TTL10_RAT
ID TTL10_RAT Reviewed; 679 AA.
AC Q5XI57; Q4V8F2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein polyglycylase TTLL10 {ECO:0000250|UniProtKB:A4Q9F3};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:A4Q9F3};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 10;
GN Name=Ttll10 {ECO:0000312|RGD:1560839};
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 115-679 (ISOFORM 1).
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).
CC -!- FUNCTION: Polyglycylase which modifies both tubulin and non-tubulin
CC proteins, generating polyglycine side chains of variable lengths on the
CC gamma-carboxyl groups of specific glutamate residues of target
CC proteins. Involved in the elongation step rather than the initiation
CC step of the polyglycylation reaction. Polyglycylates alpha-tubulin and
CC beta-tubulin. Polyglycylates non-tubulin proteins such as nucleosome
CC assembly protein NAP1. {ECO:0000250|UniProtKB:A4Q9F3}.
CC -!- CATALYTIC ACTIVITY: [Protein polyglycylase TTLL10]:
CC Reaction=(glycyl)(n)-glycyl-L-glutamyl-[protein] + ATP + glycine =
CC (glycyl)(n+1)-glycyl-L-glutamyl-[protein] + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:67184, Rhea:RHEA-COMP:17208, Rhea:RHEA-COMP:17209,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:167891, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:A4Q9F3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67185;
CC Evidence={ECO:0000250|UniProtKB:A4Q9F3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:A4Q9F3}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:A4Q9F3}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:A4Q9F3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XI57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XI57-2; Sequence=VSP_032266;
CC -!- DOMAIN: Gln-310 is the main determinant for regioselectivity, which
CC segregates between initiases and elongases in all tubulin--tyrosine
CC ligase family. A glutamine residue at this position is found in
CC elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-
CC chain elongation, whereas an arginine residue is found in initiases
CC TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
CC {ECO:0000250|UniProtKB:A4Q9E8}.
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DR EMBL; AABR03041793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC083833; AAH83833.1; -; mRNA.
DR EMBL; BC097417; AAH97417.1; -; mRNA.
DR RefSeq; NP_001019929.1; NM_001024758.2. [Q5XI57-2]
DR RefSeq; NP_001164004.1; NM_001170533.1.
DR RefSeq; XP_006239624.1; XM_006239562.3. [Q5XI57-2]
DR AlphaFoldDB; Q5XI57; -.
DR SMR; Q5XI57; -.
DR STRING; 10116.ENSRNOP00000063596; -.
DR PhosphoSitePlus; Q5XI57; -.
DR PaxDb; Q5XI57; -.
DR PRIDE; Q5XI57; -.
DR GeneID; 298692; -.
DR KEGG; rno:298692; -.
DR CTD; 254173; -.
DR RGD; 1560839; Ttll10.
DR VEuPathDB; HostDB:ENSRNOG00000020132; -.
DR eggNOG; KOG2157; Eukaryota.
DR HOGENOM; CLU_022993_1_0_1; -.
DR InParanoid; Q5XI57; -.
DR OrthoDB; 626048at2759; -.
DR PhylomeDB; Q5XI57; -.
DR TreeFam; TF329363; -.
DR Reactome; R-RNO-8955332; Carboxyterminal post-translational modifications of tubulin.
DR PRO; PR:Q5XI57; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000020132; Expressed in testis and 11 other tissues.
DR ExpressionAtlas; Q5XI57; baseline and differential.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070735; F:protein-glycine ligase activity; ISS:UniProtKB.
DR GO; GO:0070737; F:protein-glycine ligase activity, elongating; ISS:UniProtKB.
DR GO; GO:0018094; P:protein polyglycylation; ISS:UniProtKB.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027752; TTLL10.
DR PANTHER; PTHR46810; PTHR46810; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Ligase; Magnesium; Metal-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..679
FT /note="Protein polyglycylase TTLL10"
FT /id="PRO_0000324523"
FT DOMAIN 172..543
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 310..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 310
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:29973"
FT /ligand_part_note="L-glutamate acceptor residue in protein
FT target"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 353..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 366..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 409..410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 502
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 502
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 504
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 310
FT /note="Essential for specifying elongation versus
FT initiation step of the polyglycylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032266"
SQ SEQUENCE 679 AA; 77081 MW; 1BA32BE272AD19EF CRC64;
MPLHPPARRP HGHRRNGSEA QTEATTQDTG RLSCPRRVGA AVCPIQGLGH RAARRPRRGV
GTTSASRAPR PGALMPATRN RPRFIHYRVQ PPRTHVSFKR PKRSRTHQSH TKVPGWTHEK
RMGSSVEEGL RPELSQLEQD ADNLGEEEAA RLPVTSLNGL LMEGDRHPNP GQGPFFYIGG
TNGASIISNY CESKGWQRTQ DSRCEDYKLK WCEIKCRDNY CSFREGQQLL FQLPNNKLLT
TKIGLLSALR EHARTLSKAR LMPSTQAKVL KMDEFFPETY RLDIRDERQA FFTLFDETQM
WICKPTASNQ GKGIFLIRSQ EEAAALQAKT QSIEDDPIYR KMPFRAPQAR VVQRYVQNPL
LLDGKKFDVR SYMLIACAMP YMVFFGHGYA RLTLSLYNPH SSDLSGHLTN QFMQKKSPLY
MLLKDSTVWS MEHLNRYIND KFRKSKGLPR DWVFTTFTKR MQQIMSHCFL AVKSKLECKL
GYFDLIGCDF LIDENFKVWL LEMNSNPALH TNCEVLKEVI PGVVMETLDL ALETCQKSLH
SQKMLPLQSQ RRFVLLYNGE TTDLWPRLGS SRPPIRLPYA NSNHARSTCE ISSSSLTSTR
VTIADRPAAR KSMSSRTAPI CASRKSRLSD SGGVSIEESE TSVCSGLPEG SRDAAREPSL
GPTEEEREEE QRSTSHRGS
