TPGS1_MOUSE
ID TPGS1_MOUSE Reviewed; 303 AA.
AC Q99MS8; Q3U5Q9; Q9R0B5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Tubulin polyglutamylase complex subunit 1;
DE Short=PGs1;
DE AltName: Full=p32;
GN Name=Tpgs1; Synonyms=Gm16517, Gtrgeo22;
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 [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/10J; TISSUE=Brain;
RX PubMed=12242242; DOI=10.1093/genetics/162.1.307;
RA Campbell P.K., Waymire K.G., Heier R.L., Sharer C., Day D.E., Reimann H.,
RA Jaje J.M., Friedrich G.A., Burmeister M., Bartness T.J., Russell L.D.,
RA Young L.J., Zimmer M., Jenne D.E., MacGregor G.R.;
RT "Mutation of a novel gene results in abnormal development of spermatid
RT flagella, loss of intermale aggression and reduced body fat in mice.";
RL Genetics 162:307-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-303.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY AS PART OF THE TUBULIN
RP POLYGLUTAMYLASE COMPLEX, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12972506; DOI=10.1242/jcs.00743;
RA Regnard C., Fesquet D., Janke C., Boucher D., Desbruyeres E., Koulakoff A.,
RA Insina C., Travo P., Edde B.;
RT "Characterisation of PGs1, a subunit of a protein complex co-purifying with
RT tubulin polyglutamylase.";
RL J. Cell Sci. 116:4181-4190(2003).
RN [4]
RP FUNCTION, PHOSPHORYLATION AT SER-279, AND IDENTIFICATION BY MASS
RP SPECTROMETRY AS PART OF THE TUBULIN POLYGLUTAMYLASE 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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
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).
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 (PubMed:12242242,
CC PubMed:12972506, PubMed:15890843). May act in the targeting of the
CC tubulin polyglutamylase complex. Required for the development of the
CC spermatid flagellum. {ECO:0000269|PubMed:12242242,
CC ECO:0000269|PubMed:12972506, ECO:0000269|PubMed:15890843}.
CC -!- SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which
CC contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1 (PubMed:12972506).
CC Interacts with PCM1, CSTPP1 and LRRC49 (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZTW0, ECO:0000269|PubMed:12972506}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:12972506}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000269|PubMed:12972506}. Cytoplasm, cytoskeleton, cilium
CC basal body {ECO:0000269|PubMed:12972506}. Cytoplasm, cytoskeleton,
CC flagellum basal body {ECO:0000269|PubMed:12972506}. Cell projection,
CC axon {ECO:0000269|PubMed:12972506}. Cell projection, dendrite
CC {ECO:0000269|PubMed:12972506}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:12972506}.
CC Note=Associated with microtubules from neurites, centrosomes, basal
CC bodies and axonemes. {ECO:0000269|PubMed:12972506}.
CC -!- TISSUE SPECIFICITY: Broadly expressed at low levels. Highly expressed
CC in brain. Present in brain neurons (at protein level).
CC {ECO:0000269|PubMed:12242242, ECO:0000269|PubMed:12972506}.
CC -!- DEVELOPMENTAL STAGE: In testis, expression strongly increases at P22.
CC {ECO:0000269|PubMed:12242242}.
CC -!- DISRUPTION PHENOTYPE: Male mice are sterile due to defects in the
CC development of the spermatid flagellum. They have reduced body fat
CC content and fail to attack each other when caged together with other
CC males. {ECO:0000269|PubMed:12242242}.
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DR EMBL; AF303106; AAK15262.1; -; mRNA.
DR EMBL; AF084937; AAD54650.1; -; Genomic_DNA.
DR EMBL; AK153467; BAE32018.1; -; mRNA.
DR RefSeq; NP_683736.1; NM_148934.2.
DR AlphaFoldDB; Q99MS8; -.
DR BioGRID; 225223; 1.
DR CORUM; Q99MS8; -.
DR IntAct; Q99MS8; 3.
DR MINT; Q99MS8; -.
DR STRING; 10090.ENSMUSP00000020552; -.
DR iPTMnet; Q99MS8; -.
DR PhosphoSitePlus; Q99MS8; -.
DR MaxQB; Q99MS8; -.
DR PaxDb; Q99MS8; -.
DR PRIDE; Q99MS8; -.
DR ProteomicsDB; 260728; -.
DR Antibodypedia; 53504; 20 antibodies from 10 providers.
DR DNASU; 110012; -.
DR Ensembl; ENSMUST00000239401; ENSMUSP00000159326; ENSMUSG00000020308.
DR GeneID; 110012; -.
DR KEGG; mmu:110012; -.
DR UCSC; uc007fzh.1; mouse.
DR CTD; 91978; -.
DR MGI; MGI:106618; Tpgs1.
DR VEuPathDB; HostDB:ENSMUSG00000020308; -.
DR eggNOG; ENOG502S17Y; Eukaryota.
DR GeneTree; ENSGT00500000045074; -.
DR HOGENOM; CLU_084094_0_0_1; -.
DR InParanoid; Q99MS8; -.
DR OMA; FSDYIRQ; -.
DR OrthoDB; 1306505at2759; -.
DR PhylomeDB; Q99MS8; -.
DR TreeFam; TF329086; -.
DR BioGRID-ORCS; 110012; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q99MS8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q99MS8; protein.
DR Bgee; ENSMUSG00000020308; Expressed in right kidney and 235 other tissues.
DR ExpressionAtlas; Q99MS8; baseline and differential.
DR Genevisible; Q99MS8; MM.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008017; F:microtubule binding; IMP:MGI.
DR GO; GO:0015631; F:tubulin binding; IDA:MGI.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IDA:MGI.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0018095; P:protein polyglutamylation; IMP:MGI.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:MGI.
DR GO; GO:0051648; P:vesicle localization; IMP:MGI.
DR InterPro; IPR039235; TPGS1.
DR PANTHER; PTHR31932; PTHR31932; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Flagellum; Microtubule; Phosphoprotein;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..303
FT /note="Tubulin polyglutamylase complex subunit 1"
FT /id="PRO_0000249317"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZTW0"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15890843"
SQ SEQUENCE 303 AA; 32626 MW; 8EE64B892B87FAF5 CRC64;
MAALPVPLPP TKMAAVEKRR PAVAPAANFP DSGRTSVSQA AAAAESEEDF LRQLGVTEML
RAALLKVLEI RPEEPIAFLA HYFENMGLRS PTNGGAGEPP GQLLLQQQRL GRALWHLRLA
HHSQRTAFNN NVSVAYECLS ASGRKKKPGL DGRTYSELLK RVCRDGGAPE EVVAPLLRKI
QCRDHEAVPL GIFRTGMLSC FVLLEFVARA GALFQLLEDP GQAVADRRVG QAVLDTLEGA
LSAGDMATAP THYLEAGSRL GPDNLARALD RAASGRRPSV PMAREEFLEK AAALFIAKVK
PVG
