CCSAP_DANRE
ID CCSAP_DANRE Reviewed; 263 AA.
AC Q6P3G4; B0V0U9; Q4V8Y2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Centriole, cilia and spindle-associated protein;
GN Name=ccsap; ORFNames=si:dkey-162b3.6;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=22493317; DOI=10.1091/mbc.e11-11-0931;
RA Backer C.B., Gutzman J.H., Pearson C.G., Cheeseman I.M.;
RT "CSAP localizes to polyglutamylated microtubules and promotes proper cilia
RT function and zebrafish development.";
RL Mol. Biol. Cell 23:2122-2130(2012).
CC -!- FUNCTION: Plays a role in embryonic development, including proper left-
CC right asymmetry formation. Also required for proper cilia beating
CC (PubMed:22493317). Plays a role in microtubule (MT) stabilization and
CC this stabilization involves the maintenance of NUMA1 at the spindle
CC poles. Colocalizes with polyglutamylated MTs to promote MT
CC stabilization and regulate bipolar spindle formation in mitosis.
CC Binding of CCSAP to centrosomes and the spindle around centrosomes
CC during mitosis inhibits MT depolymerization, thereby stabilizing the
CC mitotic spindle (By similarity). {ECO:0000250|UniProtKB:Q6IQ19,
CC ECO:0000269|PubMed:22493317}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q6IQ19}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q6IQ19}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6IQ19}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:22493317}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q6IQ19}.
CC Cell projection, axon {ECO:0000250|UniProtKB:Q6IQ19}. Cell projection,
CC cilium {ECO:0000250|UniProtKB:Q6IQ19}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q6IQ19}. Note=Localizes at specific foci at the
CC apical surface of neuroepithelial cells where cilia form along the
CC brain ventricle lumen. {ECO:0000269|PubMed:22493317}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed ubiquitously in the developing embryo. Strongly expressed in
CC the somites and brain at 16 to 26 hours post-fertilization (hpf).
CC {ECO:0000269|PubMed:22493317}.
CC -!- SIMILARITY: Belongs to the CCSAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63997.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH97150.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR762497; CAQ15403.1; -; Genomic_DNA.
DR EMBL; BC097150; AAH97150.1; ALT_INIT; mRNA.
DR EMBL; BC063997; AAH63997.1; ALT_INIT; mRNA.
DR RefSeq; NP_001154833.1; NM_001161361.1.
DR AlphaFoldDB; Q6P3G4; -.
DR STRING; 7955.ENSDARP00000058627; -.
DR PaxDb; Q6P3G4; -.
DR PRIDE; Q6P3G4; -.
DR Ensembl; ENSDART00000058628; ENSDARP00000058627; ENSDARG00000040085.
DR GeneID; 100003801; -.
DR KEGG; dre:100003801; -.
DR CTD; 100003801; -.
DR ZFIN; ZDB-GENE-081107-51; ccsapb.
DR eggNOG; ENOG502S0N0; Eukaryota.
DR GeneTree; ENSGT00390000003512; -.
DR HOGENOM; CLU_054214_0_0_1; -.
DR InParanoid; Q6P3G4; -.
DR OMA; WLWDGWE; -.
DR OrthoDB; 1131280at2759; -.
DR PhylomeDB; Q6P3G4; -.
DR TreeFam; TF332378; -.
DR PRO; PR:Q6P3G4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000040085; Expressed in retina and 21 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0003341; P:cilium movement; IMP:ZFIN.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; IDA:UniProtKB.
DR GO; GO:1990755; P:mitotic spindle microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0048666; P:neuron development; IMP:UniProtKB.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; IMP:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; IDA:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
DR InterPro; IPR029774; CSAP.
DR PANTHER; PTHR31022; PTHR31022; 1.
DR Pfam; PF15748; CCSAP; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Developmental protein; Microtubule; Mitosis;
KW Reference proteome; Repeat.
FT CHAIN 1..263
FT /note="Centriole, cilia and spindle-associated protein"
FT /id="PRO_0000419129"
FT REGION 50..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 8..14
FT /note="ST]-E-Y-X(3)-F motif 1; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOTIF 252..258
FT /note="ST]-E-Y-X(3)-F motif 2; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 108
FT /note="T -> N (in Ref. 2; AAH97150)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="S -> P (in Ref. 2; AAH97150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 30290 MW; A3197DFBAB348FF9 CRC64;
MVTKRIRSEY MKKFKDPKWD TYAKCYEDLL KYRLSRRLLE QAHKPWFWGE WGSETASSGK
STPLSRNKVE PLKTLDEKPE RSACVTPEPA AEAETQAAEV QDREHADTNL VPCDAEVAHP
EGEEVRGKER SPAVNPDSDT QIQNMSKSKR RSSHKYTRSK VKPQAPKDPD KENRHPFALY
GAGEKQTDMA SKKTHNVGPA ASTAEIHESA LRAKTRREVE KQIKRFDKQR ARSADLEKSR
NKIIPDFNPW MTEYMRCFSA RSR
