lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Predominantly localizes in cytoplasmic bodies. Localization may be influenced by the coexpression of other TRIM proteins, hence partial nuclear localization is observed in the presence of TRIM22 or TRIM27. In cytoplasmic bodies, colocalizes with proteasomal subunits and SQSTM1.
Domain:
The B box-type zinc finger domain and the coiled-coil domain contribute to the higher and low order multimerization respectively which is essential for restriction activity. The coiled coil domain is important for higher order multimerization by promoting the initial dimerization; The B30.2/SPRY domain acts as a capsid recognition domain. Polymorphisms in this domain explain the observed species-specific differences among orthologs (By similarity); The RING-type zinc finger domain confers E3 ubiquitin ligase activity and is essential for retrovirus restriction activity, autoubiquitination and higher-order multimerization.
Sequence:
MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKTSMPDEGERSCPVCRISYQHKNIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCREDRKVICWLCERSQEHRGHHTFLTEEVAQEYQVKLQAALQMLRQKQQEAEELEADIREEKASWKTQIQYDKTNILADFEQLRHILDWVESNELQNLEKEEKDVLKRLMKSEIEMVQQTQSVRELISDLEHRLQGSVMELLQGVDGVIKRMKNVTLKNPETFPKNQRRVFRAADLKVMLKKLRELRDVQHYWVDVTVAPNNISYAVISEDMRQVSSPEPQIIYEAQGTISQTFVNFNYCTGIRGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDAMYNIEQNENYQPKYGYWVIGLEERVKCNAFQDGSFHTPSAPFIVPLSVNICPDRVGVFLDYEACTLSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCTVPMTLCSPSS
The following text describes a protein:
Function:
Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Plays an essential role in the regulation of endothelial cell senescence and vascular aging. Upon activation by ANP or BNP, stimulates the production of cyclic guanosine monophosphate (cGMP) that promotes vascular tone and volume homeostasis by activation of protein kinase cGMP-dependent 1/PRKG1 and subsequently PRKAA1, thereby controlling blood pressure and maintaining cardiovascular homeostasis.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MRACGGWRTGGRLLLPPLLVLLLLGCRSDAVQSKSACHREAKSDARGSSREVTLAVILPRNNTAYPWAWPRVGPALHLALRRISRDPHLLPGYQVRYFMENSEDDGGNCSDYIAPLMAVDLQFAHHPWAFVGPGCHYAAAPVGRFVSHWGVPMVTAGAAAYGFFNEKSTYSLMTNTGPTHKKLGECTCHIQEHFKWTNRAMLIYSDEKMDDRPCYFAIEGLYTELDKVNITTEEFVFAESKSPLDYEAIIQEIRMKGRIIYVCCSQDTFRQLMIRFRRASMPLEEYVFFYIDIFGTSLSSREPKPWFRGDPDDAVAKEAFQSVIIITYTEPQNPEYKEFLQELKVEAKRNFSFNIEDTLTNLIAGSFHDGVMLYSLALNESLAEGEIPPKGETVTKKMWNRTYYGVTGPIRIDEHGDREIDFSLWDMTDNNTGTFQVVFVYNGTEKNISQVPGVRFQWPGDGSPPRDIPLCGFKNDECHSGVLPMLQVMTILIGFFLFFSTIIAVFIYRKLKLENELAAELWRIHWEDIQISNMEKTLRSAGSKLTLSLRGSNYGSLLTTEGNFQIFAKTGCYKGNIVAIKYINRKRIELTRKVLFELKHMQDVQNEHLTRFIGACIDPPNICIITEYCPRGSLQDIMENESINLDWIFRYSLINDIVKGMEFLHNSVIVSHGNLKSSNCVVDSRFVLKITDYGLASFRSEAECDDAHSFYARKLWSAPELLRAEGPLPSGTQKGDVYSFGIILQEIALRRGAFYLEGELLSPKEIIDRVTLGEWPYLRPTVNPQCHSEELGQLMQRCWAEDTVERPEFHQIKILLRKFNRDSRTNILDNLLSRMEQYANNLEELVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAIIDNFDVYKVETIGDAYMVVSGLPVRNGKLHAREIARMSLALLEAVRSFRIRHRPDQQLKLRIGIHSGEGQRAGHMALSQRQWCGVETCAQSLPALAPALKIHVSAATRSVLEEFLGFELELRGDVEMKGKGKMRTFWLLGERNGV
The following text describes a protein:
Function:
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant.
Sequence:
MVILETPRVFLIASWGSEAVISAFTDALYRGVPWEEAVKAQAPDVIIKRISAFYRQGHWSVFEFMGAQFLVECSRACHTQFIRHRMASYWSESQRYVDYTKREIRFVVPKGFPADLLKRAYEDYARLREGFRPEYARMILPNATAVLFAVQMNARELLLNFAPLRCAYAAQAEIRHVCWQMFAHAWRLWPNLARLVWEDLPSLHRDFCTKVPRGEDCRLYAIKDAEEKHGPLPETPWLSALVHG
The following text describes a protein:
Function:
JanA and janB regulate somatic sex differentiation.
Sequence:
MAAKTMSEIKDVDLDKPGVFKYIQVQVTDKSDASNAKIIVRGYERCHYHCDIFDEIAEQVDKKLFKLKPLGGGRIKLDDKKKDICVYGYSQAYGPAKHEDSKELIEKAYPGYSVSISYDGY
The following text describes a protein:
Function:
G-protein coupled receptor for flp-15 neuropeptides. Receptor activation assays suggest binding to predicted flp-15 peptides, GGPQGPLRF-NH2 and RGPSGPLRF-NH2. Likely involved in Gi/Go-coupled signaling pathways.
Miscellaneous:
MISCELLANEOUS: Functional expression in mammalian cells is temperature-dependent and requires a temperature shift from 37 to 28 degrees Celsius for receptor activation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MEGGRNCVMTVQQWQPEYNDMNQIRAIFSLLYLLVWVGAIVGNTLVLYVLTFNQVSLSVRTVFVGCLAGSDLLMCLFSLPITAISIFSRVWVFPAIFCKLIGVFQGGTIFVSSFTLTVIALDRCVLILRPNQEIVNFPRAVFIVFCIWLLGYSLALPVGIYSDIAVYDEICGTFCEENWPDFNPDTGRSGIRRAYGLSVLVLQFGIPALISSICYWMISRVMSDQLARRRGHNIRPESETKLVNRKTRANRMMIVMVVGFVLAWMPFNAVNLYRDLFGISKWYSTVFALCHVCAMCSAVLNPIIYSWFNPQFRQSITTLFKGTDEARLIKKKPQSTSKMVSYPTNFSEIRKETEIASTKTKITIAENDYRAGDQLL
The following text describes a protein:
Function:
Acts as a blue light photoreceptor for the step-up photophobic response. Mediates photoavoidance.
Subcellular Localization:
Cell projection, cilium, flagellum. Note=Paraflagellar body, flagellum and paraxonemal bodies (PABs).
Sequence:
MYILVWKKGQQIKTFHTLDEAAQFKAASNIDEAQMFSVTVAPAISASGGSNEATNLRRLMYLSKSTNPEECNPQFLAEMARVATIRNREIGVSGFLMYSSPFFFQVIEGTDEDLDFLFAKISADPRHERCIVLANGPCTGRMYGDWHMKDSHMDSITTHPAMKTILYQIARSFSSMWSYLPKSAGNMLLLGKDPAAQPPEPMSVVVTFIYLVEFGSILSNPNLTEQAAEVLSTFVDVCVKNVEGSGGNIAKFITGICMAYWPINRTEEALTAIQQISEDLAQLRSQQAPGSAVSLMYSQAGVHYGRAMLCNAGSRKSDFTLLGDCINTTSRIATLAKKLKTPLLFSFEVRCLLGDEMREEIEGAGMHQVKGRDKPVVVYQFPGPELDVEMVRQKIEQFTPGRFRCQMPVVEYEALPISQRPPIFDDTPKGNPRPRTPGYGGRQRSDSLVDRLIMIAKLAGPSVSATGDTTLTTLTYISQATRPMSRLDLSAIMRTATRRNAQQSITGTLLHVNGLFVQTLEGPKDAVVNLYLRIRQDPRHTDVTTVHMAPLQERVYPSEWTLTSATEEMLATFPPLQDVLSQLAKSFTSLETYVPSTVVRYLTAGNNPRNLMPVSCGVVMLATDICSFTSLTEKSSLTEVWMICNTFIDACTSAICQEGGEVIKLIGDCVTAYFPGNNADSAVAAAQELFTFCRQLREAFVDVLDVRGCVSCGVGLDYGQVVMAQCGSLGLTEYVVAGAVSARVMEVEAITREVGYAIVVTEPVADRLSPQLRDHGIVPTPQAIEGLPCYGIAGEEFELDVDSIKRGIKALHAARSGEKPLTEPEEAKPDFRVSPGRVRHGDSGRRSNSAQGKRSIQVR
The following text describes a protein:
Function:
Participates in both transcription termination and antitermination.
Subcellular Localization:
Cytoplasm.
Sequence:
MAVSANRLELLQIADAVAREKSIDRGIVIAAMEDAIAKAARARYGSETDVHAEIDPKKGELRLSRHMLVVEKVENHSNQISLVDAQRANPGAQVGDTIADTLPPLEYGRIAAQSAKQVIVQKVREAERDRQYQEFKDRIGDIVNGVVKRVEYGSVIVDLGRGEAIIRRDEMLPREVFRNGDRVRAYIFDVRRETRGPQIFLSRTHPQFMAKLFAQEVPEIYDGIVEIKAVARDPGSRAKIGVISRDSSVDPVGACVGMRGSRVQAVVNELQGEKIDIIPWSPDIATFVVNALAPAEVSKVVIDEDRERIEVVVPDTNNQLSLAIGRRGQNVRLASQLTGWDIDILTEQEESERRQADFENSTRVFMESLNVDEVVGQLLASEGFTSVEELAMVDIKELAGIEGFDEETAQELQNRAREYLEQQEAELEAKRVELGVEDALKDVPGVTSKMLVKFGENDIKTVDDLAGCATDDLVGWTERKEGGETTKYPGALDGIEISRDDAEAMIMQARVKAGWITEADLAKPAEEAEASEDQPA
The following text describes a protein:
Function:
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side.
Sequence:
MSRQKLKFFCDAASVQFSLGCTSHRNFKLLIPLQPAVINVNLNTKPSFVLSNSTRHPLCVPLSSTISQRFLHVNNQKRNPDLTILSEADHQSLAVRFVSACPEPVQPYLRLMRIDRPIGTWLVFLPCAWSITLASPAGQLPDLKTLILFGLGSFFMRGAGCIINDMWDKDFDSKVERTKLRPIANNQVTRFKALCFLSIPLSISFSILLTFNWNTIGLGVCSLAPCVIYPLAKRFTYWPQAFLGITQGWGILIAWSEIYGSLTWPTLALYTSGVFWTMTYDTIYSCQVFALLCLCYLICLVFNWGAVMGWSAVCNTFQWAMVSMYITSIAWTLLYDTIYAFQDIEDDLKVGVKSTAIKFGESTKYWLAGFGSIVVGGLTTTGILCDQPWLYYLGVAGFAAHLSHQVWSVNLKDGNQCGEKFRSNRNLGLIFWGIIVLSNLIKIQTDESEVSDNQTPQKNVNS
The following text describes a protein:
Function:
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FrvAB PTS system is involved in fructose transport.
Subcellular Localization:
Cytoplasm.
Domain:
The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Sequence:
MAALTASCIDLNIQGNGAYSVLKQLATIALQNGFITDSHQFLQTLLLREKMHSTGFGSGVAVPHGKSACVKQPFVLFARKAQAIDWKASDGEDVNCWICLGVPQSGEEDQVKIIGTLCRKIIHKEFIHQLQQGDTDQVLALLNQTLSS
The following text describes a protein:
Function:
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Subcellular Localization:
Cytoplasm.
Sequence:
MKDSLQTIGVFVRPTHYQNPLFEKLEQAKEWVLKLLEDEGFESFMIDSLDGAKDARLIEKADAFLCLGGDGTILGALRMTHSYNKPCFGVRIGNLGFLSAVELNGLKDFLQDFKQDRIKLEEHLALEGRIGKTSFYAINEIVIAKKKALGVLDIKAYAGHTPFNTYKGDGLIIATPLGSTAYNLSAHGPIVHALSQSYILTPLCDFSLTQRPLVLGAEFCLNFCAHEDALVVIDGQATYDLKANQPLYIQKSPTTTKLLQKNSRDYFKVLKEKLLWGESPSKKR
The following text describes a protein:
Function:
Mediates both low-affinity uptake and efflux of sugar across the membrane; Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
GNVIAFGLFMSPLPTFYKIIRLKDTEQFSGVPYVATLLNCLLWTLYGLPFVTPNSLLVVTINGIGTALESTYLCVYLFYAPNKPRAKVLKMLAVVLTFFAAVALMVMTITHVHKTRQLIVGVLCVIVGTGMYASPMSVMVRKLVIQTKSVKYMPFLLSLTAFLNGLTWTAYAFLGKIDPFIVVPNAIGTCLATTQLILYAIYSKKEKATIKNKENGNGADAKPANNHIGFAVRCPEAVSADVNVNDEERVSRQV
The following text describes a protein:
Function:
Receptor for endogenous opioids such as beta-endorphin and endomorphin. Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone. Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe. Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors. The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1, and to a lesser extent to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15. They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B. Also couples to adenylate cyclase stimulatory G alpha proteins. The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4. Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization. Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction. The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins. The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation. Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling. Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling. Endogenous ligands induce rapid desensitization, endocytosis and recycling. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties. Involved in neurogenesis (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cell projection, axon. Perikaryon. Cell projection, dendrite. Endosome. Note=Is rapidly internalized after agonist binding.
Sequence:
YTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKTVNVCNWI
The following text describes a protein:
Function:
Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif.
Subcellular Localization:
Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side.
Sequence:
KSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLSSRNPTFMNLALHCIANVGSREMAEAFAADIPRILVAGDTMDSVKQSAALCLLRLNRTSPDLVPMGEWTSRVXTTLAQKNPEEFKTSVSLAVARLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAIRGRLTECLETILNKAQEPPKSKKVQHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIETVINALKVRPGPARAWAVPPTHRAPVTWIPGPAVTEQMCYCALSGWTVQSGLCLQALGCCWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAAKTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLVQFNLLHSKFHLCSVPTRALLLSTYIKFVNLFPEIKGTIQDVLRSDSQLKNADVELQQRAVEYLRLSCIASTDILATVLEEMPPFPERESSILAKLKRKKGPGMLPDIEDGRKERNADVNGGAEPVHVSTNSKVPCACVLCCAPPGTHALSPCPFVPEFPQDLCQQQTQILVLASRTNAPTLNSAPPPAAGGSLLVDVFSENSTSLPMMPPADENFSRFVCKNNGVLFENQLLQIGLKSEFRQNLGRMYVFYGNKTSTQFLSFSSSVLCQDSLKVPQLNVHTKPVDPTVDGGAQVQQILNIECVSDFMEAPVLNIQFRYGGTLQNIAVKLPITLNKFFQPTEMTSQDFFQRWKQLSAPQQEVQKIFKAKHSMDTEVTKAKIIGFGVALLDRVDPNPSNFVGAGVIHTKTTQVGCLLRLEPNTQAQMYRLTLRTSRDTVSQRLCELLSDQF
The following text describes a protein:
Function:
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MRNLVVINEVHGVVEGDDDSKLQIAAAAVDVDNGLFFVVSQSSALLCYSLSSSKVEWIVTLDEEGGPVVAMDWRVEVESVVIGRSSGQVVEVSDSGQEVQEVGSLKGGLLAMAASPDGELLLLATGFGQLLVMTQDWDLLYEVTLDEGLAASGSVQLSWRGDGKYFATLVTGSGASTDSSPLKIWERDTGALYASGESIPYLQTAMSWCPSGARIGTACIQPNSTSQPLIMSFEKNGLKRDKFQLEGPLDTHVNYLKWNSNSELLAMVITTKDWTGVQIWSCSNFHWYLKQELRFPSTDELNVLWDPEDPMTLVCWTASGTIRTLKLGWKSAVLDSSIALVINGLSLLVSPLSLALIPPPMSLFTITFQAPVQVVAFLQDHERCCFIAARLSDSTLSVVTLPELNDWLDLDGINHTAHSISVLSDLKQSISELRHLTWLSSGALLGALSVQPGSDKVGISGNFSGTQNGVFFQTYPGSKEILVEVDLDMVAYNPSPIMSDGVQIQGVQETPVKQAVISIIKNKAPLSDQNGDAFVQLGDGSMLLYSESQGASQFGKTVIGKFARPCPWTSVLQSENGETLLLGLDQKGSLELLGRCVLCRDCSSFVVHTAADSRSHLLYTTQRDSMHVVSLSDLSSLSEVQSKQEVNMKPEISDGRKPKGVGFQEENLKVRPLWERGARLVTALGGHDVAVIVQTIRGNLETVYPRGLVLGAIAEALKKGDFREAMGLTRRHHINLNVLVDYGGWRNFCVKASEFVKQVGKLNHITELVYALNEENIVETTYKNLLPPFPEPLSPADAATELMKSQFTANKVQTVLKSLRLGVEKEIPVSPGKELCILATLAKSRPPELKEALQRIKSLREAELQGEVAVELEAVEETGEKGKVILSAEAALKHLLWLSDADIVFKEALGLYDLHLAAMVASHAQRDPKEFIPLLKELEEMPPHLMQYSIDVRLGHYESALQNLAQGGEANFNECLQLMMDHAELFPLGLHIFRESKNRLPVLEAWGDHLMQQEKFEDAAAAYCSCNNLQKALGSYRAGGLWRGVMTIAGRMNLSREEWTSLASDLGEELQAMGMPAEAACVALEYIHDVDSGVRLLLEAREWMEAVRVSSLYAREDLLSSLIESAALECASALIEEFTEGLDKVRKYLLRYQTVRQRRLALAAKLKAEEDGEWVDDDTISEASSHLSSMSAYSHGTAATSSVTTGSGRGRKQSVRSQKKVKGGRIRAGSAGEEGGLVDYIRGMAVSPRMLDEVRRLLSVLVLQGHYSVAHHVQSSLVAYQNDQKVALETMEKDAADDNLQAGNPPSASTAAVSKSSSPAIWRLAVLEPPDGVCI
The following text describes a protein:
Function:
Mitochondrial transporter mediating uptake of thiamine diphosphate into mitochondria. It is not clear if the antiporter activity is affected by the membrane potential or by the proton electrochemical gradient.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MVGYDPKSECRNNSKVEVALAGSAAGLVTRALISPLDVIKIRFQLQVENLSSRDPRAKYHGILHAMRQILKEEGLTAFWKGHFPAQILSMGYGAVQFVTFERLTELAHRTKPYGISDFSVHFVCGGLSACAATLSLQPVDVLRTRFAAQGEPKIYRNLRHGMKMMYKTEGPLAFYKGLPPTIIAIFPYAGFQFSFYRMLKQVYEWAMPGDRKKNANIKNLLCGSGAGVISKILTYPLDLFKKRLQVDGFEEARATFGQVRKYESLLDCARKILQEEGARGFFKGLTPSLLKAAMSTGLIFFMYELFCNLFNCKKTSDNQKTGQVS
The following text describes a protein:
Function:
Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-MMS22). RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition.
Subcellular Localization:
Nucleus. Note=Nuclear punctate foci structures.
Sequence:
MDVDEPNPIVISDSEATDEEISIIYEPEFNENYLWAEENVQEASRSQKIVTERLSLDSTAGESCTPSVVTDTQVTTGLRWSLRKRKAIQKMPYSLERIKHRQLLEGYDISSFDSISNQLTLPKNASTVIHSNDILLTKRTGKPLDEQKDVTIDSIKPENSSVQSQRYDSDEEIPKKRHRTFKDLDQDIVFQSGDSTEDEQDLASTNLQNTQNDEVIFRGRVLNVRTGYRGVLPRVAWEKSLQKQQSSKVTKRKTQLLNHKGVAKRKMNRSAHIEDEEQNLLNDLIAPDDELDIEENAPPDIYLGNLPEDREANEKELKELQEYYESKYSEDAQSAGTSGFNLNEEYRNEPVYELEYDGPGSCISHVSYKDQPIIYLNSRHSDSGFSEQYNISAEDNQSVISLDAAEEHNDGIIDKMLVKPKRIKATNDANFLNTKSKRVRRYKYKYRNSCLAPSTKAIKVGKRSAHKSHLAANNPVSFVSKKNHVIDDYFFEELESQSLEQDDSSSLKPQKKRRKKKAPIYSSFSADLESRRKPVFNTVVEVPTNRYAFTKPNVRNRDSINHDMEFEEEDSNQELGPIMVVLDSILLKKPFEPPNFFKIQLSDKSFLLSKLNPADIATSLQKIFRVIIDKGITDTELVHFNESLIAFLVHLDMPELFDLIGEFHREFRSKVNSLRKKAKPIHFFQIAACQLMFLEISRYNKISAAAKFDMDVKLLDHIVSFFKLLSVCYDSVMKNPMQYLYTSYYILSAVVDVIHKKEALWDLFQKHPFSPHISLLLVNIFPTKVCRWQVLRLDSEFQPLSSAFRFINYCIETCNWNVTNSLILSLDRIFKRRRFSDFEEESDLSQNNKIIYPPTNQLTSRLMFNRYLHLLTLCELSSSDTQRVIPMGDISMNDSLSVLKNRLNLLIVLATRFDLNLEKRFQELTRPLYSKEYLNLHTQNTVRTITTLIMQASLSFLEISRIKNHPFSGKFIASLFDKLVLQQPSISGVTENFLKEFTNLVSKMKRKSVSMLKFLYPSLVAMSQENIFESSFFLLLQVYLKSLDVLGPTWVQNYLFQFIKSKAQENERWIECYCQIGKFLVDSGIFTWWTFFTYNGLDAALHFQLAFHSLIIDFCDTDSFELLKKPLYSIASDLLLISKDDAFYHFLSNLLKRAHIIVADLKPVSDENELLRLAYIFSKALKKNAYQDLLAVFLSLAKKHYDEGDISRNFLAKYLEFLNKNCLTELRNNQLFISLRRELGISSDEDEKCAFWDSFNEAGDILSKAAFVETGIVQACCTGNEIDGYLDNLSTLFTSTMLESPFAFFSDLVIAHIFENRPFFDVNIKNFLLSHFIDLFNKVLKMKFEQVSPDEFAELCKVYRALCIECATDDTFNSNSDLIAAKDAFLVSVLRIADGFWEHDKLLQLRMLDSNMNIPNQIPHTTLQSSLSAIVIKIIESNIGKIEASEPFKTFKNT
The following text describes a protein:
Function:
This is one of the three pore-forming subunits of the heterotrimeric epithelial sodium channel (ENaC), a critical regulator of sodium balance and fluid homeostasis. ENaC operates in epithelial tissues, where it mediates the electrodiffusion of sodium ions from extracellular fluid through the apical membrane of cells, with water following osmotically. It plays a key role in maintaining sodium homeostasis through electrogenic sodium reabsorption in the kidneys. Additionally, ENaC is essential for airway surface liquid homeostasis, which is crucial for proper mucus clearance.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cell projection, dendrite. Postsynaptic cell membrane.
Sequence:
MELKAEEEEVGGLQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFHYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEVCSAEDFKVVFTRYGKCYTFNSGRDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVACQEQRQLIYLPPPWGTCKAVTMDLDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHKLCRRGKCQKEAKRSSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC
The following text describes a protein:
Function:
Together with eak-4 and phosphatase eak-6, negatively regulates dauer larva formation downstream of insulin-like receptor daf-2 and in parallel of age-1, pdk-1 and akt-1.
Subcellular Localization:
Cytoplasm. Cell membrane; Peripheral membrane protein. Note=Localizes to dendrite-like structure in XXXL/R cells. Membrane localization is daf-2/InsR-independent.
Sequence:
MEKYSIRSNIVHKLDDNQPLLSERVTARLEAVNRNRVVKIVPQHRYNVRLTPSMLNRDGYINASLMEFSDVGQKYILTGIPSEDKVFAFWQMVLEQRSPTIIQFADNVEEKLEHYDKYFPDKGDVWSYGHLQVERKSYAIHQGNFHTRNFILRKGNETHRVLHFTVFGWTETTTPIMQDFLALRKVMKDTGALNMINPASALFRSTMRRYIHTPPSFAPIIQSARGSSRAGAFVVIDLLIRMIDGKKTNLYSVEDLIVKCKHMRIHCVPVALHHSFIYEAVLDYLLRRNPRFQDFKEPLIAYSESCFVKWSSMDKEIEKFINTKTWFLNESSRNKFLRSVMPPVV
The following text describes a protein:
Function:
Constitutively active protein required for microtubule and F-actin growth, structural maintenance and organization during excretory cell tubulogenesis.
Subcellular Localization:
Cytoplasm, cytoskeleton. Note=Localizes to leading edge F-actin and microtubules.
Sequence:
MTSDTIRQTLDELLLDKNGGSSNEARAFFLSQIIDQLKLISSQTDAERQLQKLQLKDPNDNIVKATPPPPPPPPPLISILQQAPPPPPPPPPPTLKAPPPPPILGLKTPSKSLKTPTPRPKECPTSFLPKKEKKTKTRTVQWSKINASVVQDDSVWGKLAKASNVDIDFDLLDNFFGIESLAVSGAAEVVKKSTRKDAHVELLTAKRSQNVAIMLKQFKNIDELIDDVSQNKPVAEIDALQNLFGMLPQSEEEEALRRYTGDISLLSPPSSFFYRLVQIQFYRLRIETQIFLSDFSRLMRELAPNVEILIRTSQEILTSPTLPRLLLIFVNMGNYLNGNNSQGNAFGFTLNSLWKLIDLKGNKQEFSLLHLLVTCEPDLVAHLQEELSTLKDASQISFDEIKISLKTLRDGRCKLEKQLETCSGASFTQFLELIKIDCKFELDEFGANYDKLTELQYQLADYFCENRNTFQLDECLKIFNFLMNRLQQTLKEHVTRETRKLKKEEKKETQTTRECEKTMKKPEKIDLFDALTASNGGPESPRKRAAGILDMRQKLGNVRIRKLRDVTTLESSFTPPPPPPLESPTDSTSSKENESVKPAKTSTNYEMCNDLESYITSLTRKRASHLPKAPPKEEPKLPEVLPEKSKIALKIEKIPEKIDKPPLPQAAPIIPKLPQKSIKAPSTVTTRSKVPPPTAAAAVRIVSVTTTTTPTKTAELRKPGARSPKTTVATVPKVTVVPVSRVPVAPSTPLSRRMSAPVVRKPTMTAEKKREITMKPSVSTSARPSLINTSSHPMVRSPLPKMSVLEKPKPLRITRPTVIPQSPTVTSSARPSGLRQPAKPKWV