ID   NSAPC_XENLA             Reviewed;         525 AA.
AC   A1L3I5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Nucleolar and spindle-associated protein 1-C;
DE            Short=NuSAP C;
GN   Name=nusap1-c;
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 [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 them
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DNA, microtubules, ipo7, kpna2 and kpnb1.
CC       Microtubule stabilization is inhibited by ipo7 and kpna2, while
CC       microtubule bundling is inhibited by kpnb1. Active GTP-bound ran causes
CC       dissociation of ipo7 and kpnb1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associates with
CC       meiotic or mitotic spindle microtubules, particularly in the vicinity
CC       of chromosomes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NUSAP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI30119.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC130118; AAI30119.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; A1L3I5; -.
DR   SMR; A1L3I5; -.
DR   Proteomes; UP000186698; Genome assembly.
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   2: Evidence at transcript 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-C"
FT                   /id="PRO_0000302040"
FT   REGION          43..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..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;  58833 MW;  9BE4D11CEE60C68E CRC64;
     MEAPTLSELE GLRYSELQKL AKTVGLKANL KADKLLKDLK VHFYPESKDE SPDYDGGSSL
     TDTDELNSSQ EKDEPVSVSF VTHRRGRGRK PLKNHDTPKD EFLSVSVGAG TESLASETDN
     TQHQNCLESK KKEVSPPTID NKHRKRSRSE DTSKQNNLET TEKRQKKASD ITSAPSAGKI
     PRYVGRLSKP ESKPSTPNFK KLHEAHFKKM ESIDKYMERK QKRLDTVSSS IQEMKMLTKK
     SNLLKLVEKT PVSDIKKPVK SRLSLLSSLP PTTGASPSRT PTNQRRSGRF SAANKSILFD
     RSGFKPSVLS SSKMNVRFSE ATKDNEHKRS LIKTPARKSS SFLAITPESE PRQMLPNVKK
     TPARKSLSVL AVTPESEPKQ MLPSVKKNEP MTTPEKAKKT DLNTTIQPST VILESTCPQN
     KEIAITPFKF TAQTTETPNT NKKGKFNLQA SLSRPLGYQP HKGKLKPWGG SEENKCGSNN
     NVSVLKNNFK QPHLQTREDR RKQHEQDRKG KRDQTLGTRR GVPVQ