ID   TPGS2_MOUSE             Reviewed;         296 AA.
AC   Q66JT5; Q6PAK1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Tubulin polyglutamylase complex subunit 2;
DE            Short=PGs2;
GN   Name=Tpgs2;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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   IDENTIFICATION BY MASS SPECTROMETRY AS PART OF THE TUBULIN POLYGLUTAMYLASE
RP   COMPLEX.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S.,
RA   Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
CC   -!- FUNCTION: Subunit of the tubulin polyglutamylase complex (TPGC). The
CC       complex mediates cilia and flagella polyglutamylation which is
CC       essential for their biogenesis and motility.
CC       {ECO:0000250|UniProtKB:Q68CL5}.
CC   -!- SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which
CC       contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1 (PubMed:15890843).
CC       Interacts with CSTPP1 and LRRC49 (By similarity).
CC       {ECO:0000250|UniProtKB:Q68CL5, ECO:0000269|PubMed:15890843}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q68CL5}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriolar satellite
CC       {ECO:0000250|UniProtKB:Q68CL5}. Note=Associated with microtubules.
CC       {ECO:0000250|UniProtKB:Q68CL5}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH80777.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC060253; AAH60253.1; -; mRNA.
DR   EMBL; BC080777; AAH80777.1; ALT_INIT; mRNA.
DR   CCDS; CCDS29105.2; -.
DR   RefSeq; NP_001004361.2; NM_001004361.2.
DR   RefSeq; NP_001136170.1; NM_001142698.1.
DR   AlphaFoldDB; Q66JT5; -.
DR   CORUM; Q66JT5; -.
DR   STRING; 10090.ENSMUSP00000111484; -.
DR   PhosphoSitePlus; Q66JT5; -.
DR   MaxQB; Q66JT5; -.
DR   PaxDb; Q66JT5; -.
DR   PRIDE; Q66JT5; -.
DR   ProteomicsDB; 259502; -.
DR   GeneID; 66648; -.
DR   KEGG; mmu:66648; -.
DR   CTD; 25941; -.
DR   MGI; MGI:1913898; Tpgs2.
DR   eggNOG; ENOG502R21Z; Eukaryota.
DR   InParanoid; Q66JT5; -.
DR   OrthoDB; 1286883at2759; -.
DR   PhylomeDB; Q66JT5; -.
DR   BioGRID-ORCS; 66648; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Tpgs2; mouse.
DR   PRO; PR:Q66JT5; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q66JT5; protein.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0018095; P:protein polyglutamylation; IEA:InterPro.
DR   InterPro; IPR018958; Knr4/Smi1-like_dom.
DR   InterPro; IPR037883; Knr4/Smi1-like_sf.
DR   InterPro; IPR039231; TPGS2.
DR   PANTHER; PTHR31854; PTHR31854; 1.
DR   SMART; SM00860; SMI1_KNR4; 1.
DR   SUPFAM; SSF160631; SSF160631; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT   CHAIN           1..296
FT                   /note="Tubulin polyglutamylase complex subunit 2"
FT                   /id="PRO_0000079305"
FT   REGION          254..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..287
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        190
FT                   /note="I -> T (in Ref. 1; AAH60253)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="A -> V (in Ref. 1; AAH60253)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  33184 MW;  0BEAAB6C4A84B376 CRC64;
     MEETTPPLQA GSKPHLEKLT LGVTRILESS PGVTEVSIIE KLPAERHVIS SWEQKNNCVM
     PEDVRNFYLM TNGFHMTWSV KLDEHIIPLG SMVINGISKL TQLIQSSVYS LPNAPTLADL
     EDDTQEGNED HQLEKPHFDC RSAIFELDSC NGNGKVCLVY KNGKPGLAHD TEIWFLDRAL
     YWHFLTDTFI AYYRLLITHL GLPQWQYAFT SYGISPQAKQ WFSMYKPITY NTSLLTEESD
     NFANKLDPSK VFKSKNKILI PKKKGPVPPA SGQKGPGPLP PPTSKPTTGS GNPVRK