IMB2_SCHPO
ID IMB2_SCHPO Reviewed; 910 AA.
AC O14089;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Importin subunit beta-2 {ECO:0000250|UniProtKB:Q92973};
DE AltName: Full=Importin-104 {ECO:0000250|UniProtKB:P38217};
DE AltName: Full=Karyopherin subunit beta-2 {ECO:0000250|UniProtKB:P38217};
DE AltName: Full=Karyopherin-104 {ECO:0000250|UniProtKB:P38217};
DE AltName: Full=Transportin {ECO:0000250|UniProtKB:Q92973};
DE Short=TRN {ECO:0000250|UniProtKB:Q92973};
GN Name=kap104 {ECO:0000303|PubMed:15116432};
GN ORFNames=SPAC2F3.06c {ECO:0000312|PomBase:SPAC2F3.06c};
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: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for arginine/glycine-rich nuclear
CC localization signals (rg-NLS) and PY-NLS in cargo substrates. Its
CC predominant cargo substrate seems to be mRNA-binding proteins. Mediates
CC docking of the importin/substrate complex to the nuclear pore complex
CC (NPC) through binding to repeat-containing nucleoporins. The complex is
CC subsequently translocated through the pore by an energy requiring, Ran-
CC dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran
CC binding leads to release of the cargo. The importin is re-exported from
CC the nucleus to the cytoplasm where GTP hydrolysis releases Ran from
CC importin. 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.
CC {ECO:0000250|UniProtKB:P38217}.
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. Interacts with nucleoporins. {ECO:0000250|UniProtKB:P38217}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC envelope {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Severely impaired growth at 32 degrees Celsius.
CC {ECO:0000269|PubMed:15116432}.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-2
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB16272.1; -; Genomic_DNA.
DR PIR; T38539; T38539.
DR RefSeq; NP_594385.1; NM_001019806.2.
DR AlphaFoldDB; O14089; -.
DR SMR; O14089; -.
DR BioGRID; 278527; 2.
DR STRING; 4896.SPAC2F3.06c.1; -.
DR MaxQB; O14089; -.
DR PaxDb; O14089; -.
DR PRIDE; O14089; -.
DR EnsemblFungi; SPAC2F3.06c.1; SPAC2F3.06c.1:pep; SPAC2F3.06c.
DR GeneID; 2542046; -.
DR KEGG; spo:SPAC2F3.06c; -.
DR PomBase; SPAC2F3.06c; kap104.
DR VEuPathDB; FungiDB:SPAC2F3.06c; -.
DR eggNOG; KOG2023; Eukaryota.
DR HOGENOM; CLU_008136_1_0_1; -.
DR InParanoid; O14089; -.
DR OMA; MFPLLEC; -.
DR PhylomeDB; O14089; -.
DR Reactome; R-SPO-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR PRO; PR:O14089; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
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:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006606; P:protein import into nucleus; ISO:PomBase.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Cytoplasm; mRNA transport; Nucleus; Protein transport; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..910
FT /note="Importin subunit beta-2"
FT /id="PRO_0000120769"
FT REPEAT 12..39
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT DOMAIN 34..122
FT /note="Importin N-terminal"
FT /evidence="ECO:0000305"
FT REPEAT 44..82
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 93..126
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 132..169
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 177..207
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 220..247
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 259..286
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 302..406
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 414..442
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 454..481
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 499..532
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 540..573
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 581..619
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 627..677
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 690..721
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 729..764
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 772..807
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 815..848
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 857..888
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REGION 333..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..381
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 910 AA; 101718 MW; 4939CD9B09877208 CRC64;
MGDNPWVLQE QVLVELSEVI KNSLSENSQT RNAALNLLEK AKDIPDLNNY LTCILINATE
LSVSIRSAAG LLLKNNVRVS SLESGSGLQS LDYTKSTVIR GLCDPEQLIR GISGNVITTI
ISRWGISTWP EVLPQLMEML SSPASTTQEG AFSALTKICE DSAQELDRDF NGTRPLDFMI
PRFIELARHE NPKIRTDALF CLNQFVLIQS QSLYAHIDTF LETCYALATD VSPNVRKNVC
QALVYLLDVR PDKIAPSLGS IVEYMLYSTQ DSDQNVALEA CEFWLAIAEQ PDLCSALGPY
LDKIVPMLLQ GMVYSDMDLL LLGNDADDYD VEDREEDIRP QHAKGKSRIT LNTQGPITQQ
GSSNADADEL EDEDEDDDEF DEDDDAFMDW NLRKCSAAAL DVLSSFWKQR LLEIILPHLK
QSLTSEDWKV QEAGVLAVGA IAEGCMDGMV QYLPELYPYF LSLLDSKKPL VRTITCWTLG
RYSKWASCLE SEEDRQKYFV PLLQGLLRMV VDNNKKVQEA GCSAFAILEE QAGPSLVPYL
EPILTNLAFA FQKYQRKNVL ILYDAVQTLA DYVGSALNDK RYIELLITPL LQKWSMIPDD
DPNLFPLFEC LSSVAVALRD GFAPFAAETY ARTFRILRNT LYLITTAQND PTVDVPDRDF
LVTTLDLVSG IIQALGSQVS PLLAQADPPL GQIIGICAKD EVPEVRQSAY ALLGDMCMYC
FDQIRPYCDA LLVDMLPQMQ LPLLHVSASN NAIWSAGEMA LQLGKDMQQW VKPLLERLIC
ILKSKKSNTT VLENVAITIG RLGVYNPELV APHLELFYQP WFEIIKTVGE NEEKDSAFRG
FCNILACNPQ ALSYLLPMFV LCVAEYENPS AELRDMFQKI LQGSVELFNG KASWQASPEV
LAQIQAQYGV
