EPN1_RAT
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 03-AUG-2022, entry version 178.
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). {ECO:0000250|UniProtKB:Q80VP1,
CC ECO:0000250|UniProtKB:Q9Y6I3, ECO:0000269|PubMed:10380931,
CC ECO:0000269|PubMed:10430869, ECO:0000269|PubMed:10692452,
CC ECO:0000269|PubMed:10791968, ECO:0000269|PubMed:10944104,
CC ECO:0000269|PubMed:11161217, ECO:0000269|PubMed:12057195,
CC ECO:0000269|PubMed:12353027, ECO:0000269|PubMed:9723620,
CC 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";
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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; O88339; -.
DR PeptideAtlas; O88339; -.
DR PRIDE; O88339; -.
DR GeneID; 117277; -.
DR KEGG; rno:117277; -.
DR UCSC; RGD:619772; rat.
DR CTD; 29924; -.
DR RGD; 619772; Epn1.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_012678_4_2_1; -.
DR InParanoid; O88339; -.
DR OrthoDB; 1263849at2759; -.
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 Genevisible; O88339; RN.
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:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0098888; C:extrinsic component of presynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
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:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
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 DisProt; DP00251; -.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR003903; UIM_dom.
DR Pfam; PF01417; ENTH; 1.
DR Pfam; PF02809; UIM; 3.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00726; UIM; 3.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50330; UIM; 3.
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
