ANK3_MOUSE
ID ANK3_MOUSE Reviewed; 1961 AA.
AC G5E8K5; G5E8K4; O08866; O08867; Q3TSJ8; Q4U205; Q4U206; Q4U256; Q4U260;
AC Q61305; Q61306; Q61307; Q61308; Q61309; Q61310; Q8CBN3; Q8VC68;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Ankyrin-3;
DE Short=ANK-3;
DE AltName: Full=Ankyrin-G;
GN Name=Ank3;
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] (ISOFORMS 1; 4 AND 6), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=7615634; DOI=10.1083/jcb.130.2.313;
RA Peters L.L., John K.M., Lu F.M., Eicher E.M., Higgins A., Yialamas M.,
RA Turtzo L.C., Otsuka A.J., Lux S.E.;
RT "Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin
RT gene family and the major ankyrin in kidney, is expressed in alternatively
RT spliced forms, including forms that lack the repeat domain.";
RL J. Cell Biol. 130:313-330(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1726 (ISOFORMS 4/5/6).
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [MRNA] OF 742-1961 (ISOFORMS 2 AND 3), SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C3H/HeJ; TISSUE=Bone marrow macrophage;
RX PubMed=9060470; DOI=10.1083/jcb.136.5.1059;
RA Hoock T.C., Peters L.L., Lux S.E.;
RT "Isoforms of ankyrin-3 that lack the NH2-terminal repeats associate with
RT mouse macrophage lysosomes.";
RL J. Cell Biol. 136:1059-1070(1997).
RN [7]
RP FUNCTION, INTERACTION WITH DMD, AND SUBCELLULAR LOCATION.
RX PubMed=19109891; DOI=10.1016/j.cell.2008.10.018;
RA Ayalon G., Davis J.Q., Scotland P.B., Bennett V.;
RT "An ankyrin-based mechanism for functional organization of dystrophin and
RT dystroglycan.";
RL Cell 135:1189-1200(2008).
RN [8]
RP INTERACTION WITH SCHIP1.
RX PubMed=18550753; DOI=10.1523/jneurosci.1044-08.2008;
RA Martin P.M., Carnaud M., Garcia del Cano G., Irondelle M., Irinopoulou T.,
RA Girault J.A., Dargent B., Goutebroze L.;
RT "Schwannomin-interacting protein-1 isoform IQCJ-SCHIP-1 is a late component
RT of nodes of Ranvier and axon initial segments.";
RL J. Neurosci. 28:6111-6117(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-830; SER-850; SER-873;
RP SER-923; SER-1114; SER-1451; SER-1462; SER-1470; SER-1473 AND SER-1795,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1560 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-830 (ISOFORMS 2 AND 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732 (ISOFORM 6), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, 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 DEVELOPMENTAL STAGE.
RX PubMed=21223964; DOI=10.1016/j.yexcr.2011.01.002;
RA Maiweilidan Y., Klauza I., Kordeli E.;
RT "Novel interactions of ankyrins-G at the costameres: the muscle-specific
RT Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C.";
RL Exp. Cell Res. 317:724-736(2011).
RN [11]
RP FUNCTION, INTERACTION WITH KCNA1, IDENTIFICATION BY MASS SPECTROMETRY,
RP INDUCTION BY MAGNESIUM, AND TISSUE SPECIFICITY.
RX PubMed=23903368; DOI=10.1038/ki.2013.280;
RA San-Cristobal P., Lainez S., Dimke H., de Graaf M.J., Hoenderop J.G.,
RA Bindels R.J.;
RT "Ankyrin-3 is a novel binding partner of the voltage-gated potassium
RT channel Kv1.1 implicated in renal magnesium handling.";
RL Kidney Int. 85:94-102(2014).
CC -!- FUNCTION: Membrane-cytoskeleton linker. May participate in the
CC maintenance/targeting of ion channels and cell adhesion molecules at
CC the nodes of Ranvier and axonal initial segments (By similarity). In
CC skeletal muscle, required for costamere localization of DMD and
CC betaDAG1. Regulates KCNA1 channel activity in function of dietary
CC Mg(2+) levels, and thereby contributes to the regulation of renal
CC Mg(2+) reabsorption (PubMed:23903368). {ECO:0000250,
CC ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:23903368}.
CC -!- SUBUNIT: May be a constituent of a NFASC/NRCAM/ankyrin G complex.
CC Interacts with RHBG (By similarity). Directly interacts with DMD and
CC betaDAG1; this interaction does not interfere with DMD-binding and is
CC required for DMD and betaDAG1 retention at costameres. Interacts (via
CC N-terminal ANK repeats) with SCHIP1 isoform 7 (via C-terminus); this
CC interaction is required for the localization at axon initial segments
CC (AISs) and nodes of Ranvier (NRs). Interacts with PLEC and FLNC (By
CC similarity). Interacts with KCNA1; this inhibits channel activity
CC (PubMed:23903368). Interacts with SCN5A (By similarity).
CC {ECO:0000250|UniProtKB:O70511, ECO:0000250|UniProtKB:Q12955,
CC ECO:0000269|PubMed:18550753, ECO:0000269|PubMed:19109891}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q12955}. Cell projection, axon
CC {ECO:0000250|UniProtKB:O70511}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q12955}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:O70511}. Lysosome {ECO:0000269|PubMed:9060470}.
CC Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O70511}.
CC Note=In skeletal muscle, localized at costameres and neuromuscular
CC junctions. In bone marrow-derived macrophages, isoforms 2 and 3 are
CC associated with lysosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=G5E8K5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=G5E8K5-2; Sequence=VSP_044356, VSP_044358;
CC Name=3;
CC IsoId=G5E8K5-3; Sequence=VSP_044356;
CC Name=4;
CC IsoId=G5E8K5-4; Sequence=VSP_044355, VSP_044357;
CC Name=5;
CC IsoId=G5E8K5-5; Sequence=VSP_044355, VSP_044357, VSP_044359;
CC Name=6;
CC IsoId=G5E8K5-6; Sequence=VSP_044355, VSP_044357, VSP_044358;
CC -!- TISSUE SPECIFICITY: Expressed in many epithelial tissues, muscles and
CC axons. Expressed in kidney, brain, skin, lung, liver, intestine,
CC pancreas, heart and testis (at protein level). In testis, expressed in
CC Leydig cells, but very weakly or not at all in Sertoli cells or
CC seminiferous tubules. Expressed in macrophages (at protein level).
CC {ECO:0000269|PubMed:23903368, ECO:0000269|PubMed:7615634,
CC ECO:0000269|PubMed:9060470}.
CC -!- DEVELOPMENTAL STAGE: In an in vitro model of myogenesis, not detected
CC in proliferating myoblasts. Hardly detectable during the first days of
CC differentiation. Expression greatly increases in mature myotubes.
CC {ECO:0000269|PubMed:21223964}.
CC -!- INDUCTION: Up-regulated by high dietary Mg(2+) levels.
CC {ECO:0000269|PubMed:23903368}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB58380.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB58381.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L40631; AAB01602.1; -; mRNA.
DR EMBL; L40631; AAB01603.1; -; mRNA.
DR EMBL; L40632; AAB01607.1; -; mRNA.
DR EMBL; AK035681; BAC29151.1; -; mRNA.
DR EMBL; AK162007; BAE36677.1; -; mRNA.
DR EMBL; AC100427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466553; EDL31985.1; -; Genomic_DNA.
DR EMBL; CH466553; EDL31989.1; -; Genomic_DNA.
DR EMBL; CH466553; EDL31990.1; -; Genomic_DNA.
DR EMBL; BC021657; AAH21657.1; -; mRNA.
DR EMBL; U89274; AAB58380.1; ALT_INIT; mRNA.
DR EMBL; U89275; AAB58381.1; ALT_INIT; mRNA.
DR CCDS; CCDS23909.1; -. [G5E8K5-1]
DR CCDS; CCDS23912.1; -. [G5E8K5-4]
DR CCDS; CCDS35931.1; -. [G5E8K5-3]
DR CCDS; CCDS59545.1; -. [G5E8K5-2]
DR CCDS; CCDS59546.1; -. [G5E8K5-6]
DR RefSeq; NP_033800.2; NM_009670.4. [G5E8K5-6]
DR RefSeq; NP_666117.2; NM_146005.3. [G5E8K5-1]
DR RefSeq; NP_733788.2; NM_170687.3. [G5E8K5-4]
DR RefSeq; NP_733789.1; NM_170688.2.
DR RefSeq; NP_733790.2; NM_170689.2.
DR RefSeq; NP_733791.2; NM_170690.2.
DR RefSeq; NP_733924.2; NM_170728.2. [G5E8K5-2]
DR RefSeq; NP_733925.2; NM_170729.2. [G5E8K5-3]
DR RefSeq; NP_733926.2; NM_170730.2.
DR RefSeq; XP_006513202.1; XM_006513139.3. [G5E8K5-5]
DR AlphaFoldDB; G5E8K5; -.
DR SMR; G5E8K5; -.
DR BioGRID; 198102; 7.
DR IntAct; G5E8K5; 9.
DR MINT; G5E8K5; -.
DR STRING; 10090.ENSMUSP00000090089; -.
DR iPTMnet; G5E8K5; -.
DR PhosphoSitePlus; G5E8K5; -.
DR SwissPalm; G5E8K5; -.
DR jPOST; G5E8K5; -.
DR MaxQB; G5E8K5; -.
DR PaxDb; G5E8K5; -.
DR PRIDE; G5E8K5; -.
DR ProteomicsDB; 296240; -. [G5E8K5-1]
DR ProteomicsDB; 296241; -. [G5E8K5-2]
DR ProteomicsDB; 296242; -. [G5E8K5-3]
DR ProteomicsDB; 296243; -. [G5E8K5-4]
DR ProteomicsDB; 296244; -. [G5E8K5-5]
DR ProteomicsDB; 296245; -. [G5E8K5-6]
DR ABCD; G5E8K5; 6 sequenced antibodies.
DR Antibodypedia; 4197; 299 antibodies from 28 providers.
DR DNASU; 11735; -.
DR Ensembl; ENSMUST00000054167; ENSMUSP00000061698; ENSMUSG00000069601. [G5E8K5-3]
DR Ensembl; ENSMUST00000092433; ENSMUSP00000090089; ENSMUSG00000069601. [G5E8K5-4]
DR Ensembl; ENSMUST00000092434; ENSMUSP00000090090; ENSMUSG00000069601. [G5E8K5-1]
DR Ensembl; ENSMUST00000181974; ENSMUSP00000138285; ENSMUSG00000069601. [G5E8K5-6]
DR Ensembl; ENSMUST00000182029; ENSMUSP00000138337; ENSMUSG00000069601. [G5E8K5-5]
DR Ensembl; ENSMUST00000182155; ENSMUSP00000138347; ENSMUSG00000069601. [G5E8K5-2]
DR Ensembl; ENSMUST00000182884; ENSMUSP00000138326; ENSMUSG00000069601. [G5E8K5-1]
DR GeneID; 11735; -.
DR KEGG; mmu:11735; -.
DR UCSC; uc007fmw.1; mouse. [G5E8K5-1]
DR UCSC; uc007fna.1; mouse. [G5E8K5-2]
DR UCSC; uc007fnb.1; mouse. [G5E8K5-3]
DR UCSC; uc007fnh.1; mouse. [G5E8K5-6]
DR UCSC; uc007fni.1; mouse. [G5E8K5-5]
DR UCSC; uc007fnk.1; mouse. [G5E8K5-4]
DR CTD; 288; -.
DR MGI; MGI:88026; Ank3.
DR VEuPathDB; HostDB:ENSMUSG00000069601; -.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000154939; -.
DR HOGENOM; CLU_000134_7_2_1; -.
DR InParanoid; G5E8K5; -.
DR OrthoDB; 1011028at2759; -.
DR TreeFam; TF351263; -.
DR BioGRID-ORCS; 11735; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Ank3; mouse.
DR PRO; PR:G5E8K5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; G5E8K5; protein.
DR Bgee; ENSMUSG00000069601; Expressed in lateral geniculate body and 252 other tissues.
DR ExpressionAtlas; G5E8K5; baseline and differential.
DR Genevisible; G5E8K5; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043194; C:axon initial segment; IDA:BHF-UCL.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
DR GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISS:BHF-UCL.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR GO; GO:0033270; C:paranode region of axon; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0042383; C:sarcolemma; ISS:BHF-UCL.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISS:BHF-UCL.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; ISS:BHF-UCL.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0030315; C:T-tubule; ISS:BHF-UCL.
DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; ISS:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISS:BHF-UCL.
DR GO; GO:0140031; F:phosphorylation-dependent protein binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL.
DR GO; GO:0030507; F:spectrin binding; ISS:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:BHF-UCL.
DR GO; GO:0071286; P:cellular response to magnesium ion; IMP:UniProtKB.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; ISO:MGI.
DR GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:MGI.
DR GO; GO:0010960; P:magnesium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0072660; P:maintenance of protein location in plasma membrane; ISO:MGI.
DR GO; GO:0071709; P:membrane assembly; ISS:BHF-UCL.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IMP:UniProtKB.
DR GO; GO:0007528; P:neuromuscular junction development; ISS:BHF-UCL.
DR GO; GO:0019228; P:neuronal action potential; IMP:BHF-UCL.
DR GO; GO:0007009; P:plasma membrane organization; ISO:MGI.
DR GO; GO:0045760; P:positive regulation of action potential; TAS:BHF-UCL.
DR GO; GO:2001259; P:positive regulation of cation channel activity; ISS:BHF-UCL.
DR GO; GO:0010650; P:positive regulation of cell communication by electrical coupling; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:1900827; P:positive regulation of membrane depolarization during cardiac muscle cell action potential; ISS:BHF-UCL.
DR GO; GO:0045838; P:positive regulation of membrane potential; ISS:BHF-UCL.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:BHF-UCL.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISS:BHF-UCL.
DR GO; GO:0099612; P:protein localization to axon; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0043266; P:regulation of potassium ion transport; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR CDD; cd08803; Death_ank3; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR037971; Ank3_Death.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR040745; Ankyrin_UPA.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR000906; ZU5_dom.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 8.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF17809; UPA_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 22.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48403; SSF48403; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 21.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS51145; ZU5; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Lysosome; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1961
FT /note="Ankyrin-3"
FT /id="PRO_0000419782"
FT REPEAT 56..85
FT /note="ANK 1"
FT REPEAT 89..118
FT /note="ANK 2"
FT REPEAT 122..151
FT /note="ANK 3"
FT REPEAT 155..184
FT /note="ANK 4"
FT REPEAT 186..213
FT /note="ANK 5"
FT REPEAT 217..246
FT /note="ANK 6"
FT REPEAT 250..279
FT /note="ANK 7"
FT REPEAT 283..312
FT /note="ANK 8"
FT REPEAT 316..345
FT /note="ANK 9"
FT REPEAT 349..378
FT /note="ANK 10"
FT REPEAT 382..411
FT /note="ANK 11"
FT REPEAT 415..444
FT /note="ANK 12"
FT REPEAT 448..477
FT /note="ANK 13"
FT REPEAT 481..510
FT /note="ANK 14"
FT REPEAT 514..543
FT /note="ANK 15"
FT REPEAT 547..576
FT /note="ANK 16"
FT REPEAT 580..609
FT /note="ANK 17"
FT REPEAT 613..642
FT /note="ANK 18"
FT REPEAT 646..675
FT /note="ANK 19"
FT REPEAT 679..708
FT /note="ANK 20"
FT REPEAT 712..741
FT /note="ANK 21"
FT REPEAT 745..774
FT /note="ANK 22"
FT REPEAT 778..807
FT /note="ANK 23"
FT DOMAIN 985..1140
FT /note="ZU5 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 1142..1289
FT /note="ZU5 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 1478..1562
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1408
FT /note="UPA domain"
FT /evidence="ECO:0000250"
FT REGION 1606..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1784..1818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1844..1884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1915..1961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1918..1961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12955"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70511"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70511"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70511"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70511"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 958
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70511"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70511"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1813
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12955"
FT MOD_RES 1883
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12955"
FT VAR_SEQ 1..867
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:7615634"
FT /id="VSP_044355"
FT VAR_SEQ 834..873
FT /note="VRKASAPEKLSDGEYISDGEEGDKCTWFKIPKVQEVLVKS -> G (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9060470"
FT /id="VSP_044356"
FT VAR_SEQ 868..872
FT /note="EVLVK -> MALPH (in isoform 4, isoform 5 and isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:7615634"
FT /id="VSP_044357"
FT VAR_SEQ 1588..1783
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7615634, ECO:0000303|PubMed:9060470"
FT /id="VSP_044358"
FT VAR_SEQ 1941
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044359"
FT CONFLICT 717
FT /note="L -> P (in Ref. 5; AAH21657)"
FT /evidence="ECO:0000305"
FT CONFLICT 1603
FT /note="C -> W (in Ref. 1; AAB01607/AAB01603 and 5;
FT AAB58381)"
FT /evidence="ECO:0000305"
FT CONFLICT 1652
FT /note="V -> I (in Ref. 2; BAC29151)"
FT /evidence="ECO:0000305"
FT MOD_RES G5E8K5-2:830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES G5E8K5-2:1560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES G5E8K5-3:830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES G5E8K5-6:732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1961 AA; 214062 MW; 58F91B5BF87867CE CRC64;
MSEEPKEKPA KPAHRKRKGK KSDANASYLR AARAGHLEKA LDYIKNGVDV NICNQNGLNA
LHLASKEGHV EVVSELLQRE ANVDAATKKG NTALHIASLA GQAEVVKVLV TNGANVNAQS
QNGFTPLYMA AQENHLEVVR FLLDNGASQS LATEDGFTPL AVALQQGHDQ VVSLLLENDT
KGKVRLPALH IAARKDDTKA AALLLQNDTN ADVESKSGFT PLHIAAHYGN INVATLLLNR
AAAVDFTARN DITPLHVASK RGNANMVKLL LDRGAKIDAK TRDGLTPLHC GARSGHEQVV
EMLLDRSAPI LSKTKNGLSP LHMATQGDHL NCVQLLLQHN VPVDDVTNDY LTALHVAAHC
GHYKVAKVLL DKKASPNAKA LNGFTPLHIA CKKNRIRVME LLLKHGASIQ AVTESGLTPI
HVAAFMGHVN IVSQLMHHGA SPNTTNVRGE TALHMAARSG QAEVVRYLVQ DGAQVEAKAK
DDQTPLHISA RLGKADIVQQ LLQQGASPNA ATTSGYTPLH LAAREGHEDV AAFLLDHGAS
LSITTKKGFT PLHVAAKYGK LEVASLLLQK SASPDAAGKS GLTPLHVAAH YDNQKVALLL
LDQGASPHAA AKNGYTPLHI AAKKNQMDIA TSLLEYGADA NAVTRQGIAS VHLAAQEGHV
DMVSLLLSRN ANVNLSNKSG LTPLHLAAQE DRVNVAEVLV NQGAHVDAQT KMGYTPLHVG
CHYGNIKIVN FLLQHSAKVN AKTKNGYTAL HQAAQQGHTH IINVLLQNNA SPNELTVNGN
TALAIARRLG YISVVDTLKV VTEEIMTTTT ITEKHKMNVP ETMNEVLDMS DDEVRKASAP
EKLSDGEYIS DGEEGDKCTW FKIPKVQEVL VKSEDAITGD TDKYLGPQDL KELGDDSLPA
EGYVGFSLGA RSASLRSFSS DRSYTLNRSS YARDSMMIEE LLVPSKEQHL TFTREFDSDS
LRHYSWAADT LDNVNLVSSP VHSGFLVSFM VDARGGSMRG SRHHGMRIII PPRKCTAPTR
ITCRLVKRHK LANPPPMVEG EGLASRLVEM GPAGAQFLGP VIVEIPHFGS MRGKERELIV
LRSENGETWK EHQFDSKNED LAELLNGMDE ELDSPEELGT KRICRIITKD FPQYFAVVSR
IKQESNQIGP EGGILSSTTV PLVQASFPEG ALTKRIRVGL QAQPVPEETV KKILGNKATF
SPIVTVEPRR RKFHKPITMT IPVPPPSGEG VSNGYKGDAT PNLRLLCSIT GGTSPAQWED
ITGTTPLTFI KDCVSFTTNV SARFWLADCH QVLETVGLAS QLYRELICVP YMAKFVVFAK
TNDPVESSLR CFCMTDDRVD KTLEQQENFE EVARSKDIEV LEGKPIYVDC YGNLAPLTKG
GQQLVFNFYS FKENRLPFSI KIRDTSQEPC GRLSFLKEPK TTKGLPQTAV CNLNITLPAH
KKAEKADRRQ SFASLALRKR YSYLTEPSMS PQSPCERTDI RMAIVADHLG LSWTELAREL
NFSVDEINQI RVENPNSLIS QSFMLLKKWV TRDGKNATTD ALTSVLTKIN RIDIVTLLEG
PIFDYGNISG TRSFADENNV FHDPVDGHPS FQVELETPMG LYCTPPNPFQ QDDHFSDISS
IESPFRTPSR LSDGLVPSQG NIEHPTGGPP VVTAEDTSLE DSKMDDSVTV TDPADPLDVD
ESQLKDLCQS ECAQCWASVP GIPNDGRQAE PLRPQTRKVG MSSEQQEKGK SGPDEEVTED
KVKSLFEDIQ LEEVEAEEMT EDQGQAMLNR VQRAELAMSS LAGWQNETPS GSLESPAQAR
RLTGGLLDRL DDSSDQARDS ITSYLTGEPG KIEANGNHTA EVIPEAKAKP YFPESQNDIG
KQSIKENLKP KTHGCGRTEE PVSPLTAYQK SLEETSKLVI EDAPKPCVPV GMKKMTRTTA
DGKARLNLQE EEGSTRSEPK QGEGYKVKTK KEIRNVEKKT H
