RMA1_CAPAN
ID RMA1_CAPAN Reviewed; 252 AA.
AC Q6R567;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=E3 ubiquitin-protein ligase RMA1H1;
DE EC=2.3.2.27;
DE AltName: Full=Protein RING membrane-anchor 1 homolog 1;
DE AltName: Full=RING-type E3 ubiquitin transferase RMA1H1 {ECO:0000305};
GN Name=RMA1H1;
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF HIS-58; CYS-61; CYS-89 AND
RP LYS-115, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARABIDOPSIS
RP PIP2-1, AND INDUCTION.
RX PubMed=19234086; DOI=10.1105/tpc.108.061994;
RA Lee H.K., Cho S.K., Son O., Xu Z., Hwang I., Kim W.T.;
RT "Drought stress-induced Rma1H1, a RING membrane-anchor E3 ubiquitin ligase
RT homolog, regulates aquaporin levels via ubiquitination in transgenic
RT Arabidopsis plants.";
RL Plant Cell 21:622-641(2009).
RN [2]
RP IDENTIFICATION, AND INDUCTION BY DROUGHT.
RX DOI=10.1016/S0168-9452(03)00165-1;
RA Park J.A., Cho S.K., Kim J.E., Chung H.S., Hong J.-P., Hwang B., Hong C.B.,
RA Kim W.T.;
RT "Isolation of cDNAs differentially expressed in response to drought stress
RT and characterization of the Ca-LEAL1 gene encoding a new family of atypical
RT LEA-like protein homologue in hot pepper (Capsicum annuum L. cv. Pukang).";
RL Plant Sci. 165:471-481(2003).
CC -!- FUNCTION: E3 ubiquitin-protein ligase required for aquaporin levels
CC regulation. {ECO:0000269|PubMed:19234086}.
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 -!- SUBUNIT: Interacts with Arabidopsis PIP2-1.
CC {ECO:0000269|PubMed:19234086}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19234086}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:19234086}. Note=Localization experiments made in a
CC heterologous system.
CC -!- INDUCTION: By drought, cold, high salt, wounding and ethylene. Not
CC induced by abscisic acid. {ECO:0000269|PubMed:19234086,
CC ECO:0000269|Ref.2}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity.
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DR EMBL; AY513612; AAR99376.1; -; mRNA.
DR RefSeq; NP_001311639.1; NM_001324710.1.
DR AlphaFoldDB; Q6R567; -.
DR PRIDE; Q6R567; -.
DR EnsemblPlants; PHT76626; PHT76626; T459_20148.
DR GeneID; 107855034; -.
DR Gramene; PHT76626; PHT76626; T459_20148.
DR KEGG; cann:107855034; -.
DR OMA; DTTFNKH; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000189700; Genome assembly.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045103; RNF5/RNF185-like.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12313; PTHR12313; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Metal-binding; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..252
FT /note="E3 ubiquitin-protein ligase RMA1H1"
FT /id="PRO_0000395676"
FT TRANSMEM 232..251
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT ZN_FING 41..90
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 102..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 58
FT /note="H->A: Strong reduction of ubiquitin ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:19234086"
FT MUTAGEN 61
FT /note="C->S: Strong reduction of ubiquitin ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:19234086"
FT MUTAGEN 89
FT /note="C->S: Strong reduction of ubiquitin ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:19234086"
FT MUTAGEN 115
FT /note="K->R: No effect on ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:19234086"
SQ SEQUENCE 252 AA; 28211 MW; D05AE7113CEBAE49 CRC64;
MNQDMALEQL DTTFNKHDTP LGKWKSMNDE VEENISGGFD CNICLDCVHE PVITLCGHLY
CWPCIYKWIY FQSVSSENSD QQQPQCPVCK AEVSEKTLIP LYGRGGQSTK PSEGKAPNLG
IVIPQRPPSP RCGGHFLLPT TDSNPSQLLQ RRGYQQQSQT RQPAYQGSYM SSPMLSPGGA
TANMLQHSMI GEVAYARIFG NSSTTMYTYP NSYNLAISSS PRMRRQLSQA DRSLGRICFF
LFCCFVTCLI LF
