ID A0A7J7EIJ2_DICBM Unreviewed; 398 AA. AC A0A7J7EIJ2; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 29-SEP-2021, entry version 3. DE RecName: Full=Alpha-tubulin N-acetyltransferase 1 {ECO:0000256|HAMAP-Rule:MF_03130}; DE Short=Alpha-TAT {ECO:0000256|HAMAP-Rule:MF_03130}; DE Short=Alpha-TAT1 {ECO:0000256|HAMAP-Rule:MF_03130}; DE Short=TAT {ECO:0000256|HAMAP-Rule:MF_03130}; DE EC=2.3.1.108 {ECO:0000256|HAMAP-Rule:MF_03130}; DE AltName: Full=Acetyltransferase mec-17 homolog {ECO:0000256|HAMAP-Rule:MF_03130}; GN Name=ATAT1 {ECO:0000256|HAMAP-Rule:MF_03130}; GN Synonyms=MEC17 {ECO:0000256|HAMAP-Rule:MF_03130}; GN ORFNames=HPG69_012653 {ECO:0000313|EMBL:KAF5915493.1}; OS Diceros bicornis minor (South-central black rhinoceros). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Rhinocerotidae; Diceros. OX NCBI_TaxID=77932 {ECO:0000313|EMBL:KAF5915493.1, ECO:0000313|Proteomes:UP000551758}; RN [1] {ECO:0000313|EMBL:KAF5915493.1, ECO:0000313|Proteomes:UP000551758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBR-YM {ECO:0000313|EMBL:KAF5915493.1}; RC TISSUE=Skin {ECO:0000313|EMBL:KAF5915493.1}; RX PubMed=32585004; RA Moodley Y., Westbury M.V., Russo I.M., Gopalakrishnan S., Rakotoarivelo A., RA Olsen R.A., Prost S., Tunstall T., Ryder O.A., Dalen L., Bruford M.W.; RT "Interspecific Gene Flow and the Evolution of Specialization in Black and RT White Rhinoceros."; RL Mol. Biol. Evol. 37:3105-3117(2020). CC -!- FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the CC lumenal side of microtubules. Promotes microtubule destabilization and CC accelerates microtubule dynamics; this activity may be independent of CC acetylation activity. Acetylates alpha-tubulin with a slow enzymatic CC rate, due to a catalytic site that is not optimized for acetyl CC transfer. Enters the microtubule through each end and diffuses quickly CC throughout the lumen of microtubules. Acetylates only long/old CC microtubules because of its slow acetylation rate since it does not CC have time to act on dynamically unstable microtubules before the enzyme CC is released. Required for normal sperm flagellar function. Promotes CC directional cell locomotion and chemotaxis, through AP2A2-dependent CC acetylation of alpha-tubulin at clathrin-coated pits that are CC concentrated at the leading edge of migrating cells. May facilitate CC primary cilium assembly. {ECO:0000256|HAMAP-Rule:MF_03130}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H(+) + N(6)- CC acetyl-L-lysyl-[alpha-tubulin]; Xref=Rhea:RHEA:15277, Rhea:RHEA- CC COMP:11278, Rhea:RHEA-COMP:11279, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:61930; EC=2.3.1.108; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03130}; CC -!- SUBUNIT: Component of the BBSome complex. Interacts with AP2 alpha- CC adaptins, including AP2A2, but not with AP1 gamma-adaptin CC (AP1G1/AP1G2); this interaction is required for efficient alpha-tubulin CC acetylation, hence clathrin-coated pits are sites of microtubule CC acetylation. {ECO:0000256|HAMAP-Rule:MF_03130}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03130}. CC Membrane, clathrin-coated pit {ECO:0000256|HAMAP-Rule:MF_03130}. Cell CC junction, focal adhesion {ECO:0000256|HAMAP-Rule:MF_03130}. Cell CC projection, axon {ECO:0000256|HAMAP-Rule:MF_03130}. Cytoplasm, CC cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03130}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03130}. CC -!- PTM: Autoacetylation strongly increases tubulin acetylation. CC {ECO:0000256|HAMAP-Rule:MF_03130}. CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family. CC {ECO:0000256|HAMAP-Rule:MF_03130}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAF5915493.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JACDTQ010002860; KAF5915493.1; -; Genomic_DNA. DR Proteomes; UP000551758; Unassembled WGS sequence. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell. DR GO; GO:0005874; C:microtubule; IEA:InterPro. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0071929; P:alpha-tubulin acetylation; IEA:UniProtKB-UniRule. DR GO; GO:0048666; P:neuron development; IEA:UniProtKB-UniRule. DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:UniProtKB-UniRule. DR HAMAP; MF_03130; mec17; 1. DR InterPro; IPR038746; Atat. DR InterPro; IPR007965; GNAT_ATAT. DR PANTHER; PTHR12327; PTHR12327; 1. DR Pfam; PF05301; Acetyltransf_16; 1. DR PROSITE; PS51730; GNAT_ATAT; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|HAMAP-Rule:MF_03130}; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_03130}; KW Cell junction {ECO:0000256|HAMAP-Rule:MF_03130}; KW Cell projection {ECO:0000256|HAMAP-Rule:MF_03130}; KW Coated pit {ECO:0000256|ARBA:ARBA00023176, ECO:0000256|HAMAP- KW Rule:MF_03130}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03130}; KW Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03130}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_03130}; KW Reference proteome {ECO:0000313|Proteomes:UP000551758}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03130}. FT DOMAIN 1..190 FT /note="N-acetyltransferase" FT /evidence="ECO:0000259|PROSITE:PS51730" FT REGION 124..137 FT /note="Acetyl-CoA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03130" FT REGION 160..169 FT /note="Acetyl-CoA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03130" FT REGION 229..261 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 281..379 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 232..247 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 314..333 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 334..353 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 354..372 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 58 FT /note="Crucial for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03130" FT MOD_RES 56 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03130" FT MOD_RES 146 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03130" SQ SEQUENCE 398 AA; 44732 MW; E54FD41A2EA43115 CRC64; MEFPFDVDAL LPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIVDEL GKASAKAQHL PAPITSASRM QSNRHVMYVL KDTSARPAGK GAIIGFLKVG YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE PHQLAIDRPS QKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHPPARKL PPKRAEGDIK PYSSSDREFL KVAVEPPWPL NRAPRRATPP AHPPPRSSSL GNSPERGPLR PFVPEQELLR SLRLCPPHPT ARLLLATDPG GSPAQRRRTR GSPPGLVAQS CCYSRHGGLN SSFPNTGNQE SKQGEQETEN RSASEEHVLS QDGSGEEPTH TVPPQAQAPP AQSWTMGGDM FNARFIRNLQ ERRSTRPW //