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Q71SP7

- FAS_BOVIN

UniProt

Q71SP7 - FAS_BOVIN

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Protein

Fatty acid synthase

Gene

FASN

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.

Catalytic activityi

Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+.
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.
An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.
Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611For beta-ketoacyl synthase activityPROSITE-ProRule annotation
Active sitei581 – 5811For malonyltransferase activityPROSITE-ProRule annotation
Active sitei878 – 8781For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation
Active sitei2310 – 23101For thioesterase activityPROSITE-ProRule annotation
Active sitei2483 – 24831For thioesterase activityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1673 – 169018NADP (ER)By similarityAdd
BLAST
Nucleotide bindingi1888 – 190316NADP (KR)By similarityAdd
BLAST

GO - Molecular functioni

  1. [acyl-carrier-protein] S-acetyltransferase activity Source: UniProtKB-EC
  2. [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB-EC
  3. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
  4. 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Source: InterPro
  5. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
  6. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
  7. enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity Source: UniProtKB-EC
  8. enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Source: InterPro
  9. myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  10. oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  11. palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  12. zinc ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Lyase, Oxidoreductase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD, NADP, Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase (EC:2.3.1.85)
Including the following 7 domains:
[Acyl-carrier-protein] S-acetyltransferase (EC:2.3.1.38)
[Acyl-carrier-protein] S-malonyltransferase (EC:2.3.1.39)
3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.41)
3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.100)
3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
Enoyl-[acyl-carrier-protein] reductase (EC:1.3.1.39)
Oleoyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.14)
Gene namesi
Name:FASN
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Cytoplasm By similarity. Melanosome By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25132513Fatty acid synthasePRO_0000180274Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei70 – 701N6-acetyllysineBy similarity
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei298 – 2981N6-acetyllysineBy similarity
Modified residuei528 – 5281N6-acetyllysineBy similarity
Modified residuei673 – 6731N6-acetyllysineBy similarity
Modified residuei996 – 9961N6-acetyllysineBy similarity
Modified residuei1706 – 17061N6-(pyridoxal phosphate)lysine; alternateBy similarity
Modified residuei1706 – 17061N6-acetyllysine; alternateBy similarity
Modified residuei1773 – 17731N6-acetyllysineBy similarity
Modified residuei1849 – 18491N6-acetyllysineBy similarity
Modified residuei1997 – 19971N6-acetyllysineBy similarity
Modified residuei2158 – 21581O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei2206 – 22061PhosphothreonineBy similarity
Modified residuei2238 – 22381PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiQ71SP7.
PRIDEiQ71SP7.

Interactioni

Subunit structurei

Homodimer which is arranged in a head to tail fashion.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ71SP7.
SMRiQ71SP7. Positions 422-822, 2121-2208, 2223-2509.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2125 – 218157Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 414414Beta-ketoacyl synthaseAdd
BLAST
Regioni429 – 817389Acyl and malonyl transferasesAdd
BLAST
Regioni1637 – 1865229Enoyl reductaseAdd
BLAST
Regioni1866 – 2119254Beta-ketoacyl reductaseAdd
BLAST
Regioni2209 – 2513305ThioesteraseAdd
BLAST

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3319.
HOVERGENiHBG005640.
InParanoidiQ71SP7.
KOiK00665.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
1.10.1470.20. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.150. 1 hit.
3.40.50.1820. 2 hits.
3.40.50.720. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR023102. Fatty_acid_synthase_dom_2.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR006162. PPantetheine_attach_site.
IPR029063. SAM-dependent_MTases-like.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF53474. SSF53474. 1 hit.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q71SP7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEEVVITGMS GKLPESENLE EFWANLIGGV DMVTDDDRRW KAGLYGLPRR
60 70 80 90 100
SGKLKDLSRF DASFFGVHPK QAHNMDPQLR LLLEVTYEAI VDAGINPASI
110 120 130 140 150
RGTNTGVWVG VSGSEASEAL SRDPETLVGY SMVGCQRAML ANRLSFFFDF
160 170 180 190 200
KGPSITLDTA CSSSLLALQR AYQAIQRGEC AMAIVGGVNI RLKPNTSVQF
210 220 230 240 250
MKLGMLSPEG TCKFFDASGN GYCRAKAVMA ILLTKKSLAR RVYATILNAG
260 270 280 290 300
TNTDGCKEKG VTFPSGEAQE QLISSLYKPA GLDPETLEYV EAHGTGTKVG
310 320 330 340 350
DPQELNGIVQ ALCGTRQSPL RIGSTKSNMG HPEPASGLAA LAKVLLSLEH
360 370 380 390 400
GLWAPNLHFH NPNPKIPALQ DGRLQVVDRP LPVLGGNVGI NSFGFGGSNV
410 420 430 440 450
HVILQPNSQP LPPPAPHAAL PRLLRASGRT LEGVQGLLEL GLQHSQNLAF
460 470 480 490 500
VSMLNDIATP SPAAMPFRGY AVLGSQGGSQ KVQQVLAGKR PLWFICSGMG
510 520 530 540 550
TQWRGMGLSL MRLSRFRDSI LRSDEAVKPL GLQVSQLLLS TDEAIFDDMV
560 570 580 590 600
ISFVSLTAIQ IALIDLLTSM GLQPDGIIGH SLGEVACGYA DGCISQEEAI
610 620 630 640 650
LSAYWRGQCI KEANIPPGAM AAVGLTWEEC KQRCPPGIVP ACHNCIDTVT
660 670 680 690 700
ISGPQASMLE FVQQLKQEGV FAKEVRTGGM AFHSYFMDAI APMLLQQLKK
710 720 730 740 750
VIREPQPRSP RWLSTSIPET QWQESLARTF SAEYNVNNLV SPVLFQEALW
760 770 780 790 800
RVPEDAVVLE IAPHALLQAV LKRGLKSSCT IIPLMKKDHR DNLEFFLSNV
810 820 830 840 850
GQLYLTGIDV NPNGLFPPVE FPAPRGTPLI SPHIKWDHSQ TWDVPTAEDF
860 870 880 890 900
PSGSSSSSAT IYKIDINPES PDHYLVDHCI DGRIIFPGTG YLCLVWKTLA
910 920 930 940 950
RALDQNMEHT PVVFEDVTLH QAVILPKTGI VLLKVRLLEA SCTFEVSENG
960 970 980 990 1000
NLIASGKVYQ WEDPNPKLFD NRYGPDPATP VDPTTAIHLS RGDVYKELQL
1010 1020 1030 1040 1050
QGFNYGPYFQ GILEASSEGN TGQLLWKDNW VTFMDTMLQM SILAPSKRSL
1060 1070 1080 1090 1100
RLPTRITAIY IHPATHQQKL YTLQDKTQVA DVVINRCLDT TVAGGIYISR
1110 1120 1130 1140 1150
IHTSVAPRHQ QEQLVPILEK FCFTPHVETG CLAGNLALQE ELQLCVGLAQ
1160 1170 1180 1190 1200
ALQTRVAQQG IKMVVPGLDG AQAPQEAPQQ GLPRLLATAC QLQLNGNLQM
1210 1220 1230 1240 1250
EMGQILAQER ALLCDDPLLS GLLNSPALKA CVTLALENMT SLKMKVVLAG
1260 1270 1280 1290 1300
DGQLYSRIPT LLNTQPLLEL DYTATDRHPQ ALEAAQAKLQ QLDITQGQWD
1310 1320 1330 1340 1350
PSDPAPSNLG GANLVVCNYA LASLGDPATA VGNMVAALKE GGFLLLHTLL
1360 1370 1380 1390 1400
RGHPLGETVT FLTCPEPQQG QRHLLSQDEW ERLFAGASLH LVALKKSFYG
1410 1420 1430 1440 1450
SVLFLCRRLA PLDSPIFLPV EDTSFQWVDS LKNILADSSS RAVWLMAVGC
1460 1470 1480 1490 1500
TTSGVVGLVN CLRKEPDGHR IRCVLVSNLN STSPIPETDP KSLELQKVLQ
1510 1520 1530 1540 1550
SDLVMNVYRD GAWGAFRHFP LEQDKPEEQT EHAFINVLTR GDLSSIRWVC
1560 1570 1580 1590 1600
SPLRHSQPTA PGFQLCTIYY ASLNFKRNHA GHGQAVPRRH PRNWASRNCL
1610 1620 1630 1640 1650
LGMEFSGRDA SGKRVMGLVP AEGLATSTLV PQSFLWDVPS NWTLEEAASV
1660 1670 1680 1690 1700
PVVYSTAYYA LMVRGRMQPG ETVLIHSGSG GVGQAAIAIA LSLGCRVFPL
1710 1720 1730 1740 1750
VGSAEKRAYL QSRFPQLNET SFANSRDTSF EQHVLWHTAG KGADLVLNSL
1760 1770 1780 1790 1800
AEEKLQASVR CLAQHGRFLE IGKFDLSKNH PLGMAIFLKN VTFHGILLDS
1810 1820 1830 1840 1850
LFEENNTMWQ EVSTLLKAGI RKGVVQPLKR TVFPRTQAED AFRYMAQGKH
1860 1870 1880 1890 1900
IGKVVIQVRE EEQEAVLHGT KPTQMVALCK TFCPAHKSYI ITGGLGGFGL
1910 1920 1930 1940 1950
ELAHWLVERG AQKLVLTSRS GIRTGYQARQ VHEWRRQGVQ VLVSTSDVST
1960 1970 1980 1990 2000
LDGTRSLITE AAQLGPVGGI FNLAVVLRDA MLDNQTPEFF QDVNKPKYNG
2010 2020 2030 2040 2050
TLNLDRVTRE ACPELDYFEV FSSVSCGRGN AGQTNYGFAN STMERICEKR
2060 2070 2080 2090 2100
RHDGLPGLAV QWGAIADVGL LMELKGTKDK AIGGTLPQRI TSCMEVLDLF
2110 2120 2130 2140 2150
LNQPHPVLSS FVLAEKATSR GPSGSHQDLV KAVTHILGIR DLATVNLDSS
2160 2170 2180 2190 2200
LSDLGLDSLM GVEVRQMLER EHNLLLSMRE IRQLTIHKLQ EISAQAGTAD
2210 2220 2230 2240 2250
ELTDSTPKFG SPAQSHTQLN LSTLLVNPEG PTLTRLNSVQ SSERPLFLVH
2260 2270 2280 2290 2300
PIEGSTTVFH SLATKLSIPT YGLQCTGAAP LDSIQSLATY YIECIRQVQP
2310 2320 2330 2340 2350
EGNYRIAGYS YGACVAFEMC SQLQAQQNAG PTNNSLFLFD GSHTFVMAYT
2360 2370 2380 2390 2400
QSYRAKLNPG CEAEAEAEAM CFFMQQFTEA EHSRVLEALL PLGDLEARVA
2410 2420 2430 2440 2450
ATVELIVQSH AGLDRHALSF AARSFYHKLR AAEEYTPRAT YHGNVTLLRA
2460 2470 2480 2490 2500
KMGSAYQEGL GADYNLSQVC DGKVSVHIIE GDHRTLLEGS GLESILSIIH
2510
SSLAEPRVSV REG
Length:2,513
Mass (Da):274,554
Last modified:July 5, 2004 - v1
Checksum:iD75B09DB855DFDAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF285607 Genomic DNA. Translation: AAR19788.1.
AY343889 mRNA. Translation: AAR17600.1.
RefSeqiNP_001012687.1. NM_001012669.1.
UniGeneiBt.30099.

Genome annotation databases

GeneIDi281152.
KEGGibta:281152.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF285607 Genomic DNA. Translation: AAR19788.1 .
AY343889 mRNA. Translation: AAR17600.1 .
RefSeqi NP_001012687.1. NM_001012669.1.
UniGenei Bt.30099.

3D structure databases

ProteinModelPortali Q71SP7.
SMRi Q71SP7. Positions 422-822, 2121-2208, 2223-2509.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q71SP7.
PRIDEi Q71SP7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281152.
KEGGi bta:281152.

Organism-specific databases

CTDi 2194.

Phylogenomic databases

eggNOGi COG3319.
HOVERGENi HBG005640.
InParanoidi Q71SP7.
KOi K00665.

Miscellaneous databases

NextBioi 20805215.

Family and domain databases

Gene3Di 1.10.1200.10. 1 hit.
1.10.1470.20. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.150. 1 hit.
3.40.50.1820. 2 hits.
3.40.50.720. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR023102. Fatty_acid_synthase_dom_2.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR006162. PPantetheine_attach_site.
IPR029063. SAM-dependent_MTases-like.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view ]
SMARTi SM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
[Graphical view ]
SUPFAMi SSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF53474. SSF53474. 1 hit.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 1 hit.
PROSITEi PS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, genomic organization and expression analysis of bovine FASN gene."
    Roy R., Eggen A., Rodellar C.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

Entry informationi

Entry nameiFAS_BOVIN
AccessioniPrimary (citable) accession number: Q71SP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3