SPTN1_MOUSE
ID SPTN1_MOUSE Reviewed; 2472 AA.
AC P16546; A3KGU6; A3KGU8; Q8K380; Q9CT05;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Spectrin alpha chain, non-erythrocytic 1;
DE AltName: Full=Alpha-II spectrin;
DE AltName: Full=Fodrin alpha chain;
GN Name=Sptan1; Synonyms=Spna2, Spta2;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP PROTEIN SEQUENCE OF 8-18; 46-51; 64-81; 85-121; 130-137; 169-227; 251-259;
RP 263-272; 275-295; 321-347; 382-402; 419-439; 442-459; 523-547; 614-627;
RP 686-708; 734-742; 792-801; 813-839; 847-862; 908-930; 990-1002; 1013-1022;
RP 1068-1082; 1197-1209; 1253-1273; 1314-1326; 1350-1359; 1370-1380;
RP 1418-1427; 1501-1519; 1547-1570; 1592-1605; 1608-1619; 1700-1713;
RP 1716-1736; 1772-1781; 1784-1794; 1808-1828; 1830-1844; 1866-1923;
RP 1926-1938; 1985-1995; 2018-2040; 2065-2075; 2088-2098; 2138-2155;
RP 2265-2281; 2354-2382; 2405-2435 AND 2455-2467, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 995-1396 (ISOFORM 2).
RC TISSUE=Macrophage;
RX PubMed=2111175; DOI=10.1016/0300-9084(90)90168-g;
RA Sri Widada J., Asselin J., Colote S., Ferraz C., Trave G., Afshar M.,
RA Haiech J., Liautard J.-P.;
RT "Identification of the calmodulin binding domain of alpha-fodrin and
RT implications for folding.";
RL Biochimie 72:19-24(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 995-1396 (ISOFORM 2).
RX PubMed=2926814; DOI=10.1016/0022-2836(89)90355-0;
RA Sri Widada J., Asselin J., Colote S., Marti J., Ferraz C., Trave G.,
RA Haiech J., Liautard J.-P.;
RT "Cloning and deletion mutagenesis using direct protein-protein interaction
RT on an expression vector. Identification of the calmodulin binding domain of
RT alpha-fodrin.";
RL J. Mol. Biol. 205:455-458(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1118-2472.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1819-2472.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [7]
RP PROTEIN SEQUENCE OF 2071-2079.
RC STRAIN=C57BL/6Cr; TISSUE=Brain;
RX PubMed=10870971;
RX DOI=10.1002/(sici)1522-2683(20000501)21:9<1853::aid-elps1853>3.0.co;2-y;
RA Tsugita A., Kawakami T., Uchida T., Sakai T., Kamo M., Matsui T.,
RA Watanabe Y., Morimasa T., Hosokawa K., Toda T.;
RT "Proteome analysis of mouse brain: two-dimensional electrophoresis profiles
RT of tissue proteins during the course of aging.";
RL Electrophoresis 21:1853-1871(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587; SER-1029; SER-1031;
RP SER-1190; SER-1217; SER-1291; SER-1323; SER-1550 AND THR-2066, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-803, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Fodrin, which seems to be involved in secretion, interacts
CC with calmodulin in a calcium-dependent manner and is thus candidate for
CC the calcium-dependent movement of the cytoskeleton at the membrane.
CC -!- SUBUNIT: Like erythrocyte spectrin, the spectrin-like proteins are
CC capable of forming dimers which can further associate to tetramers.
CC Interacts (via C-terminal spectrin repeats) with TRPC4. Interacts with
CC CALM and EMD. Interacts with isoform 1 of ACP1. Identified in a complex
CC with ACTN4, CASK, IQGAP1, MAGI2, NPHS1 and SPTBN1. Interacts with
CC SHANK3 (via ANK repeats) (By similarity). Interacts with CLN3; this
CC interaction regulates the fodrin localization at the plasma membrane
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q13813}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC Note=Expressed along the cell membrane in podocytes and presumptive
CC tubule cells during glomerulogenesis and is expressed along lateral
CC cell margins in tubule cells. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P16546-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P16546-2; Sequence=VSP_022093;
CC -!- PTM: Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by
CC calpain in vitro. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
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DR EMBL; AL928926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X12801; CAA31289.1; -; mRNA.
DR EMBL; BC027791; AAH27791.1; -; mRNA.
DR EMBL; AK011566; BAB27703.1; -; mRNA.
DR CCDS; CCDS89463.1; -. [P16546-1]
DR PIR; A43769; A43769.
DR PIR; PC7076; PC7076.
DR AlphaFoldDB; P16546; -.
DR BMRB; P16546; -.
DR SMR; P16546; -.
DR DIP; DIP-37712N; -.
DR IntAct; P16546; 32.
DR MINT; P16546; -.
DR STRING; 10090.ENSMUSP00000097797; -.
DR GlyConnect; 2738; 2 N-Linked glycans (1 site).
DR GlyGen; P16546; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; P16546; -.
DR PhosphoSitePlus; P16546; -.
DR SwissPalm; P16546; -.
DR UCD-2DPAGE; P16546; -.
DR EPD; P16546; -.
DR jPOST; P16546; -.
DR MaxQB; P16546; -.
DR PaxDb; P16546; -.
DR PeptideAtlas; P16546; -.
DR PRIDE; P16546; -.
DR ProteomicsDB; 261580; -. [P16546-1]
DR ProteomicsDB; 261581; -. [P16546-2]
DR Antibodypedia; 1910; 480 antibodies from 44 providers.
DR Ensembl; ENSMUST00000046257; ENSMUSP00000047792; ENSMUSG00000057738. [P16546-2]
DR Ensembl; ENSMUST00000095083; ENSMUSP00000092697; ENSMUSG00000057738. [P16546-1]
DR UCSC; uc008jat.1; mouse. [P16546-1]
DR MGI; MGI:98386; Sptan1.
DR VEuPathDB; HostDB:ENSMUSG00000057738; -.
DR eggNOG; KOG0040; Eukaryota.
DR GeneTree; ENSGT00940000156662; -.
DR HOGENOM; CLU_000847_0_0_1; -.
DR InParanoid; P16546; -.
DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-MMU-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR ChiTaRS; Sptan1; mouse.
DR PRO; PR:P16546; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P16546; protein.
DR Bgee; ENSMUSG00000057738; Expressed in facial nucleus and 270 other tissues.
DR ExpressionAtlas; P16546; baseline and differential.
DR Genevisible; P16546; MM.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0032437; C:cuticular plate; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0033010; C:paranodal junction; IDA:MGI.
DR GO; GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR CDD; cd11808; SH3_Alpha_Spectrin; 1.
DR CDD; cd00176; SPEC; 12.
DR InterPro; IPR035825; Alpha_Spectrin_SH3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 20.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 20.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Alternative splicing; Calcium;
KW Calmodulin-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2472
FT /note="Spectrin alpha chain, non-erythrocytic 1"
FT /id="PRO_0000073456"
FT REPEAT 45..146
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 150..251
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 256..358
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 361..465
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 468..570
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 574..676
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 679..781
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 785..888
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 891..961
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT DOMAIN 967..1026
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1096..1166
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1233..1336
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1339..1441
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1446..1549
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1552..1656
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1659..1762
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1764..1868
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 1871..1974
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT REPEAT 1978..2081
FT /note="Spectrin 18"
FT /evidence="ECO:0000255"
FT REPEAT 2092..2194
FT /note="Spectrin 19"
FT /evidence="ECO:0000255"
FT REPEAT 2206..2310
FT /note="Spectrin 20"
FT /evidence="ECO:0000255"
FT DOMAIN 2323..2358
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2366..2401
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2404..2439
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 1176..1177
FT /note="Cleavage; by mu-calpain"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 637
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 803
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16086"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1176
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1519
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 2020
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 2052
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 2066
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2421
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT VAR_SEQ 1053..1072
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2111175,
FT ECO:0000303|PubMed:2926814"
FT /id="VSP_022093"
FT CONFLICT 995
FT /note="T -> A (in Ref. 3; CAA31289)"
FT /evidence="ECO:0000305"
FT CONFLICT 1156
FT /note="D -> G (in Ref. 3; CAA31289)"
FT /evidence="ECO:0000305"
FT CONFLICT 1204
FT /note="T -> S (in Ref. 3; CAA31289)"
FT /evidence="ECO:0000305"
FT CONFLICT 1279
FT /note="E -> D (in Ref. 3; CAA31289)"
FT /evidence="ECO:0000305"
FT CONFLICT 1396
FT /note="Q -> P (in Ref. 3; CAA31289)"
FT /evidence="ECO:0000305"
FT CONFLICT 1819
FT /note="A -> S (in Ref. 6; BAB27703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2472 AA; 284597 MW; 7D778AC0B32D0AD6 CRC64;
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI
QEKLQVASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI
RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD
LEHVEVLQKK FEEFQTDLAA HEERVNEVSQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL
KGLALQRQGK LFGAAEVQRF NRDVDETIGW IKEKEQLMAS DDFGRDLASV QALLRKHEGL
ERDLAALEDK VKALCAEADR LQQSHPLSAS QIQVKREELI TNWEQIRTLA AERHARLDDS
YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFKSA
DESGQALLAA SHYASDEVRE KLSILSEERT ALLELWELRR QQYEQCMDLQ LFYRDTEQVD
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA
MEDVATRRDA LLSRRNALHE RAMHRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKEEVA ARMNEVISLW
KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH
ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL
ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI
KAVTQKGNAM VEEGHFAAED VKAKLSELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN
EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV
APMDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY
VKKLDPAQSA SRENLLEEQG SIALRQGQID NQTRITKEAG SVSLRMKQVE ELYQSLLELG
EKRKGMLEKS CKKFMLFREA NELQQWITEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL
KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGAMP RDEADSKTAS PWKSARLMVH
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN
YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAQRLI QSHPESAEDL KEKCTELNQA
WTSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER
HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKEKL DILDQERTDL EKAWVQRRMM
LDHCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK
IAALQAFADQ LIAVDHYAKG DIANRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV
DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG
ACAGSEDAVK ARLAALADQW QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL
LASEDYGKDL ASVNNLLKKH QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKEKRD
TINGRFQKIK SMATSRRAKL SESHRLHQFF RDMDDEESWI KEKKLLVSSE DYGRDLTGVQ
NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGQEE IQQRLAQFVE HWKELKQLAA
ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT
VHKDRVNDVC TNGQDLIKKN NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ
FNWKADVVES WIGEKENSLK TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK
DQLLAAKHIQ SKAIEARHAS LMKRWTQLLA NSATRKKKLL EAQSHFRKVE DLFLTFAKKA
SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL AELDRQIKSF
RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ EENDKLRQEF AQHANAFHQW
IQETRTYLLD GSCMVEESGT LESQLEATKR KHQEIRAMRS QLKKIEDLGA AMEEALILDN
KYTEHSTVGL AQQWDQLDQL GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS
GRLNHQEFKS CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET
ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD GKGRELPTAF
DYVEFTRSLF VN
