EPN1_ARATH
ID EPN1_ARATH Reviewed; 560 AA.
AC Q8VY07; Q0WLJ9; Q9LYF9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Clathrin interactor EPSIN 1;
DE AltName: Full=EPSIN-related 1;
GN Name=EPSIN1; Synonyms=EPSINR1; OrderedLocusNames=At5g11710;
GN ORFNames=T22P22.100;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH CLATHRIN; VTI11; VSR1 AND GAMMA-ADR.
RX PubMed=16905657; DOI=10.1105/tpc.105.039123;
RA Song J., Lee M.H., Lee G.-J., Yoo C.M., Hwang I.;
RT "Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of
RT soluble cargo proteins in plant cells via interactions with clathrin, AP-1,
RT VTI11, and VSR1.";
RL Plant Cell 18:2258-2274(2006).
RN [7]
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).
RN [8]
RP INTERACTION WITH AMSH3.
RX PubMed=20543027; DOI=10.1105/tpc.110.075952;
RA Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D.,
RA Geldner N., Chory J., Schwechheimer C.;
RT "The deubiquitinating enzyme AMSH3 is required for intracellular
RT trafficking and vacuole biogenesis in Arabidopsis thaliana.";
RL Plant Cell 22:1826-1837(2010).
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). Does not seem to bind to phospholipids. Plays an
CC important role in the vacuolar trafficking of soluble cargo proteins at
CC the trans-Golgi network. {ECO:0000250, ECO:0000269|PubMed:16905657}.
CC -!- SUBUNIT: Interacts with clathrin, VTI11, GAMMA-ADR and VSR1. Binds to
CC the deubiquitinating enzyme AMSH3. {ECO:0000269|PubMed:16905657,
CC ECO:0000269|PubMed:20543027}.
CC -!- INTERACTION:
CC Q8VY07; Q0WNJ6: CHC1; NbExp=3; IntAct=EBI-1162785, EBI-1162845;
CC Q8VY07; Q84K16: GAMMA-ADR; NbExp=2; IntAct=EBI-1162785, EBI-1163115;
CC Q8VY07; P93026: VSR1; NbExp=2; IntAct=EBI-1162785, EBI-1163008;
CC Q8VY07; Q9SEL6: VTI11; NbExp=3; IntAct=EBI-1162785, EBI-1162795;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16905657}.
CC Prevacuolar compartment {ECO:0000269|PubMed:16905657}. Cytoplasm
CC {ECO:0000269|PubMed:16905657}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16905657}. Note=Associated with actin filaments.
CC -!- TISSUE SPECIFICITY: Mostly expressed in cotyledons and flowers, and, to
CC a lower extent, in roots, leaves and siliques (at protein level).
CC {ECO:0000269|PubMed:16905657}.
CC -!- DISRUPTION PHENOTYPE: Defect in vacuolar trafficking.
CC {ECO:0000269|PubMed:16905657}.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87689.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163814; CAB87689.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91713.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70266.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70267.1; -; Genomic_DNA.
DR EMBL; AY074304; AAL67001.1; -; mRNA.
DR EMBL; AY096605; AAM20255.1; -; mRNA.
DR EMBL; AK227905; BAE99875.1; -; mRNA.
DR EMBL; AK230200; BAF02008.1; -; mRNA.
DR PIR; T48530; T48530.
DR RefSeq; NP_001318545.1; NM_001343211.1.
DR RefSeq; NP_001331892.1; NM_001343212.1.
DR RefSeq; NP_196732.2; NM_121209.6.
DR AlphaFoldDB; Q8VY07; -.
DR SMR; Q8VY07; -.
DR BioGRID; 16321; 4.
DR IntAct; Q8VY07; 6.
DR STRING; 3702.AT5G11710.1; -.
DR iPTMnet; Q8VY07; -.
DR PaxDb; Q8VY07; -.
DR PRIDE; Q8VY07; -.
DR ProteomicsDB; 220776; -.
DR EnsemblPlants; AT5G11710.1; AT5G11710.1; AT5G11710.
DR EnsemblPlants; AT5G11710.2; AT5G11710.2; AT5G11710.
DR EnsemblPlants; AT5G11710.3; AT5G11710.3; AT5G11710.
DR GeneID; 831043; -.
DR Gramene; AT5G11710.1; AT5G11710.1; AT5G11710.
DR Gramene; AT5G11710.2; AT5G11710.2; AT5G11710.
DR Gramene; AT5G11710.3; AT5G11710.3; AT5G11710.
DR KEGG; ath:AT5G11710; -.
DR Araport; AT5G11710; -.
DR TAIR; locus:2181920; AT5G11710.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_037572_0_0_1; -.
DR InParanoid; Q8VY07; -.
DR OMA; QNVAMNL; -.
DR OrthoDB; 737244at2759; -.
DR PhylomeDB; Q8VY07; -.
DR PRO; PR:Q8VY07; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VY07; baseline and differential.
DR Genevisible; Q8VY07; AT.
DR GO; GO:0005884; C:actin filament; IDA:TAIR.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:TAIR.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:TAIR.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR033521; EPSIN1.
DR PANTHER; PTHR12276:SF96; PTHR12276:SF96; 1.
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 Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Golgi apparatus;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..560
FT /note="Clathrin interactor EPSIN 1"
FT /id="PRO_0000397861"
FT DOMAIN 20..152
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 190..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 296..300
FT /note="Clathrin binding"
FT /evidence="ECO:0000250"
FT MOTIF 320..322
FT /note="ALPHA-ADR binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 193..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 311
FT /note="N -> D (in Ref. 4; BAF02008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 60634 MW; 29272781B09D2629 CRC64;
MDFMKVFDQT VREIKREVNL KVLKVPEMEQ KVLDATDNEP WGPHGTALAE IAQATKKFSE
CQMVMSVLWT RLSETGKDWR YVYKALAVID YLISNGSERA VDEIIEHTYQ ISSLTSFEYV
EPNGKDVGIN VRKKAENIVA LLNNKEKISE IRDKAVANRN KYVGLSSTGI TYKSGSSASF
GGSFQSGSSN FDSYKDRDSR EDKNDYESFQ KSRRGVKTEE QSYTSKKSFS RYGSTDHDNL
SSGKKSPDSA KHRSYVSAAP SNNDDDFDDF DPRGTSSNKP STGSANQVDL FGGDLIGDFL
DSGPTETSST NNNENFQEAD LFADAAFVSA SAQGAEFGSQ TQKQVDLFSA SEPSVTVSSA
PPTVDLFASS ESVVSPEAKI SIPESMATPN IVDPFAAVPM DNFDGSDPFG AFTSHSASVS
TGPQAPSVHG SATNTTSPLS FADSKPQHLQ KKDPFQVKSG IWADSLSRGL IDLNITAPKK
ASLADVGVVG DLSNEDGNKA SAASYYSGWS MGAGSGLGKT GLYSTQQQQQ QQQQQQAPDI
SDDFFSSLSN QRYQSGGFKQ
