CLAP1_CAEEL
ID CLAP1_CAEEL Reviewed; 1378 AA.
AC Q95YF0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Protein CLASP-1;
GN Name=cls-1; ORFNames=C07H6.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
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 [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22613359; DOI=10.1016/j.ydbio.2012.05.016;
RA Espiritu E.B., Krueger L.E., Ye A., Rose L.S.;
RT "CLASPs function redundantly to regulate astral microtubules in the C.
RT elegans embryo.";
RL Dev. Biol. 368:242-254(2012).
CC -!- FUNCTION: Microtubule plus-end tracking protein that promotes the
CC stabilization of dynamic microtubules (By similarity). Operates
CC redundantly with cls-2 and cls-3 in regulating microtubule processes
CC which position the spindle during asymmetric cell division.
CC {ECO:0000250, ECO:0000269|PubMed:22613359}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC cls-2 and cls-3. Simultaneous RNAi knockdown with cls-2 produces
CC defective microtubule cortical contacts resulting in abnormal nuclear
CC rotation, defects in maintenance of spindle length and spindle
CC displacement. Simultaneous RNAi knockdown with cls-2 and cls-3 shows
CC nuclear rotation defects and excessive spindle displacement.
CC {ECO:0000269|PubMed:22613359}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR EMBL; FO080423; CCD63590.1; -; Genomic_DNA.
DR RefSeq; NP_498649.1; NM_066248.4.
DR AlphaFoldDB; Q95YF0; -.
DR STRING; 6239.C07H6.3; -.
DR EPD; Q95YF0; -.
DR PaxDb; Q95YF0; -.
DR PeptideAtlas; Q95YF0; -.
DR PRIDE; Q95YF0; -.
DR EnsemblMetazoa; C07H6.3.1; C07H6.3.1; WBGene00015580.
DR GeneID; 176064; -.
DR KEGG; cel:CELE_C07H6.3; -.
DR UCSC; C07H6.3; c. elegans.
DR CTD; 176064; -.
DR WormBase; C07H6.3; CE29074; WBGene00015580; cls-1.
DR eggNOG; KOG2956; Eukaryota.
DR GeneTree; ENSGT00940000168069; -.
DR HOGENOM; CLU_005060_1_0_1; -.
DR InParanoid; Q95YF0; -.
DR OMA; SMMEYDS; -.
DR OrthoDB; 66632at2759; -.
DR PhylomeDB; Q95YF0; -.
DR PRO; PR:Q95YF0; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015580; Expressed in material anatomical entity and 4 other tissues.
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; IGI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IGI:WormBase.
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; IMP:WormBase.
DR GO; GO:0051231; P:spindle elongation; IGI:UniProtKB.
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; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Reference proteome; Repeat.
FT CHAIN 1..1378
FT /note="Protein CLASP-1"
FT /id="PRO_0000272278"
FT REPEAT 168..206
FT /note="HEAT 1"
FT REPEAT 1305..1341
FT /note="HEAT 2"
FT REGION 231..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 740..767
FT /evidence="ECO:0000255"
FT COMPBIAS 266..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 153110 MW; E2DA7981417FD1CB CRC64;
MDTNWLYVLL QKSTADPLER LKLGNVILNE VSQRKVSPHP KLVNDFLDVM SGWLTGSNFK
VSTIGLEILD AALRTSPDVL ASYYFDRCSV LIERMGDAKV QVREMAINLC LQLAYLENSS
PVMLLDRLCV PGTGFQHKQW LVKVGSLNIL REFLSSSFAL VIQQAITLIP QLCRLTNDPN
SEVRDVSTQC LIDLMVYGGK PIVAKIAATR LINEQKMATL LQRYQTTVAT RGDLPPKHTI
TMETTPAQPS RNSLLRRSLR SPAKIIHPSA STTSFTSSAR LSTPPRPTTT AAQSLSLAPQ
TPSPLSLPSP SGGQMSRSRD LTRSSLRAPA GISISRYRSS SCAPAAQCAI TLDDFKKSFT
AVPKTTIYSN HDIREKLELA NLVLRNANED WSKRANQLKL IRSIIINCDE NIDRSLLISI
INELADALEF SIRDLRSQIV REAAVTCSFL FETFGMEVKN VAECVLPAAL AQVAVSTKVI
ASSAATLTVF IVQKIQTRQI FTTLSELSSS KAKEQRRQLA VVLETLIASW DLKSKQPILK
QIAQLVQNAI CDADGETRVA GRKAFAKLEQ LHGTTADLIF RELDPAKQKM LRDGVSSSSS
SLNSDRDNNN QKQQPNQQNI SQKFLSQRSA SAVDKSIQLS VKPQTTAIPS RPTAMPMNNR
LPKSSTSTSF SAVRSSGYGQ NQSTTPNRAK TPSDGFAGSS PHYTNGNNNN KSSSSSPSTS
THQTPIQRVA SNLGSSSFVA SLTQEQANCL QNAMNTAKDE MSKNNEDDEF LLDEIRKTPP
KEVPRSYNNS PFKPSNLDSS VHRSYNNNSP FRPSSGSVGS GSNGSVQSIE HILKACTSSS
LNEKRDAIVN LNQVITDPNL CQLECKNIGD TLSRLLAEGN NTLIISILDT ISIFIKFQYK
KLDNWLKLAL GKLFAKMGAD ALPNVKSALS STQKMFLTTF DPTFQLKAVC DFMCDPVHLL
SPKSRLALLE YICLLFEEIW PEDPRCLERQ THLDTPYTRA AIRKMFAWMF DPRIGAILMP
ACERLVCALF ALNAADFTMI FGELPSECRD WAYRILQLNG QQNNQKPIEK EKERFISNNN
YKPCPLDNEE IEKPIMKTTY STYESTRKEY SQTERIATEN QYSTPPPPDY RTSTAHLAKN
HVDQAAYIRN QLDAIRDFEK ADKLNEAMAN LHGMMCEGSF TLWNQFFDEL LDSIYQILST
FSQSIRKKLA LRILQKMCTA QATKLFDSTE IAISKVLQCA CTSDDNTMGV AAEDCLRILA
SHLPLTRVVL ISRRILSQDD DDQRGVLILK MLTRMFQDID IEELHLIVND VAPCFVTAYE
SMSSTVRKCA VFGLVALVQR VGMQRMEPHL RTLNASKLNL IDLYVGRAKS SESGASSN
