ID   IMA5_CHICK              Reviewed;         538 AA.
AC   Q5ZML1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Importin subunit alpha-5;
DE   AltName: Full=Karyopherin subunit alpha-1;
GN   Name=KPNA1; ORFNames=RCJMB04_1l14;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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.
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; AJ719373; CAG31032.1; -; mRNA.
DR   RefSeq; NP_001025945.1; NM_001030774.1.
DR   AlphaFoldDB; Q5ZML1; -.
DR   SMR; Q5ZML1; -.
DR   STRING; 9031.ENSGALP00000034376; -.
DR   PaxDb; Q5ZML1; -.
DR   GeneID; 418271; -.
DR   KEGG; gga:418271; -.
DR   CTD; 3836; -.
DR   VEuPathDB; HostDB:geneid_418271; -.
DR   eggNOG; KOG0166; Eukaryota.
DR   HOGENOM; CLU_018084_6_0_1; -.
DR   InParanoid; Q5ZML1; -.
DR   OrthoDB; 1111872at2759; -.
DR   PhylomeDB; Q5ZML1; -.
DR   TreeFam; TF354205; -.
DR   PRO; PR:Q5ZML1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
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   GO; GO:0099527; P:postsynapse to nucleus signaling pathway; 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; 4.
DR   PROSITE; PS51214; IBB; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Protein transport; Reference proteome; Repeat;
KW   Transport.
FT   CHAIN           1..538
FT                   /note="Importin subunit alpha-5"
FT                   /id="PRO_0000297529"
FT   DOMAIN          1..57
FT                   /note="IBB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT   REPEAT          77..117
FT                   /note="ARM 1; truncated"
FT   REPEAT          118..161
FT                   /note="ARM 2"
FT   REPEAT          162..206
FT                   /note="ARM 3"
FT   REPEAT          207..245
FT                   /note="ARM 4"
FT   REPEAT          246..290
FT                   /note="ARM 5"
FT   REPEAT          291..330
FT                   /note="ARM 6"
FT   REPEAT          331..372
FT                   /note="ARM 7"
FT   REPEAT          373..412
FT                   /note="ARM 8"
FT   REPEAT          413..457
FT                   /note="ARM 9"
FT   REPEAT          460..504
FT                   /note="ARM 10; atypical"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..241
FT                   /note="NLS binding site (major)"
FT                   /evidence="ECO:0000250"
FT   REGION          245..437
FT                   /note="Binding to RAG1"
FT   REGION          318..406
FT                   /note="NLS binding site (minor)"
FT                   /evidence="ECO:0000250"
FT   MOTIF           42..51
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        10..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  60195 MW;  2596F89BC5D23057 CRC64;
     MTTSGKENFR LKSYKNKSLN PDEMRRRREE EGLQLRKQKR EEQLFKRRNV ATAEEEAEEE
     VMSDGGFHEA QMNNMEMTSS AVITSDMIEM IFSNSPEQQL SATQKFRKLL SKEPNPPIDE
     VISTPGVVAR FVEFLKRKEN CTLQFEAAWV LTNIASGNSL QTRIVIQAGA VPIFIELLSS
     EFEDVQEQAV WALGNIAGDS TMCRDYVLDC NILPPLLQLL SKQNRITMTR NAVWALSNLC
     RGKNPPPDFA KVSPCLSVLS WLLFVNDTDV LADACWALSY LSDGPNDKIQ AVIDAGVCRR
     LVELLMHNDY KVVSPALRAV GNIVTGDDIQ TQVILNCSAL QSLLHLLSSP KESIKKEACW
     TISNITAGNR AQIQTVIDAH IFPALINILQ TAEFRTRKEA AWAITNATSG GSAEQIKYLV
     ELGCIKPLCD LLTVMDSKIV QVALSGLENI LRLGEQESKR SGAGINPYCA LIEEAYGLDK
     IEFLQSHENQ EIYQKAFDLI EHYFGTEDED SSIAPQVDLS QQQYIFQQCE APMEGFQL