PK3C3_MOUSE
ID PK3C3_MOUSE Reviewed; 887 AA.
AC Q6PF93; Q8R3S8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3;
DE Short=PI3-kinase type 3;
DE Short=PI3K type 3;
DE Short=PtdIns-3-kinase type 3;
DE EC=2.7.1.137 {ECO:0000250|UniProtKB:Q8NEB9};
DE AltName: Full=Phosphoinositide-3-kinase class 3;
GN Name=Pik3c3 {ECO:0000312|MGI:MGI:2445019};
GN Synonyms=Vps34 {ECO:0000303|PubMed:23332761};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland;
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 [2]
RP INTERACTION WITH BECN1 AND AMBRA1.
RX PubMed=17589504; DOI=10.1038/nature05925;
RA Maria Fimia G., Stoykova A., Romagnoli A., Giunta L., Di Bartolomeo S.,
RA Nardacci R., Corazzari M., Fuoco C., Ucar A., Schwartz P., Gruss P.,
RA Piacentini M., Chowdhury K., Cecconi F.;
RT "Ambra1 regulates autophagy and development of the nervous system.";
RL Nature 447:1121-1125(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH PIK3R4 AND PIK3CB.
RX PubMed=21059846; DOI=10.1083/jcb.201006056;
RA Dou Z., Chattopadhyay M., Pan J.-A., Guerriero J.L., Jiang Y.-P.,
RA Ballou L.M., Yue Z., Lin R.Z., Zong W.-X.;
RT "The class IA phosphatidylinositol 3-kinase p110-beta subunit is a positive
RT regulator of autophagy.";
RL J. Cell Biol. 191:827-843(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SLAMF1.
RX PubMed=22493499; DOI=10.1074/jbc.m112.367060;
RA Ma C., Wang N., Detre C., Wang G., O'Keeffe M., Terhorst C.;
RT "Receptor signaling lymphocyte-activation molecule family 1 (Slamf1)
RT regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by recruiting
RT a Beclin-1/Vps34/ultraviolet radiation resistance-associated gene (UVRAG)
RT complex.";
RL J. Biol. Chem. 287:18359-18365(2012).
RN [6]
RP PHOSPHORYLATION AT THR-163 AND SER-165, MUTAGENESIS OF THR-163 AND SER-165,
RP AND IDENTIFICATION IN A COMPLEX WITH PIK3R4; BECN1; UVRAG AND ATG14.
RX PubMed=23332761; DOI=10.1016/j.cell.2012.12.016;
RA Kim J., Kim Y.C., Fang C., Russell R.C., Kim J.H., Fan W., Liu R.,
RA Zhong Q., Guan K.L.;
RT "Differential regulation of distinct Vps34 complexes by AMPK in nutrient
RT stress and autophagy.";
RL Cell 152:290-303(2013).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=24089209; DOI=10.1038/nature12639;
RA Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I.,
RA Codogno P., Satir B.H., Satir P., Cuervo A.M.;
RT "Functional interaction between autophagy and ciliogenesis.";
RL Nature 502:194-200(2013).
CC -!- FUNCTION: Catalytic subunit of the PI3K complex that mediates formation
CC of phosphatidylinositol 3-phosphate; different complex forms are
CC believed to play a role in multiple membrane trafficking pathways:
CC PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in
CC maturation of autophagosomes and endocytosis. As part of PI3KC3-C1,
CC promotes endoplasmic reticulum membrane curvature formation prior to
CC vesicle budding. Involved in regulation of degradative endocytic
CC trafficking and required for the abcission step in cytokinesis,
CC probably in the context of PI3KC3-C2. Involved in the transport of
CC lysosomal enzyme precursors to lysosomes. Required for transport from
CC early to late endosomes (By similarity). {ECO:0000250|UniProtKB:O88763,
CC ECO:0000250|UniProtKB:Q8NEB9}.
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:0000250|UniProtKB:Q8NEB9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB9};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8NEB9};
CC -!- SUBUNIT: Component of the PI3K (PI3KC3/PI3K-III/class III
CC phosphatidylinositol 3-kinase) complex the core of which is composed of
CC the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 and BECN1
CC associating with additional regulatory/auxilliary subunits to form
CC alternative complex forms. Alternative complex forms containing a forth
CC regulatory subunit in a mutually exclusive manner are: the PI3K complex
CC I (PI3KC3-C1) containing ATG14, and the PI3K complex II (PI3KC3-C2)
CC containing UVRAG. PI3KC3-C1 displays a V-shaped architecture with
CC PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1
CC subcomplex (By similarity). Both, PI3KC3-C1 and PI3KC3-C2, can
CC associate with further regulatory subunits such as RUBCN, SH3GLB1/Bif-1
CC and AMBRA1 (PubMed:17589504). PI3KC3-C1 probably associates with PIK3CB
CC (PubMed:21059846). Interacts with RAB7A in the presence of PIK3R4 (By
CC similarity). Interacts with AMBRA1 (PubMed:17589504). Interacts with
CC BECN1P1/BECN2 (By similarity). Interacts with SLAMF1 (PubMed:22493499).
CC May be a component of a complex composed of RAB5A (in GDP-bound form),
CC DYN2 and PIK3C3 (By similarity). Interacts with NCKAP1L (By
CC similarity). Interacts with ATG14; this interaction is increased in the
CC absence of TMEM39A (By similarity). Interacts with STEEP1; the
CC interaction is STING1-dependent and required for trafficking of STING1
CC from the endoplasmic reticulum (By similarity). Interacts with YWHAG
CC (By similarity). {ECO:0000250|UniProtKB:Q8NEB9,
CC ECO:0000250|UniProtKB:Q9TXI7, ECO:0000269|PubMed:17589504,
CC ECO:0000269|PubMed:21059846, ECO:0000269|PubMed:23332761}.
CC -!- INTERACTION:
CC Q6PF93; O88597: Becn1; NbExp=6; IntAct=EBI-6678149, EBI-643716;
CC Q6PF93; P23242: Gja1; NbExp=4; IntAct=EBI-6678149, EBI-298630;
CC -!- SUBCELLULAR LOCATION: Midbody {ECO:0000250|UniProtKB:Q8NEB9}. Late
CC endosome {ECO:0000250|UniProtKB:Q8NEB9}. Cytoplasmic vesicle,
CC autophagosome {ECO:0000269|PubMed:22493499}. Note=As component of the
CC PI3K complex I localized to pre-autophagosome structures. As component
CC of the PI3K complex II localized predominantly to endosomes (By
CC similarity). Localizes also to discrete punctae along the ciliary
CC axoneme and to the base of the ciliary axoneme (PubMed:24089209).
CC {ECO:0000250|UniProtKB:Q8NEB9, ECO:0000269|PubMed:24089209}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PF93-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PF93-2; Sequence=VSP_016459, VSP_016460;
CC -!- PTM: Ubiquitinated via 'Lys-29'- and 'Lys-48'-linked ubiquitination by
CC UBE3C, promoting its degradation. Deubiquitination by ZRANB1/TRABID
CC promotes its stabilization, leading to autophagosome maturation.
CC {ECO:0000250|UniProtKB:Q8NEB9}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00880}.
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DR EMBL; BC024675; AAH24675.1; -; mRNA.
DR EMBL; BC057678; AAH57678.1; -; mRNA.
DR CCDS; CCDS37752.1; -. [Q6PF93-1]
DR RefSeq; NP_852079.2; NM_181414.5. [Q6PF93-1]
DR AlphaFoldDB; Q6PF93; -.
DR SMR; Q6PF93; -.
DR BioGRID; 230382; 21.
DR ComplexPortal; CPX-75; Phosphatidylinositol 3-kinase complex, class III, ATG14 variant.
DR ComplexPortal; CPX-76; Phosphatidylinositol 3-kinase complex, class III, UVRAG variant.
DR CORUM; Q6PF93; -.
DR DIP; DIP-57222N; -.
DR IntAct; Q6PF93; 8.
DR MINT; Q6PF93; -.
DR STRING; 10090.ENSMUSP00000111479; -.
DR iPTMnet; Q6PF93; -.
DR PhosphoSitePlus; Q6PF93; -.
DR EPD; Q6PF93; -.
DR jPOST; Q6PF93; -.
DR MaxQB; Q6PF93; -.
DR PaxDb; Q6PF93; -.
DR PRIDE; Q6PF93; -.
DR ProteomicsDB; 289434; -. [Q6PF93-1]
DR ProteomicsDB; 289435; -. [Q6PF93-2]
DR Antibodypedia; 22392; 952 antibodies from 39 providers.
DR DNASU; 225326; -.
DR Ensembl; ENSMUST00000115812; ENSMUSP00000111479; ENSMUSG00000033628. [Q6PF93-1]
DR GeneID; 225326; -.
DR KEGG; mmu:225326; -.
DR UCSC; uc008ehw.1; mouse. [Q6PF93-1]
DR CTD; 5289; -.
DR MGI; MGI:2445019; Pik3c3.
DR VEuPathDB; HostDB:ENSMUSG00000033628; -.
DR eggNOG; KOG0906; Eukaryota.
DR GeneTree; ENSGT00940000156943; -.
DR HOGENOM; CLU_004869_0_0_1; -.
DR InParanoid; Q6PF93; -.
DR OMA; GRQKCKI; -.
DR OrthoDB; 204282at2759; -.
DR PhylomeDB; Q6PF93; -.
DR TreeFam; TF102032; -.
DR BRENDA; 2.7.1.137; 3474.
DR Reactome; R-MMU-109704; PI3K Cascade.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-MMU-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-MMU-1660517; Synthesis of PIPs at the late endosome membrane.
DR Reactome; R-MMU-168138; Toll Like Receptor 9 (TLR9) Cascade.
DR Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
DR BioGRID-ORCS; 225326; 32 hits in 75 CRISPR screens.
DR ChiTaRS; Pik3c3; mouse.
DR PRO; PR:Q6PF93; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q6PF93; protein.
DR Bgee; ENSMUSG00000033628; Expressed in orbitosphenoid and 284 other tissues.
DR ExpressionAtlas; Q6PF93; baseline and differential.
DR Genevisible; Q6PF93; MM.
DR GO; GO:0044754; C:autolysosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; IDA:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0035004; F:phosphatidylinositol 3-kinase activity; ISO:MGI.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IMP:MGI.
DR GO; GO:0000045; P:autophagosome assembly; IMP:MGI.
DR GO; GO:0097352; P:autophagosome maturation; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IMP:MGI.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; ISO:MGI.
DR GO; GO:0016236; P:macroautophagy; IMP:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IMP:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
DR GO; GO:0006497; P:protein lipidation; ISO:MGI.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR GO; GO:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0006622; P:protein targeting to lysosome; IC:ComplexPortal.
DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0016241; P:regulation of macroautophagy; ISO:MGI.
DR GO; GO:0050708; P:regulation of protein secretion; ISO:MGI.
DR GO; GO:0043201; P:response to leucine; IEA:Ensembl.
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; 1.
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; Autophagy; Cell cycle; Cell division;
KW Cytoplasmic vesicle; Endosome; Kinase; Lipid metabolism; Manganese;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation.
FT CHAIN 1..887
FT /note="Phosphatidylinositol 3-kinase catalytic subunit type
FT 3"
FT /id="PRO_0000088803"
FT DOMAIN 35..184
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 283..520
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 605..871
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 149..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..617
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 740..748
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 759..780
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 418..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 163
FT /note="Phosphothreonine; by AMPK"
FT /evidence="ECO:0000269|PubMed:23332761"
FT MOD_RES 165
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:23332761"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88763"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEB9"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEB9"
FT VAR_SEQ 842..848
FT /note="VQDKFRL -> ISCHRKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016459"
FT VAR_SEQ 849..887
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016460"
FT MUTAGEN 163
FT /note="T->A: Loss of phosphorylation but no loss of
FT autophagic function; when associated with A-165."
FT /evidence="ECO:0000269|PubMed:23332761"
FT MUTAGEN 165
FT /note="S->A: Loss of phosphorylation but no loss of
FT autophagic function; when associated with A-163."
FT /evidence="ECO:0000269|PubMed:23332761"
FT CONFLICT 455
FT /note="Missing (in Ref. 1; AAH57678)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="N -> S (in Ref. 1; AAH57678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 887 AA; 101487 MW; 80E8EF9EF3AF74D7 CRC64;
MGEAEKFHYI YSCDLDINVQ LKIGSLEGKR EQKSYKAVLE DPMLKFSGLY QETCSDLYVT
CQVFAEGKPL ALPVRTSYKA FSTRWNWNEW LKLPVKYPDL PRNAQVALTI WDVYGPGSAV
PVGGTTVSLF GKYGMFRQGM HDLKVWPNVE ADGSEPTRTP GRTSSTLSED QMSRLAKLTK
AHRQGHMVKV DWLDRLTFRE IEMINESEKR SSNFMYLMVE FRCVKCDDKE YGIVYYEKDG
DESSPILTSF ELVKVPDPQM SMENLVESKH HKLARSLRSG PSDHDLKPNA TTRDQLNIIV
SYPPTKQLTY EEQDLVWKFR YYLTNQEKAL TKFLKCVNWD LPQEAKQALE LLGKWKPMDV
EDSLELLSSH YTNPTVRRYA VARLRQADDE DLLMYLLQLV QALKYENFDD IKNGLEPTKK
DSQTSASESL SNSGVSSGDI DSSQIITNPL PPVASPPPAS KAKEVSDGEN LEQDLCTFLI
SRACKNSTLA NYLYWYVIVE CEDQDTQQRD PKTHEMYLNV MRRFSQALLK GDKSVRVMRS
LLAAQQTFVD RLVHLMKAVQ RESGNRKKKN ERLQALLGDN EKMNLSDVEL IPLPLEPQVK
IRGIIPETAT LFKSALMPAQ LFFKTEDGGK YPVIFKHGDD LRQDQLILQI ISLMDKLLRK
ENLDLKLTPY KVLATSTKHG FMQFIQSVPV AEVLDTEGSI QNFFRKYAPS ETGPYGISAE
VMDTYVKSCA GYCVITYILG VGDRHLDNLL LTKTGKLFHI DFGYILGRDP KPLPPPMKLN
KEMVEGMGGT QSEQYQEFRK QCYTAFLHLR RYSNLILNLF SLMVDANIPD IALEPDKTVK
KVQDKFRLDL SDEEAVHYMQ SLIDESVHAL FAAVVEQIHK FAQYWRK
