ID H3BLN3_MOUSE Unreviewed; 432 AA.
AC H3BLN3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN Name=Ttll5 {ECO:0000313|Ensembl:ENSMUSP00000135852.2,
GN ECO:0000313|MGI:MGI:2443657};
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 {ECO:0000313|Ensembl:ENSMUSP00000135852.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000135852.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000135852.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000135852.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000135852.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC Evidence={ECO:0000256|ARBA:ARBA00036640};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR ProteomicsDB; 342875; -.
DR Ensembl; ENSMUST00000176695.8; ENSMUSP00000135852.2; ENSMUSG00000012609.20.
DR Ensembl; ENSMUST00000177114.2; ENSMUSP00000135395.2; ENSMUSG00000012609.20.
DR AGR; MGI:2443657; -.
DR MGI; MGI:2443657; Ttll5.
DR VEuPathDB; HostDB:ENSMUSG00000012609; -.
DR GeneTree; ENSGT00940000162910; -.
DR ChiTaRS; Ttll5; mouse.
DR Proteomes; UP000000589; Chromosome 12.
DR Bgee; ENSMUSG00000012609; Expressed in spermatocyte and 207 other cell types or tissues.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IEA:UniProt.
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:SF145; TUBULIN POLYGLUTAMYLASE TTLL5; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|ProteomicsDB:H3BLN3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 49539 MW; 15EE5F389FF96E5A CRC64;
MPVVMARDLE ETASSSEDED LANQEDHPCI MWTGGCRRIP VLVFHAEAIL TKDNNIRVIG
ERYHLSYKIV RTDSRLVRSI LTAHGFHEVH PSSTDYNLMW TGSHLKPFLL RTLSEAQKVN
HFPRSYELTR KDRLYKNIIR MQHTHGFKAF HILPQTFLLP AEYAEFCNSY SKDRGPWIVK
PVASSRGRGV YLINNPNQIS LEENILVSRY INNPLLIDDF KFDVRLYVLV TSYDPLVIYL
YEEGLARFAT VRYDQGSKNI RNQFMHLTNY SVNKKSGDYV SCDDPEVEDY GNKWSMSAML
RYLKQEGKDT TALMAHVEDL IIKTIISAEL AIATACKTFV PHRSSCFELY GFDVLIDNTL
KPWLLEVNLS PSLACDAPLD LKIKASMISD MFTVVGFVCQ DPAQRTSNRS IYPSFESSRR
NPFQKPQLPV SA
//