wanglab/gogpt-training-data huggingface dataset:
Protein: Integrin alpha-8 [Cleaved into: Integrin alpha-8 heavy chain; Integrin alpha-8 light chain] (P53708)
Organism: Homo sapiens (Human)
Function: Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney genesis. Neuronal receptor for TNC it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons.
Subcellular location: Membrane {ECO:0000269|PubMed:24439109}; Single-pass type I membrane protein {ECO:0000269|PubMed:24439109}. Cell membrane {ECO:0000269|PubMed:24439109}.
Interaction partners:
- Nephronectin
- Integrin beta-1
- Vitronectin
- Fibronectin
- Extracellular matrix organizing protein FRAS1
- FRAS1-related extracellular matrix protein 2
- FRAS1-related extracellular matrix protein 1
- Tenascin-X
- Tenascin-N
- Tenascin
Sequence:
MSPGASRGPRGSQAPLIAPLCCAAAALGMLLWSPACQAFNLDVEKLTVYSGPKGSYFGYAVDFHIPDARTASVLVGAPKANTSQPDIVEGGAVYYCPWPAEGSAQCRQIPFDTTNNRKIRVNGTKEPIEFKSNQWFGATVKAHKGKVVACAPLYHWRTLKPTPEKDPVGTCYVAIQNFSAYAEFSPCRNSNADPEGQGYCQAGFSLDFYKNGDLIVGGPGSFYWQGQVITASVADIIANYSFKDILRKLAGEKQTEVAPASYDDSYLGYSVAAGEFTGDSQQELVAGIPRGAQNFGYVSIINSTDMTFIQNFTGEQMASYFGYTVVVSDVNSDGLDDVLVGAPLFMEREFESNPREVGQIYLYLQVSSLLFRDPQILTGTETFGRFGSAMAHLGDLNQDGYNDIAIGVPFAGKDQRGKVLIYNGNKDGLNTKPSQVLQGVWASHAVPSGFGFTLRGDSDIDKNDYPDLIVGAFGTGKVAVYRARPVVTVDAQLLLHPMIINLENKTCQVPDSMTSAACFSLRVCASVTGQSIANTIVLMAEVQLDSLKQKGAIKRTLFLDNHQAHRVFPLVIKRQKSHQCQDFIVYLRDETEFRDKLSPINISLNYSLDESTFKEGLEVKPILNYYRENIVSEQAHILVDCGEDNLCVPDLKLSARPDKHQVIIGDENHLMLIINARNEGEGAYEAELFVMIPEEADYVGIERNNKGFRPLSCEYKMENVTRMVVCDLGNPMVSGTNYSLGLRFAVPRLEKTNMSINFDLQIRSSNKDNPDSNFVSLQINITAVAQVEIRGVSHPPQIVLPIHNWEPEEEPHKEEEVGPLVEHIYELHNIGPSTISDTILEVGWPFSARDEFLLYIFHIQTLGPLQCQPNPNINPQDIKPAASPEDTPELSAFLRNSTIPHLVRKRDVHVVEFHRQSPAKILNCTNIECLQISCAVGRLEGGESAVLKVRSRLWAHTFLQRKNDPYALASLVSFEVKKMPYTDQPAKLPEGSIVIKTSVIWATPNVSFSIPLWVIILAILLGLLVLAILTLALWKCGFFDRARPPQEDMTDREQLTNDKTPEA
Protein: Rho guanine nucleotide exchange factor 1 (Lbc's second cousin) (Q9Z1I6)
Organism: Rattus norvegicus (Rat)
Function: Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12 (By similarity). Mediates angiotensin-2-induced RhoA activation.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocated to the membrane by activated GNA13 or LPA stimulation. {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-12
- Transforming protein RhoA
- RSA-14-44 protein.
- Protein-tyrosine kinase 2-beta
- CD44 antigen
- Rho guanine nucleotide exchange factor 11
- Rho guanine nucleotide exchange factor 6
- Rho guanine nucleotide exchange factor 28
- A-kinase anchor protein 13
Sequence:
MGEVAGGAAPGPPRSGLVSIIIGAEDEDFENELEANPEDQNSQFQSLEQVKRRPAHLMALLQHVALQFEPGPLLCCLHADMLSSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPSVAFELDRTRPDLISEDVQRRFIQEVVQSQQAAVTRQLEDFRSKRLMGMTPWEQELSLLEPWIGKDRGNYEARERHVAERLLSHLEEMQHTISTDEEKSAAVVTAISLYMRHLGVRTKSGDKKSGRNFFRKKVMGNRRSDEPPKTKKGLSSILDPARWNRGEPSAPDCRHLKVEVDEKPGPADRKGSLGISSRDRTVGTPGQDNPGVSLHPLSVDSLDSREPGVDTPQEPGDTPPQGPTSLEPLAPPESTEDNGETESPEPGDDGEPGRSGLEQEPEEPPGWRELVPSDTLLGLPKNQVKRQEVISELLVTEAAHVRMLRVLHDLFYQPMAEGGFFPLEELQNIFPSLDELIEVHSLFLDRLMKRRQESGYLIEEIGDVLLARFDGAEGSWFQKISSRFCSRQSFALEQLKAKQRKEPRFCAFVQEAESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQNTEEPAERAKVELAAECCREILHHVNQAVRDMEDLLRLKDYQRRLDLTHLRQSNDPMLSEFKNLDITKKKLVHEGPLTWRLTKDKAVEVHVLLLDDLLLLLQRQDEGCCSSHTSRTLTPTPDGKTMLRPVLRLTSAMTREVATDHKAFYVIFTWDQEAQIYELVAQTSSERKSWCALITETAGSLKVPAPASRPKPRPSPSSTREPLLSSSENGTGGTEAAPADARTERILNDLLPFCRPGPEGQLAATALQKVLSLKQILLSTEEDSGAGPPRDGDGVPGGGAPGPTHTQEVEENLLSLEVVIKQLEELEEEFCRLRPFLSQLGEILSPNLAAPERSAQTGLS
Protein: Adhesion G-protein coupled receptor F1 (G protein-coupled receptor 110) (G protein-coupled receptor KPG_012) (G protein-coupled receptor PGR19) (Q5T601)
Organism: Homo sapiens (Human)
Function: Orphan receptor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20149256}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:20149256}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Probable non-functional immunoglobulin heavy variable 3-16
Sequence:
MKVGVLWLISFFTFTDGHGGFLGKNDGIKTKKELIVNKKKHLGPVEEYQLLLQVTYRDSKEKRDLRNFLKLLKPPLLWSHGLIRIIRAKATTDCNSLNGVLQCTCEDSYTWFPPSCLDPQNCYLHTAGALPSCECHLNNLSQSVNFCERTKIWGTFKINERFTNDLLNSSSAIYSKYANGIEIQLKKAYERIQGFESVQVTQFRNGSIVAGYEVVGSSSASELLSAIEHVAEKAKTALHKLFPLEDGSFRVFGKAQCNDIVFGFGSKDDEYTLPCSSGYRGNITAKCESSGWQVIRETCVLSLLEELNKNFSMIVGNATEAAVSSFVQNLSVIIRQNPSTTVGNLASVVSILSNISSLSLASHFRVSNSTMEDVISIADNILNSASVTNWTVLLREEKYASSRLLETLENISTLVPPTALPLNFSRKFIDWKGIPVNKSQLKRGYSYQIKMCPQNTSIPIRGRVLIGSDQFQRSLPETIISMASLTLGNILPVSKNGNAQVNGPVISTVIQNYSINEVFLFFSKIESNLSQPHCVFWDFSHLQWNDAGCHLVNETQDIVTCQCTHLTSFSILMSPFVPSTIFPVVKWITYVGLGISIGSLILCLIIEALFWKQIKKSQTSHTRRICMVNIALSLLIADVWFIVGATVDTTVNPSGVCTAAVFFTHFFYLSLFFWMLMLGILLAYRIILVFHHMAQHLMMAVGFCLGYGCPLIISVITIAVTQPSNTYKRKDVCWLNWSNGSKPLLAFVVPALAIVAVNFVVVLLVLTKLWRPTVGERLSRDDKATIIRVGKSLLILTPLLGLTWGFGIGTIVDSQNLAWHVIFALLNAFQGFFILCFGILLDSKLRQLLFNKLSALSSWKQTEKQNSSDLSAKPKFSKPFNPLQNKGHYAFSHTGDSSDNIMLTQFVSNE
Protein: Prolyl aminopeptidase (C6L823)
Organism: Aspergillus oryzae (Yellow koji mold)
Interaction partners:
Sequence:
MAAKLVDKKLHNVPGKLRVAELLFDVPVNYSRPNDGTLRLFARSVRRLTTSFDAPKEDKQLPWLVYLQGGPGYGCRPPQENGWIGTALDKGYQVLFLDQRGTGLSSTISAGTLALKGNAIKQAEYLKNFRADNIVRDCEAVRRCLTVDYPEDKRKWSIIGQSFGGFCAVTYLSIFPEGLAEAFICGGLPPLVNDPDPVYARTYEKLEERNKAYYSKFPEDVERVKRIMQYLEENDVSVPSGRLTPARFQQLGLIFGMHGGLDSIHELVLRAWNDLEIFGFLTHPTRTSIDAAGGFDGAVIYAILHESIYCQGQASNWSADRLRSANANFSIDASRPEIWFTGEMIYKDMFDSYDELNEIKEAADILATTKDWPALYDEAQLAKNEVPVYAATYIDDMYVHFSHASNTAAKIKGIKQFITNTMYHNALRAKSDEVMQQLFALRDDSID
Protein: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase (GlcNAc-Ins deacetylase) (EC 3.5.1.103) (N-acetyl-1-D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase) (P9WJN3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol (MSH) biosynthesis pathway. Shows some amidase activity toward S-conjugates of mycothiol.
Interaction partners:
- L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
- D-inositol 3-phosphate glycosyltransferase
- Mycothiol acetyltransferase
- Uncharacterized protein Rv0963c
- Integral membrane protein
- Thioredoxin-like reductase Rv2466c
Sequence:
MSETPRLLFVHAHPDDESLSNGATIAHYTSRGAQVHVVTCTLGEEGEVIGDRWAQLTADHADQLGGYRIGELTAALRALGVSAPIYLGGAGRWRDSGMAGTDQRSQRRFVDADPRQTVGALVAIIRELRPHVVVTYDPNGGYGHPDHVHTHTVTTAAVAAAGVGSGTADHPGDPWTVPKFYWTVLGLSALISGARALVPDDLRPEWVLPRADEIAFGYSDDGIDAVVEADEQARAAKVAALAAHATQVVVGPTGRAAALSNNLALPILADEHYVLAGGSAGARDERGWETDLLAGLGFTASGT
Protein: Plasma membrane-associated coenzyme Q6 reductase PGA3 (EC 1.6.2.2) (Processing of GAS1 and ALP protein 3) (Q12746)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: NADH-dependent cytochrome b5 reductase that reduces coenzyme Q6 at the plasma membrane and mediates lifespan extension by calorie restriction by shifting fermentative to respiratory metabolism, probably through modulating the NAD(+)/NADH ratio.
Subcellular location: Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- Dihydroorotate dehydrogenase
- Cytochrome b5
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
Sequence:
MSKEDIEGTNILDEPVHGIYIPAALFVVGVAITTYMSGELKILWSLPILFMIIFVRAYSAYKRRRSLYPDRWTSLELEDQTIISKNTALYRFKLKTRLESLDIPAGHHVAVRVPIDGKQEVRYYNPISSKLESGYLDLVVKAYVDGKVSKYFAGLNSGDTVDFKGPIGTLNYEPNSSKHLGIVAGGSGITPVLQILNEIITVPEDLTKVSLLYANETENDILLKDELDEMAEKYPHFQVHYVVHYPSDRWTGDVGYITKDQMNRYLPEYSEDNRLLICGPDGMNNLALQYAKELGWKVNSTRSSGDDQVFVF
Protein: G/T mismatch-specific thymine DNA glycosylase (EC 3.2.2.29) (Thymine-DNA glycosylase) (hTDG) (Q13569)
Organism: Homo sapiens (Human)
Function: DNA glycosylase that plays a key role in active DNA demethylation: specifically recognizes and binds 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) in the context of CpG sites and mediates their excision through base-excision repair (BER) to install an unmethylated cytosine. Cannot remove 5-hydroxymethylcytosine (5hmC). According to an alternative model, involved in DNA demethylation by mediating DNA glycolase activity toward 5-hydroxymethyluracil (5hmU) produced by deamination of 5hmC. Also involved in DNA repair by acting as a thymine-DNA glycosylase that mediates correction of G/T mispairs to G/C pairs: in the DNA of higher eukaryotes, hydrolytic deamination of 5-methylcytosine to thymine leads to the formation of G/T mismatches. Its role in the repair of canonical base damage is however minor compared to its role in DNA demethylation. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine.
Subcellular location: Nucleus {ECO:0000269|PubMed:8662714}.
Interaction partners:
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 2
- Growth arrest and DNA damage-inducible protein GADD45 alpha
- DNA
- Single-strand selective monofunctional uracil DNA glycosylase
- SUMO-conjugating enzyme UBC9
- Uracil-DNA glycosylase
- DNA repair nuclease/redox regulator APEX1
- DNA
- Methyl-CpG-binding domain protein 4
Sequence:
MEAENAGSYSLQQAQAFYTFPFQQLMAEAPNMAVVNEQQMPEEVPAPAPAQEPVQEAPKGRKRKPRTTEPKQPVEPKKPVESKKSGKSAKSKEKQEKITDTFKVKRKVDRFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIERNMDVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYGENPCSSEPCGFSSNGLIESVELRGESAFSGIPNGQWMTQSFTDQIPSFSNHCGTQEQEEESHA
Protein: MAP kinase kinase MKK2/SSP33 (EC 2.7.12.2) (P32491)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine protein kinase involved in a signal transduction pathway that plays a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involves the kinase PKC1 that may act on the BCK1 kinase that then phosphorylates MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase.
Interaction partners:
- Serine/threonine-protein kinase BCK1/SLK1/SSP31
- Mitogen-activated protein kinase SLT2/MPK1
- MAP kinase kinase MKK1/SSP32
- Serine/threonine-protein kinase KDX1
- Protein SPA2
- GTP-binding protein RHO1
- Serine/threonine-protein kinase STE11
- Transcription factor RLM1
- Protein SLG1
- RHO1 GDP-GTP exchange protein 2
Sequence:
MASMFRPPESNRSHQKTPKLTLPVNLVQNAKSTNDGQHLNRSPYSSVNESPYSNNSTSATSTTSSMASNSTLLYNRSSTTTIKNRPVPPPLPPLVLTQKKDGIEYRVAGDSQLSERFSNLHVDITYKELLSSAPISTKLSNIDTTFIKKDLDTPEGEDSYPSTLLSAYDFSSSGSNSAPLSANNIISCSNLIQGKDVDQLEEEAWRFGHLKDEITTLGILGEGAGGSVAKCRLKNGKKVFALKTINTMNTDPEYQKQIFRELQFNKSFKSDYIVQYYGMFTDEQSSSIYIAMEYMGGKSLEATYKNLLKRGGRISERVIGKIAESVLRGLSYLHERKVIHRDIKPQNILLNEKGEIKLCDFGVSGEAVNSLAMTFTGTSFYMAPERIQGQPYSVTCDVWSLGLTLLEVAGGRFPFESDKITQNVAPIELLTMILTFSPQLKDEPELDISWSKTFRSFIDYCLKKDARERPSPRQMLKHPWIVGQMKKKVNMERFVKKCWEKEKDGI
Protein: T cell receptor gamma constant 1 (P0CF51)
Organism: Homo sapiens (Human)
Function: Constant region of T cell receptor (TR) gamma chain that participates in the antigen recognition. Gamma-delta TRs recognize a variety of self and foreign non-peptide antigens frequently expressed at the epithelial boundaries between the host and external environment, including endogenous lipids presented by MH-like protein CD1D and phosphoantigens presented by butyrophilin-like molecule BTN3A1. Upon antigen recognition induces rapid, innate-like immune responses involved in pathogen clearance and tissue repair. Binding of gamma-delta TR complex to antigen triggers phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs) in the CD3 chains by the LCK and FYN kinases, allowing the recruitment, phosphorylation, and activation of ZAP70 that facilitates phosphorylation of the scaffolding proteins LCP2 and LAT. This lead to the formation of a supramolecular signalosome that recruits the phospholipase PLCG1, resulting in calcium mobilization and ERK activation, ultimately leading to T cell expansion and differentiation into effector cells. Gamma-delta TRs are produced through somatic rearrangement of a limited repertoire of variable (V), diversity (D), and joining (J) genes. The potential diversity of gamma-delta TRs is conferred by the unique ability to rearrange (D) genes in tandem and to utilize all three reading frames. The combinatorial diversity is considerably increased by the sequence exonuclease trimming and random nucleotide (N) region additions which occur during the V-(D)-J rearrangements.
Subcellular location: Cell membrane {ECO:0000305}.
Interaction partners:
Sequence:
DKQLDADVSPKPTIFLPSIAETKLQKAGTYLCLLEKFFPDVIKIHWQEKKSNTILGSQEGNTMKTNDTYMKFSWLTVPEKSLDKEHRCIVRHENNKNGVDQEIIFPPIKTDVITMDPKDNCSKDANDTLLLQLTNTSAYYMYLLLLLKSVVYFAIITCCLLRRTAFCCNGEKS
Protein: DnaJ protein ERDJ7 (Chaperone protein dnaJ C79) (OsDjC79) (Endoplasmic reticulum dnaJ domain-containing protein 7) (OsERdj7) (Q2QUP1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May play a role in protein folding in the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24153418}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Os01g0757900 protein
- Heat shock 70 kDa protein BIP3
- Heat shock 70 kDa protein BIP1
- Heat shock 70 kDa protein BIP2
- Heat shock 70 kDa protein BIP5
- Heat shock 70 kDa protein BIP4
Sequence:
MSQVGSAGEGSNSMAAAPPPRLLLLVVLLLVPVSNAIYCEEDDCYDLLGVKQDANVSEIKKAYYKLSLKHHPDKNPDPESRKLFVKIANAYEILKDESTRGQYDYAIAHPEEVFYNTAQYYRAYYGHKTDPRAVLIGLLLIISAFQYLNQFGRYSKAIETVKQTPAYKNRLKALEFERTGGISSKKKGHKQMDKKVEEVLSNEVELQIQGVEKPSLWRLYGVQFILLPYSIGKVLSWKFCWFWRYRIKKLPYAWEDACYLTRMSLKIPANTWENIDDYRKENLVMKRLWEKNNMERYIAEMRKESKRRR
Protein: Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein) (P28065)
Organism: Homo sapiens (Human)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-4
- Proteasome subunit beta type-7
- Proteasome subunit alpha type-1
- Proteasome subunit beta type-10
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-7
- Proteasome subunit beta type-8
- Proteasome subunit beta type-2
- Proteasome subunit beta type-3
- Proteasome maturation protein
Sequence:
MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE
Protein: 2'-5' oligoadenylate synthetase 1H (E9Q326)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKNLSSTRIALCSTPAWRLDKFIEGHLLGDITFLTELRTDVNSISAFLKERCFQGAAHPMRVSRVVMGGSYNRYTVLKGRSEVDLLVFFNNLTCFDDQFKLQKEVIEEIQKHLCQFQQEKRLREKFKVQSSDQPNFRSVSFKLSYPKFQQEVEFHMQTAYDALYEVRRKENHNCEIYNKVYARLIRECTMLGKEGEFNICFMELQQDFLWKRPCELKNLICLVKHWYQLPDKKGFVFL
Protein: High-affinity nitrate transporter-activating protein 2.1 (OsNAR2.1) (Q6ZI50)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Acts as a dual component transporter with NTR2.1, NRT2.2 and NRT2.3. Required for high-affinity nitrate transport. Involved in the regulation of NRT2.1, NRT2.2 and NRT2.3 expression, and in both, HATS (high-affinity transport system) and LATS (low-affinity transport system) activities in plant roots. Imports nitrate with high affinity when expressed with NTR2.1, NTR2.2 or NTR2.3 in a heterologous system (Xenopus oocytes).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- High-affinity nitrate transporter 2.1
- High-affinity nitrate transporter 2.2
- High-affinity nitrate transporter 2.3
Sequence:
MARLAGVAALSLVLVLLGAGVPRPAAAAAAKTQVFLSKLPKALVVGVSPKHGEVVHAGENTVTVTWSLNTSEPAGADAAFKSVKVKLCYAPASRTDRGWRKASDDLHKDKACQFKVTVQPYAAGAGRFDYVVARDIPTASYFVRAYAVDASGTEVAYGQSSPDAAFDVAGITGIHASLKVAAGVFSTFSIAALAFFFVVEKRKKDK
Protein: Uncharacterized fimbrial-like protein ElfG (P75858)
Organism: Escherichia coli (strain K12)
Function: Part of the elfADCG-ycbUVF fimbrial operon, which promotes adhesion of bacteria to different abiotic surfaces.
Subcellular location: Fimbrium {ECO:0000305}.
Interaction partners:
- Uncharacterized fimbrial-like protein YcbU
- Probable fimbrial chaperone protein ElfD
- Probable outer membrane usher protein ElfC
- Uncharacterized fimbrial-like protein YcbV
- Uncharacterized protein YggM
- Uncharacterized fimbrial chaperone YcbF
- Uncharacterized protein YehI
- Fimbrial subunit ElfA
Sequence:
MQIIFGEKCVSLLRLFFAAVLMLWCAQTAAYSGQCHTTQGNPYIGVNFGVKTLEEEANTAGVVKDKFYQWNESNDYYVSCDCDKDNVRSGRWAFAADSPLVYLGDNWYKINDYLAAKVLLQVKGSSPTAVPFENVGTGGDTRWHICDPGGQRLGGQGASGNSGSFSLKILQPFVGSVVIPPMALARLYECYNIPAGDSCTTTGTPVLVYYLSGTINSLGSCSVNAGETIEVDLGDVFAANFRVVGHKPLGARTAELAIPVRCNTGNAGLVNVNLSLTATTDPSYPQAIKTSRPGVGVVVTDSQNNIISPAGGTLPLSIPDDADSIARMNVYPVSTTGVPPETGRFEATATVRINFD
Protein: Multicopper oxidase VdtB (EC 1.-.-.-) (Laccase vdtA) (Viriditoxin biosynthesis cluster protein B) (A0A443HK79)
Organism: Byssochlamys spectabilis (Paecilomyces variotii)
Function: Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity. The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer backbone of viriditoxin. The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC. The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis. The short-chain dehydrogenase/reductase VdtF then acts as a stereospecific reductase converting the pyrone to dihydropyrone via the reduction of the C3-C4 double bond. The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin. Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin. VdtB is responsible for the regioselective 6,6'-coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-viriditoxin at a ratio of 1:2. The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling. The highly reducing polyketide synthase VdtX is not involved in viriditoxin synthesis, but might possibly play a role in the production of additional metabolites not identified yet.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nitrate reductase
Sequence:
MPAYLLLLACNVLLVLGAHVQRELVLTWEEGAPNGQSRQMIKTNGQFPSPTLIFDEGDDVEIVVRNYMHENTTIHWHGILMQDTPWSDGVPGLSQKPIEPGESYVYRFTAYPPGQYWYHSHSRATLLDGLYGALFIRRKPGTAGPWAMISEDPEDIAAMERASNNPHIMMLSDWDYYNSTQYKEADANSRLQIFCVDSILLNGKGSVYCPGHQWLIDKQIPFMHKSWPNDTITDKGCFPFVPSTEGPWLADGNVSAIPPGLQEGCVPYSGPTEAIEVDPADRWASVNWIGGSTFKTLQPTIDEHEMWIYEVDGHYIEPRRADTFLIWAGERYSAMIRLDKKPMDYSIRVPDGGYSQMIAAFGILRYKNGDPNARQKPDRFGVTTISKPYFDYNAWPMRDAVFLDKLDLPPWPRKVPAAHGDDMHVLYLGKANSTWEFTLSGKKKYPPDRSAYEPLLYNVNSEQAHDDDLIIRTQNGTWQDIVLQVGHSPLWPVDFPHAVHKHANKYWRIGGGQGLWNYSSVEEAMADQPESFNMVNPPYRDTFLTEFTGAMWVVLRYQVTSPGAWLLHCHFEMHLDNGMAMAILDGVDKWPHVPPEYTQGFHGFREHELPGPAGFWGLVSKILRPESLVWAGGAAVVLLSLFIGGLWRLWQRRMQGTYYVLSQEDERDRFSMDKEAWKSEETKRM
Protein: Large ribosomal subunit protein uL22m (39S ribosomal protein L22, mitochondrial) (L22mt) (MRP-L22) (39S ribosomal protein L25, mitochondrial) (L25mt) (MRP-L25) (Q9NWU5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL4m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL36m
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein uL29m
Sequence:
MAAAVLGQLGALWIHNLRSRGKLALGVLPQSYIHTSASLDISRKWEKKNKIVYPPQLPGEPRRPAEIYHCRRQIKYSKDKMWYLAKLIRGMSIDQALAQLEFNDKKGAKIIKEVLLEAQDMAVRDHNVEFRSNLYIAESTSGRGQCLKRIRYHGRGRFGIMEKVYCHYFVKLVEGPPPPPEPPKTAVAHAKEYIQQLRSRTIVHTL
Protein: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit H) (NADH-plastoquinone oxidoreductase 49 kDa subunit) (NADH-plastoquinone oxidoreductase subunit H) (P0C336)
Organism: Oryza sativa subsp. indica (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01358}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01358}.
Interaction partners:
- NAD
- NAD
- NAD
- Uncharacterized protein
- Photosystem I iron-sulfur center
- NADH dehydrogenase iron-sulfur protein 4
- NADH-quinone oxidoreductase subunit L
- NADH dehydrogenase flavoprotein 2
- NAD-dependent epimerase/dehydratase domain-containing protein
- Plus3 domain-containing protein
Sequence:
MSLPLTRKDLMIVNMGPQHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNAPEFLENIQIPQRASYIRVIMLELSRIASHLLWLGPFMADLGAQTPFFYIFRERELIYDLFEAATGMRMMHNYFRIGGVAADLPYGWIDKCLDFCDYFLRGVIEYQQLITQNPIFLERVEGVGFISGEEAVNWGLSGPMLRASGIQWDLRKVDLYESYNQFDWKVQWQKEGDSLARYLVRIGEMRESIKIIQQAVEKIPGGPYENLEVRRFKKAKNSEWNDFEYRFLGKKPSPNFELSKQELYARVEAPKGELGIYLVGDDSLFPWRWKIRPPGFINLQILPQLVKKMKLADIMTILGSIDIIMGEVDR
Protein: glucuronosyltransferase (EC 2.4.1.17) (O17757)
Organism: Caenorhabditis elegans
Interaction partners:
- SXP/RAL-2 family protein Ani s 5-like cation-binding domain-containing protein
- C-type lectin domain-containing protein
Sequence:
MSTFWYALLLIIVYYSQTINGIERPKKVLVFMPISGHSHLKFMGTIANILQDEGYNVTLLLPILDEGLRDTTPLVRKIKNRILVEQSEELIEANAQFRAGGGRENTWVMNSGIIGFLKLGTKVANICKASCKNVFQNEDLINYLRDQRFDVAISEPLYTCGFALFDHLGIETTISTDSHLGLEVSKIAHGASISTSYLPAVFSSGSERMTLIGRAKNYVESYFNYYFNSKIYENELAGIEGIYKNGKGWRELSRKNAYMFVNSNPQMDIPSPRTSKFIEIGGISSGPVKQERLPEEYDRVLSLRKKNVLISFGTNAKSMFMSDDMKESLIKTFESMPDTTFIWKYENTTVDIVKQYNKRINNVMLTDWMPQTALLADPRLTLFVTHGGLGSTNEVAFSGKPSIMVPVFGDQTRNARMLERHEVALVLTKYDLTNFKKVRGTIRKMLNDKSYSMKAEKLAQMLRNQPESPKEIFIKYFNFVARFGKPHGLDSYAAEMSFIEFYYIDFMAILSIFSVALYMIVSKVLRASHNLTNLVSIKFKFD