW;  C6D04C025549E9F7 CRC64;
     MPVQAPQWTD FLSCPICTQT FDETIRKPIS LGCGHTVCKM CLNKLHRKAC PFDQTTINTD
     IELLPVNSAL LQLVGAQVPE QQPITLCSGA EDTKHYEEGK 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 KGTDQQQPPQ HSKYKTYMCR
     DMKQRGGCPR GASCTFAHSQ EELEKFRKMN KRLVPRRPLS ASLGQLNEVG LPSGAILSEE
     GGVDLPNRKT SALPNGIVST GSTVTQLISR GTDSGYETAL KPGKMDHLSS SAPGSPPDLL
     ESVPKSSISA LPVNPHPVPA RVPADLPSVS VTKQLQMVPR GSQLYNAQQA DMFYQDPRGA
     APSFEPAPPY QQGVYYPTQS MSRFVRPPPS AAEAGAPYLE HYGPYLPERV VSPQYPQPQG
     YPALAQPIYP PHYDSRRVYP PVQPYQRDDV VRGSPVPIDI PQAAVPLYVP ESRDRYQQTE
     AYCPVAPHLG QIRPSCHRPH PSLDELHRRR KEIMAQLEER KVISPPPFAP SPTLPHPFHS
     EEYLDEDLKV AGKYKGNDYS QYSPWSCDTI GSYIGTKDAK PKDVVAARSV EMANVDSKAM
     REQRLDMQRR AAETGDDDLI PFGDRPTVSR FGAISRTSKA MYQNSGPMQA MAVQGAATKS
     IISDYSPYET HGGWGGSPYS PHQNIPSQGR FNDRERLSMS DVAGHGKQLP SAEREQQLRM
     ELQQVDHQIS QQTQMRGLEA VSNRLLLQRE ATTLAGQPQP PPPPPKWPGM ISSEQLSLEL
     HQVEREIGKR TRELSMESQS SLDMKNKLGT TKQTENGQLE PQNKVPAEDL TLTFSSDVPN
     GSALTQENIG LLSNNMASLS LSEEPEGGGD GHDSQRAGVT PTSAP
//