SPA1_ARATH
ID SPA1_ARATH Reviewed; 1029 AA.
AC Q9SYX2; Q0WUH3; Q56WP1; Q9SKE4; Q9SKE5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein SUPPRESSOR OF PHYA-105 1;
DE EC=2.7.-.-;
GN Name=SPA1; OrderedLocusNames=At2g46340/At2g46350;
GN ORFNames=F11C10.3/F11C10.4;
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 [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=10205059; DOI=10.1126/science.284.5413.496;
RA Hoecker U., Tepperman J.M., Quail P.H.;
RT "SPA1, a WD-repeat protein specific to phytochrome A signal transduction.";
RL Science 284:496-499(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=11457980; DOI=10.1104/pp.126.3.1291;
RA Parks B.M., Hoecker U., Spalding E.P.;
RT "Light-induced growth promotion by SPA1 counteracts phytochrome-mediated
RT growth inhibition during de-etiolation.";
RL Plant Physiol. 126:1291-1298(2001).
RN [6]
RP CHARACTERIZATION, AND INTERACTION WITH COP1.
RX PubMed=11461903; DOI=10.1074/jbc.m103140200;
RA Hoecker U., Quail P.H.;
RT "The phytochrome A-specific signaling intermediate SPA1 interacts directly
RT with COP1, a constitutive repressor of light signaling in Arabidopsis.";
RL J. Biol. Chem. 276:38173-38178(2001).
RN [7]
RP FUNCTION.
RX PubMed=12244439; DOI=10.1007/s00425-002-0801-x;
RA Baumgardt R.-L., Oliverio K.A., Casal J.J., Hoecker U.;
RT "SPA1, a component of phytochrome A signal transduction, regulates the
RT light signaling current.";
RL Planta 215:745-753(2002).
RN [8]
RP FUNCTION.
RX PubMed=12827204; DOI=10.1038/nature01696;
RA Seo H.S., Yang J.-Y., Ishikawa M., Bolle C., Ballesteros M.L., Chua N.-H.;
RT "LAF1 ubiquitination by COP1 controls photomorphogenesis and is stimulated
RT by SPA1.";
RL Nature 423:995-999(2003).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12887588; DOI=10.1046/j.1365-313x.2003.01813.x;
RA Laubinger S., Hoecker U.;
RT "The SPA1-like proteins SPA3 and SPA4 repress photomorphogenesis in the
RT light.";
RL Plant J. 35:373-385(2003).
RN [10]
RP INTERACTION WITH COP1 AND HY5.
RX PubMed=14597662; DOI=10.1101/gad.1122903;
RA Saijo Y., Sullivan J.A., Wang H., Yang J., Shen Y., Rubio V., Ma L.,
RA Hoecker U., Deng X.W.;
RT "The COP1-SPA1 interaction defines a critical step in phytochrome A-
RT mediated regulation of HY5 activity.";
RL Genes Dev. 17:2642-2647(2003).
RN [11]
RP FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15308756; DOI=10.1105/tpc.104.024216;
RA Laubinger S., Fittinghoff K., Hoecker U.;
RT "The SPA quartet: a family of WD-repeat proteins with a central role in
RT suppression of photomorphogenesis in Arabidopsis.";
RL Plant Cell 16:2293-2306(2004).
RN [12]
RP INTERACTION WITH HFR1.
RX PubMed=15960622; DOI=10.1111/j.1365-313x.2005.02433.x;
RA Yang J., Lin R., Hoecker U., Liu B., Xu L., Wang H.;
RT "Repression of light signaling by Arabidopsis SPA1 involves post-
RT translational regulation of HFR1 protein accumulation.";
RL Plant J. 43:131-141(2005).
RN [13]
RP CHARACTERIZATION, AND MUTAGENESIS OF LEU-573; ALA-580; LYS-767; TRP-812 AND
RP GLY-869.
RX PubMed=16813572; DOI=10.1111/j.1365-313x.2006.02811.x;
RA Yang J., Wang H.;
RT "The central coiled-coil domain and carboxyl-terminal WD-repeat domain of
RT Arabidopsis SPA1 are responsible for mediating repression of light
RT signaling.";
RL Plant J. 47:564-576(2006).
RN [14]
RP FUNCTION, AND INDUCTION.
RX PubMed=16709190; DOI=10.1111/j.1365-313x.2006.02737.x;
RA Ishikawa M., Kiba T., Chua N.-H.;
RT "The Arabidopsis SPA1 gene is required for circadian clock function and
RT photoperiodic flowering.";
RL Plant J. 46:736-746(2006).
RN [15]
RP FUNCTION, CHARACTERIZATION, AND INDUCTION BY LIGHT.
RX PubMed=16813571; DOI=10.1111/j.1365-313x.2006.02812.x;
RA Fittinghoff K., Laubinger S., Nixdorf M., Fackendahl P., Baumgardt R.-L.,
RA Batschauer A., Hoecker U.;
RT "Functional and expression analysis of Arabidopsis SPA genes during
RT seedling photomorphogenesis and adult growth.";
RL Plant J. 47:577-590(2006).
RN [16]
RP FUNCTION, INTERACTION WITH CO, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16854975; DOI=10.1242/dev.02481;
RA Laubinger S., Marchal V., Le Gourrierec J., Wenkel S., Adrian J., Jang S.,
RA Kulajta C., Braun H., Coupland G., Hoecker U.;
RT "Arabidopsis SPA proteins regulate photoperiodic flowering and interact
RT with the floral inducer CONSTANS to regulate its stability.";
RL Development 133:3213-3222(2006).
RN [17]
RP INTERACTION WITH PHYA, AND INDUCTION.
RX PubMed=18722184; DOI=10.1016/j.molcel.2008.08.003;
RA Saijo Y., Zhu D., Li J., Rubio V., Zhou Z., Shen Y., Hoecker U., Wang H.,
RA Deng X.W.;
RT "Arabidopsis COP1/SPA1 complex and FHY1/FHY3 associate with distinct
RT phosphorylated forms of phytochrome A in balancing light signaling.";
RL Mol. Cell 31:607-613(2008).
RN [18]
RP DWD MOTIF.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [19]
RP FUNCTION, AND INTERACTION WITH CRY2.
RX PubMed=21514160; DOI=10.1016/j.cub.2011.03.048;
RA Zuo Z., Liu H., Liu B., Liu X., Lin C.;
RT "Blue light-dependent interaction of CRY2 with SPA1 regulates COP1 activity
RT and floral initiation in Arabidopsis.";
RL Curr. Biol. 21:841-847(2011).
RN [20]
RP INTERACTION WITH CRY1 AND CRY2, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21511872; DOI=10.1101/gad.2025111;
RA Lian H.-L., He S.-B., Zhang Y.-C., Zhu D.-M., Zhang J.-Y., Jia K.-P.,
RA Sun S.-X., Li L., Yang H.-Q.;
RT "Blue-light-dependent interaction of cryptochrome 1 with SPA1 defines a
RT dynamic signaling mechanism.";
RL Genes Dev. 25:1023-1028(2011).
RN [21]
RP INTERACTION WITH CRY1, AND DISRUPTION PHENOTYPE.
RX PubMed=21511871; DOI=10.1101/gad.2025011;
RA Liu B., Zuo Z., Liu H., Liu X., Lin C.;
RT "Arabidopsis cryptochrome 1 interacts with SPA1 to suppress COP1 activity
RT in response to blue light.";
RL Genes Dev. 25:1029-1034(2011).
RN [22]
RP INTERACTION WITH CRY2, AND SUBCELLULAR LOCATION.
RX PubMed=22739826; DOI=10.1105/tpc.112.098210;
RA Weidler G., Zur Oven-Krockhaus S., Heunemann M., Orth C., Schleifenbaum F.,
RA Harter K., Hoecker U., Batschauer A.;
RT "Degradation of Arabidopsis CRY2 is regulated by SPA proteins and
RT phytochrome A.";
RL Plant Cell 24:2610-2623(2012).
CC -!- FUNCTION: Controls normal photoperiodic flowering and regulates
CC circadian rhythms. Required for suppression of photomorphogenesis in
CC dark-grown seedlings and for normal elongation growth of adult plants.
CC Integral component of the COP1/SPA E3 ubiquitin-protein ligase complex.
CC Involved in HY5, HFR1, LAF1 and CO degradation.
CC {ECO:0000269|PubMed:11457980, ECO:0000269|PubMed:12244439,
CC ECO:0000269|PubMed:12827204, ECO:0000269|PubMed:15308756,
CC ECO:0000269|PubMed:16709190, ECO:0000269|PubMed:16813571,
CC ECO:0000269|PubMed:16854975, ECO:0000269|PubMed:21514160}.
CC -!- SUBUNIT: Interacts with CO, COP1, HFR1, HY5 and PHYA. Light induces
CC dissociation of the SPA1/COP1 complex. Binds to CRY1 in response to
CC blue light, this interaction prevents SPA1/COP1 complex formation but
CC stimulate CRY2/COP1 complex, and thus avoid COP1-dependent degradation
CC of the transcription factor HY5 by the proteasome and promotes
CC hypocotyl elongation (PubMed:21514160, PubMed:21511872,
CC PubMed:21511871, PubMed:22739826). {ECO:0000269|PubMed:11461903,
CC ECO:0000269|PubMed:14597662, ECO:0000269|PubMed:15960622,
CC ECO:0000269|PubMed:16854975, ECO:0000269|PubMed:18722184,
CC ECO:0000269|PubMed:21511871, ECO:0000269|PubMed:21511872,
CC ECO:0000269|PubMed:21514160, ECO:0000269|PubMed:22739826}.
CC -!- INTERACTION:
CC Q9SYX2; O50055: COL1; NbExp=10; IntAct=EBI-626992, EBI-1112154;
CC Q9SYX2; P43254: COP1; NbExp=17; IntAct=EBI-626992, EBI-301649;
CC Q9SYX2; Q9FE22: HFR1; NbExp=3; IntAct=EBI-626992, EBI-626001;
CC Q9SYX2; Q9SYX2: SPA1; NbExp=6; IntAct=EBI-626992, EBI-626992;
CC Q9SYX2; Q9LJR3: SPA3; NbExp=7; IntAct=EBI-626992, EBI-626921;
CC Q9SYX2; Q94BM7: SPA4; NbExp=9; IntAct=EBI-626992, EBI-626943;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:10205059,
CC ECO:0000269|PubMed:16854975}. Nucleus {ECO:0000269|PubMed:22739826}.
CC Nucleus, PML body {ECO:0000269|PubMed:21511872}. Note=Present in
CC nuclear bodies (NBs). {ECO:0000269|PubMed:21511872}.
CC -!- INDUCTION: By PHYA under continuous far-red light. Circadian-regulation
CC under constant light. Up-regulated by red, far-red and blue light, and
CC during the night phase under short-day conditions.
CC {ECO:0000269|PubMed:16709190, ECO:0000269|PubMed:16813571,
CC ECO:0000269|PubMed:16854975, ECO:0000269|PubMed:18722184}.
CC -!- DOMAIN: The coiled-coil domain (557-589) and the WD-repeat domain are
CC sufficient for SPA1 function. The coiled-coil domain is necessary and
CC sufficient for interactions with HFR1 and COP1. The protein kinase
CC domain may play a role in promoting destabilization of SPA1 under far-
CC red light. The DWD box is required for interaction with DDB1A (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced hypocotyl elongation in blue light.
CC {ECO:0000269|PubMed:21511871}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD23037.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g46340 and At2g46350.; Evidence={ECO:0000305};
CC Sequence=AAD23038.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g46340 and At2g46350.; Evidence={ECO:0000305};
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DR EMBL; AF135455; AAD30124.1; -; mRNA.
DR EMBL; AC006526; AAD23037.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006526; AAD23038.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10681.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63147.1; -; Genomic_DNA.
DR EMBL; AK227186; BAE99225.1; -; mRNA.
DR EMBL; AK221994; BAD94577.1; -; mRNA.
DR PIR; F84901; F84901.
DR PIR; G84901; G84901.
DR RefSeq; NP_001325255.1; NM_001337186.1.
DR RefSeq; NP_182157.2; NM_130197.5.
DR AlphaFoldDB; Q9SYX2; -.
DR SMR; Q9SYX2; -.
DR BioGRID; 4577; 20.
DR DIP; DIP-33538N; -.
DR IntAct; Q9SYX2; 7.
DR STRING; 3702.AT2G46340.1; -.
DR iPTMnet; Q9SYX2; -.
DR PaxDb; Q9SYX2; -.
DR PRIDE; Q9SYX2; -.
DR ProteomicsDB; 232481; -.
DR EnsemblPlants; AT2G46340.1; AT2G46340.1; AT2G46340.
DR EnsemblPlants; AT2G46340.2; AT2G46340.2; AT2G46340.
DR GeneID; 819242; -.
DR Gramene; AT2G46340.1; AT2G46340.1; AT2G46340.
DR Gramene; AT2G46340.2; AT2G46340.2; AT2G46340.
DR KEGG; ath:AT2G46340; -.
DR Araport; AT2G46340; -.
DR TAIR; locus:2039139; AT2G46340.
DR eggNOG; KOG1033; Eukaryota.
DR HOGENOM; CLU_006994_1_1_1; -.
DR InParanoid; Q9SYX2; -.
DR OMA; GCIKLLR; -.
DR OrthoDB; 857220at2759; -.
DR PhylomeDB; Q9SYX2; -.
DR PRO; PR:Q9SYX2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SYX2; baseline and differential.
DR Genevisible; Q9SYX2; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0010100; P:negative regulation of photomorphogenesis; IMP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010017; P:red or far-red light signaling pathway; IMP:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IDA:UniProtKB.
DR GO; GO:0009637; P:response to blue light; IDA:UniProtKB.
DR GO; GO:0010218; P:response to far red light; IEP:TAIR.
DR GO; GO:0010114; P:response to red light; IEP:TAIR.
DR GO; GO:0048575; P:short-day photoperiodism, flowering; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR044630; SPA1/2/3/4.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44218; PTHR44218; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Nucleotide-binding; Nucleus;
KW Phytochrome signaling pathway; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..1029
FT /note="Protein SUPPRESSOR OF PHYA-105 1"
FT /id="PRO_0000363491"
FT DOMAIN 188..529
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 714..753
FT /note="WD 1"
FT REPEAT 763..803
FT /note="WD 2"
FT REPEAT 806..846
FT /note="WD 3"
FT REPEAT 848..888
FT /note="WD 4"
FT REPEAT 892..930
FT /note="WD 5"
FT REPEAT 932..971
FT /note="WD 6"
FT REPEAT 997..1029
FT /note="WD 7"
FT REGION 42..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 557..589
FT /evidence="ECO:0000255"
FT MOTIF 866..881
FT /note="DWD box"
FT COMPBIAS 228..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 194..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 573
FT /note="L->R: No effect. Loss of function; when associated
FT with K-580."
FT /evidence="ECO:0000269|PubMed:16813572"
FT MUTAGEN 580
FT /note="A->K: Loss of function. Loss of function; when
FT associated with R-573."
FT /evidence="ECO:0000269|PubMed:16813572"
FT MUTAGEN 767
FT /note="K->E: Loss of function."
FT /evidence="ECO:0000269|PubMed:16813572"
FT MUTAGEN 812
FT /note="W->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:16813572"
FT MUTAGEN 869
FT /note="G->E: Loss of function."
FT /evidence="ECO:0000269|PubMed:16813572"
FT CONFLICT 19
FT /note="L -> S (in Ref. 4; BAE99225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1029 AA; 114686 MW; 8DEDF32BB06B4A18 CRC64;
MPVMERVAEE TVATNNIQLK ARVDDVPCNK LDARHNDMVI QSETANSDCP GSSAHRNVDL
TKPPPPEEAA GAKLSVEELT LGNYRIVQGS NNTNVDSPRA GKFEHLYRLA RGSAFRAGDG
DLDSQPRDMD QMLSRIRQQL AGAPSERQNL KPFMSRRSDQ NLEAFSERLR AAGENSIMNA
PALISEGVQM KTPVSSSNFS QLLLKRAMKG KGVVGKNQET PPEFVSDQDL GSKEKKLDIS
KSPTPHDVLP LKSSPKGNGM VSHGDGNHSK SSIGISLREF LRSSYAKREK RHGLCLFRQL
VELVDSAHSK RLFLLDLRPS LFTLVPSKKL RYIGNFGKND LESDVDEDLN RRRPVVEESS
SGGRDSKKRK MDLHLNSPGN QLQATSTGRP FKRKSPVIDL NMVDARNPDS CELQQQDYIK
NLSVSSVSRK QSMSTWLEEQ WYTCPEEING EDIGEKSNIY ALGVLLFELL CHCESGEMHA
AMMADLRHRI LPPTFLSKYP KEAGFCLWLL HPEPSSRPSA RDILKSELIC EDDSVKSTAA
AEEISELLLH FLSSLEVQKK KKASKLLQDI QTLEDDIKEA ERRYSSNVSL VRSHGAIEKR
VQSSPLDEHC TTSSALFVPT ANTDRLMSNI RQLEDAYFFM RSQINLSSSA ATARSDKTLK
DRDRCSENQN ENQDMSTKGK SSDQLEVFFE GLCKFARYSK FETCGTIRSG DLLNSASVVC
SLSFDPDEEH IAAAGISKKI KIFDFNAFMN ESVGVHYPLV EMVNKSKLSC VCWNSYIKNY
LASTDYDGVV QIWDAGTGQG FSQYTEHQKR AWSVDFSPSD PTKFVSGSDD CSVKLWSINE
KRSLGTIWSP ANVCCVQFSS YSNHLLAFGS ADYKVYCYDL RYVKTPWCTL AGHEKAVSYV
KFMDSETIVS ASTDNSLKLW NLNKTNSSGL SPGACSLTYK GHTNQKNFVG LSVLDGYIAC
GSETNEVYSY YKSLPMPMTS YKFGSVDPIS GNEYFDDNGQ FVSSVCWRKK SNMLVAANST
GNMKLLKLV
