wanglab/gogpt-training-data huggingface dataset:
Protein: ESAT-6-like protein (Q8VJK9)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAMTINYQFGDVDAHGAMIRAQAAALEAEHQAIVRDVLAAGDFWGGAGSVACQEFITALGRNFAVIYQQANAHGQKIQAAGSNMAQTDSAVGSSWA
Protein: Dysferlin isoform X10 (Dysferlin, limb girdle muscular dystrophy 2B (autosomal recessive)) (F1QIS3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004483}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004483}.
Interaction partners:
Sequence:
MLRCLLQRATNLRNVEKGERHSDPLASITFRGTKKKTKVIKNNVNPVWNEGFEWDLKGVPLDSGAELHVVVKDHEKMGRNRFLGECRVALRDVLNSPNLAATFTVSLVDTKRNSTGATITLQVSYIPPPGMTPIFQPPPQPEAQHTPVELDTVTVFSLDTMGEDDTESMLMMEVAEEPEPVPGPQGQDIGAPTAPPKKAPPNFNQGLKKKKRQSNKSPLSDKAQDLQVRLRIIEGRQLPGVNIKPVVKVTVGGQTKRTRIKKGNNPFFDETFFLNFFEKPSDLFDEPIFITVFDSKSLRKDSVIGEFKLDVGMVYNEHRHAILRKWLLLADPDDLSAGARGYLKVSMFVLAAGDEPPMDKKEGVEEKEDIEANLLRPAGLTLRGATFTLRVYRAEDLPQMDDALIDDVKHFLGFDTNRKNLVDPLVEVNFAGKTISSKILEKCANPQWNQCLTLPIRFPSMCEKMRIRILDWDRASHNDVIGTAHLCMSKISAPGGDIEVDDSIGFLPTFGPCFVNMYGSPREFTAFSDPHEALNLGKGEGVAYRGRVLLELITKLSDQVDQRSEDINSDDLLVVEKFMRKRKFSLFAAFYSATLLQDVDDAVQFEVSIGNYGNKFDNTCLPLASTTQFSRAVFDGCHYYYLPWGNVKPVVVVSSEWEDIGPRIEALNMLLSIVDRLESNLEQVQLELKARSDDQEVEQRVVQLLDDVIADCSEELPELDKWPCVTPLDKALRNLRKINMQQIVQAALALKHGPETELSAVLEQAEDWTMRLRYLSEEPQNSLPDIIIWMLQGDRRVAYHRIPAHQVLFSYGYCGKHCGQLQTVFMKCPQEDGGCSKIPAQLRIKVWFGLTADVKSFNQFAEGKLSVFAETYENQTKLALVGNWGTTGLTYPKFSDVTGRVKLPKESFKPSSGWSWAGEWFISPEKTMLYDADAGHISFLEEVFENQLRLPGGQWIGMPEGYTDVNGEKAVPKDEIECPPGWVWEDIEWSEDLKRAVDDQGWEYGITLPPDRRPKSWVPSEKMYHTNRRRRWIRLRRRDMQKMEALRKQRPDESEREGWEYASLFGWKFHLKQKKTDLFRRRRWRRRMEPLEKTGPAAIFALECSLSSFTDEKNDDKSVTTTFGVSRPTISCFFDSGTLYHLRCYLYQARDLLAMDKDSFSDAYAVVSFLHQSQKTVTVRNTLNPTWDQTLIFYEVEIFGDHLVTERSPPNIVVELYDQDTYGADEFMGRCVCQPSMASSPRLAWYPIQKAGNSAGDLLAAFELIRRDKPAVHHIPGQEGDIIPPSHIMDELVLPGFLSENQQQWPEDSDLPYPPPQREPNVYMVPQGIKPVLQRTAIEILAWGLRNLKSFQLASVTSPSLQVECGGSVVQSCVIRNIKKNPNFDVNILFIDVRLPKEELYMPPLVIKVIDNRQFGRKPVVGQCSVHSLNEFYFQPESLERDSTEEEFEVIAHTPRDDVLVDIDDKEPLIPGQQDEFMDWWSKFYASMGERTKCGSYLEKGFDMLQVYDRELEKTEGFEQFADFCQTFKLYRGRTQNDSEDPSVVGEFKGSFKIYPLPDDPSMPVPTRQFRKLPPNGIEECLVRIYIIQAFGLQPKDANGKCDPYVKITLGKKSVDDHDNYIPCTLEPVFGKMFELTCCLPLEKDLKITLYDYDMVTKDEKIGETIIDLENRFLSRHGARCGLPQSYCLSGINQWRDQLKPSQLLHRLCERRNYKLPVYKQDRIYFRGHEYTVADLDEGKPLNPHLGPVMERLALLVLRRHGLVPEHVETRPLYSPLQPDIEQGRLQMWVDLFPKSLGPPGPPFNITPRKAKKFFLRCIIWNTRDVILDDVSVTGEKMSDIYVKGWMHGHEENKQKTDVHYRSLGGEGNFNWRFLFPFHYLPAEQLCTIDKKEHFWSLDKVETKLPPKLTIQIWDNDKFSFDDFLGSLEMDLNHMLSPAKSPEKCGLEMLTQSQDKLVSLFEQKTVKGWWPCVCDKEDKKILAGKVEMSLEIVCEQEQDERPAGLGRDEPNMNPHLEEPQRPETSFLWFSSPYKTFRFIVWRRFKWLILGLFILFFIILFLGVFLYAFPNYAAMKMVGPFSGLGKGTQ
Protein: Outer envelope pore protein 37, chloroplastic (Chloroplastic outer envelope pore protein of 37 kDa) (AtOEP37) (O80565)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Voltage-dependent peptide-sensitive high conductance rectifying cation channel with a strong affinity for TIC32 that is imported into the chloroplast. Conductance is pH-dependent decreasing with decreasing pH values.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:16624824}; Multi-pass membrane protein {ECO:0000269|PubMed:16624824}.
Interaction partners:
- Protein TOC75-3, chloroplastic
- Outer envelope protein 80, chloroplastic
- Mitochondrial import receptor subunit TOM40-1
- Outer envelope pore protein 16-2, chloroplastic
- Translocase of chloroplast 159, chloroplastic
- Translocase of chloroplast 34, chloroplastic
- Outer envelope membrane protein 7
- Translocase of chloroplast 120, chloroplastic
- Putative mitochondrial outer membrane protein porin 5
- Short-chain dehydrogenase TIC 32, chloroplastic
Sequence:
MADPSSQNPNLATPPPPSSPSPTHQIQSGTSELSPPSRPPCSTLSFLKTANRPKLRVTSEFDSDSLLFLNKVSCKLFDNLAKLKLSFQNNSQREISQPQVSFTSKHVSVLYDVEEKNTFIKSTLDVHPRLQLRALHNVKAQQGEVAMEANLTEPGYSLELSSPVPIGYPRATLKFPLGEISLQEKDEEEEEKQKRTLSVNGILKRQVMNGVCTALYTDEELRLRYAYKDDALSFIPSISLPSNAASFAFKRRFSPSDKLSYWYNFDSNMWSAVYKRTYGKDYKLKAGYDSDVRLGWASLWVGDEAGKVKTTPMKMKVQFMLQVPQDDIKSSVLMFRVKKRWDI
Protein: Probable polyamine transporter At3g19553 (Q9LH39)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable cell membrane polyamine/proton symporter involved in the polyamine uptake in cells.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- DEK domain-containing chromatin-associated protein 3
- Putative cyclic nucleotide-gated ion channel 13
- Dicarboxylate transporter 2.2, chloroplastic
- Cationic amino acid transporter 7
- Interactor of constitutive active ROPs 1
- Amino acid permease 2
- Transcription factor PAR1
Sequence:
MGEEETIVNDENSSKPKPSPKLTLLPLVFLIFYEVSGGPFGVEDSVKSGGGPLLALLGFLIFPLIWSIPEALVTAELATSFPENGGYVVWISSAFGPFWGFQEGFWKWFSGVMDNALYPVLFLDYLKHSFPVLDHVAARVPALLVITFSLTYLNYRGLHIVGFSAVVLAVFSLCPFVVMALLAVPNIRPKRWLFVDTQKINWRGYFNTMFWNLNYWDKASTLAGEVDRPGKTFPKALFGAVLLVMGSYLIPLMAGTGALSSSTSGEWSDGYFAEVGMLIGGVWLKGWIQAAAAMSNLGLFEAEMSSDAFQLLGMSEIGMLPAFFAQRSKYGTPTISILCSATGVIFLSWMSFQEIIEFLNFLYALGMLLEFAAFVKLRIKKPDLHRPYRVPLNTFGVSMLCLPPSLLVILVMVLAAPKTFLISGVIIVLGFCLYPFLTLVKEKQWARFIPEETRPVSGVSSESQLDEEHGDESAASLLP
Protein: Magnetosome formation protease MamE (EC 3.4.21.-) (MM36.3) (Magnetochrome MamE) (Magnetosome serine protease MamE) (V6F2B6)
Organism: Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
Function: Acts at 2 distinct steps of magnetosome formation; required for correct localization of proteins to the magnetosome while the protease activity is required for maturation of small magnetite crystals into larger, functional ones (By similarity). Probably cleaves at least itself, MamO and MamP; cleavage requires the putative transprot domain of MamO (By similarity). Involved in localization of some proteins (at least MamA, MamC, MamF, MamI and MamJ) to the magnetosome (By similarity). One of 7 genes (mamLQBIEMO) able to induce magnetosome membrane biogenesis; coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon restores magnetosome vesicle formation but not magnetite biosynthesis.
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:14766587}; Single-pass membrane protein {ECO:0000255}. Note=Purified magnetosomes remain attached to each other. {ECO:0000269|PubMed:11571158}.
Interaction partners:
- Actin-like protein MamK
- Magnetosome protein MamH
- Magnetosome protein MamI
- Magnetosome-associated protein MamJ
- Magnetosome protein MmsF
- Magnetosome protein MamF
- Magnetosome protein MamN
- Magnetosome protein MamM
- Magnetosome protein MamQ
- Magnetosome protein MamZ
Sequence:
MTMFNGDVEDGGRSNVSCGKDLKRYLMLMGVVALVVLFGAFIYRQSSGGLRLGAMMEQMTGARGAVNVPAQHGAPSAVVDPAMSVPARARVAPPSAAGAIATFPPVVDFGPAPVVSGGPFTGVVTLLRNSVVSVTASSSGGQVMPDPLGLVNPDGLPRFANPTTRSVENIGTGVIVRNDGFIVTNYHVVRGANSVYVTVKDDVGSIRYSGEIVKMDEALDLALLKITPKVQLTAAVLGDSDAVNVADEVIAIGTPFGLDMTVSRGIISAKRKTMVIEGMTHSNLLQTDAAINQGNSGGPLVAANGTVVGINTAIYTPNGAFAGIGFAVPSNQARLFALDEVGWLPTSTAEGPAMGLVAMQRPMGVGVGAAGPVIAAGTPSPHVDGRQNMDCSNCHDIIPAGNGFQAPMMPVAAPVPPPPIPANAVSPHTDGRQNMTCNTCHQFVGGAAAGPIAFGQPMMPIAAPQQPAPAIRANAANPHTDGRQNMNCASCHQIIGSVGAAPIAAPGAGGAYRFSQPPGSLAINIQGPRGGQGAVAGSGGSRASLLGAALTPLTQRLGLQANLPAGRGVFVNGVTPNTPAASAGLRPGDVILKVDGRPVHQPEEVAAIMAEMPNGRSVRIGVLRAGDVSNMSLVTGPSGLAAAVVQAPTAPVVMAGGAPTVPGVQPVIPKVPTEFNWLGMEIETFMAPQPVVGMPGATPVAGGGKGAQVAEVLAGSRAAVAGLQANDLIIEVNNRPVTSPARLDAAIKAATAAGQQILLKVHRNGQEFWIVL
Protein: Apoptotic enhancer 1 protein (Ce-iASPP) (Inhibitor member of the ASPP family) (Protein iASPP) (Q9XVN3)
Organism: Caenorhabditis elegans
Function: Negetively regulates apoptosis via its interaction with cep-1.
Subcellular location: Nucleus {ECO:0000305|PubMed:12524540}.
Interaction partners:
- exodeoxyribonuclease III
- Apurinic-apyrimidinic endonuclease
- Ras-associating domain-containing protein
- Transcription factor cep-1
- Endonuclease III homolog
Sequence:
MVTTSSGGGIGYPANNGVTQVSLIHSSDSVRTVSTAPIYRPTSSMASTMAHKSSTAPFISANQRMSKPPVRVVAQPPPPHPQALSQQYHQQNPMMMYSAPNTRPHVIPTMQVQPTMAAQIKRNNPVNAQFQNPSEMIADYGVKPQSVEMVQRVRAVRRQVADEETELRRLRELEHETAQLQNKNYGRERELNVQGSMLKEAQLELRNASMRAQSLNKHLEEMYRRRQTAAAAALVEQRKMQQHQILLARAANQVSTQEVIRPRASVEPFQVNNTQQQQPSPQMMKSEEFSEKRDLNGQTGSYDAIDGSGDHQKIPTEPSYLAPCKENQQKYSELSKMASTDPHSNHSSPSTSSQKAPTLITFSPPSFEQKINSSTMTRDSPFVERPTSFGDSLDESRLRSGKTDLVSLRSDSLKATKRRSWAASEGTSMSEAEMIHRLLDEQRRGRSHFIPQLPTSQEEPSAITSETYAEEVVNSESKQVATSSDSTNNLELPTEQMVLGSDTTTEEDASSCSTRSDDGQNLEMEVAIERRTVKGILRRPNEKMNKGRIEFDPLALLLDAALEGELDLVRSSASKLTDVSQANDEGITALHNAICAGHYEIVRFLIENDADVNAQDSDGWTPLHCAASCNNLPMVRQLVEGGGCVLASTLSDMETPVEKCEEDEDGYDGCLKYLSAAHNSTGSINTGKVYAAYGYEAAFEDELSFDAGDELTVIEKDKVDKNWWTCEKNNGEKGQVPRTYLALYPSLKYRKKLNFVMFDLPLESNNNVE
Protein: Nucleoprotein (Nucleocapsid protein) (NC) (Protein N) (P32923)
Organism: Avian infectious bronchitis virus (strain Gray) (IBV)
Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04097}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04097}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04097}. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. {ECO:0000255|HAMAP-Rule:MF_04097}.
Interaction partners:
Sequence:
MASGKATGKTDAPAPVIKLGGPRPPKVGSSGNASWFQAIKAKKLNSPQPKFEGSGVPDNENFKTSQQHGYWRRQARFKPGKGRRKPVPDAWYFYYTGTGPAADLNWGDSQDGIVWVAAKGADVKSRSNQGTRDPDKFDQYPLRFSDGGPDGNFRWDFIPLNRGRSGRSTAASSAASSRPPSREGSRGRRSGSEDDLIARAAKIIQDQQKKGSRITKAKADEMAHRRYCKRTIPPGYKVDQVFGPRTKGKEGNFGDDKMNEEGIKDGRVTAMLNLVPSSHACLFGSRVTPKLQPDGLHLKFEFTTVVPRDDPQFDNYVKICDQCVDGVGTRPKDDEPKPKSRSSSRPATRTSSPAPRQQRLKKEKRPKKQDDEVDKALTSDEERNNAQLEFDDEPKVINWGDSALGENEL
Protein: Transcription factor ACEII (Q96WN6)
Organism: Hypocrea jecorina (Trichoderma reesei)
Function: Positive regulation of the major cellulase and xylanase genes (cbh1, cbh2, egl2 and xyn2). Binds to the 5'-GGCTAATAA-3' site present in the cbh1 promoter.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDLRQACDRCHDKKLRCPRISGSPCCSRCAKANVACVFSPPSRPFRPHEPLNHSHEHSHSHSHNHNGVGVSFDWLDLMSLEQQQEQQQGQPQHPPPPVQTLSERLAALLCALDRMLQAVPSSLDMHHVSRQQLREYADTVGTGFDLQSTLDSLLHHAQDLASLYSEAVPASFNKRTTAAEADALCAVPDCVHQDRTSLHTTPLPKLDHALLNLVMACHIRLLDVMDTLAEHGRMCAFMVATLPPDYDPKFAVPEIRVGTFVAPTDTAASMLLSVVVELQTVLVARVKDLVAMVDQVKDDARAAREAKVVRLQCGILLERAESTLGEWSRFKDGLVSARLLK
Protein: Retinaldehyde binding protein 1 (H3BN92)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XNGFCIIENFKGFTMQQAASLRTSDLRKMVDMLQPWYFTTTYNVVKPFLKSKLLERVFVHGDDLSGFYQEIDENILPSDFGGTLPKYDGKAVAEQLFGPQAQAENTAF
Protein: Short-chain specific acyl-CoA dehydrogenase, mitochondrial (SCAD) (EC 1.3.8.1) (Butyryl-CoA dehydrogenase) (Q07417)
Organism: Mus musculus (Mouse)
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q3ZBF6}.
Interaction partners:
- Enoyl-CoA hydratase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- 3-ketoacyl-CoA thiolase A, peroxisomal
- 3-ketoacyl-CoA thiolase B, peroxisomal
- Trifunctional enzyme subunit beta, mitochondrial
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Peroxisomal bifunctional enzyme
- Ethylmalonyl-CoA decarboxylase
- Acyl-coenzyme A synthetase ACSM3, mitochondrial
Sequence:
MAAALLARARGPLRRALGVRDWRRLHTVYQSVELPETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTGVIMSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
Protein: 26-29kD-proteinase (EC 3.4.22.-) (Homologue of Sarcophaga 26,29kDa proteinase) (RE18380p) (Q9V3U6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQVFLALALLAGLAFSANATNPPKWDPNYIVKGTLYIPYAEIAEPFYAWYDKNTRRSRIDYYGGMVKTYQLAGEGQYGTLLKLAPITTKTENNKLTCLQVNGTADQAVDIQSILPDAKPFSLVGTESFLGYTCDKFRLESTIGQKKNIYTLWVRYKKSPHYPSSRMPIPVRYEMRGYNTLLGSHYDHYYLDYDSYEHDDIPNEVFEIDDSLQCVGFPGPGTGHYATFNPMQEFISGTDEHVDKAFHHFKRKHGVAYHSDTEHEHRKNIFRQNLRYIHSKNRAKLTYTLAVNHLADKTEEELKARRGYKSSGIYNTGKPFPYDVPKYKDEIPDQYDWRLYGAVTPVKDQSVCGSCWSFGTIGHLEGAFFLKNGGNLVRLSQQALIDCSWAYGNNGCDGGEDFRVYQWMLQSGGVPTEEEYGPYLGQDGYCHVNNVTLVAPIKGFVNVTSNDPNAFKLALLKHGPLSVAIDASPKTFSFYSHGVYYEPTCKNDVDGLDHAVLAVGYGSINGEDYWLVKNSWSTYWGNDGYILMSAKKNNCGVMTMPTYVEM
Protein: Bccry1 (A0A384JIP4)
Organism: Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Interaction partners:
Sequence:
MFLVFPARNIFPKQLPSRLIISQRNILPLPQFLAKQQILHQSCISTSRILKMSTRKATAAAAASTKRKASSTPEPISHLNGSKKKAKVSDDDHDLSELRQPHHSAKEAEENGIVLRKYYPHEMCNPRAIAYNNDELERPIEALHAALADTQKERKGIDKGGECVVHWFKCDLRTKDNTALSMASQKAKELGIPLVTMYIVSPQDFEAHLTAPVRVDFILRTLDILKKDLAKLDIPLYVETIDKRKRVESRILELLGEWGCSHFYANMEYEVDELRREARMVRACVEKGICMDVIHDTCVVRPGELKSGQGKQYAVYTPWFKSWVAYVHENSDLLELFDAPEKNPSSARKTFAKLFETEIPDAPKNKSLTSEEKERFRSMWPAGEHAAHERLSKFADEKINKYQDHRNFPSLNSTSSLSVHFASGTLSSRTAIRTARDHNNTKKLNAGYQGIQTWISEVAWRDFYKHVLVHWPYVCMNKPFKPEYTNIEWEYNRAHFQAWTEGRTGYPIVDAAMRQLNHCGYMHNRSRMIVGSFLAKHLLLDWRMGERYFMEHLIDGDFASNNGGWGFCASTGVDPQPYFRIFNPLLQSEKFDAEGEYIRKWVEELKGVKGKAIHEPYGDKEAAKIAKKSGYPERIVEHKVSRERCLKRYKEGLGRANS
Protein: Serine rich endogenous peptide 12 (AtSCOOP12) (Phytocytokine SCOOP12) (Precursor of serine rich endogenous peptide phytocytokine 12) (B3H7I1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including root growth prevention, phospholipid signaling pathway activation (e.g. accumulation of phosphatidic acid (PA), but transient reduction of phosphatidylinositol 4,5-bisphosphate (PIP(2)) levels) and reactive oxygen species (ROS) response regulation. Moderates primary root growth, and regulates root meristems and cell elongation; this root growth regulation is associated with the modulation of ROS metabolism and alteration of cell wall structure, and depends on variations in many genes expression. Promotes ROS (e.g. superoxide anion O(2) and hydrogen peroxide H(2)O(2)) production and MAPK (e.g. MPK3, MPK4 and MPK6) activation in a MIK2-dependent manner, thus leading to the up-regulation of immune-related marker genes (e.g. WRKY30, WRKY33 and CYP81F2). Involved in biotic and oxidative stress responses; acts as a negative regulator of defense against necrotrophic pathogens such as the bacteria Erwinia amylovora and the fungus Alternaria brassicicola. Able to prime defense responses against the pathogenic bacteria Pseudomonas syringae pv. tomato DC3000. Contributes to the triggering of defense responses toward generalist herbivores such as Spodoptera littoralis, probably via the activation of jasmonate and indole glucosinolate biosynthesis. Triggers the expression of several PROSCOOP genes (e.g. PROSCOOP3, PROSCOOP7, PROSCOOP12 and PROSCOOP13).
Subcellular location: Cell membrane {ECO:0000269|PubMed:34535661}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:34535661}. Note=The precursor of SCOOP12, PROSCOOP12, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP12 in the apoplasm. {ECO:0000269|PubMed:34535661}.
Interaction partners:
- Serine rich endogenous peptide 4
- Transmembrane protein
- Transmembrane protein
Sequence:
MRNTISSKMGQVLIVLLLLCTVLCRTESALPSGQHSVLLTGRRLMGSGASGPVRSSQSSQAGGRFNDADPIAIDYGKY
Protein: Mycinamicin III 3''-O-methyltransferase (EC 2.1.1.237) (Mycinamicin biosynthesis protein F) (Q49492)
Organism: Micromonospora griseorubida
Function: O-methyltransferase that catalyzes the conversion of mycinamicin III to mycinamicin IV in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic.
Interaction partners:
Sequence:
MSPSTGVELYLDLLKRTVSNFIYQDATHVAGLITEAAFVEEARESGEDYPTVAHTMIGMKRLNNLQHCVESALRDGVPGDVLETGVWRGGACIFARGILKAYDVRDRTVWVADSFQGFPKITDDDHPMDAEMNLHQYNEAVDLPTSLATVQRNFSRYGLLDDQVRFLPGWFKDTMPTAPFERLAVLRMDGDSYGATMDVLTHAYPRLSPGGFAIIDDYCIPACREAVHEYRDRHGISDEIVEIDRQGVYWRRSA
Protein: Amino acid transporter heavy chain SLC3A1 (D2) (Neutral and basic amino acid transport protein) (NBAT) (Solute carrier family 3 member 1) (b(0,+)-type amino acid transporter-related heavy chain) (NAA-TR) (rBAT) (Q64319)
Organism: Rattus norvegicus (Rat)
Function: Involved in the high-affinity sodium-independent transport of cystine and neutral and dibasic amino acids (system B(0,+)-like activity). May function as an activator of SLC7A9 and be involved in the high-affinity reabsorption of cystine in the kidney proximal tubule.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q91WV7}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q91WV7}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- b
- Solute carrier family 7, member 15
- Solute carrier family 7 member 13
- Y+L amino acid transporter 1
- Neutral amino acid transporter B
- Large neutral amino acids transporter small subunit 1
- Amino acid transporter
- Solute carrier family 7, member 12 like 1
- Solute carrier family 7, member 12
- RCG41520, isoform CRA_b, member 12)
Sequence:
MNEDKDKRDSIQMSMKGCRTNNGFVQNEDIQEQDPDSRDTPQSNAVSIPAPEEPQLKVVRPYAGMPKEVLFQFSGQARYRVPREILFWLTVVSVFLLIGATIAIIIISPKCLDWWQAGPMYQIYPRSFKDSDKDGNGDLKGIQEKLDYITALNIKTIWITSFYKSPLKDFRYAVEDFKEIDPIFGTMKDFENLVAAVHDKGLKLIIDFIPNHTSDKHPWFQSSRTRSGKYTDYYIWHNCTHANGVTTPPNNWLSVYGNSSWQFDEERKQCYFHQFLKEQPDLNFRNPAVQEEIKEIIKFWLSKGVDGFSFDAVKFLLEAKDLRNEIQVNTSQIPDTVTRYSELYHDFTTTQVGMHDLVRDFRQTMNQFSREPGRYRFMGTEVSAESTERTMVYYGLSFIQEADFPFNKYLATLDTLSGHTVYEAITSWMENMPEGKWPNWMIGGPETSRLTSRVGSEYVNAMNMLLFTLPGTPITYYGEEIGMGDISITNLNERYDTNALLSKSPMQWDNSSNAGFTEANHTWLPTNSDYHTVNVDVQKTQPSSALRLYQDLSLLHARELLLSRGWFCLLRDDNHSVVYTRELDGIDKVFLVVLNFGESSTVLNLQETISDVPTKLRIRLSTNPASKGSDVDTHAVSLEKGEGLILEHSMKTLLHHQKAFRDKCFISNRACYSSVLDLLYSSC
Protein: BCL2-associated athanogene 3 (Q6DC38)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MATNDPLPPGWEIKIDPQTGWPFFVDHNNRTTTWNDPRHDTKKIFSNGPSMSPETPQDMHKTFINEMRQPMLRQGYIPIPVCHENPEPRLQQYPSFSYIHPAVQQNLRTDGRTPSPTPAAHCRPRSPVQTPSEACSSCSPTSHGPEGYQPQGTHQQISGLHQQPRSSNTGLRAGYIPIPVIHEGAGGVLPSQLSQSSHPTREKIYREQVPIQIQQNRAASPIQVPLRAQSPVMAQIMGERPQMQQHIGHTAIPSKIEHPVEEIIRVPTFEVPIQRVSEVPQQIHHQPVQQQQQPTQQPQPKAQPSPQVSETSNITIQVPPAPEPQETAAPQTPQEVPSSQLQPEETLEQDLSHPGLVKVQQIVERVEKLAQNVKGFDGKKNDKRYLVLEEMLTKELLALDSVDPEGRPDVRQARRDGVRRVQNILDELEMIGEMQAGNEAKGEQSMIDQLNTERVKEFS
Protein: Chemokine (C-X-C motif) ligand 11, duplicate 5 (A0A0R4IQ43)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- C-X-C chemokine receptor type 3
- Chemokine
- Stromal cell-derived factor 1
- Chemokine
- Chemokine
- C-X-C chemokine receptor type 3-2
- Stromal cell-derived factor 1
- C-C motif chemokine
- Chemokine
- Interleukin-8
Sequence:
MKTAAFLVFLACLLATQVHGQKKFNRCSCVGKGLDRVALRNIEKFEIIHPSPSCGKQEIIVTMKSSEQKCLNPESKFTQELIRRALEKRVILTDEVSVVFSGSTSR
Protein: Probable mitochondrial import receptor subunit tom70 (Translocase of outer membrane 40 kDa subunit) (O14217)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with tom20 and tom22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the tom40 translocation pore.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P07213}; Single-pass membrane protein {ECO:0000250|UniProtKB:P07213}.
Interaction partners:
- Mitochondrial import receptor subunit tom20
- Probable mitochondrial import receptor subunit tom40
- Mitochondrial import receptor subunit tom22
- Mitochondrial import receptor subunit tom7
- Mitochondrial distribution and morphology protein 10
- Metaxin-1
- SAM50-like protein SPAC17C9.06
- Mitochondrial import inner membrane translocase subunit tim44
- Mitochondrial import protein 2
- Mitochondrial import inner membrane translocase subunit tim17
Sequence:
MSGISNAENGKAIVSSGVLNSVSAFVRRHRTFVYTIGAVAVFATVGGVYHVQQKKASHKRSKKLKAHQDKAESKVNEGKNEAAKVVKEEDLKSSETGKDVETAAAAAAAAKKKKKNKKKVKAKKVGDSSVDKIATEESVKSMTKEERAKLAAELKTLGNKAYGQKEYANAIDYYTQAITCSHDPIFFSNRAACYAAIGDFEQVIKDTSEALSLDSSYVKALNRRSAAYEQLGKLDEALMDSTVSCIFDGFANESMTATVERLLKKVAEKKSSALLKERPPKLPAASFIQTYLDSFHAQPKPLFDNKFDGDAALAEAYEYLEKGEYQLSYDKAKESCLGSFSSPSVNARTHNLVGTFKFVSGDSKGSMENFNAAIKLDRKFIQPYIRLSAAYLDENDNEKMWKVLNDAESVDKTDSDLYYHRAQVRFVSGEFAEAISDYQKSIALDDSFIYSHIQLGVAQYKTHAIAESMKTFEDCKKRFPNSSEVYNYFGEILLDQQKFDDAVKNFDHAIELEKREHLTIMSAMPLINKALAVFQWKKDISQAENLCRQALSADPECDIAIASMAQFLLQQGKAREALEYFEKSAQLARTESEMVNAFSYAEATRTQIALTEKYPQLVGRLSNPM
Protein: Adenosine 5'-monophosphoramidase hnt1 (EC 3.-.-.-) (Histidine triad nucleotide-binding protein HNT1) (HINT) (Hit family protein 1) (O94586)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GPI ethanolamine phosphate transferase 1
- Low-affinity iron/zinc ion transport protein fet4
- Zinc-regulated transporter 1
- Aprataxin-like protein
Sequence:
MSCIFCKIVKGDIPCVKLAETALSLAFLDIAPTSKGHALVIPKEHAAKMHELSDESCADILPLVKKVTKAIGPENYNVLQNNGRIAHQFVDHVHFHIIPKPNEEYGLGVGWPSYPISPEEIKALGEEISSKIK
Protein: Ras-related protein Rab (Q86PD0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU367128}; Lipid-anchor {ECO:0000256|RuleBase:RU367128}.
Interaction partners:
Sequence:
MTLRSKAIMTSTSDKREHLYKILVIGGLGTGKTSFIKRYVHQFFSQNYRATIGVDFALKVLQWDANTIVRLQLWDIAGQERFGNMTRVYYKEAVGAFIVFDVTRSGTFDCVSKWKEDLDSKVQLPDGSPIPCILLANKCDQEKQGIITQPEKMDEYVRENGFAGWFETSAKENINIDEAARALVNKILINDKLISADLADGDKFNLSAADATGSDAKNKCSC
Protein: Terminase, small subunit (Gene product 16) (gp16) (Packaging protein Gp16) (P17311)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: The terminase small subunit binds to the packaging initiation site and regulates the ATPase activity of the terminase large subunit. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer once the capsid is full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by neck proteins.
Interaction partners:
Sequence:
MEGLDINKLLDISDLPGIDGEEIKVYEPLQLVEVKSNPQNRTPDLEDDYGVVRRNMHFQQQMLMDAAKIFLETAKNADSPRHMEVFATLMGQMTTTNREILKLHKDMKDITSEQVGTKGAVPTGQMNIQNATVFMGSPTELMDEIGDAYEAQEAREKVINGTTD