wanglab/gogpt-training-data huggingface dataset:
Protein: 3-keto-L-gulonate-6-phosphate decarboxylase SgbH (KGPDC) (EC 4.1.1.85) (3-dehydro-L-gulonate-6-phosphate decarboxylase) (P37678)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. May be involved in the utilization of 2,3-diketo-L-gulonate.
Interaction partners:
- Putative L-ribulose-5-phosphate 3-epimerase SgbU
- L-xylulose/3-keto-L-gulonate kinase
- L-ribulose-5-phosphate 3-epimerase UlaE
- L-ribulose-5-phosphate 4-epimerase SgbE
- Probable L-ascorbate-6-phosphate lactonase UlaG
- 3-keto-L-gulonate-6-phosphate decarboxylase UlaD
- 2,3-diketo-L-gulonate-binding periplasmic protein YiaO
- 2,3-diketo-L-gulonate TRAP transporter large permease protein YiaN
- Ascorbate-specific PTS system EIIB component
- 2,3-diketo-L-gulonate TRAP transporter small permease protein YiaM
Sequence:
MSRPLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAGANWMTIICAAPLATVEKGHAMAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALSDIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDFHAQIDAIWGGARA
Protein: Tropomyosin alpha-1 chain (Alpha-tropomyosin) (Tropomyosin-1) (P09493)
Organism: Homo sapiens (Human)
Function: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress fibers. {ECO:0000250|UniProtKB:P04692}.
Interaction partners:
- Troponin T, cardiac muscle
- Troponin I, cardiac muscle
- Actin, alpha cardiac muscle 1
- Tropomyosin alpha-3 chain
- Tropomyosin beta chain
- Myosin-7
- Troponin T, slow skeletal muscle
- Tropomyosin alpha-4 chain
- Troponin C, slow skeletal and cardiac muscles
- Actin, alpha skeletal muscle
Sequence:
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Protein: D-galactose/methyl-galactoside binding periplasmic protein MglB (D-galactose-binding periplasmic protein) (GBP) (D-galactose/D-glucose-binding protein) (GGBP) (P0AEE5)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (Probable). In addition, binds D-galactose and D-glucose and plays a role in the chemotaxis towards these two sugars by interacting with the Trg chemoreceptor. Chemotaxis requires MglB, but not MglA or MglC.
Subcellular location: Periplasm.
Interaction partners:
- Galactose/methyl galactoside import permease protein MglC
- Galactose/methyl galactoside import ATP-binding protein MglA
- Methyl-accepting chemotaxis protein III
- Maltose/maltodextrin-binding periplasmic protein
- Probable ABC transporter permease protein YphD
- HTH-type transcriptional regulator GalS
- Ribose import permease protein RbsC
- L-arabinose transport system permease protein AraH
- Autoinducer 2 import system permease protein LsrD
- Ribose import ATP-binding protein RbsA
Sequence:
MNKKVLTLSAVMASMLFGAAAHAADTRIGVTIYKYDDNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGWDLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKVVRVPYVGVDKDNLAEFSKK
Protein: Precursor of CEP2 (PCEP2) [Cleaved into: C-terminally encoded peptide 2.1 (CEP2.1); C-terminally encoded peptide 2.2 (CEP2.2)] (Q3ECM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signaling peptide that represses primary root growth rate. Regulates negatively leaves number and flowering, and modulates leaf morphology. Regulates systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes involved in N uptake and assimilation pathways.
Subcellular location: [C-terminally encoded peptide 2.1]: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}. Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.; SUBCELLULAR LOCATION: [C-terminally encoded peptide 2.2]: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}. Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.
Interaction partners:
- Protein RALF-like 16
- Protein RALF-like 7
- FLYWCH-type domain-containing protein
- Aquaporin, putative
- Defensin-like protein 220
- At2g04830
- Putative F-box/kelch-repeat protein At3g22730
- Putative F-box protein At1g67450
- Alpha-soluble NSF attachment protein 1
- Protein DETOXIFICATION 5
Sequence:
MKLFIITVVTILTISRVFDKTPATTEARKSKKMVGHEHFNEYLDPTFAGHTFGVVKEDFLEVKKLKKIGDENNLKNRFINEFAPTNPEDSLGIGHPRVLNNKFTNDFAPTNPGDSPGIRHPGVVNV
Protein: Histone deacetylase 9-B (EC 3.5.1.98) (Q6PBI4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Devoided of intrinsic deacetylase activity, promotes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) by recruiting other histone deacetylases. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Histone deacetylase 7a.
- Histone deacetylase 1
- AT-rich interactive domain-containing protein 4B
- AT-rich interactive domain-containing protein 4A
Sequence:
MHNVNNSVDIKPEVPLALDPGSPLDLRTDIRMQGSASEVTVWERQLQQELLLIQKQQQIQKQLLITEFQKQHENLVRQHQAQIQEHLKLQQELHVMKQQQEQLEKERKLELQSQERELERHRREQQVLVLRNRERTRESLTGAVASNEVKQKLQEFLLSKSTKDITLNGIPQKITQSSKLWYTASHHTSLEQSSPPLGGASSSCKISLPSPQDYRDDFPLRKTVSEPNLKVRSRLKQKVAERRSSPLLRRKEGNIMTPFKKRALELLESTASSSAPGSGPSSPNGACSALGAENGPSSLPVTTRTERWPSQSRLLGPESSVSMLNLYTSPSLPNISLGFSAASSPISAALGLQEKHVDNGAVSAVIQGLPTQLLGPVPLSVMETKVSSSHQALLQHLLQKEQLRHQKILSSGQSPVHPPSPLAMMENSPSSTRPKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQNFLEKQKQYQQQVHINKMLSKSIEQLRQPNVHLQESEEEEGEDCQEHAMQEESSPSGGVIRKHSPQNTSRSPTIPLDSHPGVIRVKEEPGASDDETMANQSSYIHQVKGRMVIQAMI
Protein: Serpin 4 (Q8MPN8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDYRLVPCGCWLLPLLGLALFPFPPVHTADVTMADAAHQEFARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAYQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEPLKVSAIIHKAFIEVNEEGTEAAAATGMFMSLTSLPMPKPDPIRFNVDHPFTFYILNKDSTALFAGSIKKL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I5ZKL8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPQAAYCYLRVVGRGSYGEVTLVKHRRDGKQYVIKKLNLRNASSRERRAAEQEAQLLSQLKHPNIVTYKESWEGGDGLLYIVMGFCEGGDLYRKLKEQKGQLLPESQVVEWFVQIAMALQYLHEKHILHRDLKTQNVFLTRTNIIKVGDLGIARVLENHSDMASTLIGTPYYMSPELFSNKPYNYKSDVWALGCCVYEMATLKHAFNAKDMNSLVYRIIEGKLPPMPKVYSAELAELIRTMLSRRPEERPSVRSILRQPYIKHHISLFLEATKAKTSKNNVKNCDSRAKPVAAVVSRKEEPNHEMIPYQPRSSEGSAVHATGEDKCLSQEKPVDIGPLKSPASLEGHTGKQDMNRTAESCATVSRINIDILPAERRDSAKDGTVEEGRPQHVDASNEVDRQCSISQEKERLQGNSKSSDQPENLLPRWSSGGGDGEGNELVKLLYSSGKDQKPQQLQESPPRLVPSHPDTGKADIISTQQSDGNQSGPVARSVNGSRSSSTASSKDRPLSARERRRLKQSQEEMLPSGPAVQRTPSSVEPVKPQEEDQPIPAQRFSSDCNITQVNPTLLREKKRLIHGLSEDELSSSTSSTDKSDGDSREGKSHTNEMRDLVQLMTQTLRLEAKESCEDLHVPNPGSEFRLHRKYRDTLVLHGKAAEEGEPPCVELPPGITPGSEKIRRIVEVLRADVIQGLGVQLLEQVYDLLEEEDELEREARLQEHMGDKYTTYSVKARQLKFFEENVSF
Protein: Probable rhamnogalacturonase B (RGase B) (RHG B) (EC 3.2.1.171) (A2R3G4)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MLLDKLSVLSFLGLAPIFAAAQLSGSVGPLTSASTKAATKTCNVLDYGAKADKSTDLGAPLASAFADCKSGGLVYVPSGDYALSTWARLSGGEAWALQIDGIIYRTGTDGGNMIYIEHSSDFELFSSTSEGAMQGLGYEFHADDNWSGPRLLRLYEVTDFSVHDFILVDSPSFHFSLDTCTNGEIYNMAIRGGNHGGLDGIDVWSNNIWVHDVEVTNKDECVTVKSPSKNILIESIYCNWSGGCGMGSFGSDTNVSDITYRNIYTWSSNNMMLIKSNGGSGFVENVLLENFIGHGNAYSLDIDSYWASMSAVDGDGVQLSNITVKNWKGTEAYGAERGPVKVVCADGAPCYDITIEDFAMWTEEGDSQWYSCESAYGSGYCLQDSDDHVSYSVTTSTVSSAPSGYSATSMAADLTTDFGSTVSIPIPTIPTSFYPGATPYSALMANSASTAAASSIASHATVHSSSASVAASVPSAVAPSESIPAATSAVVSSAAAIAPSPAVGAQEGSTTSAPSFAAPSGAGNSPQGPTGASGFGEKGQQGEQGEQGEQGEQGVCYV
Protein: Astrocytic phosphoprotein PEA-15 (15 kDa phosphoprotein enriched in astrocytes) (Q5U318)
Organism: Rattus norvegicus (Rat)
Function: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm. Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface (By similarity).
Subcellular location: Cytoplasm. Note=Associated with microtubules. {ECO:0000250}.
Interaction partners:
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 3
- FAS-associated death domain protein
Sequence:
MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEDELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA
Protein: Rifin (Q8I2E7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLLHYCKVLLFSVPLNILVHNKNKSYITPQNTRNTRLLCECELYTSIYDNDTEMKAVMGNYNQQTSQRFEEYNKRMNKNRQKCKDECDKEIQKIILKDKLQKELMHKFATLHTDIQSDAIPTCVCEKSLADKVEKTCLRCTQNLGGIVAPSSGVLAGIAEGALIVWKPAAIKAAKAAKAAAAKAASDAATQAGIEAVRLEINKLSVYFNGTTGFVDLTPIVTSSTYDNGLVLVECAKKLIGDLSSNGRGGYTGFYNTAIHTESGELYVGNFGGIGKAAHDAKLASETTALTEAKVGAVDTTYGGFQTYITASVIAIVVIILIMVIIYLILRYRRKKKNEEKTPVHKIIRRINIMCLAFFIDIFVYEILLV
Protein: Cilia- and flagella-associated protein 161 (Q6P656)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q6P8Y0}.
Interaction partners:
- Cilia- and flagella-associated protein 52
- EF-hand domain-containing family member C2
- Cilia- and flagella-associated protein 45
- Enkurin
- EF-hand domain-containing protein 1
- Protein Flattop
- Piercer of microtubule wall 1 protein
- Tektin-1
- Meiosis-specific nuclear structural protein 1
- Ciliary microtubule inner protein 2B
Sequence:
MAQNVYGPGVRIGNWNEDVYLEEELMKDFLEKRDKGKLLIQRSRRLKQNLLRPMQLSVTEDGYIHYGDKVMLVNPDDPDTEADVFLRGDLSLCMTPDEIQSHLKDELEVPCGLSAVQAKTPIGRNTFIILSVHRDATGQVLRYGQDFCLGITGGFDNKMLYLSSDHRTLLKSSKRSWLQEVYLTDEVSHVNCWQAAFPDPQLRLEYEGFPVPANAKILINHCHTNRGLAAHRHLFLSTYFGKEAEVVAHTYLDSHRVEKPRNHWMLVTGNPRDASSSMLDLPKPPTEDTRAMEQAMGLDTQ
Protein: CD1d molecule (A0A669KB34)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Endosome {ECO:0000256|ARBA:ARBA00004177}.
Interaction partners:
Sequence:
MGCLLFLLLWALLQAWGSAEVPQRLFPLRCLQISSFANSSWTRTDGLAWLGELQTHSWSNDSDTVRSLKPWSQGTFSDQQWETLQHIFRVYRSSFTRDVKEFAKMLRLSYPLELQVSAGCEVHPGNASNNFFHVAFQGKDILSFQGTSWEPTQEAPLWVNLAIQVLNQDKWTRETVQWLLNGTCPQFVSGLLESGKSELKKQGGSYTSMGLIALAVLACLLFLLIVGFTSRFKRQTSYQGVL
Protein: Transmembrane protein 44 (Q2T9K0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGEAPSPAPALWDWDYLDRCFARHRVCISFGLWICASSCWIAAHALLLYLRCAQKPRQDQSALCAACCLLTSLCDTVGALLARQLTIQVFTGAYLAAIDLVNFMFILFPVCGSKFKSNSDREARERKRRRQLRASVFALALPLSLGPCWALWVAVPKASATIRGPQRRLLASLLQENTEILGYLLGSVAAFGSWASRIPPLSRIAPPPTLGITTQHEIWRGQMSKPSQSPSRSPSGHWRAAAQRQVLGTEMCRGKTFPSIHLWTRLLSALAGLLYASAIVAHDQHPEYLLRATPWFLTSLGRAALDLAIIFLSCVMKSKMRQALGFAKEARESPDTQALLTCAEKEEENQENLDWVPLTTLSHCKSLRTMTAISRYMELTIEPVQQAGCSATRLPGDGQTSAGDASLQDPPSYPPVQVIRARVSSGSSSEVSSINSDLEWDPEDVNLEGSKENVELLGSQVHQDSVRTAHLSDDD
Protein: Single-stranded DNA-binding protein homolog sam-10 (Synaptic vesicle tag abnormal in mechanosensory neurons) (B7FAS6)
Organism: Caenorhabditis elegans
Function: Involved cell autonomously in PLM neuron pre-synaptic differentiation by negatively regulating prk-2 expression and in neurite branch positioning.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21115607}. Nucleus {ECO:0000269|PubMed:21115607}. Note=In PLM neurons, translocates into the nucleus during the 3-fold embryonic stage and remains nuclear in the adult. Nuclear localization is idb-1-dependent. {ECO:0000269|PubMed:21115607}.
Interaction partners:
- LIM interaction domain-containing protein
- Serine/threonine-protein kinase prk-2
- BLOC-1-related complex subunit 5
- F-box/WD repeat-containing protein mec-15
Sequence:
MPPQVIQQQQQSLASEMTARDRLTSYIYEYLQQTGASKTAETFKEEVLSTNPAAGLAAANSTKLSDKSFLLEWWLLFWDLYSAAPERRDAGGDPFSAEAKYFHEAMIGMPPGMNGHFAPPPMGMEMMGGHPGAFGGRFAPGRMPPGAMAPGGMPPGAFPMFPPDPRLQRMAPNQGMRMPPPPVGQPFPGAVGMPRPVGPGAPMDMSGMQRFDFMGGPPPGGGAQPFPGASGSGGMMPNGAHPHMSLNSPSMGVPPADMPPFMGMPPMPPTSSSAMPFGMSSDHQPMSAGPAAAAPGATTAGGPGTPGMIGSVPGPGSVPQVATTSVGSVGTPSSIGQQLHQPKQEITTNGEEIMKTEALTPTGGGGGGSVPPPPPAATAAVSMNGGGPGSAPGSAHSVNNNVNPGTPGSNPLSNPMSNPPLSSGPPPPGSNDAFGKDDNGEISKIREGLLDGFCA
Protein: Methionine aminopeptidase (EC 3.4.11.18) (Q4FKC0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03174}.
Interaction partners:
- Methionine aminopeptidase 2
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L5, putative
- 40S ribosomal protein S15a, putative
- 40S ribosomal protein S18, putative
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S14
- 40S ribosomal protein S15, putative
- Large ribosomal subunit protein uL5
Sequence:
MSCEGCGKLEPAMQCPTCKKLGLPPSYFCTQECFKENWSNHKLKHSNTSVANVPTMTDWAMKTFDFTGPLRPGKITPRRAVPSHIPRPDYADCAGGVSASEEKDRGSKVKVYNIQFLHDDSKKTAEIQRIKTVCQLSREVLDIATAAAKPGITTDELDRIVHEATVERNMYPSPLNYYGFPKSVCTSVNEVICHGIPDSRELEEGDILNIDVSSYLNGFHGDLNETVFIGRPDDDSVRLVHAAYECLCAGIGVVKPEALYKQVGDAIEACASQYQCSVVRTYTGHGVGHLFHTSPTVCHYANNKSLGMMRPGHVFTIEPMINLGTWQDVTWPDKWTSTTKDGRRSAQFEHTMVVTNGGVEIFTDWVDGVPTYQKQLKEWGIMLPQRKEVGSATAA
Protein: Ethylene-responsive transcription factor 4 (AtERF4) (Ethylene-responsive element-binding factor 4) (EREBP-4) (Protein RELATED TO APETALA2 5) (O80340)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a transcriptional repressor. Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways, and could also regulate other AtERFs.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor MYC2
- Probable WRKY transcription factor 40
- Defensin-like protein 16
- Zinc finger protein ZAT10
Sequence:
MAKMGLKPDPATTNQTHNNAKEIRYRGVRKRPWGRYAAEIRDPGKKTRVWLGTFDTAEEAARAYDTAARDFRGAKAKTNFPTFLELSDQKVPTGFARSPSQSSTLDCASPPTLVVPSATAGNVPPQLELSLGGGGGGSCYQIPMSRPVYFLDLMGIGNVGRGQPPPVTSAFRSPVVHVATKMACGAQSDSDSSSVVDFEGGMEKRSQLLDLDLNLPPPSEQA
Protein: Myosin-binding protein C, cardiac-type (Cardiac MyBP-C) (C-protein, cardiac muscle isoform) (Q90688)
Organism: Gallus gallus (Chicken)
Function: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle A bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role. May be involved in the early phase of myofibrillogenesis.
Interaction partners:
- Troponin T, cardiac muscle isoforms
- Myosin regulatory light chain 2A, cardiac muscle isoform
- Myosin light chain 1, cardiac muscle
- Alpha-actinin-2
- Actin, alpha cardiac muscle 1
- Tropomyosin alpha-1 chain
- Myosin regulatory light chain 2B, cardiac muscle isoform
- Cysteine and glycine rich protein 3
- Myosin binding protein C, slow type.
- Uncharacterized protein
Sequence:
MPEPAKKAVSAFTKKPKTTEVAAGSTAVFEAETEKTGIKVKWQRAGTEITDSEKYAIKAEGNKHSLTISNVGKDDEVTYAVIAGTSKVKFELKVKEPEKSEPVAPAEASPAPAASELPAPPVESNQNPEVPPAETQPEEPVDPIGLFVTRPQDGEVTVGGNITFTAKVAGESLLKKPSVKWFKGKWMDLASKVGKHLQLHDNYDRNNKVYTFEMEIIEANMTFAGGYRCEVSTKDKFDSSNFNLIVNEAPVSGEMDIRAAFRRTSLAGGGRRMTSAFLSTEGLEESGELNFSALLKKRDSFLRTANRGDGKSDSQPDVDVWEILRKAPPSEYEKIAFQYGITDLRGMLKRLKRIKKEEKKSTAFLKKLDPAYQVDKGQKIKLMVEVANPDADVKWLKNGQEIQVSGSKYIFEAIGNKRILTINHCSLADDAAYECVVAEEKSFTELFVKEPPILITHPLEDQMVMVGERVEFECEVSEEGATVKWEKDGVELTREETFKYRFKKDGKKQYLIINESTKEDSGHYTVKTNGGVSVAELIVQEKKLEVYQSIADLTVKARDQAVFKCEVSDENVKGIWLKNGKEVVPDERIKISHIGRIHKLTIEDVTPGDEADYSFIPQGFAYNLSAKLQFLEVKIDFVPREEPPKIHLDCLGQSPDTIVVVAGNKLRLDVPISGDPTPTVIWQKVNKKGELVHQSNEDSLTPSENSSDLSTDSKLLFESEGRVRVEKHEDHCVFIIEGAEKEDEGVYRVIVKNPVGEDKADITVKVIDVPDPPEAPKISNIGEDYCTVQWQPPTYDGGQPVLGYILERKKKKSYRWMRLNFDLLKELTYEAKRMIEGVVYEMRIYAVNSIGMSRPSPASQPFMPIAPPSEPTHFTVEDVSDTTVALKWRPPERIGAGGLDGYIVEYCKDGSAEWTPALPGLTERTSALIKDLVTGDKLYFRVKAINLAGESGAAIIKEPVTVQEIMQRPKICVPRHLRQTLVKKVGETINIMIPFQGKPRPKISWMKDGQTLDSKDVGIRNSSTDTILFIRKAELHHSGAYEVTLQIENMTDTVAITIQIIDKPGPPQNIKLADVWGFNVALEWTPPQDDGNAQILGYTVQKADKKTMEWYTVYDHYRRTNCVVSDLIMGNEYFFRVFSENLCGLSETAATTKNPAYIQKTGTTYKPPSYKEHDFSEPPKFTHPLVNRSVIAGYNTTLSCAVRGIPKPKIFWYKNKVDLSGDAKYRMFSKQGVLTLEIRKPTPLDGGFYTCKAVNERGEAEIECRLDVRVPQ
Protein: Beta/omega-theraphotoxin-Tp1a (Beta/omega-TRTX-Tp1a) (Protoxin-1) (ProTx-1) (ProTx1) (Protoxin-I) (ProTx-I) (P83480)
Organism: Thrixopelma pruriens (Peruvian green velvet tarantula)
Function: Ion channel impairing toxin that inhibits voltage-gated calcium channel Cav3.1/CACNA1G (IC(50)=53 nM), voltage-gated potassium channels Kv2.1/KCNB1 (IC(50)=411 nM), all sodium channels tested (Nav1.2/SCN2A (IC(50)=60-104 nM), Nav1.5/SCN5A (IC(50)=76-358 nM), Nav1.6/SCN8A (IC(50)=21-133 nM), Nav1.7/SCN9A (IC(50)=51-95 nM), and Nav1.8/SCN10A) and the nociceptor cation channel TRPA1 (IC(50)=389 nM). Acts as a potent and selective blocker of voltage-gated calcium channel Cav3.1/CACNA1G, but not of Cav3.2/CACNA1H, and Cav3.3/CACNA1I. On Nav1.7/SCN9A, primarily interacts with the DII and DIV voltage-sensor domains. Also acts as an inhibitor of nociceptor cation channel TRPA1 (IC(50)~389 nM) by binding to the S1-S4 gating domain of TRPA1. It shows moderate affinity for lipid bilayers.
Subcellular location: Secreted {ECO:0000269|PubMed:12475222}.
Interaction partners:
Sequence:
ECRYWLGGCSAGQTCCKHLVCSRRHGWCVWDGTFS
Protein: Bifunctional hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase (A0A1D8PJ13)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- acetyl-CoA C-acyltransferase
- acetyl-CoA C-acyltransferase
- 3-hydroxyisobutyryl-CoA hydrolase
- Oleate-induced peroxisomal protein POX18
- Carnitine O-acetyltransferase, mitochondrial
- Oleate-induced peroxisomal protein POX18
- Isocitrate lyase
Sequence:
MSPIDFKDKVVIITGAGGGLGKYYSLEFAKLGAKVVVNDLGGALDGQGGNSKAADIVVDEITKNGGVAVADYNNVLDGAKIVETAVKSFGTVHIIINNAGILRDSSIKKMTEKDFKLVIDVHLNGAYAVTKAAWPYFQKQKFGRVVNTSSPAGLYGNFGQTNYSAAKSALLGFAETLAKEGDRYNIKANAIAPLARSRMTESILPPPILEKLGPEKVAPLVLYLSSAENEVTGQFFEVAAGFYAQIRWERSGGVLFKPDQSFTAEVVAKRFSEVLNFDDSGKPEYLKNQHPFMLNDYTTLTTEARKLPSNDASGAPKVTLKDKVVLITGAGAGLGKEYAKWFARYGAKVVVNDFKDATKTVEEIKAAGGEAWADQHDVASQAEEIIKNVIDKYGTIDVLVNNAGILRDKSFAKMSDQEWDQVQKVHLLGTFNLSRLAWPYFAEKKYGRIVNISSTSGIYGNFGQANYASAKAGILGLSKTLAVEGARNNIKVNVVAPHAETAMTLTIFREQDKNLYHADQVAPLLVYLGSEEVEVTGETFEAGGGWIGNTRWQRAKGAVSHDEHTTVEFIRDNLKDITNFDSDTENPKSTTESSMAILSAVGGDDDDDDDEEEEDEGDEEEEEEDEEEDDPVWRFNDRDVILYNIALGATTKQLHYVYENDSDFQVIPTFGHLITFNSGKSQNSFAKLLRNFNPMLLLHGEHYLKVHKWPPPTEGAIKTTFEPISTTPKGSNVVIVHGSKSVDNDSGEVIYSNEATYFIRNCQADNKVYAERRSFATNPFPAPKRAPDYQVDVPISEDLAALYRLTGDRNPLHIDPNFAKGAKFPKPILHGMCTYGLSAKVLIDKFGMFDEIKARFTGIVFPGETLRVLAWKESDDTVVFQTHVVDRGTIAINNAAIKLVGDKAKI
Protein: MAX-1A (PH domain-containing protein) (G5ED24)
Organism: Caenorhabditis elegans
Interaction partners:
- Netrin receptor unc-5
Sequence:
MSDSSASPLRSPEDEELLAKSSRIRLWVTKRMKELEDQNERLRAQNLRCTTQLQMLRSFTEKSRKIKAEMEMSRSITGTLPVLRDENRTSDDSGLTSDDADRKQMSVSISECTPRVQRKAARTMLKNTSQGSSTSESSPCEDEAKPMPLPRRIHPTATERDSLNSYAEDYEYDIEESSFERHEEQVRNENEKYVDYVNLHEFVAIKDDKVVYSEIVKHRSTEKEYLPALPSHQPRQWENRLIQAAEKCLSVIDGADSEGTSTGPSVSPYHVSDVSRISSNNRTESPGSRKSSKLSRNSSPRVPSHHSYEDGAAYAIRDLCLGSDYYLPPDASSRCSGGTPTSRTSLIPSRETMEKSGYWTQLTDSRIKSLKRRYVVFKNGQISFYRKHNNRDEEPASKISISDIRSVTKLEQQGAAYAFQLITSTDKMNFMTESERTTHDWVTILSAAIKATTLREMASRVTPIDASISGWLTRVKCGLSKKVFAALVNQKLMFFKNSNDLVPNGFLCLQGAQISEKHNGTEEYSGSSDEQLETTKEHPNQRKNNDSLCVQIANEDPVYLILRTSEDKEKWLYYLKSASGTAALCGTPFEILVQRMMAENVANDSPLWKDLLFASGEEIPKDTMTSVDHSDRKKTLEIARACQLFVSVLMRAQATQYHIDLAQNILSTAVQQEYLRNEVYSQLIKMTSGSMPFGLQGWKLLALTIPLFLPKQYSLLWLLKRHISRWVDLPNESDETRMAIFCESALDRCLRVGGRQEGPSRLEVTSVLTRDVTRTKFPHSISVKLPNSEYQIVEFDGSTEIGQCLSSLCLKLGMRPALLSGYALYMNDPMTHSLLLLKGKQKLCDALSTWETRSRDAQRGRVISDCAAALSLRMRHYWGHLALTETPIERQFLVWRASEEIVNGRIPLSNQLCESLAALYAQMVFGDANQSLSDQQFEFISQRFYPSKMLDVACIKSLRLQINSNWSELIGMSENECVRVILQVLGKWPLFGSDLHEASMRTDNERKIYLALNDHSVSLLDRRHFDVIRTIPYSSLSTFGQFQQDFMLTIIRPLTPGSHPDEAPKERLTFSMQKNEIEQLTLHLAEYIRCQKLVWKVSK