PKHG3_MOUSE
ID PKHG3_MOUSE Reviewed; 1341 AA.
AC Q4VAC9; E9QL46; Q3TSI8; Q6A041; Q8BJP5; Q8K0L5; Q8K0T6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Pleckstrin homology domain-containing family G member 3;
DE Short=PH domain-containing family G member 3 {ECO:0000305};
GN Name=Plekhg3 {ECO:0000312|MGI:MGI:2388284}; Synonyms=Kiaa0599;
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] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-697 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Muellerian duct;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
RC STRAIN=FVB/N; TISSUE=Eye, Kidney, and Salivary 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 580-1341.
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-571, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433; SER-502; SER-571;
RP SER-737; SER-762; SER-766; SER-899; SER-900; SER-1134; SER-1136; SER-1141;
RP SER-1155 AND SER-1158, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, 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).
CC -!- FUNCTION: Plays a role in controlling cell polarity and cell motility
CC by selectively binding newly polymerized actin and activating RAC1 and
CC CDC42 to enhance local actin polymerization.
CC {ECO:0000250|UniProtKB:A1L390}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:A1L390}. Note=Colocalizes with actin at the
CC leading edge of polarized cells. {ECO:0000250|UniProtKB:A1L390}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q4VAC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4VAC9-2; Sequence=VSP_028540, VSP_028541;
CC Name=3;
CC IsoId=Q4VAC9-3; Sequence=VSP_028539, VSP_028542;
CC Name=4;
CC IsoId=Q4VAC9-4; Sequence=VSP_028536, VSP_028537, VSP_028538;
CC Name=5;
CC IsoId=Q4VAC9-5; Sequence=VSP_028535;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE36687.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK080928; BAC38083.1; -; mRNA.
DR EMBL; AK162025; BAE36687.1; ALT_INIT; mRNA.
DR EMBL; AC163033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030417; AAH30417.1; -; mRNA.
DR EMBL; BC031136; AAH31136.1; -; mRNA.
DR EMBL; BC049264; AAH49264.1; -; mRNA.
DR EMBL; BC096443; AAH96443.1; -; mRNA.
DR EMBL; AK172977; BAD32255.1; -; mRNA.
DR CCDS; CCDS25994.1; -. [Q4VAC9-1]
DR RefSeq; NP_722499.4; NM_153804.4. [Q4VAC9-1]
DR RefSeq; XP_006515938.1; XM_006515875.3. [Q4VAC9-2]
DR AlphaFoldDB; Q4VAC9; -.
DR SMR; Q4VAC9; -.
DR BioGRID; 234453; 1.
DR DIP; DIP-49616N; -.
DR IntAct; Q4VAC9; 2.
DR STRING; 10090.ENSMUSP00000074729; -.
DR iPTMnet; Q4VAC9; -.
DR PhosphoSitePlus; Q4VAC9; -.
DR jPOST; Q4VAC9; -.
DR MaxQB; Q4VAC9; -.
DR PaxDb; Q4VAC9; -.
DR PeptideAtlas; Q4VAC9; -.
DR PRIDE; Q4VAC9; -.
DR ProteomicsDB; 288225; -. [Q4VAC9-1]
DR ProteomicsDB; 288226; -. [Q4VAC9-2]
DR ProteomicsDB; 288227; -. [Q4VAC9-3]
DR ProteomicsDB; 288228; -. [Q4VAC9-4]
DR ProteomicsDB; 288229; -. [Q4VAC9-5]
DR Antibodypedia; 57155; 79 antibodies from 11 providers.
DR DNASU; 263406; -.
DR Ensembl; ENSMUST00000075249; ENSMUSP00000074729; ENSMUSG00000052609. [Q4VAC9-1]
DR Ensembl; ENSMUST00000219063; ENSMUSP00000151851; ENSMUSG00000052609. [Q4VAC9-2]
DR GeneID; 263406; -.
DR KEGG; mmu:263406; -.
DR UCSC; uc007nyi.2; mouse. [Q4VAC9-3]
DR UCSC; uc007nyj.2; mouse. [Q4VAC9-2]
DR UCSC; uc007nyk.2; mouse. [Q4VAC9-1]
DR UCSC; uc029rtp.1; mouse. [Q4VAC9-4]
DR CTD; 26030; -.
DR MGI; MGI:2388284; Plekhg3.
DR VEuPathDB; HostDB:ENSMUSG00000052609; -.
DR eggNOG; KOG3518; Eukaryota.
DR GeneTree; ENSGT00940000156521; -.
DR HOGENOM; CLU_007600_0_0_1; -.
DR InParanoid; Q4VAC9; -.
DR OMA; IMQLSHV; -.
DR PhylomeDB; Q4VAC9; -.
DR TreeFam; TF328565; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 263406; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Plekhg3; mouse.
DR PRO; PR:Q4VAC9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q4VAC9; protein.
DR Bgee; ENSMUSG00000052609; Expressed in ascending aorta and 190 other tissues.
DR ExpressionAtlas; Q4VAC9; baseline and differential.
DR Genevisible; Q4VAC9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR CDD; cd13243; PH_PLEKHG1_G2_G3; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR043324; PH_PLEKHG1_G2_G3.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1341
FT /note="Pleckstrin homology domain-containing family G
FT member 3"
FT /id="PRO_0000306864"
FT DOMAIN 93..272
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 296..394
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..707
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L390"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L390"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L390"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L390"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L390"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L390"
FT MOD_RES 1129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L390"
FT MOD_RES 1134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L390"
FT VAR_SEQ 1..613
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028535"
FT VAR_SEQ 1..197
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028536"
FT VAR_SEQ 416..431
FT /note="YPSRYRCSPERMKKAW -> CKLPFSACFIPNCVHG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028537"
FT VAR_SEQ 432..1341
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028538"
FT VAR_SEQ 449..627
FT /note="EPGHTLFSRATLPSRQQGFEMPGLKGRRKSEPTRHLLRQLSEKARAVGMKHA
FT GSAGALLDFGQPAHAQKQQPEAERAAREELEEEEELVEEEEQRQQSFSGSLEGLAGHDG
FT SEKVPGPELPGSEEEEEEEESLAVAEQGKRHRESEGSKGCRRPSNRSPTSAEKRMSFES
FT VSSLPEVET -> GEGRAVWTRTFFLGSLAQAGIICSDIVGRWSLQKAGEDSRVGWWMS
FT VDRFLFMPGFPSNNHLLCLLLTRAVHLLKGLGMFVIQDLASLLSHLNLLALLLSQSSTW
FT KSWDSFSVQVSSDSRGWVGGKTLRPSGTKSRQEIFILGHAIFLSWVFFHDGICLCARGV
FT IRMKRLLREDKNLAL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028539"
FT VAR_SEQ 451..480
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028540"
FT VAR_SEQ 586
FT /note="Q -> QVADFASSLLAALHCWHYRANALLFSRGAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028541"
FT VAR_SEQ 628..1341
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028542"
FT CONFLICT 203
FT /note="Q -> K (in Ref. 1; BAE36687)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="H -> Q (in Ref. 1; BAE36687)"
FT /evidence="ECO:0000305"
FT CONFLICT 580..585
FT /note="SLAVAE -> ADFCLL (in Ref. 4; BAD32255)"
FT /evidence="ECO:0000305"
FT CONFLICT 929
FT /note="C -> R (in Ref. 3; AAH96443/AAH31136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1341 AA; 148519 MW; FFB1EDA92BF6E197 CRC64;
MPVSTALHQD GSQERPRSLV STTSSSGSSR DSHSAMEEPT GSEASAQNGT GSPWDRHVPN
SNNNSSGWLN MKGPLSPFNG RAGTSPAYHK LSYLGRVVRE IVETERMYVQ DLRSIVEDYL
LKIIDTPGLL KPEQVSALFG NIESIYALNS QLLRDLDSCN SDPVAVASCF VERSQEFDIY
TQYCNNYPNS VAALTECMQD KQQAKFFRDR QELLQHSLPL GSYLLKPVQR VLKYHLLLQE
IAKHFDEEED GFEVVEDAID TMTCVAWYIN DMKRRHEHAV RLQEIQSLLI NWKGPDLTTY
GELVLEATFR VHRVRNDRTF FLFDKILLIT KKRGDHFVYK GHIPCSSLML IESTRDSLCF
TVTHYKHSKQ QYSIQAKTVE EKRSWTHHIK RLILENHHAT IPQKAKEAIL EMDSYYPSRY
RCSPERMKKA WSSQDEVSSH VRQGRRQSEP GHTLFSRATL PSRQQGFEMP GLKGRRKSEP
TRHLLRQLSE KARAVGMKHA GSAGALLDFG QPAHAQKQQP EAERAAREEL EEEEELVEEE
EQRQQSFSGS LEGLAGHDGS EKVPGPELPG SEEEEEEEES LAVAEQGKRH RESEGSKGCR
RPSNRSPTSA EKRMSFESVS SLPEVETDPE PGAEQEAFAA LEGPSTEEMP SDPEFPEALE
TQLHAPKGLL GVDNPAAVVD FVEPEGSEDL KPLSSEEEEE EEMEAAQEPE SLLPPSVLDQ
ASVIAERFAS SFSRRSSLAI EDGKSSGLGT PRLISRSSSV LSLEGSDKGL ARWSSIGDSL
SNPPTPEVII GADMVTDNGP SVNGTESPSA GSGCPTEQDR SSCKKKESAL STRDRQLLDK
IKNYYENAEH HDAGFSIRRR ESLSYIPKGL VRSSVSRFNS LPKPDSEPAA PVGYKRPGSS
RPASWTLFDL PGPRTDKGDP APITDAEFCP SSEIAKIWER MESSERSPRT GSGQSQANGF
ELQEPLFILE EHELGAITEE SAVASPESAS PTEQPSPAHL ARELKELVKE LSSSVQGELV
TPLHPRIVQL SHVMDSHVSE RVKNKVYQLA RQYSLRIKNI KAARPPLQWE KVTPDQEEQV
PSISGLPEEA GELSGGKARR KPVLSLLSYE QLVAQEHGTS KSSAAVETSP RRFSFSPSAV
SPRTTSPGAR SSARSPLSPF DTETFNWPDV RELCSKYTSH DKTAQVESSW PRSLLVNRSR
SLPENIVEPP MSGKADRCCG LNTHRRLGDG EASQPPLPES PPQSQLNGGD ALYVTADLTL
ENNQRVIIME KGPHPSSTVG LEEDSGKESS SPVALKGQGQ GFQASAEYQP KEHGPRDSAD
TNKQGRVRNL REKFQALNSV G
