Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

10 structures for P09186

Entry ID Method Resolution Chain Position Source
1HU9 X-ray 220 A A 1-857 PDB
1IK3 X-ray 200 A A 1-857 PDB
1JNQ X-ray 210 A A 1-857 PDB
1LNH X-ray 260 A A 1-857 PDB
1N8Q X-ray 210 A A 1-857 PDB
1NO3 X-ray 215 A A 1-857 PDB
1ROV X-ray 200 A A 1-857 PDB
1RRH X-ray 200 A A 1-857 PDB
1RRL X-ray 209 A A/B 1-857 PDB
AF-P09186-F1 Predicted AlphaFoldDB

7 variants for P09186

Variant ID(s) Position Change Description Diseaes Association Provenance
25 H>D strain: cv. Provar [UniProt] No
57 P>S strain: cv. Provar [UniProt] No
112 L>P strain: cv. Provar [UniProt] No
201 V>I strain: cv. Provar [UniProt] No
382 E>D strain: cv. Provar [UniProt] No
428 G>D strain: cv. Provar [UniProt] No
630 A>T strain: cv. Provar [UniProt] No

No associated diseases with P09186

1 regional properties for P09186

Type Name Position InterPro Accession
domain GPCR, rhodopsin-like, 7TM 42 - 418 IPR017452

Functions

Description
EC Number 1.13.11.58 With incorporation of two atoms of oxygen
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
linoleate 9S-lipoxygenase activity Catalysis of the reaction: linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate.
metal ion binding Binding to a metal ion.
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from one donor, and two oxygen atoms is incorporated into a donor.

3 GO annotations of biological process

Name Definition
fatty acid biosynthetic process The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
lipid oxidation The removal of one or more electrons from a lipid, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen.
oxylipin biosynthetic process The chemical reactions and pathways resulting in the formation of any oxylipin, any of a group of biologically active compounds formed by oxidative metabolism of polyunsaturated fatty acids.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P16050 ALOX15 Polyunsaturated fatty acid lipoxygenase ALOX15 Homo sapiens (Human) PR
P38419 CM-LOX1 Lipoxygenase 7, chloroplastic Oryza sativa subsp japonica (Rice) PR
Q06327 LOX1 Linoleate 9S-lipoxygenase 1 Arabidopsis thaliana (Mouse-ear cress) PR
Q9FNX8 LOX4 Lipoxygenase 4, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
Q9LUW0 LOX5 Linoleate 9S-lipoxygenase 5 Arabidopsis thaliana (Mouse-ear cress) PR
P38418 LOX2 Lipoxygenase 2, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
P38415 LOX1.1 Linoleate 9S-lipoxygenase A Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
10 20 30 40 50 60
MLGGLLHRGH KIKGTVVLMR KNVLHVNSVT SVGGIIGQGL DLVGSTLDTL TAFLGRPVSL
70 80 90 100 110 120
QLISATKADA NGKGKLGKAT FLEGIITSLP TLGAGQSAFK INFEWDDGSG ILGAFYIKNF
130 140 150 160 170 180
MQTEFFLVSL TLEDIPNHGS IHFVCNSWIY NAKLFKSDRI FFANQTYLPS ETPAPLVKYR
190 200 210 220 230 240
EEELHNLRGD GTGERKEWER VYDYDVYNDL GDPDKGENHA RPVLGGNDTF PYPRRGRTGR
250 260 270 280 290 300
KPTRKDPNSE SRSNDVYLPR DEAFGHLKSS DFLTYGLKSV SQNVLPLLQS AFDLNFTPRE
310 320 330 340 350 360
FDSFDEVHGL YSGGIKLPTD IISKISPLPV LKEIFRTDGE QALKFPPPKV IQVSKSAWMT
370 380 390 400 410 420
DEEFAREMLA GVNPNLIRCL KEFPPRSKLD SQVYGDHTSQ ITKEHLEPNL EGLTVDEAIQ
430 440 450 460 470 480
NKRLFLLGHH DPIMPYLRRI NATSTKAYAT RTILFLKNDG TLRPLAIELS LPHPQGDQSG
490 500 510 520 530 540
AFSQVFLPAD EGVESSIWLL AKAYVVVNDS CYHQLVSHWL NTHAVVEPFI IATNRHLSVV
550 560 570 580 590 600
HPIYKLLHPH YRDTMNINGL ARLSLVNDGG VIEQTFLWGR YSVEMSAVVY KDWVFTDQAL
610 620 630 640 650 660
PADLIKRGMA IEDPSCPHGI RLVIEDYPYA VDGLEIWDAI KTWVHEYVFL YYKSDDTLRE
670 680 690 700 710 720
DPELQACWKE LVEVGHGDKK NEPWWPKMQT REELVEACAI IIWTASALHA AVNFGQYPYG
730 740 750 760 770 780
GLILNRPTLS RRFMPEKGSA EYEELRKNPQ KAYLKTITPK FQTLIDLSVI EILSRHASDE
790 800 810 820 830 840
VYLGERDNPN WTSDTRALEA FKRFGNKLAQ IENKLSERNN DEKLRNRCGP VQMPYTLLLP
850
SSKEGLTFRG IPNSISI