IMA2_SCHPO
ID IMA2_SCHPO Reviewed; 539 AA.
AC O94374;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Importin subunit alpha-2;
DE AltName: Full=Importin-1;
DE AltName: Full=Karyopherin subunit alpha-2;
GN Name=imp1; ORFNames=SPBC1604.08c;
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 FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=12237855; DOI=10.1002/yea.902;
RA Tallada V.A., Daga R.R., Palomeque C., Garzon A., Jimenez J.;
RT "Genome-wide search of Schizosaccharomyces pombe genes causing
RT overexpression-mediated cell cycle defects.";
RL Yeast 19:1139-1151(2002).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [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: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. Active directional transport is assured by both, a Phe-Gly
CC (FG) repeat affinity gradient for these transport factors across the
CC NPC and a transport cofactor concentration gradient across the nuclear
CC envelope. Involved in nuclear protein import. Required for efficient
CC nuclera import of both an SV40 nuclear localization signal-containing
CC reporter protein and the pap1 component of the stress response MAP
CC kinase pathway. Required for proper mitotic progression.
CC {ECO:0000269|PubMed:12237855, ECO:0000269|PubMed:15116432,
CC ECO:0000269|PubMed:15937127}.
CC -!- SUBUNIT: Interacts with pap1. {ECO:0000269|PubMed:15937127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=Nucleus;
CC nucleolus; nuclear rim.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22341.1; -; Genomic_DNA.
DR PIR; T39506; T39506.
DR RefSeq; NP_596632.1; NM_001022553.2.
DR AlphaFoldDB; O94374; -.
DR SMR; O94374; -.
DR BioGRID; 276472; 192.
DR IntAct; O94374; 1.
DR STRING; 4896.SPBC1604.08c.1; -.
DR iPTMnet; O94374; -.
DR MaxQB; O94374; -.
DR PaxDb; O94374; -.
DR PRIDE; O94374; -.
DR EnsemblFungi; SPBC1604.08c.1; SPBC1604.08c.1:pep; SPBC1604.08c.
DR GeneID; 2539928; -.
DR KEGG; spo:SPBC1604.08c; -.
DR PomBase; SPBC1604.08c; imp1.
DR VEuPathDB; FungiDB:SPBC1604.08c; -.
DR eggNOG; KOG0166; Eukaryota.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; O94374; -.
DR OMA; MTEMIFS; -.
DR PhylomeDB; O94374; -.
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:O94374; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
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:0005643; C:nuclear pore; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IDA: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; IDA:PomBase.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0140516; P:mitotic nuclear pore complex disassembly; IMP:PomBase.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:PomBase.
DR GO; GO:0006606; P:protein import into nucleus; IDA:PomBase.
DR GO; GO:1905557; P:regulation of mitotic nuclear envelope disassembly; IMP: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; 4.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..539
FT /note="Importin subunit alpha-2"
FT /id="PRO_0000290665"
FT DOMAIN 1..57
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 110..149
FT /note="ARM 1"
FT REPEAT 152..191
FT /note="ARM 2"
FT REPEAT 194..235
FT /note="ARM 3"
FT REPEAT 238..277
FT /note="ARM 4"
FT REPEAT 280..319
FT /note="ARM 5"
FT REPEAT 322..361
FT /note="ARM 6"
FT REPEAT 364..403
FT /note="ARM 7"
FT REPEAT 409..448
FT /note="ARM 8"
SQ SEQUENCE 539 AA; 59853 MW; FFD4919E936E0941 CRC64;
MESRYLSDRR SRFKSKGVFK ADELRRQREE QQIEIRKQKR EESLNKRRNL NAVLQNDIDV
EEEADQSQVQ MEQQMKDEFP KLTADVMSDD IELQLGAVTK FRKYLSKETH PPIDQVIACG
VVDRFVQFLE SEHHLLQFEA AWALTNIASG TTDQTRIVVD SGAVPRFIQL LSSPEKDVRE
QVVWALGNIA GDSSACRDYV LGNGVLQPLL NILQSSASDV SMLRNATWTL SNLCRGKNPP
PNWSTISVAV PILAKLLYSE DVEIIVDACW AISYLSDGPN EKIGAILDVG CAPRLVELLS
SPSVNIQTPA LRSVGNIVTG TDAQTQIIID CGALNAFPSL LSHQKENIRK EACWTISNIT
AGNTQQIQAI IESNLIPPLV HLLSYADYKT KKEACWAISN ATSGGLGQPD QIRYLVSQGV
IKPLCDMLNG SDNKIIQVAL DAIENILKVG EMDRTMDLEN INQYAVYVEE AGGMDMIHDL
QSSGNNDIYL KAYSIIEKYF SDEDAVEDLA PETENGAFTF GNGPQAQGEF KFDSQDMAM
