TARA_MOUSE
ID TARA_MOUSE Reviewed; 2014 AA.
AC Q99KW3; Q2PZW9; Q2Q402; Q2Q403; Q2Q404; Q6ZPK4; Q8C6T3; Q8CG90;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=TRIO and F-actin-binding protein;
DE AltName: Full=Protein Tara;
DE AltName: Full=Trio-associated repeat on actin;
GN Name=Triobp; Synonyms=Kiaa1662, Tara;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Cochlea;
RX PubMed=16385458; DOI=10.1086/499495;
RA Shahin H., Walsh T., Sobe T., Abu Sa'ed J., Abu Rayan A., Lynch E.D.,
RA Lee M.K., Avraham K.B., King M.-C., Kanaan M.;
RT "Mutations in a novel isoform of TRIOBP that encodes a filamentous-actin
RT binding protein are responsible for DFNB28 recessive nonsyndromic hearing
RT loss.";
RL Am. J. Hum. Genet. 78:144-152(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
RX PubMed=16385457; DOI=10.1086/499164;
RA Riazuddin S., Khan S.N., Ahmed Z.M., Ghosh M., Caution K., Nazli S.,
RA Kabra M., Zafar A.U., Chen K., Naz S., Antonellis A., Pavan W.J.,
RA Green E.D., Wilcox E.R., Friedman P.L., Morell R.J., Riazuddin S.,
RA Friedman T.B.;
RT "Mutations in TRIOBP, which encodes a putative cytoskeletal-organizing
RT protein, are associated with nonsyndromic recessive deafness.";
RL Am. J. Hum. Genet. 78:137-143(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1579, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP INTERACTION WITH PJVK.
RX PubMed=28209736; DOI=10.1523/jneurosci.2711-16.2017;
RA Kazmierczak M., Kazmierczak P., Peng A.W., Harris S.L., Shah P., Puel J.L.,
RA Lenoir M., Franco S.J., Schwander M.;
RT "Pejvakin, a candidate stereociliary rootlet protein, regulates hair cell
RT function in a cell-autonomous manner.";
RL J. Neurosci. 37:3447-3464(2017).
CC -!- FUNCTION: May regulate actin cytoskeletal organization, cell spreading
CC and cell contraction by directly binding and stabilizing filamentous F-
CC actin. The localized formation of TARA and TRIO complexes coordinates
CC the amount of F-actin present in stress fibers. May also serve as a
CC linker protein to recruit proteins required for F-actin formation and
CC turnover. {ECO:0000250|UniProtKB:Q9H2D6}.
CC -!- SUBUNIT: Binds to TRIO and F-actin (By similarity). May also interact
CC with myosin II (By similarity). Interacts with HECTD3 (By similarity).
CC Interacts with PJVK (PubMed:28209736). {ECO:0000250|UniProtKB:Q9H2D6,
CC ECO:0000269|PubMed:28209736}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H2D6}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9H2D6}. Note=Localized
CC to F-actin in a periodic pattern. {ECO:0000250|UniProtKB:Q9H2D6}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000250|UniProtKB:Q9H2D6}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9H2D6}. Midbody
CC {ECO:0000250|UniProtKB:Q9H2D6}. Note=Centrosomal localization occurs
CC upon phosphorylation by PLK1 at Thr-445 and lasts from prophase to
CC anaphase. At telophase, relocalizes to midbody (By similarity).
CC {ECO:0000250|UniProtKB:Q9H2D6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=3;
CC IsoId=Q99KW3-3; Sequence=Displayed;
CC Name=4; Synonyms=TRIOBP isoform 5;
CC IsoId=Q99KW3-4; Sequence=VSP_017719;
CC Name=5; Synonyms=TRIOBP isoform 4;
CC IsoId=Q99KW3-5; Sequence=VSP_017721;
CC Name=1;
CC IsoId=Q99KW3-1; Sequence=VSP_017718, VSP_017720;
CC Name=2;
CC IsoId=Q99KW3-2; Sequence=VSP_016762;
CC -!- DOMAIN: Contains at least 2 actin-binding sites per coiled-coil dimer.
CC {ECO:0000250|UniProtKB:Q9H2D6}.
CC -!- PTM: Ubiquitinated by HECTD3, leading to its degradation by the
CC proteasome. {ECO:0000250|UniProtKB:Q9H2D6}.
CC -!- PTM: [Isoform 1]: Phosphorylation at Thr-445 by PLK1 ensures mitotic
CC progression and is essential for accurate chromosome segregation.
CC {ECO:0000250|UniProtKB:Q9H2D6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98227.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129417; BAC98227.2; ALT_INIT; Transcribed_RNA.
DR EMBL; DQ278602; ABB77203.1; -; mRNA.
DR EMBL; DQ228000; ABB59556.1; -; mRNA.
DR EMBL; DQ228001; ABB59557.2; -; mRNA.
DR EMBL; DQ228002; ABB59558.2; -; mRNA.
DR EMBL; AK053194; BAC35308.1; -; mRNA.
DR EMBL; AK170390; BAE41764.1; -; mRNA.
DR EMBL; BC003984; AAH03984.1; -; mRNA.
DR EMBL; BC042760; AAH42760.1; -; mRNA.
DR EMBL; BC053329; AAH53329.1; -; mRNA.
DR CCDS; CCDS37136.1; -. [Q99KW3-3]
DR CCDS; CCDS37137.1; -. [Q99KW3-4]
DR CCDS; CCDS88802.1; -. [Q99KW3-5]
DR RefSeq; NP_001034244.1; NM_001039155.1. [Q99KW3-5]
DR RefSeq; NP_001034245.1; NM_001039156.1. [Q99KW3-3]
DR RefSeq; NP_613045.3; NM_138579.4. [Q99KW3-4]
DR RefSeq; XP_017171854.1; XM_017316365.1. [Q99KW3-3]
DR AlphaFoldDB; Q99KW3; -.
DR SMR; Q99KW3; -.
DR BioGRID; 225432; 7.
DR IntAct; Q99KW3; 2.
DR STRING; 10090.ENSMUSP00000105312; -.
DR iPTMnet; Q99KW3; -.
DR PhosphoSitePlus; Q99KW3; -.
DR EPD; Q99KW3; -.
DR jPOST; Q99KW3; -.
DR MaxQB; Q99KW3; -.
DR PaxDb; Q99KW3; -.
DR PeptideAtlas; Q99KW3; -.
DR PRIDE; Q99KW3; -.
DR ProteomicsDB; 263203; -. [Q99KW3-3]
DR ProteomicsDB; 263204; -. [Q99KW3-4]
DR ProteomicsDB; 263205; -. [Q99KW3-5]
DR ProteomicsDB; 263206; -. [Q99KW3-1]
DR ProteomicsDB; 263207; -. [Q99KW3-2]
DR Antibodypedia; 288; 117 antibodies from 25 providers.
DR DNASU; 110253; -.
DR Ensembl; ENSMUST00000109689; ENSMUSP00000105311; ENSMUSG00000033088. [Q99KW3-4]
DR Ensembl; ENSMUST00000109690; ENSMUSP00000105312; ENSMUSG00000033088. [Q99KW3-3]
DR Ensembl; ENSMUST00000140228; ENSMUSP00000155397; ENSMUSG00000033088. [Q99KW3-5]
DR GeneID; 110253; -.
DR KEGG; mmu:110253; -.
DR UCSC; uc007wrx.1; mouse. [Q99KW3-5]
DR UCSC; uc007wry.1; mouse. [Q99KW3-3]
DR UCSC; uc007wrz.1; mouse. [Q99KW3-4]
DR UCSC; uc029sth.1; mouse. [Q99KW3-1]
DR CTD; 11078; -.
DR MGI; MGI:1349410; Triobp.
DR VEuPathDB; HostDB:ENSMUSG00000033088; -.
DR eggNOG; KOG4807; Eukaryota.
DR GeneTree; ENSGT00940000157340; -.
DR HOGENOM; CLU_231134_0_0_1; -.
DR InParanoid; Q99KW3; -.
DR OMA; QRDNPGT; -.
DR OrthoDB; 428862at2759; -.
DR PhylomeDB; Q99KW3; -.
DR TreeFam; TF343361; -.
DR BioGRID-ORCS; 110253; 3 hits in 69 CRISPR screens.
DR ChiTaRS; Triobp; mouse.
DR PRO; PR:Q99KW3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q99KW3; protein.
DR Bgee; ENSMUSG00000033088; Expressed in animal zygote and 188 other tissues.
DR ExpressionAtlas; Q99KW3; baseline and differential.
DR Genevisible; Q99KW3; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0120044; C:stereocilium base; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR CDD; cd13275; PH_M-RIP; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR039597; M-RIP_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Methylation; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..2014
FT /note="TRIO and F-actin-binding protein"
FT /id="PRO_0000072434"
FT DOMAIN 1440..1536
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1711..2010
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1051
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1080
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1579
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2D6"
FT MOD_RES 1604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2D6"
FT MOD_RES 1879
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q9H2D6"
FT VAR_SEQ 1..1434
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017718"
FT VAR_SEQ 981..2014
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16385457"
FT /id="VSP_017721"
FT VAR_SEQ 1391..1436
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16385457,
FT ECO:0000303|PubMed:16385458"
FT /id="VSP_017719"
FT VAR_SEQ 1435..1436
FT /note="QR -> MT (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017720"
FT VAR_SEQ 1508
FT /note="H -> HVRLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_016762"
FT CONFLICT 65
FT /note="N -> D (in Ref. 3; ABB77203)"
FT /evidence="ECO:0000305"
FT CONFLICT 1036
FT /note="P -> S (in Ref. 3; ABB77203)"
FT /evidence="ECO:0000305"
FT CONFLICT 1464
FT /note="T -> A (in Ref. 3; ABB77203)"
FT /evidence="ECO:0000305"
FT CONFLICT 1674
FT /note="E -> V (in Ref. 6; AAH42760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1708
FT /note="R -> RR (in Ref. 3; ABB77203)"
FT /evidence="ECO:0000305"
FT CONFLICT 1771
FT /note="S -> P (in Ref. 3; ABB77203)"
FT /evidence="ECO:0000305"
FT CONFLICT 1889
FT /note="E -> K (in Ref. 3; ABB77203)"
FT /evidence="ECO:0000305"
FT CONFLICT 2014
FT /note="E -> V (in Ref. 3; ABB77203)"
FT /evidence="ECO:0000305"
FT MOD_RES Q99KW3-1:445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2D6"
SQ SEQUENCE 2014 AA; 223368 MW; ABDF0F8C3AC4C476 CRC64;
MSMEQDTRAL LPTQGTAWAT ASAPVARLQG PQGDSHQACS QEPHSPSSAE APYCDLPRCP
PALQNPLRTT TCVGQSVHSL GLGLGQEPQR VWSPTTALPA EGPAAAPKNR HQDSEGIPYL
EGLARSSCTD DNDNKDEDED PNSNTSSSQD SNTPHDTSNS SSVDWDTTER PGVVPSRNRL
TEMIPRRPQE GLRADSARKA TRSPARGDTA GQRKENSGSG GQSAGQHWAK LRSESGYFSL
ERQRSGQTQA SSGTPPSGPR GTTQASSAQR DVFQAAPAQE APQTSSLPRN TQRDTQRSTP
RTSSPSRVSQ RDTPRVMSTQ RKNTPLSSPL RATPETLKIS APEDGTHVTP SPCVQDSSLN
RTSQRDSSRT PCIQWDNPRA SSPNRTTQRD NPRTPCTQRD NPRASSPNRT TQRDNPRTPC
TQRDNPRASS PNRTTQRDNP RTPCAQRDNP RAASPNRSTQ RDSPRTPCAQ RDNPRASSPN
RTAQRDNPRT PCAQRDNPRT SCTSQNTPRT PSTQADKTTA SCSKWEHLRS ACTQRDNPRT
FSQGCTQKDN PGPPSPRRAT QGSNSRNPSP HRTNKDIPWA SFPLRPTQSD SPRTSSPSRT
KQNQVPWASI SLRPTQGDKP QTSAPTRLAH NDPPQQYSPS LATTSSSSHN PGHSSASRTS
SPLHAAPRGA PQTSLESSQP PCTVCIGHRD APRASSPPRY FQYDPFPFFP DPRSSESESP
HHEPPYMPPA VCIGHRDAPR ATSPPRHTQF DPFPFLPDTS DADNESPQHD PPQFPPPVCI
GYRDAPRASS PPRQFPEPSF FQDLPRASTE SLVPSTDSMH EPPHIPTPVC IGHRDAPSFS
SPPRQAPEPS LFFQDPPGTS MESLAPSIDS LHGCPLLPPQ VCIGHRDAPR ASSPPRHPPS
DIGLLAPSPP PGSSGSRGSA PPGETRHNLE REEYTMLADL PPPRRLAQRG PEPQAQGSNE
GRTRSPGRAE VERLFGQERR KSEAPGAFQT RDEGRSQRPS QAQSQLRRQS SPAPSRQVTK
PSAKQAEPTR QSRTGPPHPK SPDKRPEGDR QLQRTSPPAR TPARPPERKA QIERHLESGH
TGPRQSLGGW QSQERLSGPQ SPNRHPEKSW GSQKEGPSLG GWPELEGPSL EGIWRGPPQE
HREQWGHSEA WEEPPSNGIQ GAPPRGQGRL QELSRPHQPT PSSENSWAGP AECSCALQPE
ASTAVGWRAE GTSPHQRSAE RPPDLDWRDL LGLLRAPEDG AWTRLPRLDW EGLLELLQAR
LPQKDPARHW HDPAKASGPE QGSSGTEDTL KTEPQTQPEG RAKATLANGH RPGQQSESPA
QLPSPACTST QWPTTKVTSG PETSPLAALE QIDHLESHSP PDLEFQPEEP EASEPSRGED
SRAVQKQADS ADKRPAEGKA GSPLKGRLVT SWRMPGDRPA LFNPYLLSLG VLRWQRPDLL
NFKKGWMSIL DEPGEWKKHW FVLTDSSLKY YRDSTAEEAD ELDGEIDLRS CTDVTEYAVQ
RNYGFQIHTK DAVYTLSAMT SGIRRNWIEA LRKTVRPTSA PDVTKLSDCN KENTLHGYGT
QKSSLKIGEQ RTGSEVIGRG GPRKADGPRP SLDYVELSPL APSSPQRMRT LSRSTPERPT
KQEDLERDLA QRSEERRKWF ESTDGRTPET PSGDGSRRGL GAPLTDDQQS RLSEEIEKKW
QELEKLPLRE NKRVPLTALL NQAHNDRRGP TSDSHEALEK EVQSLRAQLE AWRLRGEAPQ
NAPRLQEDSH IPPGYISQEA CERSLAEMES SHQQVMEQLQ RHHERELQRL QQEKEWLLAE
ETAATASAIE AMKKAYQEEL SRELSKTRSL QQGPESLRKQ HQLDMEALKQ ELQVLSERYS
QKCLEIGALT RQAEEREHTL RRCQQEGQEL LRHNQELHSH LSEEIDRLRS FIASQGTGNS
CGRSNERSSC ELEVLLRVKE NELQYLKKEV QCLRDELQVI QKDKRFTGKY QDVYVELNHI
KTRSEREIEQ LKEHLRLAMA ALQEKEAVRN SLAE
