CLA1B_XENLA
ID CLA1B_XENLA Reviewed; 1456 AA.
AC A1A5K2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=CLIP-associating protein 1-B {ECO:0000250|UniProtKB:Q7Z460};
DE AltName: Full=Cytoplasmic linker-associated protein 1-B {ECO:0000312|Xenbase:XB-GENE-6049836};
DE AltName: Full=Protein Orbit homolog;
DE Short=Xorbit;
DE Short=Xorbit/CLASP;
GN Name=clasp1b {ECO:0000312|EMBL:AAI28691.1};
GN Synonyms=clasp1 {ECO:0000312|Xenbase:XB-GENE-6049836};
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] {ECO:0000312|EMBL:AAI28691.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAI28691.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CLIP1 AND CENPE, AND
RP SUBCELLULAR LOCATION.
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). {ECO:0000269|PubMed:16390996}.
CC -!- SUBUNIT: Interacts (via C-terminus) with clip1/clip-170, and cenpe.
CC {ECO:0000269|PubMed:16390996}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16390996}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:16390996}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16390996}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16390996}. 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.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000255}.
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DR EMBL; BC128690; AAI28691.1; -; mRNA.
DR RefSeq; NP_001128506.1; NM_001135034.1.
DR AlphaFoldDB; A1A5K2; -.
DR SMR; A1A5K2; -.
DR GeneID; 445862; -.
DR KEGG; xla:445862; -.
DR CTD; 445862; -.
DR Xenbase; XB-GENE-6049836; clasp1.S.
DR OMA; MFMDTHT; -.
DR OrthoDB; 66632at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 445862; Expressed in brain and 19 other tissues.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:InterPro.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:InterPro.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0043515; F:kinetochore binding; IEA:InterPro.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
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..1456
FT /note="CLIP-associating protein 1-B"
FT /id="PRO_0000397920"
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 442..479
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 930..967
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 1260..1297
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 1378..1415
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REGION 237..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 161045 MW; 64111A33A930310C CRC64;
MEQGMDYWLG QIQQKDVGKR LQVGPDLIEY LLDRQKSIDL EQDQTLLDRM VDGLATSWVN
SSNYKVALLG MDILSALVTR LQDRFRTQIG TVLPSLMDRL GDAKDSVRDQ DQNLLIKIME
QASNPQYMWE RMFSGFKHKN FRTREGVCLC LIATLNVYGA NSLTLSKIVP HICNLLGDPN
SQVRDAAINC LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG TMILSTTDKN
FDDEDSVDGN RPSSASSSAS SKAPQTARRG VSLGTGRRPG TSSAAPKTGG TAKEGAGALD
EEDFIRAFED APTVQIYSSR DLEESLNKIR EILSDDKHDW EQRISALKKI RSLLLAGAAE
YDNFFQQLRL LDGAFKLSAK DLRSQVVREA CITLGHLSSV LGNKFDHGAE AVMPTVFNLV
PNSTKIMATS GVVTIRLIIR HTHVPRLIPI ITSNCTSKSV AVRRRCYEFL DLLLQEWQTH
SLERHVSVLA ETIKKGIHDA DSEARIVARK CYWGFHGHFS KEAEQLFHAL ESSYQKALQS
HLKNSDSIVS LPQSDRSSSS SQESLNRPLS AKRSPTGSTV SRATSKSTTG SLQRSRSDID
VNAAATSKTK AASGASTAPF SSVAALPPGS YASLGRIRTR RQSSGSTTST ASTPADTRGR
SRAKVVSQSQ PGSRSSSPGK LLGSSYGGIA TGPQRVPQMP SEKRSKIPRS QGCSRETSPS
RTVLDRFGIS QPGRIPSAMR VLSSSTDLEA AVADALLLGD SRNKMKPVRR RYEPYGMYSD
DDANSDASSA CSERSYSSKN GGIPHYLRQT EDVAEVLNHC ASSNWSERKE GLVGLQNLLK
SQRLLSRVEL KRLCEIFTRM FADPHSKRVF SMFLETLVDF VIIHKDDLQD WLFILLTQLL
KKMGADLLGS VQAKVQKALD VTRDSFPFDQ QFNILMRFIV DQTQTPNLKV KVAILKYIES
LARQMDPTDF VNSSETRLAV SRIITWTTEP KSSDVRKAAQ VVLISLFELN TPEFTMLLGA
LPKTFQDGAT KLLHNHLKNS SNSSMGSPSN TIGRTPSRHS SSRASPLTSP TNCSHGGLSP
SMLDYDTENL NSDEIYSSLR GVTEAIEKFS FRSQVDLNEP VRRDGKKESE MGSCDAGMAS
PASDLRGGTD MVEGGRMALD NKTSLLNTQP PRAFTGPRGR EYNPYAYSDS INSYDKTALK
EAVFDDDMDQ LRDVPIDHSD LVADLLKELS NHNERVEERK GALCELLKIT REDNLAVWEE
HFKTILLLLL ETLGDKDHAI RALALRVLRE ILRNQPARFK NYAELTIMKT LEAHKDSHKE
VVRAAEEAAS TLAGSIHPEQ CIKVLCPIIQ TADYPINLAA IKMQTKVIER ISKESLHQIL
PDIIPGLLQG YDNTESSVRK ASVFCLVAVY SVIGEELKPY LAQLTGSKMK LLNLYIKRAQ
TTNSNSSSSS DVSTHS
