CLA1A_XENLA
ID CLA1A_XENLA Reviewed; 1460 AA.
AC Q4U0G1; A3KNB5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=CLIP-associating protein 1-A;
DE AltName: Full=Cytoplasmic linker-associated protein 1-A;
DE Short=XCLASP1;
GN Name=clasp1-a; Synonyms=clasp;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Mimori-Kiyosue Y., Akhmanova A.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION.
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 -!- 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}. Golgi apparatus, trans-Golgi
CC network {ECO:0000250}. Note=Localizes to microtubule plus ends.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4U0G1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4U0G1-2; Sequence=VSP_039722;
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR EMBL; DQ022563; AAY43788.1; -; mRNA.
DR EMBL; BC133747; AAI33748.1; -; mRNA.
DR RefSeq; NP_001088115.1; NM_001094646.1.
DR AlphaFoldDB; Q4U0G1; -.
DR SMR; Q4U0G1; -.
DR IntAct; Q4U0G1; 1.
DR PRIDE; Q4U0G1; -.
DR GeneID; 494817; -.
DR KEGG; xla:494817; -.
DR CTD; 494817; -.
DR Xenbase; XB-GENE-6466086; clasp1.L.
DR OrthoDB; 66632at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 494817; 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 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Golgi apparatus; Kinetochore; Microtubule;
KW Mitosis; Reference proteome; Repeat.
FT CHAIN 1..1460
FT /note="CLIP-associating protein 1-A"
FT /id="PRO_0000272275"
FT REPEAT 87..124
FT /note="HEAT 1"
FT REPEAT 163..200
FT /note="HEAT 2"
FT REPEAT 407..442
FT /note="HEAT 3"
FT REPEAT 443..479
FT /note="HEAT 4"
FT REPEAT 942..979
FT /note="HEAT 5"
FT REPEAT 1272..1309
FT /note="HEAT 6"
FT REPEAT 1390..1427
FT /note="HEAT 7"
FT REGION 237..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1084
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 640..685
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 786..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 637
FT /note="L -> LDGTTSKSD (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039722"
FT CONFLICT 586
FT /note="T -> A (in Ref. 1; AAY43788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1460 AA; 161499 MW; F88E1650288C4EF4 CRC64;
MEQGMDYWLG QIQQKDVGKR LQVGPDLIEY LLDRQKSIDL EQDQTLLDRM VDGLATSWVN
SSNYKVALLG MDILSELVSR LQDRFRTQLG TVLPSLMDRL GDAKDSVREQ DQSLLIKIME
QASNPQYVWE RMFSGFKHKN FRTREGVCLC LIATLNVYGA NSLTLSKIVP HICNLLGDPN
SQVRDAAINC LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG TMILSASDKN
FDDEDSVDGN RPSSASSSAS SKAPQTARRG VSLGTARRPG PSSAAAKTGG TAKEGAGALD
EEDFIRAFED VPNVQIYSSR DLEESLNKIR EILSDDKHDW EQRITALKKI RSLLLAGAAE
YDNFFQQLRL LDGAFKLSAK DLRSQVVREA CITLGHLSSV LGNKFDHGAE AIMPTVFNLV
PNSAKIMATS GIVAIRLIIR HTHVPRLIPI ITSNCTSKSV AVRRRCYDFL DLLLQEWQTH
SLERHVSVLA ETIKKGIHDA DSEAKIVARK CYWGFHSHFS KEAEHLFHTL ESSYQKALQS
HLKNSDSIVS LPQSDRSSSS SQESLNRPLS TKRSPTGSTV SRASSTTSKS TPGSLQRSRS
DIDVNAAATS KSKAASGAST APFISVAALP PGSYASLGRI RTRRQSSGST TSTASTPADT
RGRSRAKVVS QSQPGSRSNS PGKLLGSSYG GIATGPQRVP QMPSSEKRSR IPRSQGCSRE
TSPSRIGLDR FGISQQGRIP SAMRVLSSST DLEAAVADAL LLGDSRNKKK PVRRRYEPYG
MYSDDDANSD ASSACSERSY SSKNGGIPHY LRQTEDVAEV LNHCASSNWS ERKEGLLGLQ
NLLKSQRTLS RVELKRLCEI FTRMFADPHS KRVFSMFLET LVDFVIIHKD DLQDWLFILL
TQLLKKMGAD LLGSVQAKVQ KALDVTRDSF PFDQQFNILM RFIVDQTQTP NLKVKVAILK
YIESLARQMD PTDFVNSSET RLAVSRIITW TTEPKSSDVR KAAQIVLISL FELNTPEFTM
LLGALPKTFQ DGATKLLHNH LKNSSNSSMG SPSNTIGRTP SRHSSSRASP LTSPTNCSHG
GLSPSMLDYD TENLNSDEIY SSLRGVTEAI EKFSFRSQVD LNEPVRRDSK KESELGSCDV
GIASPASDLR GGTDMVEGGR MALDNKTSLL NTQPPRAFTG PRGREYNPYA YSDSINSYDK
TALKEAVFDD DMDQLRDVSI DHSDLVADLL KELSNHNERV EERKGALCEL LKITREDNLA
VWEEHFKTIL LLLLETLGDK DHAIRALALR VLREILRNQP ARFKNYAELT IMKTLEAHKD
SHKEVVRAAE EAASTLAGSI HPEQCIKVLC PIIQTADYPI NLAAIKMQAK VIERISKESL
HQILPDIIPG LLQGYDNTES SVRKASVFCL VAIYSVIGEE LKPYLAQLTG SKMKLLNLYI
KRAQTTNSNS SSSSDVSTHS
