Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Fatty acyl-CoA reductase 1 (EC 1.2.1.84)

 FACR1_MOUSE             Reviewed;         515 AA.
Q922J9; Q8BZS2; Q9CXE8; Q9D0Q1; Q9DAU2;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
05-DEC-2018, entry version 133.
RecName: Full=Fatty acyl-CoA reductase 1 {ECO:0000305|PubMed:15220348};
EC=1.2.1.84 {ECO:0000269|PubMed:15220348};
Name=Far1 {ECO:0000312|MGI:MGI:1914670};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
STRAIN=C57BL/6J; TISSUE=Cecum, Embryo, Liver, Placenta, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II; TISSUE=Mammary tumor;
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).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15220348; DOI=10.1074/jbc.M406225200;
Cheng J.B., Russell D.W.;
"Mammalian wax biosynthesis: I. Identification of two fatty acyl-
coenzyme A reductases with different substrate specificities and
tissue distributions.";
J. Biol. Chem. 279:37789-37797(2004).
[4]
FUNCTION.
PubMed=15220349; DOI=10.1074/jbc.M406226200;
Cheng J.B., Russell D.W.;
"Mammalian wax biosynthesis. II. Expression cloning of wax synthase
cDNAs encoding a member of the acyltransferase enzyme family.";
J. Biol. Chem. 279:37798-37807(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Catalyzes the reduction of saturated and unsaturated C16
or C18 fatty acyl-CoA to fatty alcohols (PubMed:15220348,
PubMed:15220349). It plays an essential role in the production of
ether lipids/plasmalogens which synthesis requires fatty alcohols
(By similarity). In parallel, it is also required for wax
monoesters production since fatty alcohols also constitute a
substrate for their synthesis (PubMed:15220349).
{ECO:0000250|UniProtKB:Q8WVX9, ECO:0000269|PubMed:15220348,
ECO:0000269|PubMed:15220349}.
-!- CATALYTIC ACTIVITY:
Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-
chain primary fatty alcohol + CoA + 2 NADP(+);
Xref=Rhea:RHEA:52716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77396,
ChEBI:CHEBI:83139; EC=1.2.1.84;
Evidence={ECO:0000269|PubMed:15220348};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.4. {ECO:0000269|PubMed:15220348};
-!- SUBUNIT: Interacts with PEX19; PEX19 mediates the targeting of
FAR1 to peroxisomes. {ECO:0000250|UniProtKB:Q8WVX9}.
-!- SUBCELLULAR LOCATION: Peroxisome membrane
{ECO:0000269|PubMed:15220348}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q8WVX9}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q922J9-1; Sequence=Displayed;
Name=2;
IsoId=Q922J9-2; Sequence=VSP_021678, VSP_021679;
Name=3;
IsoId=Q922J9-3; Sequence=VSP_021680;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q922J9-4; Sequence=VSP_021681;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in all tissues
examined. Highest expression seen in preputial gland. Expressed in
the brain where large quantities of ether lipids are synthesized.
{ECO:0000269|PubMed:15220348}.
-!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK005531; BAB24102.1; -; mRNA.
EMBL; AK011187; BAB27453.1; -; mRNA.
EMBL; AK014486; BAB29388.1; -; mRNA.
EMBL; AK033674; BAC28423.1; -; mRNA.
EMBL; AK030067; BAC26766.1; -; mRNA.
EMBL; BC007178; AAH07178.1; -; mRNA.
CCDS; CCDS40093.1; -. [Q922J9-1]
CCDS; CCDS72024.1; -. [Q922J9-3]
RefSeq; NP_001272760.1; NM_001285831.1. [Q922J9-3]
RefSeq; NP_081655.2; NM_027379.3. [Q922J9-1]
RefSeq; XP_006508190.1; XM_006508127.3.
RefSeq; XP_006508191.1; XM_006508128.3.
RefSeq; XP_006508192.1; XM_006508129.3. [Q922J9-1]
RefSeq; XP_006508193.1; XM_006508130.3. [Q922J9-1]
RefSeq; XP_006508194.1; XM_006508131.3. [Q922J9-1]
UniGene; Mm.206919; -.
UniGene; Mm.477631; -.
ProteinModelPortal; Q922J9; -.
BioGrid; 212175; 3.
IntAct; Q922J9; 1.
STRING; 10090.ENSMUSP00000033018; -.
SwissLipids; SLP:000000210; -.
iPTMnet; Q922J9; -.
PhosphoSitePlus; Q922J9; -.
SwissPalm; Q922J9; -.
EPD; Q922J9; -.
PaxDb; Q922J9; -.
PeptideAtlas; Q922J9; -.
PRIDE; Q922J9; -.
Ensembl; ENSMUST00000033018; ENSMUSP00000033018; ENSMUSG00000030759. [Q922J9-1]
Ensembl; ENSMUST00000067929; ENSMUSP00000064334; ENSMUSG00000030759. [Q922J9-3]
Ensembl; ENSMUST00000164745; ENSMUSP00000128695; ENSMUSG00000030759. [Q922J9-1]
GeneID; 67420; -.
KEGG; mmu:67420; -.
UCSC; uc009jhn.2; mouse. [Q922J9-2]
UCSC; uc009jho.2; mouse. [Q922J9-1]
UCSC; uc009jhq.2; mouse. [Q922J9-3]
CTD; 84188; -.
MGI; MGI:1914670; Far1.
eggNOG; KOG1221; Eukaryota.
eggNOG; ENOG410XS7R; LUCA.
GeneTree; ENSGT00390000006367; -.
HOGENOM; HOG000261667; -.
HOVERGEN; HBG076152; -.
InParanoid; Q922J9; -.
KO; K13356; -.
OMA; QPYTFYG; -.
OrthoDB; EOG091G062W; -.
PhylomeDB; Q922J9; -.
TreeFam; TF313011; -.
BRENDA; 1.2.1.50; 3474.
BRENDA; 1.2.1.84; 3474.
Reactome; R-MMU-8848584; Wax biosynthesis.
ChiTaRS; Far1; mouse.
PRO; PR:Q922J9; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030759; Expressed in 272 organ(s), highest expression level in cardiac ventricle.
ExpressionAtlas; Q922J9; baseline and differential.
Genevisible; Q922J9; MM.
GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:MGI.
GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; IDA:MGI.
GO; GO:0008611; P:ether lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0046474; P:glycerophospholipid biosynthetic process; ISO:MGI.
GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; ISO:MGI.
GO; GO:0010025; P:wax biosynthetic process; IDA:UniProtKB.
CDD; cd09071; FAR_C; 1.
InterPro; IPR026055; FAR.
InterPro; IPR033640; FAR_C.
InterPro; IPR013120; Male_sterile_NAD-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR11011; PTHR11011; 1.
Pfam; PF07993; NAD_binding_4; 1.
Pfam; PF03015; Sterile; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Lipid biosynthesis;
Lipid metabolism; Membrane; NADP; Oxidoreductase; Peroxisome;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 515 Fatty acyl-CoA reductase 1.
/FTId=PRO_0000261395.
TOPO_DOM 1 465 Cytoplasmic.
{ECO:0000250|UniProtKB:Q8WVX9}.
TRANSMEM 466 483 Helical. {ECO:0000255}.
TOPO_DOM 484 515 Peroxisomal.
{ECO:0000250|UniProtKB:Q8WVX9}.
REGION 451 507 Necessary and sufficient for PEX19-
mediated localization into peroxisome
membrane. {ECO:0000250|UniProtKB:Q8WVX9}.
VAR_SEQ 242 260 GWIDNFNGPSGLFIAAGKG -> VSSSKLLSSWDSEFQVRT
V (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021678.
VAR_SEQ 261 515 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021679.
VAR_SEQ 319 376 EYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKA
PAFLYDIYLRMTGRSPR -> GDYLNHSFKMNPLNQVFRHP
YVKFCSNNLMLHYWKGVKHTVPALLLDLALRLTGQKPW
(in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021680.
VAR_SEQ 515 515 Y -> RRPRI (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021681.
CONFLICT 35 35 P -> R (in Ref. 1; BAB24102).
{ECO:0000305}.
CONFLICT 364 364 Y -> H (in Ref. 1; BAB24102).
{ECO:0000305}.
SEQUENCE 515 AA; 59435 MW; 6A9E9EF9A2F835A4 CRC64;
MVSIPEYYEG KNILLTGATG FLGKVLLEKL LRSCPRVNSV YVLVRQKAGQ TPQERVEEIL
SSKLFDRLRD ENPDFREKII AINSELTQPK LALSEEDKEI IIDSTNVIFH CAATVRFNEN
LRDAVQLNVI ATRQLILLAQ QMKNLEVFMH VSTAYAYCNR KHIDEVVYPP PVDPKKLIDS
LEWMDDGLVN DITPKLIGDR PNTYIYTKAL AEYVVQQEGA KLNVAIVRPS IVGASWKEPF
PGWIDNFNGP SGLFIAAGKG ILRTMRASNN ALADLVPVDV VVNTSLAAAW YSGVNRPRNI
MVYNCTTGST NPFHWGEVEY HVISTFKRNP LEQAFRRPNV NLTSNHLLYH YWIAVSHKAP
AFLYDIYLRM TGRSPRMMKT ITRLHKAMVF LEYFTSNSWV WNTDNVNMLM NQLNPEDKKT
FNIDVRQLHW AEYIENYCMG TKKYVLNEEM SGLPAARKHL NKLRNIRYGF NTILVILIWR
IFIARSQMAR NIWYFVVSLC YKFLSYFRAS STMRY


Related products :

Catalog number Product name Quantity
EIAAB12849 3-keto acyl-CoA synthase ELOVL6,Elongation of very long chain fatty acids protein 6,ELOVL6,FACE,Fatty acid elongase 2,Fatty acyl-CoA elongase,hELO2,Homo sapiens,Human,LCE,Long-chain fatty-acyl elongas
EIAAB12846 3-keto acyl-CoA synthase Elovl6,Elongation of very long chain fatty acids protein 6,Elovl6,Face,Fatty acid elongase 2,Fatty acyl-CoA elongase,Lce,Long-chain fatty-acyl elongase,Rat,Rattus norvegicus,r
FACR1_RAT Rat ELISA Kit FOR Fatty acyl-CoA reductase 1 96T
CSB-EL008425RA Rat Fatty acyl-CoA reductase 1(FAR1) ELISA kit 96T
FARP2 FAR2 Gene fatty acyl CoA reductase 2
FARP1 FAR1 Gene fatty acyl CoA reductase 1
E0929b Chicken ELISA Kit FOR Fatty acyl-CoA reductase 1 96T
E7106h Human Fatty Acyl CoA Reductase 2 ELISA Kit 96T
FACR2_HUMAN Human ELISA Kit FOR Fatty acyl-CoA reductase 2 96T
CSB-EL008425MO Mouse Fatty acyl-CoA reductase 1(FAR1) ELISA kit 96T
CSB-EL008426MO Mouse Fatty acyl-CoA reductase 2(FAR2) ELISA kit 96T
CSB-EL008425CH Chicken Fatty acyl-CoA reductase 1(FAR1) ELISA kit 96T
CSB-EL008426BO Bovine Fatty acyl-CoA reductase 2(FAR2) ELISA kit 96T
CSB-EL008425HU Human Fatty acyl-CoA reductase 1(FAR1) ELISA kit 96T
CSB-EL008425RA Rat Fatty acyl-CoA reductase 1(FAR1) ELISA kit SpeciesRat 96T
CSB-EL008426HU Human Fatty acyl-CoA reductase 2(FAR2) ELISA kit 96T
CSB-EL008426HU Human Fatty acyl-CoA reductase 2(FAR2) ELISA kit SpeciesHuman 96T
CSB-EL008426MO Mouse Fatty acyl-CoA reductase 2(FAR2) ELISA kit SpeciesMouse 96T
CSB-EL008426BO Bovine Fatty acyl-CoA reductase 2(FAR2) ELISA kit SpeciesBovine 96T
CSB-EL008425CH Chicken Fatty acyl-CoA reductase 1(FAR1) ELISA kit SpeciesChicken 96T
CSB-EL008425HU Human Fatty acyl-CoA reductase 1(FAR1) ELISA kit SpeciesHuman 96T
CSB-EL008425MO Mouse Fatty acyl-CoA reductase 1(FAR1) ELISA kit SpeciesMouse 96T
FACR1_MOUSE ELISA Kit FOR Fatty acyl-CoA reductase 1; organism: Mouse; gene name: Far1 96T
FACR2_MOUSE ELISA Kit FOR Fatty acyl-CoA reductase 2; organism: Mouse; gene name: Far2 96T
CSB-EL008425RA Rat fatty acyl CoA reductase 1 (FAR1) ELISA kit, Species Rat, Sample Type serum, plasma 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur