ID   CSTP1_DANRE             Reviewed;         331 AA.
AC   Q6DGK9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Centriolar satellite-associated tubulin polyglutamylase complex regulator 1;
GN   Name=cstpp1; ORFNames=zgc:92873;
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=Brain;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=34782749; DOI=10.1038/s41422-021-00584-9;
RA   Wang L., Paudyal S.C., Kang Y., Owa M., Liang F.X., Spektor A., Knaut H.,
RA   Sanchez I., Dynlacht B.D.;
RT   "Regulators of tubulin polyglutamylation control nuclear shape and cilium
RT   disassembly by balancing microtubule and actin assembly.";
RL   Cell Res. 32:190-209(2022).
CC   -!- FUNCTION: Regulator of the tubulin polyglutamylase complex (TPGC) that
CC       controls cytoskeletal organization, nuclear shape, and cilium
CC       disassembly by balancing microtubule and actin assembly. Regulates the
CC       assembly and stability of the TPGC and thereby modulates
CC       polyglutamylation of the microtubule, which antagonizes MAP4 binding.
CC       {ECO:0000250|UniProtKB:Q9H6J7}.
CC   -!- SUBUNIT: Interacts with PCM1. Interacts with the complex TPGC. Binds to
CC       alpha-tubulin. {ECO:0000250|UniProtKB:Q9H6J7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriolar satellite
CC       {ECO:0000250|UniProtKB:Q9H6J7}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9H6J7}. Note=Associated with microtubules.
CC       {ECO:0000250|UniProtKB:Q9H6J7}.
CC   -!- TISSUE SPECIFICITY: Expression in elevated in ciliated tissues/organs,
CC       including brain, spinal cord, kidney, eyes, ears and lateral line.
CC       {ECO:0000269|PubMed:34782749}.
CC   -!- DISRUPTION PHENOTYPE: Mutants survive to adulthood and produce
CC       offspring (PubMed:34782749). Embryos show a significant defect in heart
CC       looping, with an increased proportion of embryos without a looped heart
CC       (PubMed:34782749). the They have an increased percentage of ciliated
CC       cells and ciliary length in Kupffer's Vesicle, although these
CC       alterations are not observed in the ear, pronephros or neural tube
CC       (PubMed:34782749). {ECO:0000269|PubMed:34782749}.
CC   -!- SIMILARITY: Belongs to the CSTPP1 family. {ECO:0000305}.
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DR   EMBL; BC076333; AAH76333.1; -; mRNA.
DR   RefSeq; NP_001002479.1; NM_001002479.1.
DR   AlphaFoldDB; Q6DGK9; -.
DR   STRING; 7955.ENSDARP00000105334; -.
DR   PaxDb; Q6DGK9; -.
DR   GeneID; 436752; -.
DR   KEGG; dre:436752; -.
DR   CTD; 79096; -.
DR   ZFIN; ZDB-GENE-040718-182; zgc:92873.
DR   eggNOG; ENOG502QRVN; Eukaryota.
DR   InParanoid; Q6DGK9; -.
DR   OrthoDB; 1103030at2759; -.
DR   PhylomeDB; Q6DGK9; -.
DR   PRO; PR:Q6DGK9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   InterPro; IPR038968; C11orf49.
DR   PANTHER; PTHR34252; PTHR34252; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome.
FT   CHAIN           1..331
FT                   /note="Centriolar satellite-associated tubulin
FT                   polyglutamylase complex regulator 1"
FT                   /id="PRO_0000360150"
FT   REGION          283..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   331 AA;  37750 MW;  2E8182E50422EFB4 CRC64;
     MKMNTERFNL TVDEYLAETN VLFYLNDAVT QLLEHKEEYT QFGVVRYFAE YFTSVKNGNH
     VLFREFSYIK ATPHNRESFI HIFWKCFRQI GKNGDLLAMS EYSSLLQLLC PDFPAEMVQN
     TARIVLIDDV TDCLMSFSDF IYSFQIQFFY EEFVESISAI YQDLLSGKNP NTVIVPTSTS
     VEQLSSSAND KPDVQEGVDA TIFCECIEGL CERFKHKYPS TVAIKEILDN TQRVSFYGFL
     MALAKHEGIN QDIGALPNKP DLLIDPEMDQ ELERLIAQVA ISPTSNNNSS SSALGQKEMS
     KKASPRKSLH QRKRIEMESD GSTEETDSSE N