TTLL1_BOVIN
ID TTLL1_BOVIN Reviewed; 423 AA.
AC Q0VC71;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Polyglutamylase complex subunit TTLL1 {ECO:0000250|UniProtKB:Q91V51};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:Q91V51};
DE AltName: Full=Tubulin polyglutamylase TTLL1;
DE AltName: Full=Tubulin polyglutamylase complex subunit 3;
DE Short=PGs3 {ECO:0000250|UniProtKB:Q91V51};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 1 {ECO:0000250|UniProtKB:Q91V51};
GN Name=TTLL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of a polyglutamylase complex which modifies
CC tubulin, generating side chains of glutamate on the gamma-carboxyl
CC group of specific glutamate residues within the C-terminal tail of
CC tubulin. Probably involved in the side-chain elongation step of the
CC polyglutamylation reaction rather than the initiation step. Modifies
CC both alpha- and beta-tubulins with a preference for the alpha-tail.
CC Unlike most polyglutamylases of the tubulin--tyrosine ligase family,
CC only displays a catalytic activity when in complex with other proteins
CC as it is most likely lacking domains important for autonomous activity.
CC Part of the neuronal tubulin polyglutamylase complex. Mediates cilia
CC and flagella polyglutamylation which is essential for their biogenesis
CC and motility. Involved in respiratory motile cilia function through the
CC regulation of beating asymmetry. Essential for sperm flagella
CC biogenesis, motility and male fertility. Involved in KLF4 glutamylation
CC which impedes its ubiquitination, thereby leading to somatic cell
CC reprogramming, pluripotency maintenance and embryogenesis.
CC {ECO:0000250|UniProtKB:Q91V51}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP +
CC L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein]
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519,
CC Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q91V51};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC Evidence={ECO:0000250|UniProtKB:Q91V51};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which
CC contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. Interacts with PCM1,
CC CSTPP1 and LRRC49. {ECO:0000250|UniProtKB:O95922,
CC ECO:0000250|UniProtKB:Q91V51}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q91V51}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q91V51}. Cytoplasm, cytoskeleton, cilium
CC axoneme {ECO:0000250|UniProtKB:Q91V51}. Cell projection, cilium,
CC flagellum {ECO:0000250|UniProtKB:Q91V51}.
CC -!- DOMAIN: Gln-144 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}.
CC -!- SIMILARITY: Belongs to the tubulin polyglutamylase family.
CC {ECO:0000305}.
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DR EMBL; BC120322; AAI20323.1; -; mRNA.
DR RefSeq; NP_001069639.1; NM_001076171.1.
DR RefSeq; XP_005207474.1; XM_005207417.3.
DR RefSeq; XP_005207475.1; XM_005207418.1.
DR AlphaFoldDB; Q0VC71; -.
DR SMR; Q0VC71; -.
DR STRING; 9913.ENSBTAP00000015956; -.
DR PaxDb; Q0VC71; -.
DR PRIDE; Q0VC71; -.
DR Ensembl; ENSBTAT00000015956; ENSBTAP00000015956; ENSBTAG00000012030.
DR GeneID; 539530; -.
DR KEGG; bta:539530; -.
DR CTD; 25809; -.
DR VEuPathDB; HostDB:ENSBTAG00000012030; -.
DR VGNC; VGNC:36489; TTLL1.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000156720; -.
DR HOGENOM; CLU_010131_0_0_1; -.
DR InParanoid; Q0VC71; -.
DR OMA; TMYGRLP; -.
DR OrthoDB; 584228at2759; -.
DR TreeFam; TF313087; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000012030; Expressed in Ammon's horn and 103 other tissues.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IBA:GO_Central.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IEA:Ensembl.
DR GO; GO:0002395; P:immune response in nasopharyngeal-associated lymphoid tissue; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0120197; P:mucociliary clearance; IEA:Ensembl.
DR GO; GO:0018095; P:protein polyglutamylation; IBA:GO_Central.
DR GO; GO:0120222; P:regulation of blastocyst development; IEA:Ensembl.
DR GO; GO:0007288; P:sperm axoneme assembly; IEA:Ensembl.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027750; TTLL1.
DR PANTHER; PTHR12241:SF31; PTHR12241:SF31; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Flagellum;
KW Ligase; Magnesium; Metal-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..423
FT /note="Polyglutamylase complex subunit TTLL1"
FT /id="PRO_0000288848"
FT DOMAIN 1..367
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 243..244
FT /note="L-glutamate"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT REGION 391..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 144..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 144
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 181..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 194..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 220
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 241..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 259
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 344
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 144
FT /note="Essential for specifying alpha-elongation versus
FT initiation step of the polyglutamylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
SQ SEQUENCE 423 AA; 49030 MW; E2FE89A9EEC43F57 CRC64;
MAGKVKWVTD IEKSVLINNF EKRGWVQVTE NEDWNFYWMS VQTIRNVFSV ETGYRLSDDQ
IVNHFPNHYE LTRKDLMVKN IKRYRKELEK EGSPLAEKDE SGKYLYLDFV PVTYMLPADY
NLFVEEFRKS PSSTWIMKPC GKAQGKGIFL INKLSQIKKW SRDSKTSSFV TQSTKEAYVI
SLYINNPLLI GGRKFDLRLY VLVSTYRPLR CYMYKLGFCR FCTVKYTPST SELDNMFVHL
TNVAIQKHGE DYNHIHGGKW TVNNLRLYLE STRGKEVTSK LFDEIHWIIV QSLKAVAPVM
NNDKHCFECY GYDIIIDDKL KPWLIEVNAS PSLTSSTAND RILKYNLIND TLNIAVPNGE
IPDCKWNKSP PKEVLGNYEI LYDEELAQGD GAERELRSRP GQSLGPKGSR LRDAGRTVLT
TWK
