EPN3_RAT
ID EPN3_RAT Reviewed; 608 AA.
AC Q4V882;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Epsin-3;
DE AltName: Full=EPS-15-interacting protein 3;
GN Name=Epn3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250}. Nucleus {ECO:0000250}. Note=Concentrated in the
CC perinuclear region and associated with clathrin-coated vesicles close
CC to the cell periphery. May shuttle to the nucleus (By similarity).
CC {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; BC097500; AAH97500.1; -; mRNA.
DR RefSeq; NP_001019962.1; NM_001024791.1.
DR RefSeq; XP_006247265.1; XM_006247203.3.
DR AlphaFoldDB; Q4V882; -.
DR SMR; Q4V882; -.
DR STRING; 10116.ENSRNOP00000004400; -.
DR iPTMnet; Q4V882; -.
DR PhosphoSitePlus; Q4V882; -.
DR jPOST; Q4V882; -.
DR PaxDb; Q4V882; -.
DR PRIDE; Q4V882; -.
DR Ensembl; ENSRNOT00000004400; ENSRNOP00000004400; ENSRNOG00000003284.
DR GeneID; 360605; -.
DR KEGG; rno:360605; -.
DR CTD; 55040; -.
DR RGD; 1306416; Epn3.
DR eggNOG; KOG2056; Eukaryota.
DR GeneTree; ENSGT00940000158217; -.
DR HOGENOM; CLU_012678_4_2_1; -.
DR InParanoid; Q4V882; -.
DR OMA; DPWGASL; -.
DR OrthoDB; 1263849at2759; -.
DR PRO; PR:Q4V882; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003284; Expressed in esophagus and 14 other tissues.
DR Genevisible; Q4V882; RN.
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; ISO:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
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; ISO:RGD.
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 SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50330; UIM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Lipid-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..608
FT /note="Epsin-3"
FT /id="PRO_0000312178"
FT DOMAIN 12..144
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 202..221
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REPEAT 287..289
FT /note="1"
FT REPEAT 310..312
FT /note="2"
FT REPEAT 337..339
FT /note="3"
FT REPEAT 353..355
FT /note="4"
FT REPEAT 370..372
FT /note="5"
FT REPEAT 495..497
FT /note="1"
FT REPEAT 508..510
FT /note="2"
FT REPEAT 605..607
FT /note="3"
FT REGION 150..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..372
FT /note="5 X 3 AA repeats of [DE]-P-W"
FT REGION 495..607
FT /note="3 X 3 AA repeats of N-P-F"
FT REGION 498..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..608
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 239..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..608
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 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91W69"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91W69"
SQ SEQUENCE 608 AA; 65048 MW; 396354172B39C504 CRC64;
MTTSALRRQV KNIVHNYSEA EIKVREATSN DPWGPPSSLM SEIADLTFNT VAFAEVMGMV
WRRLNDSGKN WRHVYKALTL LDYLLKTGSE RVAHQCRENL YTIQTLKDFQ YIDRDGKDQG
VNVREKVKQV MALLKDEERL RQERTHALKT KERMALEGMG IGSGQLGFSR RSRGSPSSYT
SASSSPRYAS DLEQARPQTS GEEELQLQLA LAMSREEAEK GGRSWKGDDF PVANGAEPAG
QRRRDREPER EERKEEEKLK TSQSSILDLA DVFAPAPALP STHCSADPWD IPGLRPNTEP
SGSSWGPSAD PWSPVPSGNA LSRSQPWDLL PTLSSSEPWG RTPVLPSGPP ITDPWAPSSP
TPKLPSTGVD PWGASVETSN TSALGGASPF DPFAKPLEST EPMESRDSAQ ALPKGKSPSP
VELDPFGDSS PSCKQNGVKE TEALDLGVLG EALTQQPGKE ARPCRTPESF LGPSASSLVN
LDSLVKAPLA ARTRNPFLTG LSAPSPTNPF GAGEQGRPTL NQMRTGSPAL GLPPGGPVGV
PLGSMTYSAS LPLPLSSVPV GATLPASVSV FPQAGAFAPP PASLPQPLLP TSDPVGPLPP
QAGTNPFL
