RING1_GOSHI
ID RING1_GOSHI Reviewed; 338 AA.
AC P0CH30; D7PC81;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=E3 ubiquitin-protein ligase RING1;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase RING1 {ECO:0000305};
GN Name=RING1;
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AUTOUBIQUITINATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Sure-Grow 747; TISSUE=Fiber;
RX PubMed=20376576; DOI=10.1007/s12033-010-9280-7;
RA Ho M.-H., Saha S., Jenkins J.N., Ma D.-P.;
RT "Characterization and promoter analysis of a cotton RING-type ubiquitin
RT ligase (E3) gene.";
RL Mol. Biotechnol. 46:140-148(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-315.
RC STRAIN=cv. Texas Marker 1; TISSUE=Ovule;
RA Yang S.S., Cheung F., Wei N.E., Lee J.J., Ha M., Stelly D.M., Thaxton P.,
RA Sze S.H., Triplett B.A., Town C.D., Chen Z.J.;
RT "ESTs from immature ovule (-3 to 3 DPA) of G. hirsutum TM-1.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Promotes
CC polyubiquitination of target proteins. {ECO:0000269|PubMed:20376576}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- TISSUE SPECIFICITY: Mostly expressed in cotton fibers, and, to a lower
CC extent, in leaves and flowers. {ECO:0000269|PubMed:20376576}.
CC -!- DEVELOPMENTAL STAGE: Accumulates progressively in fiber during their
CC elongation and reach highest levels at 15 days post-anthesis (DPA).
CC {ECO:0000269|PubMed:20376576}.
CC -!- PTM: Auto-ubiquitinated as part of the enzymatic reaction.
CC {ECO:0000269|PubMed:20376576}.
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 EMBL; GU229884; ADI58769.1; -; Genomic_DNA.
DR EMBL; DT559682; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0CH30; -.
DR SMR; P0CH30; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000189702; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:AgBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0090378; P:seed trichome elongation; IEP:AgBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..338
FT /note="E3 ubiquitin-protein ligase RING1"
FT /id="PRO_0000396834"
FT ZN_FING 224..265
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 102..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 34
FT /note="V -> I (in Ref. 2; DT559682)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="L -> P (in Ref. 2; DT559682)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="G -> R (in Ref. 2; DT559682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 36701 MW; D083DA1A210AA420 CRC64;
MSSDGNVTGG GGANTVGVTN KPFFCYQCNR TVNVTISPPS SDPTCPICNE GFLEEYDNPN
PNQGSGFLNP NPNSIPFHDL FLTLSDPFAS LLPLLFPSSS STTTSSSASI DPNNPSLSGP
TRSGRGDPFA FDPFTFIQNH LNDLRSSGAQ IEFVIQNNPS DQGFRLPANI GDYFIGPGLE
QLIQQLAEND PNRYGTPPAS KSAIEALPLV NITKSNLNSE FNQCAVCMDD FEEGTEAKQM
PCKHLYHKDC LLPWLELHNS CPVCRHELPT DDPDYERRVR GAQGTSGGND GDNSGQRSDG
DNRTVERSFR ISLPWPFQAR GPGPAPGDNA ETRQEDLD
