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Database: UniProt
Entry: A0A0A6YXZ1_MOUSE
LinkDB: A0A0A6YXZ1_MOUSE
Original site: A0A0A6YXZ1_MOUSE 
ID   A0A0A6YXZ1_MOUSE        Unreviewed;      1244 AA.
AC   A0A0A6YXZ1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 2.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=CLIP associating protein 1 {ECO:0000313|Ensembl:ENSMUSP00000142203.3};
GN   Name=Clasp1 {ECO:0000313|Ensembl:ENSMUSP00000142203.3,
GN   ECO:0000313|MGI:MGI:1923957};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000142203.3, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:15345747}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [2] {ECO:0007829|PubMed:16452087}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000142203.3, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000142203.3,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5] {ECO:0000313|Ensembl:ENSMUSP00000142203.3}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000142203.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
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DR   AlphaFoldDB; A0A0A6YXZ1; -.
DR   jPOST; A0A0A6YXZ1; -.
DR   ProteomicsDB; 311958; -.
DR   Antibodypedia; 33401; 332 antibodies from 32 providers.
DR   Ensembl; ENSMUST00000191823.6; ENSMUSP00000142203.3; ENSMUSG00000064302.15.
DR   AGR; MGI:1923957; -.
DR   MGI; MGI:1923957; Clasp1.
DR   VEuPathDB; HostDB:ENSMUSG00000064302; -.
DR   GeneTree; ENSGT00940000154817; -.
DR   HOGENOM; CLU_1247868_0_0_1; -.
DR   ChiTaRS; Clasp1; mouse.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000064302; Expressed in myocardium of ventricle and 250 other cell types or tissues.
DR   ExpressionAtlas; A0A0A6YXZ1; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; IEA:UniProt.
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   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024395; CLASP_N_dom.
DR   InterPro; IPR034085; 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   SMART; SM01349; TOG; 3.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:A0A0A6YXZ1,
KW   ECO:0007829|MaxQB:A0A0A6YXZ1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          87..319
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          594..832
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          995..1233
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1244 AA;  136623 MW;  E85DCE496B9C9428 CRC64;
     MTTGKEKNFD DEDSVDGNRP SSASSSSSKA PSSSRRNVNL GTTRRLMSSS LGSKSSAAKE
     GAGAVDEEDF IKAFDDVPVV QIYSSRDLEE SINKIREILS DDKHDWEQRV NALKKIRSLL
     LAGAAEYDNF FQHLRLLDGA FKLSAKDLRS QVVREACITL GHLSSVLGNK FDHGAEAIMP
     TIFNLIPNSA KIMATSGVVA VRLIIRHTHI PRLIPVITSN CTSKSVAVRR RCFEFLDLLL
     QEWQTHSLER HISVLAETIK KGIHDADSEA RIEARKCYWG FHSHFSREAE HLYHTLESSY
     QKALQSHLKN SDSIVSLPQS DRSSSSSQES LNRPLSAKRS PTGSTASRGS TVSTKSVSTT
     GSLQRSRSDI DVNAAASAKS KVSSSSGSPA FSSAAALPPG SYASLDGTTT KAEGRIRTRR
     QSSGSTTNVA STPSDSRGRS RAKVVSQSQR SRSANPAGAG SRSSSPGKLL GSGLAGGSSR
     GPPVTPSSEK RSKIPRSQGC SRETSPNRIG LDRFGLGQSG RIPGSVNAMR VLSTSTDLEA
     AVADALLLGD ARSKKPVRRR YEPYGMYSDD DANSDASSVC SERSYGSRNG GIPHYLRQTE
     DVAEVLNHCA SSNWSERKEG LLGLQNLLKS QRTLSRVELK RLCEIFTRMF ADPHSKRVFS
     MFLETLVDFI IIHKDDLQDW LFVLLTQLLK KMGADLLGSV QAKVQKALDV TRDSFPFDQQ
     FNILMRFIVD QTQTPNLKVK VAILKYIESL ARQMDPTDFV NSSETRLAVS RIITWTTEPK
     SSDVRKAAQI VLISLFELNT PEFTMLLGAL PKTFQDGATK LLHNHLKNSS NTGVGSPSNT
     IGRTPSRHPS SRTSPLTSPT NCSHGGLSPS MLDYDTENLN SEEIYSSLRG VTEAIEKFSF
     RSQEDLNEPI KRDGKKDCDI VSRDGGAASP ATEGRGGSEI EGGRMALDNK TSLLNTQPPR
     AFPGPRAREY NPYPYSDTIN TYDKTALKEA VFDDDMEQLR DVPIDHSDLV ADLLKELSNH
     NERVEERKGA LLELLKITRE DSLGVWEEHF KTILLLLLET LGDKDHSIRA LALRVLREIL
     RNQPARFKNY AELTIMKTLE AHKDSHKEVV RAAEEAASTL ASSIHPEQCI KVLCPIIQTA
     DYPINLAAIK MQTKVVERIT KESLLQLLVD IIPGLLQGYD NTESSVRKAS VFCLVAIYSV
     IGEDLKPHLA QLTGSKMKLL NLYIKRAQTT NSNSSSSSDV STHS
//
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