ATAT_ANOGA
ID ATAT_ANOGA Reviewed; 483 AA.
AC Q7PNM6; A7UTW7; A7UTW8;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 4.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Alpha-tubulin N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=TAT {ECO:0000255|HAMAP-Rule:MF_03130};
DE EC=2.3.1.108 {ECO:0000255|HAMAP-Rule:MF_03130};
DE AltName: Full=Acetyltransferase mec-17 homolog {ECO:0000255|HAMAP-Rule:MF_03130};
GN ORFNames=AGAP005828;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_03130};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q7PNM6-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q7PNM6-2; Sequence=VSP_040234, VSP_040235;
CC Name=C;
CC IsoId=Q7PNM6-3; Sequence=VSP_040232, VSP_040233;
CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; AAAB01008960; EDO63742.1; -; Genomic_DNA.
DR EMBL; AAAB01008960; EDO63741.1; -; Genomic_DNA.
DR EMBL; AAAB01008960; EAA11927.5; -; Genomic_DNA.
DR RefSeq; XP_001688735.1; XM_001688683.1.
DR RefSeq; XP_001688736.1; XM_001688684.1.
DR RefSeq; XP_315853.4; XM_315853.4.
DR AlphaFoldDB; Q7PNM6; -.
DR SMR; Q7PNM6; -.
DR STRING; 7165.AGAP005828-PA; -.
DR PaxDb; Q7PNM6; -.
DR GeneID; 1276496; -.
DR KEGG; aga:AgaP_AGAP005828; -.
DR VEuPathDB; VectorBase:AGAP005828; -.
DR eggNOG; KOG4601; Eukaryota.
DR HOGENOM; CLU_025013_4_1_1; -.
DR InParanoid; Q7PNM6; -.
DR OMA; PPCSMAN; -.
DR OrthoDB; 1143678at2759; -.
DR PhylomeDB; Q7PNM6; -.
DR Proteomes; UP000007062; Chromosome 2L.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0071929; P:alpha-tubulin acetylation; IBA:GO_Central.
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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR038746; Atat.
DR InterPro; IPR007965; GNAT_ATAT.
DR PANTHER; PTHR12327; PTHR12327; 1.
DR Pfam; PF05301; Acetyltransf_16; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51730; GNAT_ATAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Alternative splicing; Reference proteome; Transferase.
FT CHAIN 1..483
FT /note="Alpha-tubulin N-acetyltransferase"
FT /id="PRO_0000402071"
FT DOMAIN 1..186
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 204..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120..133
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT BINDING 156..165
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT SITE 57
FT /note="Crucial for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT VAR_SEQ 206
FT /note="S -> R (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_040232"
FT VAR_SEQ 207..483
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_040233"
FT VAR_SEQ 285..302
FT /note="EEQELDQRLADEMERCVE -> IIHNSPTTVSTEPNSNFT (in isoform
FT B)"
FT /evidence="ECO:0000305"
FT /id="VSP_040234"
FT VAR_SEQ 303..483
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_040235"
SQ SEQUENCE 483 AA; 53608 MW; 0FDC7D7B466B42E2 CRC64;
MEFRFNMHPL FRARIVRINN SLLPTGFVAQ SRRVALDATA QISEIINTIG SMSAQAQGLS
VPVTTAQKLR NSDHHIYLMF ESNDRNGLVV GILKVGRKSL YVFDPSGETV NVTAPCVLDF
YVHESRQRGG LGRELFEHML REENIQPDEL AIDRPSEKLL GFLQKHYGLS KKIPQMNNFV
VYEGFFASKA QNSTDIDGRR MHITASPNTN LFGPTFTTTE ERRRSTSQTR TNVAPMPIIA
QPPVGRYAAK RPTCSMAQVN HYSSMVGKIS FPEENTGNGK RSVFEEQELD QRLADEMERC
VELGAGGDEP DASRYTPHHG LEVKFADQPE TLPYDDMPEP GPDPDPYDFH PHHLELHDDT
EGGGSHRDQS LSPQSVSQQA SPVHPAGSDY GVLGSRKPAR YTKQNTGLKN ISFGVGAAVM
PSGKMEFDQE ENEGFGSVKI NRPIGKSGTR GSLHDDNESV HSNGSQQGGG GHFDLKFYHN
KLW
