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Influenza virus NS1A-binding protein homolog (NS1-BP) (NS1-binding protein homolog) (Kelch family protein Nd1-L) (ND1-L2) (Nd1-S)

 NS1BP_MOUSE             Reviewed;         642 AA.
Q920Q8; Q06BK6; Q3TXI1; Q3UJE3; Q3UJS1; Q3UKH9; Q3UMK9; Q6ZQ34;
Q99KN0; Q9D978;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
25-OCT-2017, entry version 115.
RecName: Full=Influenza virus NS1A-binding protein homolog;
Short=NS1-BP;
Short=NS1-binding protein homolog;
AltName: Full=Kelch family protein Nd1-L;
AltName: Full=ND1-L2;
AltName: Full=Nd1-S;
Name=Ivns1abp; Synonyms=Kiaa0850, Nd1, Nd1L, Nd1S, Ns1, Ns1bp;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12213805; DOI=10.1074/jbc.M202596200;
Sasagawa K., Matsudo Y., Kang M., Fujimura L., Iitsuka Y., Okada S.,
Ochiai T., Tokuhisa T., Hatano M.;
"Identification of Nd1, a novel murine kelch family protein, involved
in stabilization of actin filaments.";
J. Biol. Chem. 277:44140-44146(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=KM;
Wang J., Xiao X.;
"Identification of novel variants of gene Nd1 in mouse.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
STRAIN=BALB/cJ, and C57BL/6J;
TISSUE=Amnion, Kidney, Lung, Mammary gland, Placenta, and Testis;
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 MRNA] (ISOFORMS 1 AND 2).
STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
[6]
FUNCTION.
PubMed=11418182; DOI=10.1016/S0167-4781(01)00231-7;
Kang M., Matsudo Y., Sasagawa K., Tokuhisa T., Hatano M.;
"Nd1, a novel murine Kelch family protein, may play the role of a
housekeeping gene.";
Biochim. Biophys. Acta 1519:167-174(2001).
[7]
DISRUPTION PHENOTYPE.
PubMed=15485691; DOI=10.1016/j.cardiores.2004.07.009;
Fujimura L., Matsudo Y., Kang M., Takamori Y., Tokuhisa T., Hatano M.;
"Protective role of Nd1 in doxorubicin-induced cardiotoxicity.";
Cardiovasc. Res. 64:315-321(2004).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15684717; DOI=10.1089/dna.2005.24.30;
Inoue A., Kang M., Fujimura L., Takamori Y., Sasagawa K., Itoh H.,
Tokuhisa T., Hatano M.;
"Overexpression of Nd1-s, a variant form of new kelch family protein,
perturbs the cell cycle progression of fibroblasts.";
DNA Cell Biol. 24:30-34(2005).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16317045; DOI=10.1242/jcs.02692;
Fujii R., Takumi T.;
"TLS facilitates transport of mRNA encoding an actin-stabilizing
protein to dendritic spines.";
J. Cell Sci. 118:5755-5765(2005).
[10]
INDUCTION.
PubMed=17016628;
Takamori Y., Matsudo Y., Fujimura L., Kang M., Harada Y., Moriya H.,
Tokuhisa T., Hatano M.;
"Expression of the Nd1 gene is down-regulated by doxorubicin at post-
transcriptional level.";
Int. J. Mol. Med. 18:963-967(2006).
[11]
TRANSGENIC MICE, FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
PubMed=16952015; DOI=10.1007/s11248-006-9010-x;
Matsudo Y., Takamori Y., Fujimura L., Nishio S., Sasagawa K.,
Komuro I., Tokuhisa T., Hatano M.;
"Overexpression of Nd1, a novel Kelch family protein, in the heart of
transgenic mice protects against doxorubicin-induced cardiomyopathy.";
Transgenic Res. 15:573-581(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246 AND SER-322, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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).
-!- FUNCTION: Plays a role in cell division and in the dynamic
organization of the actin skeleton as a stabilizer of actin
filaments by association with F-actin through Kelch repeats.
Protects cells from cell death induced by actin destabilization;
Protects neurons from dendritic spines and actin filaments damage
induced by the actin-destabilizing cytochalasin B when
overexpressed. Plays a role in protecting the heart from
doxorubicin-induced cardiomyopathy. Activates Erk signaling
pathway when overexpressed in cultured cell lines.
{ECO:0000269|PubMed:11418182, ECO:0000269|PubMed:12213805,
ECO:0000269|PubMed:15684717, ECO:0000269|PubMed:16317045,
ECO:0000269|PubMed:16952015}.
-!- SUBUNIT: Homodimer; through the BTB domain. Interacts with
AHR/Aryl hydrocarbon receptor (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cytoplasm,
cytoskeleton. Note=Associated with actin filaments.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Nd1-L;
IsoId=Q920Q8-1; Sequence=Displayed;
Name=2; Synonyms=Nd1-S;
IsoId=Q920Q8-2; Sequence=VSP_024812, VSP_024813;
Name=3; Synonyms=Nd1-L2;
IsoId=Q920Q8-3; Sequence=VSP_024811;
Name=4;
IsoId=Q920Q8-4; Sequence=VSP_024810;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous expression. In the heart, the
highest expression is detected in the ventricles and the lowest in
the atria. Expressed in dendrites and spines in neurons.
{ECO:0000269|PubMed:12213805, ECO:0000269|PubMed:15684717,
ECO:0000269|PubMed:16317045}.
-!- DEVELOPMENTAL STAGE: Barely detected in the heart at E15.5, but
clearly expressed in newborn heart with increased amount up to 8
weeks of age. {ECO:0000269|PubMed:16952015}.
-!- INDUCTION: Decreased expression in various organs and cultured
cell lines by doxorubicin treatment which may reduce mRNA
stability. {ECO:0000269|PubMed:16952015,
ECO:0000269|PubMed:17016628}.
-!- DOMAIN: When the BTB domain is lacking, AHR signaling induction
promoted by IVNS1ABP is massively increased; Thus, the BTB domain
inhibits AHR signaling induced by IVNS1ABP. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice develop normally with no gross
abnormalities. However, they display marked sensitivity to
doxorubicin cardiotoxicity with increased number of cardiomyocytes
apoptosis. Analysis of hearts from knockout mice reveal
vacuolization and edema of cardiomaycytes.
{ECO:0000269|PubMed:15485691}.
-!- MISCELLANEOUS: Transgenic mice overexpressing Ivns1abp develop
normally with no gross abnormalities up to 7-month old. However,
they display a marked resistance to the cardiotoxic effect of
doxorubicin which is an anti-neoplastic agent known to affect
actin skeleton and an effective drug for cancer therapy with
cardiotoxicity as side effect. Overexpression of Ivns1abp in the
heart protect cardiomyocytes from apoptosis and improved survival
rate after doxorubicin injection.
-!- MISCELLANEOUS: Disorganized actin skeleton is observed in cells
transfected with isoform 2 (Nd1-S), which lacks the six kelch
repeats.
-!- SEQUENCE CAUTION:
Sequence=BAC98039.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB055737; BAB69058.1; -; mRNA.
EMBL; AB055738; BAB69059.1; -; mRNA.
EMBL; DQ914522; ABI84241.1; -; mRNA.
EMBL; AK129229; BAC98039.1; ALT_INIT; mRNA.
EMBL; AK007291; BAB24936.1; -; mRNA.
EMBL; AK144835; BAE26089.1; -; mRNA.
EMBL; AK145071; BAE26221.1; -; mRNA.
EMBL; AK146001; BAE26822.1; -; mRNA.
EMBL; AK146329; BAE27084.1; -; mRNA.
EMBL; AK146494; BAE27212.1; -; mRNA.
EMBL; AK146645; BAE27326.1; -; mRNA.
EMBL; AK159254; BAE34935.1; -; mRNA.
EMBL; BC004092; AAH04092.1; -; mRNA.
EMBL; BC040250; AAH40250.1; -; mRNA.
CCDS; CCDS15358.1; -. [Q920Q8-4]
CCDS; CCDS15359.1; -. [Q920Q8-1]
CCDS; CCDS35735.1; -. [Q920Q8-2]
RefSeq; NP_001034600.1; NM_001039511.1. [Q920Q8-2]
RefSeq; NP_001034601.1; NM_001039512.1. [Q920Q8-4]
RefSeq; NP_473443.2; NM_054102.2. [Q920Q8-1]
UniGene; Mm.33764; -.
ProteinModelPortal; Q920Q8; -.
SMR; Q920Q8; -.
BioGrid; 228184; 5.
IntAct; Q920Q8; 2.
MINT; MINT-1634681; -.
STRING; 10090.ENSMUSP00000023918; -.
iPTMnet; Q920Q8; -.
PhosphoSitePlus; Q920Q8; -.
PaxDb; Q920Q8; -.
PeptideAtlas; Q920Q8; -.
PRIDE; Q920Q8; -.
Ensembl; ENSMUST00000023918; ENSMUSP00000023918; ENSMUSG00000023150. [Q920Q8-1]
Ensembl; ENSMUST00000097543; ENSMUSP00000095150; ENSMUSG00000023150. [Q920Q8-4]
Ensembl; ENSMUST00000111887; ENSMUSP00000107518; ENSMUSG00000023150. [Q920Q8-2]
Ensembl; ENSMUST00000186745; ENSMUSP00000140708; ENSMUSG00000023150. [Q920Q8-2]
GeneID; 117198; -.
KEGG; mmu:117198; -.
UCSC; uc007cym.1; mouse. [Q920Q8-2]
UCSC; uc007cyn.1; mouse. [Q920Q8-1]
UCSC; uc007cyo.1; mouse. [Q920Q8-4]
CTD; 10625; -.
MGI; MGI:2152389; Ivns1abp.
eggNOG; KOG4441; Eukaryota.
eggNOG; ENOG410XNX8; LUCA.
GeneTree; ENSGT00760000119153; -.
HOVERGEN; HBG082407; -.
InParanoid; Q920Q8; -.
KO; K15046; -.
OMA; PNIDDWI; -.
OrthoDB; EOG091G024F; -.
PhylomeDB; Q920Q8; -.
TreeFam; TF329218; -.
ChiTaRS; Ivns1abp; mouse.
PRO; PR:Q920Q8; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000023150; -.
CleanEx; MM_IVNS1ABP; -.
ExpressionAtlas; Q920Q8; baseline and differential.
Genevisible; Q920Q8; MM.
GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:MGI.
Gene3D; 2.120.10.80; -; 2.
InterPro; IPR011705; BACK.
InterPro; IPR017096; BTB-kelch_protein.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR015915; Kelch-typ_b-propeller.
InterPro; IPR006652; Kelch_1.
InterPro; IPR029849; NS1BP.
InterPro; IPR011333; SKP1/BTB/POZ.
PANTHER; PTHR24411:SF7; PTHR24411:SF7; 1.
Pfam; PF07707; BACK; 1.
Pfam; PF00651; BTB; 1.
Pfam; PF01344; Kelch_1; 6.
PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
SMART; SM00875; BACK; 1.
SMART; SM00225; BTB; 1.
SMART; SM00612; Kelch; 6.
SUPFAM; SSF117281; SSF117281; 1.
SUPFAM; SSF54695; SSF54695; 1.
PROSITE; PS50097; BTB; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
Kelch repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 642 Influenza virus NS1A-binding protein
homolog.
/FTId=PRO_0000285078.
DOMAIN 32 99 BTB. {ECO:0000255|PROSITE-
ProRule:PRU00037}.
DOMAIN 134 233 BACK.
REPEAT 369 415 Kelch 1.
REPEAT 416 463 Kelch 2.
REPEAT 465 512 Kelch 3.
REPEAT 513 559 Kelch 4.
REPEAT 561 606 Kelch 5.
REPEAT 608 642 Kelch 6.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6Y0}.
MOD_RES 322 322 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6Y0}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6Y0}.
VAR_SEQ 178 219 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_024810.
VAR_SEQ 179 218 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_024811.
VAR_SEQ 221 221 Q -> Y (in isoform 2).
{ECO:0000303|PubMed:12213805,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_024812.
VAR_SEQ 222 642 Missing (in isoform 2).
{ECO:0000303|PubMed:12213805,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_024813.
CONFLICT 106 106 Y -> H (in Ref. 4; BAE26822).
{ECO:0000305}.
CONFLICT 201 201 W -> R (in Ref. 4; BAE34935).
{ECO:0000305}.
CONFLICT 285 285 P -> T (in Ref. 4; BAE27084).
{ECO:0000305}.
CONFLICT 295 295 E -> K (in Ref. 4; BAE27084).
{ECO:0000305}.
CONFLICT 544 544 P -> S (in Ref. 5; AAH04092).
{ECO:0000305}.
CONFLICT 548 548 A -> S (in Ref. 4; BAE27084).
{ECO:0000305}.
CONFLICT 549 549 R -> K (in Ref. 1; BAB69058).
{ECO:0000305}.
CONFLICT 589 589 M -> I (in Ref. 4; BAE27084).
{ECO:0000305}.
SEQUENCE 642 AA; 71581 MW; 7240360079C16B50 CRC64;
MIPNGYLMFE DENFIESSVA KLNALRKSGQ FCDVRLQVCG HEMLAHRAVL ACCSPYLFEI
FNSDSDPHGV SHVKLDDLNP EAVEVLLNYA YTAQLKADKE LVKDVYSAAK KLKMDRVKQV
CGDYLLSRMD VTSCISYRNF ASCMGDSRLL NKVDAYIQEH LLQISEEEEF LKLPRLKLEV
MLEDNVCLPS NGKLYTKVIN WVQRSIWENG DSLEELMEEV QTLYYSADHK LLDGNPLDGQ
AEVFGSDDDH IQFVQKKPPR ENGHKQISGS STGCLSSPNA SMQSPKHEWK IVASEKTSNN
TYLCLAVLDS TFCVIFLHGR NSPQSSPTST PKLSKSLSFE MQPDELLEKP MSPMQYARSG
LGTAEMNGKL IAAGGYNREE CLRTVECYDP HTDHWSFLAP MRTPRARFQM AVLMGQLYVV
GGSNGHSDDL SCGEMYDPNI DDWTPVPELR TNRCNAGVCA LNGKLYIVGG SDPYGQKGLK
NCDVFDPVTK SWTSCAPLNI RRHQSAVCEL GGYLYIIGGA ESWNCLNTVE RYNPENNTWT
LIAPMNVARR GAGVAVLDGK LFVGGGFDGS HAISCVEMYD PTRNEWKMMG NMTSPRSNAG
ITTVGNTIYA VGGFDGNEFL NTVEVYNPQS NEWSPYTKIF QF


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