MYOF_MOUSE
ID MYOF_MOUSE Reviewed; 2048 AA.
AC Q69ZN7; Q7TMG0; Q80V33; Q8BU64; Q8BU70; Q8BUC1; Q8BVY6; Q8C0D1; Q8R3B4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Myoferlin;
DE AltName: Full=Fer-1-like protein 3;
GN Name=Myof; Synonyms=Fer1l3, Kiaa1207;
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 1).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1322-2048 (ISOFORMS 1/2/3).
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Embryonic head, Embryonic lung, Embryonic testis, and Tongue;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 517-2048 (ISOFORM 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 968-2048 (ISOFORMS 1/2/3).
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 [5]
RP FUNCTION, MUTAGENESIS OF ILE-67, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16280346; DOI=10.1242/dev.02155;
RA Doherty K.R., Cave A., Davis D.B., Delmonte A.J., Posey A., Earley J.U.,
RA Hadhazy M., McNally E.M.;
RT "Normal myoblast fusion requires myoferlin.";
RL Development 132:5565-5575(2005).
RN [6]
RP FUNCTION, INTERACTION WITH DNM2 AND KDR, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17702744; DOI=10.1074/jbc.m704798200;
RA Bernatchez P.N., Acevedo L., Fernandez-Hernando C., Murata T., Chalouni C.,
RA Kim J., Erdjument-Bromage H., Shah V., Gratton J.-P., McNally E.M.,
RA Tempst P., Sessa W.C.;
RT "Myoferlin regulates vascular endothelial growth factor receptor-2
RT stability and function.";
RL J. Biol. Chem. 282:30745-30753(2007).
RN [7]
RP FUNCTION.
RX PubMed=18502764; DOI=10.1074/jbc.m802306200;
RA Doherty K.R., Demonbreun A.R., Wallace G.Q., Cave A., Posey A.D.,
RA Heretis K., Pytel P., McNally E.M.;
RT "The endocytic recycling protein EHD2 interacts with myoferlin to regulate
RT myoblast fusion.";
RL J. Biol. Chem. 283:20252-20260(2008).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-174, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [11]
RP INTERACTION WITH EHD1 AND EHD2, AND INDUCTION.
RX PubMed=21177873; DOI=10.1074/jbc.m110.157222;
RA Posey A.D. Jr., Pytel P., Gardikiotes K., Demonbreun A.R., Rainey M.,
RA George M., Band H., McNally E.M.;
RT "Endocytic recycling proteins EHD1 and EHD2 interact with fer-1-like-5
RT (Fer1L5) and mediate myoblast fusion.";
RL J. Biol. Chem. 286:7379-7388(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-540 AND LYS-1494, AND
RP IDENTIFICATION BY MASS 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: Calcium/phospholipid-binding protein that plays a role in the
CC plasmalemma repair mechanism of endothelial cells that permits rapid
CC resealing of membranes disrupted by mechanical stress. Involved in
CC endocytic recycling. Implicated in VEGF signal transduction by
CC regulating the levels of the receptor KDR.
CC {ECO:0000269|PubMed:16280346, ECO:0000269|PubMed:17702744,
CC ECO:0000269|PubMed:18502764}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds Ca(2+). The ions are bound to the C2 1 domain.;
CC -!- SUBUNIT: Interacts with EHD1 (PubMed:21177873). Interacts with EHD2;
CC the interaction is direct (PubMed:21177873). Interacts with DNM2 and
CC KDR (PubMed:21177873). Interacts with RIPOR2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZM1, ECO:0000269|PubMed:17702744,
CC ECO:0000269|PubMed:21177873}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}. Cytoplasmic vesicle
CC membrane {ECO:0000250}; Single-pass type II membrane protein
CC {ECO:0000250}. Note=Found at nuclear and plasma membranes. Enriched in
CC undifferentiated myoblasts near the plasma membrane in puncate
CC structures (By similarity). Concentrated at the membrane sites of both
CC myoblast-myoblast and myoblast-myotube fusions. Detected at the
CC plasmalemma in endothelial cells lining intact blood vessels.
CC {ECO:0000250, ECO:0000269|PubMed:16280346,
CC ECO:0000269|PubMed:17702744}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q69ZN7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZN7-2; Sequence=VSP_024015, VSP_024016, VSP_024017;
CC Name=3;
CC IsoId=Q69ZN7-3; Sequence=VSP_024013, VSP_024014;
CC Name=4;
CC IsoId=Q69ZN7-4; Sequence=VSP_035934;
CC -!- TISSUE SPECIFICITY: Expressed in myoblasts (at protein level).
CC Expressed in endothelial cells. {ECO:0000269|PubMed:16280346,
CC ECO:0000269|PubMed:17702744}.
CC -!- INDUCTION: Up-regulated during myotube formation.
CC {ECO:0000269|PubMed:21177873}.
CC -!- DOMAIN: The C2 1 domain associates with lipid membranes in a calcium-
CC dependent manner. {ECO:0000250}.
CC -!- MISCELLANEOUS: Mice lacking Myof display fewer large multinucleated
CC myotubes and are impaired in their ability to regenerate skeletal
CC muscle after injury. They display a defective membrane repair in
CC endothelial cells. They show also a delayed endocytic recycling.
CC -!- SIMILARITY: Belongs to the ferlin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25649.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD32409.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK173131; BAD32409.1; ALT_SEQ; mRNA.
DR EMBL; AK031666; BAC27500.1; -; mRNA.
DR EMBL; AK075903; BAC36043.1; -; mRNA.
DR EMBL; AK086107; BAC39611.1; -; mRNA.
DR EMBL; AK087176; BAC39820.2; -; mRNA.
DR EMBL; AK087302; BAC39840.1; -; mRNA.
DR EMBL; AC115360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025649; AAH25649.1; ALT_INIT; mRNA.
DR EMBL; BC044825; AAH44825.1; -; mRNA.
DR EMBL; BC055953; AAH55953.1; -; mRNA.
DR CCDS; CCDS37970.1; -. [Q69ZN7-1]
DR RefSeq; NP_001093104.1; NM_001099634.1. [Q69ZN7-1]
DR RefSeq; NP_001289069.1; NM_001302140.1.
DR AlphaFoldDB; Q69ZN7; -.
DR SMR; Q69ZN7; -.
DR BioGRID; 230471; 6.
DR IntAct; Q69ZN7; 2.
DR STRING; 10090.ENSMUSP00000045036; -.
DR iPTMnet; Q69ZN7; -.
DR PhosphoSitePlus; Q69ZN7; -.
DR SwissPalm; Q69ZN7; -.
DR jPOST; Q69ZN7; -.
DR MaxQB; Q69ZN7; -.
DR PaxDb; Q69ZN7; -.
DR PeptideAtlas; Q69ZN7; -.
DR PRIDE; Q69ZN7; -.
DR ProteomicsDB; 286109; -. [Q69ZN7-1]
DR ProteomicsDB; 286110; -. [Q69ZN7-2]
DR ProteomicsDB; 286111; -. [Q69ZN7-3]
DR ProteomicsDB; 286112; -. [Q69ZN7-4]
DR Antibodypedia; 2467; 98 antibodies from 28 providers.
DR DNASU; 226101; -.
DR Ensembl; ENSMUST00000041475; ENSMUSP00000045036; ENSMUSG00000048612. [Q69ZN7-1]
DR GeneID; 226101; -.
DR KEGG; mmu:226101; -.
DR UCSC; uc008hit.1; mouse. [Q69ZN7-1]
DR CTD; 26509; -.
DR MGI; MGI:1919192; Myof.
DR VEuPathDB; HostDB:ENSMUSG00000048612; -.
DR eggNOG; KOG1326; Eukaryota.
DR GeneTree; ENSGT00940000154741; -.
DR HOGENOM; CLU_001183_2_1_1; -.
DR InParanoid; Q69ZN7; -.
DR OMA; YENQAFM; -.
DR OrthoDB; 20162at2759; -.
DR PhylomeDB; Q69ZN7; -.
DR TreeFam; TF316871; -.
DR BioGRID-ORCS; 226101; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Myof; mouse.
DR PRO; PR:Q69ZN7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q69ZN7; protein.
DR Bgee; ENSMUSG00000048612; Expressed in urinary bladder urothelium and 166 other tissues.
DR ExpressionAtlas; Q69ZN7; baseline and differential.
DR Genevisible; Q69ZN7; MM.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IMP:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR GO; GO:0006071; P:glycerol metabolic process; IGI:MGI.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0055001; P:muscle cell development; IGI:MGI.
DR GO; GO:0007520; P:myoblast fusion; IEA:InterPro.
DR GO; GO:0007009; P:plasma membrane organization; IBA:GO_Central.
DR GO; GO:0001778; P:plasma membrane repair; IMP:UniProtKB.
DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0033292; P:T-tubule organization; IGI:MGI.
DR CDD; cd08373; C2A_Ferlin; 1.
DR CDD; cd04011; C2B_Ferlin; 1.
DR CDD; cd04018; C2C_Ferlin; 1.
DR CDD; cd04017; C2D_Ferlin; 1.
DR CDD; cd04037; C2E_Ferlin; 1.
DR CDD; cd08374; C2F_Ferlin; 1.
DR Gene3D; 2.60.40.150; -; 6.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037726; C2A_Ferlin.
DR InterPro; IPR037720; C2B_Ferlin.
DR InterPro; IPR037722; C2C_Ferlin.
DR InterPro; IPR037723; C2D_Ferlin.
DR InterPro; IPR037724; C2E_Ferlin.
DR InterPro; IPR037725; C2F_Ferlin.
DR InterPro; IPR012968; FerIin_dom.
DR InterPro; IPR037721; Ferlin.
DR InterPro; IPR012560; Ferlin_A-domain.
DR InterPro; IPR012561; Ferlin_B-domain.
DR InterPro; IPR032362; Ferlin_C.
DR InterPro; IPR029999; Myoferlin.
DR InterPro; IPR006614; Peroxin/Ferlin.
DR PANTHER; PTHR12546; PTHR12546; 1.
DR PANTHER; PTHR12546:SF55; PTHR12546:SF55; 1.
DR Pfam; PF00168; C2; 7.
DR Pfam; PF08165; FerA; 1.
DR Pfam; PF08150; FerB; 1.
DR Pfam; PF08151; FerI; 1.
DR Pfam; PF16165; Ferlin_C; 1.
DR SMART; SM00239; C2; 7.
DR SMART; SM00694; DysFC; 2.
DR SMART; SM00693; DysFN; 2.
DR SMART; SM01200; FerA; 1.
DR SMART; SM01201; FerB; 1.
DR SMART; SM01202; FerI; 1.
DR SUPFAM; SSF49562; SSF49562; 7.
DR PROSITE; PS50004; C2; 7.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Cell membrane;
KW Cytoplasmic vesicle; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2048
FT /note="Myoferlin"
FT /id="PRO_0000281646"
FT TOPO_DOM 1..2012
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2013..2033
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2034..2048
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..101
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 183..300
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 339..475
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1110..1238
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1269..1397
FT /note="C2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1523..1641
FT /note="C2 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1759..1907
FT /note="C2 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 124..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..281
FT /note="Necessary for interaction with EHD2"
FT /evidence="ECO:0000250"
FT REGION 1964..1986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1556
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1611
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1613
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1878
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1881
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1884
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 540
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 871
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM1"
FT MOD_RES 1494
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 282..292
FT /note="IDVGFVYDEPG -> VSDSSILLSMI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024013"
FT VAR_SEQ 293..2048
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024014"
FT VAR_SEQ 472
FT /note="E -> EDFSSSGAGAASYT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024015"
FT VAR_SEQ 906..908
FT /note="LLT -> SPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024016"
FT VAR_SEQ 909..2048
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024017"
FT VAR_SEQ 1346..1570
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035934"
FT MUTAGEN 67
FT /note="I->D: Reduces calcium-sensitive phospholipid
FT binding."
FT /evidence="ECO:0000269|PubMed:16280346"
FT CONFLICT 186
FT /note="K -> E (in Ref. 2; BAC39820)"
FT /evidence="ECO:0000305"
FT CONFLICT 1322
FT /note="G -> R (in Ref. 2; BAC36043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2048 AA; 233324 MW; 00D1596472CDFB8E CRC64;
MLRVIVESAT NIPKTKFGKP DPIVSVIFKD EKKKTKKVDN ELNPVWNEIL EFDLRGIPLD
SSSSLVIVVK DFETIGQNKL IGTATVSLKD LIGDQNRSLP YKQTSLLNEK GQDTGATIDL
VIGYTPPSAP HPNDPSGTSV PGMGEEEEED QGDEDRVDGI VRGPGPKGPS GTVSEAQLAR
RITKGKSSRR MLSNKPQDFQ IRVRVIEGRQ LCGNNIRPVV KVHICGQTHR TRIKRGNNPF
FDELFFYNVH ITPSELMDEI ISIRVYNSHS LRADCLMGEF KIDVGFVYDE PGHAVMRKWL
LLNDPEDTSS GAKGYMKVSM FVLGTGDEPP PEKRDRDNDS DDVESNLLLP AGIALRWVTF
MLKIYRAEDI PQMDDAFSQT VKEIFGGNAD KKNLVDPFVE VSFAGKKVCT NIIERNANPE
WNQVVNLQIK FPSMCEKIKL TVYDWDRLTK NDVVGTTYLY LSKIAASGGE VEATTGETEV
GFVPTFGPCY LNLYGSPREY TGFPDPYDEL NSGKGEGVAY RGRIFVELNT FLEKKPPEKK
LEPISSDDLL VVEKYQRRRK YSLSAVFHSA TMLQDVGEAI QFEVSIGNYG NKFDATCKPL
ASTTQYSRAV FDGNYYYYLP WAHTKPVVTL TSYWEDISHR LDAVNTLLVM AERLQSNIEA
VKSGIQGKIP ANQLAEVWLK LIDEVIEDTR YTLPVTEGKA NVTVLDTQIR KLRSRFLSQI
HEAALRMRSE ATDVKSTLLE IEEWLDKLMQ LTEEPQNSMP DIIIWMIRGE KRLAYARIPA
HQVLYSTSGG NASGKYCGKT QTILLKYPQE KTNGPKVPVE LRVNIWLGLS AVEKKFNSFA
EGTFTVFAEM YENQALVFGK WGTSGLVGRH KFSDVTGKIK LKREFFLPPK GWEWEGDWVV
DPERSLLTEA DAGHTEFTDE VYQNENRYPG GEWKQAEDTY TDANGDKAAS PSEMTCPPGW
EWEDDAWIYD INRAVDEKGW EYGITIPPDN KPKSWVAAEK MYHTHRRRRL VRKRKKDLTQ
TASSTARAME ELEDREGWEY ASLIGWKFHW KQRSSDTFRR RRWRRKMAPS ETHGAAAIFK
LEGALGADTT EDGEEKGPEK QKHSATTVFG ANTPIVSCNF DRVYIYHLRC YIYQARNLMA
LDKDSFSDPY AHVSFLHRSK TTEIIHSTLN PTWDQTIIFD EVEIFGEPQT VLQNPPNVTI
ELFDNDQVGK DEFLGRSICS PLVKLNSETD ITPKLLWHPV MNGDKACGDV LVTAELILRN
KDGSNLPILP SQRAPNLYMV PQGIRPVVQL TAIEILAWGL RNMKNYQMAS VTSPSLVVEC
GGERVESVVI KSLKKTPNFP SSVLFMKVFL PKEELYMPPL VIKVIDHRQF GRKPVVGQCT
IDHLDRFRCD PYAGKEDIVP QLKASLMSAP PCREVVIEIE DTKPLLASKL SEKEEEIVDW
WSKFYASSGE HEKCGQYIQK GYSKLKIYDC ELEDVADFEG LTDFSDTFKL YRGKSDENED
PSVVGEFKGS FRIYPLPDDP SVPAPPRQFR ELPDSVPQEC TVRIYIVQGL QLQPQDNNGL
CDPYIKITLG KKVIEDRDHY IPNTLNPVFG RMYELSCYLP QEKDLKISVY DYDTFTRDEK
VGETTIDLEN RFLSRFGSHC GIPEQYCVSG VNTWRDQLRP TQLLQNVARF KGFPPPVLSE
DGSRIRYGGR DYHLDEFEAN KILHQHLGAP EERLALHILR TQGLVPEHVE TRTLHSTFQP
NISQGKLQMW VDVFPKSLGP PGPPFNITPR KAKKYYLRVI IWNTKDVILD EKSITGEDMS
DIYVKGWISG SEENKQKTDV HYRSLDGEGN FNWRFVFPFD YLPAEQLCIV AKKEHFWSID
QTEFRVPPRL IIQIWDNDKF SLDDYLGFLE LDLHRTIIPA KTSEKCSLDM IPDLKAMDPL
KAKTASLFEQ RSMKGWWPCY ADKDGTRVMA GKVEMTLEVL NEREADERPA GKGRSEPNMN
PKLDPPNRPE TSFLWFTNPC KTMRFIVWRR FKWVIIGLLL LLILLLFVAV LLYSLPNYLS
MKIVRPNA
