ID F8VQA1_MOUSE Unreviewed; 721 AA.
AC F8VQA1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Tubulin tyrosine ligase-like family, member 3 {ECO:0000313|Ensembl:ENSMUSP00000145329.2};
DE Flags: Fragment;
GN Name=Ttll3 {ECO:0000313|Ensembl:ENSMUSP00000145329.2,
GN ECO:0000313|MGI:MGI:2141418};
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:ENSMUSP00000145329.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000145329.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000145329.2,
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:ENSMUSP00000145329.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000145329.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-
CC glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180,
CC Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181;
CC Evidence={ECO:0000256|ARBA:ARBA00036933};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000256|ARBA:ARBA00004611}.
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DR ProteomicsDB; 309791; -.
DR Antibodypedia; 74193; 3 antibodies from 3 providers.
DR Ensembl; ENSMUST00000203524.3; ENSMUSP00000145329.2; ENSMUSG00000030276.20.
DR AGR; MGI:2141418; -.
DR MGI; MGI:2141418; Ttll3.
DR VEuPathDB; HostDB:ENSMUSG00000030276; -.
DR GeneTree; ENSGT00940000154857; -.
DR ChiTaRS; Ttll3; mouse.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000030276; Expressed in granulocyte and 149 other cell types or tissues.
DR ExpressionAtlas; F8VQA1; baseline and differential.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProt.
DR GO; GO:0140096; F:catalytic activity, acting on a protein; 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; PTHR45870; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR PANTHER; PTHR45870:SF1; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT REGION 41..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000145329.2"
SQ SEQUENCE 721 AA; 81840 MW; 5B550854AA7FBAB4 CRC64;
XNAKIHVERA VKQKKIFMIH GRYPVIRCLL RQRGWVEKKM VHPPGTALPA PQKDLDSSML
GDSDATEDED EEENEMFRES QLLDLDGFLE FDDLDGIHAL MSRMVRNETP YLIWTTRRDV
LDCRFLSKDQ MINHYARAGS FTTKVGLCLN LRNLPWFDEA DADSFFPRCY RLGAEDDKKA
FIEDFWLTAA RNVLKLVVKL EEKSQSISIQ AREEEAPEDT QPKKQEKKLV TVSSDFVDEA
LSACQEHLSS IAHKDIDKDP NSPLYLSPDD WSQFLQRYYQ IVHEGAELRY LEVQVQRCED
ILQQLQNVVP QLDMEGDRNI WIVKPGAKSR GRGIMCMNRL DEMLKLVDCN PMLMKDGKWI
VQKYIERPLL IFGTKFDLRQ WFLVTDWNPL TVWFYRDSYI RFSTQPFSLK NLDNSVHLCN
NSIQRHLEAS CHRHPMLPPD NMWSSQRFQA HLQEVDAPKA WSSVIVPGMK AAVIHALQTS
QDNVQCRKAS FELYGADFVF GEDFQPWLIE INASPTMAPS TAVTARLCAG VQADTLRVVI
DRRLDRSCDT GAFELIYKQP AVEVPQYVGI RLLVEGSTIK KPVPVGHRRT GVRSSLPHLL
TQQGSGESKD SGSPTHRSAS RKNARAESLE HTEKPEPAAV ASVSGKGKKA EVAGSLRTLP
EVAQLRRGRA GMQTQPLSTS LASIPRPGCL LPVCTDPRAG SSDSNMTSWW ALRLCQPQAR
P
//
