HTAI2_MOUSE
ID HTAI2_MOUSE Reviewed; 242 AA.
AC Q9Z2G9; Q810Y5; Q99KN6; Q9D5F8; Q9D804;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Oxidoreductase HTATIP2;
DE EC=1.1.1.-;
GN Name=Htatip2 {ECO:0000312|MGI:MGI:1859271};
GN Synonyms=Cc3 {ECO:0000303|PubMed:14695192},
GN Tip30 {ECO:0000303|PubMed:14695192};
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] {ECO:0000305, ECO:0000312|EMBL:AAC69617.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14695192;
RA Ito M., Jiang C., Krumm K., Zhang X., Pecha J., Zhao J., Guo Y.,
RA Roeder R.G., Xiao H.;
RT "TIP30 deficiency increases susceptibility to tumorigenesis.";
RL Cancer Res. 63:8763-8767(2003).
RN [2] {ECO:0000312|EMBL:AAN84531.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ {ECO:0000312|EMBL:AAN84531.1};
RA Hauser L.J., Webb L.S., Dhar M.S., Mural R.M., Larimer F.W., Johnson D.K.;
RT "Genomic organization, chromosomal mapping, and expression analysis of the
RT murine Prmt3 and Htatip2 genes.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Lung, Stomach, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000312|EMBL:AAN84531.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, 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).
RN [8] {ECO:0000312|EMBL:AAN84531.1}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 7-242.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of Tat-interacting protein 30 kDa (HIV-1 Tat-interactive
RT protein 2, 30 kDa homolog) (human) (16924205) from Mus musculus at 2.30 A
RT resolution.";
RL Submitted (FEB-2006) to the PDB data bank.
CC -!- FUNCTION: Oxidoreductase required for tumor suppression. NADPH-bound
CC form inhibits nuclear import by competing with nuclear import
CC substrates for binding to a subset of nuclear transport receptors. May
CC act as a redox sensor linked to transcription through regulation of
CC nuclear import. {ECO:0000269|PubMed:14695192}.
CC -!- SUBUNIT: Monomer. Binds nuclear transport receptors XPO4, IPO5/RANBP5,
CC IPO7, IPO9 and KPNB1 as well as GCN1L1/GCN1 and LRPPRC probably through
CC their HEAT repeats. Binds NCOA5/CIA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:14695192}; Synonyms=TIP30
CC {ECO:0000303|PubMed:14695192}, CC3 {ECO:0000303|PubMed:14695192};
CC IsoId=Q9Z2G9-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q9Z2G9-2; Sequence=VSP_051866, VSP_051867;
CC -!- DISRUPTION PHENOTYPE: Mice are haploinsufficient for tumor suppression.
CC 50% develop tumors within their second year. 30% of the tumors are
CC hepatocellular carcinomas. {ECO:0000269|PubMed:14695192}.
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DR EMBL; AF061972; AAC69617.1; -; mRNA.
DR EMBL; AY151050; AAN84531.1; -; Genomic_DNA.
DR EMBL; AK008630; BAB25792.1; -; mRNA.
DR EMBL; AK015389; BAB29825.1; -; mRNA.
DR EMBL; AK144837; BAE26091.1; -; mRNA.
DR EMBL; AC124775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466603; EDL22975.1; -; Genomic_DNA.
DR EMBL; CH466603; EDL22976.1; -; Genomic_DNA.
DR EMBL; CH466603; EDL22977.1; -; Genomic_DNA.
DR EMBL; BC004083; AAH04083.1; -; mRNA.
DR EMBL; BC017372; AAH17372.1; -; mRNA.
DR CCDS; CCDS52260.1; -. [Q9Z2G9-1]
DR RefSeq; NP_001139521.1; NM_001146049.1. [Q9Z2G9-1]
DR RefSeq; NP_001139522.1; NM_001146050.1. [Q9Z2G9-1]
DR RefSeq; NP_001139524.1; NM_001146052.1. [Q9Z2G9-1]
DR RefSeq; NP_001139525.1; NM_001146053.1. [Q9Z2G9-1]
DR PDB; 2FMU; X-ray; 2.30 A; A=7-242.
DR PDBsum; 2FMU; -.
DR AlphaFoldDB; Q9Z2G9; -.
DR SMR; Q9Z2G9; -.
DR BioGRID; 207309; 1.
DR STRING; 10090.ENSMUSP00000082374; -.
DR iPTMnet; Q9Z2G9; -.
DR PhosphoSitePlus; Q9Z2G9; -.
DR SwissPalm; Q9Z2G9; -.
DR EPD; Q9Z2G9; -.
DR jPOST; Q9Z2G9; -.
DR MaxQB; Q9Z2G9; -.
DR PaxDb; Q9Z2G9; -.
DR PeptideAtlas; Q9Z2G9; -.
DR PRIDE; Q9Z2G9; -.
DR ProteomicsDB; 273197; -. [Q9Z2G9-1]
DR ProteomicsDB; 273198; -. [Q9Z2G9-2]
DR Antibodypedia; 1770; 284 antibodies from 33 providers.
DR DNASU; 53415; -.
DR Ensembl; ENSMUST00000085272; ENSMUSP00000082374; ENSMUSG00000039745. [Q9Z2G9-1]
DR GeneID; 53415; -.
DR KEGG; mmu:53415; -.
DR UCSC; uc009hbo.2; mouse. [Q9Z2G9-2]
DR UCSC; uc009hbq.2; mouse. [Q9Z2G9-1]
DR CTD; 10553; -.
DR MGI; MGI:1859271; Htatip2.
DR VEuPathDB; HostDB:ENSMUSG00000039745; -.
DR eggNOG; KOG4039; Eukaryota.
DR GeneTree; ENSGT00390000008184; -.
DR HOGENOM; CLU_071330_2_2_1; -.
DR InParanoid; Q9Z2G9; -.
DR OrthoDB; 1601023at2759; -.
DR PhylomeDB; Q9Z2G9; -.
DR TreeFam; TF312849; -.
DR BioGRID-ORCS; 53415; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Htatip2; mouse.
DR EvolutionaryTrace; Q9Z2G9; -.
DR PRO; PR:Q9Z2G9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z2G9; protein.
DR Bgee; ENSMUSG00000039745; Expressed in urinary bladder urothelium and 209 other tissues.
DR ExpressionAtlas; Q9Z2G9; baseline and differential.
DR Genevisible; Q9Z2G9; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051170; P:import into nucleus; ISS:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR Pfam; PF13460; NAD_binding_10; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Angiogenesis; Apoptosis;
KW Cytoplasm; Developmental protein; Differentiation; NADP; Nucleus;
KW Oxidoreductase; Reference proteome; Tumor suppressor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BUP3"
FT CHAIN 2..242
FT /note="Oxidoreductase HTATIP2"
FT /id="PRO_0000072545"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BUP3"
FT ACT_SITE 147
FT /evidence="ECO:0000250|UniProtKB:Q9BUP3"
FT BINDING 19..52
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9BUP3"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BUP3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUP3"
FT VAR_SEQ 102..105
FT /note="EGFV -> VSKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051866"
FT VAR_SEQ 106..242
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051867"
FT CONFLICT 8
FT /note="P -> R (in Ref. 1; AAC69617)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="L -> P (in Ref. 3; BAB29825)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="S -> T (in Ref. 3; BAB29825)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="L -> V (in Ref. 1; AAC69617)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="V -> G (in Ref. 2; AAN84531)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="N -> S (in Ref. 1; AAC69617)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="K -> I (in Ref. 3; BAB25792)"
FT /evidence="ECO:0000305"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:2FMU"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:2FMU"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:2FMU"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:2FMU"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2FMU"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:2FMU"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2FMU"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:2FMU"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:2FMU"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2FMU"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:2FMU"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:2FMU"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:2FMU"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:2FMU"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2FMU"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:2FMU"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:2FMU"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:2FMU"
SQ 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
