IMB1_SCHPO
ID IMB1_SCHPO Reviewed; 863 AA.
AC O13864;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Importin subunit beta-1 {ECO:0000250|UniProtKB:Q06142};
DE AltName: Full=Importin-95 {ECO:0000250|UniProtKB:Q06142};
DE AltName: Full=Karyopherin subunit beta-1 {ECO:0000250|UniProtKB:Q06142};
DE AltName: Full=Karyopherin-95 {ECO:0000250|UniProtKB:Q06142};
GN Name=kap95 {ECO:0000250|UniProtKB:Q06142};
GN ORFNames=SPAC1B1.03c {ECO:0000312|PomBase:SPAC1B1.03c};
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 SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15116432; DOI=10.1002/yea.1115;
RA Chen X.Q., Du X., Liu J., Balasubramanian M.K., Balasundaram D.;
RT "Identification of genes encoding putative nucleoporins and transport
RT factors in the fission yeast Schizosaccharomyces pombe: a deletion
RT analysis.";
RL Yeast 21:495-509(2004).
RN [3]
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: Importin beta subunit that functions in nuclear protein
CC import through association with the importin alpha subunit, which binds
CC to the clasical nuclear localization signal (cNLS) in cargo substrates.
CC Docking of the importin/substrate complex to the nuclear pore complex
CC (NPC) is mediated by importin beta through binding to nucleoporin FxFG
CC repeats and 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 binds to importin beta and the three
CC components separate, leading to release of the cargo. Importin alpha
CC and beta are re-exported from the nucleus to the cytoplasm where GTP
CC hydrolysis releases Ran from importin beta. The directionality of
CC nuclear import is thought to be conferred by an asymmetric distribution
CC of the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus. {ECO:0000250|UniProtKB:Q06142}.
CC -!- SUBUNIT: Forms a complex with an importin alpha subunit. Interacts with
CC Ran; interacts specifically with the GTP-bound form of Ran (GTP-Ran),
CC protecting it from GTP hydrolysis and nucleotide exchange. Interacts
CC with nucleoporins. {ECO:0000250|UniProtKB:Q06142}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06142}. Nucleus
CC envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}.
CC Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q06142}.
CC -!- DISRUPTION PHENOTYPE: Essential for growth. Spores germinate, but fail
CC to divide. {ECO:0000269|PubMed:15116432}.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-1
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB11082.1; -; Genomic_DNA.
DR PIR; T38016; T38016.
DR RefSeq; NP_594233.1; NM_001019656.2.
DR AlphaFoldDB; O13864; -.
DR SMR; O13864; -.
DR BioGRID; 278955; 5.
DR STRING; 4896.SPAC1B1.03c.1; -.
DR iPTMnet; O13864; -.
DR MaxQB; O13864; -.
DR PaxDb; O13864; -.
DR PRIDE; O13864; -.
DR EnsemblFungi; SPAC1B1.03c.1; SPAC1B1.03c.1:pep; SPAC1B1.03c.
DR GeneID; 2542496; -.
DR KEGG; spo:SPAC1B1.03c; -.
DR PomBase; SPAC1B1.03c; kap95.
DR VEuPathDB; FungiDB:SPAC1B1.03c; -.
DR eggNOG; KOG1241; Eukaryota.
DR HOGENOM; CLU_008296_1_0_1; -.
DR InParanoid; O13864; -.
DR OMA; GRICDII; -.
DR PhylomeDB; O13864; -.
DR Reactome; R-SPO-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-68616; Assembly of the ORC complex at the origin of replication.
DR PRO; PR:O13864; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; 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; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; NAS:PomBase.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; ISO:PomBase.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006606; P:protein import into nucleus; ISO:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 3: Inferred from homology;
KW Cytoplasm; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..863
FT /note="Importin subunit beta-1"
FT /id="PRO_0000120763"
FT REPEAT 2..31
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT DOMAIN 21..101
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 33..62
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 85..124
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 129..159
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 170..201
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 212..248
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 253..299
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 314..360
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 364..392
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 399..439
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 449..481
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 496..530
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 536..586
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 592..630
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 635..671
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 677..715
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 720..767
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 778..815
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
FT REPEAT 822..861
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:Q06142"
SQ SEQUENCE 863 AA; 94747 MW; 9E02D72F5A1C6839 CRC64;
MNAGEFLAQT LSPDANVRLN AEKQLENAAR TDFAQYMVLL AQELANDNSM PYIRMAAGLA
LKNAITAREE ARKLEYQQLW QSLPVEIKQQ VKSLALQTLG SSEHQAGQSA AQLVAAIAAY
ELATNQWPDL MVTLVANVGE GQPSALKQHS LQTIGYICES VSPEVLSAQS NAILTAVVAG
ARKEEPDAAV RLAALGALYD SLEFVRENFN NEYERNYIMQ VVCEATQSPE ASIQTAAFGC
LVKIMHLYYD TMPFYMEKAL FALTTQGMYN TNEQVALQAV EFWSTVCEEE IEVNLEIQEA
QDLNEVPARQ NHGFARAAAA DILPVLLKLL CNQDEDADED DWNISMAAAT CLQLFAQVVG
DLIVNPVLAF VEQNIQNPDW HQREAAVMAF GSVLEGPNVA MLTPLVNQAL PVLINMMVDP
VIFVKDTTAW ALGQISSFVA DAINPEIHLS PMVSALLQGL TDNPRIVANC CWAFMNLVCH
FAPVDNHQTS VMTPFYEAII GSLLHVTDQK GNENNSRTSG YETLGTLITF SSDSVLPMIA
NVLSIILTRL ETSIQMQSQI LDVEDRANHD ELQSNLCNVL TSIIRRFGPD IRTSSDQIMN
LLLQTMQTAP KQSVVHEDVL LAIGAMMNSL EEQFEVYVPS FVPFLSSALS NEQEYQLCSV
AVGLVGDLAR ALNAKILPYC DDFMTRLVQD LQSSVLDRNV KPAILSCFSD IALAIGAAFQ
TYLEAVMVLL QQASSVQAPP GANFSMIDYV DALRLGIVEA YVGITQAVRT DNRLDLIQPY
VHSMFTLLNM ITADPECSES LTRAALGLLG DLAESFPKGE LKSYFAADWV AALLNSGKTK
ISSQQTKDLA RWATEQVKRQ ARA
