EPN2_RAT
ID EPN2_RAT Reviewed; 583 AA.
AC Q9Z1Z3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Epsin-2;
DE AltName: Full=EPS-15-interacting protein 2;
GN Name=Epn2;
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 [MRNA], FUNCTION, INTERACTION WITH EPS15, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10567358; DOI=10.1074/jbc.274.48.33959;
RA Rosenthal J.A., Chen H., Slepnev V.I., Pellegrini L., Salcini A.E.,
RA Di Fiore P.P., De Camilli P.;
RT "The epsins define a family of proteins that interact with components of
RT the clathrin coat and contain a new protein module.";
RL J. Biol. Chem. 274:33959-33965(1999).
RN [2]
RP UBIQUITINATION.
RX PubMed=11919637; DOI=10.1038/416451a;
RA Polo S., Sigismund S., Faretta M., Guidi M., Capua M.R., Bossi G., Chen H.,
RA De Camilli P., Di Fiore P.P.;
RT "A single motif responsible for ubiquitin recognition and
RT monoubiquitination in endocytic proteins.";
RL Nature 416:451-455(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-195; SER-431 AND
RP THR-453, AND 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 -!- FUNCTION: Plays a role in the formation of clathrin-coated
CC invaginations and endocytosis. {ECO:0000269|PubMed:10567358}.
CC -!- SUBUNIT: Binds AP-2 and clathrin (By similarity). Interacts with ITSN1
CC (By similarity). Interacts with UBQLN2 (By similarity). Binds EPS15.
CC {ECO:0000250|UniProtKB:O95208, ECO:0000250|UniProtKB:Q8CHU3,
CC ECO:0000269|PubMed:10567358}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=In punctate
CC structures throughout the cell and particularly concentrated in the
CC region of the Golgi complex. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Detected at lower levels
CC in lung, liver, muscle and testis. {ECO:0000269|PubMed:10567358}.
CC -!- DOMAIN: The NPF repeat domain is involved in EPS15 binding.
CC -!- DOMAIN: The DPW repeat domain is involved in AP-2 and clathrin binding.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:11919637}.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
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DR EMBL; AF096269; AAC79495.1; -; mRNA.
DR AlphaFoldDB; Q9Z1Z3; -.
DR SMR; Q9Z1Z3; -.
DR BioGRID; 248836; 2.
DR STRING; 10116.ENSRNOP00000039386; -.
DR iPTMnet; Q9Z1Z3; -.
DR jPOST; Q9Z1Z3; -.
DR PRIDE; Q9Z1Z3; -.
DR UCSC; RGD:619773; rat.
DR RGD; 619773; Epn2.
DR InParanoid; Q9Z1Z3; -.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q9Z1Z3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030128; C:clathrin coat of endocytic vesicle; IDA:RGD.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0048568; P:embryonic organ development; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:RGD.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0030100; P:regulation of endocytosis; IDA:RGD.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR027319; Epsin-2_metazoa.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR12276:SF50; PTHR12276:SF50; 1.
DR Pfam; PF01417; ENTH; 1.
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; Endocytosis; Lipid-binding; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..583
FT /note="Epsin-2"
FT /id="PRO_0000074518"
FT DOMAIN 12..144
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 218..237
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 243..262
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REPEAT 301..303
FT /note="1"
FT REPEAT 313..315
FT /note="2"
FT REPEAT 326..328
FT /note="3"
FT REPEAT 340..342
FT /note="4"
FT REPEAT 358..360
FT /note="5"
FT REPEAT 375..377
FT /note="6"
FT REPEAT 482..484
FT /note="1"
FT REPEAT 496..498
FT /note="2"
FT REPEAT 579..581
FT /note="3"
FT REGION 165..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..377
FT /note="6 X 3 AA repeats of [DE]-P-W"
FT REGION 411..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..581
FT /note="3 X 3 AA repeats of N-P-F"
FT COMPBIAS 165..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..455
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 170
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHU3"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95208"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 453
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95208"
SQ SEQUENCE 583 AA; 62349 MW; 2C2982B72C8FDC79 CRC64;
MTTSSIRRQM KNIVNSYSEA EIKVREATSN DPWGPSSSLM TEIADLTYNV VRFSEIMSMV
WKRLNDHGKN WRHVYKALTL LDYLIKTGSE RVAQQCRENI FAIQTLKDFQ YIDRDGKDQG
INVREKSKQL VALLKDEERL KVERVQALKT KERMAQVATG VGSNQITFGR GSSQPNLSIS
HSEQEYGKAG GSPASYHGST SPRVSSELEQ ARPQTSGEEE LQLQLALAMS REVAEQEERL
RRGDDLRLQM ALEESRRDTV KVPKKKEVKA CCKPGSHSQQ TTLLDLMDAL PSSGPVAQKT
EPWSTGTPAN QTNPWGGTVA PANISDPWPS FGTKPAASVD PWGVPTTASI QSVPKNSDPW
AASQQPASDA GKTADAWGAA KPSPASGSFE LFSNFNGTVK DDFSEFDNLR TSKKPAESGA
SVPPQDSRTT SPDLFESQSL TSASSKPSSA RKTPESFLGP NAALVNLDSL VTKPAPPAQS
LNPFLAPGAA APAPVNPFQV NQPQPLTLNQ LRGSPVLGSS ASFGSGPGVE TVAPMPSVAP
HSALGATGSS LTPLGPTAMN MVGSMGIPPS AAQPAGTTNP FLL
