ID   NSAPA_XENLA             Reviewed;         525 AA.
AC   Q1W1G1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Nucleolar and spindle-associated protein 1-A;
DE            Short=NuSAP A;
GN   Name=nusap1-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH IPO7; KPNA2 AND
RP   KPNB1, ASSOCIATION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX   PubMed=16571672; DOI=10.1091/mbc.e05-12-1178;
RA   Ribbeck K., Groen A.C., Santarella R., Bohnsack M.T., Raemaekers T.,
RA   Koecher T., Gentzel M., Goerlich D., Wilm M., Carmeliet G., Mitchison T.J.,
RA   Ellenberg J., Hoenger A., Mattaj I.W.;
RT   "NuSAP, a mitotic RanGTP target that stabilizes and cross-links
RT   microtubules.";
RL   Mol. Biol. Cell 17:2646-2660(2006).
CC   -!- FUNCTION: Microtubule-associated protein with the capacity to bundle
CC       and stabilize microtubules. May associate with chromosomes and promote
CC       the organization of meiotic or mitotic spindle microtubules around
CC       them. {ECO:0000269|PubMed:16571672}.
CC   -!- SUBUNIT: Interacts with DNA (By similarity). Interacts with
CC       microtubules, ipo7, kpna2 and kpnb1. Microtubule stabilization is
CC       inhibited by ipo7 and kpna2, while microtubule bundling is inhibited by
CC       kpnb1. Active GTP-bound ran causes dissociation of ipo7 and kpnb1.
CC       {ECO:0000250, ECO:0000269|PubMed:16571672}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16571672}. Nucleus
CC       {ECO:0000269|PubMed:16571672}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:16571672}. Note=Associates with meiotic spindle
CC       microtubules, particularly in the vicinity of chromosomes. May also
CC       associate with mitotic spindle microtubules.
CC   -!- SIMILARITY: Belongs to the NUSAP family. {ECO:0000305}.
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DR   EMBL; DQ448820; ABE01880.1; -; mRNA.
DR   RefSeq; NP_001089180.1; NM_001095711.1.
DR   AlphaFoldDB; Q1W1G1; -.
DR   SMR; Q1W1G1; -.
DR   GeneID; 734222; -.
DR   KEGG; xla:734222; -.
DR   CTD; 734222; -.
DR   Xenbase; XB-GENE-865275; nusap1.S.
DR   OrthoDB; 1573441at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 734222; Expressed in blastula and 14 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR   InterPro; IPR026756; NuSAP.
DR   PANTHER; PTHR15874; PTHR15874; 1.
DR   Pfam; PF16006; NUSAP; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; DNA-binding; Meiosis;
KW   Microtubule; Mitosis; Nucleus; Reference proteome.
FT   CHAIN           1..525
FT                   /note="Nucleolar and spindle-associated protein 1-A"
FT                   /id="PRO_0000302038"
FT   REGION          46..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  58781 MW;  453B2C158B82F7B9 CRC64;
     MEAPTLSELE GLRYSELQKL AKTAGLKANL KADKLLKALK VHFYPESKDE SPDYDGGSSL
     TDTDELNSSQ EKDEPVSVSF VTHRRGRGRK PLKNYDTPKD EFLTVSVGTG TESLASETDN
     TQDQNCLESK KKKVSPPTID NKHRKRSRSE DTSKQNNSET TEKRQKKASD ITSVPSAGKI
     PRYAGRLSKP ESKPSTPNFK KLHEAHFKKM ESIDKYMERK QKRLDTVSSS IQEMKMLTKK
     SNLLKLVEKT PVSDIKKPVK SRLSLLSSLP PTTGASPSRT PTNQRRSGRF SAANKSILFD
     RSGFKPSVLS SSKMNVRFSE ATKDNEHKRS LIKTPARKSS SFLAITPESE PRQMLPNVKK
     TPARKSLSVL AVTPESEPKQ MLPSVKKNEP MATPEKAKKT DLNTTIQPST VILESTCPQN
     KEIAITPFKF TAQTTETPNT NKKGRFDLQA SLSRPLGYQP HKGKLKPWGG SEENKCGSNN
     NVSVLKNNFK QPHLQTREDR RKQHEQDRKG KRDQTLGTRR GVPVQ