ID F1SJR6_PIG Unreviewed; 441 AA.
AC F1SJR6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 3.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=TTL family tubulin polyglutamylase complex subunit L1 {ECO:0000313|Ensembl:ENSSSCP00000000037.4};
GN Name=TTLL1 {ECO:0000313|Ensembl:ENSSSCP00000000037.4,
GN ECO:0000313|VGNC:VGNC:94566};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000000037.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000000037.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000000037.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000000037.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000256|ARBA:ARBA00004120}.
CC -!- SIMILARITY: Belongs to the tubulin polyglutamylase family.
CC {ECO:0000256|ARBA:ARBA00006118}.
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DR AlphaFoldDB; F1SJR6; -.
DR Ensembl; ENSSSCT00000000037.5; ENSSSCP00000000037.4; ENSSSCG00000000035.5.
DR VGNC; VGNC:94566; TTLL1.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000156720; -.
DR HOGENOM; CLU_010131_0_0_1; -.
DR TreeFam; TF313087; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000000035; Expressed in testis and 45 other cell types or tissues.
DR ExpressionAtlas; F1SJR6; baseline and differential.
DR Genevisible; F1SJR6; SS.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:SF31; POLYGLUTAMYLASE COMPLEX SUBUNIT TTLL1; 1.
DR PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51221; TTL; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
SQ SEQUENCE 441 AA; 50583 MW; 7E544AF8E0E21B87 CRC64;
MAGKVKWVTD IEKSVLINNF EKRGWVQVTE SEDWNFYWMS VQTIRNVFSV ETGYRLSDDQ
IVNHFPNHYE LTRKDLMVKN IKRYRKELEK EGSPLAEKDE SGKYLYLDFV PVTYMLPADY
NLFVEEFRKS PSSTWIMKPC GRAQGKGIFL INKLSQIKKW SRDSKTSSFV SQSPKEAYVI
SLYISNPLLI GGRKFDLRLY VLVSTYRPLR CYMYKLGFCR FCTVKYTPST SELDNMFVHL
TNVAIQKHGE DYNHIHGGKW TVSNLRLYLE STRGKEVTSK LFDEIHWIIV QSLKAVAPVM
NNDKHCFECY GYDIIIDDRL KPWLIEVNAS PSLTSSTAND RILKYNLIND TLNIAVPNGE
VPDCKWNKSP PKEVLGNYEI LYVGTSCCGE CVSRQHFPSL RWCPLLFLGG HCWIQSGGLS
QMSAAGAGPS VRRGAGTRGR G
//
