WIPI3_HUMAN
ID WIPI3_HUMAN Reviewed; 344 AA.
AC Q5MNZ6; A0A024R8U4; A0A218N098; O95328; Q2MCP6; Q6IBN2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=WD repeat domain phosphoinositide-interacting protein 3;
DE Short=WIPI-3;
DE AltName: Full=WD repeat-containing protein 45-like;
DE Short=WDR45-like protein;
DE AltName: Full=WD repeat-containing protein 45B;
DE AltName: Full=WIPI49-like protein;
GN Name=WDR45B; Synonyms=WDR45L, WIPI3;
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], FUNCTION, PHOSPHOINOSITIDES-BINDING,
RP INTERACTION WITH RB1CC1; TSC1 AND TSC2, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 225-ARG-226.
RC TISSUE=Liver;
RX PubMed=28561066; DOI=10.1038/ncomms15637;
RA Bakula D., Mueller A.J., Zuleger T., Takacs Z., Franz-Wachtel M.,
RA Thost A.K., Brigger D., Tschan M.P., Frickey T., Robenek H., Macek B.,
RA Proikas-Cezanne T.;
RT "WIPI3 and WIPI4 beta-propellers are scaffolds for LKB1-AMPK-TSC signalling
RT circuits in the control of autophagy.";
RL Nat. Commun. 8:15637-15637(2017).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Wang H., Ma X., Zhang Y., Wu C.;
RT "Identification and characterization of human WIPI-3 in silico.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-344.
RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
RT "Full-insert sequence of mapped XREF EST.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-344, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15602573; DOI=10.1038/sj.onc.1208331;
RA Proikas-Cezanne T., Waddell S., Gaugel A., Frickey T., Lupas A.,
RA Nordheim A.;
RT "WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family,
RT is aberrantly expressed in human cancer and is linked to starvation-induced
RT autophagy.";
RL Oncogene 23:9314-9325(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-344.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INVOLVEMENT IN NEDSBAS, AND VARIANTS NEDSBAS 225-ARG--LEU-344 DEL AND
RP 267-GLN--LEU-344 DEL.
RX PubMed=28503735; DOI=10.1111/cge.13054;
RA Suleiman J., Allingham-Hawkins D., Hashem M., Shamseldin H.E.,
RA Alkuraya F.S., El-Hattab A.W.;
RT "WDR45B-related intellectual disability, spastic quadriplegia, epilepsy,
RT and cerebral hypoplasia: A consistent neurodevelopmental syndrome.";
RL Clin. Genet. 93:360-364(2018).
RN [9] {ECO:0007744|PDB:6IYY}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 8-344, FUNCTION, AND MUTAGENESIS
RP OF ARG-62; HIS-184; SER-204; LYS-206; THR-208; ARG-211; ARG-225; ARG-226
RP AND HIS-255.
RX PubMed=30797857; DOI=10.1016/j.jmb.2019.02.019;
RA Liang R., Ren J., Zhang Y., Feng W.;
RT "Structural Conservation of the Two Phosphoinositide-Binding Sites in WIPI
RT Proteins.";
RL J. Mol. Biol. 431:1494-1505(2019).
RN [10] {ECO:0007744|PDB:6KLR}
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 8-344 IN COMPLEX WITH ATG2A,
RP INTERACTION WITH ATG2A, AND MUTAGENESIS OF 19-ASN--HIS-22; VAL-35;
RP 59-MET--ARG-62; TYR-65; 96-ILE--PHE-98 AND PHE-125.
RX PubMed=32483132; DOI=10.1038/s41467-020-16523-y;
RA Ren J., Liang R., Wang W., Zhang D., Yu L., Feng W.;
RT "Multi-site-mediated entwining of the linear WIR-motif around WIPI beta-
RT propellers for autophagy.";
RL Nat. Commun. 11:2702-2702(2020).
CC -!- FUNCTION: Component of the autophagy machinery that controls the major
CC intracellular degradation process by which cytoplasmic materials are
CC packaged into autophagosomes and delivered to lysosomes for degradation
CC (PubMed:28561066). Binds phosphatidylinositol 3-phosphate (PtdIns3P),
CC and other phosphoinositides including PtdIns(3,5)P2, forming on
CC membranes of the endoplasmic reticulum upon activation of the upstream
CC ULK1 and PI3 kinases and is recruited at phagophore assembly sites
CC where it regulates the elongation of nascent phagophores downstream of
CC WIPI2 (PubMed:28561066, PubMed:30797857). In the cellular response to
CC starvation, may also function together with the TSC1-TSC2 complex and
CC RB1CC1 in the inhibition of the mTORC1 signaling pathway
CC (PubMed:28503735). {ECO:0000269|PubMed:28503735,
CC ECO:0000269|PubMed:28561066, ECO:0000269|PubMed:30797857}.
CC -!- SUBUNIT: Interacts with the TSC1-TSC2 complex; stimulated upon
CC starvation (PubMed:28561066). Interacts with RB1CC1 (PubMed:28561066).
CC Interacts with ATG2A (PubMed:32483132). {ECO:0000269|PubMed:28561066,
CC ECO:0000269|PubMed:32483132}.
CC -!- INTERACTION:
CC Q5MNZ6; P0DTC2: S; Xeno; NbExp=4; IntAct=EBI-2819021, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC {ECO:0000269|PubMed:28561066}. Lysosome {ECO:0000269|PubMed:28561066}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in heart,
CC skeletal muscle and pancreas. Up-regulated in a variety of tumor
CC tissues including ovarian and uterine cancers.
CC {ECO:0000269|PubMed:15602573}.
CC -!- DOMAIN: The L/FRRG motif is required for recruitment to PtdIns3P.
CC {ECO:0000250|UniProtKB:Q9Y4P8}.
CC -!- DISEASE: Neurodevelopmental disorder with spastic quadriplegia and
CC brain abnormalities with or without seizures (NEDSBAS) [MIM:617977]: An
CC autosomal recessive disorder characterized by profound developmental
CC delay, progressive spastic quadriplegia and contractures, early-onset
CC refractory epilepsy in most patients, and brain malformations.
CC Neuroimaging shows ventriculomegaly, reduced cerebral white matter
CC volume, and thinning of cerebral gray matter.
CC {ECO:0000269|PubMed:28503735}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72952.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ASF79340.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AM182326; CAJ57996.1; -; mRNA.
DR EMBL; KX434429; ASF79340.1; ALT_INIT; mRNA.
DR EMBL; AC124283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89810.1; -; Genomic_DNA.
DR EMBL; CH471099; EAW89812.1; -; Genomic_DNA.
DR EMBL; AF091083; AAC72952.1; ALT_INIT; mRNA.
DR EMBL; AY691427; AAV80763.1; -; mRNA.
DR EMBL; CR456770; CAG33051.1; -; mRNA.
DR CCDS; CCDS11815.2; -.
DR RefSeq; NP_062559.2; NM_019613.3.
DR PDB; 6IYY; X-ray; 1.80 A; A=8-344.
DR PDB; 6KLR; X-ray; 2.21 A; A/B=8-344.
DR PDBsum; 6IYY; -.
DR PDBsum; 6KLR; -.
DR AlphaFoldDB; Q5MNZ6; -.
DR SMR; Q5MNZ6; -.
DR BioGRID; 121130; 63.
DR IntAct; Q5MNZ6; 21.
DR MINT; Q5MNZ6; -.
DR STRING; 9606.ENSP00000376139; -.
DR iPTMnet; Q5MNZ6; -.
DR PhosphoSitePlus; Q5MNZ6; -.
DR BioMuta; WDR45B; -.
DR DMDM; 85542094; -.
DR EPD; Q5MNZ6; -.
DR jPOST; Q5MNZ6; -.
DR MassIVE; Q5MNZ6; -.
DR MaxQB; Q5MNZ6; -.
DR PaxDb; Q5MNZ6; -.
DR PeptideAtlas; Q5MNZ6; -.
DR PRIDE; Q5MNZ6; -.
DR ProteomicsDB; 63589; -.
DR Antibodypedia; 19917; 114 antibodies from 17 providers.
DR DNASU; 56270; -.
DR Ensembl; ENST00000392325.9; ENSP00000376139.4; ENSG00000141580.16.
DR GeneID; 56270; -.
DR KEGG; hsa:56270; -.
DR MANE-Select; ENST00000392325.9; ENSP00000376139.4; NM_019613.4; NP_062559.2.
DR UCSC; uc002kfq.3; human.
DR CTD; 56270; -.
DR DisGeNET; 56270; -.
DR GeneCards; WDR45B; -.
DR HGNC; HGNC:25072; WDR45B.
DR HPA; ENSG00000141580; Low tissue specificity.
DR MalaCards; WDR45B; -.
DR MIM; 609226; gene.
DR MIM; 617977; phenotype.
DR neXtProt; NX_Q5MNZ6; -.
DR OpenTargets; ENSG00000141580; -.
DR PharmGKB; PA134894387; -.
DR VEuPathDB; HostDB:ENSG00000141580; -.
DR eggNOG; KOG2111; Eukaryota.
DR GeneTree; ENSGT00940000157510; -.
DR InParanoid; Q5MNZ6; -.
DR OMA; WSFCKFQ; -.
DR OrthoDB; 966922at2759; -.
DR PhylomeDB; Q5MNZ6; -.
DR TreeFam; TF314859; -.
DR PathwayCommons; Q5MNZ6; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR SignaLink; Q5MNZ6; -.
DR SIGNOR; Q5MNZ6; -.
DR BioGRID-ORCS; 56270; 10 hits in 1079 CRISPR screens.
DR ChiTaRS; WDR45B; human.
DR GeneWiki; WDR45L; -.
DR GenomeRNAi; 56270; -.
DR Pharos; Q5MNZ6; Tbio.
DR PRO; PR:Q5MNZ6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q5MNZ6; protein.
DR Bgee; ENSG00000141580; Expressed in secondary oocyte and 205 other tissues.
DR ExpressionAtlas; Q5MNZ6; baseline and differential.
DR Genevisible; Q5MNZ6; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0000407; C:phagophore assembly site; IDA:UniProtKB.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0062078; F:TSC1-TSC2 complex binding; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
DR GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Disease variant; Epilepsy; Lipid-binding;
KW Lysosome; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..344
FT /note="WD repeat domain phosphoinositide-interacting
FT protein 3"
FT /id="PRO_0000051445"
FT REPEAT 2..38
FT /note="WD 1"
FT REPEAT 44..87
FT /note="WD 2"
FT REPEAT 93..125
FT /note="WD 3"
FT REPEAT 130..171
FT /note="WD 4"
FT REPEAT 176..215
FT /note="WD 5"
FT REPEAT 220..259
FT /note="WD 6"
FT REPEAT 265..314
FT /note="WD 7"
FT MOTIF 224..227
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P8"
FT VARIANT 225..344
FT /note="Missing (in NEDSBAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28503735"
FT /id="VAR_081110"
FT VARIANT 267..344
FT /note="Missing (in NEDSBAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28503735"
FT /id="VAR_081111"
FT MUTAGEN 19..22
FT /note="NQDH->AQDA: Abolished interaction with ATG2A."
FT /evidence="ECO:0000269|PubMed:32483132"
FT MUTAGEN 35
FT /note="V->Q: Strongly decreased interaction with ATG2A;
FT when associated with 59-Q--A-62."
FT /evidence="ECO:0000269|PubMed:32483132"
FT MUTAGEN 59..62
FT /note="MLFR->QLRA: Strongly decreased interaction with
FT ATG2A; when associated with Q-35."
FT /evidence="ECO:0000269|PubMed:32483132"
FT MUTAGEN 62
FT /note="R->A: Does not affect binding to phosphoinositides."
FT /evidence="ECO:0000269|PubMed:30797857"
FT MUTAGEN 65
FT /note="Y->A: Strongly decreased interaction with ATG2A;
FT when associated with A-125."
FT /evidence="ECO:0000269|PubMed:32483132"
FT MUTAGEN 96..98
FT /note="IEF->AEA: Strongly decreased interaction with
FT ATG2A."
FT /evidence="ECO:0000269|PubMed:32483132"
FT MUTAGEN 125
FT /note="F->A: Strongly decreased interaction with ATG2A;
FT when associated with A-65."
FT /evidence="ECO:0000269|PubMed:32483132"
FT MUTAGEN 184
FT /note="H->A: Abolished binding to phosphoinositides."
FT /evidence="ECO:0000269|PubMed:30797857"
FT MUTAGEN 204
FT /note="S->A: Abolished binding to phosphoinositides."
FT /evidence="ECO:0000269|PubMed:30797857"
FT MUTAGEN 206
FT /note="K->A: Abolished binding to phosphoinositides."
FT /evidence="ECO:0000269|PubMed:30797857"
FT MUTAGEN 208
FT /note="T->A: Abolished binding to phosphoinositides."
FT /evidence="ECO:0000269|PubMed:30797857"
FT MUTAGEN 211
FT /note="R->A: Abolished binding to phosphoinositides."
FT /evidence="ECO:0000269|PubMed:30797857"
FT MUTAGEN 225..226
FT /note="RR->AA: Loss of PtdIns3P binding."
FT /evidence="ECO:0000269|PubMed:28561066"
FT MUTAGEN 225
FT /note="R->A: Abolished binding to phosphoinositides."
FT /evidence="ECO:0000269|PubMed:30797857"
FT MUTAGEN 226
FT /note="R->A: Abolished binding to phosphoinositides."
FT /evidence="ECO:0000269|PubMed:30797857"
FT MUTAGEN 255
FT /note="H->A: Abolished binding to phosphoinositides."
FT /evidence="ECO:0000269|PubMed:30797857"
FT CONFLICT 56..57
FT /note="HV -> TR (in Ref. 5; AAC72952)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="V -> A (in Ref. 7; CAG33051)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="H -> R (in Ref. 1; ASF79340)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="V -> A (in Ref. 6; AAV80763)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="M -> L (in Ref. 6; AAV80763 and 1; ASF79340)"
FT /evidence="ECO:0000305"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:6IYY"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:6IYY"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:6IYY"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 117..128
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:6IYY"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:6IYY"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:6IYY"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:6IYY"
SQ SEQUENCE 344 AA; 38122 MW; CC60535E1D28660C CRC64;
MNLLPCNPHG NGLLYAGFNQ DHGCFACGME NGFRVYNTDP LKEKEKQEFL EGGVGHVEML
FRCNYLALVG GGKKPKYPPN KVMIWDDLKK KTVIEIEFST EVKAVKLRRD RIVVVLDSMI
KVFTFTHNPH QLHVFETCYN PKGLCVLCPN SNNSLLAFPG THTGHVQLVD LASTEKPPVD
IPAHEGVLSC IALNLQGTRI ATASEKGTLI RIFDTSSGHL IQELRRGSQA ANIYCINFNQ
DASLICVSSD HGTVHIFAAE DPKRNKQSSL ASASFLPKYF SSKWSFSKFQ VPSGSPCICA
FGTEPNAVIA ICADGSYYKF LFNPKGECIR DVYAQFLEMT DDKL
