AB40G_ARATH
ID AB40G_ARATH Reviewed; 1423 AA.
AC Q9M9E1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ABC transporter G family member 40 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCG.40 {ECO:0000303|PubMed:18299247};
DE Short=AtABCG40 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Pleiotropic drug resistance protein 12 {ECO:0000303|PubMed:12430018, ECO:0000303|PubMed:16506311};
GN Name=ABCG40 {ECO:0000303|PubMed:18299247};
GN Synonyms=PDR12 {ECO:0000303|PubMed:12430018, ECO:0000303|PubMed:16506311},
GN PDR9 {ECO:0000303|PubMed:18299247};
GN OrderedLocusNames=At1g15520 {ECO:0000312|Araport:AT1G15520};
GN ORFNames=T16N11.3 {ECO:0000312|EMBL:AAF71978.1};
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;
RN [1]
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 [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 IDENTIFICATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12430018; DOI=10.1007/s00425-002-0889-z;
RA van den Brule S., Smart C.C.;
RT "The plant PDR family of ABC transporters.";
RL Planta 216:95-106(2002).
RN [4]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=14526118; DOI=10.1104/pp.103.024182;
RA Campbell E.J., Schenk P.M., Kazan K., Penninckx I.A.M.A., Anderson J.P.,
RA Maclean D.J., Cammue B.P.A., Ebert P.R., Manners J.M.;
RT "Pathogen-responsive expression of a putative ATP-binding cassette
RT transporter gene conferring resistance to the diterpenoid sclareol is
RT regulated by multiple defense signaling pathways in Arabidopsis.";
RL Plant Physiol. 133:1272-1284(2003).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15923333; DOI=10.1104/pp.104.058107;
RA Lee M., Lee K., Lee J., Noh E.W., Lee Y.;
RT "AtPDR12 contributes to lead resistance in Arabidopsis.";
RL Plant Physiol. 138:827-836(2005).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16506311; DOI=10.1016/j.febslet.2005.12.043;
RA Crouzet J., Trombik T., Fraysse A.S., Boutry M.;
RT "Organization and function of the plant pleiotropic drug resistance ABC
RT transporter family.";
RL FEBS Lett. 580:1123-1130(2006).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-962, 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 [9]
RP REVIEW ON ABSCISIC ACID HOMEOSTASIS.
RX PubMed=20935463; DOI=10.4161/psb.5.9.12566;
RA Kuromori T., Shinozaki K.;
RT "ABA transport factors found in Arabidopsis ABC transporters.";
RL Plant Signal. Behav. 5:1124-1126(2010).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION BY ABSCISIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=20133880; DOI=10.1073/pnas.0909222107;
RA Kang J., Hwang J.-U., Lee M., Kim Y.-Y., Assmann S.M., Martinoia E.,
RA Lee Y.;
RT "PDR-type ABC transporter mediates cellular uptake of the phytohormone
RT abscisic acid.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2355-2360(2010).
RN [11]
RP INDUCTION BY STRESS, AND TISSUE SPECIFICITY.
RX PubMed=22525244; DOI=10.1016/j.plantsci.2012.03.001;
RA Baron K.N., Schroeder D.F., Stasolla C.;
RT "Transcriptional response of abscisic acid (ABA) metabolism and transport
RT to cold and heat stress applied at the reproductive stage of development in
RT Arabidopsis thaliana.";
RL Plant Sci. 188:48-59(2012).
RN [12]
RP REVIEW ON PHYTOHORMONE TRANSPORT.
RX PubMed=26517905; DOI=10.1042/bst20150106;
RA Borghi L., Kang J., Ko D., Lee Y., Martinoia E.;
RT "The role of ABCG-type ABC transporters in phytohormone transport.";
RL Biochem. Soc. Trans. 43:924-930(2015).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH LECRK91 AND LECRK92.
RX PubMed=26011556; DOI=10.1094/mpmi-02-15-0025-r;
RA Wang Y., Cordewener J.H.G., America A.H.P., Shan W., Bouwmeester K.,
RA Govers F.;
RT "Arabidopsis lectin receptor kinases LecRK-IX.1 and LecRK-IX.2 are
RT functional analogs in regulating phytophthora resistance and plant cell
RT death.";
RL Mol. Plant Microbe Interact. 28:1032-1048(2015).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=26334616; DOI=10.1038/ncomms9113;
RA Kang J., Yim S., Choi H., Kim A., Lee K.P., Lopez-Molina L., Martinoia E.,
RA Lee Y.;
RT "Abscisic acid transporters cooperate to control seed germination.";
RL Nat. Commun. 6:8113-8113(2015).
RN [15]
RP INDUCTION BY ABSCISIC ACID AND DROUGHT.
RX PubMed=26820136; DOI=10.1007/s11103-016-0441-3;
RA Qiao Z., Li C.-L., Zhang W.;
RT "WRKY1 regulates stomatal movement in drought-stressed Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 91:53-65(2016).
CC -!- FUNCTION: High affinity abscisic acid (ABA) transporter that mediates
CC the import of ABA, with a preference for (+)-ABA, through the plasma
CC membrane, especially in guard cells, and is involved in the
CC intercellular and intracellular ABA signaling pathways leading, for
CC example, to stomatal closure, thus conferring drought tolerance
CC (PubMed:20935463, PubMed:20133880, PubMed:26517905). Together with
CC ABCG30, import into the embryo the ABA delivered from the endosperm via
CC ABCG25 and ABCG31-mediated export to suppress radicle extension and
CC subsequent embryonic growth (PubMed:26334616). May be a general defense
CC protein (By similarity). Functions as a pump to exclude Pb(2+) ions
CC and/or Pb(2+)-containing toxic compounds from the cytoplasm.
CC Contributes to Pb(2+) ions resistance. Confers some resistance to the
CC terpene sclareol (PubMed:14526118, PubMed:15923333).
CC {ECO:0000250|UniProtKB:Q76CU2, ECO:0000269|PubMed:14526118,
CC ECO:0000269|PubMed:15923333, ECO:0000269|PubMed:20133880,
CC ECO:0000269|PubMed:26334616, ECO:0000303|PubMed:20935463,
CC ECO:0000303|PubMed:26517905}.
CC -!- FUNCTION: (Microbial infection) Involved in resistance response to the
CC pathogenic oomycetes Phytophthora infestans and Phytophthora capsici.
CC {ECO:0000269|PubMed:26011556}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=abscisate(out) + ATP + H2O = abscisate(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:63960, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:62432, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:20133880, ECO:0000269|PubMed:26334616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63961;
CC Evidence={ECO:0000269|PubMed:20133880, ECO:0000269|PubMed:26334616};
CC -!- ACTIVITY REGULATION: Inhibited by glibenclamide, verapamil and vanadate
CC (ABC transporters inhibitors). {ECO:0000269|PubMed:20133880}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for abscisic acid {ECO:0000269|PubMed:20133880};
CC -!- SUBUNIT: Interacts with LECRK91 and LECRK92.
CC {ECO:0000269|PubMed:26011556}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15923333,
CC ECO:0000269|PubMed:20133880}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly observed in inflorescence meristems relative
CC to cauline leaves and developing siliques (PubMed:22525244). Ubiquitous
CC with higher levels in leaves, stems and flowers (PubMed:12430018,
CC PubMed:14526118, PubMed:15923333, PubMed:20133880). Also present in
CC primary and lateral roots (PubMed:20133880). In seeds, mainly expressed
CC in the embryo and, to a lesser extent, in the endosperm
CC (PubMed:26334616). {ECO:0000269|PubMed:12430018,
CC ECO:0000269|PubMed:14526118, ECO:0000269|PubMed:15923333,
CC ECO:0000269|PubMed:20133880, ECO:0000269|PubMed:22525244,
CC ECO:0000269|PubMed:26334616}.
CC -!- DEVELOPMENTAL STAGE: In leaves, mostly observed in guard cells.
CC {ECO:0000269|PubMed:20133880}.
CC -!- INDUCTION: Circadian-regulation. Expression increase during the dark
CC phase and decrease during the light phase. Induced by cycloheximide
CC (CHX), sclareol, and heavy metals such as Pb(2+) ions. ETR1-, EIN2-,
CC JAR1-, NPR1- and EDS5-dependent induction by incompatible fungal
CC pathogens (A.brassicicola), by compatible fungal pathogens
CC (S.sclerotiorum and F.oxysporum), and by compatible bacterial pathogens
CC (P.syringae pv tomato). Also induced by phytohormones such as salicylic
CC acid (SA), methyl jasmonate (MeJA) and ethylene. Induced by abscisic
CC acid (ABA) treatment and drought via a WRKY1-mediated regulation
CC (PubMed:20133880, PubMed:26820136). In cauline leaves, activated by
CC cold stress, but repressed by heat stress (PubMed:22525244). Within
CC inflorescence meristems, down-regulated by both cold and heat stress
CC treatments (PubMed:22525244). In developing siliques, activated by cold
CC stress, but unaffected by heat stress (PubMed:22525244).
CC {ECO:0000269|PubMed:12430018, ECO:0000269|PubMed:14526118,
CC ECO:0000269|PubMed:15923333, ECO:0000269|PubMed:20133880,
CC ECO:0000269|PubMed:22525244, ECO:0000269|PubMed:26820136}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to the oomycetes
CC Phytophthora brassicae and Phytophthora capsici (PubMed:26011556).
CC Decreased abscisic acid (ABA) uptake through the plasma membrane and
CC strongly delayed up-regulation of ABA responsive genes (e.g. NCED3,
CC ABR1 and RD29B), and associated with a slow stomatal closure in
CC response to ABA and osmotic stress resulting in reduced drought
CC tolerance (PubMed:20133880). Impairment in ABA regulation of seed
CC germination and root development (PubMed:20133880). Early seeds
CC germination on imbibition without stratification, and reduced abscisic
CC acid (ABA)-mediated inhibition of seeds germination (PubMed:26334616).
CC {ECO:0000269|PubMed:20133880, ECO:0000269|PubMed:26011556,
CC ECO:0000269|PubMed:26334616}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; AC013453; AAF71978.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29332.1; -; Genomic_DNA.
DR EMBL; BK001011; DAA00880.1; -; Genomic_DNA.
DR PIR; A86289; A86289.
DR RefSeq; NP_173005.1; NM_101421.3.
DR AlphaFoldDB; Q9M9E1; -.
DR SMR; Q9M9E1; -.
DR STRING; 3702.AT1G15520.1; -.
DR TCDB; 3.A.1.205.10; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q9M9E1; -.
DR PaxDb; Q9M9E1; -.
DR PRIDE; Q9M9E1; -.
DR ProteomicsDB; 244393; -.
DR EnsemblPlants; AT1G15520.1; AT1G15520.1; AT1G15520.
DR GeneID; 838122; -.
DR Gramene; AT1G15520.1; AT1G15520.1; AT1G15520.
DR KEGG; ath:AT1G15520; -.
DR Araport; AT1G15520; -.
DR TAIR; locus:2196593; AT1G15520.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_6_1; -.
DR InParanoid; Q9M9E1; -.
DR OMA; TIAKLFW; -.
DR OrthoDB; 324553at2759; -.
DR PhylomeDB; Q9M9E1; -.
DR PRO; PR:Q9M9E1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9E1; baseline and differential.
DR Genevisible; Q9M9E1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0080168; P:abscisic acid transport; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0042631; P:cellular response to water deprivation; IMP:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0098739; P:import across plasma membrane; IMP:UniProtKB.
DR GO; GO:0098657; P:import into cell; IMP:UniProtKB.
DR GO; GO:0010496; P:intercellular transport; IMP:UniProtKB.
DR GO; GO:0015692; P:lead ion transport; IMP:TAIR.
DR GO; GO:0048581; P:negative regulation of post-embryonic development; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; TAS:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; TAS:TAIR.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; TAS:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0090332; P:stomatal closure; IMP:UniProtKB.
DR GO; GO:0046865; P:terpenoid transport; IDA:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IMP:UniProtKB.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013581; PDR_assoc.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF08370; PDR_assoc; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; ATP-binding; Cell membrane; Glycoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Plant defense;
KW Reference proteome; Repeat; Stress response; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1423
FT /note="ABC transporter G family member 40"
FT /id="PRO_0000234639"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1174..1194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1207..1227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1257..1277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1284..1304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1314..1334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1341..1361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1395..1415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 154..427
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 505..718
FT /note="ABC transmembrane type-2 1"
FT /evidence="ECO:0000255"
FT DOMAIN 825..1077
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1150..1364
FT /note="ABC transmembrane type-2 2"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 870..877
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 962
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1423 AA; 161017 MW; B40CFF2797486D23 CRC64;
MEGTSFHQAS NSMRRNSSVW KKDSGREIFS RSSREEDDEE ALRWAALEKL PTFDRLRKGI
LTASHAGGPI NEIDIQKLGF QDTKKLLERL IKVGDDEHEK LLWKLKKRID RVGIDLPTIE
VRFDHLKVEA EVHVGGRALP TFVNFISNFA DKFLNTLHLV PNRKKKFTIL NDVSGIVKPG
RMALLLGPPS SGKTTLLLAL AGKLDQELKQ TGRVTYNGHG MNEFVPQRTA AYIGQNDVHI
GEMTVRETFA YAARFQGVGS RYDMLTELAR REKEANIKPD PDIDIFMKAM STAGEKTNVM
TDYILKILGL EVCADTMVGD DMLRGISGGQ KKRVTTGEML VGPSRALFMD EISTGLDSST
TYQIVNSLRN YVHIFNGTAL ISLLQPAPET FNLFDDIILI AEGEIIYEGP RDHVVEFFET
MGFKCPPRKG VADFLQEVTS KKDQMQYWAR RDEPYRFIRV REFAEAFQSF HVGRRIGDEL
ALPFDKTKSH PAALTTKKYG VGIKELVKTS FSREYLLMKR NSFVYYFKFG QLLVMAFLTM
TLFFRTEMQK KTEVDGSLYT GALFFILMML MFNGMSELSM TIAKLPVFYK QRDLLFYPAW
VYSLPPWLLK IPISFMEAAL TTFITYYVIG FDPNVGRLFK QYILLVLMNQ MASALFKMVA
ALGRNMIVAN TFGAFAMLVF FALGGVVLSR DDIKKWWIWG YWISPIMYGQ NAILANEFFG
HSWSRAVENS SETLGVTFLK SRGFLPHAYW YWIGTGALLG FVVLFNFGFT LALTFLNSLG
KPQAVIAEEP ASDETELQSA RSEGVVEAGA NKKRGMVLPF EPHSITFDNV VYSVDMPQEM
IEQGTQEDRL VLLKGVNGAF RPGVLTALMG VSGAGKTTLM DVLAGRKTGG YIDGNITISG
YPKNQQTFAR ISGYCEQTDI HSPHVTVYES LVYSAWLRLP KEVDKNKRKI FIEEVMELVE
LTPLRQALVG LPGESGLSTE QRKRLTIAVE LVANPSIIFM DEPTSGLDAR AAAIVMRTVR
NTVDTGRTVV CTIHQPSIDI FEAFDELFLL KRGGEEIYVG PLGHESTHLI NYFESIQGIN
KITEGYNPAT WMLEVSTTSQ EAALGVDFAQ VYKNSELYKR NKELIKELSQ PAPGSKDLYF
PTQYSQSFLT QCMASLWKQH WSYWRNPPYT AVRFLFTIGI ALMFGTMFWD LGGKTKTRQD
LSNAMGSMYT AVLFLGLQNA ASVQPVVNVE RTVFYREQAA GMYSAMPYAF AQVFIEIPYV
LVQAIVYGLI VYAMIGFEWT AVKFFWYLFF MYGSFLTFTF YGMMAVAMTP NHHIASVVSS
AFYGIWNLFS GFLIPRPSMP VWWEWYYWLC PVAWTLYGLI ASQFGDITEP MADSNMSVKQ
FIREFYGYRE GFLGVVAAMN VIFPLLFAVI FAIGIKSFNF QKR
