IPO9_MOUSE
ID IPO9_MOUSE Reviewed; 1041 AA.
AC Q91YE6; Q924M3; Q924M4;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Importin-9 {ECO:0000303|PubMed:11493596};
DE Short=Imp9 {ECO:0000303|PubMed:11493596};
DE AltName: Full=Importin-9a {ECO:0000303|PubMed:11823430};
DE Short=Imp9a {ECO:0000303|PubMed:11823430};
DE AltName: Full=Importin-9b {ECO:0000303|PubMed:11823430};
DE Short=Imp9b {ECO:0000303|PubMed:11823430};
DE AltName: Full=Ran-binding protein 9;
DE Short=RanBP9;
GN Name=Ipo9 {ECO:0000312|MGI:MGI:1918944};
GN Synonyms=Imp9 {ECO:0000303|PubMed:11493596}, Ranbp9;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH HISTONES H2B;
RP H2A; H3 AND H4.
RX PubMed=11493596; DOI=10.1093/embo-reports/kve168;
RA Muehlhaeusser P., Mueller E.-C., Otto A., Kutay U.;
RT "Multiple pathways contribute to nuclear import of core histones.";
RL EMBO Rep. 2:690-696(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH RPS7; RPL18A;
RP RPL4 AND RPL6.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [4]
RP FUNCTION.
RX PubMed=22323606; DOI=10.1073/pnas.1118880109;
RA Dopie J., Skarp K.P., Rajakyla E.K., Tanhuanpaa K., Vartiainen M.K.;
RT "Active maintenance of nuclear actin by importin 9 supports
RT transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E544-E552(2012).
CC -!- FUNCTION: Nuclear transport receptor that mediates nuclear import of
CC proteins, such as histones, proteasome and actin (PubMed:11493596,
CC PubMed:11823430, PubMed:22323606). Serves as receptor for nuclear
CC localization signals (NLS) in cargo substrates (PubMed:11493596,
CC PubMed:11823430). Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) through
CC binding to nucleoporin and the complex is subsequently translocated
CC through the pore by an energy requiring, Ran-dependent mechanism
CC (PubMed:11493596, PubMed:11823430). At the nucleoplasmic side of the
CC NPC, Ran binds to the importin, the importin/substrate complex
CC dissociates and importin is re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran (PubMed:11493596,
CC PubMed:11823430). The directionality of nuclear import is thought to be
CC conferred by an asymmetric distribution of the GTP- and GDP-bound forms
CC of Ran between the cytoplasm and nucleus (PubMed:11493596,
CC PubMed:11823430). Mediates the import of pre-assembled proteasomes into
CC the nucleus; AKIRIN2 acts as a molecular bridge between IPO9 and the
CC proteasome complex (By similarity). Mediates the nuclear import of
CC histones H2A, H2B, H4 and H4 (PubMed:11493596, PubMed:11823430). In
CC addition to nuclear import, also acts as a chaperone for histones by
CC preventing inappropriate non-nucleosomal interactions (By similarity).
CC Mediates the nuclear import of actin (PubMed:22323606).
CC {ECO:0000250|UniProtKB:Q96P70, ECO:0000269|PubMed:11493596,
CC ECO:0000269|PubMed:11823430, ECO:0000269|PubMed:22323606}.
CC -!- SUBUNIT: Interacts with histones H2A, H2B, H3 and H4 (PubMed:11493596,
CC PubMed:11823430). The binding is coupled to RanGTP cycles
CC (PubMed:11493596, PubMed:11823430). Interacts with AKIRIN2; promoting
CC association with pre-assembled proteasomes (By similarity). Associates
CC with pre-assembled proteasomes; interaction is indirect and mediated
CC via interaction with AKIRIN2 (By similarity). Interacts with PPP2R1A
CC and PPP2R1B (By similarity). {ECO:0000250|UniProtKB:Q96P70,
CC ECO:0000269|PubMed:11493596, ECO:0000269|PubMed:11823430}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96P70}. Nucleus
CC {ECO:0000250|UniProtKB:Q96P70}.
CC -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
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DR EMBL; AJ309238; CAC69407.1; -; mRNA.
DR EMBL; AF273672; AAK91127.1; -; mRNA.
DR EMBL; AF273673; AAK91128.1; -; mRNA.
DR AlphaFoldDB; Q91YE6; -.
DR SMR; Q91YE6; -.
DR DIP; DIP-34268N; -.
DR IntAct; Q91YE6; 7.
DR MINT; Q91YE6; -.
DR STRING; 10090.ENSMUSP00000036093; -.
DR iPTMnet; Q91YE6; -.
DR PhosphoSitePlus; Q91YE6; -.
DR SwissPalm; Q91YE6; -.
DR EPD; Q91YE6; -.
DR MaxQB; Q91YE6; -.
DR PaxDb; Q91YE6; -.
DR PRIDE; Q91YE6; -.
DR ProteomicsDB; 269498; -.
DR MGI; MGI:1918944; Ipo9.
DR eggNOG; KOG2274; Eukaryota.
DR InParanoid; Q91YE6; -.
DR PhylomeDB; Q91YE6; -.
DR ChiTaRS; Ipo9; mouse.
DR PRO; PR:Q91YE6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91YE6; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:MGI.
DR GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR GO; GO:0061608; F:nuclear import signal receptor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; TAS:MGI.
DR GO; GO:0031144; P:proteasome localization; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; ISA:MGI.
DR GO; GO:0042254; P:ribosome biogenesis; ISA:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Nucleus; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96P70"
FT CHAIN 2..1041
FT /note="Importin-9"
FT /id="PRO_0000120755"
FT DOMAIN 43..119
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REGION 936..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..966
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96P70"
FT CONFLICT 166
FT /note="A -> V (in Ref. 2; AAK91127)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="K -> E (in Ref. 2; AAK91127)"
FT /evidence="ECO:0000305"
FT CONFLICT 782
FT /note="L -> P (in Ref. 2; AAK91127)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="M -> V (in Ref. 2; AAK91128)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="V -> A (in Ref. 2; AAK91127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1041 AA; 116052 MW; 2307E00D0AEABEA4 CRC64;
MAAAAAAGAA SGLPGPVAQG LKEALVDTLT GILSPVQEVR AAAEEQIKVL EVTEEFGVHL
AELTVDPQGA LAIRQLASVI LKQYVETHWC AQSEKFRPPE TTERAKIVIR ELLPNGLRES
ISKVRSSVAY AVSAIAHWDW PEAWPQLFNL LMEMLVSGDL NAVHGAMRVL TEFTREVTDT
QMPLVAPVIL PEMYKIFTMA EVYGIRTRSR AVEIFTTCAH MICNMEELEK GAAKVLIFPV
VQQFTEAFVQ ALQMPDGPTS DSGFKMEVLK AVTALVKNFP KHMVSSMQQI LPIVWNTLTE
SAAFYVRTEV NYTEEVEDPV DSDGEVLGFE NLVFSIFEFV HALLENSKFK STVKKALPEL
IYYIILYMQI TEEQIKVWTA NPQQFVEDED DDTFSYTVRI AAQDLLLAVA TDFQNESAVA
LATAATRHLQ EAEQTKASGT EHWWKIHEAC MLALGSVKSI ITDSVKNGRI HFDMHGFLTN
VILADLNLSA SPFLLGRALW AASRFTVAMS PELIQQFLQA TVSGLHETQP PSVRISAVRA
IWGYCDQLKV SESTHVLQPF LPSILDGLIH LAAQFSSEVL NLVMETLCIV CTVDPEFTAS
VENKICPFTI AIFLKYSNDP VVASLAQDIF KELSQIEACQ GPMQMRLIPT LVSIMQAPAD
KIPAGLCATA IDILTTVVRN TKPPLSQLLI CQAFPAVAQC TLHTDDNATM QNGGECLRAY
VSVTLEQVAQ WHDEQGHNGL WYVMQVVSQL LDPRTSEFTA AFVGRLVSTL ISKAGRELGE
NLDQILRAIL SKMQQAETLS VMQSLIMVFA HLVHTQLEPL LEFLCSLPGP TGKPALEFVM
AEWTSRQHLF YGQYEGKVSS VALCKLLQHG INADDKRLQD IRVKGEEIYS MDEGIRTRSK
SAKNPERWTN IPLLVKILKL IINELSNVME ANAARQATPA EWNQDDSNDM WEDQEEEEEE
EEDGLAGQLL SDILATSKYE EDYYEDDEED DPDALKDPLY QIDLQAYLTD FLCQFAQQPC
YIMFSCHLND NERRVLQTIG I
