EPN3_ARATH
ID EPN3_ARATH Reviewed; 1024 AA.
AC Q93YP4; Q9LX42;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Clathrin interactor EPSIN 3;
DE AltName: Full=EPSIN-related 3;
GN Name=EPSIN3; Synonyms=EPSINR3; OrderedLocusNames=At3g59290;
GN ORFNames=F25L23.150;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-
CC bisphosphate (PtdIns(4,5)P2). May have a role in transport via
CC clathrin-coated vesicles from the trans-Golgi network to endosomes.
CC Stimulates clathrin assembly (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with clathrin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB91599.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL356014; CAB91599.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79900.1; -; Genomic_DNA.
DR EMBL; AY059878; AAL24360.1; -; mRNA.
DR EMBL; BT008432; AAP37791.1; -; mRNA.
DR PIR; T48997; T48997.
DR RefSeq; NP_567079.1; NM_115791.3.
DR AlphaFoldDB; Q93YP4; -.
DR SMR; Q93YP4; -.
DR STRING; 3702.AT3G59290.1; -.
DR iPTMnet; Q93YP4; -.
DR PaxDb; Q93YP4; -.
DR PRIDE; Q93YP4; -.
DR ProteomicsDB; 220666; -.
DR EnsemblPlants; AT3G59290.1; AT3G59290.1; AT3G59290.
DR GeneID; 825098; -.
DR Gramene; AT3G59290.1; AT3G59290.1; AT3G59290.
DR KEGG; ath:AT3G59290; -.
DR Araport; AT3G59290; -.
DR TAIR; locus:2081167; AT3G59290.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_011840_0_0_1; -.
DR InParanoid; Q93YP4; -.
DR OMA; FMTQQPY; -.
DR OrthoDB; 737244at2759; -.
DR PhylomeDB; Q93YP4; -.
DR PRO; PR:Q93YP4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93YP4; baseline and differential.
DR Genevisible; Q93YP4; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR Pfam; PF01417; ENTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Golgi apparatus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1024
FT /note="Clathrin interactor EPSIN 3"
FT /id="PRO_0000397863"
FT DOMAIN 18..150
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 152..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 403..407
FT /note="Clathrin binding"
FT /evidence="ECO:0000250"
FT MOTIF 448..450
FT /note="ALPHA-ADR binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 171..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q67YI9"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q67YI9"
SQ SEQUENCE 1024 AA; 109694 MW; 1C8A5F33EB12ED04 CRC64;
MKKAFGQTVR DLKRGVNKKV LKVPGIEQKV LDATSNESWG PHGSLLADIA HASRNYHEYQ
ITMGVLWKRL SDSGKNWRHV YKALTVLEYM VGHGSERVIE EVKEHAYQIT TLSGFQYIDS
SGKDQGSNVR KKAQSLVALV NDKERITEVR EKAAANRDKY HNSMHRPSGG YGDKYDYEGR
YGDRDEGRSS YGKEREYGYR DDDRNSRDGD RYSRDSEDRY GRDGNTDDEY RGRSRSVDNY
NGSRGRSSDR ERPIEDDGQS SSRDSGAPAD DHSQDGRGGL ERKFSEQNIG AAPPSYEEAV
SESRSPVYSE RDGGETPQVA PPGAAASPLA ENISVDNKAA DFVNESSPQQ VEAFDEFDPR
GSVSAACAPT AGASVPAPIP PTVVSTPAPP ASINAEMDLL GSLSDVFSPN PLAIVTSDST
SVETNGQANT GLAPSFSTSQ SSTQPFDDPF GDSPFKAITS ADTETSQHQS FGVPFQPTPP
TSNPNNEHNF GFGEAFSAVT DSEPGVQNMQ APPNLSVFPQ EQFDTSQSEI DILAGILPPS
GPPVSLSPQP DSTMPTSQFH PNGNSYESYH HQAAPTDLNM QGQTPFGQAS QQFNMVSHSQ
NHHEGMQFNN GGFTQQPGYA GPATSQPPQY TPGVSSHPPS ESFPHQPGSA TSASSQTPYA
TTPNVSAGQF DGGSFMTQQP YGVTQQVHVV PSHIPQRTQS GPVAAFGNNN NIVGDMHQPG
STPSSSSQTP YPTTPNAPSG QFDGGNFMTQ QPYGVIPQVH GVPSHIPQRT QSGPVAAHGN
SNNVVGDMFS PAGLSSLETS ASQPSLTPLT GAIEIVPQNQ KKFEPKSTIW ADTLSRGLVN
FNISGPKTNP LADIGVDFEA INRKEKRLEK PTITQQQVTS TINMGKAMGS GTGLGRAGAG
AMRPPTNSMV GSSMPTGMNV GGYGGMNQHQ PIGMNQNHPM GMNQNLSMGM NQNYPMGMNQ
NYPMGMGMNM NMGGYGQGYP MQPQQGMGMA PPGAPQGMTG AYNPMMGQGG YNPQQQQPYG
GGYR
