EPN2_ARATH
ID EPN2_ARATH Reviewed; 895 AA.
AC Q67YI9; Q570B8; Q67YS3; Q94A14; Q9ZW78; Q9ZW79;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Clathrin interactor EPSIN 2;
DE AltName: Full=EPSIN-related 2;
GN Name=EPSIN2; Synonyms=EPSINR2; OrderedLocusNames=At2g43160/At2g43170;
GN ORFNames=F14B2.10, F14B2.11;
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] (ISOFORM 1).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 GENE FAMILY.
RX PubMed=16231097; DOI=10.1007/s00709-005-0105-7;
RA Holstein S.E., Oliviusson P.;
RT "Sequence analysis of Arabidopsis thaliana E/ANTH-domain-containing
RT proteins: membrane tethers of the clathrin-dependent vesicle budding
RT machinery.";
RL Protoplasma 226:13-21(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CLATHRIN; VTI12; ALPHA-ADR
RP AND DELTA-ADR, AND MUTAGENESIS OF 409-LEU--PHE-413 AND 454-ASP--PHE-456.
RX PubMed=17277094; DOI=10.1104/pp.106.095349;
RA Lee G.-J., Kim H., Kang H., Jang M., Lee D.W., Lee S., Hwang I.;
RT "EpsinR2 interacts with clathrin, adaptor protein-3, AtVTI12, and
RT phosphatidylinositol-3-phosphate. Implications for EpsinR2 function in
RT protein trafficking in plant cells.";
RL Plant Physiol. 143:1561-1575(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND SER-282, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: May have a role in transport via clathrin-coated vesicles
CC from the trans-Golgi network to endosomes. Stimulates clathrin assembly
CC (By similarity). Binds to membranes enriched in phosphatidylinositol 3-
CC phosphate (PtdIns(3)P). Plays an important role in protein trafficking.
CC {ECO:0000250, ECO:0000269|PubMed:17277094}.
CC -!- SUBUNIT: Interacts with clathrin, VTI12, DELTA-ADR and ALPHA-ADR.
CC {ECO:0000269|PubMed:17277094}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17277094}.
CC Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:17277094}. Note=Localizes also to a novel cellular
CC compartment, the 'delta compartment', characterized by colocalization
CC of EPSIN2 and DELTA-ADR.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q67YI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q67YI9-2; Sequence=VSP_039700, VSP_039701;
CC -!- DOMAIN: The ENTH domain is required for PtdIns(3)P affinity and EPSIN2
CC subcellular location.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC64305.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC64306.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004450; AAC64305.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004450; AAC64306.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10216.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10217.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10218.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10219.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63201.1; -; Genomic_DNA.
DR EMBL; AY050457; AAK91471.1; -; mRNA.
DR EMBL; BT002247; AAN72258.1; -; mRNA.
DR EMBL; AK176395; BAD44158.1; -; mRNA.
DR EMBL; AK176406; BAD44169.1; -; mRNA.
DR EMBL; AK176479; BAD44242.1; -; mRNA.
DR EMBL; AK220792; BAD94036.1; -; mRNA.
DR EMBL; AK221258; BAD93910.1; -; mRNA.
DR EMBL; AK221259; BAD93914.1; -; mRNA.
DR EMBL; AK229845; BAF01674.1; -; mRNA.
DR EMBL; AK230277; BAF02079.1; -; mRNA.
DR PIR; G84862; G84862.
DR PIR; H84862; H84862.
DR RefSeq; NP_001031535.1; NM_001036458.2. [Q67YI9-2]
DR RefSeq; NP_001325306.1; NM_001337018.1. [Q67YI9-1]
DR RefSeq; NP_850386.1; NM_180055.3. [Q67YI9-1]
DR RefSeq; NP_850387.1; NM_180056.2. [Q67YI9-1]
DR RefSeq; NP_973675.1; NM_201946.4. [Q67YI9-1]
DR AlphaFoldDB; Q67YI9; -.
DR SMR; Q67YI9; -.
DR BioGRID; 4255; 6.
DR STRING; 3702.AT2G43160.1; -.
DR iPTMnet; Q67YI9; -.
DR PaxDb; Q67YI9; -.
DR PRIDE; Q67YI9; -.
DR ProteomicsDB; 221849; -. [Q67YI9-1]
DR EnsemblPlants; AT2G43160.1; AT2G43160.1; AT2G43160. [Q67YI9-1]
DR EnsemblPlants; AT2G43160.2; AT2G43160.2; AT2G43160. [Q67YI9-1]
DR EnsemblPlants; AT2G43160.3; AT2G43160.3; AT2G43160. [Q67YI9-1]
DR EnsemblPlants; AT2G43160.4; AT2G43160.4; AT2G43160. [Q67YI9-2]
DR EnsemblPlants; AT2G43160.5; AT2G43160.5; AT2G43160. [Q67YI9-1]
DR GeneID; 818918; -.
DR Gramene; AT2G43160.1; AT2G43160.1; AT2G43160. [Q67YI9-1]
DR Gramene; AT2G43160.2; AT2G43160.2; AT2G43160. [Q67YI9-1]
DR Gramene; AT2G43160.3; AT2G43160.3; AT2G43160. [Q67YI9-1]
DR Gramene; AT2G43160.4; AT2G43160.4; AT2G43160. [Q67YI9-2]
DR Gramene; AT2G43160.5; AT2G43160.5; AT2G43160. [Q67YI9-1]
DR KEGG; ath:AT2G43160; -.
DR Araport; AT2G43160; -.
DR TAIR; locus:2040981; AT2G43160.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_011840_0_0_1; -.
DR InParanoid; Q67YI9; -.
DR OMA; ISTINMG; -.
DR OrthoDB; 737244at2759; -.
DR PhylomeDB; Q67YI9; -.
DR PRO; PR:Q67YI9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q67YI9; baseline and differential.
DR Genevisible; Q67YI9; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Golgi apparatus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..895
FT /note="Clathrin interactor EPSIN 2"
FT /id="PRO_0000397862"
FT DOMAIN 18..150
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 150..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 409..413
FT /note="Clathrin binding"
FT MOTIF 454..456
FT /note="ALPHA-ADR binding"
FT COMPBIAS 179..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT VAR_SEQ 645..646
FT /note="HQ -> LA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_039700"
FT VAR_SEQ 647..895
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_039701"
FT MUTAGEN 409..413
FT /note="LADVF->AAAAA: Impaired clathrin binding."
FT /evidence="ECO:0000269|PubMed:17277094"
FT MUTAGEN 454..456
FT /note="DPF->AAA: Impaired ALPHA-ADR binding."
FT /evidence="ECO:0000269|PubMed:17277094"
FT CONFLICT 211
FT /note="R -> H (in Ref. 3; AAK91471/AAN72258)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="S -> N (in Ref. 4; BAD94036/BAF01674)"
FT /evidence="ECO:0000305"
FT CONFLICT 854
FT /note="G -> D (in Ref. 3; AAK91471/AAN72258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 895 AA; 95478 MW; 710225FDBBEC7763 CRC64;
MKKVFGQTVR DLKREVNKKV LKVPGVEQKV LDATSNEPWG PHGSLLADLA QASRNYHEYQ
LIMVVIWKRL SDTGKNWRHV YKALTVLEYM VGHGSERVID EIRERAYQIS TLSDFQYIDS
GGRDQGSNVR KKSQSLVALV NDKERIAEVR QKAAANRDKY RSSAPGGMYK PSGGYGDKYD
YGSRDEERSS YGREREYGYR DDDRNSRDGD RHSRDSEDRY GRDGNRDDDY RGRSRSVDNY
GSRGRSSERE REDDGHSSSR GSGARADDNS QDGRGGLQRK FSEQNIGAPP SYEEAVSDSR
SPVYSERDGG ETPQVTAPGA ASPPPPQVAA PEAASPPTGT NTANTTATFV NESPSQKVET
FDEFDPRSAF SAGPPAYAST DGVTAPPTVT SMSAPTTSNS VEMDLLGSLA DVFSSNALAI
VPADSIYVET NGQANAGPAP SFSTSQPSTQ SFDDPFGDSP FKAFTSTDTD STPQQNFGAS
FQPPPPAFTS EVSHPDTAHN FGFGDSFSAV ANPDPASQNV QPPSNSPGFP QEQFATSQSG
IDILAGILPP SGPPVQSGPS IPTSQFPPSG NNMYEGFHSQ PPVSTAPNLP GQTPFGQAVQ
PYNMVPHSQN MTGAMPFNSG GFMHQPGSQT PYSTPSGPAG QFMAHQGHGM PPSHGPQRTQ
SGPVTLQGNN NVMGDMFSQA TPNSLTSSSS HPDLTPLTGA IEIVPPPQKK FEPKSSVWAD
TLSRGLVNFN ISGSKTNPLA DIGVDFEAIN RREKRLEKQT NTPATSTINM GKAMGSGTGL
GRSGATAMRP PPNPMTGSGM PMGGGMGVGS YGGMNQNQPM GMGMGAGMNQ NQPMGMGMGP
GMNMNMNMGG YGQGYPMQPQ NPGMVPSPNM PGNNYNPMMG QGGYNPQQSY GGGYR
