CLAP2_DANRE
ID CLAP2_DANRE Reviewed; 1288 AA.
AC Q6NYW6;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=CLIP-associating protein 2;
DE AltName: Full=Cytoplasmic linker-associated protein 2;
GN Name=clasp2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Microtubule plus-end tracking protein that promotes the
CC stabilization of dynamic microtubules. Involved in the nucleation of
CC noncentrosomal microtubules originating from the trans-Golgi network
CC (TGN). Required for the polarization of the cytoplasmic microtubule
CC arrays in migrating cells towards the leading edge of the cell. May act
CC at the cell cortex to enhance the frequency of rescue of depolymerizing
CC microtubules. This cortical microtubule stabilizing activity is
CC regulated at least in part by phosphatidylinositol 3-kinase signaling.
CC Also performs a similar stabilizing function at the kinetochore which
CC is essential for the bipolar alignment of chromosomes on the mitotic
CC spindle. {ECO:0000250|UniProtKB:O75122}.
CC -!- SUBUNIT: Interacts with microtubules. {ECO:0000250|UniProtKB:O75122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O75122}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:O75122}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O75122}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O75122}. Golgi
CC apparatus {ECO:0000250|UniProtKB:O75122}. Golgi apparatus, trans-Golgi
CC network {ECO:0000250|UniProtKB:O75122}. Cell membrane
CC {ECO:0000250|UniProtKB:O75122}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:O75122}. Note=Localizes to microtubule plus
CC ends. {ECO:0000250|UniProtKB:O75122}.
CC -!- DOMAIN: The two SXIP sequence motifs are important for targeting to the
CC growing microtubule plus ends. {ECO:0000250|UniProtKB:O75122}.
CC -!- DOMAIN: Two TOG regions display structural characteristics similar to
CC HEAT repeat domains and mediate interaction with microtubules.
CC {ECO:0000250|UniProtKB:O75122}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR EMBL; BC066436; AAH66436.1; -; mRNA.
DR RefSeq; NP_996955.1; NM_207072.2.
DR AlphaFoldDB; Q6NYW6; -.
DR STRING; 7955.ENSDARP00000039870; -.
DR PaxDb; Q6NYW6; -.
DR Ensembl; ENSDART00000144557; ENSDARP00000113962; ENSDARG00000020345.
DR GeneID; 404604; -.
DR KEGG; dre:404604; -.
DR CTD; 23122; -.
DR ZFIN; ZDB-GENE-040426-2343; clasp2.
DR eggNOG; KOG2956; Eukaryota.
DR GeneTree; ENSGT00940000155574; -.
DR InParanoid; Q6NYW6; -.
DR OrthoDB; 66632at2759; -.
DR PhylomeDB; Q6NYW6; -.
DR Reactome; R-DRE-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q6NYW6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000020345; Expressed in retina and 26 other tissues.
DR ExpressionAtlas; Q6NYW6; baseline.
DR GO; GO:0045180; C:basal cortex; IBA:GO_Central.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
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:0010458; P:exit from mitosis; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; 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:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISS:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR034085; TOG.
DR Pfam; PF12348; CLASP_N; 1.
DR SMART; SM01349; TOG; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell membrane; Cell projection; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Golgi apparatus; Kinetochore;
KW Membrane; Microtubule; Mitosis; Reference proteome; Repeat.
FT CHAIN 1..1288
FT /note="CLIP-associating protein 2"
FT /id="PRO_0000089848"
FT REPEAT 174..209
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 210..246
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 251..288
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 718..755
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 780..817
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 1047..1086
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 1091..1128
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 1167..1204
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 1209..1246
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..312
FT /note="TOG 1"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT REGION 314..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..889
FT /note="TOG 2"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT REGION 891..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 490..493
FT /note="SXIP motif 1"
FT /evidence="ECO:0000250|UniProtKB:O75122, ECO:0000305"
FT MOTIF 527..530
FT /note="SXIP motif 2"
FT /evidence="ECO:0000250|UniProtKB:O75122, ECO:0000305"
FT COMPBIAS 314..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1288 AA; 140303 MW; A2E2882713298598 CRC64;
MALSLSQDRS FDDDDSVDGS RPSSAQAAFK VPKVPKKPAE SASSSRRPSA TGAAKSGASK
EGAGAVDEED FIKAFTDVPT VQIYSTRDLE DNLNKIREVL SDDKHDWDHR ANALKKIRSL
LVAGATDYDC FYQHLRLLDG AFKLSAKDLR SQVVREACIT VAYLSTLLGN KFDHGAEGIV
PVLFNLIPNC AKVMATSGTA AIRIIIRHTH VPRLIPLIAS NCTSKSVAVR RRCYEFLDLL
LQEWQTHSLE RHAAVLVESI KKGIRDADAE ARVEARKAYW GLRAHFPGEA ESLYNSLESS
YQRTLQSCLK SSGSVASLPQ SDRSSSSSQE SLNRPLSKWS AAPGRVPAGS KSSGSPASLQ
RSRSDVDVNA AAGAKARHSG QAGGAGRVTT GLTPGSYASL GRLRTKQTLS TASSVGSSQV
DSRGRTRSKM ASQSQRSDDS DCTPGSQSAT PVGAGSRSGS PGRVLASTAL STLSTGAQRV
SAAPGSHRRS RIPRSQGCSR DSSPTRLSVA PSNISHIYNG SKGARGSRIP RPSVSQGCSR
EASRESSRDT SPVRSFTPLG SGLGMSQSSR LSSSVSAMRV LNTGSDVEEA LADALKKPAR
RRYDTYGMYS DDDANSDASS ACSERSYSSR NGSIPTYMRQ TEDVAEVLNR CASANWSERK
EGLMGLQALL KNHRTLSRVE LKRLCEIFTR MFADPHSKRD PRGFGTVESG ISSASFKRVF
SMFLETLVDF IAVHKEDLQD WLFVLLTQLL KKMGADLLGS VQAKVQKALD VTRESFPNDL
QFTILMRFTV DQTQTPNLKV KVAILKYIET LTLQMEPQDF VNTGETRLAV SRIITWTTEP
KSSDVRKAAQ SVLISLFQLN TPEFTMLLGA LPKTFQDGAT KLLQNHLRNT GNTAQASIGS
PLTRHTPRSP ASWSSPLTSP TNTSQNTPSP SAFDYDTENM NSEEIYSSLR GVSQAIQNFS
VRSQEDMTEP PRKREGDGGE ETVDSGRTAL DNKTSLLNTM PLLSSSPRPS RDYQPVNYSD
SSFGSSSFNK SLKDADQEES LTDDSGVDQS EVVAELLKEL SNHSERVEER KAALCELMRL
IRETQLHVWD EHFKTILLLL LETLGDGEHV IRALALRVLK EILNRQPWRF KNYAELTIMK
ALEAHKDPHK EVVRAAEEAA SMLATSISPD QCIKVLCPII QSADYPINLA AIKMLTKVID
RLPKEGLIQM LPEIVPGLIQ GYDNSESSVR KACVFCLVAI YAVIGEDLKP HLSQLSGSKL
KLLNLYIKRA QSGSSGSDQS SDVGGQGL
