IMA3_CAEEL
ID IMA3_CAEEL Reviewed; 514 AA.
AC Q19969; O44925;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Importin subunit alpha-3;
DE AltName: Full=Karyopherin subunit alpha-3;
GN Name=ima-3; ORFNames=F32E10.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11311162; DOI=10.1242/dev.128.10.1817;
RA Geles K.G., Adam S.A.;
RT "Germline and developmental roles of the nuclear transport factor importin
RT alpha3 in C. elegans.";
RL Development 128:1817-1830(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, INTERACTION WITH CEBP-1, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=31417366; DOI=10.3389/fncel.2019.00348;
RA Malinow R.A., Ying P., Koorman T., Boxem M., Jin Y., Kim K.W.;
RT "Functional Dissection of C. elegans bZip-Protein CEBP-1 Reveals Novel
RT Structural Motifs Required for Axon Regeneration and Nuclear Import.";
RL Front. Cell. Neurosci. 13:348-348(2019).
CC -!- FUNCTION: Binds specifically and directly to substrates containing
CC either a simple or bipartite NLS motif (PubMed:11311162). Promotes
CC docking of import substrates to the nuclear envelope (PubMed:11311162).
CC Seems to act as a cytosolic receptor for both simple and bipartite NLS
CC motifs (PubMed:11311162). Necessary for correct nucleoporin
CC localization within the germline (PubMed:11311162). Essential gene for
CC embryonic and larval development (PubMed:11311162). May be dispensable
CC for axon development, but required for axon regeneration in both
CC mechanosensory and motor neurons (PubMed:31417366). Required for
CC oogenic development, ima-1 and ima-2 cannot functionally compensate for
CC loss of ima-3 (PubMed:11311162). {ECO:0000269|PubMed:11311162,
CC ECO:0000269|PubMed:31417366}.
CC -!- SUBUNIT: Forms a complex with an importin beta subunit
CC (PubMed:11311162). May interact with transcription factor cebp-1 (via
CC N-terminus) (PubMed:31417366). {ECO:0000269|PubMed:11311162,
CC ECO:0000269|PubMed:31417366}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11311162}. Nucleus
CC {ECO:0000269|PubMed:11311162}.
CC -!- TISSUE SPECIFICITY: Expressed in larval and adult germline and somatic
CC tissues, including neurons. {ECO:0000269|PubMed:11311162,
CC ECO:0000269|PubMed:31417366}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels throughout all
CC developmental stages. {ECO:0000269|PubMed:11311162}.
CC -!- DISRUPTION PHENOTYPE: Larval lethality (PubMed:31417366).
CC Mechanosensory neurons are born and develop normally (PubMed:31417366).
CC However, cre-mediated knockdown targeted to mechanosensory neurons
CC severely impairs axon regrowth of mechanosensory PLM neurons after
CC injury (PubMed:31417366). {ECO:0000269|PubMed:31417366}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; AF040995; AAB97171.1; -; mRNA.
DR EMBL; FO081278; CCD70435.1; -; Genomic_DNA.
DR PIR; G88733; G88733.
DR PIR; T42402; T42402.
DR RefSeq; NP_501227.1; NM_068826.4.
DR AlphaFoldDB; Q19969; -.
DR SMR; Q19969; -.
DR BioGRID; 42651; 56.
DR DIP; DIP-26417N; -.
DR IntAct; Q19969; 18.
DR STRING; 6239.F32E10.4; -.
DR iPTMnet; Q19969; -.
DR EPD; Q19969; -.
DR PaxDb; Q19969; -.
DR PeptideAtlas; Q19969; -.
DR EnsemblMetazoa; F32E10.4.1; F32E10.4.1; WBGene00002074.
DR GeneID; 177533; -.
DR KEGG; cel:CELE_F32E10.4; -.
DR UCSC; F32E10.4.1; c. elegans.
DR CTD; 177533; -.
DR WormBase; F32E10.4; CE20745; WBGene00002074; ima-3.
DR eggNOG; KOG0166; Eukaryota.
DR GeneTree; ENSGT01050000244891; -.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; Q19969; -.
DR OMA; SAQTNKV; -.
DR OrthoDB; 1111872at2759; -.
DR PhylomeDB; Q19969; -.
DR SignaLink; Q19969; -.
DR PRO; PR:Q19969; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002074; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005643; C:nuclear pore; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0007292; P:female gamete generation; IMP:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IMP:WormBase.
DR GO; GO:0007127; P:meiosis I; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006999; P:nuclear pore organization; IMP:WormBase.
DR GO; GO:0048477; P:oogenesis; IMP:WormBase.
DR GO; GO:0006606; P:protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
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; 6.
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; 1.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Nucleus; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..514
FT /note="Importin subunit alpha-3"
FT /id="PRO_0000120736"
FT DOMAIN 1..51
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 101..142
FT /note="ARM 1"
FT REPEAT 143..187
FT /note="ARM 2"
FT REPEAT 188..226
FT /note="ARM 3"
FT REPEAT 227..271
FT /note="ARM 4"
FT REPEAT 272..311
FT /note="ARM 5"
FT REPEAT 312..353
FT /note="ARM 6"
FT REPEAT 354..393
FT /note="ARM 7"
FT REPEAT 394..436
FT /note="ARM 8"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 56163 MW; 76F6DE2350E9BE89 CRC64;
MSSNRQAYYK NNAKEQIGKE KRNEEVVSIR KDKREEAISK RRNINTQIED DSETSTTPPG
PFDANLLRLT VAAAQSSDPA EQLTAVQQAR KMLSTDRNPP IDDLIGSGIL PVLVQCLSST
DPNLQFEAAW ALTNIASGTS EQTQAVVNAG AVPLFLQLLS CGNLNVCEQS VWALGNIIGD
GPHFRDYCLE LGILQPLLQF INPEIPIGFL RNVTWVIVNL CRCKDPAPSP AVVRTILPAL
SLLIHHQDTN ILIDTVWALS YLTDGGNEHI QMVIEAQVVT HLVPLLGHVD VKVQTAALRA
VGNIVTGTDE QTQLVLDSGV LRFMPGLLAH YKEKINKEAV WFVSNITAGN QQQVQDVFDA
GIMPMIIHLL DRGDFPTQKE AAWAISNVTI SGRPNQVEQM VKLGVLRPFC AMLSCTDSQI
IQVVLDGINN ILKMAGEAAE QVTSEIEECG GLDKIENLQN HENEDIYKLA FEIIDNFFSS
DDETGNVEGA QSSAFGGDVP PVPDAPNGGW NFGK
