SAT2_BOVIN
ID SAT2_BOVIN Reviewed; 170 AA.
AC Q7PCJ8; Q0II54;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Thialysine N-epsilon-acetyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q96F10};
DE AltName: Full=Diamine acetyltransferase 2 {ECO:0000250|UniProtKB:Q96F10};
DE EC=2.3.1.57 {ECO:0000250|UniProtKB:Q96F10};
DE AltName: Full=Spermidine/spermine N(1)-acetyltransferase 2 {ECO:0000303|PubMed:12803540};
DE Short=SSAT-2 {ECO:0000303|PubMed:12803540};
GN Name=SAT2 {ECO:0000250|UniProtKB:Q96F10};
GN Synonyms=SSAT2 {ECO:0000303|PubMed:12803540};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RX PubMed=12803540; DOI=10.1042/bj20030734;
RA Chen Y., Vujcic S., Liang P., Diegelman P., Kramer D.L., Porter C.W.;
RT "Genomic identification and biochemical characterization of a second
RT spermidine/spermine N1-acetyltransferase.";
RL Biochem. J. 373:661-667(2003).
CC -!- FUNCTION: Catalyzes the N-acetylation of the amino acid thialysine (S-
CC (2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene
CC group substituted with a sulfur. May also catalyze acetylation of
CC polyamines, such as norspermidine, spermidine or spermine. However,
CC ability to acetylate polyamines is weak, suggesting that it does not
CC act as a diamine acetyltransferase in vivo.
CC {ECO:0000250|UniProtKB:Q96F10}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + S-(2-aminoethyl)-L-cysteine = CoA + H(+) + S-(2-
CC acetamidoethyl)-L-cysteine; Xref=Rhea:RHEA:64804, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:156132,
CC ChEBI:CHEBI:156134; Evidence={ECO:0000250|UniProtKB:Q96F10};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64805;
CC Evidence={ECO:0000250|UniProtKB:Q96F10};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an alkane-alpha,omega-diamine = an N-
CC acetylalkane-alpha,omega-diamine + CoA + H(+); Xref=Rhea:RHEA:11116,
CC Rhea:RHEA-COMP:9766, Rhea:RHEA-COMP:9767, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:70977,
CC ChEBI:CHEBI:70988; EC=2.3.1.57;
CC Evidence={ECO:0000250|UniProtKB:Q96F10};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96F10}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96F10}.
CC Note=Intracellular organelles. {ECO:0000250|UniProtKB:Q96F10}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; BC122800; AAI22801.1; -; mRNA.
DR EMBL; BK001359; DAA01469.1; -; mRNA.
DR RefSeq; NP_976068.1; NM_203323.3.
DR AlphaFoldDB; Q7PCJ8; -.
DR SMR; Q7PCJ8; -.
DR STRING; 9913.ENSBTAP00000005531; -.
DR PaxDb; Q7PCJ8; -.
DR PRIDE; Q7PCJ8; -.
DR Ensembl; ENSBTAT00000005531; ENSBTAP00000005531; ENSBTAG00000004222.
DR GeneID; 359722; -.
DR KEGG; bta:359722; -.
DR CTD; 112483; -.
DR VEuPathDB; HostDB:ENSBTAG00000004222; -.
DR VGNC; VGNC:34297; SAT2.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR HOGENOM; CLU_013985_41_1_1; -.
DR InParanoid; Q7PCJ8; -.
DR OMA; RYSTWKG; -.
DR OrthoDB; 1228251at2759; -.
DR TreeFam; TF319736; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000004222; Expressed in metanephros cortex and 103 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019809; F:spermidine binding; IBA:GO_Central.
DR GO; GO:0046204; P:nor-spermidine metabolic process; IEA:Ensembl.
DR GO; GO:0032920; P:putrescine acetylation; IEA:Ensembl.
DR GO; GO:0032918; P:spermidine acetylation; IBA:GO_Central.
DR GO; GO:0032919; P:spermine acetylation; IEA:Ensembl.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032959; SAT2.
DR PANTHER; PTHR10545:SF51; PTHR10545:SF51; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..170
FT /note="Thialysine N-epsilon-acetyltransferase"
FT /id="PRO_0000074597"
FT DOMAIN 4..166
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 27..28
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 94..96
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96F10"
FT BINDING 102..107
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96F10"
FT BINDING 133..135
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96F10"
FT BINDING 140
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96F10"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96F10"
SQ SEQUENCE 170 AA; 19187 MW; 0DBC86BF794F611D CRC64;
MAFVMIREAK EGDCGNILRL IRELAEYEKL SDQVKISEEA LRADGFGETP FYHCLVAEIL
SAPGEPQGPC VVGYGLYYFS YSTWKGRNIY LEDIYVKPEY RGQGIGSKII KKVAEVALDK
GCSQLRLAVL DWNKRAMDLY KALGAQDLTE AEGWHCFRFE GEAMRELAGK
