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 01-MAY-2013, entry version 103.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY,
RP AND 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
RT to wounded epithelia.";
RL J. Biol. Chem. 276:29257-29267(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC Cytoplasmic vesicle, clathrin-coated vesicle. Nucleus (Probable).
CC Note=Concentrated in the perinuclear region and associated with
CC clathrin-coated vesicles close to the cell periphery. May shuttle
CC to 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 Note=No experimental confirmation available. May be produced at
CC very low levels due to a premature stop codon in the mRNA,
CC leading to nonsense-mediated mRNA decay;
CC -!- TISSUE SPECIFICITY: Detected in migrating keratinocytes from
CC wounded skin, but not in differentiating keratinocytes or in
CC normal skin. Detected in chronic wounds, basal cell carcinoma and
CC ulcerative colitis.
CC -!- INDUCTION: In keratinocytes, by wounding or contact with collagen.
CC -!- SIMILARITY: Belongs to the epsin family.
CC -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC -!- SIMILARITY: Contains 2 UIM (ubiquitin-interacting motif) repeats.
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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 IPI; IPI00300584; -.
DR IPI; IPI00386833; -.
DR RefSeq; NP_060427.2; NM_017957.2.
DR UniGene; Hs.670090; -.
DR ProteinModelPortal; Q9H201; -.
DR MINT; MINT-1199053; -.
DR STRING; 9606.ENSP00000268933; -.
DR PhosphoSite; Q9H201; -.
DR DMDM; 41017054; -.
DR PaxDb; Q9H201; -.
DR PRIDE; Q9H201; -.
DR Ensembl; ENST00000268933; ENSP00000268933; ENSG00000049283.
DR Ensembl; ENST00000510045; ENSP00000421933; ENSG00000049283.
DR GeneID; 55040; -.
DR KEGG; hsa:55040; -.
DR UCSC; uc002ira.4; human.
DR CTD; 55040; -.
DR GeneCards; GC17P048610; -.
DR HGNC; HGNC:18235; EPN3.
DR HPA; HPA055546; -.
DR MIM; 607264; gene.
DR neXtProt; NX_Q9H201; -.
DR PharmGKB; PA38513; -.
DR eggNOG; NOG263730; -.
DR HOGENOM; HOG000008298; -.
DR HOVERGEN; HBG006690; -.
DR InParanoid; Q9H201; -.
DR KO; K12471; -.
DR OrthoDB; EOG4SF97B; -.
DR PhylomeDB; Q9H201; -.
DR GenomeRNAi; 55040; -.
DR NextBio; 58495; -.
DR ArrayExpress; Q9H201; -.
DR Bgee; Q9H201; -.
DR CleanEx; HS_EPN3; -.
DR Genevestigator; Q9H201; -.
DR GermOnline; ENSG00000049283; Homo sapiens.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR027318; Epsin-3_metazoa.
DR InterPro; IPR013809; Epsin-like_N.
DR InterPro; IPR001026; Epsin_dom_N.
DR InterPro; IPR003903; Ubiquitin-int_motif.
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; ENTH_VHS; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50330; UIM; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Lipid-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 632 Epsin-3.
FT /FTId=PRO_0000074519.
FT DOMAIN 12 144 ENTH.
FT REPEAT 209 228 UIM 1.
FT REPEAT 236 255 UIM 2.
FT REPEAT 321 323 1.
FT REPEAT 344 346 2.
FT REPEAT 371 373 3.
FT REPEAT 387 389 4.
FT REPEAT 404 406 5.
FT REPEAT 524 526 1.
FT REPEAT 537 539 2.
FT REPEAT 629 631 3.
FT REGION 321 406 5 X 3 AA repeats of [DE]-P-W.
FT REGION 524 631 3 X 3 AA repeats of N-P-F.
FT BINDING 8 8 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 11 11 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 25 25 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 30 30 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 63 63 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT BINDING 73 73 Phosphatidylinositol lipid headgroup (By
FT similarity).
FT MOD_RES 182 182 Phosphoserine (By similarity).
FT MOD_RES 393 393 Phosphoserine (By similarity).
FT VAR_SEQ 188 208 SSSSSPRYTSDLEQARPQTSG -> CPASDVRGRGTAAAAG
FT PRHEP (in isoform 2).
FT /FTId=VSP_009158.
FT VAR_SEQ 209 632 Missing (in isoform 2).
FT /FTId=VSP_009159.
FT VARIANT 544 544 P -> T (in dbSNP:rs4794159).
FT /FTId=VAR_059973.
FT CONFLICT 375 375 R -> K (in Ref. 2; BAF85666).
FT CONFLICT 396 396 H -> Y (in Ref. 2; BAA91378).
FT CONFLICT 417 417 G -> S (in Ref. 2; BAF85666).
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
//
