A5YV76 (A5YV76_PIG) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Fatty acid synthase EMBL ABR09275.1

Gene names

Name:

FASN EMBL ABR09275.1

Organism

Sus scrofa (Pig) EMBL ABR09275.1

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	2512 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Contains 1 acyl carrier domain. SAAS SAAS014031

Ontologies

Keywords
Ligand	NADP PDB 2VZ9 Nucleotide-binding PDB 2VZ9 Phosphopantetheine RuleBase RU000721
Molecular function	Transferase RuleBase RU000693
Technical term	3D-structure PDB 2VZ9 PDB 2VZ8
Gene Ontology (GO)
Biological_process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Inferred from electronic annotation. Source: InterPro 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from electronic annotation. Source: InterPro 3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: InterPro [acyl-carrier-protein] S-acetyltransferase activity Inferred from electronic annotation. Source: InterPro [acyl-carrier-protein] S-malonyltransferase activity Inferred from electronic annotation. Source: InterPro enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Inferred from electronic annotation. Source: InterPro myristoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW oleoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: InterPro palmitoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Nucleotide binding	1677 – 1680	4	NADP PDB 2VZ9
	Nucleotide binding	1723 – 1724	2	NADP PDB 2VZ9
	Nucleotide binding	1794 – 1796	3	NADP PDB 2VZ9
	Nucleotide binding	1916 – 1921	6	NADP PDB 2VZ9
Sites
	Binding site	1700	1	NADP; via amide nitrogen PDB 2VZ9
	Binding site	1704	1	NADP PDB 2VZ9
	Binding site	1769	1	NADP; via carbonyl oxygen PDB 2VZ9
	Binding site	1848	1	NADP PDB 2VZ9
	Binding site	1896	1	NADP; via amide nitrogen PDB 2VZ9
	Binding site	1945	1	NADP PDB 2VZ9
	Binding site	1971	1	NADP; via carbonyl oxygen PDB 2VZ9
	Binding site	1995	1	NADP PDB 2VZ9
	Binding site	2019	1	NADP; via carbonyl oxygen PDB 2VZ9
	Binding site	2063	1	NADP; via amide nitrogen PDB 2VZ9
	Binding site	2068	1	NADP; via amide nitrogen PDB 2VZ9

Sequences

	Sequence		Length	Mass (Da)
	A5YV76 [UniParc]. Last modified July 10, 2007. Version 1. Checksum: F57ABBAAC73E4B19	FASTA	2,512	272,250
	10 20 30 40 50 60 MEEVVIAGMS GKLPESENLE EFWANLIGGV DMVTADDRRW KAGLYGLPRR MGKLKDLSRF 70 80 90 100 110 120 DASFFGVHSK QANTMDPQLR MLLEVTYEAI VDGGINPASL RGTSTGVWVG VSSSDASEAL 130 140 150 160 170 180 SRDPETLVGY SMIGCQRAMM ANRLSFFFDF KGPSITIDTA CSSSLLALQS AYQAIRGGEC 190 200 210 220 230 240 SAAVVGGLNV LLKPNSSLQF MKLGMLSQDG TCRSFDAEGT GYCRAEAVVA VLLTKKSLAR 250 260 270 280 290 300 RVYATILNAG TNTDGSKEQG VTFPSGDVQE QLIRSLYAPA GPDPESLEYI EAHGTGTKVG 310 320 330 340 350 360 DPQELNGIVN ALCATRREPL LIGSTKSNMG HPEPASGVAA LIKVLLSLEH GVWAPNLHYH 370 380 390 400 410 420 TPNPEIPALQ DGRLQVVDRP LPIRGGNVGI NSFGFGGSNV HVILQPNSRP APPPAQHAAL 430 440 450 460 470 480 PRLLQASGRT LEAVQTLLEQ GLRHSRDLAF VGMLNEIAAV SPVAMPFRGY AVLGGEAGSQ 490 500 510 520 530 540 EVQQVPGSKR PVWFICSGMG AQWQGMGLSL MRLDRFRDSI LRSDQALKPL GLRVSDLLLS 550 560 570 580 590 600 TDEAVLDDIV SSFVSLTSIQ IALIDLLTSL GLQPDGIIGH SLGEVACGYA DGCLTQEEAV 610 620 630 640 650 660 LSSYWRGYCI KEANVLPGAM AAVGLSWEEC KQRCPPGIVP ACHNSKDTVT ISGPQAAMSE 670 680 690 700 710 720 FLQQLKREDV FVKEVRTGGI AFHSYFMESI APTLLRQLRK VILDPKPRSK RWLSTSIPEA 730 740 750 760 770 780 QWQGSLARTF SAEYSVNNLV SPVLFQEALQ HVPAHAVVVE IAPHALLQAV LKRSLESSCT 790 800 810 820 830 840 IIPLMKKDHR DNLEFFLSNV GRLHLAGVSV NPNGLFPPVE FPAPRGTPLI SPHXKWDHSQ 850 860 870 880 890 900 AWDVPSAADF PSGSSCSSVA VYKFDVSPES PDHYLVDHCI DGRVLFPGTG YLWLTWKTLA 910 920 930 940 950 960 RALSQNLEET PVVFEDVTLH QATILPKTGT VSLEVRLLEA SHAFEVSDSN GSLIASGKVY 970 980 990 1000 1010 1020 QWESPDPKLF DTRAAVDPAD STAEFRLSQG DVYKDLRLRG YDYGPFFQLV LESDLEGNRG 1030 1040 1050 1060 1070 1080 RLQWNDSWVS FLDAMLHMSI LAPGQLGLYL PTRFTSIRID PVTHRQKLYT LQDTTQAADV 1090 1100 1110 1120 1130 1140 VVDRNLNTVV AGGALFLGAH SSVAPRRPQE HLKPILEKFC FTPHVESGCL AGNTALQEEL 1150 1160 1170 1180 1190 1200 QLCRGLAQAL QTKVAQQGLK MVVPGLDGAQ APREAPQQSL PRLLAAACQL QLNGNLQLEL 1210 1220 1230 1240 1250 1260 GQVLAQERPL LCDDPLLSGL LDAPALKACV DTALENMASP KMKVVEVLAG DGQLYSRIPA 1270 1280 1290 1300 1310 1320 LLNTQPVMDL DYTATDRNPQ ALEAAQAKLE QLHVTQGQWD PANPAPGSLG KADLLVCNCA 1330 1340 1350 1360 1370 1380 LATLGDPAVA VGNMAATLKE GGFLLLHTLL AGHPLGEMVG FLTSPEQGGR HLLSQDQWES 1390 1400 1410 1420 1430 1440 LFAGASLHLV ALKRSFYGSV LFLCRQQTPQ DSPVFLSVED TSFRWVDSLK DILADASSRP 1450 1460 1470 1480 1490 1500 VWLMAVGCST SGVVGMVNCL RKEPGGHRIR CVLVSNLSST SPAPEMHPSS SELQKVLQGD 1510 1520 1530 1540 1550 1560 LVMNVYRDGA WGAFRHFPLE QDRPEKQTEH AFVNVLSRGD LSSIRWVCSP LHYALPASCQ 1570 1580 1590 1600 1610 1620 DRLCSVYYTS LNFRDVMLAT GKLSPDSIPG KWLTRDCMLG MEFSGRDASG RRVMGMVPAE 1630 1640 1650 1660 1670 1680 GLATSVLLLQ HATWEVPSTW TLEEAASVPI VYTTAYYSLV VRGRMQPGES VLIHSGSGGV 1690 1700 1710 1720 1730 1740 GQAAIAIALS RGCRVFTTVG SAEKRAYLQA RFPQLDETCF ANSRDTSFEQ HVLRHTAGKG 1750 1760 1770 1780 1790 1800 VDLVLNSLAE EKLQASVRCL AQHGRFLEIG KFDLSNNHAL GMAVFLKNVT FHGILLDSLF 1810 1820 1830 1840 1850 1860 EEGGATWQEV SELLKAGIQE GVVQPLKCTV FPRTKVEAAF RYMAQGKHIG KVVIQVREEE 1870 1880 1890 1900 1910 1920 QGPAPRGLPP IALTGLSKTF CPPHKSYVIT GGLGGFGLQL AQWLRLRGAQ KLVLTSRSGI 1930 1940 1950 1960 1970 1980 RTGYQARQVR EWRRQGVQVL VSTSNASSLD GARSLITEAT QLGPVGGVFN LAMVLRDAVL 1990 2000 2010 2020 2030 2040 ENQTPEFFQD VSKPKYSGTA NLDRVTREAC PELDYFVIFS SVSCGRGNAG QANYGFANSA 2050 2060 2070 2080 2090 2100 MERICEKRRH DGLPGLAVQW GAIGDVGVVL ETMGTNDTVI GGTLPQRIAS CLEVLDLFLS 2110 2120 2130 2140 2150 2160 QPHPVLSSFV LAEKKAAAPR DGSSQKDLVK AVAHILGIRD VASINPDSTL VDLGLDSLMG 2170 2180 2190 2200 2210 2220 VEVRQILERE HDLVLSMREV RQLSLRKLQE LSSKTSTDAD PATPTSHEDS PVRQQATLNL 2230 2240 2250 2260 2270 2280 STLLVNPEGP TLTRLNSVQS AERPLFLVHP IEGSITVFHG LAAKLSIPTY GLQCTGAAPL 2290 2300 2310 2320 2330 2340 DSIQSLASYY IECIRQVQPE GPYRIAGYSY GACVAFEMCS QLQAQQSATP GNHSLFLFDG 2350 2360 2370 2380 2390 2400 SHTFVLAYTQ SVRAKMTPGC EAEAEAKAMY FFVQQFTDME QGKVLEALIP LQGLEARVAA 2410 2420 2430 2440 2450 2460 TVDLITQSHA GLDRHALSFA ARSFYQKLRA AENYWPQATY HGNVTLLRAK TGGAYGEDLG 2470 2480 2490 2500 2510 ADYNLSQVCD GKVSVHVIEG DHRTLLEGSG LESILSIIHS CLAEPRVSVR EG

References

[1]	Gao L., Chen Z. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The crystal structure of a mammalian fatty acid synthase." Maier T., Leibundgut M., Ban N. Science 321:1315-1322(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.22 ANGSTROMS) IN COMPLEX WITH NADP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

EF589048 mRNA. Translation: ABR09275.1.

RefSeq

NP_001093400.1. NM_001099930.1.

UniGene

Ssc.18175.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VZ8	X-ray	3.22	A/B	1-2512	[»]
2VZ9	X-ray	3.30	A/B	1-2512	[»]

ProteinModelPortal

A5YV76.

SMR

A5YV76. Positions 422-822, 2121-2206, 2222-2508.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

397561.

KEGG

ssc:397561.

Organism-specific databases

CTD

2194.

Phylogenomic databases

HOVERGEN

HBG005640.

KO

K00665.

Family and domain databases

Gene3D

1.10.1200.10. 1 hit.
1.10.1470.20. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.720. 2 hits.

InterPro

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.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]

Pfam

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]

SMART

SM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
[Graphical view]

SUPFAM

SSF47336. ACP_like. 1 hit.
SSF52151. Acyl_Trfase/lysoPlipase. 1 hit.
SSF50129. GroES_like. 1 hit.
SSF55048. Malonyl_transacylase_ACP-bd. 1 hit.
SSF53901. Thiolase-like. 1 hit.

PROSITE

PS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

A5YV76.

Entry information

Entry name

A5YV76_PIG

Accession

Primary (citable) accession number: A5YV76

Entry history

Integrated into UniProtKB/TrEMBL:	July 10, 2007
Last sequence update:	July 10, 2007
Last modified:	March 6, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)