ID SNX4_HUMAN Reviewed; 450 AA. AC O95219; B3KMH0; B4DQV4; D3DNA3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 182. DE RecName: Full=Sorting nexin-4 {ECO:0000303|PubMed:9819414}; GN Name=SNX4 {ECO:0000303|PubMed:9819414, ECO:0000312|HGNC:HGNC:11175}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RX PubMed=9819414; DOI=10.1128/mcb.18.12.7278; RA Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.; RT "Identification of a family of sorting nexin molecules and characterization RT of their association with receptors."; RL Mol. Cell. Biol. 18:7278-7287(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Placenta; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [6] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BIN1. RX PubMed=12668730; DOI=10.1242/jcs.00403; RA Leprince C., Le Scolan E., Meunier B., Fraisier V., Brandon N., RA De Gunzburg J., Camonis J.; RT "Sorting nexin 4 and amphiphysin 2, a new partnership between endocytosis RT and intracellular trafficking."; RL J. Cell Sci. 116:1937-1948(2003). RN [7] RP FUNCTION, INTERACTION WITH WWC1/KIBRA, MUTAGENESIS OF LYS-132, AND RP SUBCELLULAR LOCATION. RX PubMed=17994011; DOI=10.1038/ncb1656; RA Traer C.J., Rutherford A.C., Palmer K.J., Wassmer T., Oakley J., Attar N., RA Carlton J.G., Kremerskothen J., Stephens D.J., Cullen P.J.; RT "SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport RT into the endocytic recycling compartment."; RL Nat. Cell Biol. 9:1370-1380(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SNX7 AND SNX30. RX PubMed=32513819; DOI=10.1242/jcs.246306; RA Anton Z., Betin V.M.S., Simonetti B., Traer C.J., Attar N., Cullen P.J., RA Lane J.D.; RT "A heterodimeric SNX4--SNX7 SNX-BAR autophagy complex coordinates ATG9A RT trafficking for efficient autophagosome assembly."; RL J. Cell Sci. 133:0-0(2020). RN [14] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=33468622; DOI=10.1242/jcs.250670; RA Ravussin A., Brech A., Tooze S.A., Stenmark H.; RT "The phosphatidylinositol 3-phosphate-binding protein SNX4 controls ATG9A RT recycling and autophagy."; RL J. Cell Sci. 134:0-0(2021). CC -!- FUNCTION: Involved in the regulation of endocytosis and in several CC stages of intracellular trafficking (PubMed:12668730, PubMed:17994011, CC PubMed:32513819, PubMed:33468622). Plays a role in recycling CC endocytosed transferrin receptor and prevent its degradation CC (PubMed:17994011). Involved in autophagosome assembly by regulating CC trafficking and recycling of phospholipid scramblase ATG9A CC (PubMed:32513819, PubMed:33468622). {ECO:0000269|PubMed:12668730, CC ECO:0000269|PubMed:17994011, ECO:0000269|PubMed:32513819, CC ECO:0000269|PubMed:33468622}. CC -!- SUBUNIT: Heterodimer; heterodimerizes with SNX7 or SNX30 CC (PubMed:32513819). Interacts with WWC1/KIBRA (PubMed:17994011). CC Identified in a complex with WWC1/KIBRA and dynein components DYNLL1 CC and DYNC1I2 (PubMed:17994011). Interacts with BIN1 (PubMed:12668730). CC {ECO:0000269|PubMed:12668730, ECO:0000269|PubMed:17994011, CC ECO:0000269|PubMed:32513819}. CC -!- INTERACTION: CC O95219; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-724909, EBI-714543; CC O95219; O00499: BIN1; NbExp=4; IntAct=EBI-724909, EBI-719094; CC O95219; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-724909, EBI-12831978; CC O95219; P43360: MAGEA6; NbExp=3; IntAct=EBI-724909, EBI-1045155; CC O95219; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-724909, EBI-2623095; CC O95219; Q5VWJ9: SNX30; NbExp=3; IntAct=EBI-724909, EBI-8099676; CC O95219; Q9UNH6: SNX7; NbExp=2; IntAct=EBI-724909, EBI-751422; CC O95219; Q9UNH6-3: SNX7; NbExp=4; IntAct=EBI-724909, EBI-12424584; CC -!- SUBCELLULAR LOCATION: Early endosome membrane CC {ECO:0000269|PubMed:17994011, ECO:0000269|PubMed:32513819, CC ECO:0000269|PubMed:33468622}; Peripheral membrane protein CC {ECO:0000269|PubMed:17994011}; Cytoplasmic side CC {ECO:0000269|PubMed:17994011}. Note=Also detected on a juxtanuclear CC endocytic recycling compartment (ERC). {ECO:0000269|PubMed:17994011}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95219-1; Sequence=Displayed; CC Name=2; CC IsoId=O95219-2; Sequence=VSP_056665; CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is CC necessary for peripheral membrane localization. CC {ECO:0000250|UniProtKB:Q96L94}. CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}. 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; AF065485; AAC83149.1; -; mRNA. DR EMBL; AK001835; BAG50982.1; -; mRNA. DR EMBL; AK298972; BAG61066.1; -; mRNA. DR EMBL; AC080096; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC117487; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW79390.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79391.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79393.1; -; Genomic_DNA. DR EMBL; BC018762; AAH18762.1; -; mRNA. DR CCDS; CCDS3032.1; -. [O95219-1] DR RefSeq; NP_003785.1; NM_003794.3. [O95219-1] DR AlphaFoldDB; O95219; -. DR SMR; O95219; -. DR BioGRID; 114262; 66. DR CORUM; O95219; -. DR DIP; DIP-36719N; -. DR IntAct; O95219; 35. DR MINT; O95219; -. DR STRING; 9606.ENSP00000251775; -. DR TCDB; 3.A.34.1.1; the sorting nexins of the escrt complexes (sn-escrt). DR iPTMnet; O95219; -. DR MetOSite; O95219; -. DR PhosphoSitePlus; O95219; -. DR BioMuta; SNX4; -. DR DOSAC-COBS-2DPAGE; O95219; -. DR EPD; O95219; -. DR jPOST; O95219; -. DR MassIVE; O95219; -. DR MaxQB; O95219; -. DR PaxDb; 9606-ENSP00000251775; -. DR PeptideAtlas; O95219; -. DR ProteomicsDB; 4904; -. DR ProteomicsDB; 50724; -. [O95219-1] DR Pumba; O95219; -. DR Antibodypedia; 1370; 306 antibodies from 32 providers. DR DNASU; 8723; -. DR Ensembl; ENST00000251775.9; ENSP00000251775.4; ENSG00000114520.11. [O95219-1] DR GeneID; 8723; -. DR KEGG; hsa:8723; -. DR MANE-Select; ENST00000251775.9; ENSP00000251775.4; NM_003794.4; NP_003785.1. DR UCSC; uc003eib.5; human. [O95219-1] DR AGR; HGNC:11175; -. DR CTD; 8723; -. DR GeneCards; SNX4; -. DR HGNC; HGNC:11175; SNX4. DR HPA; ENSG00000114520; Low tissue specificity. DR MIM; 605931; gene. DR neXtProt; NX_O95219; -. DR OpenTargets; ENSG00000114520; -. DR PharmGKB; PA36014; -. DR VEuPathDB; HostDB:ENSG00000114520; -. DR eggNOG; KOG2273; Eukaryota. DR GeneTree; ENSGT00930000151029; -. DR HOGENOM; CLU_057138_0_0_1; -. DR InParanoid; O95219; -. DR OMA; QKSGHYL; -. DR OrthoDB; 5475877at2759; -. DR PhylomeDB; O95219; -. DR TreeFam; TF328543; -. DR PathwayCommons; O95219; -. DR SignaLink; O95219; -. DR BioGRID-ORCS; 8723; 10 hits in 1153 CRISPR screens. DR ChiTaRS; SNX4; human. DR GeneWiki; SNX4; -. DR GenomeRNAi; 8723; -. DR Pharos; O95219; Tbio. DR PRO; PR:O95219; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; O95219; Protein. DR Bgee; ENSG00000114520; Expressed in secondary oocyte and 213 other cell types or tissues. DR ExpressionAtlas; O95219; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL. DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098830; C:presynaptic endosome; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB. DR GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:UniProtKB. DR GO; GO:0005158; F:insulin receptor binding; IDA:UniProtKB. DR GO; GO:1990460; F:leptin receptor binding; IDA:UniProtKB. DR GO; GO:0035091; F:phosphatidylinositol binding; IMP:UniProtKB. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IMP:UniProtKB. DR GO; GO:1990459; F:transferrin receptor binding; IDA:UniProtKB. DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB. DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB. DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; IMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IMP:UniProtKB. DR CDD; cd07622; BAR_SNX4; 1. DR CDD; cd06864; PX_SNX4; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 3.30.1520.10; Phox-like domain; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR001683; PX_dom. DR InterPro; IPR036871; PX_dom_sf. DR InterPro; IPR034902; PX_SNX4. DR InterPro; IPR034783; SNX4. DR InterPro; IPR037430; SNX4_BAR. DR PANTHER; PTHR46596; SORTING NEXIN-4; 1. DR PANTHER; PTHR46596:SF1; SORTING NEXIN-4; 1. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR SUPFAM; SSF64268; PX domain; 1. DR PROSITE; PS50195; PX; 1. DR Genevisible; O95219; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Endosome; Lipid-binding; Membrane; KW Phosphoprotein; Protein transport; Reference proteome; Transport. FT CHAIN 1..450 FT /note="Sorting nexin-4" FT /id="PRO_0000213842" FT DOMAIN 61..187 FT /note="PX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 106 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3-phosphate)" FT /ligand_id="ChEBI:CHEBI:58088" FT /evidence="ECO:0000250|UniProtKB:Q3UR97" FT BINDING 108 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3-phosphate)" FT /ligand_id="ChEBI:CHEBI:58088" FT /evidence="ECO:0000250|UniProtKB:Q96L94" FT BINDING 132 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3-phosphate)" FT /ligand_id="ChEBI:CHEBI:58088" FT /evidence="ECO:0000250|UniProtKB:Q96L94" FT BINDING 154 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3-phosphate)" FT /ligand_id="ChEBI:CHEBI:58088" FT /evidence="ECO:0000250|UniProtKB:Q6P4T1" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..145 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056665" FT MUTAGEN 132 FT /note="K->A: Abolishes phosphatidylinositol phosphate FT binding. Abolishes endosomal location." FT /evidence="ECO:0000269|PubMed:17994011" SQ SEQUENCE 450 AA; 51909 MW; 3D5B52AC52A07686 CRC64; MEQAPPDPER QLQPAPLEPL GSPDAGLGAA VGKEAEGAGE ESSGVDTMTH NNFWLKKIEI SVSEAEKRTG RNAMNMQETY TAYLIETRSV EHTDGQSVLT DSLWRRYSEF ELLRSYLLVY YPHIVVPPLP EKRAEFVWHK LSADNMDPDF VERRRIGLEN FLLRIASHPI LCRDKIFYLF LTQEGNWKET VNETGFQLKA DSRLKALNAT FRVKNPDKRF TDLKHYSDEL QSVISHLLRV RARVADRLYG VYKVHGNYGR VFSEWSAIEK EMGDGLQSAG HHMDVYASSI DDILEDEEHY ADQLKEYLFY AEALRAVCRK HELMQYDLEM AAQDLASKKQ QCEELVTGTV RTFSLKGMTT KLFGQETPEQ REARIKVLEE QINEGEQQLK SKNLEGREFV KNAWADIERF KEQKNRDLKE ALISYAVMQI SMCKKGIQVW TNAKECFSKM //