CLAP1_CAEBR
ID CLAP1_CAEBR Reviewed; 1333 AA.
AC Q61KX5; A8X885;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Protein CLASP-1;
GN ORFNames=CBG09173;
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: Microtubule plus-end tracking protein that promotes the
CC stabilization of dynamic microtubules. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR EMBL; HE601302; CAP28846.3; -; Genomic_DNA.
DR AlphaFoldDB; Q61KX5; -.
DR STRING; 6238.CBG09173; -.
DR EnsemblMetazoa; CBG09173a.1; CBG09173a.1; WBGene00030813.
DR WormBase; CBG09173a; CBP37580; WBGene00030813; -.
DR eggNOG; KOG2956; Eukaryota.
DR HOGENOM; CLU_005060_1_0_1; -.
DR InParanoid; Q61KX5; -.
DR OMA; KISTRDM; -.
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:0030953; P:astral microtubule organization; IEA:EnsemblMetazoa.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IEA:EnsemblMetazoa.
DR GO; GO:0051231; P:spindle elongation; IEA:EnsemblMetazoa.
DR Gene3D; 1.25.10.10; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR Pfam; PF12348; CLASP_N; 1.
DR Pfam; PF02985; HEAT; 1.
DR SMART; SM01349; TOG; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Reference proteome;
KW Repeat.
FT CHAIN 1..1333
FT /note="Protein CLASP-1"
FT /id="PRO_0000272277"
FT REPEAT 168..206
FT /note="HEAT 1"
FT REPEAT 1266..1304
FT /note="HEAT 2"
FT REGION 269..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 360..389
FT /evidence="ECO:0000255"
FT COMPBIAS 269..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1333 AA; 148065 MW; 98DC058741F5DD95 CRC64;
MDTNWLYVLL QKSTADPLER LKLGNVILNE ISQRKVSPHP KLVNDFLDVM SGWLTGSNFK
VTIIGLEILD AALRTSPEVL ASYYFDRLSV LIERMGDAKV QVREMAINLC RQLAYLENSS
PVMLLDRLCV HGTGFEHKQW LVKVGSLNIL RDFLSDSFAL VIPQAINLIP QLCRLTNDPN
SEVRDASTNC LVDLMVFGGK SIIAKIANTR ILNEQKMATL LQRYESTIAT RGDLPPKHSI
PIETSSIPRN NLLRRSLRSP AKIIHPSAST TSFTSSARLS TPPRTNAPSL SPSPSTPSPL
SLPAANGRSR DLARSSLRAP AGMSLSRYRS SSCAPAAQCA ITLDDFKKAF NAVPKISIYS
NSDVREKLET ANSVLRNANE DWSKRANQLK LIRSVILNSD DSIDQRLLLS LINELADALE
FSIRDLRSQI VREAAITCSF LFEHFGMDVR NVAECVLPAA LAQVAVSTKI MASSAATLTV
FIVQKIQTRQ IFQTLFDLST SKSKEQRRQL ANLLETLISS WDLKVKQPIL KSISQLVQNA
ICDADGETRV AGRKAFAKLE QLHGAAADQI FRELDPAKQK MLRDGVSSSS SSLNSDRDNN
NQKQPQQPQQ NISQKFLSQR SASALDNKSQ VLSIAKPQQS NPSRPTAMPV NNRLPKSSTS
SSFSAVRSSG YGQSRAKTPS DGFGGTNFNN NNNNNNKSSS SSPSTSTHQT PIQRVASNLG
SSSFVASLTQ EQASSLQNAM DLAKDEMSKN NEDDEFLLAE VRKTPPKETS PPASLYARGY
GNGSNGSNNS SNNSIQSVEH ILKACTSSSI NEKRDAIISL SQKLLDRNLD SLECKNIGDT
LSRLLAEGNT TLIISILETI SIFVKCHYKK LDGWLKLALG KLFAKMGADS LPNVKSALSS
TQKMFLTTFD PSTQLKEVCD FMCDPVHLLA PKSRLALLEY ICLLFEEIWP EDPRCLERQT
QLDTPYTRAA VRKMFAWMFD PRIGAILMPA CERLVCALFA LNAADFTMIF GDLPPECRDW
AYRILQLNGQ QQSAQRQQIM EKEAITMTNN NYKPCPPEVE KFEKVSVKAS FSTYEATRVP
EPQDYRKPTV HLAKNHVEQA AYIRNQMDLM RDFQKPDRVN EAMANLHGMM CEGSFTLWNQ
FFDELLDEIY QILSTLSQSI RKKLAMRILQ KMCTAQATKL FDSTEIAISK VLQCACTSED
NTMSVAAEDC LRILATHLPL PRIVQISRRI LSQDDDDQRG VLILKMLTRM FQDIDVDELH
MIVDDVAPCF VSAYDSTSSS VRKCAVFGLV ALVQRVGMPR LETHLRKLNA TKLNLIDLYV
GRAKSSESGT SSN