PK3C3_CAEEL
ID PK3C3_CAEEL Reviewed; 901 AA.
AC Q9TXI7; Q5TYK9; Q9TXI6; Q9XZR0;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3 {ECO:0000250|UniProtKB:Q8NEB9};
DE Short=PI3-kinase type 3 {ECO:0000250|UniProtKB:Q8NEB9};
DE Short=PI3K type 3 {ECO:0000250|UniProtKB:Q8NEB9};
DE EC=2.7.1.137 {ECO:0000255|PIRNR:PIRNR000587, ECO:0000269|PubMed:11927551};
DE AltName: Full=Phosphoinositide-3-kinase class 3 {ECO:0000250|UniProtKB:Q8NEB9};
GN Name=vps-34 {ECO:0000312|WormBase:B0025.1a};
GN Synonyms=let-512 {ECO:0000312|WormBase:B0025.1a};
GN ORFNames=B0025.1 {ECO:0000312|WormBase:B0025.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:CAA73142.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=11927551; DOI=10.1093/emboj/21.7.1673;
RA Roggo L., Bernard V., Kovacs A.L., Rose A.M., Savoy F., Zetka M.,
RA Wymann M.P., Mueller F.;
RT "Membrane transport in Caenorhabditis elegans: an essential role for VPS34
RT at the nuclear membrane.";
RL EMBO J. 21:1673-1683(2002).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH BEC-1.
RX PubMed=16111945; DOI=10.1016/j.cub.2005.07.035;
RA Takacs-Vellai K., Vellai T., Puoti A., Passannante M., Wicky C., Streit A.,
RA Kovacs A.L., Mueller F.;
RT "Inactivation of the autophagy gene bec-1 triggers apoptotic cell death in
RT C. elegans.";
RL Curr. Biol. 15:1513-1517(2005).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=15843430; DOI=10.1091/mbc.e05-01-0060;
RA Hermann G.J., Schroeder L.K., Hieb C.A., Kershner A.M., Rabbitts B.M.,
RA Fonarev P., Grant B.D., Priess J.R.;
RT "Genetic analysis of lysosomal trafficking in Caenorhabditis elegans.";
RL Mol. Biol. Cell 16:3273-3288(2005).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DYN-1, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18425118; DOI=10.1038/ncb1718;
RA Kinchen J.M., Doukoumetzidis K., Almendinger J., Stergiou L.,
RA Tosello-Trampont A., Sifri C.D., Hengartner M.O., Ravichandran K.S.;
RT "A pathway for phagosome maturation during engulfment of apoptotic cells.";
RL Nat. Cell Biol. 10:556-566(2008).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21183797; DOI=10.4161/auto.7.4.14391;
RA Ruck A., Attonito J., Garces K.T., Nunez L., Palmisano N.J., Rubel Z.,
RA Bai Z., Nguyen K.C., Sun L., Grant B.D., Hall D.H., Melendez A.;
RT "The Atg6/Vps30/Beclin 1 ortholog BEC-1 mediates endocytic retrograde
RT transport in addition to autophagy in C. elegans.";
RL Autophagy 7:386-400(2011).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22272187; DOI=10.1371/journal.pbio.1001245;
RA Lu N., Shen Q., Mahoney T.R., Neukomm L.J., Wang Y., Zhou Z.;
RT "Two PI 3-kinases and one PI 3-phosphatase together establish the cyclic
RT waves of phagosomal PtdIns(3)P critical for the degradation of apoptotic
RT cells.";
RL PLoS Biol. 10:E1001245-E1001245(2012).
RN [8]
RP INTERACTION WITH BEC-1.
RX PubMed=26783301; DOI=10.1083/jcb.201506081;
RA Liu K., Jian Y., Sun X., Yang C., Gao Z., Zhang Z., Liu X., Li Y., Xu J.,
RA Jing Y., Mitani S., He S., Yang C.;
RT "Negative regulation of phosphatidylinositol 3-phosphate levels in early-
RT to-late endosome conversion.";
RL J. Cell Biol. 212:181-198(2016).
RN [9]
RP ERRATUM OF PUBMED:26783301.
RX PubMed=26975852; DOI=10.1083/jcb.20150608103012016c;
RA Liu K., Jian Y., Sun X., Yang C., Gao Z., Zhang Z., Liu X., Li Y., Xu J.,
RA Jing Y., Mitani S., He S., Yang C.;
RT "Correction: Negative regulation of phosphatidylinositol 3-phosphate levels
RT in early-to-late endosome conversion.";
RL J. Cell Biol. 212:739-739(2016).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28285998; DOI=10.1016/j.cub.2017.02.015;
RA Ames K., Da Cunha D.S., Gonzalez B., Konta M., Lin F., Shechter G.,
RA Starikov L., Wong S., Buelow H.E., Melendez A.;
RT "A Non-Cell-Autonomous Role of BEC-1/BECN1/Beclin1 in Coordinating Cell-
RT Cycle Progression and Stem Cell Proliferation during Germline
RT Development.";
RL Curr. Biol. 27:905-913(2017).
CC -!- FUNCTION: Catalytic subunit of the PI3K complex that mediates formation
CC of phosphatidylinositol 3-phosphate (PubMed:11927551). Together with
CC bec-1, mediates the production of phosphatidylinositol 3-phosphate on
CC intracellular vesicles and thereby regulates membrane trafficking
CC (PubMed:11927551, PubMed:16111945). Plays a role in endosome-to-Golgi
CC retrograde transport of mig-14 (PubMed:21183797). Involved in clearance
CC of apoptotic cell corpses by phagosomes (PubMed:22272187). Phagosome
CC maturation requires two sequential and non-overlapping pulses of
CC phosphatidylinositol-3-phosphate (PI3P) on the vesicle surface which
CC mediates recruitment of sortins snx-1 and lst-4 and small GTPases rab-
CC 5, rab-2 and rab-7, downstream of dynamin dyn-1 (PubMed:22272187,
CC PubMed:18425118). The first pulse is initiated by piki-1, then
CC maintained by vps-34 which also produces the second pulse
CC (PubMed:22272187). Required for embryonic development
CC (PubMed:22272187). Together with bec-1, involved in L3/L4 larval
CC molting stage probably by regulating cuticle shedding
CC (PubMed:11927551). Regulates the expansion of the nucleus outer
CC membrane (PubMed:11927551). Involved in the secretion and localization
CC of lrp-1 at the apical surface of hyp7 syncytium (PubMed:16111945). May
CC regulate endocytosis in hypodermal cells (PubMed:11927551). May play a
CC role in the formation of gut granules (a lysosome-related organelle)
CC (PubMed:15843430). Plays a role in germ stem cell proliferation during
CC larval development (PubMed:28285998). {ECO:0000269|PubMed:11927551,
CC ECO:0000269|PubMed:15843430, ECO:0000269|PubMed:16111945,
CC ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:21183797,
CC ECO:0000269|PubMed:22272187, ECO:0000269|PubMed:28285998}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000255|PIRNR:PIRNR000587,
CC ECO:0000269|PubMed:11927551};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11927551};
CC -!- ACTIVITY REGULATION: Inhibited by wortmannin.
CC {ECO:0000269|PubMed:11927551}.
CC -!- SUBUNIT: Interacts with bec-1 (PubMed:16111945, PubMed:26783301). May
CC interact with dyn-1 (PubMed:18425118). {ECO:0000269|PubMed:16111945,
CC ECO:0000269|PubMed:26783301, ECO:0000305|PubMed:18425118}.
CC -!- INTERACTION:
CC Q9TXI7; Q22592: bec-1; NbExp=2; IntAct=EBI-21398789, EBI-2413500;
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC {ECO:0000269|PubMed:11927551}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11927551}. Cytoplasm {ECO:0000269|PubMed:11927551}.
CC Cytoplasmic granule {ECO:0000269|PubMed:11927551}. Cell projection,
CC phagocytic cup {ECO:0000269|PubMed:18425118}. Note=Colocalizes with
CC rab-5 and dyn-1 at the phagocytic cup. {ECO:0000269|PubMed:18425118}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:B0025.1a};
CC IsoId=Q9TXI7-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:B0025.1b};
CC IsoId=Q9TXI7-2; Sequence=VSP_058340;
CC Name=c {ECO:0000312|WormBase:B0025.1c};
CC IsoId=Q9TXI7-3; Sequence=VSP_058341;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11927551}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in embryos and at L2 larval
CC stage, and to a lower extent in subsequent larval stages and in adults.
CC {ECO:0000269|PubMed:11927551}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a defect in the
CC clearance of apoptotic cell corpses in gonads, a loss of rab-5
CC recruitment to cell corpse-containing nascent phagosomes and a decrease
CC in PI3P levels on phagosome membranes (PubMed:18425118,
CC PubMed:22272187). In addition, causes a reduction in mig-14 and rme-8
CC association with puncta structures as well as an increase in mig-14
CC protein levels (PubMed:21183797). RNAi-mediated knockdown results in
CC reduced germ stem cell proliferation during larval development
CC (PubMed:28285998). {ECO:0000269|PubMed:18425118,
CC ECO:0000269|PubMed:21183797, ECO:0000269|PubMed:22272187,
CC ECO:0000269|PubMed:28285998}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000255|PIRNR:PIRNR000587}.
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; Y12543; CAA73142.1; -; mRNA.
DR EMBL; BX284601; CCD61194.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD61195.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD61196.1; -; Genomic_DNA.
DR PIR; T43628; T43628.
DR RefSeq; NP_001020953.1; NM_001025782.2.
DR RefSeq; NP_001020954.1; NM_001025783.2.
DR RefSeq; NP_491741.1; NM_059340.4. [Q9TXI7-1]
DR AlphaFoldDB; Q9TXI7; -.
DR SMR; Q9TXI7; -.
DR IntAct; Q9TXI7; 1.
DR STRING; 6239.B0025.1a; -.
DR EPD; Q9TXI7; -.
DR PaxDb; Q9TXI7; -.
DR PeptideAtlas; Q9TXI7; -.
DR EnsemblMetazoa; B0025.1a.1; B0025.1a.1; WBGene00006932. [Q9TXI7-1]
DR EnsemblMetazoa; B0025.1c.1; B0025.1c.1; WBGene00006932. [Q9TXI7-3]
DR GeneID; 172280; -.
DR KEGG; cel:CELE_B0025.1; -.
DR UCSC; B0025.1b.2; c. elegans.
DR CTD; 172280; -.
DR WormBase; B0025.1a; CE24759; WBGene00006932; vps-34. [Q9TXI7-1]
DR WormBase; B0025.1b; CE24760; WBGene00006932; vps-34. [Q9TXI7-2]
DR WormBase; B0025.1c; CE37691; WBGene00006932; vps-34. [Q9TXI7-3]
DR eggNOG; KOG0906; Eukaryota.
DR GeneTree; ENSGT00940000156943; -.
DR HOGENOM; CLU_004869_0_0_1; -.
DR InParanoid; Q9TXI7; -.
DR OMA; GRQKCKI; -.
DR OrthoDB; 204282at2759; -.
DR PhylomeDB; Q9TXI7; -.
DR Reactome; R-CEL-1632852; Macroautophagy.
DR Reactome; R-CEL-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-CEL-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-CEL-1660517; Synthesis of PIPs at the late endosome membrane.
DR Reactome; R-CEL-5668599; RHO GTPases Activate NADPH Oxidases.
DR PRO; PR:Q9TXI7; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006932; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:WormBase.
DR GO; GO:0005730; C:nucleolus; IDA:WormBase.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR GO; GO:0042395; P:ecdysis, collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:WormBase.
DR GO; GO:0090386; P:phagosome maturation involved in apoptotic cell clearance; IMP:WormBase.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IDA:WormBase.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:WormBase.
DR GO; GO:0061365; P:positive regulation of triglyceride lipase activity; IMP:WormBase.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:WormBase.
DR GO; GO:0051036; P:regulation of endosome size; IGI:UniProtKB.
DR GO; GO:0050708; P:regulation of protein secretion; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR008290; PI3K_Vps34.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 2.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cytoplasm; Endocytosis;
KW Kinase; Lipid biosynthesis; Lipid metabolism; Membrane; Nucleotide-binding;
KW Nucleus; Phagocytosis; Reference proteome; Transferase.
FT CHAIN 1..901
FT /note="Phosphatidylinositol 3-kinase catalytic subunit type
FT 3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436297"
FT DOMAIN 21..189
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 302..527
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 607..886
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 613..619
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 755..763
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 774..795
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT VAR_SEQ 1..251
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058340"
FT VAR_SEQ 1..4
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058341"
FT CONFLICT 8
FT /note="T -> R (in Ref. 1; CAA73142)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="D -> H (in Ref. 1; CAA73142)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="P -> A (in Ref. 1; CAA73142)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="E -> A (in Ref. 1; CAA73142)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="D -> H (in Ref. 1; CAA73142)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="E -> D (in Ref. 1; CAA73142)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="E -> A (in Ref. 1; CAA73142)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="C -> R (in Ref. 1; CAA73142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 901 AA; 103059 MW; 3B490B64FD3F5E78 CRC64;
MIPGMRATPT ESFSFVYSCD LQTNVQVKVA EFEGIFRDVL NPVRRLNQLF AEITVYCNNQ
QIGYPVCTSF HTPPDSSQLA RQKLIQKWNE WLTLPIRYSD LSRDAFLHIT IWEHEDDEIV
NNSTFSRRLV AQSKLSMFSK RGILKSGVID VQMNVSTTPD PFVKQPETWK YSDAWGDEID
LLFKQVTRQS RGLVEDVPWL DPFASRRIEM IRAKYKYSSP DRHVFLVLEM AAIRLGPTFY
KVVYYEDETK NMRVSTSVNG GVGIVSACTR YCVADPELLL ESLAEVKHSA MTRRIRDVED
ERHRQVKPNK QAKDRLETIV NLPSSQVLTR EQRDLVWKFR HYLRQFPKAL NKYLRSVNWV
HPQEVKTALA LMNDWELIEA EDALELLSSA FTHPAVRAYS VSRLLEAASP EQVLLYLPQL
VQALKYEQGQ QLPEEGNPVP VVSEEEGKIP SVATTPTEEL EGRDMTVVTK KEARKAASGD
LATFLIDYAL ASPKVSNYLY WHLKTEIEST KESKEEHSKM YQNIQDRLME ALVKRPDTRA
QVDSLHQQQI FVEDLIILMN EAKARGGRLN ESKSAEFRTM LSRAKHMLDL KGVHLPLDPS
FRLSSVIPDT ASFFKSEMMP AKISFKVLQP NGKADRNIPE EYTVIFKTGD DLRQDQLIQQ
MVRLIDIILK KGQLDLKLTP YLVLSTGVGQ GFVQCIKSKP LRAIQEQYKA HKMDCIREAM
KELRPGDGPF GIEPNVIDNY VRSLAGYSVI MYILGLGDRH LDNLLLCENG KLFHVDFGFI
LGRDPKPMPP PMKLTSEMVQ VMGGVKSKQF LEFVQHVDSA YRILRRHSNV LLNLFSLMLD
AGIPDIAAEP DKAIFKIEQR LRLDLSDEAA TKHIFTQIES SLNAKMAMIS DIIHAYKQNL
M
