ATG2B_HUMAN
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 03-AUG-2022, entry version 155.
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};
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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 BioGRID; 120412; 66.
DR IntAct; Q96BY7; 35.
DR MINT; Q96BY7; -.
DR STRING; 9606.ENSP00000353010; -.
DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family.
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; Q96BY7; -.
DR PeptideAtlas; Q96BY7; -.
DR PRIDE; Q96BY7; -.
DR ProteomicsDB; 76129; -.
DR Antibodypedia; 94; 150 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 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; PFKSAVH; -.
DR OrthoDB; 196897at2759; -.
DR PhylomeDB; Q96BY7; -.
DR TreeFam; TF313482; -.
DR PathwayCommons; Q96BY7; -.
DR SignaLink; Q96BY7; -.
DR SIGNOR; Q96BY7; -.
DR BioGRID-ORCS; 55102; 11 hits in 1078 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 187 other tissues.
DR Genevisible; Q96BY7; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
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:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late 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; Autophagy-rel_C.
DR InterPro; IPR026854; VPS13-like_N.
DR PANTHER; PTHR13190; PTHR13190; 1.
DR Pfam; PF09333; ATG_C; 1.
DR Pfam; PF12624; Chorein_N; 1.
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
