ID   HTAI2_GORGO             Reviewed;         242 AA.
AC   A1YER2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Oxidoreductase HTATIP2;
DE            EC=1.1.1.-;
GN   Name=HTATIP2;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT   "Positive selection in transcription factor genes on the human lineage.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ976444; ABM46630.1; -; Genomic_DNA.
DR   RefSeq; XP_018892999.1; XM_019037454.1.
DR   RefSeq; XP_018893000.1; XM_019037455.1.
DR   AlphaFoldDB; A1YER2; -.
DR   SMR; A1YER2; -.
DR   STRING; 9593.ENSGGOP00000015311; -.
DR   Ensembl; ENSGGOT00000015748; ENSGGOP00000015311; ENSGGOG00000015692.
DR   GeneID; 101152326; -.
DR   KEGG; ggo:101152326; -.
DR   CTD; 10553; -.
DR   eggNOG; KOG4039; Eukaryota.
DR   GeneTree; ENSGT00390000008184; -.
DR   HOGENOM; CLU_071330_2_2_1; -.
DR   InParanoid; A1YER2; -.
DR   OrthoDB; 1601023at2759; -.
DR   Proteomes; UP000001519; Chromosome 11.
DR   Bgee; ENSGGOG00000015692; Expressed in liver and 6 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:Ensembl.
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; IBA:GO_Central.
DR   GO; GO:0043068; P:positive regulation of programmed cell death; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR   GO; GO:0045765; P:regulation of angiogenesis; IEA:Ensembl.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF13460; NAD_binding_10; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Acetylation; Angiogenesis; Apoptosis; Cytoplasm; Developmental protein;
KW   Differentiation; NADP; Nucleus; Oxidoreductase; Reference proteome;
KW   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_0000285510"
FT   ACT_SITE        143
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000250"
FT   BINDING         19..52
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUP3"
SQ   SEQUENCE   242 AA;  27077 MW;  2F33733EE9153178 CRC64;
     MAETEALSKL REDFRMQNKS VFILGASGET GRVLLKEILE QGLFSKVTLI GRRKLTFDEE
     AYKNVNQEVV DFEKLDDYAS AFQGHDVGFC CLGTTRGKAG AEGFVRVDRD YVLKSAELAK
     AGGCKHFNLL SSKGADKSSK FLYLQVKGEV EAKVEELKFD RYSVFRPGVL LCDRQESRPG
     EWLVRKFFGS LPESWASGHS VPVVTVVRAM LNNVVRPRDK QMELLENKAI HDLGKAHGSL
     KP