ID   A0A7J7EIJ2_DICBM        Unreviewed;       398 AA.
AC   A0A7J7EIJ2;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   02-JUN-2021, entry version 2.
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}.
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DR   EMBL; JACDTQ010002860; KAF5915493.1; -; Genomic_DNA.
DR   Proteomes; UP000551758; Unassembled WGS sequence.
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|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_03130}; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   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
//