IMB3_SCHPO
ID IMB3_SCHPO Reviewed; 1095 AA.
AC O74476; Q9US74;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Importin subunit beta-3 {ECO:0000250|UniProtKB:P32337};
DE AltName: Full=Importin beta sal3 {ECO:0000303|PubMed:12399381};
GN Name=sal3 {ECO:0000303|PubMed:12399381};
GN Synonyms=pse1 {ECO:0000250|UniProtKB:P32337};
GN ORFNames=SPCC1840.03 {ECO:0000312|PomBase:SPCC1840.03};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 117-307, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12399381; DOI=10.1093/genetics/162.2.689;
RA Chua G., Lingner C., Frazer C., Young P.G.;
RT "The sal3(+) gene encodes an importin-beta implicated in the nuclear import
RT of cdc25 in Schizosaccharomyces pombe.";
RL Genetics 162:689-703(2002).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Involved in the nuclear import of cdc25 and mcs1.
CC {ECO:0000269|PubMed:12399381}.
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals (NLS) in
CC cargo substrates. Involved in the nuclear import of cdc25 and mcs1
CC (PubMed:12399381). Mediates docking of the importin/substrate complex
CC to the nuclear pore complex (NPC) through binding to repeat-containing
CC nucleoporins. The complex is subsequently translocated through the pore
CC by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic
CC side of the NPC, GTP-Ran binding leads to release of the cargo. The
CC importin is re-exported from the nucleus to the cytoplasm where GTP
CC hydrolysis releases Ran from importin. The directionality of nuclear
CC import is thought to be conferred by an asymmetric distribution of the
CC GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By
CC similarity). {ECO:0000250|UniProtKB:P32337,
CC ECO:0000269|PubMed:12399381}.
CC -!- SUBUNIT: Interacts with Ran; interacts specifically with the GTP-bound
CC form of Ran (GTP-Ran), protecting it from GTP hydrolysis and nucleotide
CC exchange. {ECO:0000250|UniProtKB:P32337}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}. Nucleus
CC envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381,
CC ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-3
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAA20126.1; -; Genomic_DNA.
DR EMBL; AB027999; BAA87303.1; -; Genomic_DNA.
DR PIR; T41171; T41171.
DR RefSeq; NP_588502.1; NM_001023492.2.
DR AlphaFoldDB; O74476; -.
DR SMR; O74476; -.
DR BioGRID; 275952; 11.
DR STRING; 4896.SPCC1840.03.1; -.
DR MaxQB; O74476; -.
DR PaxDb; O74476; -.
DR PRIDE; O74476; -.
DR EnsemblFungi; SPCC1840.03.1; SPCC1840.03.1:pep; SPCC1840.03.
DR GeneID; 2539387; -.
DR KEGG; spo:SPCC1840.03; -.
DR PomBase; SPCC1840.03; sal3.
DR VEuPathDB; FungiDB:SPCC1840.03; -.
DR eggNOG; KOG2171; Eukaryota.
DR HOGENOM; CLU_003794_0_1_1; -.
DR InParanoid; O74476; -.
DR OMA; PKRFVQE; -.
DR PhylomeDB; O74476; -.
DR PRO; PR:O74476; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; HDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005643; C:nuclear pore; NAS:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005525; F:GTP binding; NAS:PomBase.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IMP:PomBase.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IMP:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040122; Importin_beta.
DR InterPro; IPR041653; Importin_rep_4.
DR InterPro; IPR040928; Importin_rep_5.
DR InterPro; IPR041389; Importin_rep_6.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF18808; Importin_rep_4; 1.
DR Pfam; PF18816; Importin_rep_5; 1.
DR Pfam; PF18829; Importin_rep_6; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..1095
FT /note="Importin subunit beta-3"
FT /id="PRO_0000120773"
FT REPEAT 7..40
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 44..78
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 109..132
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 138..165
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 174..206
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 215..251
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 259..294
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 303..363
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 365..399
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 403..443
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 445..484
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 487..527
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 529..572
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 575..617
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 619..694
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 697..740
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 747..786
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 792..858
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 861..899
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 907..939
FT /note="HEAT 20"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 947..987
FT /note="HEAT 21"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 995..1026
FT /note="HEAT 22"
FT /evidence="ECO:0000250|UniProtKB:P32337"
FT REPEAT 1045..1073
FT /note="HEAT 23"
FT /evidence="ECO:0000250|UniProtKB:P32337"
SQ SEQUENCE 1095 AA; 121869 MW; 4FD3D581C7BFBC68 CRC64;
MSSGFPPEVL SPLLNLVQGL SSPDNTVRND AEKSLSSDWI SQRADLLLNG LAILAYQSED
PAVRSFCLVL CRRISFRTLP GDSELEVFSS ISNESKQSLQ SQLLACFVKE SVPTVRNKLC
DTIAEIARSI YDCQGEWPEL INVIFNAVNS PDESFRESVF RTITSLPRLL SGQDSAVTPL
FTTGLADPSI RVRISAARAY SAVILESKQS TRDQVIPLLP SLMNILPPLQ QDRDSDNLAD
CLMAITEIAE VFPKLFKPIF ESVIAFGLGI IKDKELDNSA RQAALELLVC FSEGAPAMCR
KSSDYTDQLV LQCLLLMTDV AGDPEDEAEE LQEWLNTDDL DQDESDANHV VAEQAMDRLS
RKLGGKTILP PSFTWLPRLI PSQKWSERHA ALMAISSIAE GAEKLMKKEL SRVLDMVLPL
LADPHPRVRW AACNAVGQMS TDFAPDMQVK YPSRILEALV PVLESPESRV QAHAAAAMVN
FSEEADNKVL EPYLDDILQR LLTLLQSPKR YVQEQAVTTI ATVADAAAKK FEKYFDAIMP
LLFNVLQQAD GKEFRTLRGK TMECATLIAL AVGKQRFLPV SQELIQILGN IQMGITDSDD
PQASYLISAW GRICRVLGSD FVPFLSSVMP PLLVAATSKP DFTIIDDEVD ESKYSEQDGW
EFIPVHGQQV GIRTSTLEDK CTATEMLVCY AAELKADFDP YVNEVLTSVV LPGLKFFFHD
GVRSACCKCI PQLLNARILA SNRDPAKVNE LWEPILRKLL DHIQNEPSVE MLADYFECFY
QSLEISGLNL SPSSMEALVA AVDLQLKGFI SRVQQREEEA KNGDIDIEED EDMILAVEND
QNLLNEINKT FSVVLKIHKT AFCPFWERLL PYMDGFLSGN DTVAKQWALC MMDDLIEFTG
PDSWNYKDHF LPYLAEGIQS SEPEIRQAAS YGIGVAAQHG GELYAEICSS ALPALFKMLE
LPDARDEEQI YATENICVAI CKICRFCSQR VQDLDKVVTY WINTLPVTHD EDDAPYAYTF
LAELMEQNHV AVASQMPTII TILAETFASG VLRGRTLTRL MEASKVYLAR FPADQVNSVI
ATLSVDNQRA LSAHF
