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O24371

- LOX31_SOLTU

UniProt

O24371 - LOX31_SOLTU

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Protein

Linoleate 13S-lipoxygenase 3-1, chloroplastic

Gene

LOX3.1

Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Required for the regulation of wound-induced gene expression, but is not involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids.2 Publications

Catalytic activityi

Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate.1 Publication
Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate.1 Publication

Cofactori

Binds 1 iron ion per subunit.PROSITE-ProRule annotation

pH dependencei

Optimum pH is 6.0.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi574 – 5741Iron; catalyticPROSITE-ProRule annotation
Metal bindingi579 – 5791Iron; catalyticPROSITE-ProRule annotation
Metal bindingi765 – 7651Iron; catalyticPROSITE-ProRule annotation
Metal bindingi769 – 7691Iron; catalyticPROSITE-ProRule annotation
Metal bindingi914 – 9141Iron; via carboxylate; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. linoleate 13S-lipoxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. oxylipin biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00382.

Names & Taxonomyi

Protein namesi
Recommended name:
Linoleate 13S-lipoxygenase 3-1, chloroplastic (EC:1.13.11.12)
Gene namesi
Name:LOX3.1
Synonyms:LOX-H3
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
  2. thylakoid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8383ChloroplastSequence AnalysisAdd
BLAST
Chaini84 – 914831Linoleate 13S-lipoxygenase 3-1, chloroplasticPRO_0000412928Add
BLAST

Expressioni

Tissue specificityi

Expressed in roots and leaves. Detected in tubers and flower buds.1 Publication

Inductioni

Up-regulated localy and systemically 30 minutes after wounding. Up-regulated by jasmonate and abscisic acid treatment. Not induced by pathogen infection.3 Publications

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO24371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 218123PLATPROSITE-ProRule annotationAdd
BLAST
Domaini221 – 914694LipoxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated
Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiO24371.
KOiK00454.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_pln.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O24371-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALAKEIMGI SLLEKSSSFM NSSSMALFNP NNYHKENHLW FNQQFQGRRN
60 70 80 90 100
LSRRKAFRQS TMAAISENLI KVVPEKAVRF KVRAVVTVRN KNKEDLKETI
110 120 130 140 150
VKHLDAFTDK IGRNVTLELI STDMDPNTKG PKKSNQAVLK DWSKKSNLKT
160 170 180 190 200
ERVNYTAEFI VDSNFGNPGA ITVTNKHQQE FFLESITIEG FACGPVHFPC
210 220 230 240 250
NSWVQPKKDH PGKRIFFSNQ PYLPDETPAG LKSLRERELR DLRGDGKGVR
260 270 280 290 300
KLSDRIYDYD IYNDLGNPDK GIDFARPKLG GDDNVPYPRR CRSGRVPTDT
310 320 330 340 350
DISAESRVEK PNPTYVPRDE QFEESKMNTF STSRLKAVLH NLIPSLMASI
360 370 380 390 400
SSNNHDFKGF SDIDNLYSKG LLLKLGLQDE VLKKLPLPKV VSSIKEGDLL
410 420 430 440 450
KYDTPKILSK DKFAWLRDDE FARQAIAGVN PVSIEKLQFF PPVSKLDPEI
460 470 480 490 500
YGPQESALKE EHILGHLNGM TVQEALDANK LFIVDHHDVY LPFLDRINAL
510 520 530 540 550
DGRKAYATRT IFFLSDVGTL KPIAIELSLP QTGPSSRSKR VVTPPVCATG
560 570 580 590 600
NWTWQIAKAH VCANDAGVHQ LVNHWLRTHA SLEPFILAAH RQLSAMHPIY
610 620 630 640 650
KLLDPHMRYT LEINGLARQS LINADGVIEA CFTPGRYCME ISAAAYKNWR
660 670 680 690 700
FDLEGLPADL IRRGMAVPDS TQPHGLKLLI EDYPYAADGL MIWGAIESWV
710 720 730 740 750
RDYVNHYYPS SAQVCSDREL QAWYAETINV GHVDLRNEEW WPTLATPEDL
760 770 780 790 800
ISILTTLIWL ASAQHAALNF GQYPYGGYVP NRPPLMRRLI PDENDPEYAV
810 820 830 840 850
FLADPQKYFF SALPSLLQAT KFMAVVDTLS THSPDEEYLG ERHQPSTWTG
860 870 880 890 900
DAEIVEAFYK FSAEIGRIEK EIDERNANTK LKNRCGAGVL PYELLAPSSG
910
PGVTCRGVPN SVSI
Length:914
Mass (Da):103,089
Last modified:January 1, 1998 - v1
Checksum:i45BBC7D7180390E4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X96406 mRNA. Translation: CAA65269.1.
PIRiT07065.
RefSeqiNP_001275115.1. NM_001288186.1.
UniGeneiStu.213.

Genome annotation databases

GeneIDi102597498.
KEGGisot:102597498.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X96406 mRNA. Translation: CAA65269.1 .
PIRi T07065.
RefSeqi NP_001275115.1. NM_001288186.1.
UniGenei Stu.213.

3D structure databases

ProteinModelPortali O24371.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 102597498.
KEGGi sot:102597498.

Phylogenomic databases

InParanoidi O24371.
KOi K00454.

Enzyme and pathway databases

UniPathwayi UPA00382 .

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProi IPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_pln.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11771. PTHR11771. 1 hit.
Pfami PF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PRINTSi PR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns."
    Royo J., Vancanneyt G., Perez A.G., Sanz C., Stormann K., Rosahl S., Sanchez-Serrano J.J.
    J. Biol. Chem. 271:21012-21019(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY WOUNDING; JASMONATE AND ABSCISIC ACID, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Leaf.
  2. "Antisense-mediated depletion of a potato lipoxygenase reduces wound induction of proteinase inhibitors and increases weight gain of insect pests."
    Royo J., Leon J., Vancanneyt G., Albar J.P., Rosahl S., Ortego F., Castanera P., Sanchez-Serrano J.J.
    Proc. Natl. Acad. Sci. U.S.A. 96:1146-1151(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "A leaf lipoxygenase of potato induced specifically by pathogen infection."
    Kolomiets M.V., Chen H., Gladon R.J., Braun E.J., Hannapel D.J.
    Plant Physiol. 124:1121-1130(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY PATHOGEN.
  4. "Lipoxygenase H1 gene silencing reveals a specific role in supplying fatty acid hydroperoxides for aliphatic aldehyde production."
    Leon J., Royo J., Vancanneyt G., Sanz C., Silkowski H., Griffiths G., Sanchez-Serrano J.J.
    J. Biol. Chem. 277:416-423(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Differential distribution of the lipoxygenase pathway enzymes within potato chloroplasts."
    Farmaki T., Sanmartin M., Jimenez P., Paneque M., Sanz C., Vancanneyt G., Leon J., Sanchez-Serrano J.J.
    J. Exp. Bot. 58:555-568(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION BY WOUNDING.

Entry informationi

Entry nameiLOX31_SOLTU
AccessioniPrimary (citable) accession number: O24371
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Depletion of LOX-H3 by co-suppression-mediated gene silencing leads to higher tuber yield, but has no effect on the number of tubers per plant.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3