SPK1_ARATH
ID SPK1_ARATH Reviewed; 1830 AA.
AC Q8SAB7; O23479; Q152R9;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Guanine nucleotide exchange factor SPIKE 1 {ECO:0000303|PubMed:11826302};
GN Name=SPK1 {ECO:0000303|PubMed:11826302};
GN OrderedLocusNames=At4g16340 {ECO:0000312|Araport:AT4G16340};
GN ORFNames=dl4200c {ECO:0000312|EMBL:CAB10411.1},
GN FCAALL.346 {ECO:0000312|EMBL:CAB78676.1};
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 {ECO:0000312|EMBL:AAL74193.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11826302; DOI=10.1105/tpc.010346;
RA Qiu J.-L., Jilk R., Marks M.D., Szymanski D.B.;
RT "The Arabidopsis SPIKE1 gene is required for normal cell shape control and
RT tissue development.";
RL Plant Cell 14:101-118(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 [GENOMIC DNA] OF 718-756.
RA Basu D., Szymanski D.B.;
RT "SPIKE1 genomic sequence (exons 17-18).";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBUNIT, INTERACTION WITH ARAC4/ROP2; ARAC6/ROP5; ARAC9/ROP8; SCAR1; SCAR2;
RP SCAR3; SCAR4; ABI1; ABI2; ABI3 AND ABI4, AND HOMODIMERIZATION.
RX PubMed=17267444; DOI=10.1242/dev.02792;
RA Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M.,
RA Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.;
RT "The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell
RT morphogenesis.";
RL Development 134:967-977(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1051 AND SER-1095, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND INTERACTION WITH ARAC4/ROP2;
RP ARAC1/ROP3; ARAC5/ROP4; ARAC6/ROP5 AND ARAC8/ROP10.
RC STRAIN=cv. Columbia;
RX PubMed=18308939; DOI=10.1073/pnas.0710294105;
RA Basu D., Le J., Zakharova T., Mallery E.L., Szymanski D.B.;
RT "A SPIKE1 signaling complex controls actin-dependent cell morphogenesis
RT through the heteromeric WAVE and ARP2/3 complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4044-4049(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1051 AND THR-1079, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=21109438; DOI=10.1016/j.cub.2010.11.016;
RA Zhang C., Kotchoni S.O., Samuels A.L., Szymanski D.B.;
RT "SPIKE1 signals originate from and assemble specialized domains of the
RT endoplasmic reticulum.";
RL Curr. Biol. 20:2144-2149(2010).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP ARAC3/ROP6.
RX PubMed=22683260; DOI=10.1016/j.cub.2012.05.019;
RA Lin D., Nagawa S., Chen J., Cao L., Chen X., Xu T., Li H., Dhonukshe P.,
RA Yamamuro C., Friml J., Scheres B., Fu Y., Yang Z.;
RT "A ROP GTPase-dependent auxin signaling pathway regulates the subcellular
RT distribution of PIN2 in Arabidopsis roots.";
RL Curr. Biol. 22:1319-1325(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF
CC proteins activate small GTPases by exchanging bound GDP for free GTP.
CC Controls actin polymerization via the two heteromeric complexes WAVE
CC and actin-related protein (ARP) 2/3 (PubMed:18308939). Involved in
CC cytoskeletal reorganization required for cell shape (e.g. trichome and
CC cotyledon) control and tissue development (PubMed:11826302). Promotes
CC polarized growth and cell-cell adhesion in the leaf epidermis probably
CC by promoting the formation of endoplasmic reticulum (ER) exit site
CC (ERES) and/or trafficking between the ER and Golgi (PubMed:21109438).
CC Triggers ARAC3/ROP6 activation required for auxin-mediated inhibition
CC of PIN2 internalization during gravitropic responses (,
CC PubMed:22683260). {ECO:0000269|PubMed:11826302,
CC ECO:0000269|PubMed:18308939, ECO:0000269|PubMed:21109438,
CC ECO:0000269|PubMed:22683260}.
CC -!- SUBUNIT: Homodimer. Component of SCAR/WAVE and ARP2/3 complexes.
CC Interacts directly with ARAC4/ROP2, ARAC1/ROP3, ARAC5/ROP4, ARAC6/ROP5,
CC ARAC8/ROP10, ARAC9/ROP8, SCAR1, SCAR2, SCAR3, SCAR4, ABI1, ABI2, ABI3
CC and ABI4 (PubMed:17267444, PubMed:18308939). Binds to the inactive GDP-
CC bound form of ARAC3/ROP6 (PubMed:22683260).
CC {ECO:0000269|PubMed:17267444, ECO:0000269|PubMed:18308939,
CC ECO:0000269|PubMed:22683260}.
CC -!- INTERACTION:
CC Q8SAB7; Q38919: ARAC4; NbExp=3; IntAct=EBI-1547917, EBI-1548187;
CC Q8SAB7; Q9SBJ6: ARAC6; NbExp=2; IntAct=EBI-1547917, EBI-1548024;
CC Q8SAB7; Q5XPJ9: SCAR2; NbExp=3; IntAct=EBI-1547917, EBI-1547795;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B2RY04}.
CC Endoplasmic reticulum membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:21109438}. Nucleus {ECO:0000269|PubMed:21109438}.
CC Note=Accumulates at, and promotes the formation of, a specialized
CC domain of the endoplasmic reticulum termed the ER exit site (ERES).
CC {ECO:0000269|PubMed:21109438}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, in roots and aerial organs.
CC {ECO:0000269|PubMed:11826302, ECO:0000269|PubMed:22683260}.
CC -!- DOMAIN: The DOCKER domain may mediate some GEF activity.
CC {ECO:0000250|UniProtKB:Q14185}.
CC -!- DISRUPTION PHENOTYPE: Dwarf in spk1-1 and spk1-5 (PubMed:22683260).
CC Seedling lethal with trichome, cotyledon, and leaf-shape defects due to
CC a misregulation of laterally clustered foci of microtubules and
CC polarized growth in epidermal cells. Sporophytic sterility. Trichomes
CC show a reduced branch number and an irregular swelling along the stalk
CC and branches (PubMed:11826302, PubMed:18308939). Enlarged endoplasmic
CC reticulum (ER) cisternae and constitutively activated ER stress
CC response (PubMed:21109438). Increased lateral root density and retarded
CC gravitropic responses associated with PIN2 internalization. In spk1-4,
CC enhanced cell shape changes induced by ROP6 overexpression, and reduced
CC active ROP6 (GTP-bound) levels (PubMed:22683260).
CC {ECO:0000269|PubMed:11826302, ECO:0000269|PubMed:18308939,
CC ECO:0000269|PubMed:21109438, ECO:0000269|PubMed:22683260}.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC ProRule:PRU00983}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10411.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78676.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF465831; AAL74193.1; -; mRNA.
DR EMBL; Z97340; CAB10411.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161543; CAB78676.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83733.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM68002.1; -; Genomic_DNA.
DR EMBL; DQ649023; ABG35746.1; -; Genomic_DNA.
DR PIR; A71430; A71430.
DR RefSeq; NP_001319958.1; NM_001341097.1.
DR RefSeq; NP_193367.7; NM_117729.8.
DR AlphaFoldDB; Q8SAB7; -.
DR SMR; Q8SAB7; -.
DR DIP; DIP-29817N; -.
DR IntAct; Q8SAB7; 17.
DR STRING; 3702.AT4G16340.1; -.
DR iPTMnet; Q8SAB7; -.
DR PaxDb; Q8SAB7; -.
DR PRIDE; Q8SAB7; -.
DR ProteomicsDB; 226778; -.
DR EnsemblPlants; AT4G16340.1; AT4G16340.1; AT4G16340.
DR EnsemblPlants; AT4G16340.2; AT4G16340.2; AT4G16340.
DR GeneID; 827328; -.
DR Gramene; AT4G16340.1; AT4G16340.1; AT4G16340.
DR Gramene; AT4G16340.2; AT4G16340.2; AT4G16340.
DR KEGG; ath:AT4G16340; -.
DR Araport; AT4G16340; -.
DR TAIR; locus:2130484; AT4G16340.
DR eggNOG; KOG1997; Eukaryota.
DR HOGENOM; CLU_237262_0_0_1; -.
DR InParanoid; Q8SAB7; -.
DR OMA; DLNDGHH; -.
DR OrthoDB; 20156at2759; -.
DR PhylomeDB; Q8SAB7; -.
DR PRO; PR:Q8SAB7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8SAB7; baseline and differential.
DR Genevisible; Q8SAB7; AT.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009958; P:positive gravitropism; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IMP:UniProtKB.
DR GO; GO:0010928; P:regulation of auxin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:TAIR.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR043161; DOCK_C_lobe_A.
DR InterPro; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR027357; DOCKER_dom.
DR PANTHER; PTHR23317; PTHR23317; 1.
DR Pfam; PF06920; DHR-2; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Auxin signaling pathway; Cytoplasm; Developmental protein;
KW Endoplasmic reticulum; Guanine-nucleotide releasing factor; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1830
FT /note="Guanine nucleotide exchange factor SPIKE 1"
FT /id="PRO_0000432532"
FT DOMAIN 463..622
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT DOMAIN 1379..1828
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 285..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 1079
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
SQ SEQUENCE 1830 AA; 206829 MW; 18CD66FB9B328A1F CRC64;
MENNNLGLRF RKLPRQPLAL PKLDPLLDEN LEQWPHLNQL VQCYGTEWVK DVNKYGHYEN
IRPDSFQTQI FEGPDTDTET EIRLASARSA TIEEDVASIS GRPFSDPGSS KHFGQPPLPA
YEPAFDWENE RAMIFGQRTP ESPAASYSSG LKISVRVLSL AFQSGLVEPF FGSIALYNQE
RKEKLSEDFY FQIQPTEMQD AKLSSENRGV FYLDAPSASV CLLIQLEKTA TEEGGVTSSV
YSRKEPVHLT EREKQKLQVW SRIMPYRESF AWAVVPLFDN NLTTNTGESA SPSSPLAPSM
TASSSHDGVY EPIAKITSDG KQGYSGGSSV VVEISNLNKV KESYSEESIQ DPKRKVHKPV
KGVLRLEIEK HRNGHGDFED LSENGSIIND SLDPTDRLSD LTLMKCPSSS SGGPRNGCSK
WNSEDAKDVS RNLTSSCGTP DLNCYHAFDF CSTTRNEPFL HLFHCLYVYP VAVTLSRKRN
PFIRVELRKD DTDIRKQPLE AIYPREPGVS LQKWVHTQVA VGARAASYHD EIKVSLPATW
TPSHHLLFTF FHVDLQTKLE APRPVVVGYA SLPLSTYIHS RSDISLPVMR ELVPHYLQES
TKERLDYLED GKNIFKLRLR LCSSLYPTNE RVRDFCLEYD RHTLQTRPPW GSELLQAINS
LKHVDSTALL QFLYPILNML LHLIGNGGET LQVAAFRAMV DILTRVQQVS FDDADRNRFL
VTYVDYSFDD FGGNQPPVYP GLATVWGSLA RSKAKGYRVG PVYDDVLSMA WFFLELIVKS
MALEQARLYD HNLPTGEDVP PMQLKESVFR CIMQLFDCLL TEVHERCKKG LSLAKRLNSS
LAFFCYDLLY IIEPCQVYEL VSLYMDKFSG VCQSVLHECK LTFLQIISDH DLFVEMPGRD
PSDRNYLSSI LIQELFLSLD HDELPLRAKG ARILVILLCK HEFDARYQKA EDKLYIAQLY
FPFVGQILDE MPVFYNLNAT EKREVLIGVL QIVRNLDDTS LVKAWQQSIA RTRLYFKLME
ECLILFEHKK AADSILGGNN SRGPVSEGAG SPKYSERLSP AINNYLSEAS RQEVRLEGTP
DNGYLWQRVN SQLASPSQPY SLREALAQAQ SSRIGASAQA LRESLHPILR QKLELWEENV
SATVSLQVLE ITENFSSMAA SHNIATDYGK LDCITTILTS FFSRNQSLAF WKAFFPIFNR
IFDLHGATLM ARENDRFLKQ IAFHLLRLAV YRNDSVRKRA VIGLQILVKS SLYFMQTARL
RALLTITLSE LMSDVQVTHM KSDNTLEESG EARRLQQSLS EMADEAKSVN LLRECGLPDD
TLLIIPEKFT ENRWSWAEVK HLSDSLVLAL DASLGHALLG SVMAMDRYAA AESFYKLGMA
FAPVPDLHIM WLLHLCDAHQ EMQSWAEAAQ CAVAVAGVIM QALVARNDGV WSKDHVSALR
KICPMVSGEF TTEASAAEVE GYGASKLTVD SAVKYLQLAN KLFSQAELYH FCASILELVI
PVYKSRKAYG QLAKCHTLLT NIYESILDQE SNPIPFIDAT YYRVGFYGEK FGKLDRKEYV
YREPRDVRLG DIMEKLSHIY ESRMDSNHIL HIIPDSRQVK AEDLQAGVCY LQITAVDAVM
EDEDLGSRRE RIFSLSTGSV RARVFDRFLF DTPFTKNGKT QGGLEDQWKR RTVLQTEGSF
PALVNRLLVT KSESLEFSPV ENAIGMIETR TTALRNELEE PRSSDGDHLP RLQSLQRILQ
GSVAVQVNSG VLSVCTAFLS GEPATRLRSQ ELQQLIAALL EFMAVCKRAI RVHFRLIGEE
DQEFHTQLVN GFQSLTAELS HYIPAILSEL
