lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MGLRAPFHFLLLLLRRPGGPFRGLASEGPREALPVIRIPQPLKLRREARARGGPAPRVSVPRPGPLLIAARRPEFSQPLRFTVGRWERAPLASRGWKHRRSRGDHFSIERTHRLVPALPEESGTGSAFAALGLQPRVLDALCQAMPSVVRPTWVQRRAIPPLLSGHHLLCAAETGSGKTLSYLLPLLQRLLRRPRLTTGPAPRGLVLVPSRELSEQVRAVAGSLGQGLELCVREIGGGRGMGSVKSQLSKEPLADLLVATPGALWKALKRQLVSLGQLCFLVLDEADTLLDESFLELVEYILSKSPIAENREELEDPFNPRAQLVLVGATFPEGVGELLSKVTDLGNLTTITSPRLHCVMPHVRQRFLRLKGSEKVTELIQALKHRGEDNPGSSGAILVFCNSSSTVNWLGYILDDHKIPHLRLQGQMPATMRAGIFQSFQNGTKDILLCTDIASRGLDSTRVELVINYDFPPTLQDYIHRAGRVGRVGSEVLGSVLSFVTHRWDVDLVQKIELAARRRRSLPGIKTFVKEPLEKAKVMNRIINET
The following text describes a protein:
Function:
Binds together with bS18 to 16S ribosomal RNA.
Sequence:
MNQYDLNLILNPNISAEQVQTEKDYIENAVRNAGAEISNLDDLGNRRLAYQVGKDREGYYLMYTIKASGNPETAIASSLRLRDNVRRVLVVKDRPEWKTKKA
The following text describes a protein:
Function:
Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Subcellular Localization:
Cytoplasm.
Sequence:
MTSRDSASSEITPAVLLRAYACGIFPMAESADDPTLFWVEPELRGVIPLGGFRVASRLARTVRSDGFRVTVNTAFKATIAGCAAPQAGREDTWINKRIRDLYSGLFELGHCHSVEAWQGDDLVGGLYGVSLGRAFFGESMFHTARDASKVALVHLVARLIHGGFELLDTQYVTEHLKNFGAVEIPRRRYTALLDKALAGEPGDFLKLSPGEAIPGARALEIIASRQ
The following text describes a protein:
Function:
Functions as a ribosomal silencing factor. Interacts with ribosomal protein uL14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
Subcellular Localization:
Cytoplasm.
Sequence:
MNEKELLELVVKAADEKRAEDILALDVQDLTSVTDYFVITSSMNSRQLDAIAANIREKVAQAGFKGSHVEGDAAGGWVLLDLGAVVVHIFSEEMRAHYNLEKLWHEANSVDISEALA
The following text describes a protein:
Function:
Phosphatase with broad substrate specificity. A truncated (soluble) version of the protein is responsible for the production of (E,E)-farnesol from (E,E)-farnesyl diphosphate. Acts as a fructose-2,6-bisphosphate 6-phosphatase.
Miscellaneous:
MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
Subcellular Localization:
[Repressible alkaline phosphatase]: Vacuole membrane; Single-pass membrane protein. Note=The full-length version is found in lysosome-like vacuoles; [Soluble alkaline phosphatase]: Cytoplasm. Note=The truncated version of the protein is soluble.
Sequence:
MMTHTLPSEQTRLVPGSDSSSRPKKRRISKRSKIIVSTVVCIGLLLVLVQLAFPSSFALRSASHKKKNVIFFVTDGMGPASLSMARSFNQHVNDLPIDDILTLDEHFIGSSRTRSSDSLVTDSAAGATAFACALKSYNGAIGVDPHHRPCGTVLEAAKLAGYLTGLVVTTRITDATPASFSSHVDYRWQEDLIATHQLGEYPLGRVVDLLMGGGRSHFYPQGEKASPYGHHGARKDGRDLIDEAQSNGWQYVGDRKNFDSLLKSHGENVTLPFLGLFADNDIPFEIDRDEKEYPSLKEQVKVALGALEKASNEDKDSNGFFLMVEGSRIDHAGHQNDPASQVREVLAFDEAFQYVLEFAENSDTETVLVSTSDHETGGLVTSRQVTASYPQYVWYPQVLANATHSGEFLKRKLVDFVHEHKGASSKIENFIKHEILEKDLGIYDYTDSDLETLIHLDDNANAIQDKLNDMVSFRAQIGWTTHGHSAVDVNIYAYANKKATWSYVLNNLQGNHENTEVGQFLENFLELNLNEVTDLIRDTKHTSDFDATEIASEVQHYDEYYHELTN
The following text describes a protein:
Function:
Component of the gamma-tubulin ring complex (gTuRC) which mediates microtubule nucleation. The gTuRC regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments, a critical step in centrosome duplication and spindle formation.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Sequence:
MDQEMRKLVKRLTQFQEGSENFRRTLQFVQSNFRFHRYLDPDSHKITRTFKGIREKLLIHSHSEKASALDRSVETFLETPLSEKSKHNKTEGHYAVLSLLLNLSNSPINAAFQARAPQHEPAPEPKFDWTRYLLEGLEPIKSFQDSSDEEWSDEEEVPLTDQRLSREGALQADSQYITPSRRHGSSKLYGAGWEELNESVVVQYWQGEQDSTLHSDHVTHHMTRQWSEREVSSEPFLSDIPRTTMTETHIIRETIWTLLGAGNSFLYQRRDDGYVAREDVQVTHLTPTALHGITRQLAELGSKVLQLQAFIDRVQSHPMSYCTPKKAHRPSISSEKELESPKVEVANGAQAGSRLPSVTDSESGLGRTRSLPDLLKDTRDQDAAETKHFNCQTYEAFADGLAKVLQDFRSSLIEEEKKVVAQDETYTLCMFKDWLLSAWVPRLHLAHTMYRQGIGGPSKELSSHRVYSLLHVLHMAIKEHFCLAFQDNKELDLLWHLWTVTTGPYISFITKWLRYGILSDPAQEFAIRRNPEIHIKAESYWKKAFSLQTLQTDDTDGALLSVPANKKGERRSSAKRSVPSAVPEFLQPVLSHILLAGKSMEILEATGKLTRARQDVLGGEMIKTEYLQYSSDLEILFQMSNCMKPGGHQTYTQAMSADNQSSSRLPRSSGSAGDVAEMVERQLSLRGYNDPLIASGISHVGLRRDHAGDDFDQVKEVERDADLSKPLELVLYRDLYPGIVRRCQSVCRQLAAVLKKDFSLQDHLLSMRRFFLLEAGDVMYDFYSELFDKIRRHESWQDTLNLNYHLQETLSVRYPEEAARIMVSVEPERLTGKMATQPIHALDSLTLHYKVPWPVDIVIHHHALDVYNQVFRFLLQVKRAQYCLQQLRFPDLLISANLGHLTEDSDHERLHRGQADETLREKLPLIHRLFILRFRLLHFVNAVHNYLMTRILYSTSLEFSAAIDQALDLDQILAAHKSYLAKISERCLLHHKVSFVREAVSKVLNLAITFQRRWDAGVHTFSIENVAKAEEEFFNCNEFLSTLLANIIRRGTFPHLEALALSLSGPKPKAKSGDQDER
The following text describes a protein:
Function:
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Subcellular Localization:
Cytoplasm.
Domain:
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Sequence:
MSGAGVLAGLGTALPARLVTNEELSRHLDTDDEWIRSRTGIGQRYWSDGASTGDLAVEAGQRALKAAGTDTVDLVVLATTTPDHPCPATAPDVADRLGLSGVAAYDIAAVCSGFIYGLASAVAHITAGLVGSALVIGAETYSTILDPLDRTTSVIFGDGAGAVVLRSGSVDERGAFLGFDLGSDGALKDLIVIPGGGSRERAAAERPQPAGAYFTMQGKPVFRHAVTRMTSSAGALLDRTGWSPASVDRFVGHQANARILHAVADQLRIDGARTVIDLDRVGNTSAASIPLALSRACGEGLLSPGDRVLLSAFGGGLTWGSTALLWPDITAL
The following text describes a protein:
Function:
Endothelins are endothelium-derived vasoconstrictor peptides. Probable ligand for G-protein coupled receptors EDNRA and EDNRB which activates PTK2B, BCAR1, BCAR3 and, GTPases RAP1 and RHOA cascade in glomerular mesangial cells. Also binds the DEAR/FBXW7-AS1 receptor. Promotes mesenteric arterial wall remodeling via activation of ROCK signaling and subsequent colocalization of NFATC3 with F-actin filaments. NFATC3 then translocates to the nucleus where it subsequently promotes the transcription of the smooth muscle hypertrophy and differentiation marker ACTA2.
Subcellular Localization:
Secreted.
Sequence:
MDLKVWISVLSVFWTGLDWTFCAVLAQPSAQTPSAAGISAQLHVRHKRCSCATFLDKECVYFCHLDIIWVNTPERVVSYGLGNAPRAKRALPDSMATSIQPRCLCVREDDSSCANFCHRRDTETGTPPRREAPLGTKPGGGTRHTERMKKNMAWKAVLRARLLLQTWRDRGRHRVRVRAPPPPSDSPQRIGSSLRRILQPEERSPLSQRGFRFSPGLRNI
The following text describes a protein:
Function:
Downstream effector of Rap required for cell adhesion and migration of neural crest precursors during development.
Sequence:
MGSSIFLGLQPSPSHWLKSSVVIHEDAPTMFYGTQLIMSPPTKNKLKRQSQLLSTMLSRTLSYKYRDLDSTFCSLGASDDPSELSTQLSAPGVLKVFGDSVCTGTHYKSVLATGSSSAQELVKEALERYALDPECAGQYVLCDVVGQAGDSGQRWQAQCFRVFGDNEKPLLIQELWKPREGLSRRFELRKKSDVEELASRDVDTTTAGINAQARRLQRIRAKGTPALTSEAAQSSPPTRLRRTVSETSLSPAPSLPEAAQRPEEPVPEAMRYSLYQCPHLLLLQGYSQQHDSLVYVLSKERHTVGQRTPSSKPSISLSAPDILPLHCTIRRHQSPEGGPAGTRLVLEPITGASVSVNFSEVGRNPVVLQHGDLLSLGLYYLLLFKDPGQAQPLPACALARLGAAPQSCRMCGAVLRARGAPSLPAAVVRRRSLLLEFEPDVEDTLLQRIMTLIEPGGDDHKLTPAFLLCLCIQHSAMHFQPGTFRHLLLKISKRVRDTVWEKTKELAEKQAQLQEPISWASFPMADLVPDLQHILFWMSNSIELLYFIQQKSPLYVQSMEEELDVTGSKESLFSCTLTASEEAMAALEEVVLYAFQQCVYYLSKCLYVCLPALLECPPFQTERRESWRSGPALPEELRRVVSVFQATLDLLQQLQMHPEVASQMLAYLFFFSGTLLLNQVLDKGPSLSCFHWPRGVQVCARLQQFLEWARSAGLGAPAERFFRKLSCTLHLLATPRAQLIQMSWATLRVTFPALNPAQLHRLLTQYQLASAMGPVSAWEPGAPDGPEAFQSEDILESYENPPPIVLPSQGFQVDLEADCVEDSIYQHLLYIRHFLWGLRGQASPDSGPAQPESIEGLYHTIPEGHLEGHGCPLANRDPGRVAVETAPPHSLPVTGAPRAQGPPGRQPTRGDRRGSQAGSLHTDSSCMLTPPSTPLGLEPAGPSWPEPSGLCGRAVLDGQRNGPGGLPGAVLEGDAIQDAEPPAEASSPSSSAEDFCYVFMVELERGPSGLGMGLIDGMHTPLGAQGLYIQTLLPGSPAASDGRLSLGDQILEVNGSSLRGVSYMRAVDLIRHGGKKMRFLVAKSDMETAKKIRFRNPPS
The following text describes a protein:
Function:
Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Carrier of the L-malonyl group (malonyl-S-PigH), which is decarboxylated by PigJ to yield a C2 carbanion acetyl-S-PigH. Then the pyrrolyl group of pyrrolyl-S-cysteinyl PigJ intermediate is captured by the C2 carbanion acetyl-S-PigH to yield the pyrrolyl-beta-ketoacyl-S-PigH. In the last step, PigH catalyzes the decarboxylative condensation between the pyrrolyl-beta-ketoacyl (pyrrolyl-beta-ketoacyl-S-PigH) and L-serine to yield 4-hydroxy-2,2'-bipyrrole-5-methanol (HBM).
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MNDVTTETYETLKQSVLHTFAQLTGYNVSELSLTSHLENDLGVDSIALAEIAVSLSRQFQLNTPLLIQDINTIKDALDGILQREFQLSEKVEPAAIALSGDADLWLGNLVRQIFASHSGYDVNALALDAEIESDLGIDSVSVASAQGELFNTLQLNSETIIANCNTLSALKQCLAARLVQEKGQDWFEQRGRGQSDSAIDHDADTTAEVTPPTATPVAINAEIGDPRTMRDFVGIEHPDIFHKAREFHLFYQDKKKRQLYFYGMPLETPCKNRAVMFDEATGQHREFLMFGSNSYLGLSNHPEIIHAIQDAASLYGATNTGCRIIAGSNVLHLELERKLAKLKGRDDCIVYPSGYSANLGCISALTSRHDLVFTDAINHMSIQDGCKLAGAQRKIYNHSLTSLEKSLAKYADHPGGKLIVTDGVFSMHGDIVDLPRLMKLAERYGARVLVDDAHSTGVLGKTGAGTSEHFNMKGQVDLELGTMSKALSGLGGYVCGDGDVVEYLRFYSNSYVFAATIPAPVAAGVIASIDVMLREPERLAKLWDNIYYFRTRLLNAGFDLENSDSAIIPIVVGDDAKTLFFGRAVRARGMFCQTVVFPGVSVGDARLRISITSEHTREDLDEAYAILVASALEVGVPVNASAHQEENASVAEA
The following text describes a protein:
Function:
Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MTESPIVLDVEIRNWVVIPILIVLFIVSALKLNISRIMQINSGKPQDVEKTMQMQTINRVRRLVSFYNRIPQKSFFIRKAYLCGTTGSKTNKGILSSIAPTQEDSNPMNMMFANSMFTDPSGITDMLKGNIMHLIPQVTMMSWVNHFFSGFVACKLPFFPLTIRFKTFLQRGIEMGSLDVSYVSSLSWYFLCWFGSEGINAILLGENMVSADSQLLQSSIEPGPPTQQTPIHKIYASEKENIEMIRYDSLMTNIEDRFLDNIKKKTSFDFNQINKNNNNNNNNTSNIKPKPIKSNLSNSKQSKRITYQKPSSLI
The following text describes a protein:
Function:
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Subcellular Localization:
Cytoplasm.
Sequence:
MKVYIETMGCAMNSRDSEHLLSELSKLDYKETNDPKTADLILINTCSVREKPERKLFSEIGQFAKIKKPNAKIGVCGCTASHMGADILKKAPSVSFVLGARNVSKISQVIHKEKAVEVAIDYDESAYAFEFFEKKAQIRSLLNISIGCDKKCAYCIVPHTRGKEISIPMDLILKEAEKLANNGTKELMLLGQNVNNYGARFSSEHAKVDFSDLLDKLSEIQGIERIRFTSPHPLHMNDGFLERFAKNPKVCKSIHMPLQSGSSAVLKMMRRGYSKEWFLNRVERLKALVPEVGISTDIIVGFPNESDKDFEDTMEVLEKVRFDTLYSFIYSPRPFTEAGAWKERVPLEVSSSRLERLQNRHKEILEEKAKLEVGKTHVVLVENRREMDNQIVGFEGRSDTGKFIEVTCKEKRNPGELVKVEIISHSKGRLMAATKGN
The following text describes a protein:
Function:
May be involved in maintaining Golgi structure and in intra-Golgi transport.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MASWLKVAEDLLEVVDRRAKIVATELSDEQSSPQPSGSSSQEGQAKKGKLREKGPLKLATGDAGSRTAAQKERKSRQPPRERIKIEKIRPSPPVDSSSVDASASKPDVSSSDVKGLDDDGGAEKEEKVVVDRKNDIGAEVVDTEVEVQSTERSAEDAAIVVDGAADSGNSEGAAESSAPSVPDERCEPSISNQDAEIVSAVNLEEKDSAMEVIHEKNIKEVPDTQVSGKSQDSKREGLSDSPESTENQQEHKLDSGSVKDQDQLEEARGLLKNVVKTGQSKEARLARVCAGLSSRLQEYKSENAQLEELLVQEREKCSSYEAHMKQLQQELSMSRVEGSRAESNMVDALTAKNAEIESLVKSLDSWKKKAAASEEKLAALQEDMDGLKRNRELTETRVIQALREELATVERRAEEERIAHNATKMAAVEREVELEHRAVEASNALARIQRAADQSSSRAMELEHKVAVLEVECASLQQELQEMEARNRRAQKKPSEEANQVIQMQAWQEEVERARQSQREAETKISSLEAELQKMRVEMAGMKRDAEHYSRQEHVELEKRYRELTDLLYHKQTQLESMASEKAALEFQLEKSIKQFHEVQMEAERSRVARRSASAWEEDADIKALEPLPLHHRHMATANQQLQKAAKLLDSGAVRATRFLWRHPVARVSLLFYLVFVHLFLMYLMHRLQDFASREGPTAMGGLANSDLP
The following text describes a protein:
Function:
Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MADKPDMGEVASFDKAKLKKTETQEKNTLPTKETIEQEKRGEVS
The following text describes a protein:
Function:
NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro). Can convert androsterone to epi-androsterone. Androsterone is first oxidized to 5-alpha-androstane-3,17-dione and then reduced to epi-andosterone. Can act on both C-19 and C-21 3-alpha-hydroxysteroids.
Subcellular Localization:
Microsome membrane; Peripheral membrane protein; Lumenal side. Early endosome membrane; Peripheral membrane protein; Lumenal side.
Sequence:
MWLYLAAFVGLYYLLHWYRERQVVSHLQDKYVFITGCDSGFGNLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKMESIAAATQWVKEHVGDRGLWGLVNNAGILTPITLCEWLNTEDSMNMLKVNLIGVIQVTLSMLPLVRRARGRIVNVSSILGRVAFFVGGYCVSKYGVEAFSDILRREIQHFGVKISIVEPGYFRTGMTNMTQSLERMKQSWKEAPKHIKETYGQQYFDALYNIMKEGLLNCSTNLNLVTDCMEHALTSVHPRTRYSAGWDAKFFFIPLSYLPTSLADYILTRSWPKPAQAV
The following text describes a protein:
Function:
Catalyzes the transfer of sulfate to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDGYGAKQEPLILTAVTKVEEARVPEEKHWTKEFQPTGKAFTGNLLHHPLVHMERLELLRNVCRDTALRNLSHTAVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAYSSIDEIPESIVHDHEKNGLPRLSSFSDSEIKKRLNLYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPSIIRKYRRNRMETKGLQFEDFVRYLGDPNHRWLDVQFGDHIIHWVTYVELCAPCEITYSVIGHHETLEDDAPYILKAAGIDRLVSYPTIPPGITVYNKTKVERYFSGISKRDIRRLYARFEGDFKLFGYRVPDFLLN
The following text describes a protein:
Function:
Chemoattractant for eosinophils and basophils. Acts as a ligand for C-C chemokine receptor CCR3 which triggers Ca(2+) mobilization in eosinophils. Also acts as a ligand for CX3C chemokine receptor CX3CR1, inducing cell chemotaxis.
Subcellular Localization:
Secreted.
Sequence:
MMGLSLASAVLLASLLSLHLGTATRGSDISKTCCFQYSHKPLPWTWVRSYEFTSNSCSQRAVIFTTKRGKKVCTHPRKKWVQKYISLLKTPKQL
The following text describes a protein:
Function:
Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation.
Subcellular Localization:
Cell membrane. Secreted, extracellular space, apoplast. Endoplasmic reticulum. Golgi apparatus. Note=Observed in a reticular pattern and a perinuclear ring. The precursor of STMP3 accumulates at the plasma membrane and is proteolytically cleaved to release the STMP3 in the apoplasm.
Sequence:
MGLKMSSNALLLSLFLLLLCLFSEIGGSETTHWKIVEEPVRGQIATPPSLTCGGQRLGGPQPRLSPCPRPRPRPRPRTGS
The following text describes a protein:
Function:
Crystallins are the dominant structural components of the vertebrate eye lens.
Sequence:
MGKIYFYEERNFQGRHYECGSDCSDLSSYFNRCNSIRVEGGNWILYEHPSYRGHQYYLWQGEYPDFQRWMGFNDSIRSCRFIPHYHGQYKMRIYERGDYQGQMMEFFDDCPNTYDRFHFNDIHSCNVFNGHWMFYEEPNYRGRQYYMRPGEYRKYSDWGASSPRIGSFRRVYHRF
The following text describes a protein:
Function:
ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
Subcellular Localization:
Nucleus.
Sequence:
MKIVAFGNPLLDTIVLLKSDALLKKYCLEKDGQKEVSQSEMKALVADLEEYEKTFVAGGCAQNTLKVVQWLLDKKCAATMFGSIGGDSEGEILKKILREHGVDTNYVTQPGYITGSTVSLVTGESRSLVAYLGAAEVMSPQDFSPNSHIIEDANLVYMEGFFITKRIQVASAIVNCCNRLNKQFVFNLSGQYLCTDYTQTVVDFVQKSSIIFGNKREFQTICPPMNESSVENLIKNLGKQGKIVVVTDGAKCVNCVGGGETLEIKVPELRAEEIVDTTGAGDAFVAGFLSGYLLKKPLKTCCELGNYAAQEIIKRRGCTIPDYPPVLK
The following text describes a protein:
Function:
Functions as a component of both the DNA-binding general transcription initiation factor complex TFIID and the transcription coactivator SAGA complex. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription. At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module). SAGA preferentially acetylates histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and deubiquitinates histone H2B. SAGA interacts with DNA via upstream activating sequences (UASs).
Subcellular Localization:
Nucleus.
Sequence:
MNGQHSSPGTPVQRPSAGPVNQAQFSQQRTNQLTSLLHTMTMYQQLAQNVGLNTPQGQVYLLQAQTIRRQLQGHAQSGQLPNQQLLQQLQSNGALQQGTPEPSNTRPRPQLNAQEQTMLLVRHRQLQTAQNYLTEMKEALGRIKNELSTNERLDTSAREALVKQESELTVKIAQFTAAISNGIRSIQQLQNRQASSANGNNTGTSTPVNASTDTRKSTASTPQLQQTQAQANAPQQRINPETSSVPETPVGVSAANVSNESTELATSATQQSGLANNVEKSQTPSYMSANHLPKVDSKSPIPFSVPPSRATLTGGYASGSIGLSTPGLSRAPHYELDNGNRLLSKRKLHDLLQQIDSEEKIEPEVEELLLEIADEFVESVTNFACRLAKHRKSDTLDVRDVQLHLERNWNIRLPGFASDDIVKSARKTGPTPSYQQKQNAIGTAKSLNKD
The following text describes a protein:
Function:
Scaffold protein in the commander complex that is essential for endosomal recycling of transmembrane cargos; the commander complex is composed of the CCC subcomplex and the retriever subcomplex (By similarity). May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (By similarity). May down-regulate activation of NF-kappa-B (By similarity). Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits (By similarity).
Subcellular Localization:
Nucleus. Cytoplasmic vesicle.
Sequence:
MAALTAEHFVALQSLLKASSKDVVRQLCQESFSSSCLDSESLLDKTCSSLSVPQGEAAQLLQALHHFTRLVAFRDLSSAEAILALFPENFHQNLKNLLTKIIVEHISTWRAEAQANQISLPRLVDLDWRVDIKTSSDNISRMAVPTCLLQMKIQEDPSLCGEKPSISAVTMELSKETLDTMLDGLGRIRDQLSAVANK
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MGTKMRLLCLAAAVAAAAILLTASAKKSADVTQLQIGVKYKPESCTLQAHKGDKIKVHYRGTLTDGSVFDSSYDRGDPFEFTLGNGQVIKGWDQGLLGMCVGEKRKLRIPAKMGYGERGSPPKIPGGATLVFDTELIAVNGRTSDGATSNSNSDL
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular Localization:
Nucleus.
Sequence:
MSGRGGRGGRGGRGGGGGFGGGRGGRRAVAANSVPWQMDPTIALDGKPSELFPPYKVPRAPVLSKKDDRQVSFFLSFREQCHDSPLYTQSRTWAAGTTSFSSSTSASSSLFGSSAKATIDIFEDGVPSYSHKFQQKERTLPDLASRPFAKEFFPAELHATLDGIDGGSSSVASSGAKRRKTTTTTTAKTIALSSAEYKTAEDVFGLSKVANGAASQEGEGGEPNYQRALQLLEMVEKKVEDGGEDAAVGILSDDDEDDWVKNNEDEDGNPVAEEDDDFEEDSGDDYNAEQYFDGNQDDDDYDEGGDDGGDYY
The following text describes a protein:
Function:
Probable transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MGRGRVEMKRIENKISRQVTFSKRRSGLLKKTNEISVLCDAEVALIVFSSNGKLFEYSTQSSMENILERYENYSYEEMNLNTTYKENWTLEYPKLMARVELLQRNIRHFMGEDLDAFNLREFRGLEKQLDTALKRVRSKKNQLMHESISQLQKKEKELQQRNNLISNKLKENEKKQIVQTNPGQSSTMTFLLQSPTVTNQTIGGPSQATDQSQNRDGYNSLMPPWMFHHVHNKG
The following text describes a protein:
Function:
Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including root growth prevention, phospholipid signaling pathway activation (e.g. accumulation of phosphatidic acid (PA), but transient reduction of phosphatidylinositol 4,5-bisphosphate (PIP(2)) levels) and reactive oxygen species (ROS) response regulation. Moderates primary root growth, and regulates root meristems and cell elongation; this root growth regulation is associated with the modulation of ROS metabolism and alteration of cell wall structure, and depends on variations in many genes expression. Promotes ROS (e.g. superoxide anion O(2) and hydrogen peroxide H(2)O(2)) production and MAPK (e.g. MPK3, MPK4 and MPK6) activation in a MIK2-dependent manner, thus leading to the up-regulation of immune-related marker genes (e.g. WRKY30, WRKY33 and CYP81F2). Involved in biotic and oxidative stress responses; acts as a negative regulator of defense against necrotrophic pathogens such as the bacteria Erwinia amylovora and the fungus Alternaria brassicicola. Able to prime defense responses against the pathogenic bacteria Pseudomonas syringae pv. tomato DC3000. Contributes to the triggering of defense responses toward generalist herbivores such as Spodoptera littoralis, probably via the activation of jasmonate and indole glucosinolate biosynthesis. Triggers the expression of several PROSCOOP genes (e.g. PROSCOOP3, PROSCOOP7, PROSCOOP12 and PROSCOOP13).
Subcellular Localization:
Cell membrane. Secreted, extracellular space, apoplast. Note=The precursor of SCOOP12, PROSCOOP12, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP12 in the apoplasm.
Sequence:
MRNTISSKMGQVLIVLLLLCTVLCRTESALPSGQHSVLLTGRRLMGSGASGPVRSSQSSQAGGRFNDADPIAIDYGKY
The following text describes a protein:
Function:
Involved in zinc homeostasis, where it plays a role in its accumulation in the endoplasmic reticulum/nucleus. Also has a role in the sequestration of cadmium into the endoplasmic reticulum.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein.
Sequence:
MFDLARQTRIILLLGIDVTFFFIEIITGYAIDSLALIADSFHMLNDIVSLLVALWATRLAHSTSHEPKYTYGWQRAEILGALSNGVFLIALCMFIFMEAIERFIEPPSVSNPTLMFFVGSLGLLSNFVGIFLFHDHGHDHPHTHTAQNYDFPEEDDIESVLPSTIVHRCNTSQQEVSHTHTQVADSATESSPLLSYTGNHNGAGTSKPVNNHGSIEQDAPKQTKKRNLNMHGVFLHVLGDALGNIGVISAALFIKYTDYSWRFLFDPCISILLTFIILFSAIPLCKSAALILLQVAPQSIKLDDVSNLINHLDGVESVHELHIWQLSDVKLIATVHVCVTLPDDKGESYTKLTTDIRNVLQSFGIYDVTIQPEFANHPLLCDQGSSS
The following text describes a protein:
Function:
Required for 60S pre-ribosomal subunits export to the cytoplasm.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSNNSREAPELTAASGDGGGLSEKLLNLRRLQSKMERSPYDYMSELFDIQSEFNSSLQLFYQHAAIKILPIDRDLVNVASDPISLAENLAETASFLGRVAIYYPERFALNDFPSRLFHLLCNSCRQIPSNPRFKLAHALTLVFRSVCIDQSLSLFMELQTLGDEKLTKLASNHIFQSIWDIRPNQHRTRKLQTLMFNMLLEAKDAVAMRVLVILWKLYKREVWFDEKTANAICTASFHETLGIMTVALSSLLKNKEPMIENDKDHYDSDSGVDSPLNHLTDKQSFAERLFSRLQHFKEGSEVKMMMLKLIARVIGLHQLTLLDFYPFVRKYIQPHQPDIINLLPAVVQACHDKVPCDVVKPLLIQIVNQFVNDRSRPEAITIGLNAVREICIRMPMLMNDDLLQDLDLYEKSHEKANSVAVRSLITLFQEFCPFDSKAKATPKAYEGVDFATDVLGDELLTDHDEEDDNDQEDDQMTIDDESLGTES