PKHG2_HUMAN
ID PKHG2_HUMAN Reviewed; 1386 AA.
AC Q9H7P9; B8ZZK6; C9J0Y4; Q6DHV6; Q96BU2; Q96D18; Q9H699;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Pleckstrin homology domain-containing family G member 2;
DE Short=PH domain-containing family G member 2;
GN Name=PLEKHG2;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP LYS-992 AND ALA-1329.
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-1386 (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 396-1386 (ISOFORM 1), AND VARIANTS HIS-647;
RP LYS-992 AND ALA-1329.
RC TISSUE=Pancreas;
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 [5]
RP FUNCTION.
RX PubMed=18045877; DOI=10.1074/jbc.m707037200;
RA Ueda H., Nagae R., Kozawa M., Morishita R., Kimura S., Nagase T., Ohara O.,
RA Yoshida S., Asano T.;
RT "Heterotrimeric G protein betagamma subunits stimulate FLJ00018, a guanine
RT nucleotide exchange factor for Rac1 and Cdc42.";
RL J. Biol. Chem. 283:1946-1953(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445 AND SER-450, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; THR-445; SER-469;
RP SER-911; SER-1049; THR-1257; SER-1261 AND SER-1310, VARIANT [LARGE SCALE
RP ANALYSIS] ALA-1329, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION, INVOLVEMENT IN LDAMD, VARIANT LDAMD TRP-204, AND CHARACTERIZATION
RP OF VARIANT LDAMD TRP-204.
RX PubMed=26573021; DOI=10.1007/s10048-015-0464-y;
RA Edvardson S., Wang H., Dor T., Atawneh O., Yaacov B., Gartner J.,
RA Cinnamon Y., Chen S., Elpeleg O.;
RT "Microcephaly-dystonia due to mutated PLEKHG2 with impaired actin
RT polymerization.";
RL Neurogenetics 17:25-30(2016).
CC -!- FUNCTION: May be a transforming oncogene with exchange activity for
CC CDC42 (By similarity). May be a guanine-nucleotide exchange factor
CC (GEF) for RAC1 and CDC42. Activated by the binding to subunits beta and
CC gamma of the heterotrimeric guanine nucleotide-binding protein (G
CC protein) (PubMed:18045877). Involved in the regulation of actin
CC polymerization (PubMed:26573021). {ECO:0000250|UniProtKB:Q6KAU7,
CC ECO:0000269|PubMed:18045877, ECO:0000269|PubMed:26573021}.
CC -!- INTERACTION:
CC Q9H7P9; Q13526: PIN1; NbExp=3; IntAct=EBI-2797213, EBI-714158;
CC Q9H7P9-3; B2R8Y4; NbExp=3; IntAct=EBI-10175686, EBI-10175581;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H7P9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H7P9-2; Sequence=VSP_028530;
CC Name=3;
CC IsoId=Q9H7P9-3; Sequence=VSP_028529;
CC -!- DISEASE: Leukodystrophy and acquired microcephaly with or without
CC dystonia (LDAMD) [MIM:616763]: An autosomal recessive neurologic
CC disorder characterized by profound intellectual disability, dystonia,
CC postnatal microcephaly, and white matter abnormalities consistent with
CC leukodystrophy. {ECO:0000269|PubMed:26573021}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15364.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15719.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK024429; BAB15719.1; ALT_INIT; mRNA.
DR EMBL; AK026111; BAB15364.1; ALT_FRAME; mRNA.
DR EMBL; AC011500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW56888.1; -; Genomic_DNA.
DR EMBL; BC013426; AAH13426.2; -; mRNA.
DR EMBL; BC015174; AAH15174.1; -; mRNA.
DR EMBL; BC075858; AAH75858.1; -; mRNA.
DR CCDS; CCDS33022.2; -. [Q9H7P9-1]
DR CCDS; CCDS86766.1; -. [Q9H7P9-2]
DR RefSeq; NP_073746.2; NM_022835.2. [Q9H7P9-1]
DR RefSeq; XP_005259220.1; XM_005259163.2. [Q9H7P9-1]
DR AlphaFoldDB; Q9H7P9; -.
DR SMR; Q9H7P9; -.
DR BioGRID; 122330; 27.
DR IntAct; Q9H7P9; 7.
DR STRING; 9606.ENSP00000392906; -.
DR GlyGen; Q9H7P9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H7P9; -.
DR PhosphoSitePlus; Q9H7P9; -.
DR BioMuta; PLEKHG2; -.
DR DMDM; 296439273; -.
DR EPD; Q9H7P9; -.
DR jPOST; Q9H7P9; -.
DR MassIVE; Q9H7P9; -.
DR MaxQB; Q9H7P9; -.
DR PaxDb; Q9H7P9; -.
DR PeptideAtlas; Q9H7P9; -.
DR PRIDE; Q9H7P9; -.
DR ProteomicsDB; 81135; -. [Q9H7P9-1]
DR ProteomicsDB; 81136; -. [Q9H7P9-2]
DR ProteomicsDB; 81137; -. [Q9H7P9-3]
DR Antibodypedia; 30324; 52 antibodies from 14 providers.
DR DNASU; 64857; -.
DR Ensembl; ENST00000409797.6; ENSP00000386492.1; ENSG00000090924.15. [Q9H7P9-2]
DR Ensembl; ENST00000425673.6; ENSP00000392906.2; ENSG00000090924.15. [Q9H7P9-1]
DR GeneID; 64857; -.
DR KEGG; hsa:64857; -.
DR MANE-Select; ENST00000425673.6; ENSP00000392906.2; NM_022835.3; NP_073746.2.
DR UCSC; uc002olj.4; human. [Q9H7P9-1]
DR CTD; 64857; -.
DR DisGeNET; 64857; -.
DR GeneCards; PLEKHG2; -.
DR HGNC; HGNC:29515; PLEKHG2.
DR HPA; ENSG00000090924; Low tissue specificity.
DR MalaCards; PLEKHG2; -.
DR MIM; 611893; gene.
DR MIM; 616763; phenotype.
DR neXtProt; NX_Q9H7P9; -.
DR OpenTargets; ENSG00000090924; -.
DR PharmGKB; PA134893492; -.
DR VEuPathDB; HostDB:ENSG00000090924; -.
DR eggNOG; KOG3518; Eukaryota.
DR GeneTree; ENSGT00940000162093; -.
DR HOGENOM; CLU_007452_0_0_1; -.
DR InParanoid; Q9H7P9; -.
DR OMA; GHRGEAC; -.
DR OrthoDB; 147068at2759; -.
DR PhylomeDB; Q9H7P9; -.
DR TreeFam; TF328565; -.
DR PathwayCommons; Q9H7P9; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q9H7P9; -.
DR BioGRID-ORCS; 64857; 52 hits in 1080 CRISPR screens.
DR ChiTaRS; PLEKHG2; human.
DR GenomeRNAi; 64857; -.
DR Pharos; Q9H7P9; Tbio.
DR PRO; PR:Q9H7P9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9H7P9; protein.
DR Bgee; ENSG00000090924; Expressed in sural nerve and 115 other tissues.
DR ExpressionAtlas; Q9H7P9; baseline and differential.
DR Genevisible; Q9H7P9; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP: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; Disease variant; Guanine-nucleotide releasing factor;
KW Intellectual disability; Leukodystrophy; Phosphoprotein;
KW Reference proteome; Tumor suppressor.
FT CHAIN 1..1386
FT /note="Pleckstrin homology domain-containing family G
FT member 2"
FT /id="PRO_0000306861"
FT DOMAIN 102..283
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 313..411
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 468..496
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028529"
FT VAR_SEQ 560..1368
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028530"
FT VARIANT 204
FT /note="R -> W (in LDAMD; results in impaired regulation of
FT actin polymerization; dbSNP:rs201201843)"
FT /evidence="ECO:0000269|PubMed:26573021"
FT /id="VAR_078577"
FT VARIANT 540
FT /note="T -> I (in dbSNP:rs35904695)"
FT /id="VAR_035324"
FT VARIANT 622
FT /note="I -> V (in dbSNP:rs16973407)"
FT /id="VAR_035325"
FT VARIANT 647
FT /note="R -> H (in dbSNP:rs10407035)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035326"
FT VARIANT 992
FT /note="R -> K (in dbSNP:rs31726)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_035327"
FT VARIANT 1302
FT /note="A -> T (in dbSNP:rs34603507)"
FT /id="VAR_035328"
FT VARIANT 1329
FT /note="P -> A (in dbSNP:rs31728)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:23186163"
FT /id="VAR_035329"
SQ SEQUENCE 1386 AA; 147969 MW; 57D35431FCEBDAFA CRC64;
MPEGAQGLSL SKPSPSLGCG RRGEVCDCGT VCETRTAPAA PTMASPRGSG SSTSLSTVGS
EGDPAPGPTP ACSASRPEPL PGPPIRLHLS PVGIPGSARP SRLERVAREI VETERAYVRD
LRSIVEDYLG PLLDGGVLGL SVEQVGTLFA NIEDIYEFSS ELLEDLENSS SAGGIAECFV
QRSEDFDIYT LYCMNYPSSL ALLRELSLSP PAALWLQERQ AQLRHSLPLQ SFLLKPVQRI
LKYHLLLQEL GKHWAEGPGT GGREMVEEAI VSMTAVAWYI NDMKRKQEHA ARLQEVQRRL
GGWTGPELSA FGELVLEGAF RGGGGGGPRL RGGERLLFLF SRMLLVAKRR GLEYTYKGHI
FCCNLSVSES PRDPLGFKVS DLTIPKHRHL LQAKNQEEKR LWIHCLQRLF FENHPASIPA
KAKQVLLENS LHCAPKSKPV LEPLTPPLGS PRPRDARSFT PGRRNTAPSP GPSVIRRGRR
QSEPVKDPYV MFPQNAKPGF KHAGSEGELY PPESQPPVSG SAPPEDLEDA GPPTLDPSGT
SITEEILELL NQRGLRDPGP STHDIPKFPG DSQVPGDSET LTFQALPSRD SSEEEEEEEE
GLEMDERGPS PLHVLEGLES SIAAEMPSIP CLTKIPDVPN LPEIPSRCEI PEGSRLPSLS
DISDVFEMPC LPAIPSVPNT PSLSSTPTLS CDSWLQGPLQ EPAEAPATRR ELFSGSNPGK
LGEPPSGGKA GPEEDEEGVS FTDFQPQDVT QHQGFPDELA FRSCSEIRSA WQALEQGQLA
RPGFPEPLLI LEDSDLGGDS GSGKAGAPSS ERTASRVREL ARLYSERIQQ MQRAETRASA
NAPRRRPRVL AQPQPSPCLP QEQAEPGLLP AFGHVLVCEL AFPLTCAQES VPLGPAVWVQ
AAIPLSKQGG SPDGQGLHVS NLPKQDLPGI HVSAATLLPE QGGSRHVQAP AATPLPKQEG
PLHLQVPALT TFSDQGHPEI QVPATTPLPE HRSHMVIPAP STAFCPEQGH CADIHVPTTP
ALPKEICSDF TVSVTTPVPK QEGHLDSESP TNIPLTKQGG SRDVQGPDPV CSQPIQPLSW
HGSSLDPQGP GDTLPPLPCH LPDLQIPGTS PLPAHGSHLD HRIPANAPLS LSQELPDTQV
PATTPLPLPQ VLTDIWVQAL PTSPKQGSLP DIQGPAAAPP LPEPSLTDTQ VQKLTPSLEQ
KSLIDAHVPA ATPLPERGGS LDIQGLSPTP VQTTMVLSKP GGSLASHVAR LESSDLTPPH
SPPPSSRQLL GPNAAALSRY LAASYISQSL ARRQGPGGGA PAASRGSWSS APTSRASSPP
PQPQPPPPPA RRLSYATTVN IHVGGGGRLR PAKAQVRLNH PALLASTQES MGLHRAQGAP
DAPFHM
