CLAP1_XENTR
ID CLAP1_XENTR Reviewed; 1452 AA.
AC A1A5G0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=CLIP-associating protein 1 {ECO:0000250|UniProtKB:Q7Z460};
DE AltName: Full=Cytoplasmic linker-associated protein 1 {ECO:0000312|Xenbase:XB-GENE-6049805};
GN Name=clasp1 {ECO:0000312|Xenbase:XB-GENE-6049805};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAI28635.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAI28635.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP INTERACTION WITH CLIP1 AND CENPE.
RX PubMed=16390996; DOI=10.1083/jcb.200508180;
RA Hannak E., Heald R.;
RT "Xorbit/CLASP links dynamic microtubules to chromosomes in the Xenopus
RT meiotic spindle.";
RL J. Cell Biol. 172:19-25(2006).
CC -!- FUNCTION: Microtubule plus-end tracking protein that promotes the
CC stabilization of dynamic microtubules during anaphase. Plays a crucial
CC role in chromatin-induced microtubule formation. May also act at
CC microtubule minus ends. May be involved in the nucleation of
CC noncentrosomal microtubules originating from the trans-Golgi network
CC (TGN) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via C-terminus) with clip1/clip-170, and cenpe.
CC {ECO:0000269|PubMed:16390996}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:A1A5K2}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:A1A5K2}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:A1A5K2}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:A1A5K2}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250}. Note=Localizes to
CC microtubule plus ends. Associates with spindle microtubules, spindle
CC poles, and kinetochores during metaphase, and shifts to the central
CC spindle in late anaphase (By similarity).
CC {ECO:0000250|UniProtKB:A1A5K2}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000255}.
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DR EMBL; BC128634; AAI28635.1; -; mRNA.
DR RefSeq; NP_001090708.1; NM_001097239.1.
DR AlphaFoldDB; A1A5G0; -.
DR SMR; A1A5G0; -.
DR PRIDE; A1A5G0; -.
DR DNASU; 100036688; -.
DR GeneID; 100036688; -.
DR KEGG; xtr:100036688; -.
DR CTD; 23332; -.
DR Xenbase; XB-GENE-6049805; clasp1.
DR InParanoid; A1A5G0; -.
DR OrthoDB; 66632at2759; -.
DR Reactome; R-XTR-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-XTR-2467813; Separation of Sister Chromatids.
DR Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-XTR-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-XTR-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-XTR-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-XTR-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-XTR-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-XTR-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR Reactome; R-XTR-8854518; AURKA Activation by TPX2.
DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0045180; C:basal cortex; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:InterPro.
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:0043515; F:kinetochore binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
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:0034453; P:microtubule anchoring; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR Gene3D; 1.25.10.10; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028399; CLASP_1.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR21567:SF28; PTHR21567:SF28; 3.
DR Pfam; PF12348; CLASP_N; 2.
DR SMART; SM01349; TOG; 4.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Kinetochore; Microtubule; Mitosis; Reference proteome;
KW Repeat.
FT CHAIN 1..1452
FT /note="CLIP-associating protein 1"
FT /id="PRO_0000397921"
FT REPEAT 68..87
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 88..124
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 163..200
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 407..442
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 443..479
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 926..963
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 1256..1293
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 1374..1411
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REGION 239..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1452 AA; 160245 MW; 67AB39EC81F41C3C CRC64;
MEQGMDYWLG QIQQKDVGKR LQVGPDLMEY LSDRQKSIDL EQDQTVLDRM VDGLATSWVN
SSNYKVALLG MDILSALVTR LQDRFRSQIG TVLPSLMDRL GDAKDSVREQ DQNLLIKIME
QASNPQYVWE RMFSGFKHKN FRTREGVCLC LIATLNVYGA HSLTLSKIVP HICNLLGDPN
SQVRDAAINC LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG TMILSSADKN
FDDEDSVDGN RPSSASSSAS SKAPQAARRG VSLGTARRPG TSSAAPKPGG TAKEGAGGVD
EEDFIRGFED VPTVQIYSSR DLEESLNKIR EILSDDKHDW EQRISALKKI RSLLLAGAAE
YDTFFPQLRL LDGAFKLSAK DLRSQVVREA CITLGHLSSV LGNKFDHGAE AIMPTVFNLV
PNSAKIMATS GVVAIRLIIR QTHVPRLIPI ITSNCTSKSV AVRRRCYEFL DLLLQEWQTH
SLERHVSVLA ETIKKGIHDA DSEARIVARK CYWGFHSHFS KEAEQLFHTL ESSYQKALQS
HLKNSDSIVS LPQSDRSSSS SQESLNRPLS AKRSPTGSTV SRASTATSKS TPGSLQRSRS
DIDVNAATCA KSKATSGASA APFSSVAALP PGSYASLGRI RTRRQSSGST TSTASTPADT
RGRSRAKVVS QSQPGSRSSS PGKLLGSGYG GIASGPQRVP QMPSSEKRSK IPRSQGCSRE
TSPSRIGLDR FGISQPGRIP SAMRVLSSST DLEAAVADAL KKPVRRRYEP YGMYSDDDAN
SDASSACSER SYSSKNGGIP HYLRQTEDVA EVLNHCASSN WSERKEGLIG LQNLLKSQRT
LSRVELKRLC EIFTRMFADP HSKRVFSMFL ETLVDFVIIH KDDLQDWLFI LLTQLLKKMG
ADLLGSVQAK VQKALDVTRD SFPFDQQFNI LMRFIVDQTQ TPNLKVKVAI LKYIESLARQ
MDPTDFVNSS ETRLAVSRII TWTTEPKSSD VRKAAQVVLI SLFELNTPEF TMLLGALPKT
FQDGATKLLH NHLKNSSNSS MGSPSNTIGR TPSRHSSSRA SPLTSPTNCS HGGLSPSMLD
YDTENLNSDE IYSSLRGVTE AIEKFSFRSQ VDLNEPVRRE GKKESELGSC DVGIASPASD
LRGGTDMVEG GRMALDNKTS LLNTQPPRAF TGPRGREYNP YAYSDSINSY DKTALKEAVF
DDDMDQLRDV PIDHSDLVAD LLKELSNHNE RVEERKGALC ELLKITREDS LAVWEEHFKT
ILLLLLETLG DKDHAIRALA LRVLREILRN QPARFKNYAE LTIMKTLEAH KDSHKEVVRA
AEEAASTLAG SIHPEQCIKV LCPIIQTADY PINLAAIKMQ TKVIERISKE SLHQILPDII
PGLLQGYDNT ESSVRKASVF CLVAIYSVIG EELKPYLAQL TGGKMKLLNL YIKRAQTTNS
NSSSSSDVST HS
