ID   IPO9_HUMAN              Reviewed;        1041 AA.
AC   Q96P70; Q8N1Y1; Q8N3I2; Q8NCG9; Q96SU6; Q9NW01; Q9P0A8; Q9ULM8;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-NOV-2009, entry version 72.
DE   RecName: Full=Importin-9;
DE            Short=Imp9;
DE   AltName: Full=Ran-binding protein 9;
DE            Short=RanbP9;
GN   Name=IPO9; Synonyms=IMP9, KIAA1192, RANBP9; ORFNames=HSPC273;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH RPS7;
RP   RPL18A; RPL4 AND RPL6.
RX   MEDLINE=21681405; PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA   Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT   "Importins fulfil a dual function as nuclear import receptors and
RT   cytoplasmic chaperones for exposed basic domains.";
RL   EMBO J. 21:377-386(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-276 AND 358-1041.
RC   TISSUE=Amygdala;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-22; 400-427 AND 908-916, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (JUN-2005) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1041.
RC   TISSUE=Placenta;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 632-1041.
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 767-1041.
RC   TISSUE=Umbilical cord blood;
RX   MEDLINE=20499367; PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for
RT   300 previously undefined genes expressed in CD34+ hematopoietic
RT   stem/progenitor cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 780-1041.
RC   TISSUE=Brain;
RX   MEDLINE=20039618; PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis
RT   from size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [8]
RP   INTERACTION WITH PPP2R1A AND PPP2R1B.
RX   PubMed=12670497; DOI=10.1016/S0006-291X(03)00434-0;
RA   Lubert E.J., Sarge K.D.;
RT   "Interaction between protein phosphatase 2A and members of the
RT   importin beta superfamily.";
RL   Biochem. Biophys. Res. Commun. 303:908-913(2003).
RN   [9]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC       receptor. Serves as receptor for nuclear localization signals
CC       (NLS) in cargo substrates. Is thought to mediate docking of the
CC       importin/substrate complex to the nuclear pore complex (NPC)
CC       through binding to nucleoporin and the complex is subsequently
CC       translocated through the pore by an energy requiring, Ran-
CC       dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC       binds to the importin, the importin/substrate complex dissociates
CC       and importin is re-exported from the nucleus to the cytoplasm
CC       where GTP hydrolysis releases Ran. The directionality of nuclear
CC       import is thought to be conferred by an asymmetric distribution of
CC       the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC       nucleus (By similarity). Mediates the nuclear import of H2B
CC       histone (By similarity), RPS7 and RPL18A. Prevents the cytoplasmic
CC       aggregation of RPS7 and RPL18A by shielding exposed basic domains.
CC       May also import H2A, H3, H4 histones (By similarity), RPL4 and
CC       RPL6.
CC   -!- SUBUNIT: Binds with high affinity to RPS7 and RPL18A. The binding
CC       is coupled to RanGTP cycles. May bind H2A, H3, H4 histones (By
CC       similarity), RPL4 and RPL6 with low affinity. Interacts with
CC       PPP2R1A and PPP2R1B.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the importin beta family.
CC   -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF28951.1; Type=Frameshift; Positions=982;
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DR   EMBL; AF410465; AAL01416.1; -; mRNA.
DR   EMBL; AK001264; BAA91588.1; ALT_INIT; mRNA.
DR   EMBL; AK027532; BAB55181.1; ALT_INIT; mRNA.
DR   EMBL; AK074740; BAC11173.1; ALT_INIT; mRNA.
DR   EMBL; AK094603; BAC04383.1; ALT_SEQ; mRNA.
DR   EMBL; BC003604; AAH03604.2; -; mRNA.
DR   EMBL; AF161391; AAF28951.1; ALT_FRAME; mRNA.
DR   EMBL; AL834323; CAD38991.1; -; mRNA.
DR   EMBL; AB033018; BAA86506.1; ALT_INIT; mRNA.
DR   IPI; IPI00185146; -.
DR   RefSeq; NP_060555.2; -.
DR   UniGene; Hs.596014; -.
DR   IntAct; Q96P70; 5.
DR   STRING; Q96P70; -.
DR   PhosphoSite; Q96P70; -.
DR   PeptideAtlas; Q96P70; -.
DR   PRIDE; Q96P70; -.
DR   Ensembl; ENST00000361565; ENSP00000354742; ENSG00000198700; Homo sapiens.
DR   Ensembl; ENST00000456707; ENSP00000387761; ENSG00000198700; Homo sapiens.
DR   GeneID; 55705; -.
DR   KEGG; hsa:55705; -.
DR   UCSC; uc001gwz.1; human.
DR   CTD; 55705; -.
DR   GeneCards; GC01P200064; -.
DR   H-InvDB; HIX0001464; -.
DR   HGNC; HGNC:19425; IPO9.
DR   PharmGKB; PA134930111; -.
DR   HOVERGEN; Q96P70; -.
DR   OMA; ALQMPDG; -.
DR   NextBio; 60559; -.
DR   ArrayExpress; Q96P70; -.
DR   Bgee; Q96P70; -.
DR   CleanEx; HS_IPO9; -.
DR   CleanEx; HS_RANBP9; -.
DR   Genevestigator; Q96P70; -.
DR   GermOnline; ENSG00000198700; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005643; C:nuclear pore; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB.
DR   GO; GO:0008536; F:Ran GTPase binding; ISS:UniProtKB.
DR   GO; GO:0000059; P:protein import into nucleus, docking; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR001494; Importin-b_N.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF03810; IBN_N; 1.
DR   PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Nucleus; Protein transport; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2   1041       Importin-9.
FT                                /FTId=PRO_0000120754.
FT   DOMAIN       43    119       Importin N-terminal.
FT   MOD_RES       2      2       N-acetylalanine.
FT   CONFLICT    632    632       E -> G (in Ref. 2; BAC11173).
FT   CONFLICT    916    916       K -> R (in Ref. 2; BAC11173).
FT   CONFLICT    935    935       R -> P (in Ref. 2; BAB55181).
FT   CONFLICT    960    960       E -> G (in Ref. 2; BAC11173).
SQ   SEQUENCE   1041 AA;  115963 MW;  A1842C357AEDFD90 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 ALQIPDGPTS DSGFKMEVLK AVTALVKNFP KHMVSSMQQI LPIVWNTLTE
     SAAFYVRTEV NYTEEVEDPV DSDGEVLGFE NLVFSIFEFV HALLENSKFK STVKKALPEL
     IYYIILYMQI TEEQIKVWTA NPQQFVEDED DDTFSYTVRI AAQDLLLAVA TDFQNESAAA
     LAAAATRHLQ EAEQTKNSGT EHWWKIHEAC MLALGSVKAI ITDSVKNGRI HFDMHGFLTN
     VILADLNLSV SPFLLGRALW AASRFTVAMS PELIQQFLQA TVSGLHETQP PSVRISAVRA
     IWGYCDQLKV SESTHVLQPF LPSILDGLIH LAAQFSSEVL NLVMETLCIV CTVDPEFTAS
     MESKICPFTI 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 EWSQDDSNDM WEDQEEEEEE
     EEDGLAGQLL SDILATSKYE EDYYEDDEED DPDALKDPLY QIDLQAYLTD FLCQFAQQPC
     YIMFSGHLND NERRVLQTIG I
//