ADDB_MOUSE
ID ADDB_MOUSE Reviewed; 725 AA.
AC Q9QYB8; Q3U0E1; Q80VH9; Q8C1C4; Q9CXE3; Q9JLE4; Q9JLE5; Q9QYB7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Beta-adducin;
DE AltName: Full=Add97;
DE AltName: Full=Erythrocyte adducin subunit beta;
GN Name=Add2;
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 [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=10602987; DOI=10.1007/s003350010004;
RA Suriyapperuma S.P., Lozovatsky L., Ciciotte S.L., Peters L.L.,
RA Gilligan D.M.;
RT "The mouse adducin gene family: alternative splicing and chromosomal
RT localization.";
RL Mamm. Genome 11:16-23(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J;
RX PubMed=10845937;
RA Muro A.F., Marro M.L., Gajovic S., Porro F., Luzzatto L., Baralle F.E.;
RT "Mild spherocytic hereditary elliptocytosis and altered levels of
RT alpha- and gamma-adducins in beta-adducin-deficient mice.";
RL Blood 95:3978-3985(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic liver, and Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-561 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532 AND SER-535, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-344; SER-530;
RP SER-532; THR-533; SER-535; SER-594; SER-598; SER-602; SER-606; SER-614;
RP SER-618; SER-620; SER-688; SER-692; SER-696; SER-698 AND SER-700, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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).
CC -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes the
CC assembly of the spectrin-actin network. Binds to the erythrocyte
CC membrane receptor SLC2A1/GLUT1 and may therefore provide a link between
CC the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin.
CC Calmodulin binds preferentially to the beta subunit (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Found in a complex with ADD2, DMTN and SLC2A1. Interacts with
CC SLC2A1 (By similarity). Heterodimer of an alpha and a beta subunit.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9QYB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QYB8-2; Sequence=VSP_000184, VSP_000185;
CC Name=3; Synonyms=Delta;
CC IsoId=Q9QYB8-3; Sequence=VSP_022596;
CC -!- DOMAIN: Each subunit is comprised of three regions: a NH2-terminal
CC protease-resistant globular head region, a short connecting subdomain,
CC and a protease-sensitive tail region.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000305}.
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DR EMBL; AF100422; AAF24972.1; -; mRNA.
DR EMBL; AF100423; AAF24973.1; -; mRNA.
DR EMBL; AF189769; AAF29502.1; -; mRNA.
DR EMBL; AF189770; AAF29503.1; -; mRNA.
DR EMBL; AK014496; BAB29395.1; -; mRNA.
DR EMBL; AK028425; BAC25943.1; -; mRNA.
DR EMBL; AK156954; BAE33913.1; -; mRNA.
DR EMBL; BC046783; AAH46783.1; -; mRNA.
DR EMBL; BC053032; AAH53032.1; -; mRNA.
DR CCDS; CCDS20308.1; -. [Q9QYB8-1]
DR CCDS; CCDS85085.1; -. [Q9QYB8-2]
DR PIR; A60670; A60670.
DR RefSeq; NP_001258786.1; NM_001271857.1. [Q9QYB8-1]
DR RefSeq; NP_001258787.1; NM_001271858.1. [Q9QYB8-1]
DR RefSeq; NP_001258788.1; NM_001271859.1. [Q9QYB8-1]
DR RefSeq; NP_001258789.1; NM_001271860.1. [Q9QYB8-2]
DR RefSeq; NP_001258790.1; NM_001271861.1. [Q9QYB8-2]
DR RefSeq; NP_038486.2; NM_013458.5. [Q9QYB8-1]
DR AlphaFoldDB; Q9QYB8; -.
DR SMR; Q9QYB8; -.
DR BioGRID; 197982; 14.
DR IntAct; Q9QYB8; 2.
DR MINT; Q9QYB8; -.
DR STRING; 10090.ENSMUSP00000032069; -.
DR iPTMnet; Q9QYB8; -.
DR PhosphoSitePlus; Q9QYB8; -.
DR REPRODUCTION-2DPAGE; Q9QYB8; -.
DR EPD; Q9QYB8; -.
DR jPOST; Q9QYB8; -.
DR MaxQB; Q9QYB8; -.
DR PaxDb; Q9QYB8; -.
DR PeptideAtlas; Q9QYB8; -.
DR PRIDE; Q9QYB8; -.
DR ProteomicsDB; 296178; -. [Q9QYB8-1]
DR ProteomicsDB; 296179; -. [Q9QYB8-2]
DR ProteomicsDB; 296180; -. [Q9QYB8-3]
DR Antibodypedia; 4066; 244 antibodies from 29 providers.
DR DNASU; 11519; -.
DR Ensembl; ENSMUST00000032069; ENSMUSP00000032069; ENSMUSG00000030000. [Q9QYB8-1]
DR Ensembl; ENSMUST00000203196; ENSMUSP00000145104; ENSMUSG00000030000. [Q9QYB8-2]
DR Ensembl; ENSMUST00000203279; ENSMUSP00000145452; ENSMUSG00000030000. [Q9QYB8-3]
DR Ensembl; ENSMUST00000203366; ENSMUSP00000144849; ENSMUSG00000030000. [Q9QYB8-2]
DR Ensembl; ENSMUST00000203724; ENSMUSP00000145296; ENSMUSG00000030000. [Q9QYB8-1]
DR Ensembl; ENSMUST00000203786; ENSMUSP00000144694; ENSMUSG00000030000. [Q9QYB8-1]
DR Ensembl; ENSMUST00000204059; ENSMUSP00000145160; ENSMUSG00000030000. [Q9QYB8-1]
DR Ensembl; ENSMUST00000205034; ENSMUSP00000145034; ENSMUSG00000030000. [Q9QYB8-2]
DR GeneID; 11519; -.
DR KEGG; mmu:11519; -.
DR UCSC; uc009crd.2; mouse. [Q9QYB8-2]
DR UCSC; uc009cre.2; mouse. [Q9QYB8-1]
DR UCSC; uc012eoj.2; mouse. [Q9QYB8-3]
DR CTD; 119; -.
DR MGI; MGI:87919; Add2.
DR VEuPathDB; HostDB:ENSMUSG00000030000; -.
DR eggNOG; KOG3699; Eukaryota.
DR GeneTree; ENSGT00940000159299; -.
DR HOGENOM; CLU_006033_9_2_1; -.
DR InParanoid; Q9QYB8; -.
DR OMA; PFVQEKA; -.
DR OrthoDB; 400524at2759; -.
DR PhylomeDB; Q9QYB8; -.
DR TreeFam; TF313003; -.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR BioGRID-ORCS; 11519; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Add2; mouse.
DR PRO; PR:Q9QYB8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QYB8; protein.
DR Bgee; ENSMUSG00000030000; Expressed in olfactory tubercle and 173 other tissues.
DR ExpressionAtlas; Q9QYB8; baseline and differential.
DR Genevisible; Q9QYB8; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0008290; C:F-actin capping protein complex; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI.
DR GO; GO:0051017; P:actin filament bundle assembly; ISO:MGI.
DR GO; GO:0051016; P:barbed-end actin filament capping; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0006811; P:ion transport; ISO:MGI.
DR GO; GO:0050900; P:leukocyte migration; ISO:MGI.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IDA:SynGO.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR027773; ADD2.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR PANTHER; PTHR10672:SF6; PTHR10672:SF6; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Calmodulin-binding; Cell membrane;
KW Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..725
FT /note="Beta-adducin"
FT /id="PRO_0000218534"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..444
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000255"
FT REGION 525..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..720
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000255"
FT COMPBIAS 525..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05764"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 533
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 674
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05764"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05764"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT VAR_SEQ 284..531
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10845937"
FT /id="VSP_022596"
FT VAR_SEQ 532..562
FT /note="STESQLMSKGDADTKDESEETVPNPFSQLTD -> VQQRLPPTEGEVYQTPG
FT AGQGTPESSGPLTP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_000184"
FT VAR_SEQ 563..725
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_000185"
FT CONFLICT 219
FT /note="R -> T (in Ref. 2; AAF29503)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="E -> Q (in Ref. 1; AAF24972/AAF24973)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="Q -> H (in Ref. 3; BAC25943)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="A -> R (in Ref. 1; AAF24972)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="G -> V (in Ref. 1; AAF24972)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="D -> V (in Ref. 2; AAF29502/AAF29503)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9QYB8-2:561
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747"
SQ SEQUENCE 725 AA; 80642 MW; 479153AB1BD6C0DA CRC64;
MSEDTVPEAA SPPPSQGQHY FDRFSEDDPE YLRLRNRAAD LRQDFNLMEQ KKRVTMILQS
PSFREELEGL IQEQMKKGNN SSNIWALRQI ADFMASTSHA VFPASSMNFS MMTPINDLHT
ADSLNLAKGE RLMRCKISSV YRLLDLYGWA QLSDTYVTLR VSKEQDHFLI SPKGVSCSEV
TASSLIKVNI LGEVVEKGSS CFPVDTTGFS LHSAIYAARP DVRCAIHLHT PATAAVSAMK
CGLLPVSHNA LLVGDMAYYD FNGEMEQEAD RINLQKCLGP TCKILVLRNH GMVALGDTVE
EAFYKVFHLQ AACEVQVSAL SSAGGTENLI LLEQEKHRPH EVGSVQWAGS TFGPMQKSRL
GEHEFEALMR MLDNLGYRTG YTYRHPFVQE KTKHKSEVEI PATVTAFVFE EDGVPVPALR
QHAQKQQKEK TRWLNTPNTY LRVNVADEVQ RNMGSPRPKT TWMKADEVEK SSSGMPIRIE
NPNQFVPLYT DPQEVLDMRN KIREQNRQDI KSAGPQSQLL ASVIAEKSRS PSTESQLMSK
GDADTKDESE ETVPNPFSQL TDQELEEYKK EVERKKLEQE QEGEKDIATE KPGSPVKSTP
ASPVQSPSKA GTKSPAVSPS KTSEDTKKTE VSEANTEPEP VKPEGLVVNG KEEEPSVEEA
LSKGLGQMTT NADTDGDSYK DKTESVTSGP LSPEGSPSKS PSKKKKKFRT PSFLKKSKKK
EKVES
