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   27-MAR-2024, entry version 182.
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.ENSMUSP00000145160; -.
DR   iPTMnet; Q9QYB8; -.
DR   MetOSite; Q9QYB8; -.
DR   PhosphoSitePlus; Q9QYB8; -.
DR   SwissPalm; Q9QYB8; -.
DR   REPRODUCTION-2DPAGE; Q9QYB8; -.
DR   EPD; Q9QYB8; -.
DR   jPOST; Q9QYB8; -.
DR   MaxQB; Q9QYB8; -.
DR   PaxDb; 10090-ENSMUSP00000032069; -.
DR   PeptideAtlas; Q9QYB8; -.
DR   ProteomicsDB; 296178; -. [Q9QYB8-1]
DR   ProteomicsDB; 296179; -. [Q9QYB8-2]
DR   ProteomicsDB; 296180; -. [Q9QYB8-3]
DR   Antibodypedia; 4066; 294 antibodies from 29 providers.
DR   DNASU; 11519; -.
DR   Ensembl; ENSMUST00000032069.8; ENSMUSP00000032069.6; ENSMUSG00000030000.11. [Q9QYB8-1]
DR   Ensembl; ENSMUST00000203196.3; ENSMUSP00000145104.2; ENSMUSG00000030000.11. [Q9QYB8-2]
DR   Ensembl; ENSMUST00000203279.2; ENSMUSP00000145452.2; ENSMUSG00000030000.11. [Q9QYB8-3]
DR   Ensembl; ENSMUST00000203366.3; ENSMUSP00000144849.2; ENSMUSG00000030000.11. [Q9QYB8-2]
DR   Ensembl; ENSMUST00000203724.3; ENSMUSP00000145296.2; ENSMUSG00000030000.11. [Q9QYB8-1]
DR   Ensembl; ENSMUST00000203786.3; ENSMUSP00000144694.2; ENSMUSG00000030000.11. [Q9QYB8-1]
DR   Ensembl; ENSMUST00000204059.3; ENSMUSP00000145160.2; ENSMUSG00000030000.11. [Q9QYB8-1]
DR   Ensembl; ENSMUST00000205034.3; ENSMUSP00000145034.2; ENSMUSG00000030000.11. [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   AGR; MGI:87919; -.
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; TSGFCLH; -.
DR   OrthoDB; 45123at2759; -.
DR   PhylomeDB; Q9QYB8; -.
DR   TreeFam; TF313003; -.
DR   Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR   BioGRID-ORCS; 11519; 3 hits in 76 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 174 other cell types or tissues.
DR   ExpressionAtlas; Q9QYB8; baseline and differential.
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:0046983; F:protein dimerization activity; ISO:MGI.
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:0050900; P:leukocyte migration; ISO:MGI.
DR   GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
DR   GO; GO:0006811; P:monoatomic ion transport; ISO:MGI.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR   GO; GO:0007416; P:synapse assembly; IDA:SynGO.
DR   CDD; cd00398; Aldolase_II; 1.
DR   Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   PANTHER; PTHR10672; ADDUCIN; 1.
DR   PANTHER; PTHR10672:SF6; BETA-ADDUCIN; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
DR   Genevisible; Q9QYB8; MM.
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
//