ID EPN1_RAT Reviewed; 575 AA. AC O88339; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 185. DE RecName: Full=Epsin-1; DE AltName: Full=EPS-15-interacting protein 1; GN Name=Epn1; 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, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND INTERACTION WITH EPS15; AP2A1 AND AP2A2. RC STRAIN=Wistar; TISSUE=Brain; RX PubMed=9723620; DOI=10.1038/29555; RA Chen H., Fre S., Slepnev V.I., Capua M.R., Takei K., Butler M.H., RA Di Fiore P.P., De Camilli P.; RT "Epsin is an EH-domain-binding protein implicated in clathrin-mediated RT endocytosis."; RL Nature 394:793-797(1998). RN [2] RP TISSUE SPECIFICITY. RX PubMed=10393179; DOI=10.1093/emboj/18.13.3629; RA Nakashima S., Morinaka K., Koyama S., Ikeda M., Kishida M., Okawa K., RA Iwamatsu A., Kishida S., Kikuchi A.; RT "Small G protein Ral and its downstream molecules regulate endocytosis of RT EGF and insulin receptors."; RL EMBO J. 18:3629-3642(1999). RN [3] RP INTERACTION WITH AP2A2. RX PubMed=10380931; DOI=10.1016/s0092-8674(00)80791-6; RA Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R., Evans P.R., RA McMahon H.T.; RT "A structural explanation for the binding of multiple ligands by the alpha- RT adaptin appendage domain."; RL Cell 97:805-815(1999). RN [4] RP PHOSPHORYLATION, AND INTERACTION WITH AP-2. RX PubMed=9920862; DOI=10.1074/jbc.274.6.3257; RA Chen H., Slepnev V.I., Di Fiore P.P., De Camilli P.; RT "The interaction of epsin and Eps15 with the clathrin adaptor AP-2 is RT inhibited by mitotic phosphorylation and enhanced by stimulation-dependent RT dephosphorylation in nerve terminals."; RL J. Biol. Chem. 274:3257-3260(1999). RN [5] RP INTERACTION WITH AP2A2. RX PubMed=10430869; DOI=10.1073/pnas.96.16.8907; RA Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.; RT "Crystal structure of the alpha appendage of AP-2 reveals a recruitment RT platform for clathrin-coat assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999). RN [6] RP INTERACTION WITH AP2B1. RX PubMed=10944104; DOI=10.1093/emboj/19.16.4216; RA Owen D.J., Vallis Y., Pearse B.M.F., McMahon H.T., Evans P.R.; RT "The structure and function of the beta 2-adaptin appendage domain."; RL EMBO J. 19:4216-4227(2000). RN [7] RP MUTAGENESIS OF 257-LEU--ASP-259 AND 260-LEU--VAL-263, SUBCELLULAR LOCATION, RP AND INTERACTION WITH CLATHRIN HEAVY CHAIN AND AP-2. RX PubMed=10692452; DOI=10.1074/jbc.275.9.6479; RA Drake M.T., Downs M.A., Traub L.M.; RT "Epsin binds to clathrin by associating directly with the clathrin-terminal RT domain. Evidence for cooperative binding through two discrete sites."; RL J. Biol. Chem. 275:6479-6489(2000). RN [8] RP FUNCTION, INTERACTION WITH ZBTB16, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP ARG-8; ARG-63; ARG-72 AND LYS-76. RX PubMed=11161217; DOI=10.1126/science.291.5506.1047; RA Itoh T., Koshiba S., Kigawa T., Kikuchi A., Yokoyama S., Takenawa T.; RT "Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding RT and endocytosis."; RL Science 291:1047-1051(2001). RN [9] RP MUTAGENESIS OF LEU-190, AND 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND THR-469, AND 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). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-160, SUBCELLULAR LOCATION, AND RP INTERACTION WITH ZNF145. RX PubMed=10791968; DOI=10.1083/jcb.149.3.537; RA Hyman J., Chen H., Di Fiore P.P., De Camilli P., Brunger A.T.; RT "Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor RT NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo RT and Heat repeats, interacts with the transcription factor promyelocytic RT leukemia Zn(2)+ finger protein (PLZF)."; RL J. Cell Biol. 149:537-546(2000). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-158 IN COMPLEX WITH RP INOSITOL-1,4,5-TRIPHOSPHATE, FUNCTION, AND MUTAGENESIS OF LEU-6; ARG-63 AND RP HIS-73. RX PubMed=12353027; DOI=10.1038/nature01020; RA Ford M.G.J., Mills I.G., Peter B.J., Vallis Y., Praefcke G.J.K., RA Evans P.R., McMahon H.T.; RT "Curvature of clathrin-coated pits driven by epsin."; RL Nature 419:361-366(2002). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 375-381 IN COMPLEX WITH AP2A2. RX PubMed=12057195; DOI=10.1016/s0969-2126(02)00784-0; RA Brett T.J., Traub L.M., Fremont D.H.; RT "Accessory protein recruitment motifs in clathrin-mediated endocytosis."; RL Structure 10:797-809(2002). CC -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5- CC bisphosphate (PtdIns(4,5)P2) (PubMed:11161217). Modifies membrane CC curvature and facilitates the formation of clathrin-coated CC invaginations (PubMed:9723620, PubMed:12353027). Regulates receptor- CC mediated endocytosis (By similarity). {ECO:0000250|UniProtKB:Q9Y6I3, CC ECO:0000269|PubMed:11161217, ECO:0000269|PubMed:12353027, CC ECO:0000269|PubMed:9723620}. CC -!- SUBUNIT: Monomer. Binds ITSN1 (By similarity). Binds clathrin, CC ZBTB16/ZNF145, AP2A1 and AP2A2. Binds ubiquitinated proteins. Interacts CC with RALBP1 in a complex also containing NUMB and TFAP2A during CC interphase and mitosis. Interacts with AP2B1. Interacts with UBQLN2 (By CC similarity). Interacts with REPS2; the interaction is direct (By CC similarity). Interacts with EPS15; the interaction is direct (By CC similarity). Interacts with ENTREP1 (By similarity). CC {ECO:0000250|UniProtKB:Q80VP1, ECO:0000250|UniProtKB:Q9Y6I3, CC ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:10430869, CC ECO:0000269|PubMed:10692452, ECO:0000269|PubMed:10791968, CC ECO:0000269|PubMed:10944104, ECO:0000269|PubMed:11161217, CC ECO:0000269|PubMed:12057195, ECO:0000269|PubMed:12353027, CC ECO:0000269|PubMed:9723620, ECO:0000269|PubMed:9920862}. CC -!- INTERACTION: CC O88339; P39083: RGA1; Xeno; NbExp=2; IntAct=EBI-7066728, EBI-15044; CC O88339; Q06407: RGA2; Xeno; NbExp=2; IntAct=EBI-7066728, EBI-15060; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane CC protein. Nucleus. Membrane, clathrin-coated pit. Note=Associated with CC the cytoplasmic membrane at sites where clathrin-coated pits are CC forming. Colocalizes with clathrin and AP-2 in a punctate pattern on CC the plasma membrane. Colocalizes with clathrin at the Golgi complex. CC Detected in presynaptic nerve terminals and in synaptosomes. May CC shuttle to the nucleus when associated with ZBTB16/ZNF145. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:9723620). Detected CC in liver, spleen and testis, and weakly in lung and thymus (at protein CC level) (PubMed:10393179). {ECO:0000269|PubMed:10393179, CC ECO:0000269|PubMed:9723620}. CC -!- DOMAIN: The NPF repeat domain is involved in EPS15 binding. CC -!- DOMAIN: The DPW repeat domain is involved in AP2A2 and clathrin CC binding. CC -!- DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction CC the AP-2 complex subunit AP2B1. {ECO:0000250}. CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:11919637}. CC -!- PTM: Phosphorylated on serine and/or threonine residues in mitotic CC cells. Phosphorylation reduces interaction with REPS2, AP-2 and the CC membrane fraction. Depolarization of synaptosomes results in CC dephosphorylation. {ECO:0000269|PubMed:9920862}. CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The bubble's bend - Issue 42 CC of January 2004; CC URL="https://web.expasy.org/spotlight/back_issues/042"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF018261; AAC33823.1; -; mRNA. DR RefSeq; NP_476477.1; NM_057136.1. DR PDB; 1EDU; X-ray; 1.80 A; A=12-160. DR PDB; 1EYH; X-ray; 1.56 A; A=15-158. DR PDB; 1H0A; X-ray; 1.70 A; A=1-158. DR PDB; 1KY6; X-ray; 2.00 A; P=375-381. DR PDBsum; 1EDU; -. DR PDBsum; 1EYH; -. DR PDBsum; 1H0A; -. DR PDBsum; 1KY6; -. DR AlphaFoldDB; O88339; -. DR BMRB; O88339; -. DR SMR; O88339; -. DR BioGRID; 250724; 16. DR CORUM; O88339; -. DR DIP; DIP-40738N; -. DR ELM; O88339; -. DR IntAct; O88339; 5. DR MINT; O88339; -. DR STRING; 10116.ENSRNOP00000021286; -. DR iPTMnet; O88339; -. DR PhosphoSitePlus; O88339; -. DR jPOST; O88339; -. DR PaxDb; 10116-ENSRNOP00000021286; -. DR PeptideAtlas; O88339; -. DR GeneID; 117277; -. DR KEGG; rno:117277; -. DR UCSC; RGD:619772; rat. DR AGR; RGD:619772; -. DR CTD; 29924; -. DR RGD; 619772; Epn1. DR eggNOG; KOG2056; Eukaryota. DR HOGENOM; CLU_012678_4_2_1; -. DR InParanoid; O88339; -. DR OrthoDB; 1532at2759; -. DR PhylomeDB; O88339; -. DR Reactome; R-RNO-182971; EGFR downregulation. DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis. DR EvolutionaryTrace; O88339; -. DR PRO; PR:O88339; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central. DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:CAFA. DR GO; GO:0005768; C:endosome; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0098794; C:postsynapse; IDA:SynGO. DR GO; GO:0045211; C:postsynaptic membrane; IDA:BHF-UCL. DR GO; GO:0098793; C:presynapse; IDA:SynGO. DR GO; GO:0042734; C:presynaptic membrane; IDA:BHF-UCL. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO. DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL. DR GO; GO:0035615; F:clathrin adaptor activity; IMP:CAFA. DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central. DR GO; GO:0140313; F:molecular sequestering activity; ISO:RGD. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD. DR GO; GO:0048268; P:clathrin coat assembly; IDA:DisProt. DR GO; GO:0048568; P:embryonic organ development; ISO:RGD. DR GO; GO:0006897; P:endocytosis; IDA:RGD. DR GO; GO:0007565; P:female pregnancy; ISO:RGD. DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD. DR GO; GO:0090148; P:membrane fission; IDA:CACAO. DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:RGD. DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD. DR GO; GO:1905445; P:positive regulation of clathrin coat assembly; IMP:CAFA. DR CDD; cd16990; ENTH_Epsin; 1. DR DisProt; DP00251; -. DR Gene3D; 1.25.40.90; -; 1. DR InterPro; IPR013809; ENTH. DR InterPro; IPR008942; ENTH_VHS. DR InterPro; IPR003903; UIM_dom. DR PANTHER; PTHR12276:SF48; EPSIN-1; 1. DR PANTHER; PTHR12276; EPSIN/ENT-RELATED; 1. DR Pfam; PF01417; ENTH; 1. DR SMART; SM00273; ENTH; 1. DR SMART; SM00726; UIM; 3. DR SUPFAM; SSF48464; ENTH/VHS domain; 1. DR PROSITE; PS50942; ENTH; 1. DR PROSITE; PS50330; UIM; 3. DR Genevisible; O88339; RN. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Coated pit; Cytoplasm; Endocytosis; KW Lipid-binding; Membrane; Methylation; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Ubl conjugation. FT CHAIN 1..575 FT /note="Epsin-1" FT /id="PRO_0000074515" FT DOMAIN 12..144 FT /note="ENTH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243" FT DOMAIN 183..202 FT /note="UIM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213" FT DOMAIN 208..227 FT /note="UIM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213" FT DOMAIN 233..252 FT /note="UIM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213" FT REPEAT 274..276 FT /note="1" FT REPEAT 294..296 FT /note="2" FT REPEAT 306..308 FT /note="3" FT REPEAT 319..321 FT /note="4" FT REPEAT 332..334 FT /note="5" FT REPEAT 349..351 FT /note="6" FT REPEAT 367..369 FT /note="7" FT REPEAT 377..379 FT /note="8" FT REPEAT 501..503 FT /note="1" FT REPEAT 517..519 FT /note="2" FT REPEAT 571..573 FT /note="3" FT REGION 149..186 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 264..283 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 274..379 FT /note="8 X 3 AA repeats of D-P-W" FT REGION 293..575 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 501..573 FT /note="3 X 3 AA repeats of N-P-F" FT MOTIF 401..410 FT /note="[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif" FT COMPBIAS 455..469 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 510..533 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 537..575 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 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 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 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 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 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 MOD_RES 382 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6I3" FT MOD_RES 418 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6I3" FT MOD_RES 419 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6I3" FT MOD_RES 420 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q80VP1" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6I3" FT MOD_RES 446 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6I3" FT MOD_RES 453 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 459 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6I3" FT MOD_RES 463 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6I3" FT MOD_RES 469 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 472 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80VP1" FT MOD_RES 493 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6I3" FT MOD_RES 533 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q80VP1" FT MUTAGEN 6 FT /note="L->E,H,Q: Reduces lipid binding." FT /evidence="ECO:0000269|PubMed:12353027" FT MUTAGEN 8 FT /note="R->A: Strongly reduces lipid binding." FT /evidence="ECO:0000269|PubMed:11161217" FT MUTAGEN 63 FT /note="R->L: Strongly reduces lipid binding. Abolishes FT lipid binding; when associated with L-73." FT /evidence="ECO:0000269|PubMed:11161217, FT ECO:0000269|PubMed:12353027" FT MUTAGEN 72 FT /note="R->A: Abolishes ZNF145 binding." FT /evidence="ECO:0000269|PubMed:11161217" FT MUTAGEN 73 FT /note="H->L: Abolishes lipid binding; when associated with FT L-63." FT /evidence="ECO:0000269|PubMed:12353027" FT MUTAGEN 76 FT /note="K->A: Strongly reduces lipid binding." FT /evidence="ECO:0000269|PubMed:11161217" FT MUTAGEN 190 FT /note="L->A: Abolishes mono-ubiquitination." FT /evidence="ECO:0000269|PubMed:11919637" FT MUTAGEN 257..259 FT /note="LMD->AAA: Strongly reduces clathrin binding." FT /evidence="ECO:0000269|PubMed:10692452" FT MUTAGEN 260..263 FT /note="LADV->AAAA: Strongly reduces clathrin binding." FT /evidence="ECO:0000269|PubMed:10692452" FT HELIX 2..15 FT /evidence="ECO:0007829|PDB:1H0A" FT HELIX 19..27 FT /evidence="ECO:0007829|PDB:1EYH" FT STRAND 30..33 FT /evidence="ECO:0007829|PDB:1EYH" FT HELIX 37..46 FT /evidence="ECO:0007829|PDB:1EYH" FT HELIX 50..64 FT /evidence="ECO:0007829|PDB:1EYH" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:1EYH" FT HELIX 71..87 FT /evidence="ECO:0007829|PDB:1EYH" FT HELIX 90..98 FT /evidence="ECO:0007829|PDB:1EYH" FT HELIX 100..104 FT /evidence="ECO:0007829|PDB:1EYH" FT HELIX 105..108 FT /evidence="ECO:0007829|PDB:1EYH" FT HELIX 120..135 FT /evidence="ECO:0007829|PDB:1EYH" FT HELIX 137..155 FT /evidence="ECO:0007829|PDB:1EYH" SQ SEQUENCE 575 AA; 60158 MW; D0B770F3B7AB5DDA CRC64; MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV VAFSEIMSMI WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM YAVQTLKDFQ YVDRDGKDQG VNVREKAKQL VALLRDEDRL REERAHALKT KEKLAQTATA SSAAVGSGPP PEAEQAWPQS SGEEELQLQL ALAMSKEEAD QPPSCGPEDD VQLQLALSLS REEHDKEERI RRGDDLRLQM AIEESKRETG GKEESSLMDL ADVFTTPAPP QASDPWGGPA SVPTAVPVAA AASDPWGAPA VPPAADPWGG AAPTPASGDP WRPAAPTGPS VDPWGGTPAP AAGEGPTSDP WGSADGGAPV SGPPSSDPWA PAPAFSDPWG GSPAKPSSNG TAVGGFDTEP DEFSDFDRLR TALPTSGSST GELELLAGEV PARSPGAFDM SGVGGSLAES VGSPPPAATP TPTPPTRKTP ESFLGPNAAL VDLDSLVSRP GPTPPGAKAS NPFLPSGAPA TGPSVTNPFQ PAPPATLTLN QLRLSPVPPV PGAPPTYISP LGGGPGLPPM MPPGPPAPNT NPFLL //