ID ANK1_MOUSE Reviewed; 1862 AA. AC Q02357; P70440; P97446; P97941; Q3TZ35; Q3UH42; Q3UHP2; Q3UYY7; Q61302; AC Q61303; Q78E45; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 2. DT 27-MAR-2024, entry version 194. DE RecName: Full=Ankyrin-1 {ECO:0000305}; DE Short=ANK-1; DE AltName: Full=Erythrocyte ankyrin; GN Name=Ank1 {ECO:0000312|MGI:MGI:88024}; Synonyms=Ank-1; 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] (ISOFORM ER1). RC TISSUE=Erythrocyte; RX PubMed=1386265; DOI=10.1007/bf00292156; RA White R.A., Birkenmeier C.S., Peters L.L., Barker J.E., Lux S.E.; RT "Murine erythrocyte ankyrin cDNA: highly conserved regions of the RT regulatory domain."; RL Mamm. Genome 3:281-285(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BR2; ER3 AND BR4). RC STRAIN=C57BL/6J; TISSUE=Cerebellum; RX PubMed=8486643; DOI=10.1016/s0021-9258(18)98384-5; RA Birkenmeier C.S., White R.A., Peters L.L., Hall E.J., Lux S.E., RA Barker J.E.; RT "Complex patterns of sequence variation and multiple 5' and 3' ends are RT found among transcripts of the erythroid ankyrin gene."; RL J. Biol. Chem. 268:9533-9540(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MU7), TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle; RX PubMed=9628825; DOI=10.1006/geno.1998.5305; RA Birkenmeier C.S., Sharp J.J., Gifford E.J., Deveau S.A., Barker J.E.; RT "An alternative first exon in the distal end of the erythroid ankyrin gene RT leads to production of a small isoform containing an NH2-terminal membrane RT anchor."; RL Genomics 50:79-88(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BR2; 5; 6 AND MU8). RC STRAIN=C57BL/6J; TISSUE=Forelimb, and Inner ear; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MU7). RC TISSUE=Heart, and Lung; 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 PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/6J; RA Birkenmeier C.B., Sharp J.J., Hall E.J., Deveau S.A., Barker J.E.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [7] RP PROTEIN SEQUENCE OF 95-106, AND HYDROXYLATION AT ASN-101. RX PubMed=21177872; DOI=10.1074/jbc.m110.193540; RA Yang M., Ge W., Chowdhury R., Claridge T.D., Kramer H.B., Schmierer B., RA McDonough M.A., Gong L., Kessler B.M., Ratcliffe P.J., Coleman M.L., RA Schofield C.J.; RT "Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family RT is catalyzed by factor-inhibiting hypoxia-inducible factor."; RL J. Biol. Chem. 286:7648-7660(2011). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=9024692; DOI=10.1083/jcb.136.3.621; RA Zhou D., Birkenmeier C.S., Williams M.W., Sharp J.J., Barker J.E., RA Bloch R.J.; RT "Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated RT with the sarcoplasmic reticulum of mammalian skeletal muscle."; RL J. Cell Biol. 136:621-631(1997). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852 AND THR-862, AND RP IDENTIFICATION BY 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-957 AND SER-1388, 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1069, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777; SER-813; SER-852; RP THR-862; THR-957; SER-1078; SER-1386; SER-1388; THR-1396; SER-1424; RP SER-1473; SER-1482 AND SER-1612, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT RP SER-55 (ISOFORMS MU7 AND MU8), AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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). CC -!- FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex CC involved in the stability and shape of the erythrocyte membrane. CC Attaches integral membrane proteins to cytoskeletal elements; binds to CC the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the CC lymphocyte membrane protein GP85, and to the cytoskeletal proteins CC fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link CC spectrin (beta chain) to the cytoplasmic domain of the erythrocytes CC anion exchange protein; they retain most or all of these binding CC functions. {ECO:0000250|UniProtKB:P16157}. CC -!- SUBUNIT: Component of the ankyrin-1 complex in the erythrocyte, CC composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1. CC Interacts with a number of integral membrane proteins and cytoskeletal CC proteins. Interacts (via N-terminus) with SPTB/spectrin (beta chain). CC Also interacts with TTN/titin. Isoform Mu17 interacts with OBSCN CC isoform 3/obscurin. Interacts with HIF1AN. Interacts (via ANK 1-5 CC repeats) with RHCE; this interaction mediates the primary membrane CC attachment site for ANK1. Interacts (via ANK 1-2 repeats) with AQP1 CC (via the N-terminal). Interacts (via ANK 1-13 repeats) with EPB42. CC Interacts directly with SLC4A1 (via the cytoplasmic domain); this CC interaction is mediated by the SLC4A1 Band 3-II and Band 3-III dimers. CC {ECO:0000250|UniProtKB:P16157}. CC -!- SUBCELLULAR LOCATION: [Isoform Er1]: Cytoplasm, cytoskeleton CC {ECO:0000250}. Note=Probably the other erythrocyte (Er) isoforms, are CC located near the surface of erythrocytic plasma membrane. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform Mu7]: Membrane {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform Mu8]: Sarcoplasmic reticulum CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=8; CC Name=Er1; CC IsoId=Q02357-1; Sequence=Displayed; CC Name=Br2; Synonyms=Cb14/11; CC IsoId=Q02357-2; Sequence=VSP_018453, VSP_018455, VSP_018457; CC Name=Er3; Synonyms=Er18; CC IsoId=Q02357-3; Sequence=VSP_018460; CC Name=Br4; Synonyms=Cb12; CC IsoId=Q02357-4; Sequence=VSP_018459; CC Name=5; CC IsoId=Q02357-5; Sequence=VSP_018454, VSP_018456; CC Name=6; CC IsoId=Q02357-6; Sequence=VSP_018454, VSP_018455; CC Name=Mu7; Synonyms=skAnk1; CC IsoId=Q02357-7; Sequence=VSP_018452, VSP_018458; CC Name=Mu8; CC IsoId=Q02357-8; Sequence=VSP_018452, VSP_018458, VSP_018460; CC -!- DOMAIN: The 55 kDa regulatory domain is involved in regulating binding CC of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein CC band 3. {ECO:0000250}. CC -!- DOMAIN: The tandem configuration of the two ZU5 and the UPA domains CC forms a structural supramodule termed ZZU. ZU5-1 mediates interaction CC with beta-spectrin, and the ZU5-1/UPA interface is required for CC ankyrin's function other than binding to spectrin (By similarity). CC {ECO:0000250}. CC -!- DOMAIN: The ANK repeat region forms a spiral around a large central CC cavity and is involved in binding of ion transporters. Adopts a T- CC shaped arrangement, in the ankyrin-1 complex, in which ANK 1-5 repeats CC are orthogonal to ANK 6-24 repeats, with the peptide binding groove of CC ANK 1-5 repeats oriented toward the membrane. The rearrangement of the CC ANK 1-5 repeats orients the canonical protein binding groove to CC directly face the membrane, to interact the membrane-embedded targets CC RHCE and AQP1. {ECO:0000250|UniProtKB:P16157}. CC -!- PTM: Regulated by phosphorylation. {ECO:0000250}. CC -!- PTM: Acylated by palmitic acid group(s). {ECO:0000250}. CC -!- PTM: Hydroxylated by HIF1AN at several asparagine and 1 aspartate CC residue within ANK repeat region; hydroxylation seems to increase the CC conformational stability of this region and may also modulate protein- CC protein interactions mediated by the ANK repeat region. {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform Er1]: Produced by alternative promoter usage. CC -!- MISCELLANEOUS: [Isoform Br2]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er3]: Incomplete sequence. Produced by CC alternative splicing of isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Br4]: Incomplete sequence. Produced by CC alternative splicing of isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform CC Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative splicing of isoform CC Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Mu7]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Mu8]: Produced by alternative splicing of CC isoform Mu7. {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; M84756; AAA37236.1; -; mRNA. DR EMBL; X69063; CAA48801.1; -; mRNA. DR EMBL; X69064; CAA48802.1; -; mRNA. DR EMBL; U73972; AAC24156.1; -; mRNA. DR EMBL; AK134267; BAE22074.1; -; mRNA. DR EMBL; AK147278; BAE27815.1; -; mRNA. DR EMBL; AK147597; BAE28015.1; -; mRNA. DR EMBL; AK158131; BAE34375.1; -; mRNA. DR EMBL; BC061219; AAH61219.1; -; mRNA. DR EMBL; U76758; AAB37323.1; -; Genomic_DNA. DR EMBL; U76758; AAB37324.1; -; Genomic_DNA. DR EMBL; U76758; AAB37325.1; -; Genomic_DNA. DR CCDS; CCDS22187.1; -. [Q02357-2] DR CCDS; CCDS52523.1; -. [Q02357-6] DR CCDS; CCDS72099.1; -. [Q02357-5] DR CCDS; CCDS72100.1; -. [Q02357-1] DR CCDS; CCDS72101.1; -. [Q02357-4] DR CCDS; CCDS80864.1; -. [Q02357-7] DR CCDS; CCDS80865.1; -. [Q02357-8] DR PIR; I49502; I49502. DR PIR; S37771; S37771. DR PIR; S37772; S37772. DR RefSeq; NP_001104253.1; NM_001110783.3. DR RefSeq; NP_001264209.1; NM_001277280.2. [Q02357-5] DR RefSeq; NP_001264210.1; NM_001277281.2. DR RefSeq; NP_001264215.1; NM_001277286.2. DR RefSeq; NP_001264218.1; NM_001277289.2. DR RefSeq; NP_001297365.1; NM_001310436.1. [Q02357-8] DR RefSeq; NP_001297366.1; NM_001310437.1. [Q02357-7] DR RefSeq; NP_112435.2; NM_031158.4. DR AlphaFoldDB; Q02357; -. DR SMR; Q02357; -. DR BioGRID; 198101; 1. DR IntAct; Q02357; 3. DR MINT; Q02357; -. DR STRING; 10090.ENSMUSP00000113571; -. DR iPTMnet; Q02357; -. DR PhosphoSitePlus; Q02357; -. DR SwissPalm; Q02357; -. DR jPOST; Q02357; -. DR MaxQB; Q02357; -. DR PaxDb; 10090-ENSMUSP00000113571; -. DR PeptideAtlas; Q02357; -. DR ProteomicsDB; 296294; -. [Q02357-1] DR ProteomicsDB; 296295; -. [Q02357-2] DR ProteomicsDB; 296296; -. [Q02357-3] DR ProteomicsDB; 296297; -. [Q02357-4] DR ProteomicsDB; 296298; -. [Q02357-5] DR ProteomicsDB; 296299; -. [Q02357-6] DR ProteomicsDB; 296300; -. [Q02357-7] DR ProteomicsDB; 296301; -. [Q02357-8] DR ABCD; Q02357; 3 sequenced antibodies. DR Antibodypedia; 4229; 496 antibodies from 34 providers. DR DNASU; 11733; -. DR Ensembl; ENSMUST00000033947.15; ENSMUSP00000033947.9; ENSMUSG00000031543.19. [Q02357-8] DR Ensembl; ENSMUST00000110688.9; ENSMUSP00000106316.3; ENSMUSG00000031543.19. [Q02357-5] DR Ensembl; ENSMUST00000121075.8; ENSMUSP00000112966.2; ENSMUSG00000031543.19. [Q02357-7] DR GeneID; 11733; -. DR KEGG; mmu:11733; -. DR UCSC; uc009lee.3; mouse. [Q02357-6] DR UCSC; uc009lef.3; mouse. [Q02357-5] DR UCSC; uc009lel.2; mouse. [Q02357-7] DR UCSC; uc009lem.2; mouse. [Q02357-8] DR AGR; MGI:88024; -. DR CTD; 286; -. DR MGI; MGI:88024; Ank1. DR VEuPathDB; HostDB:ENSMUSG00000031543; -. DR eggNOG; KOG4177; Eukaryota. DR GeneTree; ENSGT00940000155760; -. DR HOGENOM; CLU_000134_7_3_1; -. DR InParanoid; Q02357; -. DR OrthoDB; 5474900at2759; -. DR TreeFam; TF351263; -. DR Reactome; R-MMU-445095; Interaction between L1 and Ankyrins. DR Reactome; R-MMU-447043; Neurofascin interactions. DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport. DR BioGRID-ORCS; 11733; 2 hits in 79 CRISPR screens. DR ChiTaRS; Ank1; mouse. DR PRO; PR:Q02357; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; Q02357; Protein. DR Bgee; ENSMUSG00000031543; Expressed in fetal liver hematopoietic progenitor cell and 183 other cell types or tissues. DR ExpressionAtlas; Q02357; baseline and differential. DR GO; GO:0031672; C:A band; ISO:MGI. DR GO; GO:0170014; C:ankyrin-1 complex; ISS:UniProtKB. DR GO; GO:0030673; C:axolemma; ISO:MGI. DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI. DR GO; GO:0031430; C:M band; ISO:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI. DR GO; GO:0042383; C:sarcolemma; ISO:MGI. DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI. DR GO; GO:0014731; C:spectrin-associated cytoskeleton; IMP:MGI. DR GO; GO:0030018; C:Z disc; ISO:MGI. DR GO; GO:0051117; F:ATPase binding; ISO:MGI. DR GO; GO:0008093; F:cytoskeletal anchor activity; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI. DR GO; GO:0030507; F:spectrin binding; ISO:MGI. DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI. DR GO; GO:0048821; P:erythrocyte development; IMP:MGI. DR GO; GO:0098662; P:inorganic cation transmembrane transport; IMP:MGI. DR GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IMP:MGI. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:MGI. DR GO; GO:0010638; P:positive regulation of organelle organization; ISO:MGI. DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd08805; Death_ank1; 1. DR Gene3D; 2.60.220.30; -; 2. DR Gene3D; 2.60.40.2660; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. 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 PANTHER; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24198:SF173; ANKYRIN-3; 1. DR Pfam; PF00023; Ank; 2. DR Pfam; PF12796; Ank_2; 7. DR Pfam; PF13637; Ank_4; 2. DR Pfam; PF00531; Death; 1. DR Pfam; PF17809; UPA_2; 1. DR Pfam; PF00791; ZU5; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 23. DR SMART; SM00005; DEATH; 1. DR SMART; SM00218; ZU5; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 2. DR SUPFAM; SSF47986; DEATH domain; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 20. DR PROSITE; PS50017; DEATH_DOMAIN; 1. DR PROSITE; PS51145; ZU5; 2. DR Genevisible; Q02357; MM. PE 1: Evidence at protein level; KW Alternative promoter usage; Alternative splicing; ANK repeat; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Hydroxylation; Lipoprotein; KW Membrane; Phosphoprotein; Reference proteome; Repeat; KW Sarcoplasmic reticulum. FT CHAIN 1..1862 FT /note="Ankyrin-1" FT /id="PRO_0000066884" FT REPEAT 40..69 FT /note="ANK 1" FT REPEAT 73..102 FT /note="ANK 2" FT REPEAT 106..135 FT /note="ANK 3" FT REPEAT 139..168 FT /note="ANK 4" FT REPEAT 170..197 FT /note="ANK 5" FT REPEAT 201..230 FT /note="ANK 6" FT REPEAT 234..263 FT /note="ANK 7" FT REPEAT 267..296 FT /note="ANK 8" FT REPEAT 300..329 FT /note="ANK 9" FT REPEAT 333..362 FT /note="ANK 10" FT REPEAT 366..395 FT /note="ANK 11" FT REPEAT 399..428 FT /note="ANK 12" FT REPEAT 432..461 FT /note="ANK 13" FT REPEAT 465..494 FT /note="ANK 14" FT REPEAT 498..527 FT /note="ANK 15" FT REPEAT 531..560 FT /note="ANK 16" FT REPEAT 564..593 FT /note="ANK 17" FT REPEAT 597..626 FT /note="ANK 18" FT REPEAT 630..659 FT /note="ANK 19" FT REPEAT 663..692 FT /note="ANK 20" FT REPEAT 696..725 FT /note="ANK 21" FT REPEAT 729..758 FT /note="ANK 22" FT REPEAT 762..791 FT /note="ANK 23" FT DOMAIN 909..1064 FT /note="ZU5 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485" FT DOMAIN 1066..1212 FT /note="ZU5 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485" FT DOMAIN 1399..1483 FT /note="Death" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064" FT REGION 1..827 FT /note="89 kDa domain" FT REGION 812..834 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 872..900 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1197..1331 FT /note="UPA domain" FT /evidence="ECO:0000250" FT REGION 1387..1862 FT /note="55 kDa regulatory domain" FT REGION 1481..1506 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1598..1720 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1744..1767 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 817..834 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1486..1500 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1636..1652 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1653..1684 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1699..1720 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 101 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial" FT /evidence="ECO:0000269|PubMed:21177872" FT MOD_RES 229 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN" FT /evidence="ECO:0000250" FT MOD_RES 425 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16157" FT MOD_RES 427 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN" FT /evidence="ECO:0000250" FT MOD_RES 460 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN" FT /evidence="ECO:0000250" FT MOD_RES 625 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN" FT /evidence="ECO:0000250" FT MOD_RES 658 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN" FT /evidence="ECO:0000250" FT MOD_RES 691 FT /note="(3S)-3-hydroxyaspartate; by HIF1AN" FT /evidence="ECO:0000250" FT MOD_RES 724 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN" FT /evidence="ECO:0000250" FT MOD_RES 755 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16157" FT MOD_RES 757 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN" FT /evidence="ECO:0000250" FT MOD_RES 777 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 813 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 830 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16157" FT MOD_RES 852 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 862 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 957 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1069 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455" FT MOD_RES 1078 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1374 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P16157" FT MOD_RES 1376 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P16157" FT MOD_RES 1386 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1388 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1396 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1424 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 1482 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1519 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16157" FT MOD_RES 1529 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16157" FT MOD_RES 1612 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1660 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16157" FT MOD_RES 1675 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16157" FT MOD_RES 1685 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16157" FT VAR_SEQ 1..1707 FT /note="Missing (in isoform Mu7 and isoform Mu8)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9628825" FT /id="VSP_018452" FT VAR_SEQ 1..5 FT /note="MGFCK -> MAERPRRSGSDPA (in isoform Br2)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:8486643" FT /id="VSP_018453" FT VAR_SEQ 1..4 FT /note="MGFC -> MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKK FT (in isoform 5 and isoform 6)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_018454" FT VAR_SEQ 817 FT /note="G -> GTAHISIMG (in isoform Br2 and isoform 6)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:8486643" FT /id="VSP_018455" FT VAR_SEQ 1510..1664 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_018456" FT VAR_SEQ 1636..1665 FT /note="Missing (in isoform Br2)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:8486643" FT /id="VSP_018457" FT VAR_SEQ 1708..1780 FT /note="SSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTREHVQRGPPETGS FT PKAGKEPSLWAPESAFSQEVQ -> MWTFITQLLVTLVLLGFFLVSCQNVMHIVKGSLC FT FVLKHIHQELDKELGESEGLSDDEETISTRVVRRRVFLK (in isoform Mu7 and FT isoform Mu8)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9628825" FT /id="VSP_018458" FT VAR_SEQ 1831 FT /note="V -> VIVEGPLADPGDLEADIESFMKLTKV (in isoform Br4)" FT /evidence="ECO:0000303|PubMed:8486643" FT /id="VSP_018459" FT VAR_SEQ 1832..1862 FT /note="ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ -> IVEGPLADPGDLEADIE FT SFMKLTKDHTSTPKP (in isoform Er3 and isoform Mu8)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:8486643" FT /id="VSP_018460" FT CONFLICT 507 FT /note="A -> T (in Ref. 3; BAE34375)" FT /evidence="ECO:0000305" FT CONFLICT 678 FT /note="P -> L (in Ref. 1; AAA37236)" FT /evidence="ECO:0000305" FT CONFLICT 818 FT /note="D -> G (in Ref. 3; BAE34375)" FT /evidence="ECO:0000305" FT CONFLICT 1098 FT /note="K -> N (in Ref. 2; CAA48801)" FT /evidence="ECO:0000305" FT CONFLICT 1481 FT /note="G -> V (in Ref. 2; CAA48801)" FT /evidence="ECO:0000305" FT CONFLICT 1541 FT /note="T -> A (in Ref. 3; BAE27815/BAE28015)" FT /evidence="ECO:0000305" FT CONFLICT 1644 FT /note="K -> R (in Ref. 3; BAE28015)" FT /evidence="ECO:0000305" FT MOD_RES Q02357-7:55 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES Q02357-8:55 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" SQ SEQUENCE 1862 AA; 204227 MW; B5F3EBB447C3485D CRC64; MGFCKADAAT SFLRAARSGN LDKALDHLRN GVDINTCNQN GLNGLHLASK EGHVKMVVEL LHKEIILETT TKKGNTALHI AALAGQDEVV RELVNYGANV NAQSQKGFTP LYMAAQENHL EVVKFLLENG ANQNVATEDG FTPLAVALQQ GHENVVAHLI NYGTKGKVRL PALHIAARND DTRTAAVLLQ NDPNPDVLSK TGFTPLHIAA HYENLNVAQL LLNRGASVNF TPQNGITPLH IASRRGNVIM VRLLLDRGAQ IETRTKDELT PLHCAARNGH VRISEILLDH GAPIQAKTKN GLSPIHMAAQ GDHLDCVRLL LQYNAEIDDI TLDHLTPLHV AAHCGHHRVA KVLLDKGAKP NSRALNGFTP LHIACKKNHI RVMELLLKTG ASIDAVTESG LTPLHVASFM GHLPIVKNLL QRGASPNVSN VKVETPLHMA ARAGHTEVAK YLLQNKAKAN AKAKDDQTPL HCAARIGHTG MVKLLLENGA SPNLATTAGH TPLHTAAREG HVDTALALLE KEASQACMTK KGFTPLHVAA KYGKVRLAEL LLEHDAHPNA AGKNGLTPLH VAVHHNNLDI VKLLLPRGGS PHSPAWNGYT PLHIAAKQNQ IEVARSLLQY GGSANAESVQ GVTPLHLAAQ EGHTEMVALL LSKQANGNLG NKSGLTPLHL VSQEGHVPVA DVLIKHGVTV DATTRMGYTP LHVASHYGNI KLVKFLLQHQ ADVNAKTKLG YSPLHQAAQQ GHTDIVTLLL KNGASPNEVS SNGTTPLAIA KRLGYISVTD VLKVVTDETS VVLVSDKHRM SYPETVDEIL DVSEDEGDEL VGSKAERRDS RDVGEEKELL DFVPKLDQVV ESPAIPRIPC VTPETVVIRS EDQEQASKEY DEDSLIPSSP ATETSDNISP VASPVHTGFL VSFMVDARGG SMRGSRHNGL RVVIPPRTCA APTRITCRLV KPQKLNTPPP LAEEEGLASR IIALGPTGAQ FLSPVIVEIP HFASHGRGDR ELVVLRSENG SVWKEHKSRY GESYLDQILN GMDEELGSLE ELEKKRVCRI ITTDFPLYFV IMSRLCQDYD TIGPEGGSLR SKLVPLVQAT FPENAVTKKV KLALQAQPVP DELVTKLLGN QATFSPIVTV EPRRRKFHRP IGLRIPLPPS WTDNPRDSGE GDTTSLRLLC SVIGGTDQAQ WEDITGTTKL IYANECANFT TNVSARFWLS DCPRTAEAVH FATLLYKELT AVPYMAKFVI FAKMNDAREG RLRCYCMTDD KVDKTLEQHE NFVEVARSRD IEVLEGMPLF AELSGNLVPV KKAAQQRSFH FQSFRENRLA IPVKVRDSSR EPGGFLSFLR KTMKYEDTQH ILCHLNITMP PCTKGSGAED RRRTLTPLTL RYSILSESRL GFTSDTDRVE MRMAVIREHL GLSWAELARE LQFSVEDINR IRVENPNSLL DQSTALLTLW VDREGENAKM ENLYTALRNI DRSEIVNMLE GSGRQSRNLK PERRHGDREY SLSPSQVNGY SSLQDELLSP ASLQYALPSP LCADQYWNEV TVIDAIPLAA TEHDTMLEMS DMQVWSAGLT PSLVTAEDSS LECSKAEDSD AIPEWKLEGA HSEDTQGPEL GSQDLVEDDT VDSDATNGLA DLLGQEEGQR SEKKRQEVSG TEQDTETEVS LVSGQQRVHA RITDSPSVRQ VLDRSQARTL DWDKQGSTAV HPQEATQSSW QEEVTQGPHS FQRRITTIQG PEPGALQEYE QVLVSTREHV QRGPPETGSP KAGKEPSLWA PESAFSQEVQ GDELQNIPGE QVTEEQFTDE QGNIVTKKII RKVVRQVDSS GAIDTQQHEE VELRGSGLQP DLIEGRKGAQ IVKRASLKRG KQ //