ARG28_MOUSE
ID ARG28_MOUSE Reviewed; 1693 AA.
AC P97433; A0PJC1; Q69Z41; Q6DI55;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Rho guanine nucleotide exchange factor 28;
DE AltName: Full=190 kDa guanine nucleotide exchange factor;
DE Short=p190-RhoGEF;
DE Short=p190RhoGEF;
DE AltName: Full=Rho guanine nucleotide exchange factor;
DE AltName: Full=Rho-interacting protein 2;
GN Name=Arhgef28; Synonyms=Kiaa1998, Rgnef, Rhoip2, Rip2;
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 [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9199174; DOI=10.1083/jcb.137.7.1603;
RA Gebbink M.F.B.G., Kranenburg O., Poland M., van Horck F.P.G., Houssa B.,
RA Moolenaar W.H.;
RT "Identification of a novel, putative Rho-specific GDP/GTP exchange factor
RT and a RhoA-binding protein: control of neuronal morphology.";
RL J. Cell Biol. 137:1603-1613(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-649 (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Bone, and Mammary tumor;
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 INTERACTION WITH MAPK8IP1, AND MUTAGENESIS OF PHE-1563; ASN-1565 AND
RP PHE-1568.
RX PubMed=10574993; DOI=10.1074/jbc.274.49.35113;
RA Meyer D., Liu A., Margolis B.;
RT "Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190
RT rhoGEF and its localization in differentiated neurons.";
RL J. Biol. Chem. 274:35113-35118(1999).
RN [5]
RP FUNCTION, INTERACTION WITH RHOA AND MICROTUBULES, MUTAGENESIS OF TYR-1003,
RP AND SUBCELLULAR LOCATION.
RX PubMed=11058585; DOI=10.1074/jbc.m003839200;
RA van Horck F.P.G., Ahmadian M.R., Haeusler L.C., Moolenaar W.H.,
RA Kranenburg O.;
RT "Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide
RT exchange factor that interacts with microtubules.";
RL J. Biol. Chem. 276:4948-4956(2001).
RN [6]
RP FUNCTION IN NEFL EXPRESSION, AND NEFL RNA-BINDING.
RX PubMed=11435431; DOI=10.1074/jbc.m104104200;
RA Canete-Soler R., Wu J., Zhai J., Shamim M., Schlaepfer W.W.;
RT "p190RhoGEF Binds to a destabilizing element in the 3' untranslated region
RT of light neurofilament subunit mRNA and alters the stability of the
RT transcript.";
RL J. Biol. Chem. 276:32046-32050(2001).
RN [7]
RP INTERACTION WITH YWHAE AND YWHAH, AND MUTAGENESIS OF ASN-1375 AND LEU-1376.
RX PubMed=11533041; DOI=10.1074/jbc.m107709200;
RA Zhai J., Lin H., Shamim M., Schlaepfer W.W., Canete-Soler R.;
RT "Identification of a novel interaction of 14-3-3 with p190RhoGEF.";
RL J. Biol. Chem. 276:41318-41324(2001).
RN [8]
RP FUNCTION, OLIGOMERIZATION, AND IDENTIFICATION IN A COMPLEX WITH MAPK8 AND
RP MAPK8IP1.
RX PubMed=14499478; DOI=10.1016/s0169-328x(03)00263-8;
RA Wu J., Zhai J., Lin H., Nie Z., Ge W.-W., Garcia-Bermejo L., Muschel R.J.,
RA Schlaepfer W.W., Canete-Soler R.;
RT "Cytoplasmic retention sites in p190RhoGEF confer anti-apoptotic activity
RT to an EGFP-tagged protein.";
RL Brain Res. Mol. Brain Res. 117:27-38(2003).
RN [9]
RP FUNCTION, INTERACTION WITH PTK2/FAK1, PHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12702722; DOI=10.1074/jbc.m302381200;
RA Zhai J., Lin H., Nie Z., Wu J., Canete-Soler R., Schlaepfer W.W.,
RA Schlaepfer D.D.;
RT "Direct interaction of focal adhesion kinase with p190RhoGEF.";
RL J. Biol. Chem. 278:24865-24873(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=12496377; DOI=10.4049/jimmunol.170.1.19;
RA Lee J.R., Ha Y.J., Kim H.J.;
RT "Induced expression of a RhoA-specific guanine nucleotide exchange factor,
RT p190RhoGEF, following CD40 stimulation and WEHI 231 B cell activation.";
RL J. Immunol. 170:19-23(2003).
RN [11]
RP FUNCTION IN AXONAL BRANCHING AND SYNAPSE FORMATION.
RX PubMed=15378065; DOI=10.1038/nn1317;
RA Rico B., Beggs H.E., Schahin-Reed D., Kimes N., Schmidt A., Reichardt L.F.;
RT "Control of axonal branching and synapse formation by focal adhesion
RT kinase.";
RL Nat. Neurosci. 7:1059-1069(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH NEFL.
RX PubMed=16236762; DOI=10.1093/hmg/ddi392;
RA Lin H., Zhai J., Schlaepfer W.W.;
RT "RNA-binding protein is involved in aggregation of light neurofilament
RT protein and is implicated in the pathogenesis of motor neuron
RT degeneration.";
RL Hum. Mol. Genet. 14:3643-3659(2005).
RN [13]
RP FUNCTION, AND INTERACTION WITH CTNND2.
RX PubMed=17993462; DOI=10.1074/jbc.m707158200;
RA Kim H., Han J.-R., Park J., Oh M., James S.E., Chang S., Lu Q., Lee K.Y.,
RA Ki H., Song W.-J., Kim K.;
RT "Delta-catenin-induced dendritic morphogenesis. An essential role of
RT p190RhoGEF interaction through Akt1-mediated phosphorylation.";
RL J. Biol. Chem. 283:977-987(2008).
RN [14]
RP FUNCTION, AND INDUCTION BY PTK2B/PYK2.
RX PubMed=18195107; DOI=10.1083/jcb.200708194;
RA Lim Y., Lim S.-T., Tomar A., Gardel M., Bernard-Trifilo J.A., Chen X.L.,
RA Uryu S.A., Canete-Soler R., Zhai J., Lin H., Schlaepfer W.W., Nalbant P.,
RA Bokoch G., Ilic D., Waterman-Storer C., Schlaepfer D.D.;
RT "PyK2 and FAK connections to p190Rho guanine nucleotide exchange factor
RT regulate RhoA activity, focal adhesion formation, and cell motility.";
RL J. Cell Biol. 180:187-203(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Pancreas;
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: Functions as a RHOA-specific guanine nucleotide exchange
CC factor regulating signaling pathways downstream of integrins and growth
CC factor receptors. Functions in axonal branching, synapse formation and
CC dendritic morphogenesis. Functions also in focal adhesion formation,
CC cell motility and B-lymphocytes activation. May regulate NEFL
CC expression and aggregation and play a role in apoptosis.
CC {ECO:0000269|PubMed:11058585, ECO:0000269|PubMed:11435431,
CC ECO:0000269|PubMed:12496377, ECO:0000269|PubMed:12702722,
CC ECO:0000269|PubMed:14499478, ECO:0000269|PubMed:15378065,
CC ECO:0000269|PubMed:16236762, ECO:0000269|PubMed:17993462,
CC ECO:0000269|PubMed:18195107, ECO:0000269|PubMed:9199174}.
CC -!- SUBUNIT: Homooligomer; forms some cytoplasmic aggregates. Forms a
CC complex with MAPK8 and MAPK8IP1. Interacts with RHOA. Interacts with
CC microtubules. Interacts with YWHAE and YWHAH. Interacts with PTK2/FAK1.
CC Interacts with NEFL. Interacts with CTNND2; prevents interaction with
CC RHOA. {ECO:0000269|PubMed:10574993, ECO:0000269|PubMed:11058585,
CC ECO:0000269|PubMed:11533041, ECO:0000269|PubMed:12702722,
CC ECO:0000269|PubMed:14499478, ECO:0000269|PubMed:16236762,
CC ECO:0000269|PubMed:17993462}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Colocalizes with
CC the microtubule radial and cortical systems.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P97433-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97433-2; Sequence=VSP_032145, VSP_032146;
CC -!- TISSUE SPECIFICITY: Highly enriched in the brain (at protein level).
CC Also detected in lung and kidney. {ECO:0000269|PubMed:12702722,
CC ECO:0000269|PubMed:9199174}.
CC -!- INDUCTION: Up-regulated in B-lymphocytes upon CD40 stimulation. Up-
CC regulated by PTK2B/PYK2 (at protein level).
CC {ECO:0000269|PubMed:12496377, ECO:0000269|PubMed:18195107}.
CC -!- PTM: Phosphorylated on tyrosine upon stimulation of cells by laminin.
CC {ECO:0000269|PubMed:12702722}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22978.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH75734.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAD32603.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U73199; AAB18197.1; -; mRNA.
DR EMBL; AK173325; BAD32603.1; ALT_INIT; mRNA.
DR EMBL; BC022978; AAH22978.1; ALT_SEQ; mRNA.
DR EMBL; BC075734; AAH75734.1; ALT_SEQ; mRNA.
DR PIR; T30867; T30867.
DR RefSeq; NP_036156.2; NM_012026.2.
DR AlphaFoldDB; P97433; -.
DR SMR; P97433; -.
DR BioGRID; 225739; 11.
DR IntAct; P97433; 2.
DR MINT; P97433; -.
DR STRING; 10090.ENSMUSP00000105053; -.
DR iPTMnet; P97433; -.
DR PhosphoSitePlus; P97433; -.
DR MaxQB; P97433; -.
DR PaxDb; P97433; -.
DR PRIDE; P97433; -.
DR ProteomicsDB; 283256; -. [P97433-1]
DR ProteomicsDB; 283257; -. [P97433-2]
DR DNASU; 110596; -.
DR GeneID; 110596; -.
DR KEGG; mmu:110596; -.
DR UCSC; uc007rol.1; mouse. [P97433-2]
DR CTD; 64283; -.
DR MGI; MGI:1346016; Arhgef28.
DR eggNOG; KOG3519; Eukaryota.
DR eggNOG; KOG3520; Eukaryota.
DR InParanoid; P97433; -.
DR OrthoDB; 69816at2759; -.
DR PhylomeDB; P97433; -.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR BioGRID-ORCS; 110596; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Arhgef28; mouse.
DR PRO; PR:P97433; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97433; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR CDD; cd14680; PH_p190RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR037819; ARHGEF28_PH.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Differentiation; Guanine-nucleotide releasing factor; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..1693
FT /note="Rho guanine nucleotide exchange factor 28"
FT /id="PRO_0000080967"
FT DOMAIN 846..1041
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1095..1184
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 651..698
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 288..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1301
FT /note="Interaction with PTK2/FAK1; required for regulation
FT of axonal branching and synapse formation"
FT REGION 1369..1380
FT /note="Mediates cytoplasmic retention and interaction with
FT YWHAH"
FT /evidence="ECO:0000269|PubMed:11533041"
FT REGION 1421..1693
FT /note="Interaction with microtubules"
FT REGION 1493..1524
FT /note="RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 1563..1576
FT /note="Mediates cytoplasmic retention and interaction with
FT MAPK8IP1"
FT /evidence="ECO:0000269|PubMed:10574993"
FT REGION 1602..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1421..1522
FT /evidence="ECO:0000255"
FT COMPBIAS 301..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1674..1693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C6P5"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C6P5"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C6P5"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1W1"
FT MOD_RES 1535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1W1"
FT MOD_RES 1604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1322..1324
FT /note="SLV -> CGI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_032145"
FT VAR_SEQ 1325..1693
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_032146"
FT MUTAGEN 1003
FT /note="Y->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:11058585"
FT MUTAGEN 1375
FT /note="N->A: Alters interaction with YWHAH."
FT /evidence="ECO:0000269|PubMed:11533041"
FT MUTAGEN 1376
FT /note="L->A: Alters interaction with YWHAH."
FT /evidence="ECO:0000269|PubMed:11533041"
FT MUTAGEN 1563
FT /note="F->A: Alters interaction with MAPK8IP1."
FT /evidence="ECO:0000269|PubMed:10574993"
FT MUTAGEN 1565
FT /note="N->A: Alters interaction with MAPK8IP1."
FT /evidence="ECO:0000269|PubMed:10574993"
FT MUTAGEN 1568
FT /note="F->A: Alters interaction with MAPK8IP1."
FT /evidence="ECO:0000269|PubMed:10574993"
FT CONFLICT 340
FT /note="A -> P (in Ref. 3; AAH75734)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="A -> T (in Ref. 3; AAH75734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1693 AA; 190326 MW; 4E96087C449FF14C CRC64;
MELSCSEVPL YGQKTVYAKF GKNVYLPEDA EFYFVYGGSH QRHVVIADRV QDNVLQSSIP
GHWLQETVTV SVCLCSEGYS PVTMGSGSVT YVDNMACRLA RLLVTQADRL TACSHQTLLT
PFALTVEALP ALDEELVLAL TQLELPLGWT VLGNSSLEVS LHRESLLHLA VRWALPKLFH
FLLCLPGGVK ALKLPNEEAT TPLDLALQGG HSTLVEDITN FQGSHSPGFS RLRLNEEATL
QFVHSSETLT LTVNHTAEHL LEADIKLFRK YFWDRAFLVK ALEQEAKTEK ATMPSGAAET
EEEVRNLESG RSPSEEEEDA KSIKSQVDGP SEHEDQDRLA LDRSFDGLKK SKHVPASLAA
GQLSDVLNGG DEVYANCMVI DQVGDLDINY INLEGLSTHT SPESGRSMLG PQACMHTLPP
DTSPCGRPLI ENSEGTLDAA ASQSFVTPSS SRTSNLNLSF GLHGFEKEQS HLKKRSSSLD
ALVADSEGEG GSEPPICYAV GSQSSPRTGL PSGDELDSFE TNTEPDCNIS RTESLSLSST
LHSKESLLSG IRSRSYSCSS PKISSGKSRL VRDFTVCSTS EEQRSYSFQE PPGEKRIQEE
EWDEYVIPAK SESEKYKVSR TFSFLMNRMT SPRNKSKMKN KDTKEKEKMN RHQFVPGTFS
GVLQCSGCDK TLLGKESLQC ANCKANTHKG CKDAVPPCTK KFQEKYNKNK PQSILGSSSV
RDVPAPGLSL HPSSSMPIGL PAGRKEFAAQ VHPLSRSVPG TTLESFRRAV TSLESEGDSW
RSRSHSDELF QSMGSSPSTE SFMMEDVVDS SLWIDLSSDA QEFEAESWSL VVDPSFCSRQ
EKDVIKRQDV IFELMQTEVH HIQTLLIMSE VFRKGMKEEL QLDHSTVDKI FPCLDELLET
HRHFFFSMKE RRQESCAGSD RNFVINQIGD ILVQQFSEEN ASKMKRIYGE FCSHHKEAMS
LFKELQQNKK FQNFIKIRNS NLLARRRGIP ECILLVTQRI TKYPVLVERI LQYTKERTEE
HRDLCKALGL IKDMIAAVDL KVSEYEKNQK WLEILNKIEN KTYTKLKNGH VFRKQALLSQ
ERALLHDGLV YWKTATGRFK DILALLLTDV LLFLQEKDQK YIFAAVDQKP SVISLQKLIA
REVANEERGM FLISASSAGP EMYEIHTNSK EERNNWMRRI QQAVESCPEE EGGRTSESDE
ERRKAEARVA KIQQCQEILS NQDQQICTYL EEKLHIYAEL GELSGFEDVH LEPHLLIKPD
PGEPPQAASL LAAALREAES LQVAVKASKM GDVSQSSEES PGGTVLMDTP STQDVPASPT
ASLVTEGTEG RGCWDVDPGL QGVVTDLAVS DAGEKVEYRS FSGSSQSEII QAIQNLTRLL
YSLQAALTIQ DSHIEIHKLV LQQRESLAPS HSFRGGPLQD QEKSRYLEKQ REELANIHKL
QHQFQQEQRR WHRTCDQQQR EQEAQESWLQ ARERECQSQE ELLLRHRSEL DHQLQEYQQS
LERLREGQRM VERERQKMRV QQGLLGHCKH SRQRSLPAVF SPGSKEVTEL NRAESLCHEN
SFFINEAFGH MSLNTSNKPN PSGVPWDAHP LEGSHFDLAR TSESPTELKI DISQPPDVNS
ELWTTGPGHQ RPALQENSKE SYKNVADLDS FQSESSSPQD SNQRWPPATD THNRSKTKSS
DGGWTRWRCW RRG
