UniProtKB - Q6NUC6 (RC3H1_XENLA)
Protein
Roquin-1
Gene
rc3h1
Organism
Xenopus laevis (African clawed frog)
Status
Functioni
Post-transcriptional repressor. May recognize and bind to the 3'-UTR of some mRNAs and promote mRNA decay.By similarity
Catalytic activityi
- S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.By similarity EC:2.3.2.27
: protein ubiquitination Pathwayi
This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.By similarityView all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 14 | Zinc 1By similarity | 1 | |
Metal bindingi | 17 | Zinc 1By similarity | 1 | |
Metal bindingi | 33 | Zinc 2By similarity | 1 | |
Metal bindingi | 35 | Zinc 2; via pros nitrogenBy similarity | 1 | |
Metal bindingi | 38 | Zinc 1By similarity | 1 | |
Metal bindingi | 50 | Zinc 2By similarity | 1 | |
Metal bindingi | 53 | Zinc 2By similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 14 – 54 | RING-type; degeneratePROSITE-ProRule annotationAdd BLAST | 41 | |
Zinc fingeri | 415 – 443 | C3H1-typePROSITE-ProRule annotationAdd BLAST | 29 |
GO - Molecular functioni
- double-stranded RNA binding Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- mRNA 3'-UTR binding Source: UniProtKB
- RNA stem-loop binding Source: UniProtKB
- ubiquitin-protein transferase activity Source: UniProtKB
GO - Biological processi
- 3'-UTR-mediated mRNA destabilization Source: UniProtKB
- cellular response to interleukin-1 Source: UniProtKB
- nuclear-transcribed mRNA catabolic process Source: UniProtKB
- nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
- positive regulation of mRNA catabolic process Source: UniProtKB
- posttranscriptional regulation of gene expression Source: UniProtKB
- protein polyubiquitination Source: UniProtKB
- regulation of T cell proliferation Source: InterPro
Keywordsi
Molecular function | Repressor, RNA-binding, Transferase |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
Names & Taxonomyi
Protein namesi | Recommended name: Roquin-1Curated (EC:2.3.2.27By similarity)Alternative name(s): RING finger and C3H zinc finger protein 1 RING finger and CCCH-type zinc finger domain-containing protein 1 |
Gene namesi | Name:rc3h1By similarity |
Organismi | Xenopus laevis (African clawed frog) |
Taxonomic identifieri | 8355 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Organism-specific databases
Xenbasei | XB-GENE-5864202, rc3h1.L |
Subcellular locationi
Other locations
- P-body By similarity
- Cytoplasmic granule By similarity
Note: During cell stress, localizes to cytosolic stress granules.By similarity
Other locations
- cytoplasmic stress granule Source: UniProtKB
- P-body Source: UniProtKB
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000055967 | 1 – 1114 | Roquin-1Add BLAST | 1114 |
Post-translational modificationi
Proteolytically cleaved after Arg-509 and Arg-576 by MALT1 in activated CD4+ T cells; cleavage at Arg-509 and Arg-576 is critical for promoting RC3H1 degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling Th17 cell differentiation.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 509 | CleavageBy similarity | 1 | |
Sitei | 576 | CleavageBy similarity | 1 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 100917, 1 interactor |
IntActi | Q6NUC6, 1 interactor |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 130 – 178 | HEPN-NBy similarityAdd BLAST | 49 | |
Regioni | 179 – 328 | ROQBy similarityAdd BLAST | 150 | |
Regioni | 329 – 401 | HEPN-CBy similarityAdd BLAST | 73 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 958 – 1004 | Gln-richAdd BLAST | 47 |
Domaini
The RING-type zinc finger is required for proper localization to stress granules, but not to P-bodies.By similarity
The ROQ region is required for CDE RNA-binding. It may also be involved in localization to stress granules.By similarity
HEPN (higher eukaryotes and prokaryotes nucleotide-binding) are observed in both N- and C-terminal sides of ROQ domain with 3D structure even if they are poredcted on the basis of sequence.By similarity
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 14 – 54 | RING-type; degeneratePROSITE-ProRule annotationAdd BLAST | 41 | |
Zinc fingeri | 415 – 443 | C3H1-typePROSITE-ProRule annotationAdd BLAST | 29 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
OrthoDBi | 1009668at2759 |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR032671, RC3H1 IPR041523, ROQ_II IPR027370, Znf-RING_LisH IPR000571, Znf_CCCH IPR036855, Znf_CCCH_sf IPR001841, Znf_RING IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS |
PANTHERi | PTHR13139:SF6, PTHR13139:SF6, 1 hit |
Pfami | View protein in Pfam PF18386, ROQ_II, 1 hit PF00642, zf-CCCH, 1 hit PF13445, zf-RING_UBOX, 1 hit |
SMARTi | View protein in SMART SM00184, RING, 1 hit SM00356, ZnF_C3H1, 1 hit |
SUPFAMi | SSF90229, SSF90229, 1 hit |
PROSITEi | View protein in PROSITE PS50103, ZF_C3H1, 1 hit PS00518, ZF_RING_1, 1 hit PS50089, ZF_RING_2, 1 hit |
i Sequence
Sequence statusi: Complete.
Q6NUC6-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPVQAPQWTD FLSCPICTQT FDETIRKPIS LGCGHTVCKM CLNKLHRKAC
60 70 80 90 100
PFDQTTINTD IELLPVNSAL LQLVGAQVPE QQQITLCGGC GAEDTKHYEE
110 120 130 140 150
ARKCVEELAL YLKPLSTARG VGLNSTTQSV LSRPMQRKLV TLVHCQLVEE
160 170 180 190 200
EGRIRAMRAA RSLGERTVTE LILQHQNPQQ LSSNLWAAVR ARGCQFLGPA
210 220 230 240 250
MQEEALKLVL LALEDGSALS RKVLVLFVVQ RLEPRFPQAS KTSIGHVVQL
260 270 280 290 300
LYRASCFKVT KRDEDSSLMQ LKEEFRTYEA LRREHDSQIV QIAMEAGLRI
310 320 330 340 350
APDQWSSLLY GDQSHKSHMQ SIIDKLQTPA SFAQSVQELT IALQRTGDPA
360 370 380 390 400
NLNRLRPHLE LLANIDPSPD APPPTWEQLK DGLVAVKTVV HGLVDYIQNH
410 420 430 440 450
SKKGTDQQQP PQHSKYKTYM CRDMKQRGGC PRGASCTFAH SQEELEKFRK
460 470 480 490 500
MNKRLVPRRP LSASLGQLNE VGLPIGAPDE GPMDLPPRKP SGLPNGIVPG
510 520 530 540 550
SSVTQLISRS TDSGFESVLK PVKLDHLSSS APGSPPELLD SVPKTSMSAL
560 570 580 590 600
PVNAHPAASR DLPPLPVSKQ IQMVPRGSQM YAPPPADTFY QECRGAGPPF
610 620 630 640 650
DAAPYAQGVY YPPQSSQCVS RFVRPPPAAT EPATAYLDHY TPYLQDRVVS
660 670 680 690 700
TQYGTPTQQY QAIVPTQYQP HYDNRRAYPS NAPPYQREEL VRASPVPLEM
710 720 730 740 750
PPAAVSPYVA ESRERYQGIE GYYTHPGQIR PSYHREPYIR LPPQHTAQPH
760 770 780 790 800
PSLDDLHRRR KEIMAQLEER NVISPPPFAP SPTLPHSFHP EEYLDEELKI
810 820 830 840 850
PGNFKGNDYS QYSPWSFDTF GPYIGTKDNK SKDVSAGGNV EVANVDGKSL
860 870 880 890 900
RDQRIELQRR ATEPGEDDLI PFGDRPTVSR FGAISRTSKA LYQPPGPMQQ
910 920 930 940 950
AMAAHGAAKS SITDYSLYSS HSGLSGPSYP THQNLPSQGH LSERERLSKP
960 970 980 990 1000
LPTSEREQLR MELQQVNQQI SQQAQMRDME VATNRLLLRE ASSLGNQQQP
1010 1020 1030 1040 1050
PPQQPPAKWP SKVSSKQLSL ELHQVEREIG KRTRELSLES HSLSMKSKPD
1060 1070 1080 1090 1100
TIKVENGQLD DLPLSFSSEV PNGSGLTQDI TLSKTASLTL SEDPQAGGDK
1110
SDLMRSGVNS TAAP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC068669 mRNA Translation: AAH68669.1 |
RefSeqi | NP_001084548.1, NM_001091079.1 |
Genome annotation databases
GeneIDi | 414495 |
KEGGi | xla:414495 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC068669 mRNA Translation: AAH68669.1 |
RefSeqi | NP_001084548.1, NM_001091079.1 |
3D structure databases
BMRBi | Q6NUC6 |
SMRi | Q6NUC6 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 100917, 1 interactor |
IntActi | Q6NUC6, 1 interactor |
Genome annotation databases
GeneIDi | 414495 |
KEGGi | xla:414495 |
Organism-specific databases
CTDi | 414495 |
Xenbasei | XB-GENE-5864202, rc3h1.L |
Phylogenomic databases
OrthoDBi | 1009668at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR032671, RC3H1 IPR041523, ROQ_II IPR027370, Znf-RING_LisH IPR000571, Znf_CCCH IPR036855, Znf_CCCH_sf IPR001841, Znf_RING IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS |
PANTHERi | PTHR13139:SF6, PTHR13139:SF6, 1 hit |
Pfami | View protein in Pfam PF18386, ROQ_II, 1 hit PF00642, zf-CCCH, 1 hit PF13445, zf-RING_UBOX, 1 hit |
SMARTi | View protein in SMART SM00184, RING, 1 hit SM00356, ZnF_C3H1, 1 hit |
SUPFAMi | SSF90229, SSF90229, 1 hit |
PROSITEi | View protein in PROSITE PS50103, ZF_C3H1, 1 hit PS00518, ZF_RING_1, 1 hit PS50089, ZF_RING_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RC3H1_XENLA | |
Accessioni | Q6NUC6Primary (citable) accession number: Q6NUC6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 16, 2005 |
Last sequence update: | July 5, 2004 | |
Last modified: | December 2, 2020 | |
This is version 84 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |