ID G3N2Y5_BOVIN Unreviewed; 1547 AA.
AC G3N2Y5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Cytoplasmic linker associated protein 1 {ECO:0000313|Ensembl:ENSBTAP00000056256.2};
GN Name=CLASP1 {ECO:0000313|Ensembl:ENSBTAP00000056256.2,
GN ECO:0000313|VGNC:VGNC:27389};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000056256.2, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000056256.2, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000056256.2,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000056256.2}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000056256.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Golgi
CC apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
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DR STRING; 9913.ENSBTAP00000056256; -.
DR Ensembl; ENSBTAT00000065657.2; ENSBTAP00000056256.2; ENSBTAG00000019781.6.
DR VEuPathDB; HostDB:ENSBTAG00000019781; -.
DR VGNC; VGNC:27389; CLASP1.
DR eggNOG; KOG2956; Eukaryota.
DR GeneTree; ENSGT00940000154817; -.
DR InParanoid; G3N2Y5; -.
DR OMA; LMEHKVQ; -.
DR TreeFam; TF101155; -.
DR Reactome; R-BTA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-BTA-2467813; Separation of Sister Chromatids.
DR Reactome; R-BTA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-BTA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-BTA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-BTA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-BTA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-BTA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-BTA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-BTA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-BTA-68877; Mitotic Prometaphase.
DR Reactome; R-BTA-8854518; AURKA Activation by TPX2.
DR Reactome; R-BTA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000019781; Expressed in granulosa cell and 106 other cell types or tissues.
DR ExpressionAtlas; G3N2Y5; baseline and differential.
DR GO; GO:0045180; C:basal cortex; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
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: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:0040001; P:establishment of mitotic spindle localization; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0051494; P:negative regulation of cytoskeleton organization; IEA:UniProt.
DR GO; GO:1902904; P:negative regulation of supramolecular fiber organization; IEA:UniProt.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:UniProt.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR048491; XMAP215_CLASP_TOG.
DR PANTHER; PTHR21567; CLASP; 1.
DR PANTHER; PTHR21567:SF28; CLIP-ASSOCIATING PROTEIN 1; 1.
DR Pfam; PF21040; CEP104-like_TOG; 1.
DR Pfam; PF12348; CLASP_N; 1.
DR Pfam; PF21041; XMAP215_CLASP_TOG; 1.
DR SMART; SM01349; TOG; 4.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 4: Predicted;
KW Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..232
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 168..206
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 319..551
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 858..1095
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 1298..1536
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 235..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1547 AA; 169972 MW; 6258FB59FCC99BF4 CRC64;
MEPRMEACLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL VDGLATSWVN
SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQALLLKIMD
QAANPQYVWD RMLGGFKHKN FRTREGTCLC LVATLNASGA HTLTLSKIVP HICNLLGDPN
SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN
FDDEDSVDGN RPSSASSTSS KAPASSRRNV GMGTTRRLGS SSLGSKSSAA KEGAGAVDEE
DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD
NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN
SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL
ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQTHL
KSSDSVVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSAS TAGSLQRSRS
DIDVNAAASA KSKISSAAGT APFSSAAALP PGSYASLGRI RTRRQSSGSA TNVASTPADS
RGRSRAKVVS QSQRSRSANP AGAGSRSSSP GKLLGSGYSG LTGGSSRGPP VTPSSEKRSK
IPRSQGCSRE TSPNRIGLAR SSRIPRPSTS QGCSRDASRE SSRDTSPARG FAPLDRFGLG
QAGRIPGSVN AMRVLSTSTD LEAAVADALL LGDSRSKKKP VRRRYEPYGM YSDDDANSDA
SSVCSERSYG SRNGGIPHYL RQTEDVAEVL NHCASSNWAE RKEGLLGLQN LLKSQRTLSR
VELKRLCEIF TRMFADPHSK VFSMFLETLV DFIIIHKDDL QDWLFVLLTQ LLKKMGADLL
GSVQAKVQKA LDVTRDSFPF DQQFNILMRF IVDQTQTPNL KVKVAILKYI ESLARQMDPT
DFINSSETRL AVSRIITWTT EPKSSDVRKA AQIVLISLFE LNTPEFTMLL GALPKTFQDG
ATKLLHNHLK NSSNTSVGSP SNTIGRTPSR HPSSRTSPLT SPTNCSHGGL SPSRLWGCNA
DGLSRHPPPF PQPNSIPTAP SHKTLRRSYS PSMLDYDTEN LNSEEIYSSL RGVTEAIEKF
SFRSQEDLNE PIKRDGRKDC DIVSRDGGIA SPATEGRGGS EVVEGGRTAL DNKTSLLNTQ
PPRAFPGPRA RDYSPYPYSD TISAYDKTAL KEAVFDDDME QLRDVPIDHS DLVADLLKEL
SNHNERVEER KGALLELLKI TREDSLGVWE EHFKTILLLL LETLGDKDHS IRALALRVLR
EILRNQPARF KNYAELTIMK TLEAHKDSHK EVVRAAEEAA STLASSIHPE QCIKVLCPIV
QTADYPINLA AIKMQTKVVE RIAKESLLQL LADIIPGLLQ GYDNTESSVR KASVFCLVAI
YSVIGEELKP HLAQLTGSKM KLLNLYIKRA QTTNSNSSSS SDVSTHS
//
