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Oxidoreductase HTATIP2 (EC 1.1.1.-)

 HTAI2_MOUSE             Reviewed;         242 AA.
Q9Z2G9; Q810Y5; Q99KN6; Q9D5F8; Q9D804;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
28-MAR-2018, entry version 114.
RecName: Full=Oxidoreductase HTATIP2;
EC=1.1.1.-;
Name=Htatip2 {ECO:0000312|MGI:MGI:1859271};
Synonyms=Cc3 {ECO:0000303|PubMed:14695192},
Tip30 {ECO:0000303|PubMed:14695192};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC69617.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND DISRUPTION
PHENOTYPE.
PubMed=14695192;
Ito M., Jiang C., Krumm K., Zhang X., Pecha J., Zhao J., Guo Y.,
Roeder R.G., Xiao H.;
"TIP30 deficiency increases susceptibility to tumorigenesis.";
Cancer Res. 63:8763-8767(2003).
[2] {ECO:0000312|EMBL:AAN84531.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ {ECO:0000312|EMBL:AAN84531.1};
Hauser L.J., Webb L.S., Dhar M.S., Mural R.M., Larimer F.W.,
Johnson D.K.;
"Genomic organization, chromosomal mapping, and expression analysis of
the murine Prmt3 and Htatip2 genes.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Lung, Stomach, 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).
[4]
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).
[5] {ECO:0000312|EMBL:AAN84531.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and 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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Liver, Lung, 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).
[8] {ECO:0000312|EMBL:AAN84531.1}
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 7-242.
Joint center for structural genomics (JCSG);
"Crystal structure of Tat-interacting protein 30 kDa (HIV-1 Tat-
interactive protein 2, 30 kDa homolog) (human) (16924205) from Mus
musculus at 2.30 A resolution.";
Submitted (FEB-2006) to the PDB data bank.
-!- FUNCTION: Oxidoreductase required for tumor suppression. NAPDH-
bound form inhibits nuclear import by competing with nuclear
import substrates for binding to a subset of nuclear transport
receptors. May act as a redox sensor linked to transcription
through regulation of nuclear import.
{ECO:0000269|PubMed:14695192}.
-!- SUBUNIT: Monomer. Binds nuclear transport receptors XPO4,
IPO5/RANBP5, IPO7, IPO9 and KPNB1 as well as GCN1L1/GCN1 and
LRPPRC probably through their HEAT repeats. Binds NCOA5/CIA (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:14695192}; Synonyms=TIP30
{ECO:0000303|PubMed:14695192}, CC3 {ECO:0000303|PubMed:14695192};
IsoId=Q9Z2G9-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q9Z2G9-2; Sequence=VSP_051866, VSP_051867;
Note=No experimental confirmation available. {ECO:0000305};
-!- DISRUPTION PHENOTYPE: Mice are haploinsufficient for tumor
suppression. 50% develop tumors within their second year. 30% of
the tumors are hepatocellular carcinomas.
{ECO:0000269|PubMed:14695192}.
-----------------------------------------------------------------------
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EMBL; AF061972; AAC69617.1; -; mRNA.
EMBL; AY151050; AAN84531.1; -; Genomic_DNA.
EMBL; AK008630; BAB25792.1; -; mRNA.
EMBL; AK015389; BAB29825.1; -; mRNA.
EMBL; AK144837; BAE26091.1; -; mRNA.
EMBL; AC124775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466603; EDL22975.1; -; Genomic_DNA.
EMBL; CH466603; EDL22976.1; -; Genomic_DNA.
EMBL; CH466603; EDL22977.1; -; Genomic_DNA.
EMBL; BC004083; AAH04083.1; -; mRNA.
EMBL; BC017372; AAH17372.1; -; mRNA.
CCDS; CCDS52260.1; -. [Q9Z2G9-1]
RefSeq; NP_001139521.1; NM_001146049.1. [Q9Z2G9-1]
RefSeq; NP_001139522.1; NM_001146050.1. [Q9Z2G9-1]
RefSeq; NP_001139524.1; NM_001146052.1. [Q9Z2G9-1]
RefSeq; NP_001139525.1; NM_001146053.1. [Q9Z2G9-1]
UniGene; Mm.20801; -.
PDB; 2FMU; X-ray; 2.30 A; A=7-242.
PDBsum; 2FMU; -.
ProteinModelPortal; Q9Z2G9; -.
SMR; Q9Z2G9; -.
STRING; 10090.ENSMUSP00000082374; -.
iPTMnet; Q9Z2G9; -.
PhosphoSitePlus; Q9Z2G9; -.
SwissPalm; Q9Z2G9; -.
EPD; Q9Z2G9; -.
PaxDb; Q9Z2G9; -.
PeptideAtlas; Q9Z2G9; -.
PRIDE; Q9Z2G9; -.
DNASU; 53415; -.
Ensembl; ENSMUST00000085272; ENSMUSP00000082374; ENSMUSG00000039745. [Q9Z2G9-1]
GeneID; 53415; -.
KEGG; mmu:53415; -.
UCSC; uc009hbo.2; mouse. [Q9Z2G9-2]
UCSC; uc009hbq.2; mouse. [Q9Z2G9-1]
CTD; 10553; -.
MGI; MGI:1859271; Htatip2.
eggNOG; KOG4039; Eukaryota.
eggNOG; COG0702; LUCA.
GeneTree; ENSGT00390000008184; -.
HOVERGEN; HBG052833; -.
InParanoid; Q9Z2G9; -.
KO; K17290; -.
OrthoDB; EOG091G0S5T; -.
TreeFam; TF312849; -.
ChiTaRS; Casp3; mouse.
EvolutionaryTrace; Q9Z2G9; -.
PRO; PR:Q9Z2G9; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000039745; -.
CleanEx; MM_HTATIP2; -.
ExpressionAtlas; Q9Z2G9; baseline and differential.
Genevisible; Q9Z2G9; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0051170; P:nuclear import; ISS:UniProtKB.
GO; GO:0043068; P:positive regulation of programmed cell death; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
Pfam; PF13460; NAD_binding_10; 1.
SMART; SM00859; Semialdhyde_dh; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Angiogenesis;
Apoptosis; Complete proteome; Cytoplasm; Developmental protein;
Differentiation; NADP; Nucleus; Oxidoreductase; Reference proteome;
Tumor suppressor.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9BUP3}.
CHAIN 2 242 Oxidoreductase HTATIP2.
/FTId=PRO_0000072545.
NP_BIND 19 52 NADP. {ECO:0000250|UniProtKB:Q9BUP3}.
ACT_SITE 143 143 Proton acceptor.
{ECO:0000250|UniProtKB:Q9BUP3}.
ACT_SITE 147 147 {ECO:0000250|UniProtKB:Q9BUP3}.
BINDING 131 131 Substrate.
{ECO:0000250|UniProtKB:Q9BUP3}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q9BUP3}.
VAR_SEQ 102 105 EGFV -> VSKK (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_051866.
VAR_SEQ 106 242 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_051867.
CONFLICT 8 8 P -> R (in Ref. 1; AAC69617).
{ECO:0000305}.
CONFLICT 10 10 L -> P (in Ref. 3; BAB29825).
{ECO:0000305}.
CONFLICT 27 27 S -> T (in Ref. 3; BAB29825).
{ECO:0000305}.
CONFLICT 39 39 L -> V (in Ref. 1; AAC69617).
{ECO:0000305}.
CONFLICT 77 77 V -> G (in Ref. 2; AAN84531).
{ECO:0000305}.
CONFLICT 213 213 N -> S (in Ref. 1; AAC69617).
{ECO:0000305}.
CONFLICT 235 235 K -> I (in Ref. 3; BAB25792).
{ECO:0000305}.
HELIX 7 16 {ECO:0000244|PDB:2FMU}.
STRAND 20 24 {ECO:0000244|PDB:2FMU}.
HELIX 29 41 {ECO:0000244|PDB:2FMU}.
STRAND 45 53 {ECO:0000244|PDB:2FMU}.
STRAND 66 69 {ECO:0000244|PDB:2FMU}.
HELIX 72 82 {ECO:0000244|PDB:2FMU}.
STRAND 86 90 {ECO:0000244|PDB:2FMU}.
HELIX 101 108 {ECO:0000244|PDB:2FMU}.
HELIX 110 121 {ECO:0000244|PDB:2FMU}.
STRAND 126 130 {ECO:0000244|PDB:2FMU}.
HELIX 142 156 {ECO:0000244|PDB:2FMU}.
STRAND 160 166 {ECO:0000244|PDB:2FMU}.
STRAND 168 171 {ECO:0000244|PDB:2FMU}.
HELIX 195 199 {ECO:0000244|PDB:2FMU}.
STRAND 200 202 {ECO:0000244|PDB:2FMU}.
HELIX 203 215 {ECO:0000244|PDB:2FMU}.
STRAND 219 226 {ECO:0000244|PDB:2FMU}.
HELIX 227 233 {ECO:0000244|PDB:2FMU}.
SEQUENCE 242 AA; 26870 MW; 034F02137D3BF22A CRC64;
MADKEALPKL REDFKMQNKS VFILGASGET GKVLLKEILG QNLFSKVTLI GRRKLTFEEE
AYKNVNQEVV DFEKLDVYAS AFQGHDVGFC CLGTTRSKAG AEGFVRVDRD YVLKSAELAK
AGGCKHFNLL SSRGADKSSS FLYLQVKGEV EAKVEELKFD RLSVFRPGVL LCDRQESRPG
EWLARKFFGS LPDSWASGYA VPVVTVVRAM LNNLVSPSSG QMELLENKAI LHLGKDRDVP
KL


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