Full text data of ACSL1
ACSL1
(FACL1, FACL2, LACS, LACS1, LACS2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Long-chain-fatty-acid--CoA ligase 1; 6.2.1.3 (Acyl-CoA synthetase 1; ACS1; Long-chain acyl-CoA synthetase 1; LACS 1; Long-chain acyl-CoA synthetase 2; LACS 2; Long-chain fatty acid-CoA ligase 2; Palmitoyl-CoA ligase 1; Palmitoyl-CoA ligase 2)
Long-chain-fatty-acid--CoA ligase 1; 6.2.1.3 (Acyl-CoA synthetase 1; ACS1; Long-chain acyl-CoA synthetase 1; LACS 1; Long-chain acyl-CoA synthetase 2; LACS 2; Long-chain fatty acid-CoA ligase 2; Palmitoyl-CoA ligase 1; Palmitoyl-CoA ligase 2)
hRBCD
IPI00012728
IPI00012728 Splice Isoform 1 Of Long-chain-fatty-acid--CoA ligase 1 Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate, low expression in retics and young erythrocytes soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a Type III membrane protein, mitochondrion Isoform 1 or 2 expected molecular weight found in band at molecular weight
IPI00012728 Splice Isoform 1 Of Long-chain-fatty-acid--CoA ligase 1 Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate, low expression in retics and young erythrocytes soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a Type III membrane protein, mitochondrion Isoform 1 or 2 expected molecular weight found in band at molecular weight
UniProt
P33121
ID ACSL1_HUMAN Reviewed; 698 AA.
AC P33121; D3DP57; P41215; Q8N8V7; Q8TA99;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1993, sequence version 1.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 1;
DE EC=6.2.1.3;
DE AltName: Full=Acyl-CoA synthetase 1;
DE Short=ACS1;
DE AltName: Full=Long-chain acyl-CoA synthetase 1;
DE Short=LACS 1;
DE AltName: Full=Long-chain acyl-CoA synthetase 2;
DE Short=LACS 2;
DE AltName: Full=Long-chain fatty acid-CoA ligase 2;
DE AltName: Full=Palmitoyl-CoA ligase 1;
DE AltName: Full=Palmitoyl-CoA ligase 2;
GN Name=ACSL1; Synonyms=FACL1, FACL2, LACS, LACS1, LACS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=1607358;
RA Abe T., Fujino T., Fukuyama R., Minoshima S., Shimizu N., Toh H.,
RA Suzuki H., Yamamoto T.;
RT "Human long-chain acyl-CoA synthetase: structure and chromosomal
RT location.";
RL J. Biochem. 111:123-128(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8584017; DOI=10.1007/BF01076899;
RA Ghosh B., Barbosa E., Singh I.;
RT "Molecular cloning and sequencing of human palmitoyl-CoA ligase and
RT its tissue specific expression.";
RL Mol. Cell. Biochem. 151:77-81(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-8; 12-19; 341-349; 377-386; 562-572; 633-640 AND
RP 655-675, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-698 (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=10548543; DOI=10.1042/0264-6021:3440135;
RA Malhotra K.T., Malhotra K., Lubin B.H., Kuypers F.A.;
RT "Identification and molecular characterization of acyl-CoA synthetase
RT in human red cells and erythroid precursor.";
RL Biochem. J. 344:135-143(1999).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Activation of long-chain fatty acids for both synthesis
CC of cellular lipids, and degradation via beta-oxidation.
CC Preferentially uses palmitoleate, oleate and linoleate.
CC -!- CATALYTIC ACTIVITY: ATP + a long-chain fatty acid + CoA = AMP +
CC diphosphate + an acyl-CoA.
CC -!- COFACTOR: Magnesium.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC type III membrane protein (By similarity). Peroxisome membrane;
CC Single-pass type III membrane protein (By similarity). Microsome
CC membrane; Single-pass type III membrane protein (By similarity).
CC Endoplasmic reticulum membrane; Single-pass type III membrane
CC protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P33121-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33121-2; Sequence=VSP_009604;
CC Note=May be due to a competing acceptor splice site. No
CC experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, heart, skeletal
CC muscle, kidney and erythroid cells, and to a lesser extent in
CC brain, lung, placenta and pancreas.
CC -!- DEVELOPMENTAL STAGE: Expressed during the early stages of
CC erythroid development while expression is very low in
CC reticulocytes and young erythrocytes.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04704.1; Type=Erroneous initiation;
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DR EMBL; D10040; BAA00931.1; -; mRNA.
DR EMBL; L09229; AAB00959.1; -; mRNA.
DR EMBL; CH471056; EAX04662.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04663.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04665.1; -; Genomic_DNA.
DR EMBL; BC026290; AAH26290.1; -; mRNA.
DR EMBL; BC050073; AAH50073.1; -; mRNA.
DR EMBL; AK096117; BAC04704.1; ALT_INIT; mRNA.
DR PIR; JX0202; JX0202.
DR RefSeq; NP_001986.2; NM_001995.3.
DR RefSeq; XP_005262885.1; XM_005262828.1.
DR RefSeq; XP_005262886.1; XM_005262829.1.
DR RefSeq; XP_005262888.1; XM_005262831.1.
DR UniGene; Hs.406678; -.
DR ProteinModelPortal; P33121; -.
DR SMR; P33121; 81-639.
DR IntAct; P33121; 3.
DR STRING; 9606.ENSP00000281455; -.
DR DrugBank; DB00131; Adenosine monophosphate.
DR DrugBank; DB00171; Adenosine triphosphate.
DR PhosphoSite; P33121; -.
DR DMDM; 417241; -.
DR PaxDb; P33121; -.
DR PRIDE; P33121; -.
DR Ensembl; ENST00000281455; ENSP00000281455; ENSG00000151726.
DR Ensembl; ENST00000504342; ENSP00000425006; ENSG00000151726.
DR Ensembl; ENST00000515030; ENSP00000422607; ENSG00000151726.
DR GeneID; 2180; -.
DR KEGG; hsa:2180; -.
DR UCSC; uc003iwt.1; human.
DR CTD; 2180; -.
DR GeneCards; GC04M185676; -.
DR HGNC; HGNC:3569; ACSL1.
DR HPA; HPA011316; -.
DR HPA; HPA011964; -.
DR MIM; 152425; gene.
DR neXtProt; NX_P33121; -.
DR PharmGKB; PA27966; -.
DR eggNOG; COG1022; -.
DR HOGENOM; HOG000159459; -.
DR HOVERGEN; HBG050452; -.
DR InParanoid; P33121; -.
DR KO; K01897; -.
DR OMA; AKCPIVE; -.
DR OrthoDB; EOG71CFKN; -.
DR PhylomeDB; P33121; -.
DR BioCyc; MetaCyc:HS07766-MONOMER; -.
DR BRENDA; 6.2.1.3; 2681.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; ACSL1; human.
DR GeneWiki; ACSL1; -.
DR GenomeRNAi; 2180; -.
DR NextBio; 8801; -.
DR PRO; PR:P33121; -.
DR ArrayExpress; P33121; -.
DR Bgee; P33121; -.
DR CleanEx; HS_ACSL1; -.
DR Genevestigator; P33121; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0033211; P:adiponectin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
DR GO; GO:0043651; P:linoleic acid metabolic process; TAS:Reactome.
DR GO; GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0034201; P:response to oleic acid; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
DR GO; GO:0042178; P:xenobiotic catabolic process; IEA:Ensembl.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW Microsome; Mitochondrion; Mitochondrion outer membrane; Nitration;
KW Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1 698 Long-chain-fatty-acid--CoA ligase 1.
FT /FTId=PRO_0000193104.
FT TRANSMEM 25 45 Helical; Signal-anchor for type III
FT membrane protein; (Potential).
FT TOPO_DOM 46 698 Cytoplasmic (Potential).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 9 9 Nitrated tyrosine (By similarity).
FT MOD_RES 84 84 Phosphotyrosine (By similarity).
FT MOD_RES 207 207 N6-acetyllysine (By similarity).
FT MOD_RES 356 356 N6-acetyllysine (By similarity).
FT MOD_RES 386 386 N6-acetyllysine (By similarity).
FT MOD_RES 620 620 Phosphoserine (By similarity).
FT MOD_RES 632 632 N6-acetyllysine (By similarity).
FT VAR_SEQ 508 517 Missing (in isoform 2).
FT /FTId=VSP_009604.
FT CONFLICT 21 23 YVR -> CV (in Ref. 2; AAB00959).
FT CONFLICT 37 38 AA -> SRR (in Ref. 2; AAB00959).
FT CONFLICT 44 47 YATR -> RPRH (in Ref. 2; AAB00959).
FT CONFLICT 55 56 CD -> WH (in Ref. 2; AAB00959).
FT CONFLICT 229 229 A -> S (in Ref. 2; AAB00959).
FT CONFLICT 385 385 L -> V (in Ref. 2; AAB00959).
FT CONFLICT 400 401 EL -> DV (in Ref. 2; AAB00959).
FT CONFLICT 477 477 A -> T (in Ref. 2; AAB00959).
FT CONFLICT 492 494 VDV -> GWQL (in Ref. 2; AAB00959).
FT CONFLICT 502 502 A -> S (in Ref. 2; AAB00959).
FT CONFLICT 695 695 T -> I (in Ref. 2; AAB00959).
SQ SEQUENCE 698 AA; 77943 MW; FD6669453589D362 CRC64;
MQAHELFRYF RMPELVDFRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKP LKPPCDLSMQ
SVEVAGSGGA RRSALLDSDE PLVYFYDDVT TLYEGFQRGI QVSNNGPCLG SRKPDQPYEW
LSYKQVAELS ECIGSALIQK GFKTAPDQFI GIFAQNRPEW VIIEQGCFAY SMVIVPLYDT
LGNEAITYIV NKAELSLVFV DKPEKAKLLL EGVENKLIPG LKIIVVMDAY GSELVERGQR
CGVEVTSMKA MEDLGRANRR KPKPPAPEDL AVICFTSGTT GNPKGAMVTH RNIVSDCSAF
VKATENTVNP CPDDTLISFL PLAHMFERVV ECVMLCHGAK IGFFQGDIRL LMDDLKVLQP
TVFPVVPRLL NRMFDRIFGQ ANTTLKRWLL DFASKRKEAE LRSGIIRNNS LWDRLIFHKV
QSSLGGRVRL MVTGAAPVSA TVLTFLRAAL GCQFYEGYGQ TECTAGCCLT MPGDWTAGHV
GAPMPCNLIK LVDVEEMNYM AAEGEGEVCV KGPNVFQGYL KDPAKTAEAL DKDGWLHTGD
IGKWLPNGTL KIIDRKKHIF KLAQGEYIAP EKIENIYMRS EPVAQVFVHG ESLQAFLIAI
VVPDVETLCS WAQKRGFEGS FEELCRNKDV KKAILEDMVR LGKDSGLKPF EQVKGITLHP
ELFSIDNGLL TPTMKAKRPE LRNYFRSQID DLYSTIKV
//
ID ACSL1_HUMAN Reviewed; 698 AA.
AC P33121; D3DP57; P41215; Q8N8V7; Q8TA99;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1993, sequence version 1.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 1;
DE EC=6.2.1.3;
DE AltName: Full=Acyl-CoA synthetase 1;
DE Short=ACS1;
DE AltName: Full=Long-chain acyl-CoA synthetase 1;
DE Short=LACS 1;
DE AltName: Full=Long-chain acyl-CoA synthetase 2;
DE Short=LACS 2;
DE AltName: Full=Long-chain fatty acid-CoA ligase 2;
DE AltName: Full=Palmitoyl-CoA ligase 1;
DE AltName: Full=Palmitoyl-CoA ligase 2;
GN Name=ACSL1; Synonyms=FACL1, FACL2, LACS, LACS1, LACS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=1607358;
RA Abe T., Fujino T., Fukuyama R., Minoshima S., Shimizu N., Toh H.,
RA Suzuki H., Yamamoto T.;
RT "Human long-chain acyl-CoA synthetase: structure and chromosomal
RT location.";
RL J. Biochem. 111:123-128(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8584017; DOI=10.1007/BF01076899;
RA Ghosh B., Barbosa E., Singh I.;
RT "Molecular cloning and sequencing of human palmitoyl-CoA ligase and
RT its tissue specific expression.";
RL Mol. Cell. Biochem. 151:77-81(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-8; 12-19; 341-349; 377-386; 562-572; 633-640 AND
RP 655-675, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-698 (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=10548543; DOI=10.1042/0264-6021:3440135;
RA Malhotra K.T., Malhotra K., Lubin B.H., Kuypers F.A.;
RT "Identification and molecular characterization of acyl-CoA synthetase
RT in human red cells and erythroid precursor.";
RL Biochem. J. 344:135-143(1999).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Activation of long-chain fatty acids for both synthesis
CC of cellular lipids, and degradation via beta-oxidation.
CC Preferentially uses palmitoleate, oleate and linoleate.
CC -!- CATALYTIC ACTIVITY: ATP + a long-chain fatty acid + CoA = AMP +
CC diphosphate + an acyl-CoA.
CC -!- COFACTOR: Magnesium.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC type III membrane protein (By similarity). Peroxisome membrane;
CC Single-pass type III membrane protein (By similarity). Microsome
CC membrane; Single-pass type III membrane protein (By similarity).
CC Endoplasmic reticulum membrane; Single-pass type III membrane
CC protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P33121-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33121-2; Sequence=VSP_009604;
CC Note=May be due to a competing acceptor splice site. No
CC experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, heart, skeletal
CC muscle, kidney and erythroid cells, and to a lesser extent in
CC brain, lung, placenta and pancreas.
CC -!- DEVELOPMENTAL STAGE: Expressed during the early stages of
CC erythroid development while expression is very low in
CC reticulocytes and young erythrocytes.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04704.1; Type=Erroneous initiation;
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DR EMBL; D10040; BAA00931.1; -; mRNA.
DR EMBL; L09229; AAB00959.1; -; mRNA.
DR EMBL; CH471056; EAX04662.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04663.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04665.1; -; Genomic_DNA.
DR EMBL; BC026290; AAH26290.1; -; mRNA.
DR EMBL; BC050073; AAH50073.1; -; mRNA.
DR EMBL; AK096117; BAC04704.1; ALT_INIT; mRNA.
DR PIR; JX0202; JX0202.
DR RefSeq; NP_001986.2; NM_001995.3.
DR RefSeq; XP_005262885.1; XM_005262828.1.
DR RefSeq; XP_005262886.1; XM_005262829.1.
DR RefSeq; XP_005262888.1; XM_005262831.1.
DR UniGene; Hs.406678; -.
DR ProteinModelPortal; P33121; -.
DR SMR; P33121; 81-639.
DR IntAct; P33121; 3.
DR STRING; 9606.ENSP00000281455; -.
DR DrugBank; DB00131; Adenosine monophosphate.
DR DrugBank; DB00171; Adenosine triphosphate.
DR PhosphoSite; P33121; -.
DR DMDM; 417241; -.
DR PaxDb; P33121; -.
DR PRIDE; P33121; -.
DR Ensembl; ENST00000281455; ENSP00000281455; ENSG00000151726.
DR Ensembl; ENST00000504342; ENSP00000425006; ENSG00000151726.
DR Ensembl; ENST00000515030; ENSP00000422607; ENSG00000151726.
DR GeneID; 2180; -.
DR KEGG; hsa:2180; -.
DR UCSC; uc003iwt.1; human.
DR CTD; 2180; -.
DR GeneCards; GC04M185676; -.
DR HGNC; HGNC:3569; ACSL1.
DR HPA; HPA011316; -.
DR HPA; HPA011964; -.
DR MIM; 152425; gene.
DR neXtProt; NX_P33121; -.
DR PharmGKB; PA27966; -.
DR eggNOG; COG1022; -.
DR HOGENOM; HOG000159459; -.
DR HOVERGEN; HBG050452; -.
DR InParanoid; P33121; -.
DR KO; K01897; -.
DR OMA; AKCPIVE; -.
DR OrthoDB; EOG71CFKN; -.
DR PhylomeDB; P33121; -.
DR BioCyc; MetaCyc:HS07766-MONOMER; -.
DR BRENDA; 6.2.1.3; 2681.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; ACSL1; human.
DR GeneWiki; ACSL1; -.
DR GenomeRNAi; 2180; -.
DR NextBio; 8801; -.
DR PRO; PR:P33121; -.
DR ArrayExpress; P33121; -.
DR Bgee; P33121; -.
DR CleanEx; HS_ACSL1; -.
DR Genevestigator; P33121; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0033211; P:adiponectin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
DR GO; GO:0043651; P:linoleic acid metabolic process; TAS:Reactome.
DR GO; GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0034201; P:response to oleic acid; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
DR GO; GO:0042178; P:xenobiotic catabolic process; IEA:Ensembl.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW Microsome; Mitochondrion; Mitochondrion outer membrane; Nitration;
KW Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1 698 Long-chain-fatty-acid--CoA ligase 1.
FT /FTId=PRO_0000193104.
FT TRANSMEM 25 45 Helical; Signal-anchor for type III
FT membrane protein; (Potential).
FT TOPO_DOM 46 698 Cytoplasmic (Potential).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 9 9 Nitrated tyrosine (By similarity).
FT MOD_RES 84 84 Phosphotyrosine (By similarity).
FT MOD_RES 207 207 N6-acetyllysine (By similarity).
FT MOD_RES 356 356 N6-acetyllysine (By similarity).
FT MOD_RES 386 386 N6-acetyllysine (By similarity).
FT MOD_RES 620 620 Phosphoserine (By similarity).
FT MOD_RES 632 632 N6-acetyllysine (By similarity).
FT VAR_SEQ 508 517 Missing (in isoform 2).
FT /FTId=VSP_009604.
FT CONFLICT 21 23 YVR -> CV (in Ref. 2; AAB00959).
FT CONFLICT 37 38 AA -> SRR (in Ref. 2; AAB00959).
FT CONFLICT 44 47 YATR -> RPRH (in Ref. 2; AAB00959).
FT CONFLICT 55 56 CD -> WH (in Ref. 2; AAB00959).
FT CONFLICT 229 229 A -> S (in Ref. 2; AAB00959).
FT CONFLICT 385 385 L -> V (in Ref. 2; AAB00959).
FT CONFLICT 400 401 EL -> DV (in Ref. 2; AAB00959).
FT CONFLICT 477 477 A -> T (in Ref. 2; AAB00959).
FT CONFLICT 492 494 VDV -> GWQL (in Ref. 2; AAB00959).
FT CONFLICT 502 502 A -> S (in Ref. 2; AAB00959).
FT CONFLICT 695 695 T -> I (in Ref. 2; AAB00959).
SQ SEQUENCE 698 AA; 77943 MW; FD6669453589D362 CRC64;
MQAHELFRYF RMPELVDFRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKP LKPPCDLSMQ
SVEVAGSGGA RRSALLDSDE PLVYFYDDVT TLYEGFQRGI QVSNNGPCLG SRKPDQPYEW
LSYKQVAELS ECIGSALIQK GFKTAPDQFI GIFAQNRPEW VIIEQGCFAY SMVIVPLYDT
LGNEAITYIV NKAELSLVFV DKPEKAKLLL EGVENKLIPG LKIIVVMDAY GSELVERGQR
CGVEVTSMKA MEDLGRANRR KPKPPAPEDL AVICFTSGTT GNPKGAMVTH RNIVSDCSAF
VKATENTVNP CPDDTLISFL PLAHMFERVV ECVMLCHGAK IGFFQGDIRL LMDDLKVLQP
TVFPVVPRLL NRMFDRIFGQ ANTTLKRWLL DFASKRKEAE LRSGIIRNNS LWDRLIFHKV
QSSLGGRVRL MVTGAAPVSA TVLTFLRAAL GCQFYEGYGQ TECTAGCCLT MPGDWTAGHV
GAPMPCNLIK LVDVEEMNYM AAEGEGEVCV KGPNVFQGYL KDPAKTAEAL DKDGWLHTGD
IGKWLPNGTL KIIDRKKHIF KLAQGEYIAP EKIENIYMRS EPVAQVFVHG ESLQAFLIAI
VVPDVETLCS WAQKRGFEGS FEELCRNKDV KKAILEDMVR LGKDSGLKPF EQVKGITLHP
ELFSIDNGLL TPTMKAKRPE LRNYFRSQID DLYSTIKV
//
MIM
152425
*RECORD*
*FIELD* NO
152425
*FIELD* TI
*152425 ACYL-CoA SYNTHETASE LONG CHAIN FAMILY, MEMBER 1; ACSL1
;;FATTY ACID CoA LIGASE, LONG CHAIN 2; FACL2;;
read moreLONG CHAIN ACYL-CoA SYNTHETASE 2; LACS2;;
PALMITOYL-CoA LIGASE 2;;
FATTY ACID CoA LIGASE, LONG CHAIN 1; FACL1;;
LONG CHAIN ACYL-CoA SYNTHETASE; LACS;;
ACYL-CoA SYNTHETASE 1; ACS1;;
PALMITOYL-CoA LIGASE 1
*FIELD* TX
DESCRIPTION
Activation of long chain fatty acids by long chain acyl-coenzyme A (CoA)
synthetase (LACS, or ACSL1; EC 6.2.1.3) is the first reaction in their
metabolism. Thus, LACS, which is also known as palmitoyl-CoA ligase,
plays a key role in both the synthesis of cellular lipids and the
degradation of fatty acids (summary by Suzuki et al., 1990).
CLONING
Suzuki et al. (1990) isolated and sequenced a cDNA for rat LACS.
Minoshima et al. (1991) isolated a human cDNA for LACS from a human
liver cDNA library using the rat cDNA as a probe.
By searching databases for sequences containing acyl-CoA synthetase
motifs 1 and 2, Watkins et al. (2007) identified human ACSL1. The
deduced 698-amino acid protein contains all 5 motifs characteristic of
acyl-CoA synthetases. Phylogenetic analysis revealed that ACSL1 belongs
to a family of long chain acyl-CoA synthetases.
GENE STRUCTURE
Watkins et al. (2007) determined that the ACSL1 gene contains 21 exons.
MAPPING
Using flow-sorted human chromosomes, Minoshima et al. (1991)
demonstrated that the FACL2 gene is located on human chromosome 4.
However, using in situ hybridization, Stanczak et al. (1992) mapped the
gene, which they called FACL1, to chromosome 3q13. Cantu et al. (1995)
confirmed that the FACL2 gene maps to chromosome 4q34-q35 by
fluorescence in situ hybridization. Watkins et al. (2007) mapped the
ACSL1 gene to the minus strand of chromosome 4q34-q35 by genomic
sequence analysis.
*FIELD* RF
1. Cantu, E. S.; Sprinkle, T. J.; Ghosh, B.; Singh, I.: The human
palmitoyl-CoA ligase (FACL2) gene maps to the chromosome 4q34-q35
region by fluorescence in situ hybridization (FISH) and somatic cell
hybrid panels. Genomics 28: 600-602, 1995.
2. Minoshima, S.; Fukuyama, R.; Yamamoto, T.; Shimizu, N.: Mapping
of human long-chain acyl-CoA synthetase to chromosome 4. (Abstract) Cytogenet.
Cell Genet. 58: 1888 only, 1991.
3. Stanczak, H.; Stanczak, J. J.; Singh, I.: Chromosomal localization
of the human gene for palmitoyl-CoA ligase (FACL1). Cytogenet. Cell
Genet. 59: 17-19, 1992.
4. Suzuki, H.; Kawarabayasi, Y.; Kondo, J.; Abe, T.; Nishikawa, K.;
Kimura, S.; Hashimoto, T.; Yamamoto, T.: Structure and regulation
of rat long-chain acyl-CoA synthetase. J. Biol. Chem. 265: 8681-8685,
1990.
5. Watkins, P. A.; Maiguel, D.; Jia, Z.; Pevsner, J.: Evidence for
26 distinct acyl-coenzyme A synthetase genes in the human genome. J.
Lipid Res. 48: 2736-2750, 2007.
*FIELD* CN
Patricia A. Hartz - updated: 10/4/2011
*FIELD* CD
Victor A. McKusick: 8/6/1991
*FIELD* ED
mgross: 12/02/2011
mgross: 12/2/2011
mgross: 11/30/2011
terry: 10/4/2011
terry: 9/19/2008
mgross: 1/6/2004
mgross: 2/22/2001
terry: 4/25/2000
alopez: 10/1/1998
dkim: 7/24/1998
alopez: 2/20/1998
carol: 1/20/1995
terry: 5/11/1994
carol: 5/18/1992
supermim: 3/16/1992
carol: 2/22/1992
carol: 2/14/1992
*RECORD*
*FIELD* NO
152425
*FIELD* TI
*152425 ACYL-CoA SYNTHETASE LONG CHAIN FAMILY, MEMBER 1; ACSL1
;;FATTY ACID CoA LIGASE, LONG CHAIN 2; FACL2;;
read moreLONG CHAIN ACYL-CoA SYNTHETASE 2; LACS2;;
PALMITOYL-CoA LIGASE 2;;
FATTY ACID CoA LIGASE, LONG CHAIN 1; FACL1;;
LONG CHAIN ACYL-CoA SYNTHETASE; LACS;;
ACYL-CoA SYNTHETASE 1; ACS1;;
PALMITOYL-CoA LIGASE 1
*FIELD* TX
DESCRIPTION
Activation of long chain fatty acids by long chain acyl-coenzyme A (CoA)
synthetase (LACS, or ACSL1; EC 6.2.1.3) is the first reaction in their
metabolism. Thus, LACS, which is also known as palmitoyl-CoA ligase,
plays a key role in both the synthesis of cellular lipids and the
degradation of fatty acids (summary by Suzuki et al., 1990).
CLONING
Suzuki et al. (1990) isolated and sequenced a cDNA for rat LACS.
Minoshima et al. (1991) isolated a human cDNA for LACS from a human
liver cDNA library using the rat cDNA as a probe.
By searching databases for sequences containing acyl-CoA synthetase
motifs 1 and 2, Watkins et al. (2007) identified human ACSL1. The
deduced 698-amino acid protein contains all 5 motifs characteristic of
acyl-CoA synthetases. Phylogenetic analysis revealed that ACSL1 belongs
to a family of long chain acyl-CoA synthetases.
GENE STRUCTURE
Watkins et al. (2007) determined that the ACSL1 gene contains 21 exons.
MAPPING
Using flow-sorted human chromosomes, Minoshima et al. (1991)
demonstrated that the FACL2 gene is located on human chromosome 4.
However, using in situ hybridization, Stanczak et al. (1992) mapped the
gene, which they called FACL1, to chromosome 3q13. Cantu et al. (1995)
confirmed that the FACL2 gene maps to chromosome 4q34-q35 by
fluorescence in situ hybridization. Watkins et al. (2007) mapped the
ACSL1 gene to the minus strand of chromosome 4q34-q35 by genomic
sequence analysis.
*FIELD* RF
1. Cantu, E. S.; Sprinkle, T. J.; Ghosh, B.; Singh, I.: The human
palmitoyl-CoA ligase (FACL2) gene maps to the chromosome 4q34-q35
region by fluorescence in situ hybridization (FISH) and somatic cell
hybrid panels. Genomics 28: 600-602, 1995.
2. Minoshima, S.; Fukuyama, R.; Yamamoto, T.; Shimizu, N.: Mapping
of human long-chain acyl-CoA synthetase to chromosome 4. (Abstract) Cytogenet.
Cell Genet. 58: 1888 only, 1991.
3. Stanczak, H.; Stanczak, J. J.; Singh, I.: Chromosomal localization
of the human gene for palmitoyl-CoA ligase (FACL1). Cytogenet. Cell
Genet. 59: 17-19, 1992.
4. Suzuki, H.; Kawarabayasi, Y.; Kondo, J.; Abe, T.; Nishikawa, K.;
Kimura, S.; Hashimoto, T.; Yamamoto, T.: Structure and regulation
of rat long-chain acyl-CoA synthetase. J. Biol. Chem. 265: 8681-8685,
1990.
5. Watkins, P. A.; Maiguel, D.; Jia, Z.; Pevsner, J.: Evidence for
26 distinct acyl-coenzyme A synthetase genes in the human genome. J.
Lipid Res. 48: 2736-2750, 2007.
*FIELD* CN
Patricia A. Hartz - updated: 10/4/2011
*FIELD* CD
Victor A. McKusick: 8/6/1991
*FIELD* ED
mgross: 12/02/2011
mgross: 12/2/2011
mgross: 11/30/2011
terry: 10/4/2011
terry: 9/19/2008
mgross: 1/6/2004
mgross: 2/22/2001
terry: 4/25/2000
alopez: 10/1/1998
dkim: 7/24/1998
alopez: 2/20/1998
carol: 1/20/1995
terry: 5/11/1994
carol: 5/18/1992
supermim: 3/16/1992
carol: 2/22/1992
carol: 2/14/1992