lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the coat protein complex II (COPII), that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII is composed of at least five proteins: the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. Acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein.
Sequence:
MAAPVPPGAQRPNNPQNTAPPNSLVANMHNLNIHRPPPPMHGSGPRPSPPFGQPPPQPYPQSAPSYGPPGGVAAAPPSGPRPVGFGSPPPMGPGMSMPGGPVTNGPPPMMSPGGPGPITNGPPMMGPGGFPRGSQFPGGSMMGPPPPYGQPPNAHSLPGGSPLTSPPAHSIPPPTTFPGAPYARPGGFPYGLPPQQHPSAPGTPGSMYSMGPVPNQSMTTVSGPSKVDLNQIPRPGSSSGPIMYETRQENQANPPPPATVDYIARDTGNCSPRNMRCTIHQIPCTVDLLSTSGMQLALIIQPLALSHPSEEPIQQVVDFGESGPVRCARCKGYINPFMKFVDQGRKFICNLCGYTDETPRDYQCNLGPDGKRRDADERPELCRGTVDFVATKEYMVRDPMPAVYFFLIDVSMNAIQTGATAAACSAIQQVLSDLPEGPRTFVGIATFDSTIHFYNLKRALQQPLMLIVPDVQDVYTPLETDVIVQLSECRQHLEILLESIPTMFQESKSPESAFGAAIKAAFLAMKSTGGKLMVFQSVLPSVGIGALSSREADGRANASADEKEAHKLLQPADKTLRTMAIEFAEYQVCVDLFITSQAYVDMASISDIPRTTGGQVYCYYPFSALSDPPKLYNDLRWNITRPQGFEAVMRVRCSQGIQVQEYSGSFCKRIPTDIDLPAIDCDKAVMVTLKHDDKLQDGAECGFQCALLYTTITGERRIRVINLSLPCTSMLSNLFRSADLDSQFACMLKQAANEIPTKALSLVKEQAISSCITALSSYRKFCATVTSAGQLILPEALKLLPLYTLALTKGVGLRSDGRIDDRSFWINHVSSLSTPLAIPLIYPRMIAVHDLDTKEDNEETVVPSPIPLTSEDLRDDGVYFLENGDDGLIYVGESVNSDILMKLFNVPSAADIPSQYVLEKYDNQLSKKFNDVVNEIRRQRSSYLRMLLNIILSANEIPTKALSLVKEQAISSCITALSSYRKFCATVTSAGQLILPEALKLLPLYTLALTKGVGLRSDGRIDDRSFWINHVSSLSTPLAIPLIYPRMIAVHDLDTKEDNEETVVPSPIPLTSEDLRDDGVYFLENGDDGLIYVGESVNSDILMKLFNVPSAADIPSQYVLEKYDNQLSKKFNDVVNEIRRQRSSYLRLKLCKRGDPTGMLFLSYMVEDRTAGGPSYMDFLVQVHRQIQGKLN
The following text describes a protein:
Function:
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Subcellular Localization:
Cytoplasm.
Sequence:
MAGIYLHIPFCKTRCIYCDFYSTTRSELKTHYVHTLCRELEMRKEYLKGEPVETIYFGGGTPSQLEEADFKHIFETIRENYGMEHCREITLEANPDDLSQEYLKMLSSLPFNRISMGIQTFDDTTLQLLKRRHSSQTAVEAVRRCREAGFQNISIDLIYGLPGETKERWVNDLRQAIRLDVEHISAYHLTYEEDTPIYNMLKQHQIEEVDEDSSLQFFTLLIEHLQNAGYEHYEISNFCRPDKYSRHNTSYWRGIPYLGCGPSAHSFNGTTREWNVSSIDLYIKGIEGNQRDFETENLDQTTRYNEFIITTIRTVWGTPIEKLKQEFGNELWEYCRKMSAPYLENGKLEIHEGALRLTREGIFISDSIMSDLLWVN
The following text describes a protein:
Function:
Sodium-phosphate symporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MPKYHDYDYLFAFSMIGAFVNAYGIGANDVANSFATSVSSKSLTFRQAMVCAAFCEFLGAVLVGARVASTIKNGIIDLDVFNGNASVVLLAFTCSIIGSASWLTFATRNAMPVSTTHTTVGSVIGVGIAVSGANGVKWGWNGVAQIFASWGIAPAVAGVCAACVYLITKLVVLKSRNPVMVGLWTAPVYFFIVSGVLTVSIIVKGSPSLNLDELPPSTTIAAVLGTASVVALLSILFWLPYVHGKVVKGDYTLKWYHFFMGPLLWRRPAPEDAVTADMAVPDYKLHDFDEPAEQQAVSERTAAAVRAQPVVAGAALQRIDHSNDIESGANSDTHGSSPSTEEKNAKLVQPGFCNDSPSHLARVEAELEGAHALPAEHTPGRPTPPAYRTFEGSWLEPWNLYTIIRYNMLPWMWYSVSAGLRTDIHAMQAHGSEKEKAKLRQMHAVAEQYDNRVEHLYSFMQVMTACTASFAHGANDVSNAIGPLAVVYSIWSTSLFPESKEPVPIWILAFGGAAIVIGLGTYGWKLMSVLGNRLTMHSPSRGFSMELGASITVVIASYLGLPVSSTQSITGATLAVGLCNGDYKAMNWKMLAWIFFSWILTLPIAGLISGCLLAIVLNAPSWYTPAPVL
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:
MNEEEKKKYPFDELKLDESIIFSLYIQKYFYCANIQKKTIPPLIKKENVLLHSQTGSGKTLCFVIPILQYLIHHRNKLCPNDEKFIKRNDLFNKKNVNDTVSYNKDQIERIYETVENINIEKKNAYRDVNVNIDIRNFLLYTHNMLRNTNEEDISKKVEINQNDNKVMTYKDKIISDDQVNIIKKDEINIQKNNNQEEIIRKNDLQNITFATTCNSNYQDDKQETNKEKHEQKIEEKYNEQNIQTNNQTKKPHNNNNNNNNNNSKKKTQKLLNIQAIIITPTRELCIQIYNLINKFLFFLRFYISHTLNNNMDNNVLTKENFFINCLLFRGAVKISEDIKIIENEILKNNRYQIIISTPGKLSSLLSEYNNKYFNTNELKYFVLDEGDKLLEDSYIRYMENIIKNIQAYDYTTCICSATCLQEENVYNLFQVKKKNFIKCINTNNQDNSSTVINTYQMPDRIQNYYIILRNIDKALFLFKFLNTMVNDNETVIVFFPTCLCVEFFFHLFKNIFNTKKINKQNESKNKKNKNKIYKGIHNDNVDNINVDNISVDNISVDNINVDNHIDYIFQLNSKYNNIFSDADMANFVKLICYMNKYIGEKKNNFNFLKIHRKMKDKKRVATYNKIINTCVSNKGTKKKENRNINSERKIIFCTDIISRGINMDIHWVINYDAANKNMTYIHRSGRTGRFDKTGKNIILLNKEEKEYIYFLKNKNVHVVNFKKTDMFQHMINYEKTLLKSEHIINNDALRIIEINHNEKKKNNITINKNSFFNLYPQILYDKKLIGKHQNGDLQIQKGEHKKNKNNLLILNKKLVMFFLKYITFFVIENREIYLLSTKAFLSYIEFYKNHQLKFIFSFNKLNLTHLCYAFSLIKIPKFKEKSKIKNFQNINIQSFQIPYKNEEKEKKRQEHLKEKQIDIITQEQKKENQIKMQKKKKRKTIVQRKHEQRELEENEIDSLFYEENLYKKLKKKKITKDEYDRLLNMDDIDKMFSSTSKTSKCTNLTNNTHFFKSNRKKSKKRMKTYNIKIKKNKRKKKKRS
The following text describes a protein:
Function:
Endogenous opiate; Stimulates the adrenal glands to release cortisol.
Subcellular Localization:
Secreted.
Sequence:
MKESGQSQLRHLLSLCVLESQNKKSIDRTGGRNIWRNVCWKEEQETSAEEKEADNMEAQKTRLVLLLVAGAAVGVVKGERRQCWEHLSCQELNTESSVKDGVQICESTLNRMPLLPGAPHHQPSPSSEPLSLFSIPSPQTRRSYSMEHFRWGKPIGRKRRPVKIYGGNSVEEEEESSEMRRRELPRESNGLQNKEELQKLQEDGHDDDDDDDGTYKMKHFRWGAPPASKRYGGFMRSWDEHSQRPLITLLKTVINKEGEVQKREQ
The following text describes a protein:
Function:
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity; Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section.
Sequence:
MPSDLCYWLISAPLKDGDPDVMLNEVRQEIPGVFAAKWEIPELKAGTLSSLLTLSDSLPKIDSAFTTTASKLLDQLRSLVDNDNGKIAQHARVNDRPAEEYLMAGGDGFKWDKGRWGEGGKVTEVVGALSKEMAVIEATQREKAQSYNLAKGGLTTLQRKQIGNLSQRSLLDIVKKEHLVEDSEYLETLIVAVPKNLAKDWSNKYERLTSMVVPRSSQQIASDDEYVLQTVTVFKKVRDDFIHKCRENKFIVRDFTWDDSALEKQRRQLAELEIEEKELWTGLLRLTRINFSEAYQILAHLKTVRLFVESVLRYGLPADYAGVIIKPDRKTAAKTLRSITTHYAYLNNSSRDSSARKGKGKGSSSAMGDDVGGEWASVMEAEYYDIVLFEIPMVIC
The following text describes a protein:
Function:
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Miscellaneous:
MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue.
Subcellular Localization:
Cytoplasm.
Sequence:
MKTNLLNYDLQGLTRHFADMGEKPFRAKQVMRWMHQSGAQNFDEMTDLAKSLRHKLNEQAGIEIPKLMMSQKSSDGTRKWLLDVGTGNGVETVFIPESDRGTLCISSQVGCALECTFCSTGRQGFNRNLTAAEIIGQLWWANKAMGVTPKNERVISNVVMMGMGEPMANFDNVVTALSIMLDDHGYGLSRRRVTVSTSGMVPQMDRLRDVMPVALAVSLHASNDEVRNQIVPLNKKYPLKELMAACQRYLVKAPRDFITFEYVMLDGINDKAQHARELIELVTDVPCKFNLIPFNPFPNSGYERSSNENIRVFRDILQQAGFVVTVRKTRGDDIDAACGQLAGQVQDKTRRQQKWQQILIGQQG
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 FruAB PTS system is involved in fructose transport.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain; In the N-terminal, the PTS system fructose-specific possesses a duplicated EIIB domain (EIIB' domain) which lacks the active site and functions to facilitate phosphoryl transfer between the EIIA domain of diphosphoryl transfer protein (DTP) and the EIIB domain. The presence of the EIIB' domain is required for normal high affinity recognition of DTP by the PTS system fructose-specific as well as for normal rates of phosphoryl transfer between the EIIA and EIIB domains of DTP and PTS system fructose-specific, respectively; The EIIC type-2 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Sequence:
MKLFLTQSANVGDVKAYLLHEVFRAAAQKANVSIVGTPAEADLVLVFGSVLPNNPDLVGKKVFIIGEAIAMISPEVTLANALANGADYVAPKSAVSFTGVSGVKNIVAVTACPTGVAHTFMSAEAIEAYAKKQGWNVKVETRGQVGAGNEITVEEVAAADLVFVAADIDVPLDKFKGKPMYRTSTGLALKKTEQEFDKAFKEAKIFDGGNNAGTKEESREKKGVYKHLMTGVSHMLPLVVAGGLLIAISFMFSFNVIENTGVFQDLPNMLINIGSGVAFKLMIAVFAGYVAFSIADRPGLAVGLIAGMLASEAGAGILGGIIAGFLAGYVVKGLNVIIRLPASLTSLKPILILPLLGSMIVGLTMIYLINPPVAEIMKELSNWLTSMGEVNAIVLGAIIGAMMCIDMGGPVNKAAYTFSVGLIASQVYTPMAAAMAAGMVPPIGMTVATWIARNKFTVSQCDAGKASFVLGLCFISEGALPFVAADPIRVIISSVIGGAVAGAISMGLNITLQAPHGGLFVIPFVSEPLKYLGAIAIGALSTGVVYAIIKSKNNAE
The following text describes a protein:
Function:
Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of mRNAs, a modification that plays a role in the efficiency of mRNA splicing and is required for sex determination. In the WMM complex, acts as a key regulator of m6A methylation by bridging fl(2)d to the RNA-binding component nito. Required for sex determination and dosage compensation via Sxl alternative splicing: m6A methylation acts as a key regulator of Sxl pre-mRNA and promotes female-specific alternative splicing of Sxl, which determines female physiognomy.
Miscellaneous:
MISCELLANEOUS: Was named Xiong after the Chinese character for maleness.
Subcellular Localization:
Nucleus.
Sequence:
MEKKAKESLRRYKKAARHSATHSSSSDSTSDSDSGSSSYSSTDSEQGVGGVGVGVGVPGGAGGPGGSGSVHGHPHTHGHGHHPRSAERHHRKKKSSRRGGSSSGDEPSSSRRKRDKRDHVQKKLVAKRNHIKRKLKEARLKKRAAAALSGHVHRSLSPTTRAKLKKLAERKRLRAASKEQRERDKLRVVQRDRERDHHRLGSSRSPPSSSTTTTTKIRIHQDIVGKRQKSPGLGSGLGGGSSSSSSRMHHQLMSREKIIIQTRARGRTPSLERERERERERERERERERHDLSLRERDRRDRERERAEREAARDKERAEALARCQERQRERERLAREKLRRQEEEEGGKRGGPGRDLDLPPYGSRERSLDTVERERERERSGRHVRDKRELDPYEREQEYLEERHGHGLIDEMRRYRRRDLSPMPEHYAPRLRDPRELYSEEERERAYKRAYLDARYSSREREAWLEARELRERELQGREYRDLETEDTLYPDERERLIRDRERDRERERDRERERNIGPRGDFRPEWEREWEEEGAGGGPGGPSGTPGRPGGFVGGPKRGKPPAHAGGGPPSQQQHHSASEPDWDADERERERERERDRERERDREDRPDTGGGGAGGDRPSIKNEPAWLEHDQREKPRGWQQQSSNSGGDWRDNDDAPPAPSHPHPASPHHHVHPRGERGSGRGFRRGGHGHGDHGERPGYRSHPPPLMTLPVQPPGGYSRGFPHKRLPYGSGRDGAALGARDGGLPGSSTFLKKHTHAPLVSPTQTPLLNPLLNAAKPNAAAQASAVAAATTAVAAAKAAAQSAANATTNPGILAQVSKLNTVCIKQEDASEDSAGTPELGAQDSPTQSLNLNQSLSSEGNPVKQELIRTSAVEGELSEISDSDDDILNKTDKVRPKNELPTETEQEMDTNADEVKSEALHIVAGHPIKGEEGDEVLDFEEISDGELEEDARHKGIGDALGVDWQGLIAETRQQASDAQAAQQGVDRGTSAKQRWQPYRVLLDLGISFGMAGEGYARCVMEEARQQLLQEKEQGQQRELDGDEEPPAKIPSPLLDYREFLASQQQLEPLACVQMGLRSAAVERQRLVGNVCGPGSRALSARQDLRLRRQLCGLPARECEFPRSVPIVGEGLRNLAMQMFQRRLLDVK
The following text describes a protein:
Function:
Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system). Can transport lactose, melibiose, the synthetic disaccharide lactulose or the analog methyl-1-thio-beta,D-galactopyranoside (TMG), but not sucrose or fructose. The substrate specificity is directed toward the galactopyranosyl moiety of the substrate.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQPLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNAGAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALILAVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFDQQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQLAMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA
The following text describes a protein:
Function:
FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Oxidizes thioredoxin in vitro. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space, and can act independently of the oxidoreductase MIA40. Can oxidize the cytochrome c oxidase assembly protein COX19, a typical substrate of MIA40.
Sequence:
MDVPLRALEGWGQALLQQLPSNGSSSGKQWASARPGLSHVSQGGAARWAVPGQLRHPSLHVSGPHAAWRRPSTGVTASSASTAAVRGGGLTPATIAASPLASVSASMPTAPARAPAPAPFAASSMATATSPLAAGAASMSAAAQAAATAKAEVGRATWTLLHMLAAQFPDRPSRQQQRDARTLVDCLTRIYPCGDCAEHFAEIVRRDPPAVGSGREFRRWLCGVHNRVNSRLGKPVFNCDLVEARWAPLGCSAEEAAAGEPAAAGAGKGCELLGVGAKGGR
The following text describes a protein:
Function:
Involved in the assembly of dense bodies and M lines during body wall muscle development. Acts by recruiting downstream of integrin-associated protein pat-6/actopaxin several dense bodies and M line components including unc-89, lim-9, scpl-1 and unc-96 to integrin-mediated attachment sites.
Subcellular Localization:
Basal cell membrane; Single-pass type I membrane protein. Cytoplasm, myofibril, sarcomere, M line. Note=Colocalizes with unc-89, unc-112, pat-3 and pat-6 at the M-line and with alpha-actinin, unc-112, pat-3 and pat-6 in dense bodies. In body wall muscle cells, colocalizes with beta-integrin pat-3 at integrin adhesion sites.
Sequence:
MVFDARLGYDPDEWEECPEPEHFLVFSGFTRYMLTFAAIAFVYYFFKLLDDKNKKESGEKEEPQTSVESVLAKAGDKLHDVKEQVQQHIPESAEELMREADQYLKEQAHSVQNNVHQFAEQAANKFPSLEVDLNLGHPIDATREKFDTVLSSVNNHLHETKNMDLSPTSRDSTQFEQIPSIAPEESAFGHDFEHVPPHLKTAAEQYYAQQHQPPPVPQHKIVQPVPISPTDQQLLHEFDIYDAPAHQRMNQISEQLGQLGQKTPAQLQQLQHAQLAHQQLQQQGVFQPIQQPSPLQIQTHPQQPYFDFSQLSPASQARYNQQQFVDISQLSPGAGALIAEQQASGAFQPVTKKLGREKRLSEQDERALQDWEKEKALLEADRLKKLLDHEVGGDSTDLDSSQKAYDHFAPASHISYESHSGAAQIQPMTPTAPKRADVPAPQVTSITNVRDSQLTDYDISDFHAHDEPHYHTVLTPQQLQQNQQQHQQPSAIDRRRTTADSDDYVKVSEPIYDYPPKGHEAPVAEPKRISPTEAAQLQELYQEYDLGLDLPGVAPIQGVAKPPVQQRTPLQIQQQVVQNVQNQPNMMARQNSVPESPRTVINVPISRKTDVPIQVQQQQNQFSYNVPIQVKDDPRNLATADLFVQDAQEYVAHQQNQQDKGSFVMEEEMLSLHEPETGSNKKKLTPKNPSFEATSRQVRTNDVFERIEHDEHDDMTYAPEIQSVEIPPDQMSETSENMIDYFDKVAAESEQQIQHLQEQQNTLKKQQIETSIPDSSLLKPVGRAPQILPAFGNRISSNSSLGSAGRSGSGVSSSDVYPYRHLRKQSSLLSVLGVTSMQEMLLAITSLDSLSEAMRKAGLETTNLIFGIDYTASNKYQGEESFGGRSLHTIHPHVTNPYQQVISILGRTLAPFAGQGRLGVYGFGDAKTGDWSVFNLKGEGGDCRSLDEVLNVYNTVTPTVALSGPTNFAPLIYQAMEICQKSRDYHILVIIADGQVTNERATRRAIVQACQHPLSIIVVGVGDGPWDMMRIFDESLPKRPWDNFHFVEFHEIVKKSTNMEDGDVKLAVQSLLEIPDQYRCICELGLLDRSIPPRGSEIRREMMHNPL
The following text describes a protein:
Function:
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Sequence:
MSEVITQEYTEDGKVLRRIRSFVRREGRLTKGQEAAMKECWPTMGIDYQPELLDWQQVFGNDNPVVLEIGFGMGASLVEMAKNAPEKNFLGIEVHSPGVGACLASAREAGVTNLRVMCHDAVEVFAHMIPDNSLHTLQLFFPDPWHKKRHHKRRIVQLEFAEMVRQKLMIGSGVFHMATDWENYAEHMVEVMNQAPGFANLATDGDYVPRPDERPLTKFEQRGHRLGHGVWDIKYQRTA
The following text describes a protein:
Function:
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MINSMQFLYLVASYLIGNILTAYIVTKLRHNVDIRDEGSGNPGARNMGRVYGKGYFIATFLGDAIKGAIVVAVAKYLFEDPTFVMLTLLAVIIGHIYPVLFKGKGGKGISTFIGGLIAFDYLIALTLLGIFIVFYLIFKGFTKPGLITIACLPICMILYSYSIVTTILSGIIIVLILYVNRE
The following text describes a protein:
Function:
Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.
Sequence:
STSTMANRPKAYGNSAEVASKIDAKYSQEDEMEIVAWISSLVQSSPEGKGKEAMKQNKEMENISVFLKAAAKYANIPAQDMFQTVDLYEGGNLGQVQSTIFKVGAEAKNRGLHGIGVKKAEENKRVFDEQKMREGRNIIGLQMGTNQGASQSGMSAYGLGRQMTQKKAGICKPNPTYTGSMQMGTNQVASQRGMTAYGLGRQLTPQK
The following text describes a protein:
Function:
Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA (By similarity).
Subcellular Localization:
Peroxisome.
Sequence:
MAEKPQLVNNLPEDVETDECMNKYTHIYSPDLLSDQVAFITGGGSGIGFRIAEVLMRHGCDTVIASRNLEKISQAAKKLTSTTGRRCLPIAMDVRQPETILAAVDETLKTFGRVDILINNAAGNFLCPATSLSFNAFKTVMEIDTMGTFNTSKVIYDKWFKDHGGSIVNISATLGYRGQALQVHAGSAKAANDAMTRHLAVEWGPSGVRVNTVAPGPISGTEGYRRLGGSHAETAGAFHSIPLQRAGNKTEMAHAVLFLASRASSYVTGSVLVADGGAWLTSANDVERLLGIVSSRSAKL
The following text describes a protein:
Function:
Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Subcellular Localization:
Cell membrane.
Sequence:
MHVGTLIKFEGVSFRYEGSESYAIRDVNLEIRRGDFLLIAGMSGSGKSTLLRMMNGLIPHFYRGEMAGRVLVDGVDTREASVAQLARKVGLVFQNPDNQIVTLRVDREVAFGLENLGMSREEMVKRVNYALSKLKIEHLERRSTYELSGGEKQLVAIASIVAMKPDILVLDEPTSELDPFGAARIVRILKELNREGITIIVAEHRLDLFAPSSNRLLVVHEGRIKFDGDPREILYDDPHSLGVKPPGVVKFAKNYGVKGRPLTVGELIRAAAR
The following text describes a protein:
Function:
Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Miscellaneous:
MISCELLANEOUS: This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocatalyst that acts repeatedly and over many reaction cycles.
Subcellular Localization:
Cytoplasm.
Sequence:
MLSVEKFRVGERVVWIGVIFSGRVQGIAFAFDRGTLMKRIHDLAEHLGKRGVSISLDVQPSDYPEKVFKVLIGELDNASFLRELSFEGVTPFEKKVYEWLTKNVKRGSVITYGDLAKALNTSPRAVGGAMKRNPYPIVVPCHRVVAHDGIGYYSSGIEEKKFLLEIEGVKEWTS
The following text describes a protein:
Function:
Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long-chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-chain fatty acids-CoA and bile acids from the cytosol to the peroxisome lumen for beta-oxydation. Has fatty acyl-CoA thioesterase and ATPase activities. Probably hydrolyzes fatty acyl-CoAs into free fatty acids prior to their ATP-dependent transport into peroxisomes. Thus, play a role in regulation of LCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation.
Subcellular Localization:
Peroxisome membrane; Multi-pass membrane protein.
Sequence:
MAAFSKYLTARNSSLAGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVDKVFFSRLAQILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTKYLYEEYLQSFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLVVSGLFLTRLRRPIGRMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFILFRFSMGFIDNIIAKYLATVVGYLVVSRPFLDLSHPRHLKSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFTARITELMQVLKDLNHGKYERTMVSQQEKGIEGVQVIPLIPGAGEIIIADNIIKFDHVPLATPNGDILIRDLNFEVQSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKGISDLVLKEYLDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKQITEDTVEFGS
The following text describes a protein:
Function:
Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. Acts both as a positive and negative regulator of the Wnt signaling pathway, depending on the context: acts as a positive regulator by promoting LRP6 phosphorylation. Also acts as a negative regulator by acting as a scaffold protein for the beta-catenin destruction complex and promoting stabilization of Axin at the cell membrane. Promotes CTNNB1 ubiquitination and degradation. Involved in kidney development (By similarity).
Subcellular Localization:
Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=Shuttles between nucleus and cytoplasm. Detected in nuclear paraspeckles that are found close to splicing speckles. Translocates to the cell membrane following binding to PtdIns(4,5)P2 (By similarity).
Sequence:
MESQQDEAVQTKGASTSSDAQDQGAEKGAKNKTTEATEGPTSEPPLSGPGRLKKTAMKLFGGKKGICTLPSFFGGGRSKGSGKVSSKKSLNKSKTHDGLSEASQGPEDVVIEETDLSTPLSKSSAQFPSSQSANGALEIGSKHKTSGTEAIEKAGVEKVPSVHKPKKSLKSFFSSIRRHRKGKTSGADQSVPGAKELEGARTRSHEHVSSISLPSSEEIFRDTRKENAKPQDAPGPKMSPAQVHFSPTTEKAACKNPEKLTRTCASEFMQPKPVLEGGSLEEPHTSETEGKVVAGEVNPPNGPVGDQLSLLFGDVTSLKSFDSLTGCGDIIAEQDMDSMTDSMASGGQRANRDGTKRSSCLVTYQGGGEEMALPDDDDNDDEEEEEEEEEEEEEEEEEEEEEEEEEEEELLEDEEEVKDGEENDDLEYLWASAQIYPRFNMNLGYHTAISPSHQGYMLLDPVQSYPNLGLGELLTPQSDQQESAPNSDEGYYDSTTPGFEDDSGEALGLAHRDCLPRDSYSGDALYEFYEPDDSLEHSPPGDDCLYDLRGRNSEMLDPFLNLEPFSSRPPGAMETEEERLVTIQKQLLYWELRREQREAQEACAREAHAREAYARDTHTRESYGRNVRARETQALEAHSQEGRVQETKVRQEKPALEYQMRPLGPSVMGLVAGTSGGSQTSHRGTTSAFPATSSSEPDWRDFRPLEKRFEGTCSKKDQSTCLMQLFQSDAMFEPDMQEANFGGSPRKAYPSYSPPEEPEEEEEEKEGNATVSFSQALVEFTSNGNLFTSMSYSSDSDSSFTQNLPELPPMVTFDIADVERDGEGKCEENPEFNNDEDLTASLEAFELGYYHKHAFNSYHSRFYQGLPWGVSSLPRYLGLPGVHPRPPPAAMALNRRSRSLDNAESLELELSSSHLAQGYMESDELQAHQEDSDEEGEEEEGEWGRDSPLSLYTEPPGVYDWPPWAHCPLPVGPGLAWMSPNQLYEPFNQSSYVQATCCVPPVAMPVSVPGRTPGDSVSQLARPSHLPLPMGPCYNLQSQASQSGRAKPRDVLLPVDEPSCSSISGANSQSQAKPVGITHGIPQLPRVRPEPFQLQPNHYRASNLDLSKERGEQGASLSTSYSSTAMNGNLAK
The following text describes a protein:
Function:
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Sequence:
MNKGVFVVIEGVDGAGKTALIEGFKKLYPTKFLNYQLTYTREPGGTLLAEKIRQLLLNETMEPLTEAYLFAAARTEHISKLIKPAIEKEQLVISDRFVFSSFAYQGLSKKIGIDTVKQINHHALRNMMPNFTFILDCNFKEALQRMQKRGNDNLLDEFIKGKNDFDTVRSYYLSLVDKKNCFLINGDNKQEHLEKFIELLTRCLQQPTHY
The following text describes a protein:
Function:
Serine protease.
Sequence:
MNSMKTEENKSFSAMEDDQRTRPEVSKDTVMKQTHADTPVDHCLSGIRKCSSTFKLKSEVNKHETALEMQNPNLNNKECCFTFTLNGNSRKLDRSVFTAYGKPSESIYSALSANDYFSERIKNQFNKNIIVYEEKTIDGHINLGMPLKCLPSDSHFKITFGQRKSSKEDGHILRQCENPNMECILFHVVAIGRTRKKIVKINELHEKGSKLCIYALKGETIEGALCKDGRFRSDIGEFEWKLKEGHKKIYGKQSMVDEVSGKVLEMDISKKKALQQKDIHKKIKQNESATDEINHQSLIQSKKKVHKPKKDGETKDVEHSREQILPPQDLSHYIKDKTRQTIPRIRNYYFCSLPRKYRQINSQVRRRPHLGRRYAINLDVQKEAINLLKNYQTLNEAIMHQYPNFKEEAQWVRKYFREEQKRMNLSPAKQFNIYKKDFGKMTANSVSVATCEQLTYYSKSVGFMQWDNNGNTGNATCFVFNGGYIFTCRHVVHLMVGKNTHPSLWPDIISKCAKVTFTYTEFCPTPDNWFSIEPWLKVSNENLDYAILKLKENGNAFPPGLWRQISPQPSTGLIYLIGHPEGQIKKIDGCTVIPLNERLKKYPNDCQDGLVDLYDTTSNVYCMFTQRSFLSEVWNTHTLSYDTCFSDGSSGSPVFNASGKLVALHTFGLFYQRGFNVHALIEFGYSMDSILCDIKKTNESLYKSLNDEKLETYDEEKGKQESSLQDHQIEPMEC
The following text describes a protein:
Function:
Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin. Stimulates PI4KB kinase activity. Involved in long-term synaptic plasticity through its interaction with PICK1. May also play a role in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel.
Subcellular Localization:
Postsynaptic density.
Sequence:
MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRCKSCPLGPVGQQLEGPGQREAALGPHQAGVPDTHRSDHRWRPSCVCRGQAWAVGRWPSHSHVIGQADCPGFREQHRHLCFQWEGFLEATGSRRRLAEAGGQGGLGAEAGRSLGCTRAGADLGSRRGSEDPRPGFSAGPTSFVAIAWILAYTHSLTHSFIHQITSEHSHVLVPGIH