EPN_DICDI
ID EPN_DICDI Reviewed; 686 AA.
AC Q54EH1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Epsin;
GN Name=epnA; ORFNames=DDB_G0291512;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=18827012; DOI=10.1242/jcs.032573;
RA Brady R.J., Wen Y., O'Halloran T.J.;
RT "The ENTH and C-terminal domains of Dictyostelium epsin cooperate to
RT regulate the dynamic interaction with clathrin-coated pits.";
RL J. Cell Sci. 121:3433-3444(2008).
CC -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-
CC bisphosphate (PtdIns(4,5)P2). {ECO:0000269|PubMed:18827012}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000269|PubMed:18827012}.
CC -!- DOMAIN: The ENTH domain coordinates with the clathrin-binding C-
CC terminal domain to allow a dynamic interaction of epsin with coated
CC pits. {ECO:0000269|PubMed:18827012}.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000177; EAL61740.1; -; Genomic_DNA.
DR RefSeq; XP_635269.1; XM_630177.1.
DR AlphaFoldDB; Q54EH1; -.
DR SMR; Q54EH1; -.
DR STRING; 44689.DDB0266727; -.
DR PaxDb; Q54EH1; -.
DR EnsemblProtists; EAL61740; EAL61740; DDB_G0291512.
DR GeneID; 8628213; -.
DR KEGG; ddi:DDB_G0291512; -.
DR dictyBase; DDB_G0291512; epnA.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_401399_0_0_1; -.
DR InParanoid; Q54EH1; -.
DR OMA; GMNQPMM; -.
DR Reactome; R-DDI-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR PRO; PR:Q54EH1; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0030122; C:AP-2 adaptor complex; IDA:dictyBase.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:dictyBase.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:dictyBase.
DR GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0030276; F:clathrin binding; IDA:dictyBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:dictyBase.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IMP:dictyBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:dictyBase.
DR GO; GO:0035304; P:regulation of protein dephosphorylation; IDA:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
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 3: Inferred from homology;
KW Coated pit; Membrane; Reference proteome.
FT CHAIN 1..686
FT /note="Epsin"
FT /id="PRO_0000328494"
FT DOMAIN 14..145
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 177..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 75837 MW; 886E3AA276FB7259 CRC64;
METMIKSYIK KGKDAVLNTP EIERKVRDAT SNDKWGPSGT QMQEISRASY NYECFPIIMG
VIWKRINDPG KFWRHVYKSL LLIDYLVRNG SPQVIRDCRH HTMEIKTLVE FQYIEEEKDV
GLSVRERAKQ VIDLLQDDQR IKEERDKAKT NQNKYVGIGN DSRDFGYGGG SYGGGGYDSD
SYGSNQRDSY GGNQRDSYGG NQRDSYGGNQ RETTRRDSFN GRDEGYGNNN NNNNNNSYDS
DPYSNTRAEY ENYSNRAETR RNNEFGDDSN NSYNNNNNFN NNNNNNNSYN NSNNSNNSNN
NNNNNNYNNS NNNSNNIQNN PNAASGGRSR PRAASGSGPS PATPNFQSSQ QQQQPTLIDF
SEPTPANKPM VFDPLADLAS GMNNTNNNNN NNNNNSNSFG GFQSVNNNQN SFNFNNNNQQ
QQQQNNFLQL TQSNPQQSNN NNNNNNFFNQ QPQQAQQFGQ FQNSSMNKDP FAKDEFGDFA
GANGNADFNP FDQQSGDFSN KNDGQQKPKD TNDPWSKKDL FDLSNLGNQN PNQSPVNNTN
NNNNGNTRSQ PARVANGPIT SAGSTIPTMR PQPMMNQGFN GGMMNQGMGG FNQGGGMNNM
NGMNQGGMNN MNGMNQGGMN QGGMGGFNQG GMNNMGGMNQ GGMNNMGGMN NMGGMNSMNG
MNQGGMGFNQ SGANRNTNSM GSAGRF
