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Database: UniProt
Entry: A0A4P1R907_LUPAN
LinkDB: A0A4P1R907_LUPAN
Original site: A0A4P1R907_LUPAN 
ID   A0A4P1R907_LUPAN        Unreviewed;       521 AA.
AC   A0A4P1R907;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=TanjilG_23368 {ECO:0000313|EMBL:OIW05582.1};
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW05582.1, ECO:0000313|Proteomes:UP000188354};
RN   [1] {ECO:0000313|EMBL:OIW05582.1, ECO:0000313|Proteomes:UP000188354}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC   TISSUE=Whole plant {ECO:0000313|EMBL:OIW05582.1};
RX   PubMed=27557478; DOI=10.1111/pbi.12615;
RA   Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA   Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA   Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA   McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT   "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT   an emerging health food: insights into plant-microbe interactions and
RT   legume evolution.";
RL   Plant Biotechnol. J. 15:318-330(2017).
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}.
CC   -!- SIMILARITY: Belongs to the HRD1 family.
CC       {ECO:0000256|ARBA:ARBA00010089}.
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DR   EMBL; CM007368; OIW05582.1; -; Genomic_DNA.
DR   RefSeq; XP_019454327.1; XM_019598782.1.
DR   RefSeq; XP_019454328.1; XM_019598783.1.
DR   RefSeq; XP_019454329.1; XM_019598784.1.
DR   AlphaFoldDB; A0A4P1R907; -.
DR   STRING; 3871.A0A4P1R907; -.
DR   GeneID; 109355562; -.
DR   OrthoDB; 2912447at2759; -.
DR   Proteomes; UP000188354; Chromosome LG08.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd16479; RING-H2_synoviolin; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22763:SF184; E3 UBIQUITIN-PROTEIN LIGASE HRD1; 1.
DR   PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188354};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   TRANSMEM        43..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          292..330
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          340..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  58890 MW;  9E147E4556C6A6C9 CRC64;
     MMRLQTYAGL SLIATLAVTY HAFNSRGQFY PAMVYLATSK ISLVLVLNMG LVIMCVLWQL
     TKLIFLGSLR EAEIERLNEQ SWREVVEILF AITIFRQDFS VSFLAMVTTL LLIKALHWLA
     QKRLEYIETT PSVTKLSHVR IVSFMGFLFL LDIIFLYSSV KHLILTWQPS VSLFFAFEYV
     ILATTTASIF VKYIFYVSDM LMDGQWEKKP VYTFYLELIK DLLHLSMYLC FFLVIFINYG
     VPLHLIRELY ETFRNFKIRV ADYLRYRKIT SNMNDRFPDA TPDELNASDA TCIICREEMT
     TAKKLICGHL FHVHCLRSWL ERQHTCPTCR AMVVPAENGT TSAGGLQASQ SDAHRHGTGA
     GSTAQAEVGN GVATDNLNRH QARLQAAAAA ASMYEKSYVY PSATSLARSQ GYTQYPPVQR
     PVPESSSAEL NREIASNSKQ AQTHYVIPDG PMNVSSPPMG NFDSLVEAQR KLLQLQIEIL
     QNQLQLLQKT NVDKSVDEGI SVSDSRGKGI ASSFVSNHEE I
//
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