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IMB5_SCHPO
ID   IMB5_SCHPO              Reviewed;         993 AA.
AC   Q10297;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 3.
DT   25-MAY-2022, entry version 138.
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; ORFNames=SPAC22H10.03c;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   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).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15116432}.
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DR   EMBL; CU329670; CAA93604.2; -; Genomic_DNA.
DR   PIR; T38205; T38205.
DR   RefSeq; NP_593739.2; NM_001019170.2.
DR   AlphaFoldDB; Q10297; -.
DR   SMR; Q10297; -.
DR   BioGRID; 278375; 54.
DR   STRING; 4896.SPAC22H10.03c.1; -.
DR   MaxQB; Q10297; -.
DR   PaxDb; Q10297; -.
DR   EnsemblFungi; SPAC22H10.03c.1; SPAC22H10.03c.1:pep; SPAC22H10.03c.
DR   GeneID; 2541885; -.
DR   KEGG; spo:SPAC22H10.03c; -.
DR   PomBase; SPAC22H10.03c; kap114.
DR   VEuPathDB; FungiDB:SPAC22H10.03c; -.
DR   eggNOG; KOG2274; Eukaryota.
DR   HOGENOM; CLU_008920_1_1_1; -.
DR   InParanoid; Q10297; -.
DR   OMA; CLRAPPV; -.
DR   PRO; PR:Q10297; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005635; C:nuclear envelope; HDA: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; ISO:PomBase.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006606; P:protein import into nucleus; ISO:PomBase.
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   3: Inferred from homology;
KW   Nucleus; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..993
FT                   /note="Importin subunit beta-5"
FT                   /id="PRO_0000120777"
FT   DOMAIN          24..100
FT                   /note="Importin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
SQ   SEQUENCE   993 AA;  111864 MW;  A1D63EFD6EAC2098 CRC64;
     MVESKIIKLL EQVQSADPNS RIQAELGLRD LEKYHDFAAK LTDIASSGAS VPLRQGSLIY
     LQRYIVHHWS PLFEQFQDGP IPDENVKKHV RETLLHLLVS LDNFTLIKAV AYAVSLIANV
     DYPDEWPEVV PAVLHLLQST NENSINASLD VLDELVDESL VEEQFFIIAP QLASILYQFI
     FSAPPNDSMR MLQARGIKLF RSCLELIEIY KETKAEHVRV FLEQILPPWM DMFSHKFEVS
     LVDDRQVILP DSCGYFCIMG EIAMTLTKLR ELFPSKLTPY VVTFVELVWN IIEKLLDPYI
     REVVFSDGLD DSAFGDKYPI RYLVELLLFV SVALQSKFVQ NLFVSNTVPV PPLPPCIPLL
     VQYTQLPKHQ IEVYESDVSE YIANEFSMDF ASDTVRGAAI SVLSAFEEHT TLPIQQSLRE
     MSATYILNNE INWIYQEALL YACCSVDAAS DDTYDDYLDP IYEAIKVRID YSDAPILLLS
     RFFLFIGYFS ESTVVASQFF QIIMNNLVNA LQVDTVQYAA MKAIERFCSV GKVKPILSLQ
     PMILEVLSQY ASKSSDEALV LLVEAISSAV KLDCAKAAEL GNSVIPLLFN LVATNASDPY
     ICGIIEDTFE DIIHAANNYE SMCEITLPEL LQVLNQEDPI MVNIGATLLS CLIRAGPSPL
     PNGFVGYVLP PVYKITQIHS GDTELLQLSQ EILKGLLEKD TPQLLETEIS GSSGFQYILF
     ILHQLLDKES DDSACFLVGP ILLELADHAS QMVDLQSILL SCIKRLAIAE QPRFIQSIIY
     VFAKLIVKDS LGMMHFLTSS LLNEQGLTAF EVLMTVWCDN FVYFSNFKNI SIICIAMTKI
     YSFDSPLLDS VQVKGELISH SNRIITRSQS KLHPEEYSYV SVGEKILRLL SEEFVSLSKD
     AIVEEVSDDG ADDWDDGPIS AETFGLSAND VNELSKDEFS GVDNSEDEDN TDLQFYLLEF
     FKEAMKSNLH NINEVVFRLP QEEQDALVQI KEK
 
 
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