IMB1_RAT
ID IMB1_RAT Reviewed; 875 AA.
AC P52296;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Importin subunit beta-1;
DE AltName: Full=Karyopherin subunit beta-1;
DE AltName: Full=Nuclear factor p97;
DE AltName: Full=Pore targeting complex 97 kDa subunit;
DE Short=PTAC97;
GN Name=Kpnb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Buffalo; TISSUE=Liver;
RX PubMed=7878057; DOI=10.1073/pnas.92.5.1769;
RA Radu A., Blobel G., Moore M.M.;
RT "Identification of a protein complex that is required for nuclear protein
RT import and mediates docking of import substrate to distinct nucleoporins.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1769-1773(1995).
RN [2]
RP SUBCELLULAR LOCATION, AND BINDING TO NUCLEOPORINS.
RX PubMed=7604027; DOI=10.1073/pnas.92.14.6532;
RA Moroianu J., Hijikata M., Blobel G., Radu A.;
RT "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1
RT or alpha 2 subunit binds nuclear localization signal and beta subunit
RT interacts with peptide repeat-containing nucleoporins.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6532-6536(1995).
CC -!- FUNCTION: Functions in nuclear protein import, either in association
CC with an adapter protein, like an importin-alpha subunit, which binds to
CC nuclear localization signals (NLS) in cargo substrates, or by acting as
CC autonomous nuclear transport receptor. Acting autonomously, serves
CC itself as NLS receptor. Docking of the importin/substrate complex to
CC the nuclear pore complex (NPC) is mediated by KPNB1 through binding to
CC nucleoporin FxFG repeats and the complex is subsequently translocated
CC through the pore by an energy requiring, Ran-dependent mechanism. At
CC the nucleoplasmic side of the NPC, Ran binds to importin-beta and the
CC three components separate and importin-alpha and -beta are re-exported
CC from the nucleus to the cytoplasm where GTP hydrolysis releases Ran
CC from importin. The directionality of nuclear import is thought to be
CC conferred by an asymmetric distribution of the GTP- and GDP-bound forms
CC of Ran between the cytoplasm and nucleus. Mediates autonomously the
CC nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. In
CC association with IPO7, mediates the nuclear import of H1 histone. In
CC vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Imports
CC SNAI1 and PRKCI into the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:Q14974}.
CC -!- SUBUNIT: Forms a complex with an importin alpha subunit (By
CC similarity). Interacts with XPO1 (By similarity). Forms a heterodimer
CC with IPO7 (By similarity). The KPNB1/IPO7 heterodimer interacts with H1
CC histone (By similarity). Interacts with SNUPN (By similarity).
CC Interacts with H2A, H2B, H3 and H4 histones (By similarity). Component
CC of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259
CC (By similarity). Component of a nuclear export receptor complex
CC composed of KPNB1, Ran, SNUPN and XPO1 (By similarity). Interacts with
CC SRY (By similarity). Interacts with PRKCI/atypical protein kinase C
CC iota (By similarity). Interacts with KPNA2 (By similarity). Interacts
CC with KPNA7 (By similarity). Interacts with SNAI1 (via zinc fingers) and
CC SNAI2 (via zinc fingers) (By similarity). Interacts with SLC35G1 and
CC STIM1 (By similarity). Interacts with DCAF8 (By similarity). Interacts
CC with RAN (By similarity). Interacts with NUMA1 (via C-terminus); this
CC interaction is inhibited by RanGTP (By similarity). Interacts with
CC ZBED1/hDREF; required for nuclear import of ZBED1/hDREF (By
CC similarity). Interacts with SRP19 (By similarity). Interacts with
CC RPL23A (via BIB domain), RPS7 and RPL5 (By similarity). Interacts with
CC PARP16 (By similarity). {ECO:0000250|UniProtKB:P70168,
CC ECO:0000250|UniProtKB:Q14974}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7604027}. Nucleus
CC envelope {ECO:0000269|PubMed:7604027}.
CC -!- PTM: Mono-ADP-ribosylated by PARP16. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-1
CC subfamily. {ECO:0000305}.
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DR EMBL; L38644; AAC42047.1; -; mRNA.
DR PIR; I59350; I59350.
DR RefSeq; NP_058759.1; NM_017063.1.
DR AlphaFoldDB; P52296; -.
DR SMR; P52296; -.
DR BioGRID; 247024; 5.
DR CORUM; P52296; -.
DR DIP; DIP-37024N; -.
DR IntAct; P52296; 6.
DR MINT; P52296; -.
DR STRING; 10116.ENSRNOP00000012376; -.
DR iPTMnet; P52296; -.
DR PhosphoSitePlus; P52296; -.
DR jPOST; P52296; -.
DR PaxDb; P52296; -.
DR PeptideAtlas; P52296; -.
DR PRIDE; P52296; -.
DR DNASU; 24917; -.
DR GeneID; 24917; -.
DR KEGG; rno:24917; -.
DR UCSC; RGD:2909; rat.
DR CTD; 3837; -.
DR RGD; 2909; Kpnb1.
DR eggNOG; KOG1241; Eukaryota.
DR InParanoid; P52296; -.
DR OrthoDB; 769199at2759; -.
DR PhylomeDB; P52296; -.
DR Reactome; R-RNO-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-RNO-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
DR Reactome; R-RNO-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-RNO-909733; Interferon alpha/beta signaling.
DR PRO; PR:P52296; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:RGD.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISO:RGD.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005643; C:nuclear pore; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:RGD.
DR GO; GO:0061676; F:importin-alpha family protein binding; ISO:RGD.
DR GO; GO:0019894; F:kinesin binding; IPI:RGD.
DR GO; GO:0061608; F:nuclear import signal receptor activity; ISO:RGD.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030953; P:astral microtubule organization; ISO:RGD.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; ISO:RGD.
DR GO; GO:0045184; P:establishment of protein localization; ISO:RGD.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; ISO:RGD.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0031291; P:Ran protein signal transduction; ISO:RGD.
DR GO; GO:0006610; P:ribosomal protein import into nucleus; ISO:RGD.
DR GO; GO:0006404; P:RNA import into nucleus; ISO:RGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00185; ARM; 3.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Cytoplasm; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..875
FT /note="Importin subunit beta-1"
FT /id="PRO_0000120747"
FT REPEAT 2..31
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT DOMAIN 21..100
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 33..64
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 84..122
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 128..159
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 169..201
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 211..246
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 252..301
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 313..359
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 363..393
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 401..437
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 448..484
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 499..536
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 543..591
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 599..638
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 643..680
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 685..723
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 731..775
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 785..828
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REPEAT 830..872
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REGION 285..461
FT /note="Essential for high affinity interaction with RPL23A"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT REGION 328..341
FT /note="IAB-binding"
FT REGION 333..418
FT /note="Ran-GTP binding"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT MOD_RES 210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT MOD_RES 834
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
FT MOD_RES 866
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14974"
SQ SEQUENCE 875 AA; 97124 MW; 9CD77A05744014C4 CRC64;
MELITILEKT VSPDRLELEA AQKFLERAAV ENLPTFLVEL SRVLANPGNS QVARVAAGLQ
IRLLTSKDPD IKAQYQQRWL AIDANARREV KNYVLQTLGT ETYRPSSASQ CVAGIACAEI
PVSQWPELIP QLVANVTNPN STEHMKESTL EAIGYICQDI DPEQLQDKSN EILTAIIQGM
RKEEPSNNVK LAATNALLNS LEFTKANFDK ESERHFIMQV VCEATQCPDT RVRVAALQNL
VKIMSLYYQY METYMGPALF AITIEAMKSD IDEVALQGIE FWSNVCDEEM DLAIEASEAA
EQGRPPEHTS KFYAKGALQY LVPILTQTLT KQDENDDDDD WNPCKAAGVC LMLLSTCCED
DIVPHVLPFI KEHIKNPDWR YRDAAVMAFG SILEGPEPNQ LKPLVIQAMP TLIELMKDPS
VVVRDTTAWT VGRICELLPE AAINDVYLAP LLQCLIEGLS AEPRVASNVC WAFSSLAEAA
YEAADVADDQ EEPATYCLSS SFELIVQKLL ETTDRPDGHQ NNLRSSAYES LMEIVKNSAK
DCYPAVQKTT LVIMERLQQV LQMESHIQST SDRIQFNDLQ SLLCATLQNV LWKVQHQDAL
QISDVVMASL LRMFQSTAGS GGVQEDALMA VSTLVEVLGG EFLKYMEAFK PFLGIGLKNY
AECQVCLAAV GLVGDLCRAL QSNILPFCDE VMQLLLENLG NENVHRSVKP QILSVFGDIT
LAIGGEFKKY LEVVLNTLQQ ASQAQVDKSD FDMVDYLNEL RESCLEAYTG IVQGLKGDQE
NVHPDVMLVQ PRVEFILSFI DHIAGDEDHT DGVVACAAGL IGDLCTAFGK DVLKLVEARP
MIHELLTEGR RSKTNKAKTL ATWATKELRK LKNQA
