RC3H1_XENLA
ID RC3H1_XENLA Reviewed; 1114 AA.
AC Q6NUC6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Roquin-1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q5TC82};
DE AltName: Full=RING finger and C3H zinc finger protein 1;
DE AltName: Full=RING finger and CCCH-type zinc finger domain-containing protein 1;
GN Name=rc3h1 {ECO:0000250|UniProtKB:Q5TC82};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP REVIEW, AND MISCELLANEOUS.
RX PubMed=23550652; DOI=10.1111/imr.12056;
RA Heissmeyer V., Vogel K.U.;
RT "Molecular control of Tfh-cell differentiation by Roquin family proteins.";
RL Immunol. Rev. 253:273-289(2013).
CC -!- FUNCTION: Post-transcriptional repressor. May recognize and bind to the
CC 3'-UTR of some mRNAs and promote mRNA decay.
CC {ECO:0000250|UniProtKB:Q4VGL6}.
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:0000250|UniProtKB:Q5TC82};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q5TC82}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q4VGL6}.
CC Cytoplasmic granule {ECO:0000250|UniProtKB:Q4VGL6}. Note=During cell
CC stress, localizes to cytosolic stress granules.
CC {ECO:0000250|UniProtKB:Q4VGL6}.
CC -!- DOMAIN: The RING-type zinc finger is required for proper localization
CC to stress granules, but not to P-bodies.
CC {ECO:0000250|UniProtKB:Q4VGL6}.
CC -!- DOMAIN: The ROQ region is required for CDE RNA-binding. It may also be
CC involved in localization to stress granules.
CC {ECO:0000250|UniProtKB:Q4VGL6}.
CC -!- DOMAIN: HEPN (higher eukaryotes and prokaryotes nucleotide-binding) are
CC observed in both N- and C-terminal sides of ROQ domain with 3D
CC structure even if they are poredcted on the basis of sequence.
CC {ECO:0000250|UniProtKB:Q5TC82}.
CC -!- PTM: Proteolytically cleaved after Arg-509 and Arg-576 by MALT1 in
CC activated CD4(+) T cells; cleavage at Arg-509 and Arg-576 is critical
CC for promoting RC3H1 degradation in response to T-cell receptor (TCR)
CC stimulation, and hence is necessary for prolonging the stability of a
CC set of mRNAs controlling Th17 cell differentiation.
CC {ECO:0000250|UniProtKB:Q4VGL6}.
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DR EMBL; BC068669; AAH68669.1; -; mRNA.
DR RefSeq; NP_001084548.1; NM_001091079.1.
DR AlphaFoldDB; Q6NUC6; -.
DR BMRB; Q6NUC6; -.
DR SMR; Q6NUC6; -.
DR BioGRID; 100917; 1.
DR IntAct; Q6NUC6; 1.
DR DNASU; 414495; -.
DR GeneID; 414495; -.
DR KEGG; xla:414495; -.
DR CTD; 414495; -.
DR Xenbase; XB-GENE-5864202; rc3h1.L.
DR OrthoDB; 1009668at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 414495; Expressed in blastula and 19 other tissues.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:1900151; P:regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0042129; P:regulation of T cell proliferation; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032671; RC3H1.
DR InterPro; IPR041523; ROQ_II.
DR InterPro; IPR027370; Znf-RING_LisH.
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:SF6; PTHR13139:SF6; 1.
DR Pfam; PF18386; ROQ_II; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Reference proteome; Repeat; Repressor;
KW RNA-binding; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1114
FT /note="Roquin-1"
FT /id="PRO_0000055967"
FT ZN_FING 14..54
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 415..443
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 130..178
FT /note="HEPN-N"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT REGION 179..328
FT /note="ROQ"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT REGION 329..401
FT /note="HEPN-C"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT REGION 918..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT SITE 509
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
FT SITE 576
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q4VGL6"
SQ SEQUENCE 1114 AA; 123577 MW; E836C7514BF2A3B7 CRC64;
MPVQAPQWTD FLSCPICTQT FDETIRKPIS LGCGHTVCKM CLNKLHRKAC PFDQTTINTD
IELLPVNSAL LQLVGAQVPE QQQITLCGGC GAEDTKHYEE ARKCVEELAL YLKPLSTARG
VGLNSTTQSV LSRPMQRKLV TLVHCQLVEE EGRIRAMRAA RSLGERTVTE LILQHQNPQQ
LSSNLWAAVR ARGCQFLGPA MQEEALKLVL LALEDGSALS RKVLVLFVVQ RLEPRFPQAS
KTSIGHVVQL LYRASCFKVT KRDEDSSLMQ LKEEFRTYEA LRREHDSQIV QIAMEAGLRI
APDQWSSLLY GDQSHKSHMQ SIIDKLQTPA SFAQSVQELT IALQRTGDPA NLNRLRPHLE
LLANIDPSPD APPPTWEQLK DGLVAVKTVV HGLVDYIQNH SKKGTDQQQP PQHSKYKTYM
CRDMKQRGGC PRGASCTFAH SQEELEKFRK MNKRLVPRRP LSASLGQLNE VGLPIGAPDE
GPMDLPPRKP SGLPNGIVPG SSVTQLISRS TDSGFESVLK PVKLDHLSSS APGSPPELLD
SVPKTSMSAL PVNAHPAASR DLPPLPVSKQ IQMVPRGSQM YAPPPADTFY QECRGAGPPF
DAAPYAQGVY YPPQSSQCVS RFVRPPPAAT EPATAYLDHY TPYLQDRVVS TQYGTPTQQY
QAIVPTQYQP HYDNRRAYPS NAPPYQREEL VRASPVPLEM PPAAVSPYVA ESRERYQGIE
GYYTHPGQIR PSYHREPYIR LPPQHTAQPH PSLDDLHRRR KEIMAQLEER NVISPPPFAP
SPTLPHSFHP EEYLDEELKI PGNFKGNDYS QYSPWSFDTF GPYIGTKDNK SKDVSAGGNV
EVANVDGKSL RDQRIELQRR ATEPGEDDLI PFGDRPTVSR FGAISRTSKA LYQPPGPMQQ
AMAAHGAAKS SITDYSLYSS HSGLSGPSYP THQNLPSQGH LSERERLSKP LPTSEREQLR
MELQQVNQQI SQQAQMRDME VATNRLLLRE ASSLGNQQQP PPQQPPAKWP SKVSSKQLSL
ELHQVEREIG KRTRELSLES HSLSMKSKPD TIKVENGQLD DLPLSFSSEV PNGSGLTQDI
TLSKTASLTL SEDPQAGGDK SDLMRSGVNS TAAP
