CSTP1_RAT
ID CSTP1_RAT Reviewed; 331 AA.
AC Q5M9F0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Centriolar satellite-associated tubulin polyglutamylase complex regulator 1;
GN Name=Cstpp1;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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: 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 TTLL1, TPGS1, TPGS2 and
CC LRRC49; the interactions link CSTPP1 to 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 -!- SIMILARITY: Belongs to the CSTPP1 family. {ECO:0000305}.
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DR EMBL; BC087159; AAH87159.1; -; mRNA.
DR RefSeq; NP_001013940.1; NM_001013918.1.
DR AlphaFoldDB; Q5M9F0; -.
DR STRING; 10116.ENSRNOP00000039464; -.
DR iPTMnet; Q5M9F0; -.
DR PhosphoSitePlus; Q5M9F0; -.
DR PaxDb; Q5M9F0; -.
DR PRIDE; Q5M9F0; -.
DR Ensembl; ENSRNOT00000095774; ENSRNOP00000088632; ENSRNOG00000014798.
DR GeneID; 295930; -.
DR KEGG; rno:295930; -.
DR UCSC; RGD:1309540; rat.
DR CTD; 79096; -.
DR RGD; 1309540; RGD1309540.
DR eggNOG; ENOG502QRVN; Eukaryota.
DR GeneTree; ENSGT00390000012935; -.
DR HOGENOM; CLU_064579_0_0_1; -.
DR InParanoid; Q5M9F0; -.
DR OMA; NIHHRRK; -.
DR OrthoDB; 1103030at2759; -.
DR PhylomeDB; Q5M9F0; -.
DR TreeFam; TF329168; -.
DR PRO; PR:Q5M9F0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000014798; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q5M9F0; RN.
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 1: Evidence at protein 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_0000281429"
FT REGION 1..225
FT /note="Required for interaction with TPGS1, LRRC49, and
FT TTLL1"
FT /evidence="ECO:0000250|UniProtKB:Q9H6J7"
FT REGION 1..111
FT /note="Required for interaction with PCM1"
FT /evidence="ECO:0000250|UniProtKB:Q9H6J7"
FT REGION 112..331
FT /note="Required for interaction with TPGS2"
FT /evidence="ECO:0000250|UniProtKB:Q9H6J7"
FT REGION 292..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 331 AA; 37476 MW; 64CCA6B1EA9A8B37 CRC64;
MLSPERLALP DYEYLAQRHV LTYMEDAVCQ LLENKEDISQ YGIARFFTEY FNSVCQGTHI
LFREFSFIQA TPHNRASFLR AFWRCFRTVG KNGDLLTMRE YHCLLQLLCP DFPLELTQKA
ARIVLMDDAM DCLMSFSDFL FAFQIQFYYS EFLESVAAIY QDLLSGKNPN TVIVPTSSSG
QHRQRPALGD AGMLDGVEAS LFCQRLENLC DRHKYSCPPP ALVKEILSNV QRLTFYGFLV
ALSKHHGINQ ALGALPDKGD LMHDPAMDEE LERLLVQVPG LVNSITATSE ASCLPSRTPP
RVGSPWKPLH RSRKLDAESD GSTEETDESE T