IMA1_SCHPO
ID IMA1_SCHPO Reviewed; 542 AA.
AC O14063; Q9UTV5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Importin subunit alpha-1;
DE AltName: Full=Cell untimely torn protein 15;
DE AltName: Full=Karyopherin subunit alpha-1;
DE AltName: Full=Serine-rich RNA polymerase I suppressor protein;
GN Name=cut15; ORFNames=SPCC962.03c;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9740803; DOI=10.1016/s0960-9822(07)00425-3;
RA Matsusaka T., Imamoto N., Yoneda Y., Yanagida M.;
RT "Mutations in fission yeast Cut15, an importin alpha homolog, lead to
RT mitotic progression without chromosome condensation.";
RL Curr. Biol. 8:1031-1034(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-199, 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 [4]
RP FUNCTION, INTERACTION WITH PAP1, AND SUBCELLULAR LOCATION.
RX PubMed=15937127; DOI=10.1534/genetics.105.042598;
RA Umeda M., Izaddoost S., Cushman I., Moore M.S., Sazer S.;
RT "The fission yeast Schizosaccharomyces pombe has two importin-alpha
RT proteins, Imp1p and Cut15p, which have common and unique functions in
RT nucleocytoplasmic transport and cell cycle progression.";
RL Genetics 171:7-21(2005).
RN [5]
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: Binds specifically and directly to substrates containing
CC either a simple or bipartite NLS motif. Promotes docking of import
CC substrates to the nuclear envelope. Seems to act as a cytosolic
CC receptor for both simple and bipartite NLS motifs. Has an essential
CC role in mitotic chromosome condensation. Involved in nuclear protein
CC import. Required for efficient nuclear import of both an SV40 nuclear
CC localization signal-containing reporter protein and the pap1 component
CC of the stress response MAP kinase pathway. Required for proper mitotic
CC progression. {ECO:0000269|PubMed:15937127, ECO:0000269|PubMed:9740803}.
CC -!- SUBUNIT: Interacts with pap1. {ECO:0000269|PubMed:15937127}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:15937127, ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:9740803}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; AB010574; BAA24518.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20435.1; -; Genomic_DNA.
DR EMBL; AB027972; BAA87276.1; -; Genomic_DNA.
DR PIR; T41650; T41650.
DR RefSeq; NP_587868.1; NM_001022860.2.
DR AlphaFoldDB; O14063; -.
DR SMR; O14063; -.
DR BioGRID; 275991; 15.
DR IntAct; O14063; 1.
DR STRING; 4896.SPCC962.03c.1; -.
DR MaxQB; O14063; -.
DR PaxDb; O14063; -.
DR EnsemblFungi; SPCC962.03c.1; SPCC962.03c.1:pep; SPCC962.03c.
DR GeneID; 2539426; -.
DR KEGG; spo:SPCC962.03c; -.
DR PomBase; SPCC962.03c; cut15.
DR VEuPathDB; FungiDB:SPCC962.03c; -.
DR eggNOG; KOG0166; Eukaryota.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; O14063; -.
DR OMA; EMIQMLY; -.
DR PhylomeDB; O14063; -.
DR Reactome; R-SPO-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-SPO-68616; Assembly of the ORC complex at the origin of replication.
DR PRO; PR:O14063; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA: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; IDA:PomBase.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:PomBase.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IDA:PomBase.
DR Gene3D; 1.20.5.690; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032413; Arm_3.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR036975; Importin-a_IBB_sf.
DR InterPro; IPR024931; Importin_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF16186; Arm_3; 1.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Nucleus; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..542
FT /note="Importin subunit alpha-1"
FT /id="PRO_0000120743"
FT DOMAIN 1..60
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 114..155
FT /note="ARM 1"
FT REPEAT 156..197
FT /note="ARM 2"
FT REPEAT 198..240
FT /note="ARM 3"
FT REPEAT 241..282
FT /note="ARM 4"
FT REPEAT 283..324
FT /note="ARM 5"
FT REPEAT 325..366
FT /note="ARM 6"
FT REPEAT 367..408
FT /note="ARM 7"
FT REPEAT 409..453
FT /note="ARM 8"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 60425 MW; 57F5EF5A2E55FE30 CRC64;
MSASSRFIPE HRRQNYKGKG TFQADELRRR RETQQIEIRK QKREENLNKR RNLVDVQEPA
EETIPLEQDK ENDLELELQL PDLLKALYSD DIEAQIQATA KFRKALSKET NPPIQKVIDA
GVVPRFVEFL SHENNLLKFE ASWALTNVAS GSSNQTHVVV EANAVPVFVS LLSSSEQDVR
EQAVWALGNI AGDSPMCRDH VLQCGVLEPL LNIIESNRRL SMLRNSTWTL SNMCRGKNPQ
PDWNSISQVI PVLSKLIYTL DEDVLVDALW AISYLSDGAN EKIQAIIDAG IPRRLVELLM
HPSAQVQTPA LRSVGNIVTG DDVQTQVIIN CGALSALLSL LSSPRDGVRK EACWTISNIT
AGNSSQIQYV IEANIIPPLI HLLTTADFKI QKEACWAISN ATSGGARRPD QIRYLVEQGA
IKPLCNLLAC QDNKIIQVAL DGIENILRVG ELDRANNPDK INLYAVYVED AGGMDLIHEC
QNSSNSEIYQ KAYNIIEKFF GEEDEIEELE PETVGDTFTF GTTQEPAGDF QFSATNAEDM
AM
