FLY1_ARATH
ID FLY1_ARATH Reviewed; 562 AA.
AC Q5PP23; O49446; Q0WN63;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Transmembrane E3 ubiquitin-protein ligase FLY1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:23482858};
DE AltName: Full=Protein FLYING SAUCER 1 {ECO:0000303|PubMed:23482858};
DE AltName: Full=RING-type E3 ubiquitin transferase FLY1 {ECO:0000305};
DE Flags: Precursor;
GN Name=FLY1 {ECO:0000303|PubMed:23482858};
GN OrderedLocusNames=At4g28370 {ECO:0000312|Araport:AT4G28370};
GN ORFNames=F20O9.50 {ECO:0000312|EMBL:CAA16876.2};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 369-562.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, SUBCELLULAR LOCATION, TISSUE
RP 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 regulates the degree of
CC methylesterification of pectin in seed mucilage. May be involved in the
CC recycling of pectin methylesterase enzymes in the endomembrane system
CC of seed coat epidermal cells. Possesses E3 ubiquitin-protein ligase
CC activity in vitro when associated with the E1 enzyme UBA1 and the E2
CC enzyme UBC8. May be involved in xylem development.
CC {ECO:0000269|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:0000269|PubMed:23482858};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:23482858}; 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:0000305|PubMed:23482858}.
CC -!- DISRUPTION PHENOTYPE: Seed coat mutant displaying primary wall
CC detachment, reduced mucilage extrusion, and increased mucilage
CC adherence. Decreased degree of homogalacturonan methylesterification in
CC seed mucilage. {ECO:0000269|PubMed:23482858}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16876.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79639.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021749; CAA16876.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161572; CAB79639.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85475.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66313.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66314.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66315.1; -; Genomic_DNA.
DR EMBL; BT020274; AAV84495.1; -; mRNA.
DR EMBL; AK229589; BAF01437.1; -; mRNA.
DR PIR; D85330; D85330.
DR RefSeq; NP_001328219.1; NM_001341912.1.
DR RefSeq; NP_001328220.1; NM_001341913.1.
DR RefSeq; NP_001328221.1; NM_001341914.1.
DR RefSeq; NP_194566.3; NM_118978.4.
DR AlphaFoldDB; Q5PP23; -.
DR IntAct; Q5PP23; 4.
DR STRING; 3702.AT4G28370.1; -.
DR PaxDb; Q5PP23; -.
DR PRIDE; Q5PP23; -.
DR ProteomicsDB; 230626; -.
DR EnsemblPlants; AT4G28370.1; AT4G28370.1; AT4G28370.
DR EnsemblPlants; AT4G28370.2; AT4G28370.2; AT4G28370.
DR EnsemblPlants; AT4G28370.3; AT4G28370.3; AT4G28370.
DR EnsemblPlants; AT4G28370.4; AT4G28370.4; AT4G28370.
DR GeneID; 828953; -.
DR Gramene; AT4G28370.1; AT4G28370.1; AT4G28370.
DR Gramene; AT4G28370.2; AT4G28370.2; AT4G28370.
DR Gramene; AT4G28370.3; AT4G28370.3; AT4G28370.
DR Gramene; AT4G28370.4; AT4G28370.4; AT4G28370.
DR KEGG; ath:AT4G28370; -.
DR Araport; AT4G28370; -.
DR TAIR; locus:2121333; AT4G28370.
DR eggNOG; KOG0828; Eukaryota.
DR HOGENOM; CLU_038877_0_0_1; -.
DR InParanoid; Q5PP23; -.
DR OMA; PHNFMRV; -.
DR OrthoDB; 935391at2759; -.
DR PhylomeDB; Q5PP23; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5PP23; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5PP23; baseline and differential.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0080001; P:mucilage extrusion from seed coat; IMP:TAIR.
DR GO; GO:0048363; P:mucilage pectin metabolic process; IMP:TAIR.
DR GO; GO:0009827; P:plant-type cell wall modification; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..562
FT /note="Transmembrane E3 ubiquitin-protein ligase FLY1"
FT /id="PRO_0000443822"
FT TOPO_DOM 33..262
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..321
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..397
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..458
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ZN_FING 512..556
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 562 AA; 64604 MW; 889CDB7DF209BEEA CRC64;
MKKREHLGLG FFEWQIILWL SIWLAISQQA LGLRPIREKP RSWSDEWLFG RKQEAEVGPF
SAWNITGTYR GTWKFLNSLN SSSKFQDFQK ENGNSVVELV AVPTKITGVH YVQGVVVFHD
VFDNEQNVGG AQINLEGVYI WPFRQLRLVA NSGKESDSGQ EDNNLLSNPY HLLGIFSSQV
FQESPRDRLL KRKLSPVNEM EKHCNIEIAA QVSRVASSEN NGDKNYYHME GLMESPGVGD
DGDCFSPLLL NATSVNVEVY YNKAVNYTLM VTFVSFLQVL LLIRQMEHGN TQSGAAKVSI
VMIGQQAIMD AYLCLLHLTA GILVESLFNA FATAAFFKFV VFSIFEMRYL LAIWKATRPS
NSGEGWETMR RELSFLYSRF YGILLGGILI MYQFHNYMQP ILLLMYSFWI PQIVANVVRD
SRKPLHPYYI LGMTATRLAI PLYVFGCPHN FMRVEPNKVW CICLCTFMGL QAVILLLQHY
FGSRCFVPRQ MLPEKYNYHR RFNRDVSRTT DCVICMTAID LRQHTSDCMV TPCEHFFHSG
CLQRWMDIKM ECPTCRRSLP PA
