SAN_DROME
ID SAN_DROME Reviewed; 184 AA.
AC Q9NHD5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable N-acetyltransferase san;
DE EC=2.3.1.258 {ECO:0000250|UniProtKB:Q9GZZ1};
DE AltName: Full=N-epsilon-acetyltransferase san;
DE EC=2.3.1.- {ECO:0000305|PubMed:14653991};
DE AltName: Full=Protein atado {ECO:0000303|PubMed:18801358};
DE AltName: Full=Protein separation anxiety {ECO:0000303|PubMed:14653991};
GN Name=san; Synonyms=span; ORFNames=CG12352;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION
RP IN A COMPLEX WITH ARD1 AND NAT1, ACETYLATION AT LYS-47, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=14653991; DOI=10.1016/j.cub.2003.11.018;
RA Williams B.C., Garrett-Engele C.M., Li Z., Williams E.V., Rosenman E.D.,
RA Goldberg M.L.;
RT "Two putative acetyltransferases, san and deco, are required for
RT establishing sister chromatid cohesion in Drosophila.";
RL Curr. Biol. 13:2025-2036(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18801358; DOI=10.1016/j.ydbio.2008.08.021;
RA Pimenta-Marques A., Tostoes R., Marty T., Barbosa V., Lehmann R.,
RA Martinho R.G.;
RT "Differential requirements of a mitotic acetyltransferase in somatic and
RT germ line cells.";
RL Dev. Biol. 323:197-206(2008).
RN [6]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE (MICROBIAL
RP INFECTION).
RX PubMed=22851751; DOI=10.1128/iai.00670-12;
RA Von Ohlen T., Luce-Fedrow A., Ortega M.T., Ganta R.R., Chapes S.K.;
RT "Identification of critical host mitochondrion-associated genes during
RT Ehrlichia chaffeensis infections.";
RL Infect. Immun. 80:3576-3586(2012).
RN [7]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE (MICROBIAL
RP INFECTION).
RX PubMed=23306065; DOI=10.1016/j.ijmm.2012.12.002;
RA Drolia R., Von Ohlen T., Chapes S.K.;
RT "Ehrlichia chaffeensis replication sites in adult Drosophila
RT melanogaster.";
RL Int. J. Med. Microbiol. 303:40-49(2013).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ARG-84 AND TYR-124.
RX PubMed=27996020; DOI=10.1038/srep39118;
RA Ribeiro A.L., Silva R.D., Foyn H., Tiago M.N., Rathore O.S., Arnesen T.,
RA Martinho R.G.;
RT "Naa50/San-dependent N-terminal acetylation of Scc1 is potentially
RT important for sister chromatid cohesion.";
RL Sci. Rep. 6:39118-39118(2016).
CC -!- FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of
CC proteins that retain their initiating methionine (By similarity). Has a
CC broad substrate specificity: able to acetylate the initiator methionine
CC of most peptides (By similarity). Also displays N-epsilon-
CC acetyltransferase activity by mediating acetylation of the side chain
CC of specific lysines on proteins. Autoacetylates (PubMed:14653991).
CC Required for the establishment of sister chromatid cohesion and couple
CC the processes of cohesion and DNA replication to ensure that only
CC sister chromatids become paired together (PubMed:14653991,
CC PubMed:18801358, PubMed:27996020). Required for the interaction between
CC Scc1/vtd and SMC3, possibly by mediating N-terminal acetylation of
CC Scc1/vtd (PubMed:27996020). {ECO:0000250|UniProtKB:Q9GZZ1,
CC ECO:0000269|PubMed:14653991, ECO:0000269|PubMed:18801358,
CC ECO:0000269|PubMed:27996020}.
CC -!- FUNCTION: (Microbial infection) Required for optimal replication of
CC E.chaffeensis in the immune tissues, hemocytes, and fat body.
CC {ECO:0000269|PubMed:22851751, ECO:0000269|PubMed:23306065}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein];
CC Xref=Rhea:RHEA:50564, Rhea:RHEA-COMP:12726, Rhea:RHEA-COMP:12727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133398, ChEBI:CHEBI:133399; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein];
CC Xref=Rhea:RHEA:50568, Rhea:RHEA-COMP:12728, Rhea:RHEA-COMP:12729,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133400, ChEBI:CHEBI:133401; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein];
CC Xref=Rhea:RHEA:50572, Rhea:RHEA-COMP:12730, Rhea:RHEA-COMP:12731,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133402, ChEBI:CHEBI:133403; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein];
CC Xref=Rhea:RHEA:50576, Rhea:RHEA-COMP:12732, Rhea:RHEA-COMP:12733,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133404, ChEBI:CHEBI:133405; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein];
CC Xref=Rhea:RHEA:50580, Rhea:RHEA-COMP:12734, Rhea:RHEA-COMP:12735,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133406, ChEBI:CHEBI:133407; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.258;
CC Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC -!- SUBUNIT: Component of an acetyltransferase complex, at least composed
CC of san, Ard1 and Nat1. {ECO:0000269|PubMed:14653991}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14653991}.
CC Note=During interphase, it localizes to the cytoplasm. During the entry
CC into mitosis, it becomes distributed throughout the entire cell in a
CC punctate pattern. From metaphase through telophase, it is distributed
CC uniformly throughout the cell. {ECO:0000269|PubMed:14653991}.
CC -!- PTM: Autoacetylated. {ECO:0000305|PubMed:14653991}.
CC -!- DISRUPTION PHENOTYPE: Flies display disrupt centromeric sister
CC chromatid cohesion very early in division (PubMed:14653991,
CC PubMed:18801358). This failure of sister chromatid cohesion does not
CC require separase and is correlated with a failure of the cohesin
CC component Scc1 to accumulate in centromeric regions (PubMed:14653991).
CC In contrast, no mitotic defects are observed in germ line cells during
CC oogenesis (PubMed:18801358). {ECO:0000269|PubMed:14653991,
CC ECO:0000269|PubMed:18801358}.
CC -!- DISRUPTION PHENOTYPE: (Microbial infection) After infection with
CC E.chaffeensis, results in reduced bacterial replication rate and
CC increased survival (PubMed:22851751). RNAi-mediated knockdown in the
CC whole organism, in the fat body or hemocytes results in a similar
CC phenotype to the genetic knockout (PubMed:23306065). However, knockdown
CC in the eye, salivary gland or wing has no effect (PubMed:23306065).
CC {ECO:0000269|PubMed:22851751, ECO:0000269|PubMed:23306065}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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; AF225902; AAF34715.1; -; mRNA.
DR EMBL; AE013599; AAG22284.1; -; Genomic_DNA.
DR EMBL; AY070826; AAL48448.1; -; mRNA.
DR RefSeq; NP_524779.1; NM_080040.5.
DR AlphaFoldDB; Q9NHD5; -.
DR SMR; Q9NHD5; -.
DR BioGRID; 69228; 8.
DR IntAct; Q9NHD5; 2.
DR STRING; 7227.FBpp0087227; -.
DR iPTMnet; Q9NHD5; -.
DR PaxDb; Q9NHD5; -.
DR PRIDE; Q9NHD5; -.
DR DNASU; 44724; -.
DR EnsemblMetazoa; FBtr0088126; FBpp0087227; FBgn0024188.
DR GeneID; 44724; -.
DR KEGG; dme:Dmel_CG12352; -.
DR CTD; 44724; -.
DR FlyBase; FBgn0024188; san.
DR VEuPathDB; VectorBase:FBgn0024188; -.
DR eggNOG; KOG3138; Eukaryota.
DR GeneTree; ENSGT00390000009110; -.
DR HOGENOM; CLU_013985_5_3_1; -.
DR InParanoid; Q9NHD5; -.
DR OMA; IVETKEH; -.
DR OrthoDB; 1536763at2759; -.
DR PhylomeDB; Q9NHD5; -.
DR BioGRID-ORCS; 44724; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 44724; -.
DR PRO; PR:Q9NHD5; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0024188; Expressed in ovary and 21 other tissues.
DR Genevisible; Q9NHD5; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0031415; C:NatA complex; IDA:FlyBase.
DR GO; GO:0031248; C:protein acetyltransferase complex; IPI:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IDA:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cell cycle; Cytoplasm; Reference proteome;
KW Transferase.
FT CHAIN 1..184
FT /note="Probable N-acetyltransferase san"
FT /id="PRO_0000074578"
FT DOMAIN 6..155
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 138..141
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT ACT_SITE 112
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 77..90
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT BINDING 117..126
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT MOD_RES 47
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:14653991"
FT MUTAGEN 84
FT /note="R->A: Abolishes N-alpha-acetyltransferase activity;
FT impaired sister chromatid cohesion during mitosis.; when
FT associated with F-124."
FT /evidence="ECO:0000269|PubMed:27996020"
FT MUTAGEN 124
FT /note="Y->F: Abolishes N-alpha-acetyltransferase activity;
FT impaired sister chromatid cohesion during mitosis.; when
FT associated with A-84."
FT /evidence="ECO:0000269|PubMed:27996020"
SQ SEQUENCE 184 AA; 20994 MW; 4C3B707833086974 CRC64;
MTRSSIELGD VTPHNIKQLK KLNTVVFPVS YNDKFYVDVL EAGELAKLAY YNDIVVGAVC
CRIDNTENQR RLYIMTLGCL SPYRRLGIGT VMFEHIMNFA EKDGNFDSIF LHVQINNNGA
IEFYKKFGFE IVDTKEQYYK RIEPADAHVL QKTLRRTAPN SNSTATSTTA NSNSRSKARQ
FTFV
