FLY2_ARATH
ID FLY2_ARATH Reviewed; 559 AA.
AC Q500V2; Q9SIU7;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Transmembrane E3 ubiquitin-protein ligase FLY2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Protein FLYING SAUCER 2 {ECO:0000303|PubMed:23482858};
DE AltName: Full=RING-type E3 ubiquitin transferase FLY2 {ECO:0000305};
DE Flags: Precursor;
GN Name=FLY2 {ECO:0000303|PubMed:23482858};
GN OrderedLocusNames=At2g20650 {ECO:0000312|Araport:AT2G20650};
GN ORFNames=F23N11.3 {ECO:0000312|EMBL:AEC07052.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23482858; DOI=10.1105/tpc.112.107888;
RA Voiniciuc C., Dean G.H., Griffiths J.S., Kirchsteiger K., Hwang Y.T.,
RA Gillett A., Dow G., Western T.L., Estelle M., Haughn G.W.;
RT "Flying saucer1 is a transmembrane RING E3 ubiquitin ligase that regulates
RT the degree of pectin methylesterification in Arabidopsis seed mucilage.";
RL Plant Cell 25:944-959(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that may be involved in xylem
CC development. {ECO:0000305|PubMed:23482858}.
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:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:Q5PP23}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in stems. Expressed in root xylem
CC and seed coat. {ECO:0000269|PubMed:23482858}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000250|UniProtKB:Q5PP23}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:23482858}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21704.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15208.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006234; AAM15208.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007048; AAD21704.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07052.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07053.1; -; Genomic_DNA.
DR EMBL; BT022115; AAY34176.1; -; mRNA.
DR PIR; F84591; F84591.
DR RefSeq; NP_179657.2; NM_127629.4.
DR RefSeq; NP_973491.1; NM_201762.2.
DR AlphaFoldDB; Q500V2; -.
DR STRING; 3702.AT2G20650.1; -.
DR iPTMnet; Q500V2; -.
DR PaxDb; Q500V2; -.
DR PRIDE; Q500V2; -.
DR ProteomicsDB; 230544; -.
DR EnsemblPlants; AT2G20650.1; AT2G20650.1; AT2G20650.
DR EnsemblPlants; AT2G20650.2; AT2G20650.2; AT2G20650.
DR GeneID; 816593; -.
DR Gramene; AT2G20650.1; AT2G20650.1; AT2G20650.
DR Gramene; AT2G20650.2; AT2G20650.2; AT2G20650.
DR KEGG; ath:AT2G20650; -.
DR Araport; AT2G20650; -.
DR TAIR; locus:2046036; AT2G20650.
DR eggNOG; KOG0828; Eukaryota.
DR HOGENOM; CLU_038877_0_0_1; -.
DR InParanoid; Q500V2; -.
DR OMA; HYVQGSV; -.
DR OrthoDB; 935391at2759; -.
DR PhylomeDB; Q500V2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q500V2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q500V2; baseline and differential.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
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:0004842; F:ubiquitin-protein transferase activity; ISS:TAIR.
DR GO; GO:0009827; P:plant-type cell wall modification; ISS:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Membrane; Metal-binding; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..559
FT /note="Transmembrane E3 ubiquitin-protein ligase FLY2"
FT /id="PRO_0000443823"
FT TOPO_DOM 30..259
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..318
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..394
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..458
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ZN_FING 509..553
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 559 AA; 63945 MW; B3A9FED95F308CD5 CRC64;
MNNLGNFGVW GFGFFSLSIW FAVLQQANGL RPIRETARSW GDEWLFGKKE KGGAGPFSAW
NITGTYRGTW KFLDTVNSSS KFPDFRKESG NSVIELVTSP TKITGVHYVQ GAVVFHDVFD
NEHNVGGAQI KVEGVYIWPF RQLRLVANSG KKSDSGLEDD YLLSNPYHLL GIFSSQVFQE
SPRDRILKQK TSPIYEMEKH CNIEIAAQIS QSTSSENNGD KDRYQIEGLM ESPAVDDEVD
CFSPLSLNAT SINVEVYYNK AVNYTLMVTF VSFLQVLLLI RQMEHSNTQS GAAKVSIVMI
GQQAIMDSYL CLLHLTAGIL VESLFNAFAT AAFFKFVVFS IFEMRYLLSI WKATRPSTSG
EGWETMRREL SFLYSRFYGI LLGGILLMYE FHNYMRPILL LMYSFWIPQI VANVVRDSRK
PLHPYYILGM TVTRLAIPLY VFGCPKNFMR VEPSKAWCVS LCAFMGFQAG VLLLQHYFGS
RCFVPRKLLP EKYSYYRRLD HNVNRSRDCV ICMTTIDLRH RINDCMVTPC EHIFHSGCLQ
RWMDIKMECP TCRRPLPPA
