KA120_YEAST
ID KA120_YEAST Reviewed; 1032 AA.
AC Q02932; D6W3P2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Importin beta-like protein KAP120;
DE AltName: Full=Karyopherin-120;
GN Name=KAP120; OrderedLocusNames=YPL125W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 ASSOCIATION WITH THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [4]
RP FUNCTION.
RX PubMed=11071906; DOI=10.1091/mbc.11.11.3777;
RA Stage-Zimmermann T., Schmidt U., Silver P.A.;
RT "Factors affecting nuclear export of the 60S ribosomal subunit in vivo.";
RL Mol. Biol. Cell 11:3777-3789(2000).
RN [5]
RP FUNCTION.
RX PubMed=12829295; DOI=10.1016/s0378-1097(03)00384-7;
RA Zettel M.F., Garza L.R., Cass A.M., Myhre R.A., Haizlip L.A., Osadebe S.N.,
RA Sudimack D.W., Pathak R., Stone T.L., Polymenis M.;
RT "The budding index of Saccharomyces cerevisiae deletion strains identifies
RT genes important for cell cycle progression.";
RL FEMS Microbiol. Lett. 223:253-258(2003).
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 FUNCTION.
RX PubMed=16507575; DOI=10.1074/jbc.m600238200;
RA Bakhrat A., Baranes K., Krichevsky O., Rom I., Schlenstedt G.,
RA Pietrokovski S., Raveh D.;
RT "Nuclear import of Ho endonuclease utilizes two nuclear localization
RT signals and four importins of the ribosomal import system.";
RL J. Biol. Chem. 281:12218-12226(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH GSP1 AND RFP1.
RX PubMed=16581791; DOI=10.1128/mcb.26.8.3170-3180.2006;
RA Caesar S., Greiner M., Schlenstedt G.;
RT "Kap120 functions as a nuclear import receptor for ribosome assembly factor
RT Rpf1 in yeast.";
RL Mol. Cell. Biol. 26:3170-3180(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals (NLS) in
CC cargo substrates. Thought to mediate docking of the importin/substrate
CC complex to the nuclear pore complex (NPC) through binding to
CC nucleoporin and the complex is subsequently translocated through the
CC pore by an energy requiring, RAN-dependent mechanism. Required for
CC nuclear import of Ho endonuclease and RFP1, and involved in rRNA-
CC processing and assembly or export of 60S ribosomal subunits.
CC {ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:12829295,
CC ECO:0000269|PubMed:16507575, ECO:0000269|PubMed:16581791}.
CC -!- SUBUNIT: Interacts with GTP-bound GSP1 and RFP1. Associates with the
CC nuclear pore complex. {ECO:0000269|PubMed:16581791}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 6300 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; U43503; AAB68237.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11308.1; -; Genomic_DNA.
DR PIR; S61997; S61997.
DR RefSeq; NP_015200.1; NM_001183939.1.
DR PDB; 6FVB; X-ray; 3.30 A; A=2-1032.
DR PDBsum; 6FVB; -.
DR AlphaFoldDB; Q02932; -.
DR SMR; Q02932; -.
DR BioGRID; 36056; 164.
DR DIP; DIP-4000N; -.
DR IntAct; Q02932; 12.
DR STRING; 4932.YPL125W; -.
DR iPTMnet; Q02932; -.
DR MaxQB; Q02932; -.
DR PaxDb; Q02932; -.
DR PRIDE; Q02932; -.
DR EnsemblFungi; YPL125W_mRNA; YPL125W; YPL125W.
DR GeneID; 855978; -.
DR KEGG; sce:YPL125W; -.
DR SGD; S000006046; KAP120.
DR VEuPathDB; FungiDB:YPL125W; -.
DR eggNOG; KOG1993; Eukaryota.
DR GeneTree; ENSGT00390000014071; -.
DR HOGENOM; CLU_003886_0_0_1; -.
DR InParanoid; Q02932; -.
DR OMA; SFHYVFH; -.
DR BioCyc; YEAST:G3O-34024-MON; -.
DR PRO; PR:Q02932; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02932; 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: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: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; Nucleus; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1032
FT /note="Importin beta-like protein KAP120"
FT /id="PRO_0000255954"
FT DOMAIN 31..103
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:6FVB"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 106..122
FT /evidence="ECO:0007829|PDB:6FVB"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:6FVB"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 185..201
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 213..228
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 238..258
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 269..284
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 295..308
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:6FVB"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 324..344
FT /evidence="ECO:0007829|PDB:6FVB"
FT TURN 358..362
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 363..370
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 374..387
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 393..401
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 419..433
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 439..447
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 458..472
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 483..489
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 491..496
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 503..520
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 526..542
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 546..560
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 571..583
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 585..588
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 592..608
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 615..634
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 636..638
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 639..656
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 660..663
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 664..674
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 682..698
FT /evidence="ECO:0007829|PDB:6FVB"
FT TURN 702..704
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 710..714
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 717..722
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 726..728
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 729..742
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 745..750
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 752..763
FT /evidence="ECO:0007829|PDB:6FVB"
FT TURN 764..767
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 770..786
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 794..801
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 804..812
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 814..816
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 820..835
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 838..850
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 855..860
FT /evidence="ECO:0007829|PDB:6FVB"
FT TURN 863..865
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 871..875
FT /evidence="ECO:0007829|PDB:6FVB"
FT TURN 876..879
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 880..892
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 896..910
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 915..919
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 921..934
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 939..941
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 944..946
FT /evidence="ECO:0007829|PDB:6FVB"
FT STRAND 947..949
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 956..958
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 964..976
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 978..981
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 984..998
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 1001..1010
FT /evidence="ECO:0007829|PDB:6FVB"
FT HELIX 1013..1023
FT /evidence="ECO:0007829|PDB:6FVB"
SQ SEQUENCE 1032 AA; 119623 MW; 493EDA2B43298F10 CRC64;
MASSLNELNL VQVLEQASNP QHIRSDVQKL AEQQLRQWET QAGFHYLLQS IYLNLSNSLQ
IRWLAVIQFK NGVDKYWRST RINAIPKDEK ASIRGRLFEM IDEQNNQLCI QNAQASARIA
RLDFPVEWPT LFEDLENLLN DEIIRKDSVK IYNILMHINQ IVKVLGTARI GRCRPAMQSK
VPLILPLIVR IYLQSFEEWT TSSNLNYEDL SSLQVSYLAL KVLRRIICEG YDRPQTDQSV
CDFIKLSVSH FEMLISNHEN FKKFDIYEKF IKCLGKLYFN LVTGSPANFI LLPCSTQILI
TYTRLIFDKA PKVYRENSDV TGDFWEQTAI RGLLILKRVI NFIHKKGAIT LKARSDKLTI
DASINKINTE FLNENLITRL VDTLMEWYLR LRPTELENWF MDPEEWINEQ MATSYEYQIR
PCAENVFQDL MNTFSELLVP YLLKKIENDA SKLSNSLDDF LRKDAIYASF QLSASAVSEM
VDFDRLLIQV FLPEATNTNI SGDELRIIRR RVALIINEWS TVKCSEESKS LCYKLFTNFL
TDEDDKVVLL TTVQTVRTMV DDWNFNKDTF QPFLTENVHL LLRKILPSVS LTETRLYVLN
TLSDIIIQTK PLISRDLLVE ILQIIPNLWE IATNNASEAI LANALLRLLR NLVSSLGSQS
HLTWDIAIPV VALACDPSSM QYQLLSEDGY ELWGMLLQNF SSHDQEFDDK FVELVPFLKY
GIETHTEILP TLLEIIKSYA LILNPVDFFS NNTFQDIFKQ MSKYLLKLRE DSFQLVLEIW
EILILSNESD YENLLLQKFY ETGVLSALFD AIFLEEAPSS YLCSQIIQII ARISYVNPDA
LMTFLATYHD NLPTSNENAR MPESIRKIVS KDQTYDSVVN KLLTGWIVCF RDIFDPKFKK
VHILGISSLL RTGLVPILTE FSSIASLWIE MLEEINETNR GDCEKYHLND IVTEQSIAFH
PLTAEQLRYH QLCKNNDPVH NISLKDFISQ SMEYLESHLG VERYQEFLKT INPSLLENLQ
MFLSIQPQEA RP
