CLAP2_RAT
ID CLAP2_RAT Reviewed; 1286 AA.
AC Q99JD4;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=CLIP-associating protein 2;
DE AltName: Full=Cytoplasmic linker-associated protein 2;
GN Name=Clasp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11290329; DOI=10.1016/s0092-8674(01)00288-4;
RA Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
RA Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
RA Galjart N.;
RT "Clasps are CLIP-115 and -170 associating proteins involved in the regional
RT regulation of microtubule dynamics in motile fibroblasts.";
RL Cell 104:923-935(2001).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-20; SER-333; SER-413;
RP SER-535; SER-581 AND SER-947, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 by attaching their plus-ends to cortical platforms
CC composed of ERC1 and PHLDB2. This cortical microtubule stabilizing
CC activity is regulated at least in part by phosphatidylinositol 3-kinase
CC signaling. Also performs a similar stabilizing function at the
CC kinetochore which is essential for the bipolar alignment of chromosomes
CC on the mitotic spindle. Acts as a mediator of ERBB2-dependent
CC stabilization of microtubules at the cell cortex.
CC {ECO:0000250|UniProtKB:O75122}.
CC -!- SUBUNIT: Interacts with microtubules. Interacts with MAPRE1; probably
CC required for targeting to the growing microtubule plus ends. Interacts
CC with CLIP2, ERC1, MAPRE3, PHLDB2 and RSN. The interaction with ERC1 may
CC be mediated by PHLDB2. Interacts with GCC2; recruits CLASP2 to Golgi
CC membranes (By similarity). Interacts with MACF1 (By similarity).
CC {ECO:0000250|UniProtKB:O75122, ECO:0000250|UniProtKB:Q8BRT1}.
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:Q8BRT1}. 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. Localizes to centrosomes, kinetochores and the mitotic spindle
CC from prometaphase. Subsequently localizes to the spindle midzone from
CC anaphase and to the midbody from telophase. In migrating cells
CC localizes to the plus ends of microtubules within the cell body and to
CC the entire microtubule lattice within the lamella. Localizes to the
CC cell cortex and this requires ERC1 and PHLDB2. The MEMO1-RHOA-DIAPH1
CC signaling pathway controls localization of the phosphorylated form to
CC the cell membrane (By similarity). {ECO:0000250|UniProtKB:O75122}.
CC -!- DOMAIN: The two SXIP sequence motifs mediate interaction with MAPRE1;
CC this is necessary for targeting to the growing microtubule plus ends.
CC {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 -!- PTM: Phosphorylated by GSK3B. Phosphorylation by GSK3B may negatively
CC regulate binding to microtubule lattices in lamella.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR EMBL; AJ288060; CAC35166.1; -; mRNA.
DR RefSeq; NP_446174.1; NM_053722.2.
DR AlphaFoldDB; Q99JD4; -.
DR BioGRID; 250360; 4.
DR IntAct; Q99JD4; 2.
DR MINT; Q99JD4; -.
DR STRING; 10116.ENSRNOP00000012545; -.
DR iPTMnet; Q99JD4; -.
DR PhosphoSitePlus; Q99JD4; -.
DR jPOST; Q99JD4; -.
DR PaxDb; Q99JD4; -.
DR PRIDE; Q99JD4; -.
DR GeneID; 114514; -.
DR KEGG; rno:114514; -.
DR UCSC; RGD:619789; rat.
DR CTD; 23122; -.
DR RGD; 619789; Clasp2.
DR VEuPathDB; HostDB:ENSRNOG00000009161; -.
DR eggNOG; KOG2956; Eukaryota.
DR HOGENOM; CLU_005060_0_0_1; -.
DR InParanoid; Q99JD4; -.
DR OrthoDB; 66632at2759; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q99JD4; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000009161; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; Q99JD4; baseline and differential.
DR Genevisible; Q99JD4; RN.
DR GO; GO:0045180; C:basal cortex; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:RGD.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0002162; F:dystroglycan binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:RGD.
DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISO:RGD.
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:0051895; P:negative regulation of focal adhesion assembly; ISO:RGD.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:RGD.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; ISO:RGD.
DR GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; ISO:RGD.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:RGD.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISO:RGD.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; IMP:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0010470; P:regulation of gastrulation; ISO:RGD.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:RGD.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR GO; GO:0006903; P:vesicle targeting; ISO:RGD.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Cell projection; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Golgi apparatus; Kinetochore;
KW Membrane; Microtubule; Mitosis; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1286
FT /note="CLIP-associating protein 2"
FT /id="PRO_0000089851"
FT REPEAT 179..214
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 215..251
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 256..293
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 702..739
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 764..801
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 1046..1083
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 1090..1127
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 1208..1245
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Golgi localization"
FT /evidence="ECO:0000250"
FT REGION 17..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..317
FT /note="TOG 1"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT REGION 320..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..565
FT /note="Interaction with microtubules, MAPRE1 and MAPRE3"
FT /evidence="ECO:0000250"
FT REGION 492..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..873
FT /note="TOG 2"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT REGION 864..1286
FT /note="Interaction with RSN and localization to the Golgi
FT and kinetochores"
FT /evidence="ECO:0000250"
FT REGION 870..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1286
FT /note="Required for cortical localization"
FT /evidence="ECO:0000250"
FT MOTIF 500..503
FT /note="SXIP motif 1; mediates interaction with MAPRE1 and
FT targeting to microtubule plus ends"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOTIF 523..526
FT /note="SXIP motif 2; mediates interaction with MAPRE1 and
FT targeting to microtubule plus ends"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT COMPBIAS 454..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BRT1"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BRT1"
FT MOD_RES 779
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 944
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75122"
SQ SEQUENCE 1286 AA; 140638 MW; C1742635DADC3F09 CRC64;
MRRLICKRIC DYKSFDDEES VDGNRPSSAA SAFKVPAPKT PGNPVNSARK PGSAGGPKAG
GTSKEGGAGA VDEDDFIKAF TDVPSIQIYS SRELEETLNK IREILSDDKH DWDQRANALK
KIRSLLVAGA AQYDCFFQHL RLLDGALKLS AKDLRSQVVR EACITVAHLS TVLGNKFDHG
AEAIVPTLFN LVPNSAKVMA TSGCAAIRFI IRHTHVPRLI PLITSNCTSK SVPVRRRSFE
FLDLLLQEWQ THSLERHAAV LVETIKKGIH DADAEARVEA RKTYMGLRNH FPGEAETLYN
SLEPSYQKSL QTYLKSSGSV ASLPQSDRSS SSSQESLNRP FSSKWSTANP SAVAGRVSVG
GSKASPLPGS LQRSRSDIDV NAAAGAKAHH AAGQAVRSGR LGAGALNPGS YASLEDTSDK
MDGTASEDGR VRAKLSTPLV AVGNAKTDSR GRSRTKMVSQ SQPGSRSGSP GRVLTTTALS
TVSSGAQRIL VNSASAQKRS KIPRSQGCSR EASPSRLSVA RSSRIPRPSV SQGCSREASR
ESSRDTSPVR SFQPLGPGYG MSQSSRLSSS VSAMRVLNTG SDVEEAVADA LLLGDIRTKK
KPARRRYESY GMHSDDDANS DASSACSERS YSSRNGSIPT YMRQTEDVAE VLNRCASSNW
SERKEGLLGL QNLLKNQRTL SRVELKRLCE IFTRMFADPH GKVFSMFLET LVDFIQVHKD
DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ KALDVTRESF PNDLQFNILM RFTVDQTQTP
SLKVKVAILK YIETLAKQMD PGDFINSSET RLAVSRVITW TTEPKSSDVR KAAQSVLISL
FELNTPEFTM LLGALPKTFQ DGATKLLHNH LRNTGNGTQS SMGSPLTRPT PRSPANWSSP
LTSPTNTSQN TLSPSAFDYD TENMNSEDIY SSLRGVTEAI QNFSFRSQED MSEPLKRDPK
KEDGDTVCSG PGMSDPRAGG DAPDSSQPAL DNKASLLHSV PLHSSPRSRD YNPYNYSDSI
SPFNKSALKE AMFDDDADQF PDDLSLDHSD LVAELLKELS NHNERIEERK IALYELMKLT
QEESFSVWDE HFKTILLLLL ETLGDKEPTI RALALKVLKE ILRHQPARFK NYAELTVMKT
LEAHKDPHKE VVRSAEEAAS VLATSISPEQ CIKVLCPIIQ TADYPINLAA IKMQTKVIER
VSKETLNLLL PEIMPGLIQG YDNSESSVRK ACVFCLVAVH AVIGDELKPH LSQLTGSKMK
LLNLYIKRAQ TGSAGADPTT DVSGQS
