ID   TTLL9_HUMAN             Reviewed;         439 AA.
AC   Q3SXZ7; A6NH06; A6NIS5; B3KSG8; Q3SXZ8; Q5JYS3; Q5JYS4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Probable tubulin polyglutamylase TTLL9 {ECO:0000250|UniProtKB:A2APC3};
DE            EC=6.3.2.- {ECO:0000250|UniProtKB:A2APC3};
DE   AltName: Full=Tubulin--tyrosine ligase-like protein 9;
GN   Name=TTLL9 {ECO:0000312|HGNC:HGNC:16118}; Synonyms=C20orf125;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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: Probable tubulin polyglutamylase that generates side chains
CC       of glutamate on the gamma-carboxyl group of specific glutamate residues
CC       within the C-terminal tail of target proteins. Similar to TTLL1, may
CC       acquire enzymatic activity only in complex with other proteins as it is
CC       most likely lacking domains important for autonomous activity. Mediates
CC       tubulin polyglutamylation which induces establishment of microtubule
CC       heterogeneity in sperm flagella, thereby playing a role in normal
CC       motile flagella axoneme structure and sperm flagella beating pattern.
CC       {ECO:0000250|UniProtKB:A2APC3}.
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:A2APC3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC         Evidence={ECO:0000250|UniProtKB:A2APC3};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC       {ECO:0000250|UniProtKB:A2APC3}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:A2APC3}. Cytoplasm, cytoskeleton, flagellum
CC       axoneme {ECO:0000250|UniProtKB:A2APC3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3SXZ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3SXZ7-2; Sequence=VSP_035765, VSP_035767, VSP_035769;
CC       Name=3;
CC         IsoId=Q3SXZ7-3; Sequence=VSP_035765, VSP_035766, VSP_035767,
CC                                  VSP_035768;
CC   -!- DOMAIN: Gln-173 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--tyrosine ligase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW76401.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK093491; BAG52730.1; -; mRNA.
DR   EMBL; AL031658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW76401.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471077; EAW76403.1; -; Genomic_DNA.
DR   EMBL; BC104024; AAI04025.1; -; mRNA.
DR   EMBL; BC104025; AAI04026.1; -; mRNA.
DR   CCDS; CCDS42863.1; -. [Q3SXZ7-1]
DR   RefSeq; NP_001008409.1; NM_001008409.2. [Q3SXZ7-1]
DR   RefSeq; XP_006723787.1; XM_006723724.2.
DR   RefSeq; XP_011526948.1; XM_011528646.1.
DR   AlphaFoldDB; Q3SXZ7; -.
DR   SMR; Q3SXZ7; -.
DR   BioGRID; 127895; 14.
DR   IntAct; Q3SXZ7; 5.
DR   STRING; 9606.ENSP00000442515; -.
DR   iPTMnet; Q3SXZ7; -.
DR   PhosphoSitePlus; Q3SXZ7; -.
DR   BioMuta; TTLL9; -.
DR   DMDM; 215274204; -.
DR   MassIVE; Q3SXZ7; -.
DR   MaxQB; Q3SXZ7; -.
DR   PaxDb; 9606-ENSP00000442515; -.
DR   Antibodypedia; 49885; 49 antibodies from 12 providers.
DR   DNASU; 164395; -.
DR   Ensembl; ENST00000375922.8; ENSP00000495141.1; ENSG00000131044.19. [Q3SXZ7-2]
DR   Ensembl; ENST00000375938.8; ENSP00000365105.4; ENSG00000131044.19. [Q3SXZ7-1]
DR   Ensembl; ENST00000535842.6; ENSP00000442515.1; ENSG00000131044.19. [Q3SXZ7-1]
DR   GeneID; 164395; -.
DR   KEGG; hsa:164395; -.
DR   MANE-Select; ENST00000535842.6; ENSP00000442515.1; NM_001008409.5; NP_001008409.1.
DR   UCSC; uc002wwy.2; human. [Q3SXZ7-1]
DR   AGR; HGNC:16118; -.
DR   CTD; 164395; -.
DR   DisGeNET; 164395; -.
DR   GeneCards; TTLL9; -.
DR   HGNC; HGNC:16118; TTLL9.
DR   HPA; ENSG00000131044; Tissue enhanced (choroid plexus, fallopian tube, testis).
DR   MIM; 619838; gene.
DR   neXtProt; NX_Q3SXZ7; -.
DR   OpenTargets; ENSG00000131044; -.
DR   PharmGKB; PA25666; -.
DR   VEuPathDB; HostDB:ENSG00000131044; -.
DR   eggNOG; KOG2157; Eukaryota.
DR   GeneTree; ENSGT00940000159879; -.
DR   HOGENOM; CLU_010131_0_1_1; -.
DR   InParanoid; Q3SXZ7; -.
DR   OMA; IWIMKPP; -.
DR   OrthoDB; 7265at2759; -.
DR   PhylomeDB; Q3SXZ7; -.
DR   TreeFam; TF313087; -.
DR   PathwayCommons; Q3SXZ7; -.
DR   Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR   SignaLink; Q3SXZ7; -.
DR   BioGRID-ORCS; 164395; 11 hits in 1076 CRISPR screens.
DR   ChiTaRS; TTLL9; human.
DR   GenomeRNAi; 164395; -.
DR   Pharos; Q3SXZ7; Tdark.
DR   PRO; PR:Q3SXZ7; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q3SXZ7; Protein.
DR   Bgee; ENSG00000131044; Expressed in right uterine tube and 134 other cell types or tissues.
DR   ExpressionAtlas; Q3SXZ7; baseline and differential.
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:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR   GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR   PANTHER; PTHR12241:SF39; TUBULIN POLYGLUTAMYLASE TTLL9-RELATED; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS51221; TTL; 1.
DR   Genevisible; Q3SXZ7; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell projection; Cilium; Cytoplasm;
KW   Cytoskeleton; Flagellum; Ligase; Magnesium; Metal-binding; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..439
FT                   /note="Probable tubulin polyglutamylase TTLL9"
FT                   /id="PRO_0000324517"
FT   DOMAIN          40..380
FT                   /note="TTL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         173..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         173
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         211..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         224..226
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         248
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         254..255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         272
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
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         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         341
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   BINDING         357
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   SITE            173
FT                   /note="Essential for specifying alpha-elongation versus
FT                   initiation step of the polyglutamylase activity"
FT                   /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT   VAR_SEQ         1..50
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035765"
FT   VAR_SEQ         169..191
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035766"
FT   VAR_SEQ         236..250
FT                   /note="VFAECLLWSGHRRQD -> YIPLRAWLYRDGFARFSNTRFTLNSIDDQY
FT                   (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035767"
FT   VAR_SEQ         270..439
FT                   /note="GCKWTLQRFRQYLASKHGPEAVETLFRDIDNIFVKSLQSVQKVIISDKHCFE
FT                   LYGYDILIDQDLKPWLLEVNASPSLTASSQEDYELKTCLLEDTLHVVDMEARLTGREKR
FT                   VGGFDLMWNDGPVSREEGAPDLSGMGNFVTNTHLGCVNDRKKQLRQLFCSLQVQKKASS
FT                   -> VAPGGQCVPITDSQQPGRL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035768"
FT   VAR_SEQ         374..439
FT                   /note="LTGREKRVGGFDLMWNDGPVSREEGAPDLSGMGNFVTNTHLGCVNDRKKQLR
FT                   QLFCSLQVQKKASS -> SLRADSPCW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035769"
FT   VARIANT         76
FT                   /note="Y -> C (in dbSNP:rs17093689)"
FT                   /id="VAR_039805"
FT   CONFLICT        274
FT                   /note="T -> M (in Ref. 4; AAI04026)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   439 AA;  51472 MW;  ED6172FE902F791C CRC64;
     MVPSREALLG PGTTAIRCPK KLQNQNYKGH GLSKGKEREQ RASIRFKTTL MNTLMDVLRH
     RPGWVEVKDE GEWDFYWCDV SWLRENFDHT YMDEHVRISH FRNHYELTRK NYMVKNLKRF
     RKQLEREAGK LEAAKCDFFP KTFEMPCEYH LFVEEFRKNP GITWIMKPVA RSQGKGIFLF
     RRLKDIVDWR KDTRSSDDQK DDIPVENYVA QRYIENPYLI GGRKFDLRVY VLVMSVFAEC
     LLWSGHRRQD VHLTNVAVQK TSPDYHPKKG CKWTLQRFRQ YLASKHGPEA VETLFRDIDN
     IFVKSLQSVQ KVIISDKHCF ELYGYDILID QDLKPWLLEV NASPSLTASS QEDYELKTCL
     LEDTLHVVDM EARLTGREKR VGGFDLMWND GPVSREEGAP DLSGMGNFVT NTHLGCVNDR
     KKQLRQLFCS LQVQKKASS
//