PI3R4_MOUSE
ID PI3R4_MOUSE Reviewed; 1358 AA.
AC Q8VD65; Q56A65; Q8C948; Q8C9D7; Q9CVC5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Phosphoinositide 3-kinase regulatory subunit 4;
DE Short=PI3-kinase regulatory subunit 4;
DE EC=2.7.11.1;
GN Name=Pik3r4; Synonyms=Vps15 {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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-536 AND 1188-1358.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Stomach, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-638.
RC STRAIN=Czech II; TISSUE=Eye, and 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [5]
RP IDENTIFICATION IN A COMPLEX WITH PIK3C3 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 [6]
RP IDENTIFICATION IN A COMPLEX WITH PIK3C3; 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: Regulatory subunit of the PI3K complex that mediates
CC formation of phosphatidylinositol 3-phosphate; different complex forms
CC are 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. Involved in regulation of
CC degradative endocytic trafficking and cytokinesis, probably in the
CC context of PI3KC3-C2 (By similarity). {ECO:0000250|UniProtKB:Q99570}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
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 PI3K complex I
CC (PI3KC3-C1) containing ATG14, and PI3K complex II (PI3KC3-C2)
CC containing UVRAG (PubMed:23332761). PI3KC3-C1 displays a V-shaped
CC architecture with PIK3R4 serving as a bridge between PIK3C3 and the
CC ATG14:BECN1 subcomplex. Both, PI3KC3-C1 and PI3KC3-C2, can associate
CC with further regulatory subunits, such as RUBCN, SH3GLB1/Bif-1, AMBRA1
CC and NRBF2 (By similarity). PI3KC3-C1 probably associates with PIK3CB
CC (PubMed:21059846). Interacts with RAB7A in the presence of PIK3C3/VPS34
CC (By similarity). Interacts with NRBF2 (By similarity).
CC {ECO:0000250|UniProtKB:Q99570, ECO:0000269|PubMed:21059846,
CC ECO:0000269|PubMed:23332761}.
CC -!- INTERACTION:
CC Q8VD65; P23242: Gja1; NbExp=3; IntAct=EBI-6678184, EBI-298630;
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000250}. Cytoplasmic vesicle,
CC autophagosome {ECO:0000305}. Membrane {ECO:0000250|UniProtKB:Q99570};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q99570}. 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. Localizes
CC also to discrete punctae along the ciliary axoneme (PubMed:24089209).
CC {ECO:0000269|PubMed:24089209, ECO:0000305}.
CC -!- PTM: Myristoylated. {ECO:0000250}.
CC -!- PTM: Probably autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC157514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK008703; BAB25843.1; -; mRNA.
DR EMBL; AK042361; BAC31236.1; -; mRNA.
DR EMBL; AK042953; BAC31417.1; -; mRNA.
DR EMBL; AK087938; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC017537; AAH17537.1; -; mRNA.
DR EMBL; BC092149; AAH92149.1; -; mRNA.
DR CCDS; CCDS40753.1; -.
DR RefSeq; NP_001074778.1; NM_001081309.1.
DR AlphaFoldDB; Q8VD65; -.
DR SMR; Q8VD65; -.
DR BioGRID; 217660; 15.
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 DIP; DIP-57219N; -.
DR IntAct; Q8VD65; 7.
DR MINT; Q8VD65; -.
DR STRING; 10090.ENSMUSP00000067400; -.
DR iPTMnet; Q8VD65; -.
DR PhosphoSitePlus; Q8VD65; -.
DR EPD; Q8VD65; -.
DR MaxQB; Q8VD65; -.
DR PaxDb; Q8VD65; -.
DR PRIDE; Q8VD65; -.
DR ProteomicsDB; 289416; -.
DR Antibodypedia; 33331; 490 antibodies from 34 providers.
DR DNASU; 75669; -.
DR Ensembl; ENSMUST00000065778; ENSMUSP00000067400; ENSMUSG00000032571.
DR Ensembl; ENSMUST00000191268; ENSMUSP00000139427; ENSMUSG00000032571.
DR GeneID; 75669; -.
DR KEGG; mmu:75669; -.
DR UCSC; uc009rio.1; mouse.
DR CTD; 30849; -.
DR MGI; MGI:1922919; Pik3r4.
DR VEuPathDB; HostDB:ENSMUSG00000032571; -.
DR eggNOG; KOG1240; Eukaryota.
DR GeneTree; ENSGT00390000016225; -.
DR HOGENOM; CLU_001696_0_0_1; -.
DR InParanoid; Q8VD65; -.
DR OMA; RELILHM; -.
DR OrthoDB; 1312453at2759; -.
DR PhylomeDB; Q8VD65; -.
DR TreeFam; TF102034; -.
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; 75669; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Pik3r4; mouse.
DR PRO; PR:Q8VD65; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VD65; protein.
DR Bgee; ENSMUSG00000032571; Expressed in primary oocyte and 248 other tissues.
DR ExpressionAtlas; Q8VD65; baseline and differential.
DR Genevisible; Q8VD65; MM.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0071561; C:nucleus-vacuole junction; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; ISO:MGI.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0006622; P:protein targeting to lysosome; IC:ComplexPortal.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0032801; P:receptor catabolic process; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
DR GO; GO:0016241; P:regulation of macroautophagy; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045162; Vps15-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR17583; PTHR17583; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasmic vesicle; Endosome; Kinase; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99570"
FT CHAIN 2..1358
FT /note="Phosphoinositide 3-kinase regulatory subunit 4"
FT /id="PRO_0000086525"
FT DOMAIN 26..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 413..450
FT /note="HEAT 1"
FT REPEAT 458..495
FT /note="HEAT 2"
FT REPEAT 572..610
FT /note="HEAT 3"
FT REPEAT 612..648
FT /note="HEAT 4"
FT REPEAT 991..1030
FT /note="WD 1"
FT REPEAT 1040..1079
FT /note="WD 2"
FT REPEAT 1093..1134
FT /note="WD 3"
FT REPEAT 1139..1178
FT /note="WD 4"
FT REPEAT 1182..1223
FT /note="WD 5"
FT REPEAT 1237..1278
FT /note="WD 6"
FT REPEAT 1327..1358
FT /note="WD 7"
FT REGION 1307..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99570"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99570"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99570"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99570"
FT MOD_RES 1316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99570"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q99570"
FT CONFLICT 292..305
FT /note="QMINREPEKRLEAE -> MLQIRAIEFYLTMS (in Ref. 2;
FT BAC31236)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="P -> S (in Ref. 2; BAC31417)"
FT /evidence="ECO:0000305"
FT CONFLICT 529..603
FT /note="ELQALHEMVQQKVVTLLSDPENIVKQTLMESGITRLCVFFGRQKANDVLLSH
FT MITFLNDKNDWHLRGAFFDSIVG -> GCVTPLLKSPSFTPNRYWYLVKAVICDSLGK
FT (in Ref. 2; BAC31417)"
FT /evidence="ECO:0000305"
FT CONFLICT 529..559
FT /note="ELQALHEMVQQKVVTLLSDPENIVKQTLMES -> GCVTPLLKSPSFTPNRY
FT WYLVKAVICDSLG (in Ref. 2; BAC31417)"
FT /evidence="ECO:0000305"
FT CONFLICT 621..637
FT /note="QQGLSDAEEFVIVKALN -> HAPPVPVLGNRSCSGQQ (in Ref. 3;
FT AAH92149)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1358 AA; 152599 MW; 113FC5EBBDA01E19 CRC64;
MGNQLAGIAP SQILSVESYF SDIHDFEYDK SLGSTRFFKV ARAKHREGLV VVKVFAIQDP
TLPLTSYKQE LEELKIRLHS AQNCLPFQKA AEKASEKAAM LFRQYVRDNL YDRISTRPFL
NNIEKRWIAF QILTAVDQAH KSGVRHGDIK TENVMVTSWN WVLLTDFASF KPTYLPEDNP
ADFNYFFDTS RRRTCYIAPE RFVDGGMFAT ELEYMRDPST PLVDLNSNQR ARGELKRAMD
IFSAGCVIAE LFTEGVPLFD LSQLLAYRNG HFFPEQVLNK IEDRSIRDLV TQMINREPEK
RLEAEDYLKQ QRGNAFPEIF YTFLQPYMAQ FAKETFLSAD ERILVIRKDL GNIIHNLCGH
DLPEKAEGES RASGLVVLVS VITSCLQTLK SCDSKLAALE LILHLAPRLS VEILLDRITP
YLLHFSNDSV PRVRAEALRT LTKVLALVQE VPRNDVNIYP EYILPGIAHL AQDDATIVRL
AYAENIALLA ETALRFLELV QLKTLNMENE PDNEEVDEAT RPNGDYDTEL QALHEMVQQK
VVTLLSDPEN IVKQTLMESG ITRLCVFFGR QKANDVLLSH MITFLNDKND WHLRGAFFDS
IVGVAAYVGW QSSSILKPLL QQGLSDAEEF VIVKALNALT CMCQLGLLQK PHVYEFASDI
APFLCHPNLW IRYGAVGFIT VVAHQISTAD VYCKLMPYLD PYITQPVIQI ERKLVLLSVL
KEPVSRSIFD YALRSKDIAS LFRHLHMRQK KRNGSLLDCP PPEDPTIAQL LKKLLSQGMT
EEEEDKLLAL KDFMMKSNRA KANAVDQSHL HDSSQKGVID LAALGITGRQ VDLVKTKQEP
DEKRARKHVK QDSNVNEEWK SMFGSLEPPN IPQALPKTSD HEVVQPGKPP RSESSAGICV
PLSTSPQVSE AAHIPSKKPV IPVVSSTVLP STYQIRITTC KTELQQLIQQ KREQCNAERI
AKQMMENAEW ESKPPPPGWR PKGLLVAHLH EHKSAVNRIR VSDEHLLFAT CSNDGTVKIW
NSQKMEGKTT TTRSILTYSR IGGRVKTLTF CQGSHYLAIA SDNGAVQLLG IEASKLPKSP
KIHPLQSRIL DQKEDGCVVD MHHFNSGAQS VLAYATVNGS LVGWDLRSSS NAWTLKHDLK
SGLITSFAVD IHQCWLCIGT SSGAMACWDM RFQLPISSHC HPSRARIRRL SMHPLYQSWV
IAAVQGNNEV SMWDMETGDR RLTLWASSAP PLSELQPSPH SVHGIYCSPA DGNPILLTAG
SDMKIRFWDL VSPERSYVVA GSTGSPSVSY YKKIIEGTEV VQEIQNKQKV GPSDDTPRRG
PESLPVGHHD IITDIATFQT TQGFIVTASR DGIVKVWK
