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Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Helicase with 2 CARD domains) (Helicard) (Interferon induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (RIG-I-like receptor 2) (RLR-2)

 IFIH1_MOUSE             Reviewed;        1025 AA.
Q8R5F7; A2AUY7; Q3U6S2; Q68EM4; Q8BYC9; Q8BZ01; Q8K5C7; Q8R144;
Q8VE79; Q99KS4; Q9D2Z5;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
22-NOV-2017, entry version 139.
RecName: Full=Interferon-induced helicase C domain-containing protein 1;
EC=3.6.4.13;
AltName: Full=Helicase with 2 CARD domains;
Short=Helicard;
AltName: Full=Interferon induced with helicase C domain protein 1;
AltName: Full=Melanoma differentiation-associated protein 5;
Short=MDA-5;
AltName: Full=RIG-I-like receptor 2;
Short=RLR-2;
Name=Ifih1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CLEAVAGE SITES,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12015121; DOI=10.1016/S0960-9822(02)00842-4;
Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K.,
Tschopp J.;
"Overexpression of Helicard, a CARD-containing helicase cleaved during
apoptosis, accelerates DNA degradation.";
Curr. Biol. 12:838-843(2002).
[2]
ERRATUM.
Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K.,
Tschopp J.;
Curr. Biol. 12:1633-1633(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11805321; DOI=10.1073/pnas.022637199;
Kang D.-C., Gopalkrishnan R.V., Wu Q., Jankowsky E., Pyle A.M.,
Fisher P.B.;
"mda-5: an interferon-inducible putative RNA helicase with double-
stranded RNA-dependent ATPase activity and melanoma growth-suppressive
properties.";
Proc. Natl. Acad. Sci. U.S.A. 99:637-642(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Bone marrow, Cecum, Thymus, and Vagina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION.
PubMed=16625202; DOI=10.1038/nature04734;
Kato H., Takeuchi O., Sato S., Yoneyama M., Yamamoto M., Matsui K.,
Uematsu S., Jung A., Kawai T., Ishii K.J., Yamaguchi O., Otsu K.,
Tsujimura T., Koh C.S., Reis e Sousa C., Matsuura Y., Fujita T.,
Akira S.;
"Differential roles of MDA5 and RIG-I helicases in the recognition of
RNA viruses.";
Nature 441:101-105(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-648, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
FUNCTION.
PubMed=17942531; DOI=10.1128/JVI.01080-07;
Loo Y.M., Fornek J., Crochet N., Bajwa G., Perwitasari O.,
Martinez-Sobrido L., Akira S., Gill M.A., Garcia-Sastre A.,
Katze M.G., Gale M. Jr.;
"Distinct RIG-I and MDA5 signaling by RNA viruses in innate
immunity.";
J. Virol. 82:335-345(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[11]
FUNCTION.
PubMed=19656871; DOI=10.1128/JVI.00770-09;
Pichlmair A., Schulz O., Tan C.P., Rehwinkel J., Kato H., Takeuchi O.,
Akira S., Way M., Schiavo G., Reis e Sousa C.;
"Activation of MDA5 requires higher-order RNA structures generated
during virus infection.";
J. Virol. 83:10761-10769(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-291; SER-302;
SER-645 AND SER-648, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
REVIEW ON FUNCTION.
PubMed=21616437; DOI=10.1016/j.immuni.2011.05.003;
Loo Y.M., Gale M. Jr.;
"Immune signaling by RIG-I-like receptors.";
Immunity 34:680-692(2011).
[14]
REVIEW ON FUNCTION.
PubMed=21884169; DOI=10.1111/j.1600-065X.2011.01052.x;
Kato H., Takahasi K., Fujita T.;
"RIG-I-like receptors: cytoplasmic sensors for non-self RNA.";
Immunol. Rev. 243:91-98(2011).
[15]
REVIEW ON FUNCTION.
PubMed=20950133; DOI=10.1089/jir.2010.0057;
Onoguchi K., Yoneyama M., Fujita T.;
"Retinoic acid-inducible gene-I-like receptors.";
J. Interferon Cytokine Res. 31:27-31(2011).
[16]
REVIEW ON FUNCTION.
PubMed=21245900; DOI=10.1038/ni0211-114;
Garcia-Sastre A.;
"2 methylate or not 2 methylate: viral evasion of the type I
interferon response.";
Nat. Immunol. 12:114-115(2011).
[17]
FUNCTION.
PubMed=21217758; DOI=10.1038/ni.1979;
Zuest R., Cervantes-Barragan L., Habjan M., Maier R., Neuman B.W.,
Ziebuhr J., Szretter K.J., Baker S.C., Barchet W., Diamond M.S.,
Siddell S.G., Ludewig B., Thiel V.;
"Ribose 2'-O-methylation provides a molecular signature for the
distinction of self and non-self mRNA dependent on the RNA sensor
Mda5.";
Nat. Immunol. 12:137-143(2011).
[18]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 545-697, AND SUBUNIT.
PubMed=22314235; DOI=10.1038/emboj.2012.19;
Berke I.C., Modis Y.;
"MDA5 cooperatively forms dimers and ATP-sensitive filaments upon
binding double-stranded RNA.";
EMBO J. 31:1714-1726(2012).
-!- FUNCTION: Innate immune receptor which acts as a cytoplasmic
sensor of viral nucleic acids and plays a major role in sensing
viral infection and in the activation of a cascade of antiviral
responses including the induction of type I interferons and
proinflammatory cytokines. Its ligands include mRNA lacking 2'-O-
methylation at their 5' cap and long-dsRNA (>1 kb in length). Upon
ligand binding it associates with mitochondria antiviral signaling
protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1
and IKBKE which phosphorylate interferon regulatory factors: IRF3
and IRF7 which in turn activate transcription of antiviral
immunological genes, including interferons (IFNs); IFN-alpha and
IFN-beta. Responsible for detecting the Picornaviridae family
members such as encephalomyocarditis virus (EMCV), mengo
encephalomyocarditis virus (ENMG), and theiler's murine
encephalomyelitis virus (TMEV). Can also detect other viruses such
as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also
involved in antiviral signaling in response to viruses containing
a dsDNA genome, such as vaccinia virus. Plays an important role in
amplifying innate immune signaling through recognition of RNA
metabolites that are produced during virus infection by
ribonuclease L (RNase L). May play an important role in enhancing
natural killer cell function and may be involved in growth
inhibition and apoptosis in several tumor cell lines.
{ECO:0000269|PubMed:12015121, ECO:0000269|PubMed:16625202,
ECO:0000269|PubMed:17942531, ECO:0000269|PubMed:19656871,
ECO:0000269|PubMed:21217758}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Monomer in the absence of ligands and homodimerizes in
the presence of dsRNA ligands. Can assemble into helical or linear
polymeric filaments on long dsRNA. Interacts with MAVS/IPS1.
Interacts with V protein of Sendai virus. Binding to
paramyxoviruses V proteins prevents IFN-beta induction, and the
further establishment of an antiviral state. Interacts with PCBP2.
Interacts with NLRC5. Interacts with PIAS2-beta. Interacts with
DDX60. Interacts with ANKRD17. Interacts with IKBKE. Interacts
(via the CARD domains) with TKFC, the interaction is inhibited by
viral infection (By similarity). {ECO:0000250|UniProtKB:Q9BYX4}.
-!- INTERACTION:
P11207:P/V (xeno); NbExp=3; IntAct=EBI-16019291, EBI-6148694;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12015121}.
Nucleus {ECO:0000305}. Note=May be found in the nucleus, during
apoptosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8R5F7-1; Sequence=Displayed;
Name=2;
IsoId=Q8R5F7-2; Sequence=VSP_013339;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expression is prominent in lung, liver,
kidney, heart and spleen (at protein level). Widely expressed at
low level. {ECO:0000269|PubMed:12015121}.
-!- INDUCTION: By interferon (IFN).
-!- PTM: During apoptosis, processed into 3 cleavage products. The
helicase-containing fragment, once liberated from the CARD
domains, translocate from the cytoplasm to the nucleus. The
processed protein significantly sensitizes cells to DNA
degradation. {ECO:0000269|PubMed:12015121}.
-!- PTM: Sumoylated. Sumoylation positively regulates its role in type
I interferon induction and is enhanced by PIAS2-beta.
{ECO:0000250|UniProtKB:Q9BYX4}.
-!- PTM: Ubiquitinated by RNF125, leading to its degradation by the
proteasome. USP17/UPS17L2-dependent deubiquitination positively
regulates the receptor. {ECO:0000250|UniProtKB:Q9BYX4}.
-!- SIMILARITY: Belongs to the helicase family. RLR subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH25508.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY075132; AAL77205.1; -; mRNA.
EMBL; AF374384; AAM21359.1; -; mRNA.
EMBL; AK018602; BAB31303.2; -; mRNA.
EMBL; AK037057; BAC29687.2; -; mRNA.
EMBL; AK040519; BAC30614.1; -; mRNA.
EMBL; AK153018; BAE31652.1; -; mRNA.
EMBL; AL929246; CAM21790.1; -; Genomic_DNA.
EMBL; BC004031; AAH04031.1; -; mRNA.
EMBL; BC019605; AAH19605.1; -; mRNA.
EMBL; BC025508; AAH25508.1; ALT_INIT; mRNA.
EMBL; BC080200; AAH80200.1; -; mRNA.
CCDS; CCDS16068.1; -. [Q8R5F7-1]
CCDS; CCDS50594.1; -. [Q8R5F7-2]
RefSeq; NP_001157949.1; NM_001164477.1. [Q8R5F7-2]
RefSeq; NP_082111.2; NM_027835.3. [Q8R5F7-1]
UniGene; Mm.136224; -.
PDB; 3TS9; X-ray; 2.00 A; A=545-697.
PDBsum; 3TS9; -.
ProteinModelPortal; Q8R5F7; -.
SMR; Q8R5F7; -.
BioGrid; 214799; 2.
DIP; DIP-60085N; -.
IntAct; Q8R5F7; 2.
MINT; MINT-4118007; -.
STRING; 10090.ENSMUSP00000028259; -.
iPTMnet; Q8R5F7; -.
PhosphoSitePlus; Q8R5F7; -.
PaxDb; Q8R5F7; -.
PeptideAtlas; Q8R5F7; -.
PRIDE; Q8R5F7; -.
Ensembl; ENSMUST00000028259; ENSMUSP00000028259; ENSMUSG00000026896. [Q8R5F7-1]
Ensembl; ENSMUST00000112459; ENSMUSP00000108078; ENSMUSG00000026896. [Q8R5F7-2]
GeneID; 71586; -.
KEGG; mmu:71586; -.
UCSC; uc008jvm.2; mouse. [Q8R5F7-1]
UCSC; uc012bvy.1; mouse. [Q8R5F7-2]
CTD; 64135; -.
MGI; MGI:1918836; Ifih1.
eggNOG; KOG0354; Eukaryota.
eggNOG; COG1111; LUCA.
GeneTree; ENSGT00510000046789; -.
HOVERGEN; HBG106019; -.
InParanoid; Q8R5F7; -.
KO; K12647; -.
OMA; YNNIMRR; -.
OrthoDB; EOG091G01PQ; -.
PhylomeDB; Q8R5F7; -.
TreeFam; TF330258; -.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
PRO; PR:Q8R5F7; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026896; -.
CleanEx; MM_IFIH1; -.
ExpressionAtlas; Q8R5F7; baseline and differential.
Genevisible; Q8R5F7; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0039530; P:MDA-5 signaling pathway; ISS:UniProtKB.
GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; ISS:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
GO; GO:0035549; P:positive regulation of interferon-beta secretion; ISS:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISS:UniProtKB.
GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
GO; GO:0009615; P:response to virus; IMP:UniProtKB.
CDD; cd00079; HELICc; 1.
InterPro; IPR031964; CARD_dom.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR006935; Helicase/UvrB_N.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR021673; RLR_CTR.
Pfam; PF16739; CARD_2; 2.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF04851; ResIII; 1.
Pfam; PF11648; RIG-I_C-RD; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51789; RLR_CTR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiviral defense; ATP-binding;
Complete proteome; Cytoplasm; Helicase; Hydrolase; Immunity;
Innate immunity; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; RNA-binding;
Ubl conjugation; Zinc.
CHAIN 1 1025 Interferon-induced helicase C domain-
containing protein 1.
/FTId=PRO_0000102013.
DOMAIN 7 97 CARD 1.
DOMAIN 110 190 CARD 2.
DOMAIN 317 510 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 700 872 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 893 1020 RLR CTR. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 907 907 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 910 910 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 962 962 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 964 964 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
SITE 208 209 Cleavage.
SITE 216 217 Cleavage.
SITE 251 252 Cleavage.
MOD_RES 289 289 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 645 645 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 648 648 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 828 828 Phosphoserine; by RIOK3.
{ECO:0000250|UniProtKB:Q9BYX4}.
VAR_SEQ 207 255 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013339.
CONFLICT 100 100 T -> I (in Ref. 6; AAH80200).
{ECO:0000305}.
CONFLICT 339 339 V -> E (in Ref. 4; BAE31652).
{ECO:0000305}.
CONFLICT 412 414 IST -> TRP (in Ref. 6; AAH25508).
{ECO:0000305}.
CONFLICT 624 624 Y -> H (in Ref. 6; AAH25508).
{ECO:0000305}.
CONFLICT 629 629 T -> A (in Ref. 3; AAM21359).
{ECO:0000305}.
CONFLICT 647 647 K -> E (in Ref. 6; AAH25508/AAH04031/
AAH80200). {ECO:0000305}.
CONFLICT 889 889 K -> E (in Ref. 4; BAB31303).
{ECO:0000305}.
HELIX 550 565 {ECO:0000244|PDB:3TS9}.
HELIX 577 593 {ECO:0000244|PDB:3TS9}.
HELIX 596 617 {ECO:0000244|PDB:3TS9}.
HELIX 620 640 {ECO:0000244|PDB:3TS9}.
HELIX 671 691 {ECO:0000244|PDB:3TS9}.
HELIX 694 696 {ECO:0000244|PDB:3TS9}.
SEQUENCE 1025 AA; 115971 MW; 708FCAC690C9F6D8 CRC64;
MSIVCSAEDS FRNLILFFRP RLKMYIQVEP VLDHLIFLSA ETKEQILKKI NTCGNTSAAE
LLLSTLEQGQ WPLGWTQMFV EALEHSGNPL AARYVKPTLT DLPSPSSETA HDECLHLLTL
LQPTLVDKLL INDVLDTCFE KGLLTVEDRN RISAAGNSGN ESGVRELLRR IVQKENWFST
FLDVLRQTGN DALFQELTGG GCPEDNTDLA NSSHRDGPAA NECLLPAVDE SSLETEAWNV
DDILPEASCT DSSVTTESDT SLAEGSVSCF DESLGHNSNM GRDSGTMGSD SDESVIQTKR
VSPEPELQLR PYQMEVAQPA LDGKNIIICL PTGSGKTRVA VYITKDHLDK KKQASESGKV
IVLVNKVMLA EQLFRKEFNP YLKKWYRIIG LSGDTQLKIS FPEVVKSYDV IISTAQILEN
SLLNLESGDD DGVQLSDFSL IIIDECHHTN KEAVYNNIMR RYLKQKLRNN DLKKQNKPAI
PLPQILGLTA SPGVGAAKKQ SEAEKHILNI CANLDAFTIK TVKENLGQLK HQIKEPCKKF
VIADDTRENP FKEKLLEIMA SIQTYCQKSP MSDFGTQHYE QWAIQMEKKA AKDGNRKDRV
CAEHLRKYNE ALQINDTIRM IDAYSHLETF YTDEKEKKFA VLNDSDKSDD EASSCNDQLK
GDVKKSLKLD ETDEFLMNLF FDNKKMLKKL AENPKYENEK LIKLRNTILE QFTRSEESSR
GIIFTKTRQS TYALSQWIME NAKFAEVGVK AHHLIGAGHS SEVKPMTQTE QKEVISKFRT
GEINLLIATT VAEEGLDIKE CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVTSSGSGV
TEREIVNDFR EKMMYKAINR VQNMKPEEYA HKILELQVQS ILEKKMKVKR SIAKQYNDNP
SLITLLCKNC SMLVCSGENI HVIEKMHHVN MTPEFKGLYI VRENKALQKK FADYQTNGEI
ICKCGQAWGT MMVHKGLDLP CLKIRNFVVN FKNNSPKKQY KKWVELPIRF PDLDYSEYCL
YSDED


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