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FACR2_MOUSE
ID   FACR2_MOUSE             Reviewed;         515 AA.
AC   Q7TNT2; B2KFC6; Q3TTT7; Q8BH72; Q8CAK7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Fatty acyl-CoA reductase 2 {ECO:0000305|PubMed:15220348};
DE            EC=1.2.1.84 {ECO:0000269|PubMed:15220348};
GN   Name=Far2 {ECO:0000312|MGI:MGI:2687035};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, Head, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15220348; DOI=10.1074/jbc.m406225200;
RA   Cheng J.B., Russell D.W.;
RT   "Mammalian wax biosynthesis: I. Identification of two fatty acyl-coenzyme A
RT   reductases with different substrate specificities and tissue
RT   distributions.";
RL   J. Biol. Chem. 279:37789-37797(2004).
CC   -!- FUNCTION: Catalyzes the reduction of saturated but not unsaturated C16
CC       or C18 fatty acyl-CoA to fatty alcohols. A lower activity can be
CC       observed with shorter fatty acyl-CoA substrates (PubMed:15220348). It
CC       may play a role in the production of ether lipids/plasmalogens and wax
CC       monoesters which synthesis requires fatty alcohols as substrates (By
CC       similarity). {ECO:0000250|UniProtKB:Q8WVX9,
CC       ECO:0000269|PubMed:15220348}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain
CC         primary fatty alcohol + CoA + 2 NADP(+); Xref=Rhea:RHEA:52716,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:77396, ChEBI:CHEBI:83139; EC=1.2.1.84;
CC         Evidence={ECO:0000269|PubMed:15220348};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52717;
CC         Evidence={ECO:0000305|PubMed:15220348};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2
CC         NADP(+); Xref=Rhea:RHEA:36315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.2.1.84;
CC         Evidence={ECO:0000269|PubMed:15220348};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316;
CC         Evidence={ECO:0000305|PubMed:15220348};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 NADPH + octadecanoyl-CoA = CoA + 2 NADP(+) +
CC         octadecan-1-ol; Xref=Rhea:RHEA:36319, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32154, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.84;
CC         Evidence={ECO:0000269|PubMed:15220348};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36320;
CC         Evidence={ECO:0000305|PubMed:15220348};
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC       {ECO:0000269|PubMed:15220348}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q96K12}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TNT2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TNT2-2; Sequence=VSP_021682;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in the meibomian glands of
CC       the eyelid and the sebaceous glands of the skin. Also expressed in the
CC       brain where large quantities of ether lipids are synthesized.
CC       {ECO:0000269|PubMed:15220348}.
CC   -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AK038584; BAC30056.1; -; mRNA.
DR   EMBL; AK043388; BAC31532.1; -; mRNA.
DR   EMBL; AK043589; BAC31590.1; -; mRNA.
DR   EMBL; AK161201; BAE36237.1; -; mRNA.
DR   EMBL; CU207318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC055759; AAH55759.1; -; mRNA.
DR   CCDS; CCDS39718.1; -. [Q7TNT2-2]
DR   CCDS; CCDS85188.1; -. [Q7TNT2-1]
DR   RefSeq; NP_001334445.1; NM_001347516.1. [Q7TNT2-1]
DR   RefSeq; NP_848912.1; NM_178797.3. [Q7TNT2-2]
DR   RefSeq; XP_006507133.1; XM_006507070.3. [Q7TNT2-1]
DR   AlphaFoldDB; Q7TNT2; -.
DR   STRING; 10090.ENSMUSP00000107234; -.
DR   SwissLipids; SLP:000000211; -.
DR   iPTMnet; Q7TNT2; -.
DR   PhosphoSitePlus; Q7TNT2; -.
DR   MaxQB; Q7TNT2; -.
DR   PaxDb; Q7TNT2; -.
DR   PeptideAtlas; Q7TNT2; -.
DR   PRIDE; Q7TNT2; -.
DR   ProteomicsDB; 267705; -. [Q7TNT2-1]
DR   ProteomicsDB; 267706; -. [Q7TNT2-2]
DR   Antibodypedia; 2982; 91 antibodies from 18 providers.
DR   Ensembl; ENSMUST00000032443; ENSMUSP00000032443; ENSMUSG00000030303. [Q7TNT2-1]
DR   Ensembl; ENSMUST00000111607; ENSMUSP00000107234; ENSMUSG00000030303. [Q7TNT2-2]
DR   GeneID; 330450; -.
DR   KEGG; mmu:330450; -.
DR   UCSC; uc009etb.1; mouse. [Q7TNT2-1]
DR   UCSC; uc009etc.1; mouse. [Q7TNT2-2]
DR   CTD; 55711; -.
DR   MGI; MGI:2687035; Far2.
DR   VEuPathDB; HostDB:ENSMUSG00000030303; -.
DR   eggNOG; KOG1221; Eukaryota.
DR   GeneTree; ENSGT00390000006367; -.
DR   HOGENOM; CLU_024661_0_0_1; -.
DR   InParanoid; Q7TNT2; -.
DR   OMA; WLEYTEN; -.
DR   OrthoDB; 815047at2759; -.
DR   PhylomeDB; Q7TNT2; -.
DR   TreeFam; TF313011; -.
DR   BRENDA; 1.2.1.84; 3474.
DR   Reactome; R-MMU-9640463; Wax biosynthesis.
DR   BioGRID-ORCS; 330450; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Far2; mouse.
DR   PRO; PR:Q7TNT2; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q7TNT2; protein.
DR   Bgee; ENSMUSG00000030303; Expressed in tail skin and 138 other tissues.
DR   Genevisible; Q7TNT2; MM.
DR   GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IDA:MGI.
DR   GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; IDA:MGI.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; ISO:MGI.
DR   GO; GO:0010025; P:wax biosynthetic process; TAS:MGI.
DR   CDD; cd09071; FAR_C; 1.
DR   InterPro; IPR026055; FAR.
DR   InterPro; IPR033640; FAR_C.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11011; PTHR11011; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF03015; Sterile; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Lipid biosynthesis; Lipid metabolism; Membrane; NADP;
KW   Oxidoreductase; Peroxisome; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..515
FT                   /note="Fatty acyl-CoA reductase 2"
FT                   /id="PRO_0000261402"
FT   TOPO_DOM        1..464
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96K12"
FT   TRANSMEM        465..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        485..515
FT                   /note="Peroxisomal"
FT                   /evidence="ECO:0000250|UniProtKB:Q96K12"
FT   VAR_SEQ         497..515
FT                   /note="VSFCYKFISYFRASSTLKV -> CPLFKL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_021682"
FT   CONFLICT        84
FT                   /note="A -> T (in Ref. 1; BAC30056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="P -> H (in Ref. 1; BAE36237)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="Q -> E (in Ref. 1; BAE36237)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   515 AA;  59167 MW;  86CBE93ECC4116C2 CRC64;
     MSMIAAFYSN KSILITGATG FLGKVLMEKL FRTSPHLKVI YILVRPKSGQ TLQERVFQIL
     NSKLFEKVKE VCPNVHEKIR PISADLNQRD FAISKEDVQE LLSCTNIIFH CAATVRFDAH
     LREAVQLNVT ATQQLLLMAS QMPKLEAFIH ISTAFSNCNL SHIDEVIYPC PVEPRKIIDS
     MEWLDDSIIE EITPKLIGDR PNTYTYTKAL GEIVVQQESG NLNVAIVRPS IVGATWQEPF
     PGWVDNLNGP SGLIIATGKG FLRSIKATPM AVADVIPVDT VVNLTIAVGW YTAVHRPKST
     LIYHSTSGNL NPCNWYKMGL QVLATIEKIP FESAFRRPNA DFTTSNFTTH YWNTVSHRVP
     AIIYDFYLRL TGRKPRMLKL MNRLLKTISM LEYFINHSWE WSTNNTEMLL SELSPEDQRV
     FNFDVRQLNW LEYIENYVLG VKKYLLKEDL AGIPKAKQHL RRLRNIHYLF NTALFLIIWR
     LLIARSQMAR NVWFFIVSFC YKFISYFRAS STLKV
 
 
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