lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
[Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C. It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation. They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after endocytosis of the virion. Plays a role in the packaging of ribonucleoproteins during virus assembly; [Glycoprotein C]: Structural component of the virion that interacts with glycoprotein N. Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation. They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after endocytosis of the virion.
Subcellular Localization:
[Glycoprotein N]: Virion membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein. Host endoplasmic reticulum membrane; Single-pass type I membrane protein. Note=Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs; [Glycoprotein C]: Virion membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein. Host endoplasmic reticulum membrane; Single-pass type I membrane protein. Note=Interaction between Glycoprotein N and Glycoprotein C is essential for proper targeting of Glycoprotein C to the Golgi complex, where virion budding occurs.
Domain:
[Glycoprotein N]: Contains a Golgi retention signal on its C-terminus. The cytoplasmic tail specifically interacts with the ribonucleoproteins and is critical for genome packaging.
Sequence:
MVRTYLLLLLLCGPATPFFNHLMDVTRRLLDSSNATWQRDQPDTHRLSRLDAHVMSMLGVGSHIDEVSVNHSQHLHNFRSYNCEEGRRTLTMMDPKSGKFKRLKCNENQTLSKDCASCIEKKSSIMKSEHLVYDDAICQSDYSSPEAMPDHETHLCRIGPLHIQHCTHEAKRVQHVSWFWIDGKLRVYDDFSVSWTEGKFLSLFDCLNETSKDHNCNKAVCLEGRCSGDLQFCTEFTCSYAKADCNCKRNQVSGVAVVHTKHGSFMPECMGQSLWSVRKPLSKRSVTVQQPCMDCESDCKVDHILVIVRHFYPDHYQACLGSTCLTGRAKDKEFKIPFKMADRLSDSHFEIRIWDKERSNEYFLESRCESVDACAAITCWFCRANWANIHCFSKEQVLILVAVSSLCILLLASVLRALKVIATFTWKIIKPFWWILSLLCRTCSKRLNKRAERLKESIHSLEEGLNNVDEGPREQNNPARAVARPNVRQKMFNLTRLSPVVVGMLCLACPVESCSDSISVTASSQRCSTSSDGVNSCFVSTSSLLQVSPKGQESCLILKGPTGTAVDSIRIKTTDIKLECVRRDLYWVPRVTHRCIGTRRCHLMGACKGEACSEFKINDYSPEWGHEEELMAQLGWSYCVEQCGGALCQCFNMRPSCFYLRKTFSHLSQDAFNIYECSEWSYRINVLVSTNSTHSNLTLKLGVPDSIPHGLISLSSVSQPPAIAYSECFGEDLHGTKFHTVCNRRTDYTLGRIGEIQCPTKADALAVSKRCISSDSIIFSKVHKDSVDCQSSIIDPMTIRNRNKLPSTVGSVTFWPTETSVEAAIPDLASATMLIRLDGYTIQFRSDSNKCSPRFLSLSGCYNCEAGAKLELEHVTDFGTALGILECPSLGYTTYYEVKNTLEKSIRTMHLNGSHVEAKCYFRCPNSESQLTIRGELIYLFNDDIRHHNQTLSPGLSPKSGSGWDPFGWFKASWLRAIWAILGGTVSLIIGVVIIYMVFTLCLKVKKS
The following text describes a protein:
Function:
General amino acid permease with broad substrate specificity.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAVLNLKRETVDIEETAKKDIKPYFASNVEAVDIDEDPDVSRYDPQTGVKRALKNRHISLLALGGVIGPGCLVGAGNALNKGGPLALLLGFSIIGIIAFSVMESIGEMITLYPSGGGFTTLARRFHSDALPAVCGYAYVVVFFAVLANEYNTLSSILQFWGPQVPLYGYILIFWFAFEIFQLVGVGLFGETEYWLAWLKIVGLVAYYIFSIVYISGDIRNRPAFGFHYWNSPGALSHGFKGIAIVFVFCSTFYSGTESVALAATESKNPGKAVPLAVRQTLWRILVVYIGIAVFYGATVPFDDPNLSASTKVLKSPIAIAISRAGWAGGAHLVNAFILITCISAINGSLYIGSRTLTHLAHEGLAPKILAWTDRRGVPIPAITVFNALGLISLMNVSVGAANAYSYIVNLSGVGVFIVWGVISYTHLRIRKAWVAQGRSIEELPYEALFYPWTPVLSLAANIFLALIQGWSYFVPFDAGNFVDAYILLPVGILLYIGICVFKSNHFRTVDLRSINLDEGRRKDMEADLSDQESSLASSETMKDYKSATFFRYLSNIFT
The following text describes a protein:
Function:
Acts as a ribosome collision sensor, splitting the ribosome into its 2 subunits. Detects stalled/collided 70S ribosomes which it binds and splits by an ATP-hydrolysis driven conformational change. Acts upstream of the ribosome quality control system (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes and their subsequent degradation. Probably generates substrates for RQC; Endonuclease that is involved in the suppression of homologous recombination and thus may have a key role in the control of bacterial genetic diversity.
Sequence:
MIYPQNFEQKIGFDQIRQLLKDKCLSTLGEERVSDMSFTEQFEEVEEKLNQVTEFVRIIQEEDGFPDQFFFDVRPSLKRVRIEGMYLDEQELFDLRRSLETIRDIVRFLHRNEEEEENDVPYPSLKRLAGDIAVFPQLIGKIDGILNKYGKIKDNASSELARIRRELSSTMGSISRSLNSILRNAQSEGYVDKDVAPTMRDGRLVIPVAPGLKRKIKGIVHDESASGKTVFIEPAEVVEANNRIRELEGDERREIIRILTEFSNILRPSIPDILQSYEFLAEIDFIRAKSYFAIQTNSLKPTVEKEQLLDWTMAVHPLLQLSLAKHGKKVVPLDIELNQKQRILIISGPNAGGKSVCLKTVGLLQYMLQCGMLIPLHERSHAGMFSSIFIDIGDEQSIEDDLSTYSSHLTNMKIMMKSCNERSLILIDEFGGGTEPQIGGAIAEAVLKRFNQKGTFGVITTHYQNLKHFAEDHEGVVNGAMLYDRHLMQALFQLQIGNPGSSFAVEIARKIGLPEDVIADASEIVGSEYINADKYLQDIVRDKRYWEGKRQTIRQREKHMEDTIARYQTEMEELQKSRKEIIRQAKEEAERMLQESNARIENTIRTIKEAQAEKEKTRLVRQELNDFRTSLETMTSKEQEEKIARKMEKLKEKQERKKNKKNEPKTAASQTAATPKVIPITVGENVKIKGQTSVGQVMEINGKNATVAFGSIKTTVKLDRLERSNAAPKTEGIAKSTFVSSQTHDQMYEKKLNFKQDIDVRGMRGDEALQAITYFVDDAILVGMDRVRILHGTGTGILRTLIRQYLSTVPGVSHYADEHVQFGGAGITVVDFD
The following text describes a protein:
Function:
Cell adhesion molecule that promotes cell-cell contacts and plays important roles in the development of the nervous system. Acts by forming homophilic or heterophilic trans-dimers.
Subcellular Localization:
Cell junction, adherens junction. Cell membrane; Single-pass type I membrane protein.
Sequence:
METTQKEYWYFMVLMLILSWHGDATLPKTADSVVKLETNTTLTCTCPWSGNLSQISWEKRTDSQKEKVAVYHTTYGLHEFGKYKGRVKFLKSLPLDGSILITQTTEEDLGLYQCSVHSFPKGSWTKDIRVEKTAVDIDGSENRSEVVVEKGHNFTLRCHYVQNGTVHQVTFEKLGEKSKDTIALCNFSDGNFTGSDYKQRILLNCSSIQASLLIMNITDKDGGIYRCRLRTNSGNQTTTLSLSLLKWAGLPNMNLIFYAGAGAAGFIVLVILVATTLVYQNRRKKKRMKTRDKFQVVKKRQLNNYEQASVYDRMKKKAKHQDTDEIYVNIPNPPRRTKKKT
The following text describes a protein:
Function:
DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Nucleus.
Sequence:
MDALREAEAKLTVYVHPSNAADVRRAVARQLSSLLFSYEDRFDGVLLAHEATVESEQGKILNGLVPYFGVPVHANLLLYSPKPDMMLEGKVEMLGKESIHAIVLGVFSAAIMLDDIHEKFKFKRKKYGGKFVSRSDKQHVIKKGSMIRFSVKRYGLIFSPLDSFKIFIHCLLSTVKHLYSKVMALVCYYICNLLVVCSTCCTLFTNMHCSSMLELFFPWCAYYDRSPEKSHFDTMALKSNNKTM
The following text describes a protein:
Function:
An odorant receptor which affects chemotaxis to the volatile odorant diacetyl. Specifies AWA neuronal cell fate via the odr-7 pathway.
Subcellular Localization:
Cell projection, cilium membrane; Multi-pass membrane protein.
Sequence:
MPMPSALRYLQYTGCALTEVLSIYLFLLIFSKASLKIGSYKYLMATFTVFSMIYGIVEVLTQPVMHIEGTALIVYMDSFLRYEKVLGFHITAFYCSSFGVCVLLLSTHFCYRYMAVCRPHIVRNYTGARLLYFFIPAAVLGTTWLVTVEICEQPTPFNSEYLRESLKFYYDEDSYAVAQLSAVYYYYDKCGVLVIHWLQCFSILILYSIMGTSITSIVLFAFKTYKTVQTNTLMSAATRDLHRQLLFTLIIQSLVPFVILFAPVGLLFLLPFFNVHLGYFANAPGAWISFYPAIDALIALLMIRDFRNAVFCRKHNSSAQVTGNYDSMTISNFRRQSHM
The following text describes a protein:
Function:
Palmitoyl acyltransferase.
Subcellular Localization:
Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein.
Domain:
The DHHC domain is required for palmitoyltransferase activity.
Sequence:
MHRSGTTMAWNVFKFCTALRGLGSIMILLVLGVVGVTYYAVVLTNYGPALSQGGLDSLAALTILILFHFLLAMLLWSYFSVVFTDPGVVPPNWRPSTDEERGESDPLNSLDFVGLQSDSSSSNPRVRFCRKCNQLKPSRCHHCSVCGRCVLKMDHHCVWVVNCVGALNYKYFLLFLFYTFLETTLVTLVLMPHFIAFFSDEEIPGTPGTLATTFLAFVLNLAFALSVMGFLIMHISLVAGNTTTIEAYEKKTTTKWRYDLGKKKNFEQVFGMDKRYWLIPGYTEEDLRRMPELQGLEYPSKPDFDSQ
The following text describes a protein:
Function:
GPI-anchored cell surface protein that regulates T-lymphocytes proliferation, differentiation, and activation. Regulates the T-cell receptor (TCR) signaling by interacting with component CD3Z/CD247 at the plasma membrane, leading to CD3Z/CD247 phosphorylation modulation. Restricts the entry of murine coronavirus, mouse hepatitis virus, by interfering with spike protein-mediated membrane fusion. Also plays an essential role in placenta formation by acting as the main receptor for syncytin-A (SynA). Therefore, participates in the normal fusion of syncytiotrophoblast layer I (SynT-I) and in the proper morphogenesis of both fetal and maternal vasculatures within the placenta. May also act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MSATSNMRVFLPVLLAALLGMEQVHSLMCFSCTDQKNNINCLWPVSCQEKDHYCITLSAAAGFGNVNLGYTLNKGCSPICPSENVNLNLGVASVNSYCCQSSFCNFSAAGLGLRASIPLLGLGLLLSLLALLQLSP
The following text describes a protein:
Function:
Involved in pre-mRNA splicing. This protein is associated with snRNP U2. It binds stem loop IV of U2 snRNA.
Miscellaneous:
MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MVEPARKKQRIDRDTHHTVAEPVTEAKNTLYVSQLNEKINMQRLRVNLFLLFATFGEVLKVSMNFKKQRGQAFITMRTIDQASLAQISLNGERFFGKPLKVEFSKSETKTL
The following text describes a protein:
Function:
Component of the Clr4 methyltransferase complex (ClrC) which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me. ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 methyltransferase activity for the methylation of H3K9. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci. Rik1 is involved in the RNAi-mediated targeting of ClrC to heterochromatic repeat elements. Rik1 also has a function in meiotic telomere clustering.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Chromosome.
Sequence:
MALCVHSFWATAVDTATSCHFISSENCLVLLQALKINIYLCSEVHGLQFFTSIPLFSTVKHIRPYRPPGLDRDYLFVVLNDDTYFSIYWDEDYQKVIVDHPPVRYRVTFPWNRNAKSYCLVDLRMRAIFLSIDEISMICIRILSAEERLKTGRSIDSGFPFSFPVHLIYDMCILNDSSTPTLVVLHSDGLDCYVTAFLLDLSSKSLGKGIRLFERVKPSMIMPFGKRGLLVFESLFIHCMYRGNFVTINGPCTTYMHWTPLKGQKMHYIVCDTNGYLFGVYSSILGKNKWSLVMERLPIPPFDFITSLNSIHEGLLFIGSKNSESKLINLSTLKDVDSIPNLGPIHDLLVLKNDIEKSFLVCAGTPRNASLIYFQHALKLDILGQTKISGILRAMVLPSYPEHKLFLGFPSETVAFNIKEDFQLELDPSLSTKERTIALSGTNGEFVQVTSTFLCIYDSAKRSRLVYIEKITNAACYQEYSAIVINGTALAIFKKDTEVARKVFESEISCLDFSAQFQIGVGFWSKQVMILTFSDNSSISCAFQTNVPSLPRNIILEGVGVDRNLLLVSSGSGEFKSYVLFKNNLVFSETKHFGTTPVSFRRFTMNIGTYIICNNDCPHMVYGFNGALCYMPLSMPQSYDVCQFRDNSGKDFLISVSLGGLKFLQLNPLPELTPRKVLLEHVPLQAIIFQNKLLLRTLENRYEDYESYKENYHLELVDSYDDNSFRVFSFTENERCEKVLKINESSLLVGTSIIEQDKLVPVNGRLILLEFEKELQSLKVVSSMVLSAAVIDLGVYNDRYIVAFGQQVAIVKLTEERLMIDSRISLGSIVLQLIVEGNEIAIADSIGRFTIMYFDGQKFIVVARYLFGENIVKAALYEGTVYIIATNSGLLKLLRYNKDAKNFNDRFICESVYHLHDKVSKFQNFPITNTNSFLEPKMLFATEIGAIGSIVSLKDKELELEELTRKIRKLKFSYLSSMDYESIEADLISPVPFIDGDLVIDVKRWASSELFRLCRSVEHRESLNSYQKVQALLEEIQSLC
The following text describes a protein:
Function:
Monovalent cation-selective ion channel activated by intracellular Ca(2+) in a voltage- and temperature-dependent manner. Mediates the transport of Na(+), K(+) and Cs(+) ions equally well. Activated directly by increase in intracellular Ca(2+), but is impermeable to it. The activation mechanism of TRPM5 involves a multistep process. TRPM5 activation involves ligand binding (i.e., tastant molecule, glucose stimulation) to Gq/G-protein coupled receptors (GPCR) and leads to the breakdown of phosphatidylinositol bisphosphate (PIP2) into diacylglycerol (DAG) and inositol trisphosphate (IP3), IP3 binds to its receptors in the endoplasmic reticulum and cause Ca(2+) release. Simultaneously with the intracellular Ca(2+) release, DAG activates the protein kinase C (PKC), which phosphorylates the TRPM5 channel. This phosphorylation combined with the bound Ca(2+), leads to a robust inward current allowing the entry of sodium ions (Na+) into the cell. This ion influx depolarizes the cell membrane, generating action potentials that propagate TRPM5 signals. Is a key player in sensing sweet, umami and bitter stimuli (Probable). May also be involved in sensing semiochemicals. Involved in insulin secretion by pancreatic beta cells.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Contains two Ca(2+)-binding sites that are allosterically coupled. The binding site in the intracellular domain modulates the voltage dependence and the accessibility of Ca(2+) in the transmembrane domain.
Sequence:
MQTTQSSCPGSPPDTEDGWEPILCRGEINFGGSGKKRGKFVKVPSSVAPSVLFELLLTEWHLPAPNLVVSLVGEERPLAMKSWLRDVLRKGLVKAAQSTGAWILTSALHVGLARHVGQAVRDHSLASTSTKIRVVAIGMASLDRILHRQLLDGVHQKEDTPIHYPADEGNIQGPLCPLDSNLSHFILVESGALGSGNDGLTELQLSLEKHISQQRTGYGGTSCIQIPVLCLLVNGDPNTLERISRAVEQAAPWLILAGSGGIADVLAALVSQPHLLVPQVAEKQFREKFPSECFSWEAIVHWTELLQNIAAHPHLLTVYDFEQEGSEDLDTVILKALVKACKSHSQEAQDYLDELKLAVAWDRVDIAKSEIFNGDVEWKSCDLEEVMTDALVSNKPDFVRLFVDSGADMAEFLTYGRLQQLYHSVSPKSLLFELLQRKHEEGRLTLAGLGAQQARELPIGLPAFSLHEVSRVLKDFLHDACRGFYQDGRRMEERGPPKRPAGQKWLPDLSRKSEDPWRDLFLWAVLQNRYEMATYFWAMGREGVAAALAACKIIKEMSHLEKEAEVARTMREAKYEQLALDLFSECYGNSEDRAFALLVRRNHSWSRTTCLHLATEADAKAFFAHDGVQAFLTKIWWGDMATGTPILRLLGAFTCPALIYTNLISFSEDAPQRMDLEDLQEPDSLDMEKSFLCSRGGQLEKLTEAPRAPGDLGPQAAFLLTRWRKFWGAPVTVFLGNVVMYFAFLFLFTYVLLVDFRPPPQGPSGSEVTLYFWVFTLVLEEIRQGFFTDEDTHLVKKFTLYVEDNWNKCDMVAIFLFIVGVTCRMVPSVFEAGRTVLAIDFMVFTLRLIHIFAIHKQLGPKIIIVERMMKDVFFFLFFLSVWLVAYGVTTQALLHPHDGRLEWIFRRVLYRPYLQIFGQIPLDEIDEARVNCSLHPLLLESSASCPNLYANWLVILLLVTFLLVTNVLLMNLLIAMFSYTFQVVQGNADMFWKFQRYHLIVEYHGRPALAPPFILLSHLSLVLKQVFRKEAQHKRQHLERDLPDPLDQKIITWETVQKENFLSTMEKRRRDSEGEVLRKTAHRVDLIAKYIGGLREQEKRIKCLESQANYCMLLLSSMTDTLAPGGTYSSSQNCGCRSQPASARDREYLESGLPPSDT
The following text describes a protein:
Function:
Specifically catalyzes coenzyme A (CoA)-dependent acylation of 1-acyl-sn-glycerol 3-phosphate (2-lysophosphatidic acid/LPA) to generate phosphatidic acid (PA), an important metabolic intermediate and precursor for both triglycerides and glycerophospholipids. Does not esterify other lysophospholipids. Acyl donors are long chain (at least C16) fatty acyl-CoAs: arachidonoyl-CoA, linoleoyl-CoA, oleoyl-CoA and at a lesser extent palmitoyl-CoA. Additionally possesses low triacylglycerol lipase and CoA-independent acylglycerol transacylase activities and thus may play a role in acyl-chain remodeling of triglycerides. In vitro may express hydrolytic activity against glycerolipids triacylglycerol, diacylglycerol and monoacylglycerol, with a strong preference for oleic acid as the acyl moiety. However, the triacylglycerol hydrolase activity is controversial and may be very low. Possesses phospholipase A2 activity.
Subcellular Localization:
Lipid droplet. Membrane; Single-pass membrane protein.
Sequence:
MYDAERGWSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGIPLEQTLQVLSDLVRKARSRNIGIFHPSFNIGKFLRQDLYKYLPANVHQLISGKICVSLTRVSDGENVLVSDFQSKDEVVDALICSCFIPFYSGLIPPSFRGVRYVDGGASDNVPFIDAKTTITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLRGYLDAFRFLEEKGICNKPQRGLKSSSEGMDSEVTAPGWENTSLDSSPEPAALAMRLDGDELLDHLRLSILPWDESILDTLSPELATAVSEAMKDKGGYMSKICNLLPIRIMSYVMLPCTLPVESAIAIVQRLVTWLPDMPDDVQWLQWVTSQVFTRALMCLLPASRSQMPVSSEQASPCKPEQDWHCWTPCSPEDCPAEAKAEATPRSILRSSLNFFWGNKVPAGAEGLSTFPSFSLEKNL
The following text describes a protein:
Function:
Actin maturation protease that specifically mediates the cleavage of immature acetylated N-terminal actin, thereby contributing to actin maturation. Cleaves N-terminal acetylated methionine of immature cytoplasmic beta- and gamma-actins Actb and Actg1 after translation. Cleaves N-terminal acetylated cysteine of muscle alpha-actins Acta1, Actc1 and Acta2 after canonical removal of N-terminal methionine.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal proline-rich disordered region contributes to the interaction with PFN2.
Sequence:
MTSPCSFPLKPTISPIIHETPDTNIPPPLPLNPPDLALPSPPCSLHTSISSPLPPPPPPPAPPPPPPPPPLPSAVEPVLPHVYGLKNSQLLKEALEKAGPAPKGKEDVKRLLKLHKDRFRSDLQWILFCADLPSCIQEGPQCGLVALWMAEALLSTPDSVSLERLVQVAKERGYTAQGEMFSVADMAKLAQETLDCQAELLCGGLGGPNRERVLQHLITGHPLLIPYDEDFNHEPCQKKGHKAHWAVSAGVLIGVQNVPSPGYIEDSELPGLFHPVPGAPHQPPSFPEESSPGALFLLSKQGKSWHYQLWDYSQVRESNLQLTDFSPARAADGQVYVVPAGGVEAGLCGQALLLRPQEGSH
The following text describes a protein:
Function:
Polyribosome-associated RNA-binding protein that plays a role in neuronal development and synaptic plasticity through the regulation of protein synthesis of mRNAs. Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors. Mainly acts as an activator of mRNA translation: promotes translation of stored mRNAs in oocytes. Can also act as a negative translational regulator of specific mRNAs. Represses translation of the microtubule-associated protein futsch mRNA to regulate microtubule-dependent synaptic growth and function. Localizes to specific N6-methyladenosine (m6A)-containing RNAs as part of a complex with the m6A reader Ythdf and thereby regulates axonal growth in the mushroom bodies and neuromuscular junctions. Specifically recognizes and binds a subset of N6-methyladenosine (m6A)-containing mRNAs in embryos, promoting formation of a phase-separated membraneless compartment that mediates degradation of maternal mRNAs. May also be involved in microRNA (miRNA)-mediated translational suppression as part of the RNA-induced silencing complex (RISC). Required for stability of the central pair of microtubules in the spermatid axoneme. Regulates photoreceptor structure and neuromuscular junction (NMJ) neurotransmission in the eye. During embryogenesis, involved in germline fate determination.
Subcellular Localization:
Cytoplasm, Cytoplasmic ribonucleoprotein granule. Cytoplasm. Perikaryon. Cell projection, neuron projection. Synapse. Cytoplasm, Stress granule. Note=Localizes in the neuronal soma and cell processes, and in pre- and postsynaptic neurons, as well as in postsynaptic muscles.
Domain:
The C-terminal disordered region undergoes liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors.
Sequence:
MEDLLVEVRLDNGAYYKGQVTAVADDGIFVDVDGVPESMKYPFVNVRLPPEETVEVAAPIFEEGMEVEVFTRTNDRETCGWWVGIIKMRKAEIYAVAYIGFETSYTEICELGRLRAKNSNPPITAKTFYQFTLPVPEELREEAQKDGIHKEFQRTIDAGVCNYSRDLDALIVISKFEHTQKRASMLKDMHFRNLSQKVMLLKRTEEAARQLETTKLMSRGNYVEEFRVRDDLMGLAIGSHGSNIQAARTVDGVTNIELEEKSCTFKISGETEESVQRARAMLEYAEEFFQVPRELVGKVIGKNGRIIQEIVDKSGVFRIKVSAIAGDDEQDQNIPRELAHVPFVFIGTVESIANAKVLLEYHLSHLKEVEQLRQEKMEIDQQLRAIQESSMGSTQSFPVTRRSERGYSSDIESVRSMRGGGGGQRGRVRGRGGGGPGGGNGLNQRYHNNRRDEDDYNSRGDHQRDQQRGYNDRGGGDNTGSYRGGGGGAGGPGNNRRGGINRRPPRNDQQNGRDYQHHNHTTEEVRETREMSSVERADSNSSYEGSSRRRRRQKNNNGPSNTNGAVANNNNKPQSAQQPQQQQPPAPGNKAALNAGDASKQNSGNANAAGGASKPKDASRNGDKQQAGTQQQQPSQVQQQQAAQQQQPKPRRNKNRSNNHTDQPSGQQQLAENVKKEGLVNGTS
The following text describes a protein:
Function:
Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues in glycosaminoglycan chains. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N-resulfated heparin.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MKKKQQQHPGGGTDPWPHGAPVGGAPPCLGSCKRRIPLLPFLRFSLRDYGFCMATLLVFCLGSLFYQLSGGPPRFLLDLRQYLGNSTYLDDHGPPPSKVLPFPSQVVYNRVGKCGSRTVVLLLRILSEKHGFNLVTSDIHNKTRLTKNEQMELIKNISTAEQPYLFTRHVHFLNFSRFGGDQPVYINIIRDPVSRFLSNYFFRRFGDWRGEQNHMIRTPSMRQEERYLDINECILENYPECSNPRLFYIIPYFCGQHPRCREPGEWALERAKLNVNENFLLVGILEELEDVLLLLERFLPHYFKGVLSIYKDPEHRKLGNMTVTVRKTVPSPEAVQILYQRMRYEYEFYHYVREQFHLLKRKLGLKSRVSGPPVRPQFFIPTPLETEEPIDDEEQDDEKWLEDIYKR
The following text describes a protein:
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). Required for activated transcription of the MtnA gene.
Subcellular Localization:
Nucleus.
Sequence:
MNQIEIQELTTHLSQALDQNYDVVNMDAVLCVICALEGTTITKEQLEATRLAKYINQLRRRTKNEHLARRAKSLLKKWREMVGIQQTATENLAHPSQISSSQPALDLVKSPITSFITEPIAPSQQIVSDLHSNIDSAEPPLSGEHTLLHPNFSNLVNSIKDSDRHENIAITTLHTHKDRRHSHSIRSCHVASPQPIVIDHSVNSVINLTDDSTVKINEASVVIDIASDSDENDNNGSLNPKKLNSIVPAPLPIPSTPSSRQRKLKKEKRSKEREGQVATNTRFGAKASDGFQQAALTTDSEIFSLSNSSMSSIVSGDATSSYSQNKSRLNSNELTFTGRFKAVDHLFRSTESGKHKIDEYSAYDSNASCSRLSPSTVDEVKKAEHLFDAQLTNTTANQIPMSAVSIGYESNTRHEYLESDSPSQIPKRRGRKKGSKGVDALIAKESSSLSQQIFFGGSTVKKVKTTKELFNEIQSRKLSVSMQSSASNLSNSSTNRDLPSHTTFPRQTSSCSDTSMNSPHILETLSGSAIFASKIDDLGNTDSDTVTSDPSHDSNKSQEIKECTSLDSNSNSIQSLPLANNRENLIPTNVNDITTQLMHLIHSLNSPLSEIEIERVYQEKIIPCTCIVIEGVQGTLGESNNSTLDEQSYNAKISLNSKDNLSCHNQDNYSTSQRSVNGEVIDTQPKLVKSIFDLDFDDNDDPLYFIMDEIQKPIARADELKNNKSDTKNINFGASAQNASLNIIHFNDDAQQDNSNQERGKNETQNAIPAFTVHEDPDCLARQRFYIQTNKVTSFHINALHNYYIPNINGNWDSVESFTSFQSEHTIMDTMESYTVTNGADVVPKYGLLTSDRIRKDLSSLKSIKPYRVKNFTSLISPFLGVAKCLPTCRRARRRFKNFVNSSTANDKISNNFESLENMKTSFKNCNPLNVKIDGTTSAIYSHNENHVPMQVNTNVEQLPPSQSFSSNAISYNLLKLADDKVCHDGISDKSSNTGCQGNSPYSSSSSSSYSGRKEDQHIITKNLQNKNIQLNSRKSDMKRRKRIYLENDSKKKKHYRKRIKTAVNRTFSNLHRNLYSIDSENGMKNDYKNEYGNSNNEEYAIVQRPAGDGENCSNHIVLTIKKTPSKINSPANSMTAFSPPSTSDGANLQKSILDLRLEDTNISQSITEIPQKKDLSKTDRIVHQSRSSAYRRIFRKPDKSQTKFIDLDLKHLFHLKANSPCISANAKLHNKLFFPHELSRDNTSGIRERLINYSSSSSSSYDDDSEVENTSFLKKANVNKFSASNNRNLKTETETCAATAISEFKFESDEDSILTSLGDSDIDIQDEIQVINDKVDYCNDFQNNKMLESFNSIFVDSLRTNTKNASDNMGSSAHITSLESLKPENADAITRYCNNNNLGVNLSNELSNISAKPLKSFDSTMKLPSLGIEHCTGIKTSSDMASTNIAEKKLTRIQQFKEWHQVLQLRSYNNEPLIVLPYVLLE
The following text describes a protein:
Function:
Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.
Subcellular Localization:
Synapse, synaptosome.
Sequence:
LDNRLLSSEEIQLKIHQLKDESLECSERICLLASECQDAGIKIISMLDEQGEQLNRIEGSMDHIEKDVKEAEKSLMELSKCCGLNVCPSKNRKKAGRKPCKTILDDEEDLNHNVVFEQPRYVTHLKKKELLEARSRGCKAQKANDARDCKTEENLTQVGNILGNLKNMALEMGNVLHKQNKQVNWINKKADINTSLIEQANAKAKNCIDY
The following text describes a protein:
Function:
Plant non-specific lipid-transfer protein that binds phospholipids in vitro. Required for correct pollen exine patterning by controlling the continuity and homogeneity of the primexine distribution.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor. Note=Localizes to the microspore plasma membrane.
Sequence:
MERSHLAVLLGLLAFAAGVPAAAAATAVEGAQAATAEASCEPSILATQVSLFCAPDMPTAQCCEPVVASVDLGGGVPCLCRVAAEPQLIISGLNATHLLTLYAACGGLRPGGARLAAACEGPAPPASIVTAPPPPVAFRRKPPAREAPPPPPAAEKLSPPPQQHDDSDHNKRVGPLPRGSPPPYAQSVPVGPAAAPPPPRSGASSSLQAPLAATTTIVAITLIAAAQY
The following text describes a protein:
Function:
Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites. Decreases the levels of the pro-proliferative prostaglandins such as prostaglandin E2 (whose activity is increased in cancer because of an increase in the expression of cyclooxygenase 2) and generates oxo-fatty acid products that can profoundly influence cell function by abrogating pro-inflammatory cytokine expression. Converts resolvins E1, D1 and D2 to their oxo products, which represents a mode of resolvin inactivation. Resolvin E1 plays important roles during the resolution phase of acute inflammation, while resolvins D1 and D2 have a unique role in obesity-induced adipose inflammation.
Sequence:
MGKDKGYNGGHVINTASIAGLHVAPASPAYNTSKCAVVAMTRAFGSKLHLDRHGVKVSCLCPDPIDTELWTQVSEHLSSEERTAAYFDVQNQKVQRWRYWTSTKDWGRRLPPDTRRSTGKKAACSISVTSPTNPNWKEAVYSGILLGLKYMGKDNGFNGGHIISTSSIAGIYVLPSVPAYNASKVAVVAMTRAKLHLDRHGVRVNCVCPDPINTPLWGQISGHFKLDPITAPLHDVYDKRAQRPEDVARGFIKLLEDDDKNGAALLSLHTDGLQYYNFQEPTPEF