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IMA2_CAEEL
ID   IMA2_CAEEL              Reviewed;         531 AA.
AC   P91276;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Importin subunit alpha-2;
DE   AltName: Full=Karyopherin subunit alpha-2;
GN   Name=ima-2 {ECO:0000303|PubMed:12221121, ECO:0000312|WormBase:F26B1.3};
GN   ORFNames=F26B1.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|EMBL:AAG49386.1};
RN   [1] {ECO:0000305}
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] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Bristol N2;
RA   Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA   Thierry-Mieg D., Thierry-Mieg J.;
RT   "The Caenorhabditis elegans transcriptome project, a complementary view of
RT   the genome.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12221121; DOI=10.1091/mbc.e02-02-0069;
RA   Geles K.G., Johnson J.J., Jong S., Adam S.A.;
RT   "A role for Caenorhabditis elegans importin IMA-2 in germ line and
RT   embryonic mitosis.";
RL   Mol. Biol. Cell 13:3138-3147(2002).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP   AKIR-1.
RX   PubMed=30563860; DOI=10.1534/genetics.118.301458;
RA   Bowman R., Balukof N., Ford T., Smolikove S.;
RT   "A novel role for alpha-importins and Akirin in establishment of meiotic
RT   sister chromatid cohesion in Caenorhabditis elegans.";
RL   Genetics 211:617-635(2019).
CC   -!- FUNCTION: Nuclear transport receptor that mediates nuclear import of
CC       proteins, and which is involved in sister chromatid cohesion
CC       (PubMed:11311162, PubMed:12221121, PubMed:30563860). Binds specifically
CC       and directly to substrates containing either a simple or bipartite
CC       nuclear localization signals (NLS) motif (By similarity). Promotes
CC       docking of import substrates to the nuclear envelope (By similarity).
CC       Together with akir-1 adapter, required for the import and load of
CC       cohesin complex proteins in meiotic nuclei (PubMed:30563860).
CC       {ECO:0000250|UniProtKB:Q19969, ECO:0000269|PubMed:11311162,
CC       ECO:0000269|PubMed:12221121, ECO:0000269|PubMed:30563860}.
CC   -!- SUBUNIT: Forms a complex with an importin beta subunit
CC       (PubMed:11311162). Interacts with akir-1 (PubMed:30563860).
CC       {ECO:0000269|PubMed:11311162, ECO:0000269|PubMed:30563860}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11311162,
CC       ECO:0000269|PubMed:12221121}. Nucleus {ECO:0000269|PubMed:11311162,
CC       ECO:0000269|PubMed:12221121, ECO:0000269|PubMed:30563860}. Nucleus
CC       envelope {ECO:0000269|PubMed:12221121}. Note=In interphase germ cells
CC       and embryonic cells, localizes to the cytoplasm and nuclear envelope,
CC       whereas in developing oocytes, it localizes in the cytoplasm and
CC       nucleus. {ECO:0000269|PubMed:12221121}.
CC   -!- TISSUE SPECIFICITY: Germline tissues (PubMed:11311162,
CC       PubMed:12221121). Expressed exclusively in germ line cells from the
CC       early embryonic through adult stages (PubMed:12221121).
CC       {ECO:0000269|PubMed:11311162, ECO:0000269|PubMed:12221121}.
CC   -!- DEVELOPMENTAL STAGE: Expressed weakly in early larvae, levels of
CC       expression increase in larval stage 4 and adult stages when germ cells
CC       are continually proliferating. {ECO:0000269|PubMed:11311162}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality associated with a terminal
CC       aneuploid phenotype: embryos display severe defects in nuclear envelope
CC       formation, accumulating nucleoporins and lamin in the cytoplasm
CC       (PubMed:12221121). Worms lacking both akir-1 and ima-2 show reduced
CC       gonad size and aberrant diakinesis oocyte formation; defects are caused
CC       by impaired meiotic recombination (PubMed:30563860).
CC       {ECO:0000269|PubMed:12221121, ECO:0000269|PubMed:30563860}.
CC   -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR   EMBL; AF040996; AAB97172.1; -; mRNA.
DR   EMBL; FO080500; CCD64196.1; -; Genomic_DNA.
DR   EMBL; AF326936; AAG49386.1; -; mRNA.
DR   PIR; T30167; T30167.
DR   RefSeq; NP_491824.1; NM_059423.5.
DR   AlphaFoldDB; P91276; -.
DR   SMR; P91276; -.
DR   BioGRID; 37782; 9.
DR   DIP; DIP-26785N; -.
DR   IntAct; P91276; 3.
DR   STRING; 6239.F26B1.3; -.
DR   iPTMnet; P91276; -.
DR   EPD; P91276; -.
DR   PaxDb; P91276; -.
DR   PeptideAtlas; P91276; -.
DR   PRIDE; P91276; -.
DR   EnsemblMetazoa; F26B1.3.1; F26B1.3.1; WBGene00002073.
DR   GeneID; 172329; -.
DR   KEGG; cel:CELE_F26B1.3; -.
DR   UCSC; F26B1.3.1; c. elegans.
DR   CTD; 172329; -.
DR   WormBase; F26B1.3; CE09675; WBGene00002073; ima-2.
DR   eggNOG; KOG0166; Eukaryota.
DR   GeneTree; ENSGT01050000244891; -.
DR   HOGENOM; CLU_018084_6_0_1; -.
DR   InParanoid; P91276; -.
DR   OMA; VKECCWL; -.
DR   OrthoDB; 1111872at2759; -.
DR   PhylomeDB; P91276; -.
DR   SignaLink; P91276; -.
DR   PRO; PR:P91276; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00002073; Expressed in germ line (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; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0051177; P:meiotic sister chromatid cohesion; IMP:UniProtKB.
DR   GO; GO:0007084; P:mitotic nuclear membrane reassembly; IMP:WormBase.
DR   GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:UniProtKB.
DR   GO; GO:0051983; P:regulation of chromosome segregation; 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; 5.
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; Meiosis; Nucleus; Protein transport; Reference proteome; Repeat;
KW   Transport.
FT   CHAIN           1..531
FT                   /note="Importin subunit alpha-2"
FT                   /id="PRO_0000120735"
FT   DOMAIN          5..67
FT                   /note="IBB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT   REPEAT          122..161
FT                   /note="ARM 1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          164..203
FT                   /note="ARM 2"
FT                   /evidence="ECO:0000305"
FT   REPEAT          250..290
FT                   /note="ARM 3"
FT                   /evidence="ECO:0000305"
FT   REPEAT          293..331
FT                   /note="ARM 4"
FT                   /evidence="ECO:0000305"
FT   REPEAT          334..374
FT                   /note="ARM 5"
FT                   /evidence="ECO:0000305"
FT   REPEAT          377..416
FT                   /note="ARM 6"
FT                   /evidence="ECO:0000305"
FT   REPEAT          420..459
FT                   /note="ARM 7"
FT                   /evidence="ECO:0000305"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   531 AA;  59176 MW;  0CB7CEB45E67A114 CRC64;
     MTLTETSLSH NAEEGKDEGG RLQQYKNLTK HEELRRRRTE CSVEIRKQKG ADMMMKRRNI
     VDVDEGGNSE SELEEPEKIS HQQSSTRLSN DEIRAILSNN PSEDDMVRCF ESLRKSLSKT
     KNPPIDEVIH CGLLQALVQA LSVENERVQY EAAWALTNIV SGSTEQTIAA VEAGVTIPLI
     HLSVHQSAQI SEQALWAVAN IAGDSSQLRD YVIKCHGVEA LMHLMEKVDQ LGDSHVRTIA
     WAFSNMCRHK NPHAPLEVLR VLSKGLVKLV QHTDRQVRQD ACWAVSYLTD GPDEQIELAR
     ESGVLPHVVA FFKEAENLVA PALRTLGNVA TGNDSLTQAV IDLGSLDEIL PLMEKTRSSS
     IVKECCWLVS NIIAGTQKQI QAVLDANLLP VLINVLKSGD HKCQFEASWA LSNLAQGGTN
     RQVVAMLEDN VVPALCQALL QTNTDMLNNT LETLYTLMLT VQNGYPHKVD ILHDQVEENG
     GLDSLERLQE SQSEQIYTQA YRIITQFFTD DDAGEKESHE NADPQDNKWS F
 
 
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