IMB5_YEAST
ID IMB5_YEAST Reviewed; 1004 AA.
AC P53067; D6VV94;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Importin subunit beta-5;
DE AltName: Full=114 kDa karyopherin;
DE AltName: Full=Karyopherin subunit beta-5;
DE AltName: Full=Karyopherin-114;
GN Name=KAP114; OrderedLocusNames=YGL241W; ORFNames=HRC1004;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8750240; DOI=10.1002/yea.320111507;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left
RT arm of chromosome VII, reveals the presence of eight open reading frames.";
RL Yeast 11:1519-1523(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
RP FUNCTION IN TBP IMPORT.
RX PubMed=10535958; DOI=10.1073/pnas.96.22.12542;
RA Morehouse H., Buratowski R.M., Silver P.A., Buratowski S.;
RT "The importin/karyopherin Kap114 mediates the nuclear import of TATA-
RT binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12542-12547(1999).
RN [5]
RP FUNCTION IN HISTONE H2A/H2B IMPORT.
RX PubMed=11309407; DOI=10.1083/jcb.153.2.251;
RA Mosammaparast N., Jackson K.R., Guo Y., Brame C.J., Shabanowitz J.,
RA Hunt D.F., Pemberton L.F.;
RT "Nuclear import of histone H2A and H2B is mediated by a network of
RT karyopherins.";
RL J. Cell Biol. 153:251-262(2001).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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 [8]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for nuclear protein import and mediates docking of
CC import substrate to distinct nucleoporins. Serves a receptor for
CC nuclear localization signals. Mediates the nuclear import of TATA-
CC binding protein (TBP) and of histones H2A and H2B.
CC {ECO:0000269|PubMed:10535958, ECO:0000269|PubMed:11309407}.
CC -!- SUBUNIT: Interacts with NAP1. {ECO:0000269|PubMed:18086883}.
CC -!- INTERACTION:
CC P53067; P32835: GSP1; NbExp=3; IntAct=EBI-9174, EBI-7926;
CC P53067; P38632: MMS21; NbExp=2; IntAct=EBI-9174, EBI-11017;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus,
CC nuclear pore complex {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
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DR EMBL; Z49149; CAA89014.1; -; Genomic_DNA.
DR EMBL; Z72763; CAA96960.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07878.1; -; Genomic_DNA.
DR PIR; S53939; S53939.
DR RefSeq; NP_011273.1; NM_001181107.1.
DR PDB; 6AHO; X-ray; 2.50 A; A=1-1004.
DR PDBsum; 6AHO; -.
DR AlphaFoldDB; P53067; -.
DR SMR; P53067; -.
DR BioGRID; 32999; 112.
DR DIP; DIP-5881N; -.
DR IntAct; P53067; 24.
DR MINT; P53067; -.
DR STRING; 4932.YGL241W; -.
DR iPTMnet; P53067; -.
DR MaxQB; P53067; -.
DR PaxDb; P53067; -.
DR PRIDE; P53067; -.
DR EnsemblFungi; YGL241W_mRNA; YGL241W; YGL241W.
DR GeneID; 852610; -.
DR KEGG; sce:YGL241W; -.
DR SGD; S000003210; KAP114.
DR VEuPathDB; FungiDB:YGL241W; -.
DR eggNOG; KOG2274; Eukaryota.
DR GeneTree; ENSGT00390000008224; -.
DR HOGENOM; CLU_008920_1_1_1; -.
DR InParanoid; P53067; -.
DR OMA; CLRAPPV; -.
DR BioCyc; YEAST:G3O-30713-MON; -.
DR PRO; PR:P53067; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53067; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
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; IMP: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 Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..1004
FT /note="Importin subunit beta-5"
FT /id="PRO_0000120778"
FT DOMAIN 21..100
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:6AHO"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 51..68
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 105..126
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 187..205
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 243..263
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 271..289
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 304..320
FT /evidence="ECO:0007829|PDB:6AHO"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 346..354
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 356..363
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 372..380
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 385..400
FT /evidence="ECO:0007829|PDB:6AHO"
FT TURN 401..404
FT /evidence="ECO:0007829|PDB:6AHO"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:6AHO"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 431..447
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 453..469
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 477..494
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 498..514
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 523..541
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 546..561
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 571..587
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 592..605
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 611..634
FT /evidence="ECO:0007829|PDB:6AHO"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 641..654
FT /evidence="ECO:0007829|PDB:6AHO"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 665..681
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 685..700
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 704..707
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 708..710
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 711..722
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 728..731
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 735..744
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 746..749
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 750..752
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 753..766
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 770..786
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 788..795
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 805..817
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 823..837
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 842..846
FT /evidence="ECO:0007829|PDB:6AHO"
FT STRAND 848..854
FT /evidence="ECO:0007829|PDB:6AHO"
FT STRAND 873..878
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 879..895
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 965..979
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 981..983
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 984..990
FT /evidence="ECO:0007829|PDB:6AHO"
FT HELIX 993..1002
FT /evidence="ECO:0007829|PDB:6AHO"
SQ SEQUENCE 1004 AA; 113921 MW; 1F4C02AA6AB2FF39 CRC64;
MDINELIIGA QSADKHTREV AETQLLQWCD SDASQVFKAL ANVALQHEAS LESRQFALLS
LRKLITMYWS PGFESYRSTS NVEIDVKDFI REVLLKLCLN DNENTKIKNG ASYCIVQISA
VDFPDQWPQL LTVIYDAISH QHSLNAMSLL NEIYDDVVSE EMFFEGGIGL ATMEIVFKVL
NTETSTLIAK IAALKLLKAC LLQMSSHNEY DEASRKSFVS QCLATSLQIL GQLLTLNFGN
VDVISQLKFK SIIYENLVFI KNDFSRKHFS SELQKQFKIM AIQDLENVTH INANVETTES
EPLLETVHDC SIYIVEFLTS VCTLQFSVEE MNKIITSLTI LCQLSSETRE IWTSDFNTFV
SKETGLAASY NVRDQANEFF TSLPNPQLSL IFKVVSNDIE HSTCNYSTLE SLLYLLQCIL
LNDDEITGEN IDQSLQILIK TLENILVSQE IPELILARAI LTIPRVLDKF IDALPDIKPL
TSAFLAKSLN LALKSDKELI KSATLIAFTY YCYFAELDSV LGPEVCSETQ EKVIRIINQV
SSDAEEDTNG ALMEVLSQVI SYNPKEPHSR KEILQAEFHL VFTISSEDPA NVQVVVQSQE
CLEKLLDNIN MDNYKNYIEL CLPSFINVLD SNNANNYRYS PLLSLVLEFI TVFLKKKPND
GFLPDEINQY LFEPLAKVLA FSTEDETLQL ATEAFSYLIF NTDTRAMEPR LMDIMKVLER
LLSLEVSDSA AMNVGPLVVA IFTRFSKEIQ PLIGRILEAV VVRLIKTQNI STEQNLLSVL
CFLTCNDPKQ TVDFLSSFQI DNTDALTLVM RKWIEAFEVI RGEKRIKENI VALSNLFFLN
DKRLQKVVVN GNLIPYEGDL IITRSMAKKM PDRYVQVPLY TKIIKLFVSE LSFQSKQPNP
EQLITSDIKQ EVVNANKDDD NDDWEDVDDV LDYDKLKEYI DDDVDEEADD DSDDITGLMD
VKESVVQLLV RFFKEVASKD VSGFHCIYET LSDSERKVLS EALL
