EPN3_HUMAN
ID EPN3_HUMAN Reviewed; 632 AA.
AC Q9H201; A8K6J3; A8KAB2; Q9BVN6; Q9NWK2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Epsin-3;
DE AltName: Full=EPS-15-interacting protein 3;
GN Name=EPN3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Keratinocyte;
RX PubMed=11359770; DOI=10.1074/jbc.m101663200;
RA Spradling K.D., McDaniel A.E., Lohi J., Pilcher B.K.;
RT "Epsin 3 is a novel extracellular matrix-induced transcript specific to
RT wounded epithelia.";
RL J. Biol. Chem. 276:29257-29267(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-544.
RC TISSUE=Colon, Placenta, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11359770}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:11359770}.
CC Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:11359770}. Nucleus {ECO:0000305|PubMed:11359770}.
CC Note=Concentrated in the perinuclear region and associated with
CC clathrin-coated vesicles close to the cell periphery. May shuttle to
CC the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H201-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H201-2; Sequence=VSP_009158, VSP_009159;
CC -!- TISSUE SPECIFICITY: Detected in migrating keratinocytes from wounded
CC skin, but not in differentiating keratinocytes or in normal skin.
CC Detected in chronic wounds, basal cell carcinoma and ulcerative
CC colitis. {ECO:0000269|PubMed:11359770}.
CC -!- INDUCTION: In keratinocytes, by wounding or contact with collagen.
CC {ECO:0000269|PubMed:11359770}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
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DR EMBL; AF324241; AAG45223.1; -; mRNA.
DR EMBL; AK000785; BAA91378.1; -; mRNA.
DR EMBL; AK291658; BAF84347.1; -; mRNA.
DR EMBL; AK292977; BAF85666.1; -; mRNA.
DR EMBL; CH471109; EAW94607.1; -; Genomic_DNA.
DR EMBL; BC001038; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC051365; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC077722; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS11570.1; -. [Q9H201-1]
DR RefSeq; NP_060427.2; NM_017957.2. [Q9H201-1]
DR AlphaFoldDB; Q9H201; -.
DR SMR; Q9H201; -.
DR BioGRID; 120369; 54.
DR ELM; Q9H201; -.
DR IntAct; Q9H201; 27.
DR MINT; Q9H201; -.
DR STRING; 9606.ENSP00000268933; -.
DR iPTMnet; Q9H201; -.
DR PhosphoSitePlus; Q9H201; -.
DR BioMuta; EPN3; -.
DR DMDM; 41017054; -.
DR EPD; Q9H201; -.
DR jPOST; Q9H201; -.
DR MassIVE; Q9H201; -.
DR MaxQB; Q9H201; -.
DR PaxDb; Q9H201; -.
DR PeptideAtlas; Q9H201; -.
DR PRIDE; Q9H201; -.
DR ProteomicsDB; 80463; -. [Q9H201-1]
DR ProteomicsDB; 80464; -. [Q9H201-2]
DR Antibodypedia; 30580; 140 antibodies from 27 providers.
DR DNASU; 55040; -.
DR Ensembl; ENST00000268933.8; ENSP00000268933.3; ENSG00000049283.19. [Q9H201-1]
DR Ensembl; ENST00000510045.5; ENSP00000421933.1; ENSG00000049283.19. [Q9H201-2]
DR GeneID; 55040; -.
DR KEGG; hsa:55040; -.
DR MANE-Select; ENST00000268933.8; ENSP00000268933.3; NM_017957.3; NP_060427.2.
DR UCSC; uc002ira.5; human. [Q9H201-1]
DR CTD; 55040; -.
DR DisGeNET; 55040; -.
DR GeneCards; EPN3; -.
DR HGNC; HGNC:18235; EPN3.
DR HPA; ENSG00000049283; Tissue enhanced (esophagus, stomach).
DR MIM; 607264; gene.
DR neXtProt; NX_Q9H201; -.
DR OpenTargets; ENSG00000049283; -.
DR PharmGKB; PA38513; -.
DR VEuPathDB; HostDB:ENSG00000049283; -.
DR eggNOG; KOG2056; Eukaryota.
DR GeneTree; ENSGT00940000158217; -.
DR HOGENOM; CLU_012678_4_2_1; -.
DR InParanoid; Q9H201; -.
DR OMA; DPWGASL; -.
DR OrthoDB; 1263849at2759; -.
DR PhylomeDB; Q9H201; -.
DR TreeFam; TF313361; -.
DR PathwayCommons; Q9H201; -.
DR SignaLink; Q9H201; -.
DR BioGRID-ORCS; 55040; 303 hits in 1073 CRISPR screens.
DR GenomeRNAi; 55040; -.
DR Pharos; Q9H201; Tbio.
DR PRO; PR:Q9H201; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9H201; protein.
DR Bgee; ENSG00000049283; Expressed in lower esophagus mucosa and 93 other tissues.
DR ExpressionAtlas; Q9H201; baseline and differential.
DR Genevisible; Q9H201; HS.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
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; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Lipid-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..632
FT /note="Epsin-3"
FT /id="PRO_0000074519"
FT DOMAIN 12..144
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 209..228
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 236..255
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REPEAT 321..323
FT /note="1"
FT REPEAT 344..346
FT /note="2"
FT REPEAT 371..373
FT /note="3"
FT REPEAT 387..389
FT /note="4"
FT REPEAT 404..406
FT /note="5"
FT REPEAT 524..526
FT /note="1"
FT REPEAT 537..539
FT /note="2"
FT REPEAT 629..631
FT /note="3"
FT REGION 172..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..406
FT /note="5 X 3 AA repeats of [DE]-P-W"
FT REGION 326..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..631
FT /note="3 X 3 AA repeats of N-P-F"
FT REGION 525..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..632
FT /note="Pro 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 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91W69"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91W69"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91W69"
FT VAR_SEQ 188..208
FT /note="SSSSSPRYTSDLEQARPQTSG -> CPASDVRGRGTAAAAGPRHEP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009158"
FT VAR_SEQ 209..632
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009159"
FT VARIANT 544
FT /note="P -> T (in dbSNP:rs4794159)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_059973"
FT CONFLICT 375
FT /note="R -> K (in Ref. 2; BAF85666)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="H -> Y (in Ref. 2; BAA91378)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="G -> S (in Ref. 2; BAF85666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 68222 MW; 13940F2FBD6215D0 CRC64;
MTTSALRRQV KNIVHNYSEA EIKVREATSN DPWGPPSSLM SEIADLTFNT VAFTEVMGML
WRRLNDSGKN WRHVYKALTL LDYLLKTGSE RVAHQCRENL YTIQTLKDFQ YIDRDGKDQG
VNVREKVKQV MALLKDEERL RQERTHALKT KERMALEGIG IGSGQLGFSR RYGEDYSRSR
GSPSSYNSSS SSPRYTSDLE QARPQTSGEE ELQLQLALAM SREEAEKPVP PASHRDEDLQ
LQLALRLSRQ EHEKEVRSWQ GDGSPMANGA GAVVHHQRDR EPEREERKEE EKLKTSQSSI
LDLADIFVPA LAPPSTHCSA DPWDIPGFRP NTEASGSSWG PSADPWSPIP SGTVLSRSQP
WDLTPMLSSS EPWGRTPVLP AGPPTTDPWA LNSPHHKLPS TGADPWGASL ETSDTPGGAS
TFDPFAKPPE STETKEGLEQ ALPSGKPSSP VELDLFGDPS PSSKQNGTKE PDALDLGILG
EALTQPSKEA RACRTPESFL GPSASSLVNL DSLVKAPQVA KTRNPFLTGL SAPSPTNPFG
AGEPGRPTLN QMRTGSPALG LAGGPVGAPL GSMTYSASLP LPLSSVPAGL TLPASVSVFP
QAGAFAPQPL LPTPSSAGPR PPPPQTGTNP FL
