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CLAP2_CAEBR
ID   CLAP2_CAEBR             Reviewed;         791 AA.
AC   Q61J98; A8X9V7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Protein CLASP-2;
DE   Flags: Fragment;
GN   Name=cls-2; ORFNames=CBG09877;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Probable microtubule plus-end tracking protein that promotes
CC       the stabilization of dynamic microtubules. Required for the formation
CC       of mitotic and meiotic spindles. Specifically promotes the
CC       polymerization of kinetochore-bound microtubules. Also required for
CC       cytoplasmic streaming (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with hcp-1 and hcp-2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC       Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250}. Note=Localized to kinetochores
CC       during metaphase, and to the spindle region. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAP29422.3; Type=Erroneous gene model prediction; Note=The C-terminus of this protein appears likely to be in the unsequenced region.; Evidence={ECO:0000305};
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DR   EMBL; HE601459; CAP29422.3; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q61J98; -.
DR   SMR; Q61J98; -.
DR   STRING; 6238.CBG09877; -.
DR   PRIDE; Q61J98; -.
DR   EnsemblMetazoa; CBG09877.1; CBG09877.1; WBGene00031391.
DR   WormBase; CBG09877; CBP37613; WBGene00031391; Cbr-cls-2.
DR   eggNOG; KOG2956; Eukaryota.
DR   HOGENOM; CLU_005060_1_0_1; -.
DR   InParanoid; Q61J98; -.
DR   OMA; FSWMSDQ; -.
DR   OrthoDB; 66632at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0045180; C:basal cortex; IBA:GO_Central.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR   GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024395; CLASP_N_dom.
DR   InterPro; IPR034085; TOG.
DR   Pfam; PF12348; CLASP_N; 1.
DR   SMART; SM01349; TOG; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Kinetochore; Meiosis; Microtubule; Mitosis; Reference proteome.
FT   CHAIN           1..>791
FT                   /note="Protein CLASP-2"
FT                   /id="PRO_0000272279"
FT   REGION          259..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         791
SQ   SEQUENCE   791 AA;  87466 MW;  5ABA367EBBB0F50D CRC64;
     MSRVVSRTVP GGACVVNKDD FLKSFNDVDK VSVSSLADAK SKFDQVIAIL SKSQEDWNKR
     RTQLQIIRSI VINCEDVIGR DQLLGQLVRL ADCLDLSVKD LRSQILREAA ITCSFLFEKY
     GNDVHQIAER CLPTAFSQLA VSTKVMATSG ATLTLFLVQY VQTKQIFTCL TTYSTSKDKN
     QRRQLCVLLE IVIEHWNDKL KKSILPQIME LIKSAISDAD PETRAAGRKA FNKLDAIHSE
     EADKLFASVD ANKQKMLRAS DAASSSTSVN SERGSAPFRS KLSAGSVGGM RNVPNISSKF
     LAQRSASAID TKQVTRMTTS VSRTPNTRPM TTRTLSKVDT SPGGSKFARP TVGTLGPRTT
     SNLRARGSVP TSQPGSRNGS PPRRPSTTGT LPMEMQRVKS NLGSSSFVSS LTPDQAESLQ
     KAMNTAKESL GQPSRTEDDE FLLPKRKPKT PQKSAVDISR VEAVIRACVS TSANEKRDGI
     KMLSIIVSEP NLSQIELKNI GQVLNRLLGE ATNPVVLESV ASFVKAHHSR LSEWLKLGLG
     KMFAKKGSEM MPIMKKHIVT TINAILSSFD PALQLKATCE LMCDPIHLLS PKARVALLEY
     LTDLLEKHME RGSPFNTKEV KATILKMFSW MSDQRNMQQI VPHGEKVLCG LFALNAADFS
     ALFNDFNPDY REWAYRILQA HGHNQHAPAP ESPSPVRDQQ VRANISNTAA QIEDFVVARN
     FELSAEKSPT SRGMLTSGFK RTDAEPLRPL ESDMNTQRMD DISINESFDR LKVRILETTG
     FYAAFKVDFQ E
 
 
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