Reviewed, UniProtKB/Swiss-Prot Q96CM8 (ACSF2_HUMAN)

Names and origin

Protein names

Recommended name:
    Acyl-CoA synthetase family member 2, mitochondrial
    EC=6.2.1.-

Gene names

Name:	ACSF2
ORF Names:	UNQ493/PRO1009

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	615 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipodyte differentiation.
Subcellular location	MitochondrionPotential.
Induction	By PPARG.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Molecular function	Ligase
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 41	41	Mitochondrion Potential
	Chain	42 – 615	574	Acyl-CoA synthetase family member 2, mitochondrial		PRO_0000315793
Natural variations
	Natural variant	75	1	G → V: dbSNP rs17856448.		VAR_038304
	Natural variant	316	1	V → M: dbSNP rs3744523.		VAR_038305

Sequences

	Sequence		Length	Mass (Da)
	Q96CM8-1 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: A3356EEA7C14730B	FASTA	615	68,125
	10 20 30 40 50 60 MAVYVGMLRL GRLCAGSSGV LGARAALSRS WQEARLQGVR FLSSREVDRM VSTPIGGLSY 70 80 90 100 110 120 VQGCTKKHLN SKTVGQCLET TAQRVPEREA LVVLHEDVRL TFAQLKEEVD KAASGLLSIG 130 140 150 160 170 180 LCKGDRLGMW GPNSYAWVLM QLATAQAGII LVSVNPAYQA MELEYVLKKV GCKALVFPKQ 190 200 210 220 230 240 FKTQQYYNVL KQICPEVENA QPGALKSQRL PDLTTVISVD APLPGTLLLD EVVAAGSTRQ 250 260 270 280 290 300 HLDQLQYNQQ FLSCHDPINI QFTSGTTGSP KGATLSHYNI VNNSNILGER LKLHEKTPEQ 310 320 330 340 350 360 LRMILPNPLY HCLGSVAGTM MCLMYGATLI LASPIFNGKK ALEAISRERG TFLYGTPTMF 370 380 390 400 410 420 VDILNQPDFS SYDISTMCGG VIAGSPAPPE LIRAIINKIN MKDLVVAYGT TENSPVTFAH 430 440 450 460 470 480 FPEDTVEQKA ESVGRIMPHT EARIMNMEAG TLAKLNTPGE LCIRGYCVML GYWGEPQKTE 490 500 510 520 530 540 EAVDQDKWYW TGDVATMNEQ GFCKIVGRSK DMIIRGGENI YPAELEDFFH THPKVQEVQV 550 560 570 580 590 600 VGVKDDRMGE EICACIRLKD GEETTVEEIK AFCKGKISHF KIPKYIVFVT NYPLTISGKI 610 QKFKLREQME RHLNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Adipose tissue.
[3]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-75. Tissue: Kidney and Skin.
[5]	"Identification of novel PPARgamma target genes in primary human adipocytes." Perera R.J., Marcusson E.G., Koo S., Kang X., Kim Y., White N., Dean N.M. Gene 369:90-99(2006) [PubMed: 16380219] [Abstract] Cited for: FUNCTION, INDUCTION.
[6]	"Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome." Watkins P.A., Maiguel D., Jia Z., Pevsner J. J. Lipid Res. 48:2736-2750(2007) [PubMed: 17762044] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY358660 mRNA. Translation: AAQ89023.1. AK024573 mRNA. Translation: BAB14930.1. CH471109 Genomic DNA. Translation: EAW94612.1. BC012053 mRNA. Translation: AAH12053.1. BC014123 mRNA. Translation: AAH14123.1.
RefSeq	NP_079425.3.
UniGene	Hs.288959
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Proteomic databases
PeptideAtlas	Q96CM8.
Genome annotation databases
Ensembl	ENSG00000167107. Homo sapiens. [Contig view]
GeneID	80221.
KEGG	hsa:80221.
Organism-specific databases
HGNC	HGNC:26101. ACSF2.
MIM	610465. gene.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q96CM8.
HOVERGEN	Q96CM8.
Gene expression databases
ArrayExpress	Q96CM8.
CleanEx	HS_ACSF2.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PRINTS	PR00154. AMPBINDING.
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	70634.
SOURCE	Search...

Entry information

Entry name

ACSF2_HUMAN

Accession

Primary (citable) accession number: Q96CM8
Secondary accession number(s): Q9H7G2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	November 4, 2008
This is version 42 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)