ID F6WP65_HORSE Unreviewed; 1007 AA.
AC F6WP65;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Tubulin tyrosine ligase like 3 {ECO:0000313|Ensembl:ENSECAP00000002855.2};
GN Name=TTLL3 {ECO:0000313|Ensembl:ENSECAP00000002855.2};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000002855.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000002855.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000002855.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000002855.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000002855.2};
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 AlphaFoldDB; F6WP65; -.
DR SMR; F6WP65; -.
DR STRING; 9796.ENSECAP00000002855; -.
DR PaxDb; 9796-ENSECAP00000002855; -.
DR Ensembl; ENSECAT00000004131.3; ENSECAP00000002855.2; ENSECAG00000003474.4.
DR GeneTree; ENSGT00940000154857; -.
DR HOGENOM; CLU_010131_5_0_1; -.
DR InParanoid; F6WP65; -.
DR OMA; MINHFPA; -.
DR OrthoDB; 7265at2759; -.
DR TreeFam; TF313087; -.
DR Proteomes; UP000002281; Chromosome 16.
DR Bgee; ENSECAG00000003474; Expressed in testis and 23 other cell types or tissues.
DR ExpressionAtlas; F6WP65; baseline.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0070736; F:protein-glycine ligase activity, initiating; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0003341; P:cilium movement; 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; 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:UP000002281}.
FT REGION 36..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 112366 MW; 0961D07BB137A9C2 CRC64;
MPGPGAALLL SPGEWGAAHR GSAAWVLQEG DLGCSWPKKP QLPEPRTSSP APWPWARHSL
SRPPETLPWP GTTSARCDGA RAGGKRRTGS PASARPLGCA FGSLARCTPA QGAAYPRPLG
PPQASALEEA SPQDGSLVLW RGFSKASHHM GRLRSAKMHV ERAVKQKKIF MIQGRYPVIR
CLLRRRGWVE KKMVRHSGTA LPLPRKDLDS SVVGNSDTTE DEDEDEDETF QPPQLFDFDD
LLEFDDLDGT HALMSRMVRN EIPYFIWTTR RDVLDCRFLS KDQMINHYAR AGSFTTKVGL
CLNLRNLPWF DEADADSFFP RCYRLGAEDD KKAFIEDFWL TAARNVLKLV VKSEWKSYSI
QAEEEEASGD KQPEKQDGKP GMVSSEFVDE ALRACEEHLS NLAHMDIDKD LEAPMYLSPE
GWSLFLQHYY QVVHEGAELR HIDTQVRRCE DILQQLRTVV PQMDMEGDRN IWIVKPGAKS
RGRGIMCMDH LEEMLKLVDG NPMMMKDGKW VVQKYIERPL LIFGTKFDLR QWFLVTDWNP
LTVWFYRDSY IRFSTQPFSL ENLDNSVHLC NNSIQKHLEN SCHRHPLLPS DNMWSSQKFQ
AHLRDMGAPN AWATVIVPGM KAAVIHALQT SQDTVQGRKA SFELYGADFV FGEDFQPWLI
EINASPTMAP STAVTARLCA GVQADTLRVV IDRRLDRNCD TGAFELIYKQ PPVEVPQYVG
IRLLVEGSAI KKPLAMCHRR TGVRPALPHL LTQQGSGEGK DLGTLTHRSA PRKAAGDRSL
GHTEKPDSTA TTSAPGKGKK GKAKSATALV RPNLPKWDPS STGMGCIFTM TFASGDRQPH
PLNRLPLSLK NPQALAPYHF PSFHTKARLP SSYVLRPQGR VLRLQHSKLV GPKALSTTGK
ALMTLPTAKV FICFPPNPEL KLASNVLKPR KAVAPPWHPG NALCSLPFEV GNLPSTQRKI
KAKGKFKARL DKPKAEACLM KTVSLPSKTS APHRYIPWAG GAWGTRG
//
