wanglab/gogpt-training-data huggingface dataset:
Protein: L-malyl-CoA/beta-methylmalyl-CoA lyase (EC 4.1.3.24) ((3S)-malyl-CoA/beta-methylmalyl-CoA lyase) (B6E2X2)
Organism: Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Function: Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to beta-methylmalyl-CoA.
Interaction partners:
Sequence:
MSFRTQPPAPARLNRCQLFGPGSRPAIFEKMAQSAADVINLDLEDSVAPDDKPQARRNIIEASHNIDWGNKYLSVRINGLDTPFWYRDVVELLEDGSERIDQIMIPKVGCAADVYAVDALVTAIEAAKGRKKRISLEVIIESAAGIAHVEEIAAASPRLQAMSLGAADFAASMGMATTGIGGTQENYYMLHAGVKHWSDPWHWAQAAIVAACRTHGILPVDGPFGDFSDDEGFRAQALRSATLGMVGKWAIHPKQVALANEVFTPSDAAVAEAREILAAMEKAKAEGAGATVYKGRLVDIASIRQAEVIVRQAEMAKV
Protein: FIIR2 protein (Q9S573)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MMIPQTLTNTNLFIDGVSFAGDVPSLTLPKLAVKTEQYRAGGMDAPVSIDMGLEAMEAKFSTNGARREALNFFGLADQSAFNGVFRGSFKGQKGASVPVVATLRGLLKEVDPGDWKAGEKAEFKYAVAVSYYKLEVDGREVYEIDPVNGVRAINGVDQLAGMRNDLGL
Protein: Vacuolin-C (Q54WZ3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MIESKIPSQFSINSHNNVCEASSYSDHSFDDNTQSIPLSQVVIRSDFANETSERQSKIIIERFNQGIKNPAFTDSPALGRAFPRLDSSYFALSNRDKVAELFDPRGQRFSTVYSADPTTIIEYNGGIPKTSRYFTLYGKTVLNVPSGHFAKALSKNRPVIYGEGPHVIIDPTFIFDEATGFVNQQEPFINHSTINVLRVPSGKVAKVWVGTQPLILESRREPYVFVDAQFKVVEQIGSQDKYFHNSSATFMEHGSIKRIIPHTGEVAVTYNNGVLEIIQTPKDGKPVIIDSPTHNFECFIQTSLQTCLFPSNETKQQAIKDNKNATSDEVNLKIFQTRDSLRVGVVLVIAFRIIDPQIALTKLGKEGIINHIENISFADMGKAIQLSTLQEIMYFNDTKPSATIDASAQTIQDRVKSHLARDLYEYGIELARLQIETIKVLDTEIAKKLAGQSVTSAEFTTKQATLVKEYDIKTTEARLKAETDNIALEQKGIAIIAEAQAKLESAKKQAEALLVTANAQKKVQEIQGELYSKFPILAEIELAKIKSEALKSSTLYITPQDAGNFMNSPFFFMERMLGKQQTNIKS
Protein: Ribonuclease A a1 (Q5GAM6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MEMSLRPLLLVFVLGLVSTPSTLAQDDPRYTKFLTQHYDAKPKGRDARYCESMMRRRGLTSPCKEVNTFIHGNKGSIKAICGANGSPYGENLRISQSPFQITTCKHTGGSPRPPCRYRASAGFRHVVIACENGLPVHFDESFISL
Protein: Double-strand-break repair protein rad21 homolog, putative (Q57XR0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- SCD domain-containing protein
- Sister chromatid cohesion protein
- Structural maintenance of chromosomes protein
- DNA polymerase eta
- separase
- Uncharacterized protein
- Sister chromatid cohesion protein
- Structural maintenance of chromosomes protein
Sequence:
MFYSTYVLTKDGPLAKIWLAAHWERRITRSDVRLMDLRKCVVDIVQPVVPIALRTSGELLVGVVRIYAVKVHGLKKDAENAILLIRVASPQANAGHFKKAAPGTGTAALLNGDAEAATFNWGGRRVGRTQGVVGIRAAGINGSHEEALEARFDEIADLLQGPVCALGGVNDHVRNGIDSTTMTGSVWYTWNSGSQGTEDLNGTQQDYDGFEMVRADIQAFGDNVSETSSRKSSLPSIERGRSSALTAAGGALGDFMPLPQPAYDLDIGAPLPDDGDAAILPDFMPPALGVDEAADPFLSAYGADNELNAALTQQQNSSRRHRAAGATTTKMLDKENTTVSGEAVRRWMENRNDIVEAAPRRGPLDQQEIQDRRVLAQDFNKGELWAAVDGSPLARVAGPALTASYIDAVKPLVEKQMEEEAAEREARQQREKNAHVVDENPDEFIIAGDSGDMFMDENFMQSGRKRDREEMEGNDNGESNVGGGASRRQSEAVALATLKHIRNLLSKSQGKGKGKAASGKKSKALPREHCTLHELCEGMARREAARTFVSVLTLASKQLVWAKQAPNDVELGLTNAASEVQLTV
Protein: DNA primase large subunit (F4HRU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEVIRSQKRTVSNDVVSTPTLPLYLTAPHMEVRLEEFELFAIDRLRVLKGVSDGLARARNPNEMDDLVETLWKEHMRLSNVSEMINKDIISHFVLRLVYCRSDELKKWFLSMETALFRHRFRLKKIEEQRAIVGEFGLPYKAVIGAELESLKERLGLVARSHGQISSDGTCNMLYFDPMFTLSHLAVKLVPFLMEKFLSFLSFAVENIYYKVPFEEVPDLVASRRVLLQKGFAFVAGTQLVSLVVTQFRSHLSKALILTNRKWTTTIREREKDRLTPIVEALSTSYLGPDYSQSNEYADISLKDIDQVSKSSFPLCMRHLFEKLREDHHLKHGGRMQLGLFLKGVGLKLDDALAFWREEFTKKVGSERFDKEYAYAIRHNYGKEGKRTDYTPYACSKIITSAPGAGDHHGCPYRHFSEDNLKAALSRMGLSSRGMEDVMDKVRNRHYQLACTLTFEAVYGTSCDTGINHPNQYFEESQKILKSKTPAAPV
Protein: Mediator of RNA polymerase II transcription subunit 19 (Mediator complex subunit 19) (Q9VVL6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 6
Sequence:
MMSNYGNMMDSPKSSPHGGGRSPVVARQDSSGTLKTTISLGKTPTIIHTGPFYSMKEPPAKAELTGDKDLMTEYGLHHTLTKFKEKKFKESLASFLQNIPGINDLITHPVENSTLRSVIEKPPIGGKELLPLTPVQLAGFRLHPGPLPEQYRTTYVTPARKHKNKHKKQKHKDGVTTGQESTLLDSAGLETYEKKHKKQKRHEDDKERKKRKKEKKRKKKNQSPEPGVGLLPGGASLGGAAGVMGATSLGSLGGGPGGPGLSSLSASMGPGVVGNMNSFSSSMQMQQQQQMPMQQQQMSSGGLLGSVLGTSGGPGGGGGGGGGGGGGVGGSLLMSQF
Protein: Chaperone protein PapD (P15319)
Organism: Escherichia coli
Function: Binds and caps interactive surfaces on P pilus subunits to prevent them from participating in non-productive interactions. Facilitates the import of P pilus subunits into the periplasm, probably also facilitates their folding. Chaperone-subunit complexes are then targeted to the PapC outer membrane usher where the chaperone must uncap from the subunits. Coexpression of this chaperone with individual, otherwise toxic, P pilus subunits (tested with PapA, PapE and PapG) suppresses their growth inhibitory phenotype.
Subcellular location: Periplasm {ECO:0000269|PubMed:9351822}.
Interaction partners:
Sequence:
MIRKKILMAAIPLFVISGADAAVSLDRTRAVFDGSEKSMTLDISNDNKQLPYLAQAWIENENQEKIITGPVIATPPVQRLEPGAKSMVRLSTTPDISKLPQDRESLFYFNLREIPPRSEKANVLQIALQTKIKLFYRPAAIKTRPNEVWQDQLILNKVSGGYRIENPTPYYVTVIGLGGSEKQAEEGEFETVMLSPRSEQTVKSANYNTPYLSYINDYGGRPVLSFICNGSRCSVKKEK
Protein: Histone chaperone RTT106/FACT complex subunit SPT16-like middle domain-containing protein (Q388G3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- FACT complex subunit
- Cell division control protein 73 C-terminal domain-containing protein
- RNA polymerase-associated protein CTR9
- Transcription initiation protein, putative
- Uncharacterized protein
- Spt4/RpoE2 zinc finger domain-containing protein
- Casein kinase II subunit beta
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase subunit beta
Sequence:
MSSLAGVAAALAAPPVENWGQLSWIDDQHKGQSDVKQLKEEEDEGKKTVLQPVLKLLSLPKRQQQNSGAPANAAQKPIIQIPVSAISSVTATTKNDLSILLQPQASVTAVPGANVSLELTSVRFAIPNVCVGHERTEEAGREVLAEAQERLREHQRRVLGGNGAMGAGPGDQALMAMGGGRREDECVIAVFDDLTLSFPSGRFKLIVTNYTLLLEERKRAGGDGGIVTMVPLTDVVQLYLCDIPTSRNTSNKSVDAEDDTDFPQYVVVILRNPVKVRATTYNHIVITCPVGFVLDEQHAWSCELKTQEEIDRVLSSLPHKQSAAKDATQQQAAKGDTFPPTITGRVSELLIRVLKTIAGVKALGGHNKDYQTRNGNSVLRCLYQSNEGLLYVLQSALLFLHRPATRISYGDIQRIEVDESERGSTTFQMTVYGNLGKRARGGADKVTIASLPITEKEALLTYLQSKVEVVRTGAALEDSDGDDDDDSGDGEDDESSDEEDSFDDDDDDDDDDDDDDDDGADRKKRKRSSSKRDESGKRRDKEHKHGRHKKHKKDH
Protein: Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta (GMP-PDE delta) (Protein p17) (O43924)
Organism: Homo sapiens (Human)
Function: Promotes the release of prenylated target proteins from cellular membranes. Modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location. Required for normal ciliary targeting of farnesylated target proteins, such as INPP5E. Modulates the subcellular location of target proteins by acting as a GTP specific dissociation inhibitor (GDI) (By similarity). Increases the affinity of ARL3 for GTP by several orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:9712853}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9712853}; Peripheral membrane protein {ECO:0000269|PubMed:9712853}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24166846}.
Interaction partners:
- X-linked retinitis pigmentosa GTPase regulator
- GTP-binding protein Rheb
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- ADP-ribosylation factor-like protein 2
- ADP-ribosylation factor-like protein 3
- ADP-ribosylation factor-like protein 13B
- GMP reductase 1
- Guanylate kinase
- GMP synthase
- Inosine triphosphate pyrophosphatase
Sequence:
MSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVSRELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPASVLTGNVIIETKFFDDDLLVSTSRVRLFYV
Protein: Phosphoesterase (EC 3.1.4.-) (A0A0H2URP5)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MAKQTIIVMSDSHGDSLIVEEVRDRYVGKVDAVFHNGDSELRPDSPLWEGIRVVKGNMDFYAGYPERLVTELGSTKIIQTHGHLFDINFNFQKLDYWAQEEEAAICLYGHLHVPSAWLEGKILFLNPGSISQPRGTIRECLYARVEIDDSYFKVDFLTRDHEVYPGLSKEFSR
Protein: NADP-dependent malic enzyme 2 (AtNADP-ME2) (NADP-malic enzyme 2) (EC 1.1.1.40) (Q9LYG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19725876}.
Interaction partners:
- Malate synthase
- Pyruvate, phosphate dikinase 1, chloroplastic
- Fumarate hydratase 1, mitochondrial
- Fumarate hydratase 2
- Malate dehydrogenase, chloroplastic
- Alanine aminotransferase 1, mitochondrial
- L-lactate dehydrogenase
- D-lactate dehydrogenase [cytochrome], mitochondrial
- Glutamate--glyoxylate aminotransferase 1
- Acetolactate synthase, chloroplastic
Sequence:
MGSTPTDLPGEDVADNRSGVGGGISDVYGEDSATLDQLVTPWVTSVASGYTLMRDPRYNKGLAFTDKERDAHYLTGLLPPVILSQDVQERKVMHNLRQYTVPLQRYMALMDLQERNERLFYKLLIDNVEELLPVVYTPTVGEACQKYGSIFRKPQGLYISLNEKGKILEVLKNWPQRGIQVIVVTDGERILGLGDLGCQGMGIPVGKLSLYTALGGIRPSACLPITIDVGTNNEKLLNDEFYIGLKQRRATGQEYAEFLHEFMCAVKQNYGEKVLVQFEDFANHNAFDLLSKYSDSHLVFNDDIQGTASVVLAGLIAAQKVLGKKLADHTFLFLGAGEAGTGIAELIALKISKETGAPITETRKKIWLVDSKGLIVSSRKESLQHFKQPWAHEHKPVKDLIGAVNAIKPTVLIGTSGVGQTFTKEVVEAMATNNEKPLILALSNPTSQAECTAEQAYTWTKGRAIFGSGSPFDPVVYDGKTYLPGQANNCYIFPGLGLGLIMSGAIRVRDDMLLAASEALAAQVTEEHYANGLIYPPFSNIREISANIAACVAAKTYDLGLASNLPRAKDLVKFAESSMYSPVYRNYR
Protein: F-box/WD repeat-containing protein 10 (F-box and WD-40 domain-containing protein 10) (Ubiquitin ligase-specificity factor) (Q5XX13)
Organism: Homo sapiens (Human)
Function: Probable substrate-recognition component of a SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Overexpression is leading to degradation of CBX5 and CBX1.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
Sequence:
MENLESRLKNAPYFRCEKGTDSIPLCRKCETCVLAWKIFSTKEWFCRINDISQRRFLVGILKQLNSLYLLHYFQNILQTTQGKDFIYNRSRINLSKKEGKVVKSSLNQMLDKTVEQKMKEILYWFANSTQWTKANYTLLLLQMCNPKLLLTAANVIRVLFLREENNISGLNQDITDVCFSPEKDHSSKSATSQVYWTAKTQHTSLPLSKAPENEHLLGAASNPEEPWRNSLRCISEMNRLFSGKGDITKPGYDPCNLLVDLDDIRDLSSGFSKYRDFIRYLPIHLSKYILRMLDRHTLNKCASVSQHWAAMAQQVKMDLSAHGFIQNQITFLQGSYTRGIDPNYANKVSIPVPKMVDDGKSMRVKHPKWKLRTKNEYNLWTAYQNEETQQVLIEERNVFCGTYNVRILSDTWDQNRVIHYSGGDLIAVSSNRKIHLLDIIQVKAIPVEFRGHAGSVRALFLCEEENFLLSGSYDLSIRYWDLKSGVCTRIFGGHQGTITCMDLCKNRLVSGGRDCQVKVWDVDTGKCLKTFRHKDPILATRINDTYIVSSCERGLVKVWHIAMAQLVKTLSGHEGAVKCLFFDQWHLLSGSTDGLVMAWSMVGKYERCLMAFKHPKEVLDVSLLFLRVISACADGKIRIYNFLNGNCMKVLKANGRGDPVLSFFIQGNRMVVNTESNVLMFQFEHIKWQYAVEKTKQKKNKEKEEEKEENSLMEILSKCNIQVHSPRESVSSKQTVIQELLPGKPPKSRVLLKPAKFSSAVLIEELQSQGKSKSPRRDADDVEKAQKQGQLETPGKLPSHPKKKSWKIPMSPDQFLLTVSALQHAHNSGEFAYPCRPQTEITDVWGPSISYPRKVLNFKGKSIQRAVDRLRLSNPPIDVKRTSIPLEIQKLQPNLKISLHSPRVQSTIPQPMIIRSRFSGSLKGGDQVTSSIERAVCSTGPLTSMQVIKPNRMLAPQVGTATLSLKKERPRIYTALDPFRVNTEFVLLTVKEEKEHQEAKMKEYQARESTGVVDPGKVSKAAWIRKIKGLPIDNFTKQGKTAAPELGQNVFI
Protein: RIM-binding protein, isoform J (A0A0B4KGQ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYESMHHHQSAAAAVAAGTTPNGMLDALSLQLRDAEMRRTEIERAHQETLAQIRNLSGSARPDAEAVENLQSRARELEKKVALENVRCEELQIELTSALKAKQASRSACSGMGSVSSGGGATIPTSASSSTVTWAPTISHQDQGSEIDIIMAKIEQDNRVLAELEQPRTSASASMSALPPSSMLSTVNSEFRTISKSELEEELNRYKRAVLGGSGGGGGGVGGGGGGVSALSSGYSSLPQSLASTLPNGGASTSLSGTSLGSHSAAAAAAAHSVSAGSGGVVGGGGQGGLSSISALVPNSISGISSSLSSHAIQSMQYGTGQTSVEKLLSGTSGITGIPPLPVNIHTMKAMPTALSQRGTIQLYNLQSTTMPLLSLNSHNLPPAGSTSYSALGAGGGTSLTHPTMANLGLLDTGTLLGSTGLSGLGVGPSVGGITGATSLYGLSGGGGGAGGLGSSYGPPFLDVASSASYPFTAAALRQASKMKMLDEIDIPLTRYNRSSPCSPIPPNNWGLDEFTDGLSVSMMHNRGGLALGALDLDTRNHGLNGASEPQVDMLDIPGKGRCCVFIARFPYDPPEEAEGELSLCAGDYLLVWTSGEPQGGYLDAELLDGRRGLVPASFVQRLVGDDLLEFHQAVLSTLRDAEDGSMQCDTTSLPSLPPHNPLLTHTHEDLARLSETHTDLEHDQDDISDNVPAPKHLTLERQLNKSVLIGWSPPEPVGYNLIDSYHVYVDGVLKVTVKANERTRALIEGVDSTRPHRISVRSVTQNRQTSRDAACTMIIGRDTAHLGPSAVRASHITCSSAVISWLPANSNHQHVVCVNNVEVRTVKPGMYRHTITGLAPSTQYRVTVRAKHLRAVGQHAANVGQTGGAGRPGQEEAPGAYADFRTLTKGLPDPPQEIQLEAGPQDGTILVTWQPVNRPTSTGPVTGYAVYADGKKVTDINSPTGDHALIDIGKLGVFNPRAVTIRTKSRDSQSADSAPILIPNTVRNAVARRGPNQMGMGPQLPQGPHGMTVQQQMGGMPGQPGQQGQHMMGGQQDHGQYDPNQMQQQQQQQGQPGQPGHQGYQPGQPGAQRGMVPIPGRPQGPQQQQQQPYGPQGPMGGPRFRGPVPGQLNMQGQQMQGQMQGQMQGQMQGQMSGQMPGQMPGQMPGQMPGQMAGQMAGQMPGQMPGQMPGQMSGQMPGQMMGPRGPLNQQQQQQQQMQQGQMMPGQQAGQQQAQPGQPGQPGQMPGAQKKPRYFVAMFDYDPSTMSPNPDGCDEELPFQEGDTIKVFGDKDADGFYWGELRGRRGYVPHNMVSEVEDTTASMTAGGQMPGQMPGQMGQGQGVGVGGTAQVMPGQGAPQQSMRNVSRDRWGDIYANMPVKRMIALYDYDPQELSPNVDAEQVELCFKTGEIILVYGDMDEDGFYMGELDGVRGLVPSNFLADAPDQYNNQMGPGGVAGRGGLSQRGRGQGPGARGPPPPPRDNMMPGMGGRGQPGKNARPASPTLLDNTGHPAPDHQTQGMIGRVGNVGLQQQQQQQQQQQQLQQQQQYGQQQTQMGQQQQQQQQMGQPGMMGQQMGQPMGQQMGQMGQMGQMGQQQMGQQQMGQQQQPPTTQAQTGGLFSGATSLLSGATSAATGGLFGSKQPPKTDPMQPQGGVQPAQQQANAFGAQQPGMGMQQQGGMQSGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQPGMQQQQQQPQQVPPQAQAPPPGPGAGLLGGLKGIAAAAPGGDVLSKGKDLFGKFGFGFGK
Protein: Beta-theraphotoxin-Cm1b (Beta-TRTX-Cm1b) (CcoTx-II) (Ceratotoxin-2) (CcoTx2) (P84508)
Organism: Ceratogyrus marshalli (Straighthorned baboon tarantula) (Ceratogyrus cornuatus)
Function: Inhibits several voltage-gated sodium channels and only one voltage-gated calcium channel (Cav2.2/CACNA1B (IC(50)=1.1 uM) and Nav1.2/SCN2A (IC(50)=3.7-80 nM), Nav1.3/SCN3A (IC(50)=88-5570 nM), Nav1.1/SCN1A (IC(50)=170-407 nM), Nav1.7/SCN9A (IC(50)=95.5-230 nM), Nav1.6/SCN6A (IC(50)=49.9-3990 nM), Nav1.4/SCN4A (IC(50)=113-400 nM or >10 uM), Nav1.5/SCN5A (IC(50)=1524-1634 nM or >10 uM)). The toxin acts by shifting the voltage dependence of channel activation to more depolarized potentials and by blocking the inward component of the sodium current. It shows moderate affinity for lipid bilayers without cholesterol and high affinity for lipid bilayers containing cholesterol. In vivo, this toxin causes general ataxia, lack of response to stimuli, and semiparalysis. After a few minutes, the mice are unable to stand, and breathing is reduced in rhythm and intensity. Symptoms gradually increase with progressive slowing of breathing and flaccid paralysis; death occurred within 10 to 20 minutes post injection. Animals remain totally flaccid, and no symptoms of excitatory neurotoxicity are observed.
Subcellular location: Secreted {ECO:0000269|PubMed:16267209}.
Interaction partners:
Sequence:
DCLGWFKSCDPKNDKCCKNYTCSRRDRWCKYYL
Protein: Endonuclease 8 1 (DNA glycosylase/AP lyase Nei 1) (EC 3.2.2.-) (DNA-(apurinic or apyrimidinic site) lyase Nei 1) (EC 4.2.99.18) (Endonuclease VIII 1) (P9WNB9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. DNA glycosylase that recognizes and removes damaged pyrimidines. Excises Tg:A (thymine glycol, prefers 5R isomers), Tg:G, 5,6-dihydrouracil:G base pairs and urea:A, also excises oxidized purine derivatives guanidinohydantoin:C and spiroiminodihydantoin:C. Poorly cleaves dsDNA with uracil substitutions, thus also acting as a weak uracil-DNA glycosylase. Acts on DNA bubble and 3'-fork structures, suggesting a role in replication-associated DNA repair. Activity on 7,8-dihydro-8-oxoguanine (8-oxoG) is debated; a report shows weak activity, whereas another shows none. Has AP (apurinic/apyrimidinic) activity and introduces nicks in dsDNA strand, inefficiently cleaves ssDNA with AP sites and uracil. Probably cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Cleaves ssDNA containing an AP site. Complements an E.coli fpg mutY but not nei nth double mutant.
Interaction partners:
- Endonuclease 8 2 lyase Nei 2)
- Endonuclease III lyase)
- Ribose-5-phosphate isomerase B
- DNA polymerase I
- Probable ATP-dependent helicase Lhr
- Adenine DNA glycosylase
- Thioredoxin-like reductase Rv2466c
- Aminopeptidase N
Sequence:
MPEGHTLHRLARLHQRRFAGAPVSVSSPQGRFADSASALNGRVLRRASAWGKHLFHHYVGGPVVHVHLGLYGTFTEWARPTDGWLPEPAGQVRMRMVGAEFGTDLRGPTVCESIDDGEVADVVARLGPDPLRSDANPSSAWSRITKSRRPIGALLMDQTVIAGVGNVYRNELLFRHRIDPQRPGRGIGEPEFDAAWNDLVSLMKVGLRRGKIIVVRPEHDHGLPSYLPDRPRTYVYRRAGEPCRVCGGVIRTALLEGRNVFWCPVCQT
Protein: Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 (EC 1.8.1.-) (Q3TMV7)
Organism: Mus musculus (Mouse)
Function: Probable FAD-dependent oxidoreductase; involved in the cellular oxidative stress response (By similarity). Required for normal sarcomere structure and muscle fiber integrity (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:30345904}. Cytoplasm {ECO:0000269|PubMed:30345904}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:Q8WU10}.
Interaction partners:
- Protein orai-2
Sequence:
MEAPRPAGTFVVVGGGIAGVTCAEQLAVSFPEEDILLVTASPVIKAVTNFRQVSKVLEEFDVEEQPGTMLESRFPNIKVIESGVKQLKSEDHCIFTEDGREFVYKKLCLCAGAKPKLIYEGNPRVLGIRDTDSAQEFQKELAKARRIMIVGNGGIALELAYEIEGCEVVWAIKDNAIGNTFFDAGAAEFLTSKLMSEKSEAKIAHKRTIYTVEEAKKETRTKSKADYVGSALGPDWHGGLALKGTEEFSHSVHIETRCEVKKIYLEEEFKIMKKKSLAFPKDHHKSVTADKEMWPVYVELTNGTIYGCDFLVSATGVTPNVHPFLHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDICTACWQPSPVWQQMRLWTQARQMGYYAAKCMAAASMGHPIDMDFSFELFAHVTKFFNYKVVLLGKYNAQGLGADHELMLRCTRGQEYVKVVMQNGRMMGAVLIGETDLEETFENLILNQMDLSSYGEDLLDPNIDIEDYFD
Protein: RE59670p (Q86PD5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTWEPQGEGLQQIIAILKESQSPDTATKMAVQMKLEEFNRYPDFNNYLIYVLTKLKTEDEPTRSLSGLILKNNIRMHGTTLQPEIVEYIKHECLQAVGDASPLIRATVGILITTIASNGGLHNWPQLLPSLCEMLDNQDYNVCEGAFSALQKICEDSAEILDSAALNRPLNIMIPKFLEYFKHSSPKIRSHAIACINQFIINRSQALMLNIDSFIENLFHLSSDEDHEVRKNVCHGLVMLLEVRMDRLMPHMSQIIEYMLLRTQDTDEGVALEASEFWLSLAEQSICKDVLAPYLAQLAPVLVRGMRYSEVDIILLKGNVEEDDMVPDREEDIRPHFHKSRAHTIRSTQEGGAGATGDDDDDEFEDGMDDDSSLSEWNLRKCSAAALDVLANVFREDCLPVVLPILKETLFHQEWVIKESGVLALGAIAEGCMQGMIQHLPELIPYLISCLSDKKALVRSITCWTLSRYANWVVNQPHDQYLKPLMEELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLEYILKTLVFAFSKYQHKNLLILYDAVGTLADSVGHHLNKPQYIDILMPPLIDKWNLLKDDDKDLFPLLECLSSIATALQSGFLPYCDPVYRRCISLIEQTINQEMLCKQNQTYDHPDKERMIVALDLLSGLAEGLDRHIETLVANSNIMHLLYQCMQDVLPEVRQSSFALLGDLTKACFPHVHPFMADFFPILGQNLNPDFISVCNNATWAIGEICMKLGEETKQYIRLVLSDLFIIINRPNTPKTLLENTAITIGRLGYVCPVEVAPYLPEFVRQWCTSLRHIRDNDEKDSAFRGMCHMITVNPAGVVADFIFFCDAIASWVNPPEDLHQMIQKILHGFKTQVGEENWRRFVEQFPPTLAERLTTMYNI
Protein: Uridine phosphorylase 2 (UPase 2) (UrdPase 2) (EC 2.4.2.3) (Liver-specific uridine phosphorylase) (L-UrdPase) (Q8CGR7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (Probable).
Interaction partners:
- Cytidine deaminase
- Uridine phosphorylase 1
- Thymidine phosphorylase
Sequence:
MASILPASNRSMRPDKNTYERKRSVYVKNPYLEGMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFAQFMHKELRLEGDGEDIEDICAGTDRYCMFKTGPVLSVSHGMGIPSISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILDNVVTRSTELDKELANDLFNCSREIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAYRAGVRNIEMESTVFAAMCGLCGLRAAVVCVTLLDRLESDQINLSHDVLVEYQQRPQLLISNFIKKQLGLCDQMS
Protein: Dynamin-binding protein (Scaffold protein Tuba) (M0R4F8)
Organism: Rattus norvegicus (Rat)
Function: Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions in epithelial cells (By similarity). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (By similarity). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6XZF7}. Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:Q6TXD4}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6TXD4}. Synapse {ECO:0000269|PubMed:14506234}. Cell junction {ECO:0000250|UniProtKB:Q6XZF7}. Note=Localizes to the apical junction, colocalizes with TJP1. {ECO:0000250|UniProtKB:Q6XZF7}.
Interaction partners:
- Actin nucleation-promoting factor WASL
- Myc box-dependent-interacting protein 1
- Amphiphysin
- Amphiphysin
- Uncharacterized protein.
Sequence:
MEPGSVVRAIFDFCPSVSEELPLFVGDVIEVLTVVDEFWLLGKKEDVTGQFPSSFVEIVTIPSLKEGERLFVCTCDFISREPNSLSLHRGDLVIIDGTPTAGWLQGRSSLGARGFFPSSCIHELCLSSQSRQWHSQNMLLQVPEYSMGQARALMGLSAQLDEELDFREGDVITIIGVPEPGWFEGELEGRRGIFPEGFVELLGPLRTADESVNAGSGDDSTLNDEVDVSPEEVESEGDEDDQQAGTYGIALYRFQALESNELDFEVGDKIRILGTLEDGWLEGRLKGKTGIFPHRFVKLCPSNRSEETMALPQGDSFPKNSESSAGEMGDSVVEEARQDPQECEEETPDSGLPEQTSEEPLDHVAPECVVDKISGQDEDASGSSPDVDLEGPRAEDPSTPDLSQEVNGISSLPPQVPLQPEEEKSQHYLTAGGSRQCPDTFSKLFPLEAKTRNYSSLPPRRTYTQGWSLQKPAPHLHRASSLTASRVNRPGHFSHTAMASCAQKHQTSAENAASLCCAPERPKRRPGLPDKEPATEITPASQGDNLDLDSKLTQQLIEFEKSLSGPSTEPKKIVRRFSIMDFYSEKDIVRGSSNSLPSRNFPERRKALRPPPPRPHTPTSTSPHLLVDQSPKPGPPLVVRPSRPAPLPPPTQQRLNTASPKPTSCALPGWEAPEKEGSEYTEKSPAQLFPCPSVLARIQDVEHDLDMHTRAQEELNLLLEEKQDESLRAETLETLKSYESTIQSLNLELQQLREMTLLSSQSSSLAAPSGSVSTEKPEQRMLEKRAKVVAELLQTEKDYIRDLEMCVERVMVPLQQAQVPNIDFEGLFGNMQTVIKVSKQLLAALEITDAVGPVFLDHRDELEGTYRLYCQNHDEAISLLDIYEKDERIQKHLQDYLADLKSLYHEWGCTNYINLGSFLIKPVQRIMRYPLLLMELLNSTPESHPDKAPLTSAVLAIKEINANINEYKRRKDLVLKYRKADEDSLMEKISKLNIHSIIKKSSRVSSHLKHLTGFAPQLKDEAFEETEKNFRMQERLIKSFIRDLSLYLQHIRESACVKVVAAMSIWDLCMERGHHDLEQFEKVHRYISDQLFTRFKERTERLVINPLNQLLNMFTGPYKLVQKRFDKLLDFYNCTERAEKLKDKKTLEDLQSARNNYEALNSQLLDELPKFQQYAQSLFTNCIHGYAEAHCDFVQKALEQLQPLLSLLKASDREGNLIAIFHEEHSRVLQQLQVFTFFPEALPAPRKPFERKTTDRQSSRKALLGMPSYMLQSEELRSSLLARYPPEKLFHVQRNFNAAQDLDVSLLEGDLVGVIKKKDPMGSQNRWLVDNGVTKGFVYSSFLKPYNPRCSHSDSSVVSHSSTESEHSGSSPSFHRQNSSSALTFNSNSMTVSFTSGLPQKQPQDTSPLRECVPETLGVSSNTGNPETGPSPCPSDPGFSCQRRPGNPADGTREISQPASTLRGCQRRSLHSEVLGYPVPGRSDQGSDSIKGTSRACQTAGDRDRGLGSSEAEGNQVYFAIYTFKARNPNELTVLANQRLRILEFKDVTGNTEWWLAEVNGKKGYVPSNYIRKTEYT
Protein: Malate dehydrogenase, mitochondrial (EC 1.1.1.37) (P08249)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P04636}.
Interaction partners:
- Citrate synthase, mitochondrial
- Aspartate aminotransferase, mitochondrial
- Fumarate hydratase, mitochondrial
- Citrate synthase
- Malate dehydrogenase, cytoplasmic
- Aspartate aminotransferase, cytoplasmic
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Pyruvate carboxylase, mitochondrial
- ATP-citrate synthase
- NAD-dependent malic enzyme, mitochondrial
Sequence:
MLSALARPAGAALRRSFSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGVAADLSHIETRANVKGYLGPEQLPDCLKGCDVVVIPAGVPRKPGMTRDDLFNTNATIVATLTAACAQHCPEAMVCIIANPVNSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANTFVAELKGLDPARVNVPVIGGHAGKTIIPLISQCTPKVDFPQDQLATLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVDAMNGKEGVVECSFVQSKETECTYFSTPLLLGKKGLEKNLGIGKITPFEEKMIAEAIPELKASIKKGEDFVKNMK