LOCUS       NP_002257                529 aa            linear   PRI 27-APR-2025
DEFINITION  importin subunit alpha-1 [Homo sapiens].
ACCESSION   NP_002257 XP_001133253 XP_001133254 XP_001133256 XP_001133258
            XP_001133262 XP_001133265 XP_001133267 XP_001133271
VERSION     NP_002257.1
DBSOURCE    REFSEQ: accession NM_002266.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Suleman,M., Said,A., Khan,H., Rehman,S.U., Alshammari,A.,
            Crovella,S. and Yassine,H.M.
  TITLE     Mutational analysis of SARS-CoV-2 ORF6-KPNA2 binding interface and
            identification of potent small molecule inhibitors to recuse the
            host immune system
  JOURNAL   Front Immunol 14, 1266776 (2024)
   PUBMED   38283360
  REMARK    GeneRIF: Mutational analysis of SARS-CoV-2 ORF6-KPNA2 binding
            interface and identification of potent small molecule inhibitors to
            recuse the host immune system.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Lange,A., Mills,R.E., Lange,C.J., Stewart,M., Devine,S.E. and
            Corbett,A.H.
  TITLE     Classical nuclear localization signals: definition, function, and
            interaction with importin alpha
  JOURNAL   J Biol Chem 282 (8), 5101-5105 (2007)
   PUBMED   17170104
  REMARK    Review article
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Teng,S.C., Wu,K.J., Tseng,S.F., Wong,C.W. and Kao,L.
  TITLE     Importin KPNA2, NBS1, DNA repair and tumorigenesis
  JOURNAL   J Mol Histol 37 (5-7), 293-299 (2006)
   PUBMED   16752129
  REMARK    GeneRIF: This review focuses on recent experimental evidences
            demonstrating how NBS1 is translocated into the nucleus by an
            importin KPNA2 which mediates NBS1 subcellular localization and the
            functions of the NBS1 complex in tumorigenesis.
            Review article
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Dorr,S.N., Schlicker,M.N. and Hansmann,I.N.
  TITLE     Genomic structure of karyopherin alpha2 (KPNA2) within a low-copy
            repeat on chromosome 17q23-q24 and mutation analysis in patients
            with Russell-Silver syndrome
  JOURNAL   Hum Genet 109 (5), 479-486 (2001)
   PUBMED   11735022
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Herold,A., Truant,R., Wiegand,H. and Cullen,B.R.
  TITLE     Determination of the functional domain organization of the importin
            alpha nuclear import factor
  JOURNAL   J Cell Biol 143 (2), 309-318 (1998)
   PUBMED   9786944
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Weis,K., Ryder,U. and Lamond,A.I.
  TITLE     The conserved amino-terminal domain of hSRP1 alpha is essential for
            nuclear protein import
  JOURNAL   EMBO J 15 (8), 1818-1825 (1996)
   PUBMED   8617227
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Moroianu,J., Hijikata,M., Blobel,G. and Radu,A.
  TITLE     Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers:
            alpha 1 or alpha 2 subunit binds nuclear localization signal and
            beta subunit interacts with peptide repeat-containing nucleoporins
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6532-6536 (1995)
   PUBMED   7604027
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Weis,K., Mattaj,I.W. and Lamond,A.I.
  TITLE     Identification of hSRP1 alpha as a functional receptor for nuclear
            localization sequences
  JOURNAL   Science 268 (5213), 1049-1053 (1995)
   PUBMED   7754385
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Cuomo,C.A., Kirch,S.A., Gyuris,J., Brent,R. and Oettinger,M.A.
  TITLE     Rch1, a protein that specifically interacts with the RAG-1
            recombination-activating protein
  JOURNAL   Proc Natl Acad Sci U S A 91 (13), 6156-6160 (1994)
   PUBMED   8016130
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Bukrinsky,M.I., Sharova,N., Dempsey,M.P., Stanwick,T.L.,
            Bukrinskaya,A.G., Haggerty,S. and Stevenson,M.
  TITLE     Active nuclear import of human immunodeficiency virus type 1
            preintegration complexes
  JOURNAL   Proc Natl Acad Sci U S A 89 (14), 6580-6584 (1992)
   PUBMED   1631159
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U28386.1, AK024833.1 and
            AA744568.1.
            
            On or before Jan 26, 2007 this sequence version replaced
            XP_001133254.1, XP_001133256.1, XP_001133258.1, XP_001133265.1,
            XP_001133267.1, XP_001133271.1, XP_001133253.1, XP_001133262.1.
            
            Summary: The import of proteins into the nucleus is a process that
            involves at least 2 steps. The first is an energy-independent
            docking of the protein to the nuclear envelope and the second is an
            energy-dependent translocation through the nuclear pore complex.
            Imported proteins require a nuclear localization sequence (NLS)
            which generally consists of a short region of basic amino acids or
            2 such regions spaced about 10 amino acids apart. Proteins involved
            in the first step of nuclear import have been identified in
            different systems. These include the Xenopus protein importin and
            its yeast homolog, SRP1 (a suppressor of certain
            temperature-sensitive mutations of RNA polymerase I in
            Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein
            interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and
            may be involved in the nuclear transport of proteins. KPNA2 also
            may play a role in V(D)J recombination. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Feb
            2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053343.1, AK291954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330459.8/ ENSP00000332455.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..529
                     /product="importin subunit alpha-1"
                     /note="importin-alpha-P1; pendulin; importin subunit
                     alpha-2; RAG cohort protein 1; karyopherin alpha 2 (RAG
                     cohort 1, importin alpha 1); nuclear pore-targeting
                     complex 58kD component"
                     /calculated_mol_wt=57731
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P52292.1)"
     Region          10..528
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          43..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          45..54
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52292.1)"
     Region          71..111
                     /region_name="ARM 1, truncated"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          112..151
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          115..147
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(138,142,146,180,184,188,227,231,235)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          142..238
                     /region_name="NLS binding site (major).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          155..191
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          197..236
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          200..244
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          246..282
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          253..278
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(269,273,277,311,315,319,353,357,361)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          283..322
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          286..322
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          315..403
                     /region_name="NLS binding site (minor).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          328..362
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          367..409
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          370..404
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          410..456
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          413..447
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          457..496
                     /region_name="ARM 10, atypical"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          460..495
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P52292.1)"
     CDS             1..529
                     /gene="KPNA2"
                     /gene_synonym="IPOA1; PTAC58; QIP2; RCH1; SRP1-alpha;
                     SRP1alpha"
                     /coded_by="NM_002266.4:130..1719"
                     /db_xref="CCDS:CCDS32713.1"
                     /db_xref="GeneID:3838"
                     /db_xref="HGNC:HGNC:6395"
                     /db_xref="MIM:600685"
ORIGIN      
        1 mstnenantp aarlhrfknk gkdstemrrr rievnvelrk akkddqmlkr rnvssfpdda
       61 tsplqenrnn qgtvnwsvdd ivkginssnv enqlqatqaa rkllsrekqp pidniiragl
      121 ipkfvsflgr tdcspiqfes awaltniasg tseqtkavvd ggaipafisl lasphahise
      181 qavwalgnia gdgsvfrdlv ikygavdpll allavpdmss lacgylrnlt wtlsnlcrnk
      241 npappidave qilptlvrll hhddpevlad tcwaisyltd gpnerigmvv ktgvvpqlvk
      301 llgaselpiv tpalraigni vtgtdeqtqv vidagalavf pslltnpktn iqkeatwtms
      361 nitagrqdqi qqvvnhglvp flvsvlskad fktqkeavwa vtnytsggtv eqivylvhcg
      421 iieplmnllt akdtkiilvi ldaisnifqa aeklgetekl simieecggl dkiealqnhe
      481 nesvykasls liekyfsvee eedqnvvpet tsegytfqvq dgapgtfnf
//
