SAT2_PIG
ID SAT2_PIG Reviewed; 170 AA.
AC Q7PCJ9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-119.
RA Fahrenkrug S.C., Freking B.A., Rohrer G.A., Smith T.P.L., Casas E.,
RA Stone R.T., Heaton M.P., Grosse W.M., Bennett G.A., Laegreid W.W.,
RA Keele J.W.;
RT "Design and use of two pooled tissue normalized cDNA libraries for EST
RT discovery in swine.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-170.
RA Neilan J.G., Kutish G.F., Lu Z., Zsak A., Rock D.L.;
RT "Sequence analysis of African swine fever virus infected and non-infected
RT porcine macrophage cDNA libraries.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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; BF198274; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CB470125; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BK001358; DAA01468.1; -; mRNA.
DR RefSeq; NP_001123434.1; NM_001129962.2.
DR AlphaFoldDB; Q7PCJ9; -.
DR SMR; Q7PCJ9; -.
DR STRING; 9823.ENSSSCP00000019018; -.
DR PaxDb; Q7PCJ9; -.
DR PeptideAtlas; Q7PCJ9; -.
DR PRIDE; Q7PCJ9; -.
DR Ensembl; ENSSSCT00000019536; ENSSSCP00000019018; ENSSSCG00000017952.
DR Ensembl; ENSSSCT00015049048; ENSSSCP00015019528; ENSSSCG00015036850.
DR Ensembl; ENSSSCT00035068642; ENSSSCP00035027778; ENSSSCG00035051544.
DR Ensembl; ENSSSCT00055029955; ENSSSCP00055023856; ENSSSCG00055015080.
DR Ensembl; ENSSSCT00065068599; ENSSSCP00065029864; ENSSSCG00065050091.
DR GeneID; 100170117; -.
DR KEGG; ssc:100170117; -.
DR CTD; 112483; -.
DR VGNC; VGNC:92586; SAT2.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR InParanoid; Q7PCJ9; -.
DR OMA; RYSTWKG; -.
DR OrthoDB; 1228251at2759; -.
DR Proteomes; UP000008227; Chromosome 12.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000017952; Expressed in granulosa cell and 46 other tissues.
DR ExpressionAtlas; Q7PCJ9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019809; F:spermidine binding; IBA:GO_Central.
DR GO; GO:0032918; P:spermidine acetylation; IBA:GO_Central.
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_0000074600"
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; 19171 MW; 1B1E063A20550568 CRC64;
MASVLIREAK EGDCGNILRM IRELAEYEKL SDQVKISEEA LRADGFGENP FFHCLVAEIL
PAPGEPQGSC MVGYGLYYFI YSTWTGRNIY LEDIYVKPEY RGQGIGSKII KKVAEVALDK
GCSQFRLAVL DWNKKAVDLY KTLGARDLTE AEGWHSFRFE GEAMRELAGK
