GNOM_ARATH
ID GNOM_ARATH Reviewed; 1451 AA.
AC Q42510; Q38883; Q56ZY3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=ARF guanine-nucleotide exchange factor GNOM;
DE AltName: Full=Pattern formation protein EMB30;
DE AltName: Full=Protein EMBRYO DEFECTIVE 30;
DE AltName: Full=Protein MIZU-KUSSEI2;
DE AltName: Full=Protein VASCULAR NETWORK 7;
GN Name=GN; Synonyms=EMB30, GBF3, MIZ2, VAN7; OrderedLocusNames=At1g13980;
GN ORFNames=F16A14.20, F7A19.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISRUPTION PHENOTYPE, FUNCTION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF GLU-658.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=8020095; DOI=10.1016/0092-8674(94)90444-8;
RA Shevell D.E., Leu W.-M., Gillmor C.S., Xia G., Feldmann K.A., Chua N.-H.;
RT "EMB30 is essential for normal cell division, cell expansion, and cell
RT adhesion in Arabidopsis and encodes a protein that has similarity to
RT Sec7.";
RL Cell 77:1051-1062(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT PRO-95, AND MUTANTS
RP EMB30-1/T391/U87; B4049 AND TA477.
RC STRAIN=cv. C24, cv. Columbia, and cv. Landsberg erecta;
RX PubMed=8628228; DOI=10.1007/bf02172979;
RA Busch M., Mayer U., Juergens G.;
RT "Molecular analysis of the Arabidopsis pattern formation of gene GNOM: gene
RT structure and intragenic complementation.";
RL Mol. Gen. Genet. 250:681-691(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-1451.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RA Mayer U., Buettner G., Juergens G.;
RT "Apical-basal pattern formation in the Arabidopsis embryo: studies on the
RT role of the gnom gene.";
RL Development 117:149-162(1993).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=10514379; DOI=10.1126/science.286.5438.316;
RA Steinmann T., Geldner N., Grebe M., Mangold S., Jackson C.L., Paris S.,
RA Gaelweiler L., Palme K., Juergens G.;
RT "Coordinated polar localization of auxin efflux carrier PIN1 by GNOM ARF
RT GEF.";
RL Science 286:316-318(1999).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=10887076; DOI=10.1242/dev.127.15.3197;
RA Koizumi K., Sugiyama M., Fukuda H.;
RT "A series of novel mutants of Arabidopsis thaliana that are defective in
RT the formation of continuous vascular network: calling the auxin signal flow
RT canalization hypothesis into question.";
RL Development 127:3197-3204(2000).
RN [9]
RP HOMODIMERIZATION, INTERACTION WITH CYP19-4/CYP5, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=10715321; DOI=10.2307/3870940;
RA Grebe M., Gadea J., Steinmann T., Kientz M., Rahfeld J.-U., Salchert K.,
RA Koncz C., Juergens G.;
RT "A conserved domain of the Arabidopsis GNOM protein mediates subunit
RT interaction and cyclophilin 5 binding.";
RL Plant Cell 12:343-356(2000).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11090208; DOI=10.2307/3871104;
RA Shevell D.E., Kunkel T., Chua N.H.;
RT "Cell wall alterations in the arabidopsis emb30 mutant.";
RL Plant Cell 12:2047-2060(2000).
RN [11]
RP MUTAGENESIS OF MET-696, SUBCELLULAR LOCATION, FUNCTION, AND GENE FAMILY.
RX PubMed=12553910; DOI=10.1016/s0092-8674(03)00003-5;
RA Geldner N., Anders N., Wolters H., Keicher J., Kornberger W., Muller P.,
RA Delbarre A., Ueda T., Nakano A., Juergens G.;
RT "The Arabidopsis GNOM ARF-GEF mediates endosomal recycling, auxin
RT transport, and auxin-dependent plant growth.";
RL Cell 112:219-230(2003).
RN [12]
RP REVIEW.
RX PubMed=12878008; DOI=10.1016/s1360-1385(03)00132-8;
RA Muday G.K., Peer W.A., Murphy A.S.;
RT "Vesicular cycling mechanisms that control auxin transport polarity.";
RL Trends Plant Sci. 8:301-304(2003).
RN [13]
RP DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=14681187; DOI=10.1242/dev.00926;
RA Geldner N., Richter S., Vieten A., Marquardt S., Torres-Ruiz R.A.,
RA Mayer U., Juergens G.;
RT "Partial loss-of-function alleles reveal a role for GNOM in auxin
RT transport-related, post-embryonic development of Arabidopsis.";
RL Development 131:389-400(2004).
RN [14]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14742722; DOI=10.1091/mbc.e03-06-0443;
RA Cox R., Mason-Gamer R.J., Jackson C.L., Segev N.;
RT "Phylogenetic analysis of Sec7-domain-containing Arf nucleotide
RT exchangers.";
RL Mol. Biol. Cell 15:1487-1505(2004).
RN [15]
RP GENE FAMILY.
RX PubMed=17653190; DOI=10.1038/nature05967;
RA Richter S., Geldner N., Schrader J., Wolters H., Stierhof Y.D., Rios G.,
RA Koncz C., Robinson D.G., Juergens G.;
RT "Functional diversification of closely related ARF-GEFs in protein
RT secretion and recycling.";
RL Nature 448:488-492(2007).
RN [16]
RP FUNCTION.
RX PubMed=18394892; DOI=10.1016/j.cub.2008.03.021;
RA Kleine-Vehn J., Dhonukshe P., Sauer M., Brewer P.B., Wisniewska J.,
RA Paciorek T., Benkova E., Friml J.;
RT "ARF GEF-dependent transcytosis and polar delivery of PIN auxin carriers in
RT Arabidopsis.";
RL Curr. Biol. 18:526-531(2008).
RN [17]
RP HOMODIMERIZATION, DOMAIN, AND MEMBRANE-ASSOCIATION.
RX PubMed=18203920; DOI=10.1105/tpc.107.056515;
RA Anders N., Nielsen M., Keicher J., Stierhof Y.D., Furutani M., Tasaka M.,
RA Skriver K., Juergens G.;
RT "Membrane association of the Arabidopsis ARF exchange factor GNOM involves
RT interaction of conserved domains.";
RL Plant Cell 20:142-151(2008).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF GLY-951.
RX DOI=10.1104/pp.108.131003;
RA Miyazawa Y., Takahashi A., Kobayashi A., Kaneyasu T., Fujii N.,
RA Takahashi H.;
RT "GNOM-mediated vesicular trafficking plays an essential role in
RT hydrotropism of Arabidopsis roots.";
RL Plant Physiol. 149:835-840(2009).
RN [19]
RP FUNCTION.
RX DOI=10.1016/j.plantsci.2009.06.009;
RA Miyazawa Y., Ito Y., Moriwaki T., Kobayashi A., Fujii N., Takahashi H.;
RT "A molecular mechanism unique to hydrotropism in roots.";
RL Plant Sci. 177:297-301(2009).
RN [20]
RP REVIEW, AND FUNCTION.
RX PubMed=20036441; DOI=10.1016/j.ejcb.2009.11.020;
RA Richter S., Anders N., Wolters H., Beckmann H., Thomann A., Heinrich R.,
RA Schrader J., Singh M.K., Geldner N., Mayer U., Juergens G.;
RT "Role of the GNOM gene in Arabidopsis apical-basal patterning--From mutant
RT phenotype to cellular mechanism of protein action.";
RL Eur. J. Cell Biol. 89:138-144(2010).
RN [21]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21118984; DOI=10.1073/pnas.1016260107;
RA Naramoto S., Kleine-Vehn J., Robert S., Fujimoto M., Dainobu T.,
RA Paciorek T., Ueda T., Nakano A., Van Montagu M.C., Fukuda H., Friml J.;
RT "ADP-ribosylation factor machinery mediates endocytosis in plant cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21890-21895(2010).
RN [22]
RP FUNCTION.
RX PubMed=21138974; DOI=10.1242/dev.059147;
RA Wolters H., Anders N., Geldner N., Gavidia R., Juergens G.;
RT "Coordination of apical and basal embryo development revealed by tissue-
RT specific GNOM functions.";
RL Development 138:117-126(2011).
RN [23]
RP FUNCTION.
RX PubMed=21569134; DOI=10.1111/j.1365-313x.2011.04636.x;
RA Rakusova H., Gallego-Bartolome J., Vanstraelen M., Robert H.S., Alabadi D.,
RA Blazquez M.A., Benkova E., Friml J.;
RT "Polarization of PIN3-dependent auxin transport for hypocotyl gravitropic
RT response in Arabidopsis thaliana.";
RL Plant J. 67:817-826(2011).
CC -!- FUNCTION: Activates the ARF proteins by exchanging bound GDP for free
CC GTP. Plays a role in vesicular protein sorting. Acts as the major
CC regulator of endosomal vesicle trafficking but is also involved in the
CC endocytosis process. Could function redundantly with GNL1 in the
CC retrograde Golgi to endoplasmic reticulum trafficking. Regulates
CC vesicle trafficking required for the coordinated polar localization of
CC auxin efflux carriers which in turn determines the direction of auxin
CC flow. Mediates the sorting of PIN1 from endosomal compartments to the
CC basal plasma membrane and the polarization of PIN3 to the bottom side
CC of hypocotyl endodermal cells. Involved in the specification of apical-
CC basal pattern formation in the early embryo and during root formation.
CC Required for correct cell wall organization leading to normal cell
CC adhesion during seedling development. Also plays an essential role in
CC hydrotropism of seedling roots. {ECO:0000269|PubMed:10514379,
CC ECO:0000269|PubMed:11090208, ECO:0000269|PubMed:12553910,
CC ECO:0000269|PubMed:14681187, ECO:0000269|PubMed:18394892,
CC ECO:0000269|PubMed:20036441, ECO:0000269|PubMed:21118984,
CC ECO:0000269|PubMed:21138974, ECO:0000269|PubMed:21569134,
CC ECO:0000269|PubMed:8020095, ECO:0000269|Ref.18, ECO:0000269|Ref.19,
CC ECO:0000269|Ref.6}.
CC -!- ACTIVITY REGULATION: Inhibited by brefeldin A (BFA).
CC {ECO:0000269|PubMed:10514379}.
CC -!- SUBUNIT: Homodimer. Interacts with CYP19-4/CYP5 in vitro.
CC {ECO:0000269|PubMed:10715321}.
CC -!- INTERACTION:
CC Q42510; Q8LDP4: CYP19-4; NbExp=6; IntAct=EBI-1998836, EBI-2320844;
CC Q42510; Q42510: GN; NbExp=8; IntAct=EBI-1998836, EBI-1998836;
CC Q42510; P49598: PP2CA; NbExp=3; IntAct=EBI-1998836, EBI-1764934;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endosome membrane; Peripheral
CC membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Soluble and partially membrane-bound.
CC -!- TISSUE SPECIFICITY: Stems, leaves, flowers, siliques, floral
CC inflorescence and roots. Expressed in the whole plant (at the protein
CC level). {ECO:0000269|PubMed:10715321, ECO:0000269|PubMed:8020095}.
CC -!- DEVELOPMENTAL STAGE: Continually expressed in both embryogenesis and
CC postembryonic organ development. Strongly expressed in actively
CC dividing or elongating cells but only weakly or not at all in
CC differentiated tissues other than the vasculature.
CC {ECO:0000269|PubMed:14681187}.
CC -!- DOMAIN: The DCB domain is required for both homodimerization and
CC interaction with CYP protein. Heterotypic interaction of DCB domain
CC with the N-terminal part of the SEC7 domain is required for membrane
CC association and catalytic activity of the protein.
CC {ECO:0000269|PubMed:10715321, ECO:0000269|PubMed:18203920}.
CC -!- DISRUPTION PHENOTYPE: Lack of morphological features of apical-basal
CC polarity resulting of no root, no true hypocotyl and abnormal shoot
CC apical meristem. Cell wall alterations. Defects in cell adhesion.
CC Aberrant leaf venation. {ECO:0000269|PubMed:10887076,
CC ECO:0000269|PubMed:11090208, ECO:0000269|PubMed:8020095,
CC ECO:0000269|Ref.6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94131.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U56140; AAB01205.1; -; mRNA.
DR EMBL; U56141; AAB01206.1; -; Genomic_DNA.
DR EMBL; U36432; AAA91150.1; -; mRNA.
DR EMBL; U36433; AAA91151.1; -; Genomic_DNA.
DR EMBL; AC007576; AAD39284.1; -; Genomic_DNA.
DR EMBL; AC068197; AAF79403.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29092.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29093.1; -; Genomic_DNA.
DR EMBL; AK220827; BAD94131.1; ALT_INIT; mRNA.
DR PIR; S65571; S65571.
DR RefSeq; NP_001184991.1; NM_001198062.1.
DR RefSeq; NP_172851.1; NM_101264.4.
DR AlphaFoldDB; Q42510; -.
DR SMR; Q42510; -.
DR BioGRID; 23198; 4.
DR IntAct; Q42510; 3.
DR STRING; 3702.AT1G13980.1; -.
DR iPTMnet; Q42510; -.
DR PaxDb; Q42510; -.
DR PRIDE; Q42510; -.
DR ProteomicsDB; 247011; -.
DR EnsemblPlants; AT1G13980.1; AT1G13980.1; AT1G13980.
DR EnsemblPlants; AT1G13980.2; AT1G13980.2; AT1G13980.
DR GeneID; 837958; -.
DR Gramene; AT1G13980.1; AT1G13980.1; AT1G13980.
DR Gramene; AT1G13980.2; AT1G13980.2; AT1G13980.
DR KEGG; ath:AT1G13980; -.
DR Araport; AT1G13980; -.
DR TAIR; locus:2035853; AT1G13980.
DR eggNOG; KOG0928; Eukaryota.
DR HOGENOM; CLU_001204_1_0_1; -.
DR InParanoid; Q42510; -.
DR OMA; WQHQWHT; -.
DR OrthoDB; 815698at2759; -.
DR PhylomeDB; Q42510; -.
DR PRO; PR:Q42510; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42510; baseline and differential.
DR Genevisible; Q42510; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0010540; P:basipetal auxin transport; IMP:TAIR.
DR GO; GO:0007155; P:cell adhesion; IMP:TAIR.
DR GO; GO:0071555; P:cell wall organization; IMP:TAIR.
DR GO; GO:0070417; P:cellular response to cold; IDA:TAIR.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:TAIR.
DR GO; GO:0006897; P:endocytosis; IMP:TAIR.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; IGI:TAIR.
DR GO; GO:0010274; P:hydrotropism; IMP:UniProtKB.
DR GO; GO:0010311; P:lateral root formation; IMP:TAIR.
DR GO; GO:0009942; P:longitudinal axis specification; IMP:TAIR.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0048209; P:regulation of vesicle targeting, to, from or within Golgi; TAS:TAIR.
DR GO; GO:0048765; P:root hair cell differentiation; IGI:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR InterPro; IPR032691; Sec7_N.
DR Pfam; PF01369; Sec7; 1.
DR Pfam; PF12783; Sec7_N; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cytoplasm; Endocytosis; Endosome;
KW ER-Golgi transport; Guanine-nucleotide releasing factor; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1451
FT /note="ARF guanine-nucleotide exchange factor GNOM"
FT /id="PRO_0000120211"
FT DOMAIN 557..752
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 1..246
FT /note="DCB domain"
FT REGION 1430..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 658
FT /evidence="ECO:0000255"
FT VARIANT 95
FT /note="Q -> P (in strain: cv. Landsberg erecta)"
FT /evidence="ECO:0000269|PubMed:8628228"
FT MUTAGEN 579
FT /note="G->R: In B4049; abnormal embryo development."
FT MUTAGEN 599..601
FT /note="Missing: In TA477; abnormal embryo development."
FT MUTAGEN 658
FT /note="E->K: In emb30-1/T391/U87; abnormal embryo
FT development."
FT /evidence="ECO:0000269|PubMed:8020095"
FT MUTAGEN 696
FT /note="M->L: Confers brefeldin A (BFA) resistance."
FT /evidence="ECO:0000269|PubMed:12553910"
FT MUTAGEN 951
FT /note="G->E: Defects in hydrotropic response."
FT /evidence="ECO:0000269|Ref.18"
FT CONFLICT 111
FT /note="T -> I (in Ref. 2; AAA91150)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="A -> G (in Ref. 2; AAA91150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1451 AA; 162619 MW; 666E21C74B426996 CRC64;
MGRLKLHSGI KAIEEEPEDF ECTDSSNTTT LACMIDTEIA AVLAVMRRNV RWGGRYMSGD
DQLEHSLIQS LKALRKQVFS WNQPWHTISP MLYLQPFLDV IRSDETGAPI TSIALSSVYK
ILNLNVIDQN TANIEDAMHL VVDSVTSCRF EVTDPASEEV VLMKILQVLL ACMKNKASVM
LSNQHVCTVV NTCFRVVHQA GMKGELLQRV ARHTMHELVR CIFSHLPDVE RTETTLVNRA
GSIKQEKAGV DSDYAIVSKP VEDGNANSEY DVENSMATFA TGAQSLMDDG PVGPGSRKPA
SPYDLHIMTE PYGVPSMVEI FHFLCSLLNV VEHVGMGSRS NTIAFDEDVP LFALNLINSA
IELGGSSIRH HPRLLSLIQD ELFRNLMQFG LSMSPLILSM VCSIVLNLYQ HLRTELKLQL
EAFFSCVILR LAQGKYGPSY QQQEVAMEAL VNFCRQKSFM VEMYANLDCD ITCSNVFEEL
SNLLSKSTFP VNCPLSAMHI LALDGLIAVI QGMAERISNG LTGLDLGPVH LDEYTPFWMV
KCDNYSDPNH WVSFVRRRKY IKRRLMIGAD HFNRDPKKGL EFLQGTHLLP DKLDPQSVAC
FFRYTAGLDK NLVGDFLGNH DEFCVQVLNE FAGTFDFQYM NLDTALRLFL ETFRLPGESQ
KIQRVLEAFS ERYYMQSPEI LANKDAALVL SYSIIMLNTD QHNVQVKKKM TEEDFIRNNR
HINGGNDLPR EFLSELFHSI CNNEIRTTPE QGAGFPEMTP SRWIDLMHKS KKTAPYILAD
SRAYLDHDMF AIMSGPTIAA ISVVFDHAEH EDVYQTCIDG FLAIAKISAC HHLEDVLDDL
VVSLCKFTTL LNPSSVDEPV LAFGDDAKAR MATITIFTIA NKYGDYIRTG WRNILDCILR
LHKLGLLPAR VASDAADESE HSSEQGQGKP LANSLSSAHL QSMGTPRRSS GLMGRFSQLL
SLDTEEPRSQ PTEQQLAAHQ RTLQTIQKCH IDSIFTESKF LQAESLLQLA RALIWAAGRP
QKGTSSPEDE DTAVFCLELL IAITLNNRDR IVLLWQGVYE HIATIAQSTV MPCNLVDKAI
FGLLRICQRL LPYKESLADE LLRSLQLVLK LDARVADAYC EQIAIEVSRL VKANANHIRS
QAGWRTITSL LSITARHPEA SESGFDAVSF VMSEGTHLYP ANYVLCVDAA RQFAESRVGQ
SERSIRALDL MGDSLEFLAK WALSAKENMG EEDFGKMSQD IGEMWLRLVQ GLRKVCLDQR
EDVRNHALQS LQKCLGGVDG INLAHSMWSQ CFDKVIFTVL DDLLEIAAGS QKDYRNMEGT
LLLAIKLLSK VFLQQLQELS QLSTFCKLWL GVLTRMEKYM KVKVRGKKSD KLQESVPELL
KNILLVMKTK GVLLQRSALG GDSLWELTWL HVNNIAPSMR LELFPDQESS QLGDDETVSN
GLSSPENTTG S
