PREX2_HUMAN
ID PREX2_HUMAN Reviewed; 1606 AA.
AC Q70Z35; B4DFX0; Q32KL0; Q32KL1; Q6R7Q3; Q6R7Q4; Q9H805; Q9H961;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein {ECO:0000305};
DE Short=P-Rex2;
DE Short=PtdIns(3,4,5)-dependent Rac exchanger 2;
DE AltName: Full=DEP domain-containing protein 2;
GN Name=PREX2 {ECO:0000312|HGNC:HGNC:22950}; Synonyms=DEPDC2;
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 [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Skeletal muscle;
RX PubMed=15304343; DOI=10.1016/j.febslet.2004.06.096;
RA Donald S., Hill K., Lecureuil C., Barnouin R., Krugmann S.,
RA John Coadwell W., Andrews S.R., Walker S.A., Hawkins P.T., Stephens L.R.,
RA Welch H.C.E.;
RT "P-Rex2, a new guanine-nucleotide exchange factor for Rac.";
RL FEBS Lett. 572:172-176(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Mammary gland;
RA Joseph R.E., Norris F.A.;
RT "Cloning and characterization of P-Rex2: an inositol polyphosphate 4-
RT phosphatase domain containing guanine nucleotide exchange factor.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-1606 (ISOFORM 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 216-1588 (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 549-1588 (ISOFORM 1).
RC TISSUE=Embryo, and Teratocarcinoma;
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 [5]
RP IDENTIFICATION (ISOFORM 3), FUNCTION, AND ALTERNATIVE SPLICING.
RX PubMed=15304342; DOI=10.1016/j.febslet.2004.06.097;
RA Rosenfeldt H., Vazquez-Prado J., Gutkind J.S.;
RT "P-REX2, a novel PI-3-kinase sensitive Rac exchange factor.";
RL FEBS Lett. 572:167-171(2004).
RN [6]
RP FUNCTION.
RX PubMed=15897194; DOI=10.1074/jbc.m412495200;
RA Joseph R.E., Norris F.A.;
RT "Substrate specificity and recognition is conferred by the pleckstrin
RT homology domain of the Dbl family guanine nucleotide exchange factor P-
RT Rex2.";
RL J. Biol. Chem. 280:27508-27512(2005).
RN [7]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-537 AND GLU-1571.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Functions as a RAC1 guanine nucleotide exchange factor (GEF),
CC activating Rac proteins by exchanging bound GDP for free GTP. Its
CC activity is synergistically activated by phosphatidylinositol 3,4,5-
CC trisphosphate and the beta gamma subunits of heterotrimeric G protein.
CC Mediates the activation of RAC1 in a PI3K-dependent manner. May be an
CC important mediator of Rac signaling, acting directly downstream of both
CC G protein-coupled receptors and phosphoinositide 3-kinase.
CC {ECO:0000269|PubMed:15304342, ECO:0000269|PubMed:15304343,
CC ECO:0000269|PubMed:15897194}.
CC -!- SUBUNIT: Interacts with RAC1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=P-Rex2;
CC IsoId=Q70Z35-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q70Z35-3; Sequence=VSP_025150, VSP_025152;
CC Name=4;
CC IsoId=Q70Z35-4; Sequence=VSP_055612, VSP_055613, VSP_055614;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in skeletal muscle,
CC heart and placenta, absent from peripheral blood leukocytes. Isoform 2
CC is expressed in skeletal muscle, kidney, small intestine, and placenta.
CC Isoform 3 is expressed in the heart. {ECO:0000269|PubMed:15304343}.
CC -!- DOMAIN: PH domain confers substrate specificity and recognition. Able
CC to discriminate between RAC1, RHOA, and CDC42.
CC -!- DOMAIN: DH domain alone was unable to confer substrate specificity and
CC recognition.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK024079; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14375.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG57581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA05334.1; Type=Miscellaneous discrepancy; Note=Non-canonical splice intron-exon junction.; Evidence={ECO:0000305};
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DR EMBL; AJ437636; CAD26885.2; -; mRNA.
DR EMBL; AY508996; AAS82571.1; -; mRNA.
DR EMBL; AY508997; AAS82572.1; -; mRNA.
DR EMBL; AC011853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK023049; BAB14375.1; ALT_INIT; mRNA.
DR EMBL; AK024079; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK294299; BAG57581.1; ALT_INIT; mRNA.
DR EMBL; BK005160; DAA05333.1; -; mRNA.
DR EMBL; BK005161; DAA05334.1; ALT_SEQ; mRNA.
DR CCDS; CCDS6201.1; -. [Q70Z35-1]
DR RefSeq; NP_079146.2; NM_024870.3. [Q70Z35-1]
DR RefSeq; NP_079446.3; NM_025170.5. [Q70Z35-3]
DR PDB; 6BNM; X-ray; 1.90 A; A=219-377.
DR PDBsum; 6BNM; -.
DR AlphaFoldDB; Q70Z35; -.
DR SMR; Q70Z35; -.
DR BioGRID; 123199; 15.
DR IntAct; Q70Z35; 7.
DR STRING; 9606.ENSP00000288368; -.
DR GlyGen; Q70Z35; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q70Z35; -.
DR PhosphoSitePlus; Q70Z35; -.
DR BioMuta; PREX2; -.
DR DMDM; 74758897; -.
DR EPD; Q70Z35; -.
DR jPOST; Q70Z35; -.
DR MassIVE; Q70Z35; -.
DR MaxQB; Q70Z35; -.
DR PaxDb; Q70Z35; -.
DR PeptideAtlas; Q70Z35; -.
DR PRIDE; Q70Z35; -.
DR ProteomicsDB; 68577; -. [Q70Z35-1]
DR ProteomicsDB; 68579; -. [Q70Z35-3]
DR Antibodypedia; 2764; 70 antibodies from 15 providers.
DR DNASU; 80243; -.
DR Ensembl; ENST00000288368.5; ENSP00000288368.4; ENSG00000046889.19. [Q70Z35-1]
DR GeneID; 80243; -.
DR KEGG; hsa:80243; -.
DR MANE-Select; ENST00000288368.5; ENSP00000288368.4; NM_024870.4; NP_079146.2.
DR UCSC; uc003xxv.2; human. [Q70Z35-1]
DR CTD; 80243; -.
DR DisGeNET; 80243; -.
DR GeneCards; PREX2; -.
DR HGNC; HGNC:22950; PREX2.
DR HPA; ENSG00000046889; Tissue enhanced (brain).
DR MIM; 612139; gene.
DR neXtProt; NX_Q70Z35; -.
DR OpenTargets; ENSG00000046889; -.
DR PharmGKB; PA164725103; -.
DR VEuPathDB; HostDB:ENSG00000046889; -.
DR eggNOG; KOG3519; Eukaryota.
DR eggNOG; KOG4428; Eukaryota.
DR GeneTree; ENSGT00940000155894; -.
DR HOGENOM; CLU_003935_0_0_1; -.
DR InParanoid; Q70Z35; -.
DR OMA; VRQYNQK; -.
DR OrthoDB; 24217at2759; -.
DR PhylomeDB; Q70Z35; -.
DR TreeFam; TF328639; -.
DR PathwayCommons; Q70Z35; -.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q70Z35; -.
DR SIGNOR; Q70Z35; -.
DR BioGRID-ORCS; 80243; 15 hits in 1070 CRISPR screens.
DR ChiTaRS; PREX2; human.
DR GeneWiki; PREX2; -.
DR GenomeRNAi; 80243; -.
DR Pharos; Q70Z35; Tbio.
DR PRO; PR:Q70Z35; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q70Z35; protein.
DR Bgee; ENSG00000046889; Expressed in calcaneal tendon and 161 other tissues.
DR Genevisible; Q70Z35; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd04439; DEP_1_P-Rex; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037367; Rex2_DEP_1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00049; DEP; 2.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50186; DEP; 2.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Guanine-nucleotide releasing factor;
KW Reference proteome; Repeat.
FT CHAIN 1..1606
FT /note="Phosphatidylinositol 3,4,5-trisphosphate-dependent
FT Rac exchanger 2 protein"
FT /id="PRO_0000286795"
FT DOMAIN 23..214
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 245..361
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 390..464
FT /note="DEP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 491..566
FT /note="DEP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 592..671
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 677..754
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1581..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 48..112
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055612"
FT VAR_SEQ 906..979
FT /note="FSRVLKNRAWPTFKQAKSKISPLHSSDFCPTNCHVNVMEVSYPKTSTSLGSA
FT FGVQLDSRKHNSHDKENKSSEQ -> VQASERFYNFTARHAVWEHSFDLHSVSSTFPVP
FT VTMEFLLLPPPLLGISQDGRQHCIPEDLPSQEMLLAERAPV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_025150"
FT VAR_SEQ 980..1606
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_025152"
FT VAR_SEQ 1049
FT /note="D -> E (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055613"
FT VAR_SEQ 1050..1606
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055614"
FT VARIANT 312
FT /note="D -> N (in dbSNP:rs11784582)"
FT /id="VAR_032163"
FT VARIANT 537
FT /note="V -> I (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs147538692)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035973"
FT VARIANT 1571
FT /note="A -> E (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035974"
FT CONFLICT 158
FT /note="T -> I (in Ref. 2; AAS82571/AAS82572)"
FT /evidence="ECO:0000305"
FT CONFLICT 1076
FT /note="E -> V (in Ref. 2; AAS82571 and 4; AK024079)"
FT /evidence="ECO:0000305"
FT CONFLICT 1268
FT /note="C -> R (in Ref. 2; AAS82571)"
FT /evidence="ECO:0000305"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:6BNM"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:6BNM"
FT STRAND 246..256
FT /evidence="ECO:0007829|PDB:6BNM"
FT STRAND 259..268
FT /evidence="ECO:0007829|PDB:6BNM"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:6BNM"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:6BNM"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6BNM"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:6BNM"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6BNM"
FT STRAND 322..332
FT /evidence="ECO:0007829|PDB:6BNM"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:6BNM"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:6BNM"
FT HELIX 346..364
FT /evidence="ECO:0007829|PDB:6BNM"
SQ SEQUENCE 1606 AA; 182622 MW; D9E938D65CE2C7DD CRC64;
MSEDSRGDSR AESAKDLEKQ LRLRVCVLSE LQKTERDYVG TLEFLVSAFL HRMNQCAASK
VDKNVTEETV KMLFSNIEDI LAVHKEFLKV VEECLHPEPN AQQEVGTCFL HFKDKFRIYD
EYCSNHEKAQ KLLLELNKIR TIRTFLLNCM LLGGRKNTDV PLEGYLVTPI QRICKYPLIL
KELLKRTPRK HSDYAAVMEA LQAMKAVCSN INEAKRQMEK LEVLEEWQSH IEGWEGSNIT
DTCTEMLMCG VLLKISSGNI QERVFFLFDN LLVYCKRKHR RLKNSKASTD GHRYLFRGRI
NTEVMEVENV DDGTADFHSS GHIVVNGWKI HNTAKNKWFV CMAKTPEEKH EWFEAILKER
ERRKGLKLGM EQDTWVMISE QGEKLYKMMC RQGNLIKDRK RKLTTFPKCF LGSEFVSWLL
EIGEIHRPEE GVHLGQALLE NGIIHHVTDK HQFKPEQMLY RFRYDDGTFY PRNEMQDVIS
KGVRLYCRLH SLFTPVIRDK DYHLRTYKSV VMANKLIDWL IAQGDCRTRE EAMIFGVGLC
DNGFMHHVLE KSEFKDEPLL FRFFSDEEME GSNMKHRLMK HDLKVVENVI AKSLLIKSNE
GSYGFGLEDK NKVPIIKLVE KGSNAEMAGM EVGKKIFAIN GDLVFMRPFN EVDCFLKSCL
NSRKPLRVLV STKPRETVKI PDSADGLGFQ IRGFGPSVVH AVGRGTVAAA AGLHPGQCII
KVNGINVSKE THASVIAHVT ACRKYRRPTK QDSIQWVYNS IESAQEDLQK SHSKPPGDEA
GDAFDCKVEE VIDKFNTMAI IDGKKEHVSL TVDNVHLEYG VVYEYDSTAG IKCNVVEKMI
EPKGFFSLTA KILEALAKSD EHFVQNCTSL NSLNEVIPTD LQSKFSALCS ERIEHLCQRI
SSYKKFSRVL KNRAWPTFKQ AKSKISPLHS SDFCPTNCHV NVMEVSYPKT STSLGSAFGV
QLDSRKHNSH DKENKSSEQG KLSPMVYIQH TITTMAAPSG LSLGQQDGHG LRYLLKEEDL
ETQDIYQKLL GKLQTALKEV EMCVCQIDDL LSSITYSPKL ERKTSEGIIP TDSDNEKGER
NSKRVCFNVA GDEQEDSGHD TISNRDSYSD CNSNRNSIAS FTSICSSQCS SYFHSDEMDS
GDELPLSVRI SHDKQDKIHS CLEHLFSQVD SITNLLKGQA VVRAFDQTKY LTPGRGLQEF
QQEMEPKLSC PKRLRLHIKQ DPWNLPSSVR TLAQNIRKFV EEVKCRLLLA LLEYSDSETQ
LRRDMVFCQT LVATVCAFSE QLMAALNQMF DNSKENEMET WEASRRWLDQ IANAGVLFHF
QSLLSPNLTD EQAMLEDTLV ALFDLEKVSF YFKPSEEEPL VANVPLTYQA EGSRQALKVY
FYIDSYHFEQ LPQRLKNGGG FKIHPVLFAQ ALESMEGYYY RDNVSVEEFQ AQINAASLEK
VKQYNQKLRA FYLDKSNSPP NSTSKAAYVD KLMRPLNALD ELYRLVASFI RSKRTAACAN
TACSASGVGL LSVSSELCNR LGACHIIMCS SGVHRCTLSV TLEQAIILAR SHGLPPRYIM
QATDVMRKQG ARVQNTAKNL GVRDRTPQSA PRLYKLCEPP PPAGEE
