MYO17_ARATH
ID MYO17_ARATH Reviewed; 1531 AA.
AC F4K5J1; E9N630; F4K5J2; K9KY88; Q0WQJ2;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Myosin-17;
DE AltName: Full=Myosin XI K;
DE Short=AtXIK;
GN Name=XI-K; Synonyms=XIK; OrderedLocusNames=At5g20490; ORFNames=F7C8.80;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Park E., Nebenfuehr A.;
RT "Transport of secretory vesicle by myosin XIK is necessary for maintenance
RT of optimal tip growth in root hairs of Arabidopsis thaliana.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 1270-1531.
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17458634; DOI=10.1007/s00709-006-0233-8;
RA Ojangu E.L., Jaerve K., Paves H., Truve E.;
RT "Arabidopsis thaliana myosin XIK is involved in root hair as well as
RT trichome morphogenesis on stems and leaves.";
RL Protoplasma 230:193-202(2007).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18503043; DOI=10.1093/jxb/ern114;
RA Sparkes I.A., Teanby N.A., Hawes C.;
RT "Truncated myosin XI tail fusions inhibit peroxisome, Golgi, and
RT mitochondrial movement in tobacco leaf epidermal cells: a genetic tool for
RT the next generation.";
RL J. Exp. Bot. 59:2499-2512(2008).
RN [12]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18178669; DOI=10.1104/pp.107.113654;
RA Peremyslov V.V., Prokhnevsky A.I., Avisar D., Dolja V.V.;
RT "Two class XI myosins function in organelle trafficking and root hair
RT development in Arabidopsis.";
RL Plant Physiol. 146:1109-1116(2008).
RN [13]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19060218; DOI=10.1073/pnas.0810730105;
RA Prokhnevsky A.I., Peremyslov V.V., Dolja V.V.;
RT "Overlapping functions of the four class XI myosins in Arabidopsis growth,
RT root hair elongation, and organelle motility.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:19744-19749(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1517, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1517, AND IDENTIFICATION BY
RP 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 [17]
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 [18]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20351265; DOI=10.1073/pnas.0911482107;
RA Ueda H., Yokota E., Kutsuna N., Shimada T., Tamura K., Shimmen T.,
RA Hasezawa S., Dolja V.V., Hara-Nishimura I.;
RT "Myosin-dependent endoplasmic reticulum motility and F-actin organization
RT in plant cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6894-6899(2010).
RN [19]
RP FUNCTION.
RX PubMed=22672737; DOI=10.1186/1471-2229-12-81;
RA Ojangu E.L., Tanner K., Pata P., Jaerve K., Holweg C.L., Truve E.,
RA Paves H.;
RT "Myosins XI-K, XI-1, and XI-2 are required for development of pavement
RT cells, trichomes, and stigmatic papillae in Arabidopsis.";
RL BMC Plant Biol. 12:81-81(2012).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=22969781; DOI=10.3389/fpls.2012.00184;
RA Peremyslov V.V., Klocko A.L., Fowler J.E., Dolja V.V.;
RT "Arabidopsis Myosin XI-K localizes to the motile endomembrane vesicles
RT associated with F-actin.";
RL Front. Plant Sci. 3:184-184(2012).
RN [21]
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 [22]
RP INTERACTION WITH MYOB1; MYOB2 AND MYOB3.
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 [23]
RP INTERACTION WITH PHOX1 AND PHOX2.
RX PubMed=28096376; DOI=10.1073/pnas.1620577114;
RA Kurth E.G., Peremyslov V.V., Turner H.L., Makarova K.S., Iranzo J.,
RA Mekhedov S.L., Koonin E.V., Dolja V.V.;
RT "Myosin-driven transport network in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1385-E1394(2017).
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 the tip growth of root hair cells
CC and in the elongation of trichome stalk and branches. Plays a major
CC role in trafficking of Golgi stacks, mitochondria and peroxisomes
CC during root hair development. Acts as the primary contributor to ER
CC streaming with a major role in the movement of Golgi bodies. Required
CC for development of pavement cells, trichomes, and stigmatic papillae.
CC {ECO:0000269|PubMed:17458634, ECO:0000269|PubMed:18178669,
CC ECO:0000269|PubMed:18503043, ECO:0000269|PubMed:19060218,
CC ECO:0000269|PubMed:19369591, ECO:0000269|PubMed:20351265,
CC ECO:0000269|PubMed:20581304, ECO:0000269|PubMed:21914656,
CC ECO:0000269|PubMed:22672737}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with MYOB1, MYOB2 and
CC MYOB3 (PubMed:23995081). Interacts with PHOX1 and PHOX2
CC (PubMed:28096376). {ECO:0000250|UniProtKB:Q39160,
CC ECO:0000269|PubMed:23995081, ECO:0000269|PubMed:28096376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17288617,
CC ECO:0000269|PubMed:17500056, ECO:0000269|PubMed:18503043,
CC ECO:0000269|PubMed:20351265, ECO:0000269|PubMed:22969781}.
CC Note=Colocalizes with peroxisome, cytoplasmic vesicles, endomembrane
CC vesicles, endoplasmic reticulum and/or organelles.
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=F4K5J1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:17458634}.
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 growth of root hair cells, twisted shape
CC of stem trichomes, and irregular size, branch positioning, and branch
CC expansion of leaf trichomes. Affected organization of the ER network
CC and orientation of the actin filament bundles.
CC {ECO:0000269|PubMed:17458634, ECO:0000269|PubMed:18178669,
CC ECO:0000269|PubMed:19060218, ECO:0000269|PubMed:20351265}.
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=AER51968.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF296833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92852.2; -; Genomic_DNA.
DR EMBL; HQ427882; ADV74830.1; -; mRNA.
DR EMBL; JN229265; AER51968.1; ALT_FRAME; mRNA.
DR EMBL; AK228703; BAF00607.1; -; mRNA.
DR RefSeq; NP_001318612.1; NM_001343671.1. [F4K5J1-1]
DR PDB; 7KFL; X-ray; 2.35 A; A/B=1105-1499.
DR PDBsum; 7KFL; -.
DR AlphaFoldDB; F4K5J1; -.
DR SMR; F4K5J1; -.
DR BioGRID; 17447; 7.
DR STRING; 3702.AT5G20490.1; -.
DR iPTMnet; F4K5J1; -.
DR PaxDb; F4K5J1; -.
DR PRIDE; F4K5J1; -.
DR ProteomicsDB; 251308; -. [F4K5J1-1]
DR EnsemblPlants; AT5G20490.2; AT5G20490.2; AT5G20490. [F4K5J1-1]
DR GeneID; 832171; -.
DR Gramene; AT5G20490.2; AT5G20490.2; AT5G20490. [F4K5J1-1]
DR KEGG; ath:AT5G20490; -.
DR Araport; AT5G20490; -.
DR TAIR; locus:2149932; AT5G20490.
DR eggNOG; KOG0160; Eukaryota.
DR InParanoid; F4K5J1; -.
DR OMA; VAPVNII; -.
DR OrthoDB; 311886at2759; -.
DR PRO; PR:F4K5J1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K5J1; baseline and differential.
DR Genevisible; F4K5J1; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0035619; C:root hair tip; IDA:TAIR.
DR GO; GO:0030133; C:transport vesicle; 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:0051301; P:cell division; IGI:TAIR.
DR GO; GO:0010154; P:fruit development; IGI:TAIR.
DR GO; GO:0051645; P:Golgi localization; IMP:TAIR.
DR GO; GO:0048467; P:gynoecium development; IGI:TAIR.
DR GO; GO:0090436; P:leaf pavement cell development; IGI:TAIR.
DR GO; GO:0051646; P:mitochondrion localization; IMP:TAIR.
DR GO; GO:0060151; P:peroxisome localization; IMP:TAIR.
DR GO; GO:0009791; P:post-embryonic development; IGI:TAIR.
DR GO; GO:0048768; P:root hair cell tip growth; IMP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR GO; GO:0010090; P:trichome morphogenesis; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IGI:TAIR.
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; 5.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Coiled coil; Cytoplasm; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1531
FT /note="Myosin-17"
FT /id="PRO_0000422872"
FT DOMAIN 8..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 62..732
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 758..787
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 783..812
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 806..835
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 831..860
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 854..883
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1159..1470
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 495..529
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 531..554
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 589..613
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 613..635
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1071..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 884..1056
FT /evidence="ECO:0000255"
FT COMPBIAS 1071..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 209..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT CONFLICT 409
FT /note="F -> V (in Ref. 2; AER51968)"
FT /evidence="ECO:0000305"
FT HELIX 1108..1124
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1135..1146
FT /evidence="ECO:0007829|PDB:7KFL"
FT TURN 1147..1150
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1157..1169
FT /evidence="ECO:0007829|PDB:7KFL"
FT STRAND 1170..1173
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1175..1193
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1236..1238
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1254..1290
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1292..1295
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1309..1335
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1340..1364
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1366..1368
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1371..1391
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1393..1396
FT /evidence="ECO:0007829|PDB:7KFL"
FT TURN 1397..1399
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1400..1403
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1404..1413
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1423..1428
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1436..1445
FT /evidence="ECO:0007829|PDB:7KFL"
FT STRAND 1449..1451
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1458..1473
FT /evidence="ECO:0007829|PDB:7KFL"
FT HELIX 1492..1497
FT /evidence="ECO:0007829|PDB:7KFL"
SQ SEQUENCE 1531 AA; 173377 MW; D6C90682FB78AC5E CRC64;
MVGPVNIIVG SHVWIEDPGA AWIDGEVVKI NGEEVHAHTT NGKTVVANIA NVFPKDTEAP
PGGVDDMTKL SYLHEPGVLN NLAMRYELNE IYTYTGNILI AVNPFQRLPH LYDTHMMEQY
KGAGFGELSP HVFAIAEVAY RAMINEGKSN SILVSGESGA GKTETTKMLM RYLAYLGGRS
GVEGRTVEQQ VLESNPVLEA FGNAKTLRNN NSSRFGKFVE LQFDNCGRIS GAAVRTYLLE
RSRVCQISDP ERNYHCFYLL CAAPPEEREK FKLGDPKLFH YLNQSKCYKL DGVDDTEEYL
ATRRAMDIVG ISEEEQDAIF RVVAAILHLG NVNFAKGKEI DSSVLKDEKS RYHLDVCAEL
LRCDAKKMED ALIKRVMVTP EEVITRTLDP DSATGSRDAL AKTIYSRLFD WLVDKINNSI
GQDPNSKTII GVLDIYGFES FKINSFEQFC INFTNEKLQQ HFNQHVFKME QEDYTKEEIN
WSYIEFVDNK DVLELIEKKP GGVIALLDEA CMFPKSTHET FAQKLYQTFK NYKRFTKPKL
SRTSFAISHY AGEVTYQADL FLDKNKDYVV AEHQDLLIAS SDTFVAGLFP RLPEETSSKT
KFSSIGSRFK LQLQSLMETL SSTEPHYIRC VKPNNVLKPA IFENVNVIQQ LRCGGVLEAI
RISCAGYPTK RTFYEFLNRF GVLAPEVLEG NYDDKVACKM LLDKIGLKGY ELGKTKVFLR
AGQMAELDAR RAEVLGNAAR RIQRQSRTFI ACKEFRALRG AAIVLQSNCR GKLACNLYEE
MRRQAAAVKI QKIFRRHIAR ESYLRIRHST ITVQTALRGM VARNEFRFRK QMKAATIIQA
RLRSHLTHSY YKQLQKAALS TQCGWRSRVA RKELRTLKMA ARDTGALREA KDKLEKRVEE
LTWRLQLEKR QRTELEEAKT QEYAKQQEAL ETMRLQVEEA NAAVIREREA ARKAIEEAPP
VIKETPVLVE DTEKINSLTS EVEALKASLQ AERQAAENLR KAFSEAEARN SELATELENA
TRKADQLHES VQRLEEKLSN SESEIQVLRQ QALAISPTSR TMATRSKTML LPRTPENGNY
LNGGTKTTPD MTLAVREPES EEKPQKHLNE KQQENQDLLV KCISQNLGYN GDKPVAACVI
YKCLLHWRSF EVERTSVFDR IIQTIATAIE VPDNNEVLAY WLSNSATLLL LLQRTLKATG
AASLTPQRRR TTSASLFGRM SQGLRGSPQS AGLSFLNRQG LTKLDDLRQV EAKYPALLFK
QQLTAFLEKI YGMIRDNLKK EISPLLGLCI QAPRTSRASL VKGRAQANAV AQQALIAHWQ
SIRKSLNSYL NLMKANNAPP FLVRKVFTQI FSFINVQLFN SLLLRRECCS FSNGEYVKAG
LAELEQWCIE ATDEYAGSAW DELRHIRQAV GFLVIHQKPK KTLDEITREL CPVLSIQQLY
RISTMYWDDK YGTHSVSSDV IANMRVMMTE DSNNAVSSSF LLDDDSSIPF TVEDISKSMQ
QVDVNDIEPP QLIRENSGFG FLLTRKEGST S
