MYO15_ARATH
ID MYO15_ARATH Reviewed; 1522 AA.
AC Q0WPU1; Q9SMY9;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Myosin-15;
DE AltName: Full=Myosin XI I;
DE Short=AtXI-I;
GN Name=XI-I; Synonyms=KAKU1 {ECO:0000303|PubMed:23973298};
GN OrderedLocusNames=At4g33200 {ECO:0000312|Araport:AT4G33200};
GN ORFNames=F4I10.130 {ECO:0000312|EMBL:CAB36794.2};
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 [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 [2]
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 [3]
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 [4]
RP GENE FAMILY.
RX PubMed=10984423; DOI=10.1242/jcs.113.19.3353;
RA Hodge T., Cope M.J.;
RT "A myosin family tree.";
RL J. Cell Sci. 113:3353-3354(2000).
RN [5]
RP GENE FAMILY.
RX PubMed=11516337; DOI=10.1186/gb-2001-2-7-research0024;
RA Reddy A.S., Day I.S.;
RT "Analysis of the myosins encoded in the recently completed Arabidopsis
RT thaliana genome sequence.";
RL Genome Biol. 2:RESEARCH0024.1-RESEARCH0024.17(2001).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17288617; DOI=10.1186/1471-2229-7-6;
RA Reisen D., Hanson M.R.;
RT "Association of six YFP-myosin XI-tail fusions with mobile plant cell
RT organelles.";
RL BMC Plant Biol. 7:6-6(2007).
RN [7]
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=17500056; DOI=10.1074/jbc.m700645200;
RA Li J.F., Nebenfuehr A.;
RT "Organelle targeting of myosin XI is mediated by two globular tail
RT subdomains with separate cargo binding sites.";
RL J. Biol. Chem. 282:20593-20602(2007).
RN [8]
RP FUNCTION.
RX PubMed=19369591; DOI=10.1104/pp.109.136853;
RA Avisar D., Abu-Abied M., Belausov E., Sadot E., Hawes C., Sparkes I.A.;
RT "A comparative study of the involvement of 17 Arabidopsis myosin family
RT members on the motility of Golgi and other organelles.";
RL Plant Physiol. 150:700-709(2009).
RN [9]
RP FUNCTION.
RX PubMed=20581304; DOI=10.1105/tpc.110.076315;
RA Peremyslov V.V., Prokhnevsky A.I., Dolja V.V.;
RT "Class XI myosins are required for development, cell expansion, and F-Actin
RT organization in Arabidopsis.";
RL Plant Cell 22:1883-1897(2010).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21233331; DOI=10.1104/pp.110.170720;
RA Peremyslov V.V., Mockler T.C., Filichkin S.A., Fox S.E., Jaiswal P.,
RA Makarova K.S., Koonin E.V., Dolja V.V.;
RT "Expression, splicing, and evolution of the myosin gene family in plants.";
RL Plant Physiol. 155:1191-1204(2011).
RN [11]
RP FUNCTION.
RX PubMed=21914656; DOI=10.1093/jxb/err265;
RA Avisar D., Abu-Abied M., Belausov E., Sadot E.;
RT "Myosin XIK is a major player in cytoplasm dynamics and is regulated by two
RT amino acids in its tail.";
RL J. Exp. Bot. 63:241-249(2012).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP WIT1 AND WIT2.
RX PubMed=23973298; DOI=10.1016/j.cub.2013.07.035;
RA Tamura K., Iwabuchi K., Fukao Y., Kondo M., Okamoto K., Ueda H.,
RA Nishimura M., Hara-Nishimura I.;
RT "Myosin XI-i links the nuclear membrane to the cytoskeleton to control
RT nuclear movement and shape in Arabidopsis.";
RL Curr. Biol. 23:1776-1781(2013).
RN [13]
RP INTERACTION WITH MYOB1 AND MYOB7.
RX PubMed=23995081; DOI=10.1105/tpc.113.113704;
RA Peremyslov V.V., Morgun E.A., Kurth E.G., Makarova K.S., Koonin E.V.,
RA Dolja V.V.;
RT "Identification of myosin XI receptors in Arabidopsis defines a distinct
RT class of transport vesicles.";
RL Plant Cell 25:3022-3038(2013).
RN [14]
RP REVIEW.
RX PubMed=25740919; DOI=10.1093/jxb/erv082;
RA Zhou X., Graumann K., Meier I.;
RT "The plant nuclear envelope as a multifunctional platform LINCed by SUN and
RT KASH.";
RL J. Exp. Bot. 66:1649-1659(2015).
RN [15]
RP FUNCTION, INTERACTION WITH WIT1 AND WIT2, AND SUBUNIT.
RX PubMed=25759303; DOI=10.1080/19491034.2014.1003512;
RA Zhou X., Groves N.R., Meier I.;
RT "Plant nuclear shape is independently determined by the SUN-WIP-WIT2-myosin
RT XI-i complex and CRWN1.";
RL Nucleus 6:144-153(2015).
CC -!- FUNCTION: Myosin heavy chain that is required for the cell cycle-
CC regulated transport of various organelles and proteins for their
CC segregation. Functions by binding with its tail domain to receptor
CC proteins on organelles and exerting force with its N-terminal motor
CC domain against actin filaments, thereby transporting its cargo along
CC polarized actin cables. Involved in trafficking of Golgi stacks and
CC mitochondria. Plays a role in nuclear shape determination. Drives
CC nuclear movement along actin filaments (PubMed:23973298). As component
CC of the SUN-WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic
CC forces to the nuclear envelope (NE), leading to nuclear shape changes
CC (PubMed:25759303). {ECO:0000269|PubMed:19369591,
CC ECO:0000269|PubMed:20581304, ECO:0000269|PubMed:21914656,
CC ECO:0000269|PubMed:23973298, ECO:0000269|PubMed:25759303}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with MYOB1 and MYOB7
CC (PubMed:23995081). Interacts with WIT1 and WIT2 (PubMed:23973298,
CC PubMed:25759303). Core component of the LINC complex which is composed
CC of inner nuclear membrane SUN domain-containing proteins coupled to
CC outer nuclear membrane WIP and WIT proteins. The LINC complex also
CC involves nucleoskeletal proteins CRWN/LINC and possibly KAKU4 and the
CC cytoskeletal myosin KAKU1 (PubMed:25759303). {ECO:0000250,
CC ECO:0000269|PubMed:23973298, ECO:0000269|PubMed:23995081,
CC ECO:0000269|PubMed:25759303}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17288617,
CC ECO:0000269|PubMed:17500056}. Nucleus membrane
CC {ECO:0000269|PubMed:23973298}. Note=Colocalizes with peroxisome,
CC cytoplasmic vesicles and/or organelles. Nucleus membrane localization
CC is dependent of the WIT2 association. {ECO:0000269|PubMed:17288617,
CC ECO:0000269|PubMed:17500056}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q0WPU1-1; Sequence=Displayed;
CC -!- DOMAIN: IQ domain mediates interaction with calmodulin. {ECO:0000250}.
CC -!- DOMAIN: The tail domain is a globular cargo-binding domain.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Impaired nuclear movement. Abnormal nucleus shape
CC with invaginated envelope. {ECO:0000269|PubMed:23973298}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. Plant myosin class XI subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36794.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80037.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035525; CAB36794.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161583; CAB80037.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86188.1; -; Genomic_DNA.
DR EMBL; AK228969; BAF00858.1; -; mRNA.
DR PIR; D85390; D85390.
DR PIR; T05200; T05200.
DR RefSeq; NP_195046.3; NM_119474.5. [Q0WPU1-1]
DR AlphaFoldDB; Q0WPU1; -.
DR SMR; Q0WPU1; -.
DR BioGRID; 14741; 3.
DR STRING; 3702.AT4G33200.1; -.
DR iPTMnet; Q0WPU1; -.
DR PaxDb; Q0WPU1; -.
DR PRIDE; Q0WPU1; -.
DR ProteomicsDB; 251007; -. [Q0WPU1-1]
DR EnsemblPlants; AT4G33200.1; AT4G33200.1; AT4G33200. [Q0WPU1-1]
DR GeneID; 829456; -.
DR Gramene; AT4G33200.1; AT4G33200.1; AT4G33200. [Q0WPU1-1]
DR KEGG; ath:AT4G33200; -.
DR Araport; AT4G33200; -.
DR TAIR; locus:2125929; AT4G33200.
DR eggNOG; KOG0160; Eukaryota.
DR InParanoid; Q0WPU1; -.
DR PhylomeDB; Q0WPU1; -.
DR PRO; PR:Q0WPU1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WPU1; baseline and differential.
DR Genevisible; Q0WPU1; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; ISS:TAIR.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; TAS:TAIR.
DR GO; GO:0007097; P:nuclear migration; IMP:UniProtKB.
DR GO; GO:2000769; P:regulation of establishment or maintenance of cell polarity regulating cell shape; IMP:UniProtKB.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd15475; MyosinXI_CBD; 1.
DR CDD; cd01384; MYSc_Myo11; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR037975; MyosinXI_CBD.
DR InterPro; IPR036018; MYSc_Myo11.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Coiled coil; Cytoplasm; Membrane; Motor protein; Myosin;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1522
FT /note="Myosin-15"
FT /id="PRO_0000422870"
FT DOMAIN 12..61
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 67..737
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 763..792
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 788..817
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 811..840
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 836..865
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 859..888
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1164..1456
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 499..533
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 535..558
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 593..618
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 618..640
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT COILED 889..1059
FT /evidence="ECO:0000255"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 214..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1522 AA; 173363 MW; 9BC436B0BFE5227C CRC64;
MRNCLPMELN LRKGDKVWVE DKDLAWIAAD VLDSFDNKLH VETSTGKKVF VSPEKLFRRD
PDDEEHNGVD DMTKLTYLHE AGVLYNLQRR YALNDIYTYT GSILIAVNPF KKLPHLYNGH
MMEQYMGAPF GELSPHVFAV SDVAYRAMID DSRSQSILVS GESGAGKTET TKLIMQYLTF
VGGRATDDDR SVEQQVLESN PLLEAFGNAK TVRNDNSSRF GKFVEIQFDT NGRISGAAIR
TYLLERSRVV RITDPERNYH CFYQLCASGN DAEKYKLSNP RQFHYLNQSK TYELEGVSSA
EEYKNTRRAM DIVGISQDEQ EGIFRTLAAI LHLGNVEFSS GREHDSSVVK DPESRHHLQM
AADLFKCDAN LLLASLCTRS ILTREGIIIK ALDPNAAVTS RDTLAKTVYA HLFDWLVDKI
NKSVGQDPES RFQIGVLDIY GFECFKNNSF EQFCINFANE KLQQHFNEHV FKMEQDEYRK
EEINWSYIEF IDNQDVLDLI EKKPIGVIAL LDEACMFPRS THESFSMKLF QNFRFHPRLE
KPKFSETDFT LSHYAGKVTY QTEAFLDKNR DYTIVEHCNL LSSSKCPFVA GIFPSAPEES
TRSSYKFSSV SSRFKQQLQA LMETLSKTEP HYVRCVKPNS LNRPQKFESL SVLHQLRCGG
VLEAVRISLA GYPTRRNYSD FVDRFGLLAP EFMDESNDEQ ALTEKILSKL GLGNYQLGRT
KVFLRAGQIG ILDSRRAEVL DASARLIQRR LRTFVTHQNF ISARASAISI QAYCRGCLSR
NAYATRRNAA AAVLVQKHVR RWLSRCAFVK LVSAAIVLQS CIRADSTRLK FSHQKEHRAA
SLIQAHWRIH KFRSAFRHRQ SSIIAIQCRW RQKLAKREFR KLKQVANEAG ALRLAKTKLE
KRLEDLEWRL QLEKRLRTSG EEAKSSEISK LQKTLESFSL KLDAARLATI NECNKNAVLE
KQLDISMKEK SAVERELNGM VELKKDNALL KNSMNSLEKK NRVLEKELLN AKTNCNNTLQ
KLKEAEKRCS ELQTSVQSLE EKLSHLENEN QVLMQKTLIT SPERIGQILG EKHSSAVVPA
QNDRRSVFET PTPSKHIMPF SHSLSESRRS KLTAERNLEN YELLSRCIKE NLGFNDDKPL
AACVIYKCLL HWRAFESEST AIFNIIIEGI NEALKGGDEN GVLPYWLSNA SALLCLLQRN
LRSNSFLNAS AQRSGRAAYG VKSPFKLHGP DDGASHIEAR YPALLFKQQL TACVEKIYGL
IRDNLKKELS PLLGSCIQAP KASRGIAGKS RSPGGVPQQS PSSQWESILK FLDSLMSRLR
ENHVPSFFIR KLVTQVFSFI NLSLFNSLLL RRECCTFSNG EYVKSGISEL EKWIANAKEE
FAGTSWHELN YIRQAVGFLV IHQKKKKSLD EIRQDLCPVL TIRQIYRIST MYWDDKYGTQ
SVSSEVVSQM RVLVDKDNQK QTSNSFLLDD DMSIPFSAED IDKAIPVLDP SEIEPPKFVS
EYTCAQSLVK KPSIASTSKQ II
