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Acetyl-coenzyme A synthetase 2-like, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 2) (Acetyl-CoA synthetase 2) (AceCS2) (Acyl-CoA synthetase short-chain family member 1)

 ACS2L_HUMAN             Reviewed;         689 AA.
Q9NUB1; B3KXL2; B4DJZ3; D3DW48; F5H6F4; F8W7Y1; Q5TF42; Q8IV99;
Q8N234; Q96JI1; Q96JX6; Q9NU28;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
23-APR-2003, sequence version 2.
27-SEP-2017, entry version 145.
RecName: Full=Acetyl-coenzyme A synthetase 2-like, mitochondrial;
EC=6.2.1.1;
AltName: Full=Acetate--CoA ligase 2;
AltName: Full=Acetyl-CoA synthetase 2;
Short=AceCS2;
AltName: Full=Acyl-CoA synthetase short-chain family member 1;
Flags: Precursor;
Name=ACSS1; Synonyms=ACAS2L, KIAA1846;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 169-689 (ISOFORM 1), AND VARIANT
MET-488.
TISSUE=Placenta, Thalamus, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
MET-488.
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 336-689 (ISOFORM 1).
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[6]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[7]
ACETYLATION AT LYS-642, MUTAGENESIS OF LYS-642, FUNCTION, ENZYME
REGULATION, PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=16788062; DOI=10.1073/pnas.0603968103;
Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., Verdin E.;
"Reversible lysine acetylation controls the activity of the
mitochondrial enzyme acetyl-CoA synthetase 2.";
Proc. Natl. Acad. Sci. U.S.A. 103:10224-10229(2006).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 638-649 IN COMPLEX WITH
SIRT3.
PubMed=19535340; DOI=10.1074/jbc.M109.014928;
Jin L., Wei W., Jiang Y., Peng H., Cai J., Mao C., Dai H., Choy W.,
Bemis J.E., Jirousek M.R., Milne J.C., Westphal C.H., Perni R.B.;
"Crystal structures of human SIRT3 displaying substrate-induced
conformational changes.";
J. Biol. Chem. 284:24394-24405(2009).
-!- FUNCTION: Important for maintaining normal body temperature during
fasting and for energy homeostasis. Essential for energy
expenditure under ketogenic conditions (By similarity). Converts
acetate to acetyl-CoA so that it can be used for oxidation through
the tricarboxylic cycle to produce ATP and CO(2). {ECO:0000250,
ECO:0000269|PubMed:16788062}.
-!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
acetyl-CoA.
-!- ENZYME REGULATION: Inhibited by acetylation at Lys-642 and
activated by deacetylation. {ECO:0000269|PubMed:16788062}.
-!- SUBUNIT: Interacts with SIRT3. {ECO:0000269|PubMed:19535340}.
-!- INTERACTION:
Q08AM6:VAC14; NbExp=5; IntAct=EBI-10313831, EBI-2107455;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:16788062}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9NUB1-1; Sequence=Displayed;
Name=2;
IsoId=Q9NUB1-2; Sequence=VSP_007249;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9NUB1-3; Sequence=VSP_044693, VSP_044694;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9NUB1-4; Sequence=VSP_045546, VSP_045547;
Note=No experimental confirmation available.;
-!- PTM: Reversibly acetylated on Lys-642. The acetyl-CoA synthase
activity is inhibited by acetylation and activated by
deacetylation. {ECO:0000269|PubMed:16788062}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB55390.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC03853.1; Type=Frameshift; Positions=250; Evidence={ECO:0000305};
Sequence=BAC03853.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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EMBL; AK027817; BAB55390.1; ALT_INIT; mRNA.
EMBL; AK092295; BAC03853.1; ALT_SEQ; mRNA.
EMBL; AK127566; BAG54524.1; -; mRNA.
EMBL; AK296306; BAG59005.1; -; mRNA.
EMBL; AL035661; CAI21828.1; -; Genomic_DNA.
EMBL; AL080312; CAI21828.1; JOINED; Genomic_DNA.
EMBL; AL080312; CAI18917.1; -; Genomic_DNA.
EMBL; AL035661; CAI18917.1; JOINED; Genomic_DNA.
EMBL; CH471133; EAX10106.1; -; Genomic_DNA.
EMBL; CH471133; EAX10109.1; -; Genomic_DNA.
EMBL; BC039261; AAH39261.1; -; mRNA.
EMBL; BC044588; AAH44588.1; -; mRNA.
EMBL; AB058749; BAB47475.1; -; mRNA.
CCDS; CCDS13167.1; -. [Q9NUB1-1]
CCDS; CCDS58764.1; -. [Q9NUB1-3]
CCDS; CCDS58765.1; -. [Q9NUB1-4]
RefSeq; NP_001239604.1; NM_001252675.1. [Q9NUB1-2]
RefSeq; NP_001239605.1; NM_001252676.1. [Q9NUB1-3]
RefSeq; NP_001239606.1; NM_001252677.1. [Q9NUB1-4]
RefSeq; NP_115890.2; NM_032501.3. [Q9NUB1-1]
UniGene; Hs.529353; -.
PDB; 3GLR; X-ray; 1.80 A; B=638-649.
PDB; 3GLT; X-ray; 2.10 A; B=638-649.
PDB; 3GLU; X-ray; 2.50 A; B=638-649.
PDB; 4BVE; X-ray; 2.05 A; B=638-647.
PDB; 4BVF; X-ray; 2.70 A; B=638-647.
PDB; 4BVG; X-ray; 2.50 A; B=638-647.
PDB; 4C78; X-ray; 2.00 A; C=638-647.
PDBsum; 3GLR; -.
PDBsum; 3GLT; -.
PDBsum; 3GLU; -.
PDBsum; 4BVE; -.
PDBsum; 4BVF; -.
PDBsum; 4BVG; -.
PDBsum; 4C78; -.
ProteinModelPortal; Q9NUB1; -.
SMR; Q9NUB1; -.
BioGrid; 124122; 8.
DIP; DIP-61208N; -.
IntAct; Q9NUB1; 3.
STRING; 9606.ENSP00000316924; -.
DrugBank; DB00131; Adenosine monophosphate.
DrugBank; DB00171; Adenosine triphosphate.
SwissLipids; SLP:000000448; -.
iPTMnet; Q9NUB1; -.
PhosphoSitePlus; Q9NUB1; -.
BioMuta; ACSS1; -.
DMDM; 30172968; -.
EPD; Q9NUB1; -.
MaxQB; Q9NUB1; -.
PaxDb; Q9NUB1; -.
PeptideAtlas; Q9NUB1; -.
PRIDE; Q9NUB1; -.
Ensembl; ENST00000323482; ENSP00000316924; ENSG00000154930. [Q9NUB1-1]
Ensembl; ENST00000432802; ENSP00000388793; ENSG00000154930. [Q9NUB1-4]
Ensembl; ENST00000537502; ENSP00000439304; ENSG00000154930. [Q9NUB1-3]
GeneID; 84532; -.
KEGG; hsa:84532; -.
UCSC; uc002wub.4; human. [Q9NUB1-1]
CTD; 84532; -.
DisGeNET; 84532; -.
EuPathDB; HostDB:ENSG00000154930.14; -.
GeneCards; ACSS1; -.
H-InvDB; HIX0015699; -.
HGNC; HGNC:16091; ACSS1.
HPA; HPA041014; -.
HPA; HPA043228; -.
MIM; 614355; gene.
neXtProt; NX_Q9NUB1; -.
OpenTargets; ENSG00000154930; -.
PharmGKB; PA24430; -.
eggNOG; KOG1175; Eukaryota.
eggNOG; COG0365; LUCA.
GeneTree; ENSGT00760000119178; -.
HOVERGEN; HBG014401; -.
InParanoid; Q9NUB1; -.
KO; K01895; -.
OMA; VNCLDQH; -.
OrthoDB; EOG091G039C; -.
PhylomeDB; Q9NUB1; -.
TreeFam; TF354241; -.
BRENDA; 6.2.1.1; 2681.
Reactome; R-HSA-71384; Ethanol oxidation.
ChiTaRS; ACSS1; human.
EvolutionaryTrace; Q9NUB1; -.
GenomeRNAi; 84532; -.
PRO; PR:Q9NUB1; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000154930; -.
CleanEx; HS_ACSS1; -.
ExpressionAtlas; Q9NUB1; baseline and differential.
Genevisible; Q9NUB1; HS.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0003987; F:acetate-CoA ligase activity; IDA:UniProtKB.
GO; GO:0016208; F:AMP binding; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019413; P:acetate biosynthetic process; IEA:Ensembl.
GO; GO:0006085; P:acetyl-CoA biosynthetic process; IDA:UniProtKB.
GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
GO; GO:0006069; P:ethanol oxidation; TAS:Reactome.
GO; GO:0019542; P:propionate biosynthetic process; IEA:Ensembl.
CDD; cd05966; ACS; 1.
InterPro; IPR011904; Ac_CoA_lig.
InterPro; IPR032387; ACAS_N.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
Pfam; PF16177; ACAS_N; 1.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Direct protein sequencing; Ligase; Mitochondrion;
Nucleotide-binding; Polymorphism; Reference proteome; Transit peptide.
TRANSIT 1 37 Mitochondrion.
{ECO:0000269|PubMed:16788062}.
CHAIN 38 689 Acetyl-coenzyme A synthetase 2-like,
mitochondrial.
/FTId=PRO_0000000596.
NP_BIND 417 419 ATP. {ECO:0000250}.
NP_BIND 441 446 ATP. {ECO:0000250}.
REGION 224 227 Coenzyme A binding. {ECO:0000250}.
COMPBIAS 45 53 Poly-Ala.
BINDING 341 341 Coenzyme A. {ECO:0000250}.
BINDING 533 533 ATP. {ECO:0000250}.
BINDING 548 548 ATP. {ECO:0000250}.
BINDING 556 556 Coenzyme A; via carbonyl oxygen.
{ECO:0000250}.
BINDING 559 559 ATP. {ECO:0000250}.
MOD_RES 396 396 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 642 642 N6-acetyllysine.
{ECO:0000269|PubMed:16788062}.
VAR_SEQ 1 22 MAARTLGRGVGRLLGSLRGLSG -> MRRRKERQPWDRFHF
LHFAPHG (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044693.
VAR_SEQ 23 143 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044694.
VAR_SEQ 446 447 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_007249.
VAR_SEQ 556 575 SGHRLGTAEIEDAIADHPAV -> LQIVGFFREAIRNSGDL
LEH (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045546.
VAR_SEQ 576 689 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045547.
VARIANT 488 488 V -> M (in dbSNP:rs6050249).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_048184.
MUTAGEN 642 642 K->Q: Loss of activity.
{ECO:0000269|PubMed:16788062}.
CONFLICT 233 233 K -> I (in Ref. 1; BAG54524).
{ECO:0000305}.
CONFLICT 277 277 V -> M (in Ref. 4; AAH39261).
{ECO:0000305}.
SEQUENCE 689 AA; 74857 MW; 66E84E39302AD08B CRC64;
MAARTLGRGV GRLLGSLRGL SGQPARPPCG VSAPRRAASG PSGSAPAVAA AAAQPGSYPA
LSAQAAREPA AFWGPLARDT LVWDTPYHTV WDCDFSTGKI GWFLGGQLNV SVNCLDQHVR
KSPESVALIW ERDEPGTEVR ITYRELLETT CRLANTLKRH GVHRGDRVAI YMPVSPLAVA
AMLACARIGA VHTVIFAGFS AESLAGRIND AKCKVVITFN QGLRGGRVVE LKKIVDEAVK
HCPTVQHVLV AHRTDNKVHM GDLDVPLEQE MAKEDPVCAP ESMGSEDMLF MLYTSGSTGM
PKGIVHTQAG YLLYAALTHK LVFDHQPGDI FGCVADIGWI TGHSYVVYGP LCNGATSVLF
ESTPVYPNAG RYWETVERLK INQFYGAPTA VRLLLKYGDA WVKKYDRSSL RTLGSVGEPI
NCEAWEWLHR VVGDSRCTLV DTWWQTETGG ICIAPRPSEE GAEILPAMAM RPFFGIVPVL
MDEKGSVVEG SNVSGALCIS QAWPGMARTI YGDHQRFVDA YFKAYPGYYF TGDGAYRTEG
GYYQITGRMD DVINISGHRL GTAEIEDAIA DHPAVPESAV IGYPHDIKGE AAFAFIVVKD
SAGDSDVVVQ ELKSMVATKI AKYAVPDEIL VVKRLPKTRS GKVMRRLLRK IITSEAQELG
DTTTLEDPSI IAEILSVYQK CKDKQAAAK


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E6964h Human Acyl CoA Synthetase Short Chain Family, Memb 96T
CSB-EL001204MO Mouse acyl-CoA synthetase short-chain family member 3 (ACSS3) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL001204BO Bovine acyl-CoA synthetase short-chain family member 3 (ACSS3) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL001203HU Human acyl-CoA synthetase short-chain family member 2 (ACSS2) ELISA kit, Species Human, Sample Type serum, plasma 96T


 

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