IMA6_RAT
ID IMA6_RAT Reviewed; 539 AA.
AC Q56R16; A0A0H2UHW5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Importin subunit alpha-6 {ECO:0000305};
DE AltName: Full=Karyopherin subunit alpha-5;
GN Name=Kpna5 {ECO:0000312|RGD:1561324};
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 [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-539.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=16906019; DOI=10.1097/01.fpc.0000220570.82842.4d;
RA Plant K.E., Everett D.M., Gordon Gibson G., Lyon J., Plant N.J.;
RT "Transcriptomic and phylogenetic analysis of Kpna genes: a family of
RT nuclear import factors modulated in xenobiotic-mediated liver growth.";
RL Pharmacogenet. Genomics 16:647-658(2006).
CC -!- FUNCTION: Functions in nuclear protein import as an adapter protein for
CC nuclear receptor KPNB1. Binds specifically and directly to substrates
CC containing either a simple or bipartite NLS motif. Docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) is
CC mediated by KPNB1 through binding to nucleoporin FxFG repeats and the
CC complex is subsequently translocated through the pore by an energy
CC requiring, Ran-dependent mechanism. At the nucleoplasmic side of the
CC NPC, Ran binds to importin-beta and the three components separate and
CC importin-alpha and -beta are re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran from importin. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between
CC the cytoplasm and nucleus. Mediates nuclear import of STAT1 homodimers
CC and STAT1/STAT2 heterodimers by recognizing non-classical NLSs of STAT1
CC and STAT2 through ARM repeats 8-9 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with importin subunit beta-1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic
CC central region composed of 10 repeats, and a short hydrophilic C-
CC terminus. The N-terminal hydrophilic region contains the importin beta
CC binding domain (IBB domain), which is sufficient for binding importin
CC beta and essential for nuclear protein import (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The IBB domain is thought to act as an intrasteric
CC autoregulatory sequence by interacting with the internal autoinhibitory
CC NLS. Binding of KPNB1 probably overlaps the internal NLS and
CC contributes to a high affinity for cytoplasmic NLS-containing cargo
CC substrates. After dissociation of the importin/substrate complex in the
CC nucleus the internal autohibitory NLS contributes to a low affinity for
CC nuclear NLS-containing proteins (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The major and minor NLS binding sites are mainly involved in
CC recognition of simple or bipartite NLS motifs. Structurally located
CC within in a helical surface groove they contain several conserved Trp
CC and Asn residues of the corresponding third helices (H3) of ARM repeats
CC which mainly contribute to binding (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; AABR07045039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07045040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY779029; AAX07456.1; -; mRNA.
DR RefSeq; NP_001020284.1; NM_001025113.1.
DR AlphaFoldDB; Q56R16; -.
DR STRING; 10116.ENSRNOP00000039571; -.
DR PhosphoSitePlus; Q56R16; -.
DR jPOST; Q56R16; -.
DR PaxDb; Q56R16; -.
DR PRIDE; Q56R16; -.
DR Ensembl; ENSRNOT00000097623; ENSRNOP00000079511; ENSRNOG00000030109.
DR GeneID; 294392; -.
DR KEGG; rno:294392; -.
DR UCSC; RGD:1561324; rat.
DR CTD; 3841; -.
DR RGD; 1561324; Kpna5.
DR eggNOG; KOG0166; Eukaryota.
DR GeneTree; ENSGT01050000244950; -.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; Q56R16; -.
DR OMA; EMIQMLY; -.
DR OrthoDB; 1111872at2759; -.
DR PhylomeDB; Q56R16; -.
DR TreeFam; TF354205; -.
DR PRO; PR:Q56R16; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000030109; Expressed in jejunum and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR Gene3D; 1.20.5.690; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032413; Arm_3.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR036975; Importin-a_IBB_sf.
DR InterPro; IPR024931; Importin_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF16186; Arm_3; 1.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS51214; IBB; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..539
FT /note="Importin subunit alpha-6"
FT /id="PRO_0000326083"
FT DOMAIN 1..60
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 76..118
FT /note="ARM 1; truncated"
FT REPEAT 119..162
FT /note="ARM 2"
FT REPEAT 163..207
FT /note="ARM 3"
FT REPEAT 208..246
FT /note="ARM 4"
FT REPEAT 247..291
FT /note="ARM 5"
FT REPEAT 292..331
FT /note="ARM 6"
FT REPEAT 332..373
FT /note="ARM 7"
FT REPEAT 374..413
FT /note="ARM 8"
FT REPEAT 414..456
FT /note="ARM 9"
FT REPEAT 460..505
FT /note="ARM 10; atypical"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..242
FT /note="NLS binding site (major)"
FT /evidence="ECO:0000250"
FT REGION 319..407
FT /note="NLS binding site (minor)"
FT /evidence="ECO:0000250"
FT MOTIF 45..54
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 22..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 60632 MW; E802BED6C320FC2A CRC64;
MDSMASPGKD NYRMKSYKNK ALNPQEMRRR REEEGIQLRK QKREEQLFKR RNVSLPRNDD
CMLESPIQDP DVSSTVPIPE EDMITADMIQ MIFSNNAEQQ LTATQKFRKL LSKEPNPPID
QVIQKPGVVQ RFVKFLERNE NCTLQFEAAW ALTNIASGTF LHTKVVIETG AVPIFIRLLT
SEHEDVQEQA VWALGNIAGD NAECRDFVLN CEILPPLLEL LTNSNRLTTT RNAVWALSNL
CRGKNPPPNF SKVSPCLNVL SRLLFSSDPD VLADVCWALS YLSDGPNDKI QVVIDSGVCR
RLVELLMHND YKVVSPALRA VGNIVTGDDI QTQVILNCSA LPCLLHLLGS PKESVRKEAC
WTISNITAGN RMQIQAVIDG SIFPVLIEVL QKAEFRTRKE AAWAITNATS GGAPEQIRYL
VTLGCIKPLC DLLTVMDSKI VQVALNGLEN ILRLGERESK QNGVGINPYC ALIEEAYGLD
KIEFLQSHEN QEIYQKAFDL IERYFGVEED DPSLVPQVDE QQRQFLFQQC EAPGEGFQL
