IMA5_BOVIN
ID IMA5_BOVIN Reviewed; 538 AA.
AC A2VE08;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Importin subunit alpha-5;
DE AltName: Full=Karyopherin subunit alpha-1;
DE Contains:
DE RecName: Full=Importin subunit alpha-5, N-terminally processed;
GN Name=KPNA1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=19420384; DOI=10.1095/biolreprod.109.077396;
RA Tejomurtula J., Lee K.B., Tripurani S.K., Smith G.W., Yao J.;
RT "Role of importin alpha8, a new member of the importin alpha family of
RT nuclear transport proteins, in early embryonic development in cattle.";
RL Biol. Reprod. 81:333-342(2009).
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 -!- SUBUNIT: Heterodimer; with KPNB1 (By similarity). Interacts with ANP32E
CC (By similarity). Interacts with APEX1 (via its N-terminus) (By
CC similarity). Interacts with ZIC3 (By similarity). Interacts with SNAI1
CC (via zinc fingers) (By similarity). Interacts with CTNNBL1 (via its N-
CC terminal) (By similarity). Interacts with AICDA (via its NLS) (By
CC similarity). Interacts with NSMF; the interaction occurs in a calcium-
CC independent manner after synaptic NMDA receptor stimulation and is
CC required for nuclear import of NSMF but is competed by CABP1 (By
CC similarity). Interacts with DCAF8 (By similarity). Interacts with ITSN1
CC isoform 2 (By similarity). {ECO:0000250|UniProtKB:P52294,
CC ECO:0000250|UniProtKB:P83953, ECO:0000250|UniProtKB:Q60960}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19420384}.
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 -!- PTM: Polyubiquitinated in the presence of RAG1 (in vitro).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; BC133509; AAI33510.1; -; mRNA.
DR RefSeq; NP_001075202.1; NM_001081733.2.
DR AlphaFoldDB; A2VE08; -.
DR SMR; A2VE08; -.
DR STRING; 9913.ENSBTAP00000014799; -.
DR PaxDb; A2VE08; -.
DR PRIDE; A2VE08; -.
DR Ensembl; ENSBTAT00000014799; ENSBTAP00000014799; ENSBTAG00000011143.
DR GeneID; 539679; -.
DR KEGG; bta:539679; -.
DR CTD; 3836; -.
DR VEuPathDB; HostDB:ENSBTAG00000011143; -.
DR VGNC; VGNC:30700; KPNA1.
DR eggNOG; KOG0166; Eukaryota.
DR GeneTree; ENSGT01050000244950; -.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; A2VE08; -.
DR OMA; MTEMIFS; -.
DR OrthoDB; 1111872at2759; -.
DR TreeFam; TF354205; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000011143; Expressed in neutrophil and 109 other tissues.
DR ExpressionAtlas; A2VE08; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
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 GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0014901; P:satellite cell activation involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0014841; P:skeletal muscle satellite cell proliferation; IEA:Ensembl.
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 Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Ubl conjugation.
FT CHAIN 1..538
FT /note="Importin subunit alpha-5"
FT /id="PRO_0000424490"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52294"
FT CHAIN 2..538
FT /note="Importin subunit alpha-5, N-terminally processed"
FT /id="PRO_0000297527"
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..36
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..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P52294"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Importin subunit alpha-5, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P52294"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52294"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52294"
SQ SEQUENCE 538 AA; 60194 MW; 43F9FF00C8FB294C CRC64;
MTTPGKENFR LKSYKNKSLN PDEMRRRREE EGLQLRKQKR EEQLFKRRNV ATAEEETEEE
VMSDGGFHEA QINNMEMAPG GVITSDMIEM IFSNSPEQQL SATQKFRKLL SKEPNPPIDE
VISTPGVVAR FVEFLKRKEN CTLQFESAWV LTNIASGNSL QTRIVIQAGA VPIFIELLSS
EFEDVQEQAV WALGNIAGDS TMCRDYVLDC NILPPLLQLF SKQNRLTMTR NAVWALSNLC
RGKSPPPEFA KVSPCLNVLS WLLFVSDTDV LADACWALSY LSDGPNDKIQ AVIDAGVCRR
LVELLMHNDY KVVSPALRAV GNIVTGDDVQ TQVILNCSAL QSLLHLLSSP KESIKKEACW
TISNITAGNR AQIQTVIDAN IFPALISILQ TAEFRTRKEA AWAITNATSG GSAEQIKYLV
ELGCIKPLCD LLTVMDSKIV QVALNGLENI LRLGEQEAKR NGTGINPYCA LIEEAYGLDK
IEFLQSHENQ EIYQKAFDLI EHYFGTEDED SSIAPQVDLS QQQYIFQQCE APMEGFQL
