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Database: UniProt
Entry: Q0P4F7
LinkDB: Q0P4F7
Original site: Q0P4F7 
ID   ACSF2_DANRE             Reviewed;         606 AA.
AC   Q0P4F7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   15-MAR-2017, entry version 57.
DE   RecName: Full=Acyl-CoA synthetase family member 2, mitochondrial;
DE            EC=6.2.1.-;
DE   Flags: Precursor;
GN   Name=acsf2; ORFNames=zgc:152887;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acyl-CoA synthases catalyze the initial reaction in
CC       fatty acid metabolism, by forming a thioester with CoA. Has some
CC       preference toward medium-chain substrates. Plays a role in
CC       adipocyte differentiation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000305}.
DR   EMBL; BC122098; AAI22099.1; -; mRNA.
DR   UniGene; Dr.79130; -.
DR   ProteinModelPortal; Q0P4F7; -.
DR   SMR; Q0P4F7; -.
DR   STRING; 7955.ENSDARP00000081474; -.
DR   PaxDb; Q0P4F7; -.
DR   PRIDE; Q0P4F7; -.
DR   ZFIN; ZDB-GENE-060825-7; acsf2.
DR   eggNOG; KOG1177; Eukaryota.
DR   eggNOG; COG0318; LUCA.
DR   HOGENOM; HOG000229999; -.
DR   HOVERGEN; HBG103408; -.
DR   InParanoid; Q0P4F7; -.
DR   PhylomeDB; Q0P4F7; -.
DR   PRO; PR:Q0P4F7; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Fatty acid metabolism; Ligase;
KW   Lipid metabolism; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     13       Mitochondrion. {ECO:0000255}.
FT   CHAIN        14    606       Acyl-CoA synthetase family member 2,
FT                                mitochondrial.
FT                                /FTId=PRO_0000315798.
FT   NP_BIND     256    264       ATP. {ECO:0000250}.
FT   BINDING     484    484       ATP. {ECO:0000250}.
FT   BINDING     499    499       ATP. {ECO:0000250}.
FT   BINDING     590    590       ATP. {ECO:0000250}.
SQ   SEQUENCE   606 AA;  67514 MW;  D2FD627E986DF056 CRC64;
     MSSKILLTNL RTSASFCKTL KFPQRPRTPF IASQQSCAIH VDNPPSIPTL TTSYVHGLSS
     HPLQSSTVDQ CLQATVERYP DREAMVFVQD GIRKTFAEFY QDVEKAAAGL LAAGLKRGDR
     LGMWGPNIYE WVLMQFATAK AGIILVAVNP AYQLQEVEFA LRKVQCNAVV CPTKFKSQHY
     CDMLKQLCPE METASPGGIK SSRLPDLHTV IVTDSQQPGS FLLKDLMQAG SSQHYQQLQD
     LQKKLVCDDP INIQFTSGTT GKPKGATLSH HNIVNNAYFT GMRIGYNWRK NVRICLPVPL
     YHCFGSVGGG VIMALYGTTV IFPSTGYDGR ANLRAIEKEK CTFVYGTPTM YIDMLGQPDL
     AKFDLSSVRG GIAAGSPCPP EVMRKILNVM GIKEMVIGYG TTENSPVTFC GFPVDSAERK
     IVTVGCISPH TEAKVVDPTT GEIVPLGAQG ELMIRGYCVM LEYWQDEEKT RECITKDRWY
     KTGDIASLDQ FAYCKIEGRI KDLIIRGGEN IYPAEIEQFL HTHPKILEAQ VVGVKDERMG
     EEVCACIRLK EGQECTVEEI KAYCKGKIAH YKVPRYILFV QDYPLTITGK IQKHKLRERT
     EKQLGL
//
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