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, 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).
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}.
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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 Genevisible; Q02357; MM.
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.
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
//
