IMB4_YEAST
ID IMB4_YEAST Reviewed; 1113 AA.
AC P40069; D3DM16;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Importin subunit beta-4 {ECO:0000305};
DE AltName: Full=Importin-123;
DE AltName: Full=Karyopherin subunit beta-4 {ECO:0000305};
DE AltName: Full=Karyopherin-123 {ECO:0000303|PubMed:8849456};
DE AltName: Full=Ran-binding protein YRB4 {ECO:0000303|PubMed:9321403};
GN Name=KAP123 {ECO:0000303|PubMed:8849456};
GN Synonyms=YRB4 {ECO:0000303|PubMed:9321403};
GN OrderedLocusNames=YER110C {ECO:0000312|SGD:S000000912};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP GENE NAME.
RX PubMed=8849456; DOI=10.1126/science.274.5287.624;
RA Aitchison J.D., Blobel G., Rout M.P.;
RT "Kap104p: a karyopherin involved in the nuclear transport of messenger RNA
RT binding proteins.";
RL Science 274:624-627(1996).
RN [4]
RP PROTEIN SEQUENCE OF 895-903 AND 1073-1099, FUNCTION, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH GSP1 AND RPL25.
RX PubMed=9321403; DOI=10.1093/emboj/16.20.6237;
RA Schlenstedt G., Smirnova E., Deane R., Solsbacher J., Kutay U.,
RA Goerlich D., Ponstingl H., Bischoff F.R.;
RT "Yrb4p, a yeast ran-GTP-binding protein involved in import of ribosomal
RT protein L25 into the nucleus.";
RL EMBO J. 16:6237-6249(1997).
RN [5]
RP FUNCTION.
RX PubMed=9182759; DOI=10.1016/s0092-8674(00)80254-8;
RA Rout M.P., Blobel G., Aitchison J.D.;
RT "A distinct nuclear import pathway used by ribosomal proteins.";
RL Cell 89:715-725(1997).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9238021; DOI=10.1073/pnas.94.16.8590;
RA Seedorf M., Silver P.A.;
RT "Importin/karyopherin protein family members required for mRNA export from
RT the nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8590-8595(1997).
RN [7]
RP REVIEW.
RX PubMed=11423015; DOI=10.1186/gb-2001-2-6-reviews3008;
RA Stroem A.C., Weis K.;
RT "Importin-beta-like nuclear transport receptors.";
RL Genome Biol. 2:REVIEWS3008.1-REVIEWS3008.9(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH YAP1.
RX PubMed=11274141; DOI=10.1074/jbc.m009258200;
RA Isoyama T., Murayama A., Nomoto A., Kuge S.;
RT "Nuclear import of the yeast AP-1-like transcription factor Yap1p is
RT mediated by transport receptor Pse1p, and this import step is not affected
RT by oxidative stress.";
RL J. Biol. Chem. 276:21863-21869(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH HISTONES H3 AND H4.
RX PubMed=11694505; DOI=10.1074/jbc.m106845200;
RA Mosammaparast N., Guo Y., Shabanowitz J., Hunt D.F., Pemberton L.F.;
RT "Pathways mediating the nuclear import of histones H3 and H4 in yeast.";
RL J. Biol. Chem. 277:862-868(2002).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [11]
RP FUNCTION.
RX PubMed=12612077; DOI=10.1128/mcb.23.6.2042-2054.2003;
RA Sydorskyy Y., Dilworth D.J., Yi E.C., Goodlett D.R., Wozniak R.W.,
RA Aitchison J.D.;
RT "Intersection of the Kap123p-mediated nuclear import and ribosome export
RT pathways.";
RL Mol. Cell. Biol. 23:2042-2054(2003).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP REPEAT STRUCTURE.
RX PubMed=23541588; DOI=10.1016/j.jmb.2013.02.035;
RA Kobayashi J., Matsuura Y.;
RT "Structural basis for cell-cycle-dependent nuclear import mediated by the
RT karyopherin Kap121p.";
RL J. Mol. Biol. 425:1852-1868(2013).
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals (NLS) in
CC cargo substrates. Its predominant cargo substrate seems to be ribosomal
CC proteins (PubMed:9321403). Required for import of the ribosomal
CC assembly factor NMD3 (PubMed:12612077). May be involved in nuclear
CC transport of YAP1 (PubMed:11274141). Mediates the nuclear import of
CC histones H3 and H4 (PubMed:11694505). Mediates docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) through
CC binding to repeat-containing nucleoporins. The complex is subsequently
CC translocated through the pore by an energy requiring, Ran-dependent
CC mechanism (PubMed:11423015). At the nucleoplasmic side of the NPC, GTP-
CC Ran binding leads to release of the cargo (PubMed:9321403). 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
CC (PubMed:11423015). {ECO:0000269|PubMed:11274141,
CC ECO:0000269|PubMed:12612077, ECO:0000269|PubMed:9321403,
CC ECO:0000305|PubMed:11423015}.
CC -!- SUBUNIT: Interacts with Ran (GSP1); interacts specifically with the
CC GTP-bound form of Ran (GTP-Ran), protecting it from GTP hydrolysis and
CC nucleotide exchange (PubMed:9321403). Interacts with RPL25; this
CC interaction is dissociated by binding to Ran-GTP (PubMed:9321403).
CC Interacts with YAP1 (PubMed:11274141). Interacts with histones H3 and
CC H4; via their NLS (PubMed:11694505). {ECO:0000269|PubMed:11274141,
CC ECO:0000269|PubMed:11694505, ECO:0000269|PubMed:9321403}.
CC -!- INTERACTION:
CC P40069; P52919: NBP1; NbExp=6; IntAct=EBI-9166, EBI-11886;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9238021,
CC ECO:0000269|PubMed:9321403}. Nucleus {ECO:0000269|PubMed:9238021,
CC ECO:0000269|PubMed:9321403}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:9321403}.
CC -!- MISCELLANEOUS: Present with 38300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
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DR EMBL; U18916; AAC03208.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07770.1; -; Genomic_DNA.
DR PIR; S50613; S50613.
DR RefSeq; NP_011035.1; NM_001179000.1.
DR AlphaFoldDB; P40069; -.
DR SMR; P40069; -.
DR BioGRID; 36855; 379.
DR DIP; DIP-2356N; -.
DR IntAct; P40069; 201.
DR MINT; P40069; -.
DR STRING; 4932.YER110C; -.
DR CarbonylDB; P40069; -.
DR iPTMnet; P40069; -.
DR MaxQB; P40069; -.
DR PaxDb; P40069; -.
DR PRIDE; P40069; -.
DR EnsemblFungi; YER110C_mRNA; YER110C; YER110C.
DR GeneID; 856846; -.
DR KEGG; sce:YER110C; -.
DR SGD; S000000912; KAP123.
DR VEuPathDB; FungiDB:YER110C; -.
DR eggNOG; KOG2171; Eukaryota.
DR GeneTree; ENSGT00550000075074; -.
DR HOGENOM; CLU_003794_1_1_1; -.
DR InParanoid; P40069; -.
DR OMA; VRGNAAY; -.
DR BioCyc; YEAST:G3O-30274-MON; -.
DR PRO; PR:P40069; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40069; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:SGD.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:SGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IDA:SGD.
DR GO; GO:2000220; P:regulation of pseudohyphal growth; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport.
FT CHAIN 1..1113
FT /note="Importin subunit beta-4"
FT /id="PRO_0000120776"
FT REPEAT 3..35
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT DOMAIN 25..92
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 40..74
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 92..115
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 120..147
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 157..191
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 208..244
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 252..287
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 296..348
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 350..384
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 388..428
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 430..469
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 472..513
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 515..558
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 560..605
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 607..680
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 683..737
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 744..783
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 790..856
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 859..894
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 902..934
FT /note="HEAT 20"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 942..991
FT /note="HEAT 21"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 999..1030
FT /note="HEAT 22"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 1049..1084
FT /note="HEAT 23"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT REPEAT 1085..1110
FT /note="HEAT 24"
FT /evidence="ECO:0000250|UniProtKB:P32337,
FT ECO:0000305|PubMed:23541588"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1113 AA; 122601 MW; 9DC524C28BB71A46 CRC64;
MDQQFLSQLE QTLHAITSGV GLKEATKTLQ TQFYTQPTTL PALIHILQNG SDDSLKQLAG
VEARKLVSKH WNAIDESTRA SIKTSLLQTA FSEPKENVRH SNARVIASIG TEELDGNKWP
DLVPNLIQTA SGEDVQTRQT AIFILFSLLE DFTSSLSGHI DDFLALFSQT INDPSSLEIR
SLSAQALNHV SALIEEQETI NPVQAQKFAA SIPSVVNVLD AVIKADDTMN AKLIFNCLND
FLLLDSQLTG NFIVDLIKLS LQIAVNSEID EDVRVFALQF IISSLSYRKS KVSQSKLGPE
ITVAALKVAC EEIDVDDELN NEDETGENEE NTPSSSAIRL LAFASSELPP SQVASVIVEH
IPAMLQSANV FERRAILLAI SVAVTGSPDY ILSQFDKIIP ATINGLKDTE PIVKLAALKC
IHQLTTDLQD EVAKFHEEYL PLIIDIIDSA KNIVIYNYAT VALDGLLEFI AYDAIAKYLD
PLMNKLFYML ESNESSKLRC AVVSAIGSAA FAAGSAFIPY FKTSVHYLEK FIQNCSQIEG
MSEDDIELRA NTFENISTMA RAVRSDAFAE FAEPLVNSAY EAIKTDSARL RESGYAFIAN
LAKVYGENFA PFLKTILPEI FKTLELDEYQ FNFDGDAEDL AAFADSANEE ELQNKFTVNT
GISYEKEVAS AALSELALGT KEHFLPYVEQ SLKVLNEQVD ESYGLRETAL NTIWNVVKSV
LLASKVEPES YPKGIPASSY VNADVLAVIQ AARETSMGNL SDEFETSMVI TVMEDFANMI
KQFGAIIIMD NGDSSMLEAL CMQVLSVLKG THTCQTIDIE EDVPRDEELD ASETEATLQD
VALEVLVSLS QALAGDFAKV FDNFRPVVFG LFQSKSKNKR SSAVGAASEL ALGMKEQNPF
VHEMLEALVI RLTSDKSLEV RGNAAYGVGL LCEYASMDIS AVYEPVLKAL YELLSAADQK
ALAAEDDEAT REIIDRAYAN ASGCVARMAL KNSALVPLEQ TVPALLAHLP LNTGFEEYNP
IFELIMKLYQ ENSPVITNET PRIIEIFSAV FTKENDRIKL EKESTLGREE NMERLKQFQT
EEMKHKVIEL LKYLNTTYNG IVAQNPVLAA VIA
