wanglab/gogpt-training-data huggingface dataset:
Protein: Catalase-1 (EC 1.11.1.6) (Q96528)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Glycolate oxidase 2
- Superoxide dismutase 1
- Glycolate oxidase 3
- Peroxisomal
- Glycolate oxidase 1
- Peroxisomal
- Catalase-3
- Catalase-2
- Superoxide dismutase 2, chloroplastic
- Superoxide dismutase 1, chloroplastic
Sequence:
MDPYRVRPSSAHDSPFFTTNSGAPVWNNNSSLTVGTRGPILLEDYHLLEKLANFDRERIPERVVHARGASAKGFFEVTHDITQLTSADFLRGPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDLVGNNFPVFFVRDGMKFPDMVHALKPNPKSHIQENWRILDFFSHHPESLHMFSFLFDDLGIPQDYRHMEGAGVNTYMLINKAGKAHYVKFHWKPTCGIKCLSDEEAIRVGGANHSHATKDLYDSIAAGNYPQWNLFVQVMDPAHEDKFDFDPLDVTKIWPEDILPLQPVGRLVLNKNIDNFFNENEQIAFCPALVVPGIHYSDDKLLQTRIFSYADSQRHRLGPNYLQLPVNAPKCAHHNNHHDGFMNFMHRDEEVNYFPSRLDPVRHAEKYPTTPIVCSGNREKCFIGKENNFKQPGERYRSWDSDRQERFVKRFVEALSEPRVTHEIRSIWISYWSQADKSLGQKLATRLNVRPNF
Protein: Golgi pH regulator (Protein GPR89) (Q8BS95)
Organism: Mus musculus (Mouse)
Function: Voltage dependent anion channel required for acidification and functions of the Golgi apparatus that may function in counter-ion conductance (By similarity). Plays a role in lymphocyte development, probably by acting as a RABL3 effector in hematopoietic cells.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:B7ZAQ6}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Oxysterol-binding protein-related protein 8
- Oxysterol-binding protein-related protein 5
Sequence:
MSFLIDSSIMITSQILFFGFGWLFFMRQLFKDYEVRQYVVQVIFSVTFAFSCTMFELIIFEILGVLNSSSRYFHWKLNLCVILLILVFMVPFYIGYFIVSNIQLLHKQRLLFSCLLWLTFMYFFWKLGDPFPILSPKHGILSIEQLISRVGVIGVTLMALLSGFGAVNCPYTYMSYFLRNVTDTDILALERRLLQTMDMIISKKKRMAVARRTMFQRGDVQNKPSGLWGMLKSVTASAPGSENLTLIQQEVDALEELSRQLFLETADLYATKERIEYSKTFKGKYFNFLGYFFSIYCVWKIFMATINIVLDRVGKTDPVTRGIEITVNYLGIQFDVKFWSQHISFILVGIIIVTSIRGLLITLTKFFYAISSSKSSNVIVLLLAQIMGMYFVSSVLLIRMSMPPEYRTIITEVLGELQFNFYHRWFDVIFLVSALSSILFLYLAHKQAPEKHMAP
Protein: histidine kinase (EC 2.7.13.3) (Q1DF44)
Organism: Myxococcus xanthus (strain DK1622)
Interaction partners:
- Response regulator
- Response regulator
- histidine kinase
- Response regulator
- Response regulator
- RedB protein
- Response regulator
- Response regulator/chemotaxis protein CheW
- Chemotaxis protein CheY
- Response regulator
Sequence:
MSPARDEPSSPPSPPMALKERAARLFREHLSAVRVRTDRLFAGLMLGQWAVGIVIALFGPRGSGAQLQAAVLVGTLLSAFPMVMARWRPGSMPTRHVVAVCQALWSSLLIYLTDGRVETHFHIFGSLAFLALYRDPWVLLSASITTVVDHVMRGTLWSHSLYGGLPPELWRFVEHAFWVAFIDVVLVYSCRGMLRELREVAVRRAELELAREREHAKARELDRALRELSGFQEHLIRVEKLAAVGQLAASVGHELRNPLAAVRNSHAYLSRKLTRDPAGAADDPRVPQFLGLMERELNACAKIISDLLDFARERPPALQPCPLRPLVDEAIGVVPQREGVRIVNDVPESLPVPHLDKEQFRQVLVNLVQNAVEAMPVGRNGVVSVVAEGGDASPWRIRVMDDGAGIPPEVLPKIFEPLFTTKTRGTGLGLAIVANMVQRHGGTISVRSEAERGSEFLIELPAAAAAQAA
Protein: Sm-like protein LSM6A (AtLSM6A) (U6 snRNA-associated Sm-like protein LSM6A) (Q9M1Z3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of LSM protein complexes, which are involved in RNA processing. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates developmental gene expression by the decapping of specific development-related transcripts. Component of the nuclear LSM2-LSM8 complex which is involved splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6 small nuclear RNAs (snRNAs) and is essential for accurate splicing of selected development-related mRNAs through the stabilization of the spliceosomal U6 snRNA. Plays a critical role in the regulation of development-related gene expression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23221597}. Nucleus {ECO:0000269|PubMed:23221597}.
Interaction partners:
- Sm-like protein LSM3A
- Sm-like protein LSM7
- Sm-like protein LSM4
- Sm-like protein LSM2
- Sm-like protein LSM5
- Sm-like protein LSM8
- Sm-like protein LSM3B
- Sm-like protein LSM1A
- Small nuclear ribonucleoprotein E
- Sm-like protein LSM1B
Sequence:
MSGVEEKVSGTTKTPADFLKSIRGRPVVVKLNSGVDYRGTLTCLDGYMNIAMEQTEEYVNGQLKNKYGDAFIRGNNVLYISTVNMTVADGA
Protein: Large ribosomal subunit protein eL22 (60S ribosomal protein L22) (F6RKM7)
Organism: Equus caballus (Horse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL14
- 60S ribosomal protein L13
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL2
- 60S ribosomal protein L27
- 60S ribosomal protein L36
Sequence:
MAPVEQFLQERIKVNGKAGNLGGGVVTIERSKSKITVTSEVPFSKRYLKYLTKKYLKKNNLRDWLRVVANSKESYELRYFQINQDEEEEEDED
Protein: Cytoskeleton-binding toxin CbtA (Toxin CbtA) (Toxin YeeV) (P64524)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type IV toxin-antitoxin (TA) system. Acts as a dual toxin inhibitor that blocks cell division and cell elongation in genetically separable interactions with FtsZ and MreB. Interacts with cytoskeletal proteins FtsZ and MreB; inhibits FtsZ GTP-dependent polymerization and GTPase activity as well as MreB ATP-dependent polymerization. Binds to both the N- and C-terminus of FtsZ, likely blocking its polymerization and localization, leading to blockage of cell division. Overexpression results in inhibition of growth in liquid cultures and decrease in colony formation; these effects are overcome by concomitant expression of antitoxin CbeA (YeeU). In other experiments cells swell, by 6 hours are lemon-shaped and by 24 hours those that have not lysed are spherical with diminished polar regions. Toxic effects are neutralized by cognate antitoxin CbeA, although there is no direct interaction between the 2 proteins. Toxic effects are also neutralized by overexpression of noncogate antitoxins YafW and YpjF.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28931012}.
Interaction partners:
- Cytoskeleton bundling-enhancing antitoxin CbeA
- Antitoxin YafW
- Toxin GhoT
- Endoribonuclease antitoxin GhoS
- Antitoxin YfjZ
- Inner membrane protein YgfX
- Cell shape-determining protein MreB
- mRNA interferase toxin RelE
- Cell division protein FtsZ
Sequence:
MKTLPVLPGQAASSRPSPVEIWQILLSRLLDQHYGLTLNDTPFADERVIEQHIEAGISLCDAVNFLVEKYALVRTDQPGFSACTRSQLINSIDILRARRATGLMTRDNYRTVNNITLGKYPEAK
Protein: Hippocalcin-like protein 1 (Neural visinin-like protein 3) (NVL-3) (NVP-3) (Visinin-like protein 3) (VILIP-3) (P62748)
Organism: Mus musculus (Mouse)
Function: May be involved in the calcium-dependent regulation of rhodopsin phosphorylation.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P37235}; Lipid-anchor {ECO:0000250|UniProtKB:P37235}.
Interaction partners:
Sequence:
MGKQNSKLRPEVLQDLREHTEFTDHELQEWYKGFLKDCPTGHLTVDEFKKIYANFFPYGDASKFAEHVFRTFDTNSDGTIDFREFIIALSVTSRGKLEQKLKWAFSMYDLDGNGYISRSEMLEIVQAIYKMVSSVMKMPEDESTPEKRTDKIFRQMDTNNDGKLSLEEFIKGAKSDPSIVRLLQCDPSSASQF
Protein: Heat shock 70 kDa protein (HSP70) (Q5B2V1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in osmoadaptation.
Interaction partners:
- Ribosome associated DnaJ chaperone Zuotin, putative
- DnaJ domain protein Psi, putative
- 30 kDa heat shock protein
- Heat shock protein
- Heat shock protein 90
- Protein mitochondrial targeting protein
- Puatative oxidoreductase
- UBA/TS-N domain protein
- DnaJ domain protein
- Calnexin, putative
Sequence:
MAPAVGIDLGTTYSCVGVFRDDRIDIIANDQGNRTTPSFVAFTDTERLIGDAAKNQVAMNPHNTVFDAKRLIGRRFGDAEVQADMKHWPFKVVDKSGKPIIEVEFKGETKQFTPEEISSMVLTKMRETAEAFLGGTVNNAVITVPAYFNDSQRQATKDAGLIAGLNVLRIINEPTAAAIAYGLDKKVEGERNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRLVNHFVTEFKRKHKKDLSTNARALRRLRTACERAKRTLSSAAQTSIEIDSLFEGIDFYTSITRARFEELCQDLFRGTMEPVERVLRDAKIDKSSVHEIVLVGGSTRIPKIQRLVSDYFNKEANKSINPDEAVAYGAAVQAAILSGDTSSKSTNEILLLDVAPLSVGIETAGGVMTPLVKRNTTIPTKKSETFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELTGIPPAPRGVPQIEVTFDLDANGIMNVSAVEKGTGKTNKITITNDKGRLSKEDIERMLADAEKYKAEDEAEAARIQAKNGLESYAYSLKNTISEGQLQISEDDKKKVSDKIDEVISWLDNNQTAEKDEYESQQKELEGVANPIISAAYAAAGGAPGGAAPGAGAAPGGGAGFRNDGVVEENEELD
Protein: Properdin (Complement factor P) (P11680)
Organism: Mus musculus (Mouse)
Function: A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes (By similarity). Inhibits CFI-CFH mediated degradation of Inhibits CFI-CFH mediated degradation of Complement C3 beta chain (C3b) (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P27918}.
Interaction partners:
- Complement factor B
- Complement C3
- Natural cytotoxicity triggering receptor 1
- Complement factor D
- Complement C4-B
- Mannose-binding protein A
- Mannose-binding protein C
- Ficolin-1
- C4b-binding protein
- Complement C1s-1 subcomponent
Sequence:
MPAEMQAPQWLLLLLVILPATGSDPVLCFTQYEESSGRCKGLLGRDIRVEDCCLNAAYAFQEHDGGLCQACRSPQWSAWSLWGPCSVTCSEGSQLRHRRCVGRGGQCSENVAPGTLEWQLQACEDQPCCPEMGGWSEWGPWGPCSVTCSKGTQIRQRVCDNPAPKCGGHCPGEAQQSQACDTQKTCPTHGAWASWGPWSPCSGSCLGGAQEPKETRSRSCSAPAPSHQPPGKPCSGPAYEHKACSGLPPCPVAGGWGPWSPLSPCSVTCGLGQTLEQRTCDHPAPRHGGPFCAGDATRNQMCNKAVPCPVNGEWEAWGKWSDCSRLRMSINCEGTPGQQSRSRSCGGRKFNGKPCAGKLQDIRHCYNIHNCIMKGSWSQWSTWSLCTPPCSPNATRVRQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGTPRPLCEALQGQKLVVEEKRSCLHVPVCKDPEEKKP
Protein: Mitofilin (Q55BP9)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- Glutathione S-transferase domain-containing protein
- Probable mitochondrial Rho GTPase gemA
- Uncharacterized protein
- Translocase of outer mitochondrial membrane
- Uncharacterized transmembrane protein DDB_G0283573
- Translocase of outer mitochondrial membrane
- Bacterial surface antigen
- SMP-LTD domain-containing protein
Sequence:
MSFLKINKIALKSSTTILKSSSPLSGKTKFNHINSRSSSRSNENNYEKRYYSSFSMKEDPEPSKPFGFKPLIALVLVGGISAYLYKAWDNQDFMFSSKLPYQREEVEKFKKIMKEIHQDSQRENLNIEKESKESKESDQQQQHQQQQQQQHHQQEEEKEEEKVGVENTTLEDNIIESIKNHEEEMKNELVSLIESVQDKYAHSNDDEINADEREMDSETGVSISDEISKLIEEHKQNEEESLPDLLDVNYGVLSIIPEAVKSAEETVENALKKFTHSNDDDDDTTTTSIIINTSDELKNHNINIENGNEESLVDSLDVNYNVLSIIPEKVKSAEEKVENVLKKFEEQYLEKVEKLISENMKLKVDFDKLINGKDDELKRVEEEIREKYRSSLDAAIEELNKDLDEKLKDMDQFIKSKVFDNQAVLQETLEKQKSNLINIFKQQAESIKQSELEKRAITQLTQCIVDLQKLLHDKSAIDGANGKGLLVRSFKNLTDLSNYDQLIKELLSTLPEGFEKKPVIPLDTLNNQFQDIAKKLRKSQLIDPNDNSLLGKAVSELASLFIIPEKGMVQGNDYDAILARAEDHLRKNNLSSAIKEMESIQQQSSKSSTNIDNHHLSKLTSNWIKQAKERDQLENISKLLELKLELIHKQQQQIKEEQQK
Protein: Xaa-Pro dipeptidase (EC 3.4.13.9) (Imidodipeptidase) (Peptidase D) (Proline dipeptidase) (Q0WUQ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- CLP protease regulatory subunit CLPX1
- Serine protease SPPA, chloroplastic
- tRNAse Z TRZ4, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- tRNase Z TRZ3, mitochondrial
- Mitochondrial intermediate peptidase, mitochondrial
- Probable cytochrome c oxidase subunit 5C-1
Sequence:
MSSLSPPPIPMELHAGNRKKLLESIRRQLSSSNRSLDGFVLLQGGEEKNRYCTDHTELFRQESYFAYLFGVREPDFYGAIDIGSGKSILFIPRLPDDYAVWLGEIKPLSHFKETYMVDMVFYVDEIIQVFNEQFKGSGKPLLYLLHGLNTDSSNFSKPASFEGIDKFETDLTTLHPILAECRVIKSSLELQLIQFANDISSEAHIEVMRKVTPGMKEYQMESMFLHHSYMYGGCRHCSYTCICATGDNSAVLHYGHAAAPNDRTFEDGDLALLDMGAEYHFYGSDITCSFPVNGKFTSDQSLIYNAVLDAHNSVISAMKPGVNWVDMHKLAEKIILESLKKGSILTGDVDDMMVQRLGAVFMPHGLGHFMGIDTHDTGGYPKGVERPKKPGLKSLRTARDLLEGMVITVEPGCYFIKALLFPAMANATTSKFFNRETIERFRNFGGVRIESDLVVTANGCKNMTNVPRETWEIEAVMAGGPWPPTK
Protein: Major prion protein (PrP) (PrP27-30) (PrP33-35C) (CD antigen CD230) (Q95211)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P04156}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P04156}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000250|UniProtKB:P04156}.
Interaction partners:
- Neural cell adhesion molecule 1
- Tyrosine-protein kinase
- Amyloid-beta precursor protein
- Neural cell adhesion molecule 2
- Caveolin-1
- Stress-induced-phosphoprotein 1
- Endoplasmic reticulum chaperone BIP
- Alpha-synuclein
- Caveolin
- Glycogen synthase kinase-3 beta
Sequence:
MAHLGYWMLLLFVATWSDVGLCKKRPKPGGGWNTGGSRYPGQSSPGGNRYPPQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGTHNQWGKPSKPKTSMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNSFVHDCVNITVKQHTVTTTTKGENFTETDIKIMERVVEQMCITQYQQESQAAYQRAAGVLLFSSPPVILLISFLIFLIVG
Protein: Phosphotransferase (EC 2.7.1.-) (Q5B5C5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Glucose-6-phosphate isomerase
- Phosphoglucomutase
- ATP-dependent 6-phosphofructokinase
- Glycosyl hydrolases family 32 superfamily
- fructan beta-fructosidase
- Mannitol-1-phosphate 5-dehydrogenase
- Phosphoglucomutase, putative
- Phosphomannomutase
- Fructose-1,6-bisphosphatase
- Alpha-glucosidase
Sequence:
MSSPLVKVLHRMQALFSNIVAALETMLLFPSLFRDSSRGGGKSRAAFRRRRALDALADEIEIIFSKPLTLKNMLAMSEKIREQFRAGLESSPINMLPSYNHALPTGLEQGTFLALDVGGSTMRVALIELCGQGKMEVLRVSSSLIDNDVKLLEGTSFFDWMAEKIEEMLREVGTNYGREEAPLSMGLSWSFPIEQTSISSGLVIHMGKGFRCSMGTVGQELGSLIVQSCQKRGLNVRVDAIVNDSSAALLSRAYVDPTTRMSLILGTGTNVAIHFPVHAIGLGKFGKRPQGWFDYAKHVIINSEMSMFGGGVLPMTRWDDILNRTHLRPDYQPLEYMATGRYLGEIVRLIIVDAVETAQLFGGELPHSMRDAYSLDTSIVAFIEADTSPFLTASAALLQKEHTMSRPPSPEDLRFLLRVCRTISKRAAGYLATAIHSMWCLRNEAEISQGPPSPSFKGPRDVTVTESGSNSDCLSIACDGSVINKYPGFRDRCQAYLDQLTQETNTSKVSQISEEGSCIRLEPAPEGAIFGAAVAVAVAVAGKLEQTIV
Protein: Ferredoxin--NADP reductase, apicoplast (EC 1.18.1.2) (C6KT68)
Organism: Plasmodium falciparum (isolate 3D7)
Function: May play a role in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Subcellular location: Plastid, apicoplast {ECO:0000305}.
Interaction partners:
- Ferredoxin, apicoplast
- FAD synthase
- Anamorsin homolog
- NADH-cytochrome b5 reductase, putative
Sequence:
MKIRFVFILSVLISGVCCISKNVSRRVANRMTAHSRFLFVHDKYKRNKNFKLKNNKEENNFINLYTVKNPLKCKIVDKINLVRPNSPNEVYHLEINHNGLFKYLEGHTCGIIPYYNELDNNPNNQINKDHNIINTTNHTNHNNIALSHIKKQRCARLYSISSSNNMENLSVAIKIHKYEQTENAPNITNYGYCSGFIKNLKINDDIYLTGAHGYFNLPNDAIQKNTNFIFIATGTGISPYISFLKKLFAYDKNNLYNRNSNYTGYITIYYGVYNEDSILYLNELEYFQKMYPNNINIHYVFSYKQNSDATSFYVQDEIYKRKTEFLNLFNNYKCELYICGHKSIRYKVMDILKSHDQFDEKKKKRVHVEVY
Protein: Aquaporin (D5MCS1)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVIKVNSGGLYGADVFELKTFGKYRGEMNRKPDFEQKNSSDIVPKMVEDEKDYTIYSKCAAEFIAVLLFVYIGSMQAAGVFLHDGVLHAAFAHGVAIFVLAATFGGVSGAHINPAVTFGIALVGRISPIHAVCYVVSQLLGSVFGALLVRISLPYKMYNVISAGATLCGKGYNWQEGLTAEIVTTYILVQTVLLCAVDTDKNRLAPLAIGFSLIIEILAAGAISGASMNPARSFGPNIMGQVFLKPEHLDAQYMYWNYHWIYYIGPIIGAFIAAGVYRMFFARDYRVLA
Protein: Indole glucosinolate O-methyltransferase 5 (EC 2.1.1.-) (Q9SRD4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in indole glucosinolate biosynthesis. Catalyzes methoxylation reactions of the glucosinolate indole ring. Converts the hydroxy intermediates 4-hydroxy-indol-3-yl-methylglucosinolate (4OH-I3M) and 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) to 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3-yl-methylglucosinolate, respectively.
Interaction partners:
- Cytochrome P450 81F4
- Allergen, putative
Sequence:
MGHLIPQTGDEETELGLAAVRLANCAAFPMVFKAAIELGVIDTLYLAARDDVTGSSSFLTPSEIAIRLPTKPSNPEAPALLDRILRLLASYSMVKCQIIDGNRVYKAEPICRYFLKDNVDEELGTLASQLIVTLDTVFLNTWGELKNVVLEGGVAFGRANGGLKLFDYISKDERLSKLFNRTGFSVAVLKKILQVYSGFEGVNVLVDVGGGVGDTLGFVTSKYPNIKGINFDLTCALTQAPSYPNVEHVAGDMFVDVPKGDAILLKRILHDWTDEDCEKILKNCWKALPENGKVIVMEVVTPDEADNRDVISNIAFDMDLLMLTQLSGGKERSRAEYVAMAANSGFPRCNFVCSAYHLWVIELTKQA
Protein: Chlorophyll a-b binding protein 2.4, chloroplastic (Photosystem II light harvesting complex gene 2.4) (Protein LIGHT-HARVESTING CHLOROPHYLL B-BINDING 2.4) (Q9XF87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated (By similarity). Mediates rapid phosphorylation and migration of LHCII-PSII to photosystem I (PSI) after transition to state 2 (red) light conditions, thus leading to the formation of PSI-PSII-LHCII and PSI-LHCII supercomplex to balance the relative excitation of PSI and PSII. Involved in the production of reactive oxygen species (ROS) and stomatal closure upon abscisic acid (ABA) treatment. Required to prevent water loss (By similarity).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:23995216}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Chlorophyll a-b binding protein CP26, chloroplastic
- Photosystem I subunit O
- Photosystem II CP43 reaction center protein
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem II reaction center protein H
- Chlorophyll a-b binding protein 3, chloroplastic
- Chlorophyll a-b binding protein
- Chlorophyll a-b binding protein 2.2, chloroplastic
- Photosystem I iron-sulfur center
- ATP synthase gamma chain 1, chloroplastic
Sequence:
MATSAIQHSSFAGQTTLKPSNDLLRKIGASNGGGRIIMRRTVKSTPQSIWYGPDRPKYLGPFSENTPSYLTGEYPGDYGWDTAGLSADPETFAKNRELEVIHSRWAMLGALGCTFPEILSKNGVKFGEAVWFKAGSQIFSEGGLDYLGNPNLIHAQSILAIWACQVVLMGFIEGYRIGGGPLGEGLDPLYPGGAFDPLNLAEDPEAFSELKVKELKNGRLAMFSMFGFFVQAIVTGKGPIENLFDHIADPVANNAWAYATNFVPGK
Protein: Phospholipase A2 group V (EC 3.1.1.4) (PLA2-10) (Phosphatidylcholine 2-acylhydrolase 5) (P97391)
Organism: Mus musculus (Mouse)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), preferentially releasing fatty acyl groups with a low degree of unsaturation such as oleoyl (C18:1) and linoleoyl (C18:2) groups. Hydrolyzes low-density lipoprotein (LDL) phospholipids releasing unsaturated fatty acids that drive macrophage polarization toward an M2 phenotype. May act in an autocrine and paracrine manner. Contributes to lipid remodeling of cellular membranes at different subcellular locations and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of cardiolipin, a major component of the inner membrane of mitochondria and bacterial membranes (By similarity). Promotes phagocytosis of bacteria in macrophages through production of lysophosphatidylethanolamines (By similarity). Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing the phospholipids of the bacterial membrane. Promotes phagocytosis and killing of ingested fungi likely through controlling phagosome-lysosome fusion and phagosome maturation. Plays a role in biosynthesis of cysteinyl leukotrienes (CysLTs) in myeloid cells (By similarity). In eosinophils, triggers perinuclear arachidonate release and LTC4 synthesis in a PLA2G4A-independent way (By similarity). In neutrophils, amplifies CysLTs biosynthesis initiated by PLA2G4A (By similarity). Promotes immune complex clearance in macrophages via stimulating synthesis of CysLTs, which act through CYSLTR1 to trigger phagocytosis. May regulate antigen processing in antigen-presenting cells. In pulmonary macrophages regulates IL33 production required for activation of group 2 innate lymphoid cells. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:10531350}. Cell membrane {ECO:0000269|PubMed:10531350}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:16407308}. Recycling endosome {ECO:0000269|PubMed:16407308}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:16407308}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:16407308}.
Interaction partners:
- Group 3 secretory phospholipase A2
- Group XIIA secretory phospholipase A2
- Group XIIB secretory phospholipase A2-like protein
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Phospholipase A and acyltransferase 3
- Polyunsaturated fatty acid 5-lipoxygenase
- Phospholipase A2
- Group 10 secretory phospholipase A2
- Group IIC secretory phospholipase A2
- Group IID secretory phospholipase A2
Sequence:
MKGLLTLAWFLACSVPAVPGGLLELKSMIEKVTGKNAFKNYGFYGCYCGWGGRGTPKDGTDWCCQMHDRCYGQLEEKDCAIRTQSYDYRYTNGLVICEHDSFCPMRLCACDRKLVYCLRRNLWTYNPLYQYYPNFLC
Protein: Protein RED1 (Reductional division protein 1) (P14291)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable constituent of the synaptonemal complex during meiosis. May interact with HOP1. Required for meiosis I chromosome segregation.
Subcellular location: Nucleus.
Interaction partners:
- Meiosis-specific protein HOP1
- Meiosis-specific serine/threonine-protein kinase MEK1
- Synaptonemal complex protein ZIP1
- Meiotic recombination protein REC8
- Serine/threonine-protein kinase MEC1
- Meiosis-specific protein SPO11
- Meiotic recombination protein DMC1
- Protein ZIP2
- Protein ECM11
- Meiosis-specific protein MEI4
Sequence:
MEGLKKKIFGVCLKNDLAQTRNETKGIHYGLMTLETSKQLQEFLHLLVIKREVIQNFELLFHIINVAVKITDSNLPSDDIWHFILKLRFSSEINIDEDSKVLNYLLETGIAMENPVSWKCLAVISSILSSVPQSKKIITNLIETEHAKKIGQLFDNIQDLQQGNFLVEILSNCFKKSASNSKKVEKIPQLWQSRSKNKFFFENEFYPFSSKNGSLQTCQFLCNNFMSTLSFTGILRQVSYSGSETLKNLRIFKKKDDENSYFIQCIYNKIYLWLDEKAPLEFERKKIRITKNLKNKIQIKLRQPFHECVRTTADKTALLFNKTKGFQLEFEDEKLGETFFHNVNNIPKISEVQNFLVLDYIEEEPENEGEEEEQIGRADEQKEDEEEESLDELSTPMVYPIKSSIPHNHNEKVQLVTPDRSVSIRSDEWDLKSNTEDEEGNVLADLKISSTKETKRQTDYVHIDSEDQSPVVSAQMRKMRRESTKTLEILRQEFKDKDVQNKEDQSEQIQNPFVNTSSLVVGKSCLVNPKEKPNIDQTVVGITELKSNSSIKKRDINILDTIFGQPPSKKQKQFHKKEKKKQQKKLTNFKPIIDVPSQDKRNLRSNAPTKPKSIKVSKLRTDKKVTGEKSSPETAAEKVDDQTVRSNDEQAMSRATKEKCFPDVNEGKEITKDDAKVSLESKKNNETFVDSSVVEKHTPPDKDCNNCNITDILESTTVIDLQSPHGLSAPGQNTFTNKLQEQIYSSINHFSNELVRKISIINQELNKKILKELSEKYQKLFSELQDNFQNDTNEMLKFMGEIKDMMNLPEDQLVHAIRTRKFDNNKR
Protein: Non-lysosomal glucosylceramidase (NLGase) (EC 3.2.1.45) (F4HR96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Neutral ceramidase 2
- Neutral ceramidase 3
- Neutral ceramidase 1
- Ceramide kinase
- beta-galactosidase
- Putative F-box protein At1g32420
- Sphingolipid delta
- Beta-galactosidase 17
- Beta-galactosidase 2
- Kanadaptin-like protein
Sequence:
MQNVPEDQNKMVIDDKLPPFSWERKLNSQAKTPSEFKLSKRDHMHLFPLGYRLWRHTKDEAAKGRASIFDIFRKHHITGDHGVPLGGIGSGSIGRSYKGEFQQFKLFPKICEEAPILTNQFSAFVSRPGGVKHSTVLCPSKPQVVKDNGGYLCQGQAPNMGIESWDWNMTGEKSTYHALYPRSWTVYDGEPDPELRIVSRQVSPFIPHNYEESSLPVSVFNFTVTNTGAEPAIVTLLFTWENSVGGASGLTGQHFNSTMKAKDGVHAVALQHKTANGHPPVSYAIAAKETEDVRVSSCPCFIVSGTTPNQITAGDMWDEIKKNASFDKLTSNACSPSKPGTSIGAAIAAKVKVPPGCDRTVTFSLSWDCPEARFDEKTYHRRYTRFYGSLGNAAVAMAHDALLNFPEWETQIEEWQAPVLADTTLPEWYRVTLFNELYYFNSGGTMWTDGLPPKQSLDSIGRRKISLGLSTIDKNDQDQNNVALDILGRIDAVCSQIHAPLTSNAALGNTMIQNTTENIGQFLYLEGVQYLMYNTYDVHFYSSFALLMLFPKIELSIQRDFAAAVLMHDSSKKQVMSSGEFVTRKVLGAVPHDIGLNDPWFELNAYNLFNTDRWKDLNSKFVLQVYRDVVATGDLNFAKAVWPSVYTAIAYLDQFDKDGDGMIENEGFPDQTYDAWSCSGVSAYCGGLWVAALQAGSALAREIGDNGAAVYFNAKYEKARSVYEKLWNGSYFNYDNSRSGSSSSILADQMAGQWYARACGLKPIAKEEWIKKALETVYDFNVMRVRDGTRGAVNGMLPDGRVDTSTMVSREVWAGTTYSVAACMIQEGLADKGFRTASGIYEAAWSDRGLGCAFQTPEAWTTNDEYRSLCYMRPLAIWGIQWAHTMPKPNREQEVSLRPQEEDATSVLFQQHAGFIKVAHYLKNTKGKDHRNRLQTAYETFLKTIRL