ENT1_SCHPO
ID ENT1_SCHPO Reviewed; 702 AA.
AC O74423;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Epsin-1;
GN Name=ent1; ORFNames=SPCC162.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-86 AND THR-103.
RX PubMed=15659877;
RA Sakamoto C., Kawamoto C., Takeuchi K., Miyamoto I., Shuntoh H.;
RT "Fission yeast epsin, Ent1p is required for endocytosis and involved in
RT actin organization.";
RL Kobe J. Med. Sci. 50:47-57(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-216; SER-218;
RP SER-223; SER-255 AND THR-406, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP GENE MODEL REVISION.
RX PubMed=24929437; DOI=10.1038/nsmb.2843;
RA Duncan C.D., Mata J.;
RT "The translational landscape of fission-yeast meiosis and sporulation.";
RL Nat. Struct. Mol. Biol. 21:641-647(2014).
CC -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol 3,5-
CC bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate
CC (PtdIns(4,5)P2). Required for endocytosis and localization of actin.
CC {ECO:0000269|PubMed:15659877}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15659877}. Membrane
CC {ECO:0000255|PROSITE-ProRule:PRU00243, ECO:0000269|PubMed:15659877};
CC Peripheral membrane protein {ECO:0000269|PubMed:15659877}.
CC Note=Localizes in a punctate pattern. Colocalizes with F-actin.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA19587.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CU329672; CAA19587.1; ALT_SEQ; Genomic_DNA.
DR PIR; T41024; T41024.
DR RefSeq; NP_588237.1; NM_001023227.2.
DR AlphaFoldDB; O74423; -.
DR SMR; O74423; -.
DR BioGRID; 275955; 4.
DR STRING; 4896.SPCC162.07.1; -.
DR iPTMnet; O74423; -.
DR PaxDb; O74423; -.
DR PRIDE; O74423; -.
DR EnsemblFungi; SPCC162.07.1; SPCC162.07.1:pep; SPCC162.07.
DR GeneID; 2539390; -.
DR KEGG; spo:SPCC162.07; -.
DR PomBase; SPCC162.07; ent1.
DR VEuPathDB; FungiDB:SPCC162.07; -.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_012678_0_0_1; -.
DR InParanoid; O74423; -.
DR Reactome; R-SPO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR PRO; PR:O74423; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; ISO:PomBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:PomBase.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; ISM:PomBase.
DR GO; GO:0000147; P:actin cortical patch assembly; ISO:PomBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013182; DUF1720.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR003903; UIM_dom.
DR Pfam; PF08226; DUF1720; 2.
DR Pfam; PF01417; ENTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00726; UIM; 2.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50330; UIM; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Endocytosis; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..702
FT /note="Epsin-1"
FT /id="PRO_0000074523"
FT DOMAIN 10..142
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 226..245
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 254..273
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 136..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..212
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 86
FT /note="G->S: Aberrant cell morphology and depolarization of
FT F-actin."
FT /evidence="ECO:0000269|PubMed:15659877"
FT MUTAGEN 103
FT /note="T->A: Aberrant cell morphology and depolarization of
FT F-actin."
FT /evidence="ECO:0000269|PubMed:15659877"
SQ SEQUENCE 702 AA; 79751 MW; 6B3ED8F0BD3400AA CRC64;
MKAAVRSVKN FSKGYTDTQI KVRNATTNDS WGPSGTAMAE IAELTYDQNE MLEVMDIIDR
RLNDKGKNWR HVFKSLSLLE YCLHNGSENV VRWAKDNIYI ITTLREFVYV DDNGHDQGQN
VRTKAKEITS LLEDEHALKE ARGDSRERDR DRDRTRSSRF DDDDDDRAPY EESRLSRAPS
RASRYDDDDR DHRSRRRSRS RRPGRSRSRR RSRRPSPSAE HNSAEENDPE LQRVIEESKR
QAEEDAKRRN MANDSEAELQ KAIQLSKEED EARQRHQRER EQQEQAFMGN QQNAYQPVDF
FGNPVQPQPT GFLQQQPTGF IRPQNTGFVQ PQYTGFVQPQ HTGFVQPQAT GFMQPQRTGF
VQPQATGFVQ PQATGFVQPQ ATGFMQPQRT GFVQPQATGF MQPQRTGFVQ PQATGFMQPQ
RTGFVQPQAT GFIQPQRTGF VQPQQNGFFN PQPTGYMQPQ RTGMMQPQRT GFSQPFESNN
PFPVMQPQRT GFGQTPNAPM MAPNHTGYVH PQPTGLQRQT TGYTGNNNPY SRPLQSQSTG
ILQQQQQQSA PRLEPTKTGS NNPFAQFSNL PSQSTAPATK PMKPVRTGDD RFSNIAQAIS
TGNPMGTDSF GNIGLTRVPT QHTGSKFTNS AGQTIQAQAT GNTHNPFQSQ QATGYYKQPM
QQQQNMQQPY YNQQNYNYQN QQPMQGMQQQ SMQPQVGSLI DL
