SXM1_YEAST
ID SXM1_YEAST Reviewed; 944 AA.
AC Q04175; D6VT29;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Importin beta SMX1;
DE AltName: Full=Suppressor of mRNA export mutant protein 1;
DE AltName: Full=karyopherin-108;
GN Name=SXM1; Synonyms=KAP108; OrderedLocusNames=YDR395W;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION.
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LHP1; RPL16; ROL25;
RP RPL31A; NSP1; NUP1 AND NUP159.
RX PubMed=9412461; DOI=10.1083/jcb.139.7.1655;
RA Rosenblum J.S., Pemberton L.F., Blobel G.;
RT "A nuclear import pathway for a protein involved in tRNA maturation.";
RL J. Cell Biol. 139:1655-1661(1997).
RN [5]
RP FUNCTION, AND INTERACTION WITH LHP1 AND RPL11.
RX PubMed=9817748; DOI=10.1083/jcb.143.4.887;
RA Rosenblum J.S., Pemberton L.F., Bonifaci N., Blobel G.;
RT "Nuclear import and the evolution of a multifunctional RNA-binding
RT protein.";
RL J. Cell Biol. 143:887-899(1998).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NSP1; NUP116 AND NUP159.
RX PubMed=9891088; DOI=10.1128/mcb.19.2.1547;
RA Seedorf M., Damelin M., Kahana J., Taura T., Silver P.A.;
RT "Interactions between a nuclear transporter and a subset of nuclear pore
RT complex proteins depend on Ran GTPase.";
RL Mol. Cell. Biol. 19:1547-1557(1999).
RN [7]
RP FUNCTION.
RX PubMed=12684370; DOI=10.1128/ec.2.2.209-221.2003;
RA Nikolaev I., Cochet M.-F., Felenbok B.;
RT "Nuclear import of zinc binuclear cluster proteins proceeds through
RT multiple, overlapping transport pathways.";
RL Eukaryot. Cell 2:209-221(2003).
RN [8]
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 [9]
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 [10]
RP FUNCTION.
RX PubMed=15004228; DOI=10.1091/mbc.e03-11-0839;
RA Freedman N.D., Yamamoto K.R.;
RT "Importin 7 and importin alpha/importin beta are nuclear import receptors
RT for the glucocorticoid receptor.";
RL Mol. Biol. Cell 15:2276-2286(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH PAB1.
RX PubMed=15769879; DOI=10.1261/rna.7291205;
RA Brune C., Munchel S.E., Fischer N., Podtelejnikov A.V., Weis K.;
RT "Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the
RT cytoplasm and functions in mRNA export.";
RL RNA 11:517-531(2005).
RN [12]
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 [13]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Nuclear transport factor (karyopherin) involved in protein
CC transport between the cytoplasm and nucleoplasm. Required for the
CC nuclear import of ribosomal proteins (RPL11, RPL16, RPL25, RPL31A), the
CC poly(A)-binding protein PAB1, the HO endonuclease or the tRNA and snRNA
CC chaperone LHP1. Indirectly involved in nuclear mRNA export through its
CC PAB1 nuclear import activity. {ECO:0000269|PubMed:12684370,
CC ECO:0000269|PubMed:15004228, ECO:0000269|PubMed:15769879,
CC ECO:0000269|PubMed:16507575, ECO:0000269|PubMed:9238021,
CC ECO:0000269|PubMed:9412461, ECO:0000269|PubMed:9817748}.
CC -!- SUBUNIT: Associates with the nucleopore complex. Interacts with LHP1,
CC PAB1, RPL11, RPL16, RPL25, RPL31A in order to import them into the
CC nucleus. Interacts also with the nucleopore complex proteins
CC (nucleoporins) NSP1, NUP1, NUP116 and NUP159.
CC {ECO:0000269|PubMed:15769879, ECO:0000269|PubMed:9412461,
CC ECO:0000269|PubMed:9817748, ECO:0000269|PubMed:9891088}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nuclear pore complex.
CC -!- MISCELLANEOUS: Present with 16300 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; U32274; AAB64837.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12239.1; -; Genomic_DNA.
DR PIR; S69679; S69679.
DR RefSeq; NP_010683.3; NM_001180703.3.
DR AlphaFoldDB; Q04175; -.
DR SMR; Q04175; -.
DR BioGRID; 32457; 177.
DR DIP; DIP-1678N; -.
DR IntAct; Q04175; 31.
DR MINT; Q04175; -.
DR STRING; 4932.YDR395W; -.
DR iPTMnet; Q04175; -.
DR MaxQB; Q04175; -.
DR PaxDb; Q04175; -.
DR PRIDE; Q04175; -.
DR EnsemblFungi; YDR395W_mRNA; YDR395W; YDR395W.
DR GeneID; 852004; -.
DR KEGG; sce:YDR395W; -.
DR SGD; S000002803; SXM1.
DR VEuPathDB; FungiDB:YDR395W; -.
DR eggNOG; KOG1991; Eukaryota.
DR HOGENOM; CLU_004196_0_0_1; -.
DR InParanoid; Q04175; -.
DR OMA; TMTTMVM; -.
DR BioCyc; YEAST:G3O-29943-MON; -.
DR PRO; PR:Q04175; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04175; 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:0006406; P:mRNA export from nucleus; IGI: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 InterPro; IPR013713; XPO2_central.
DR Pfam; PF08506; Cse1; 1.
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 Cytoplasm; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..944
FT /note="Importin beta SMX1"
FT /id="PRO_0000269756"
FT DOMAIN 25..97
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
SQ SEQUENCE 944 AA; 108405 MW; 33D6E0524AF0568A CRC64;
MVQEQAILSC IEQTMVADAK IIKEAEQQLF EFQKQPGFTS FLLNIVSDDN FALNVRLSSA
IYLKNKIHRS WDTKREDGIK ADEKLSIKER LIETLVKNCE NNHIRPILTE TINGILVGQE
DWDLAPIIKN LLSSGDASYI YPGLLLLFQL CKAHRWDMVG SRDYIDSVIE ELFPIVEGIA
SNIGSQTDYR SNEILYLILK SFKYACLNNL PQYFSQPERI MSWVQLHLYL CSKPLPVEVM
ELDPADRSLD KRVKVNKWGF GNLNRFLQRY NKITKAITKE FIDYIFNTIV PIILREFFKD
IEAWGNNSLW LSDSSLYFLI SFLEKCVTID QLYPLIEPHL QIIFENVIFP CLCANEQSIE
LLEDDQEEYT RRYFDINREG STPDAASADF IFLIGSKRPE KLNNILPFIN DIFTRFDANS
SDINMAFKEE GALRTLSNLF SFIDEPSVLE NIFGHFIVPL LSQDKYMFLV ARSLETIALY
SEEFKDMNIL SQLFELTYTN FLNSNVLPVQ IEAADAIKCL IVSNPQIHPA VSAHVPGMME
KLLKLSKIFE IDILSEVMEA LVERFSDELS PFAKDLASNL VEQFLRIAQA LVENPSETYS
ASDQEQEIQA SGLLQTMTTM VMSMNKVPLI ESLAPVVKFV VLHAQISFIT EAVDLLDALT
ISSHLLYNQI APPIWELLHD ILDSFQTYAM DYFEAYSIFF ETIVMTGFPQ DQTYVQPLLE
ILSAKLESEV DYDIEHVMQI LMYFALSMRD IPLFSKAIKV STNDELGLDS KCIVKLGLAN
LFAKPIETLQ IMENEGFTIN FFTNWFNEKF YSVFAIKLQV LVILTLLKMP EVPNSVSPLL
NNLTNKLVEL TLSLPKAIRN RDAVTEGKSL EGDLTPEEEE EYFIECDDDM KETVLDQINV
FQEVHTFFKN LQNEDAGKYE KIINYLDESK RDSLQVILEF VSQH
