ID ATG2B_HUMAN Reviewed; 2078 AA. AC Q96BY7; Q6ZRE7; Q96DQ3; Q9NW80; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 5. DT 27-MAR-2024, entry version 164. DE RecName: Full=Autophagy-related protein 2 homolog B {ECO:0000303|PubMed:22219374}; GN Name=ATG2B {ECO:0000303|PubMed:22219374, ECO:0000312|HGNC:HGNC:20187}; GN Synonyms=C14orf103 {ECO:0000312|HGNC:HGNC:20187}; 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 [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-800 AND 1065-2078, AND VARIANTS RP ASP-1124; GLU-1383 AND THR-1567. RC TISSUE=Embryo, and Thymus; 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 MRNA] OF 1304-2078, AND VARIANTS GLU-1383 RP AND THR-1567. 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND IDENTIFICATION BY RP 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 [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22219374; DOI=10.1091/mbc.e11-09-0785; RA Velikkakath A.K., Nishimura T., Oita E., Ishihara N., Mizushima N.; RT "Mammalian Atg2 proteins are essential for autophagosome formation and RT important for regulation of size and distribution of lipid droplets."; RL Mol. Biol. Cell 23:896-909(2012). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-840 AND SER-899, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-886; SER-1018 AND RP SER-1526, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP INTERACTION WITH WDR45, AND MUTAGENESIS OF 1025-TYR--SER-1027. RX PubMed=28820312; DOI=10.1080/15548627.2017.1359381; RA Zheng J.X., Li Y., Ding Y.H., Liu J.J., Zhang M.J., Dong M.Q., Wang H.W., RA Yu L.; RT "Architecture of the ATG2B-WDR45 complex and an aromatic Y/HF motif crucial RT for complex formation."; RL Autophagy 13:1870-1883(2017). RN [9] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=31721365; DOI=10.1111/gtc.12733; RA Osawa T., Ishii Y., Noda N.N.; RT "Human ATG2B possesses a lipid transfer activity which is accelerated by RT negatively charged lipids and WIPI4."; RL Genes Cells 25:65-70(2020). CC -!- FUNCTION: Lipid transfer protein required for both autophagosome CC formation and regulation of lipid droplet morphology and dispersion CC (PubMed:22219374, PubMed:31721365). Tethers the edge of the isolation CC membrane (IM) to the endoplasmic reticulum (ER) and mediates direct CC lipid transfer from ER to IM for IM expansion (PubMed:22219374, CC PubMed:31721365). Binds to the ER exit site (ERES), which is the CC membrane source for autophagosome formation, and extracts phospholipids CC from the membrane source and transfers them to ATG9 (ATG9A or ATG9B) to CC the IM for membrane expansion (By similarity). Lipid transfer activity CC is enhanced by WDR45/WIPI4, which promotes ATG2B-association with CC phosphatidylinositol 3-monophosphate (PI3P)-containing membranes CC (PubMed:31721365). {ECO:0000250|UniProtKB:Q2TAZ0, CC ECO:0000269|PubMed:22219374, ECO:0000269|PubMed:31721365}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl- CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q2TAZ0}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2- CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, CC ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:31721365}; CC -!- SUBUNIT: Interacts with WDR45/WIPI4. {ECO:0000269|PubMed:31721365}. CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane CC {ECO:0000269|PubMed:22219374}; Peripheral membrane protein CC {ECO:0000269|PubMed:22219374}. Lipid droplet CC {ECO:0000269|PubMed:22219374}. Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:P53855}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P53855}. CC -!- DOMAIN: The chorein N-terminal domain mediates lipid transfer activity. CC {ECO:0000250|UniProtKB:Q2TAZ0}. CC -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91504.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB70872.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC87363.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AL355102; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359240; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK001104; BAA91504.1; ALT_INIT; mRNA. DR EMBL; AK055200; BAB70872.1; ALT_SEQ; mRNA. DR EMBL; AK128275; BAC87363.1; ALT_INIT; mRNA. DR EMBL; BC015016; AAH15016.3; -; mRNA. DR CCDS; CCDS9944.2; -. DR RefSeq; NP_060506.5; NM_018036.6. DR AlphaFoldDB; Q96BY7; -. DR EMDB; EMD-15604; -. DR EMDB; EMD-15605; -. DR BioGRID; 120412; 84. DR IntAct; Q96BY7; 34. DR MINT; Q96BY7; -. DR STRING; 9606.ENSP00000353010; -. DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family. DR GlyCosmos; Q96BY7; 1 site, 1 glycan. DR GlyGen; Q96BY7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96BY7; -. DR PhosphoSitePlus; Q96BY7; -. DR BioMuta; ATG2B; -. DR DMDM; 308153682; -. DR EPD; Q96BY7; -. DR jPOST; Q96BY7; -. DR MassIVE; Q96BY7; -. DR MaxQB; Q96BY7; -. DR PaxDb; 9606-ENSP00000353010; -. DR PeptideAtlas; Q96BY7; -. DR ProteomicsDB; 76129; -. DR Pumba; Q96BY7; -. DR Antibodypedia; 94; 158 antibodies from 28 providers. DR DNASU; 55102; -. DR Ensembl; ENST00000359933.6; ENSP00000353010.4; ENSG00000066739.12. DR GeneID; 55102; -. DR KEGG; hsa:55102; -. DR MANE-Select; ENST00000359933.6; ENSP00000353010.4; NM_018036.7; NP_060506.6. DR UCSC; uc001yfi.4; human. DR AGR; HGNC:20187; -. DR CTD; 55102; -. DR DisGeNET; 55102; -. DR GeneCards; ATG2B; -. DR HGNC; HGNC:20187; ATG2B. DR HPA; ENSG00000066739; Low tissue specificity. DR MIM; 616226; gene. DR neXtProt; NX_Q96BY7; -. DR OpenTargets; ENSG00000066739; -. DR PharmGKB; PA162377102; -. DR VEuPathDB; HostDB:ENSG00000066739; -. DR eggNOG; KOG2993; Eukaryota. DR GeneTree; ENSGT00620000087966; -. DR HOGENOM; CLU_001781_0_0_1; -. DR InParanoid; Q96BY7; -. DR OMA; VDNHFCL; -. DR OrthoDB; 5476854at2759; -. DR PhylomeDB; Q96BY7; -. DR TreeFam; TF313482; -. DR PathwayCommons; Q96BY7; -. DR SignaLink; Q96BY7; -. DR SIGNOR; Q96BY7; -. DR BioGRID-ORCS; 55102; 11 hits in 1154 CRISPR screens. DR ChiTaRS; ATG2B; human. DR GenomeRNAi; 55102; -. DR Pharos; Q96BY7; Tbio. DR PRO; PR:Q96BY7; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q96BY7; Protein. DR Bgee; ENSG00000066739; Expressed in Brodmann (1909) area 23 and 189 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell. DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central. DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell. DR GO; GO:0120013; F:lipid transfer activity; IDA:GO_Central. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central. DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central. DR GO; GO:0044804; P:nucleophagy; IBA:GO_Central. DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central. DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central. DR InterPro; IPR026849; ATG2. DR InterPro; IPR015412; Atg2/VPS13_C. DR InterPro; IPR026885; ATG2_mid_RBG. DR InterPro; IPR026854; VPS13-like_N. DR PANTHER; PTHR13190; AUTOPHAGY-RELATED 2, ISOFORM A; 1. DR PANTHER; PTHR13190:SF20; AUTOPHAGY-RELATED PROTEIN 2 HOMOLOG B; 1. DR Pfam; PF09333; ATG2-VPS13_C; 1. DR Pfam; PF13329; ATG2_CAD; 1. DR Pfam; PF12624; Chorein_N; 1. DR Genevisible; Q96BY7; HS. PE 1: Evidence at protein level; KW Autophagy; Endoplasmic reticulum; Lipid droplet; Lipid transport; Membrane; KW Phosphoprotein; Reference proteome; Transport. FT CHAIN 1..2078 FT /note="Autophagy-related protein 2 homolog B" FT /id="PRO_0000089909" FT DOMAIN 13..108 FT /note="Chorein N-terminal" FT /evidence="ECO:0000255" FT REGION 473..495 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 868..888 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1375..1405 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1387..1401 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 255 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 379 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80XK6" FT MOD_RES 497 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 840 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 886 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 899 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1008 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80XK6" FT MOD_RES 1012 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q80XK6" FT MOD_RES 1016 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80XK6" FT MOD_RES 1018 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1022 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q80XK6" FT MOD_RES 1526 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 1124 FT /note="N -> D (in dbSNP:rs9323945)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_045956" FT VARIANT 1383 FT /note="Q -> E (in dbSNP:rs3759601)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_021523" FT VARIANT 1567 FT /note="I -> T (in dbSNP:rs2289622)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_023096" FT MUTAGEN 1025..1027 FT /note="YFS->AAA: Strongly reduced interaction with FT WDR45/WIPI4." FT /evidence="ECO:0000269|PubMed:28820312" FT CONFLICT 765 FT /note="Q -> R (in Ref. 2; BAB70872)" FT /evidence="ECO:0000305" FT CONFLICT 1905 FT /note="K -> E (in Ref. 2; BAA91504)" FT /evidence="ECO:0000305" FT CONFLICT 1932 FT /note="F -> S (in Ref. 2; BAC87363)" FT /evidence="ECO:0000305" FT CONFLICT 2062 FT /note="R -> G (in Ref. 2; BAA91504)" FT /evidence="ECO:0000305" SQ SEQUENCE 2078 AA; 232763 MW; AA573F5C64D96C36 CRC64; MPWPFSESIK KRACRYLLQR YLGHFLQEKL SLEQLSLDLY QGTGSLAQVP LDKWCLNEIL ESADAPLEVT EGFIQSISLS VPWGSLLQDN CALEVRGLEM VFRPRPRPAT GSEPMYWSSF MTSSMQLAKE CLSQKLTDEQ GEGSQPFEGL EKFAETIETV LRRVKVTFID TVLRIEHVPE NSKTGTALEI RIERTVYCDE TADESSGINV HQPTAFAHKL LQLSGVSLFW DEFSASAKSS PVCSTAPVET EPKLSPSWNP KIIYEPHPQL TRNLPEIAPS DPVQIGRLIG RLELSLTLKQ NEVLPGAKLD VDGQIDSIHL LLSPRQVHLL LDMLAAIAGP ENSSKIGLAN KDRKNRPMQQ EDEYRIQMEL NRYYLRKDSL SVGVSSEQSF YETETARTPS SREEEVFFSM ADMDMSHSLS SLPPLGDPPN MDLELSLTST YTNTPAGSPL SATVLQPTWG EFLDHHKEQP VRGSTFPSNL VHPTPLQKTS LPSRSVSVDE SRPELIFRLA VGTFSISVLH IDPLSPPETS QNLNPLTPMA VAFFTCIEKI DPARFSTEDF KSFRAVFAEA CSHDHLRFIG TGIKVSYEQR QRSASRYFST DMSIGQMEFL ECLFPTDFHS VPPHYTELLT FHSKEETGSH SPVCLQLHYK HSENRGPQGN QARLSSVPHK AELQIKLNPV CCELDISIVD RLNSLLQPQK LATVEMMASH MYTSYNKHIS LHKAFTEVFL DDSHSPANCR ISVQVATPAL NLSVRFPIPD LRSDQERGPW FKKSLQKEIL YLAFTDLEFK TEFIGGSTPE QIKLELTFRE LIGSFQEEKG DPSIKFFHVS SGVDGDTTSS DDFDWPRIVL KINPPAMHSI LERIAAEEEE ENDGHYQEEE EGGAHSLKDV CDLRRPAPSP FSSRRVMFEN EQMVMPGDPV EMTEFQDKAI SNSHYVLELT LPNIYVTLPN KSFYEKLYNR IFNDLLLWEP TAPSPVETFE NISYGIGLSV ASQLINTFNK DSFSAFKSAV HYDEESGSEE ETLQYFSTVD PNYRSRRKKK LDSQNKNSQS FLSVLLNINH GLIAVFTDVK QDNGDLLENK HGEFWLEFNS GSLFCVTKYE GFDDKHYICL HSSSFSLYHK GIVNGVILPT ETRLPSSTRP HWLEPTIYSS EEDGLSKTSS DGVGGDSLNM LSVAVKILSD KSESNTKEFL IAVGLKGATL QHRMLPSGLS WHEQILYFLN IADEPVLGYN PPTSFTTFHV HLWSCALDYR PLYLPIRSLL TVETFSVSSS VALDKSSSTL RIILDEAALH LSDKCNTVTI NLSRDYVRVM DMGLLELTIT AVKSDSDGEQ TEPRFELHCS SDVVHIRTCS DSCAALMNLI QYIASYGDLQ TPNKADMKPG AFQRRSKVDS SGRSSSRGPV LPEADQQMLR DLMSDAMEEI DMQQGTSSVK PQANGVLDEK SQIQEPCCSD LFLFPDESGN VSQESGPTYA SFSHHFISDA MTGVPTENDD FCILFAPKAA MQEKEEEPVI KIMVDDAIVI RDNYFSLPVN KTDTSKAPLH FPIPVIRYVV KEVSLVWHLY GGKDFGIVPP TSPAKSYISP HSSPSHTPTR HGRNTVCGGK GRNHDFLMEI QLSKVKFQHE VYPPCKPDCD SSLSEHPVSR QVFIVQDLEI RDRLATSQMN KFLYLYCSKE MPRKAHSNML TVKALHVCPE SGRSPQECCL RVSLMPLRLN IDQDALFFLK DFFTSLSAEV ELQMTPDPEV KKSPGADVTC SLPRHLSTSK EPNLVISFSG PKQPSQNDSA NSVEVVNGME EKNFSAEEAS FRDQPVFFRE FRFTSEVPIR LDYHGKHVSM DQGTLAGILI GLAQLNCSEL KLKRLSYRHG LLGVDKLFSY AITEWLNDIK KNQLPGILGG VGPMHSLVQL VQGLKDLVWL PIEQYRKDGR IVRGFQRGAA SFGTSTAMAA LELTNRMVQT IQAAAETAYD MVSPGTLSIE PKKTKRFPHH RLAHQPVDLR EGVAKAYSVV KEGITDTAQT IYETAAREHE SRGVTGAVGE VLRQIPPAVV KPLIVATEAT SNVLGGMRNQ IRPDVRQDES QKWRHGDD //