EPN3_MOUSE
ID EPN3_MOUSE Reviewed; 636 AA.
AC Q91W69; Q9CV55;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Epsin-3;
DE AltName: Full=EPS-15-interacting protein 3;
GN Name=Epn3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-636.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-185 AND SER-257, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250}. Note=Concentrated in the perinuclear region and
CC associated with clathrin-coated vesicles close to the cell periphery.
CC May shuttle to the nucleus (By similarity). {ECO:0000250}.
CC -!- INDUCTION: In keratinocytes, by wounding or contact with collagen.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
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DR EMBL; BC016454; AAH16454.1; -; mRNA.
DR EMBL; AK009469; BAB26309.1; -; mRNA.
DR CCDS; CCDS25257.1; -.
DR RefSeq; NP_082260.1; NM_027984.3.
DR RefSeq; XP_006534329.1; XM_006534266.3.
DR AlphaFoldDB; Q91W69; -.
DR SMR; Q91W69; -.
DR BioGRID; 215009; 1.
DR DIP; DIP-59492N; -.
DR IntAct; Q91W69; 3.
DR STRING; 10090.ENSMUSP00000121390; -.
DR iPTMnet; Q91W69; -.
DR PhosphoSitePlus; Q91W69; -.
DR MaxQB; Q91W69; -.
DR PaxDb; Q91W69; -.
DR PRIDE; Q91W69; -.
DR ProteomicsDB; 275636; -.
DR Antibodypedia; 30580; 140 antibodies from 27 providers.
DR DNASU; 71889; -.
DR Ensembl; ENSMUST00000127305; ENSMUSP00000121390; ENSMUSG00000010080.
DR GeneID; 71889; -.
DR KEGG; mmu:71889; -.
DR UCSC; uc007kyu.2; mouse.
DR CTD; 55040; -.
DR MGI; MGI:1919139; Epn3.
DR VEuPathDB; HostDB:ENSMUSG00000010080; -.
DR eggNOG; KOG2056; Eukaryota.
DR GeneTree; ENSGT00940000158217; -.
DR HOGENOM; CLU_012678_4_2_1; -.
DR InParanoid; Q91W69; -.
DR OMA; DPWGASL; -.
DR OrthoDB; 1263849at2759; -.
DR PhylomeDB; Q91W69; -.
DR TreeFam; TF313361; -.
DR BioGRID-ORCS; 71889; 4 hits in 79 CRISPR screens.
DR ChiTaRS; Epn3; mouse.
DR PRO; PR:Q91W69; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91W69; protein.
DR Bgee; ENSMUSG00000010080; Expressed in lip and 60 other tissues.
DR Genevisible; Q91W69; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:1990175; F:EH domain binding; IDA:MGI.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR027318; Epsin-3_metazoa.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR12276:SF16; PTHR12276:SF16; 1.
DR Pfam; PF01417; ENTH; 1.
DR Pfam; PF02809; UIM; 2.
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; Cytoplasmic vesicle; Lipid-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..636
FT /note="Epsin-3"
FT /id="PRO_0000074520"
FT DOMAIN 12..144
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 202..221
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 229..248
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REPEAT 315..317
FT /note="1"
FT REPEAT 338..340
FT /note="2"
FT REPEAT 365..367
FT /note="3"
FT REPEAT 381..383
FT /note="4"
FT REPEAT 398..400
FT /note="5"
FT REPEAT 523..525
FT /note="1"
FT REPEAT 536..538
FT /note="2"
FT REPEAT 633..635
FT /note="3"
FT REGION 153..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..400
FT /note="5 X 3 AA repeats of [DE]-P-W"
FT REGION 523..635
FT /note="3 X 3 AA repeats of N-P-F"
FT REGION 607..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 82
FT /note="D -> G (in Ref. 2; BAB26309)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="P -> S (in Ref. 2; BAB26309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 68240 MW; BD18518618FA7A72 CRC64;
MTTSALRRQV KNIVHNYSEA EIKVREATSN DPWGPPSSLM SEIADLTFNT VAFAEVMGMV
WRRLNDSGKN WRHVYKALTL LDYLLKTGSE RVAHQCRENL YTIQTLKDFQ YIDRDGKDQG
VNVREKVKQV MALLKDEERL RQERTHALKT KERMALEGMG IGSGQLGYSR RSRGSPSSYT
SASSSPRYAS DLEQARPQTS GEEELQLQLA LAMSREEAER PVPPASHRDE DLQLQLALSL
SRQEHEKGVR SWKGDDSPVA NGAEPAGQRR QRDREPEREE RKEEEKLKTS QSSILDLADI
FAPAPALPST HCSADPWDIP GLRPNTEPSG SSWGPSADPW SPVPSGNALS RSQPWDLLPT
LSSSEPWGRT PVLPSGPPIA DPWAPSSPTR KLPSTGADPW GASMETSDTS ALGGASPFDP
FAKPLESTEP KESRDSAQAL PTGKSPSTVE LDPFGDSSPS CKQNGMKEPE ALDLGVLGEA
LPQQPGKEAR PCRTPESFLG PSASSLVNLD SLVKAPLAAR TRNPFLTGLG VPSPTNPFGA
GDQGRPTLNQ MRTGSPALGL PPGGPVGAPV GSMTYSASLP LPLSSVPVGA TLPASVSVFP
QAGAFAPPPA SLPQPLLPTS GPMGPLPPQA GTNPFL
