lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
Sequence:
MRTDSSKMTDVESGVANFASSARAGRRNALPDIQSSAATDGTSDLPLKLEALSVKEDAKEKDEKTTQDQLEKPQNEEK
The following text describes a protein:
Function:
Involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Mediates Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. May mediate Ca(2+)-regulation of exocytosis in insulin secreted cells.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be due to competing donor and acceptor splice sites.
Subcellular Localization:
Cytoplasm. Cell membrane; Single-pass type III membrane protein. Cytoplasmic vesicle, secretory vesicle, acrosome.
Domain:
The first C2 domain/C2A does not mediate Ca(2+)-dependent phospholipid binding; The second C2 domain/C2B is responsible for SYNCRIP and inositol 1,3,4,5-tetrakisphosphate (IP4)-binding.
Sequence:
MQADRSMKMGHALNPFSTSAPLDATAGPSLIPDLITRIPWPRWTLFIAILAAGVLLVSCLLCVICCYCHRHRHRKQPKDKETVGLGSARNSTTTHLVQPDVDCLEPCSGGDQQWGRLLLSLEYDFGSQEIRVGLRQAGNLKAEGTADPYAWVSVSTQSGRRHETKVHRGTLSPMFEETCCFLVPPAELPKATLKVQLWDFKRFSEHEPLGELQLPLGTVDLQHVLESWYQLGPPGTTEPEQMGELCFSLRYVPSSGSLTVVVLEARGLNPGLAEAYVKIQLMLNQRKWKKSKTSSKKGTTTPYFNEAFVFLVPVSQLQSVDLVLAVWARGLQLRTEPVGKVLLGSRASGQPLQHWADMLAHARRPIAQWHHLRSPREVDRVLALQPRLPLLRPRS
The following text describes a protein:
Function:
Demethylates proteins that have been reversibly carboxymethylated.
Sequence:
MSDLQRNAMKKSLGIPPLPSRLPGRGGGGWHARRQRRDYTPVAWDHYFEKRKDVGVKDKDLFRVYFSGNEGPLLLLLHGGGHSALSWAVFTEAVTKLCQCQVLAFDIRGHGDTKTSDDKDLSADRLADDVGDLVTSIYGDSPPPILLIGHSMGGAIAVHVGVKQLLPSLIGLTLIDVVEGTALDALSSMQNFLKSRPEAFKSLEHGIEWSVRSGQIHNVQSARVSMAGQLVRCNDSSTVPPEPERHPTPPHGIIDAITEQEDEDGEEDRATTSKDTHQQTAQDNLPVQNKKAECWKWRIDLSGTEQYWKGWFTNMSKLFLSVEVPKLLLLAGVDRLDKELTIGQMQGKFQMILLPQCGHCVHEDAPDKVAEVIVTFLLRYKLTEAKGDFVRPIPAC
The following text describes a protein:
Function:
Endoplasmic reticulum-localized palmitoyltransferase that could catalyze the addition of palmitate onto protein substrates.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The DHHC domain is required for palmitoyltransferase activity.
Sequence:
MTNLNCFGRHRRRTAPHNATGSRSELVAPPIHSRINGWSSPLHSFQFIALLIFSFMAIVAFGIYVPLLPAPWSYAAYALIGSAFVLHLFSHVTAVTIDPADVNVRRRKDYSSPMPTFDNSKHPHVIDNLHCTLCEVDVSPKAKHCSTCNKCIADFDHHCKWLNNCVGGRNYWFFFTAVSSAVIGVILLIPLVLFVFIEHYVNPAVLRTAPQFQTVKGNGTWLVFLPVAPVETSSISLLVVSFITALLSLAALLLLCHLLCFHIYLLSQGISTYEYIVRKRQSPNPKEKQQVPPALPSNGATAQSLELQEPPLNCDAPLSSRSCTFKLEDRGPMPEPICAEMEEASGEHHLSYSSESATQKIAGESVMSLPVVWSLSETERPQASQVEVKPLEGRPVVQDPLGSSIMDTALVHQQLMTEQPQYLHFKQKMP
The following text describes a protein:
Function:
Controls stomatal patterning.
Subcellular Localization:
Secreted.
Sequence:
MRMGEIRKWYVAIMAMVQIVSWVCATSRHIASTQVSFHPGIISPQAAENNSRRPILTPNENTEVKEMEKGRKIGSKPPTCEKKCYGCEPCEAIQVPTISSPPHISTQYTNYQPEGWRCHCAP
The following text describes a protein:
Function:
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Domain:
The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes.
Sequence:
MSPLNDLKINLNGQYTFFLNQNVISKYSGSLRKMIKQSKKKRNKKKRIITIEINDFPGGPDGFELVSRFCYHNGEILIDVSNVSTLYCCSVFLGMSEKFCFSNLFLQTEKFLEEVFYGSWSDIVSCLKNCEQVFFQADSYGLVDKLIFAALNKISQNSDDFSSSSLSSFASSLSPEMAKNTSESDGRYISRSVACGRSNEWWFEDMTNLSPKIILKLVMIIGAYKTNIKSLVLTRFLLHYLKTKLQTKSRTTTELMRNKLEYSDLADTAVRGVISAGTRTFSCRKLFWILRVLSSFSLSRESRIGLETLIGEMLEQATLDDLLISARGSRESGFYNVDLVIRLLKVFVKNREEEEEESRERNMKEIGKLIDKYLREISPDQNLKVPKFLGVAESLPDSARDCFDGVYRAIDIYLQSHPNLTPQDRTEICRCLNYKKLTMETCKQLARNPKIPPEIAIEALKSRCGNQEHTTSDVKVANKSFSCRYSEEKKKPVVLHLEITEKLAERLKTKGGYNLKVMDSFREGL
The following text describes a protein:
Function:
Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Note=Localizes to lipid rafts.
Domain:
The Ig-like V-type domain mediates the interaction with MHCII.
Sequence:
MNRGIPFRHLLLVLQLALLPAVTQGKKVVLGKKGDTVELTCNASQKKNTQFHWKNSNQIKILGIQGSFLTKGPSKLSDRADSRKSLWDQGCFSMIIKNLKIEDSDTYICEVENKKEEVELLVFGLTANSDTHLLEGQSLTLTLESPPGSSPSVKCRSPGGKNIQGGRTISVPQLERQDSGTWTCTVSQDQKTVEFKIDIVVLAFQKASSTVYKKEGEQVEFSFPLAFTLEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRAAQFQENLTCEVWGPTSPKLTLSLKLENKGATVSKQAKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVVPTWPTPVQPMALIVLGGVAGLLLFTGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI
The following text describes a protein:
Function:
Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated H3 'Lys-4'.
Miscellaneous:
MISCELLANEOUS: Present with 290 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Domain:
The JmjC domain is required for enzymatic activity.
Sequence:
MEEIPALYPTEQEFKNPIDYLSNPHIKRLGVRYGMVKVVPPNGFCPPLSIDMENFTFQPRIQNLENLDLKNRCRLFFMKQLNNFKRSVKDPSKLILREPYTIVEYSDSTHASEILKKKVYFYDVFSELIKDNRTLTDTTQSFRRKLKFRDISQLRGDISLWRTISKKFNVPIGLLKEIFEKYIASYYIFLHSLNENVHTALHADQYPKSLLSDDEDDFDLGPDSNSGSDFEEDDDDACIVCRKTNDPKRTILCDSCDKPFHIYCLSPPLERVPSGDWICNTCIVGNGYYGFTQDTHDYSLPEFQEYCKRQNSRLLPARKLSIDELEEMFWSLVTKNRRSSLTTVKYGADIHNELPGQITGFPTREFIPKNINGDELIDYLKYCDHPMNLTNLPMAHNSLLPLFKRNISGMTIPWIYIGSLFSTFCWHMEDQYTLSANYQHEGDPKVWYSIPESGCTKFNDLLNDMSPDLFIKQPDLLHQLVTLISPYDPNFKKSGIPVYKAVQKPNEYIITFPKCYHAGFNTGYNFNEAVNFTIDFWLPYGFGAITDYKLTQKACVFDMFDLMINVLDKYNKDTLLFNDAFVRQCYSSLIVFYNTELKRIRKIQAIVPRTTLLEVHTDPNDEDEEYDIFCSQCKTICSIAFVLRKNNYDSIRTYKRHKKNHLSIRQWNELSTTDSKVSILCTQDYLKSIQNLNNSDGEEPYIDDELYFTKSLKDIDSLIKQVGVKLDR
The following text describes a protein:
Function:
Galactose-binding lectin. Exhibits hemagglutination activity in a calcium- and magnesium-dependent manner. Also binds to several carbohydrates including lactose, D-galactose and GalNAc in a calcium- and magnesium-dependent manner. Likely to have antifungal activity as it is able to inhibit the activity of the A.flavus alpha-amylase.
Sequence:
AEETSFVFSKFKPLEPNLILQGDALVTVAGVLQLTNVDKNGVPEPSSLGRATYSAPINIWDSATGLVASFATSFRFTIYAPNIATIADGLAFFLAPVASAPDSGGGFLGLFDSAVSGSTYQTVAVEFDTYENTVFTDPPYTHIGFDVNSISSIKTVKWSLANGEAAKVLITYNSAVKLLVASLVYPSSKTSFILADIVDLSSVLPEWVRVGFSAATGASGGKIETHDVFSWSFASKLAGXXTKDSSFLDGG
The following text describes a protein:
Function:
Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.
Sequence:
MLGERDSRVANINQKIAQELGVRAEQVEAAVTLLDGGATVPFIARYRKEATGALDDAQLRTLEERLGYLRELEDRRKAILESIREQGKLDAALEATIMAADSKARLEDIYLPFKPKRRTKAEIAKEAGLEPLANQLMAEPGNDPKVVAESFINAEKGVADAAAALDGARAILVERFDEDADLIGALREEMWTNARMASKVRDGKKTEGEKFADYFEFSEPLTRLPSHRILAMFRGEKEEILDLQIQAEAEAPPPGVPSAYELKIMKRFGIADLKRAGDRWLIDTVRWAWRTKIQVHLNIDLRMRLWNAAETEAVRVFASNLRDLLLAAPAGTRVTMGLDPGYRTGVKVAVTDATGKVVDTAVIYPHEPQRQWNESLAILGKLALKHRVELIAIGNGTASRETDKLAGDLVKGLAELKMNKIVVSEAGASVYSASAFASEELPGLDVTLRGAVSIARRLQDPLAELVKIEPKAIGVGQYQHDLGQAKLAKSLDAVVEDCVNAVGVDVNTASAPLLARVSGVGSGLAQSIVAHRDANGPFKSRKSLKDVPRLGPKAFEQCAGFLRILGGEDPLDASGVHPEAYPVVRRILAATKSDIKALIGSSEIVRTLKPKDFVDETFGLPTVTDILRELEKPGRDPRPAFKAAVFKEGVEEIKHLQKGMILEGTVTNVAAFGAFVDIGVHQDGLVHISAMSKTFIKDPREVVKPGDIVKVKVLDFEVARKRISLTLRLDDEVGAKKDAPGMQRDNGSRNAARMTSSAPRKQESSGGGALAEALRRAAEKSGGKRV
The following text describes a protein:
Function:
Acts as a cofactor to fushi tarazu (ftz). Facilitates the binding of ftz to DNA. Binds the sequence element 5'-YCYYGGYCR-3' in the zebra element of ftz. Probably functions as a nuclear receptor for a yet unknown ligand. In contrast to vertebrate homologs, not activated by phospholipids.
Subcellular Localization:
Nucleus.
Sequence:
MDTFNVPMLAESSNTNYATEATSNHHHLQHQHQQQHSHQQQQQQQLLMPHHHKDQMLAAGSSPMLPFYSHLQLQQKDATATIGPAAAAAAVEAATTSANADNFSSLQTIDASQLDGGISLSGLCDRFFVASPNPHSNSNMTLMGTATAATTTTTNNNNNNNTNNNNNNNVEAKTVRPSNGNSVIIESVTMPSFANILFPTHRSANECIDPALLQKNPQNPNGNNSSIIVPPVEYHQLKPLEVNSSTSVSTSNFLSSTTAQLLDFEVQVGKDDGHISTTTTTGPGSGSASGSGSGSGSGSGSIARTIGTATPTTTTSMSNTANPTRSSLHSIEELAASSCAPRAASPNSNHTSSASTTPQQQQQQQHHMQSGNHSGSNLSSDDESMSEDEFGLEIDDNGGYQDTTSSHSQQSGGGGGGGGGNLLNGSSGGSSAGGGYMLLPQAASSSGNNGNPNAGHMSSGSVGNGSGGAGNGGAGGNSGPGNPMGGTSATPGHGGEVIDFKHLFEELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNKKVYTCVAERSCHIDKTQRKRCPYCRFQKCLEVGMKLEAVRADRMRGGRNKFGPMYKRDRARKLQVMRQRQLALQALRNSMGPDIKPTPISPGYQQAYPNMNIKQEIQIPQVSSLTQSPDSSPSPIAIALGQVNASTGGVIATPMNAGTGGSGGGGLNGPSSVGNGNSSNGSSNGNNNSSTGNGTSGGGGGNNAGGGGGGTNSNDGLHRNGGNGNSSCHEAGIGSLQNTADSKLCFDSGTHPSSTADALIEPLRVSPMIREFVQSIDDREWQTQLFALLQKQTYNQVEVDLFELMCKVLDQNLFSQVDWARNTVFFKDLKVDDQMKLLQHSWSDMLVLDHLHHRIHNGLPDETQLNNGQVFNLMSLGLLGVPQLGDYFNELQNKLQDLKFDMGDYVCMKFLILLNPSVRGIVNRKTVSEGHDNVQAALLDYTLTCYPSVNDKFRGLVNILPEIHAMAVRGEDHLYTKHCAGSAPTQTLLMEMLHAKRKG
The following text describes a protein:
Function:
Endonuclease that displays both RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase activity. As the only authenticated RNase HI in M.tuberculosis, probably plays an important role in the physiology of this organism, being likely involved in bacterial replication; Catalyzes the hydrolysis of the phospho group from alpha-ribazole 5'-phosphate to form alpha-ribazole. May also catalyze the conversion of adenosylcobalamin 5'-phosphate to adenosylcobalamin (vitamin B12) (By similarity). Has a possible role in B12 recycling, but the primary role of the C-terminal domain of this phosphatase enzyme could be phosphate generation to help bacterial survival within the macrophage, which is a phosphate-deprived environment.
Domain:
Is composed of two domains, the N-terminal domain displays RNase activity and the C-terminal domain has both acid phosphatase and CobC activity, together with a role in enhancing the RNase H and dsRNase activities of the N-terminal domain.
Sequence:
MKVVIEADGGSRGNPGPAGYGAVVWTADHSTVLAESKQAIGRATNNVAEYRGLIAGLDDAVKLGATEAAVLMDSKLVVEQMSGRWKVKHPDLLKLYVQAQALASQFRRINYEWVPRARNTYADRLANDAMDAAAQSAAADADPAKIVATESPTSPGWTGARGTPTRLLLLRHGQTELSEQRRYSGRGNPGLNEVGWRQVGAAAGYLARRGGIAAVVSSPLQRAYDTAVTAARALALDVVVDDDLVETDFGAWEGLTFAEAAERDPELHRRWLQDTSITPPGGESFDDVLRRVRRGRDRIIVGYEGATVLVVSHVTPIKMLLRLALDAGSGVLYRLHLDLASLSIAEFYADGASSVRLVNQTGYL
The following text describes a protein:
Function:
Proton-sensing G-protein coupled receptor activated by extracellular pH, which is required to monitor pH changes and generate adaptive reactions. Activated by an optimal pH of 6.0-6.6, a more acidic pH compared to mammals. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase. Gpr4 is mainly coupled to G(s) G proteins and mediates activation of adenylate cyclase activity. Acts as a key regulator of respiratory sensitivity to CO2/H(+): acts by mediating detection of protons generated by the formation of carbonic acid in the blood, an important mechanism to impulse to breathe. The acidic shift of optimum pH compared to mammals may facilitate adaptation to lower blood pH during diving.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
A multitude of proton-sensing residues, which include extracellular histidine residues or triad of buried acidic residues, contribute to activation of the G-protein coupled receptor activity and pH sensitivity.
Sequence:
MSNFTPDACNVDSGLDSVLPPSLYALVFTLGLPANLLALWAAWLQVRKGRELGVYLLNLSLSDLLLICALPPWTDYYLRRDVWGYGPGACRLFGFVFYTNLYVGAAFLSCVSADRYLAVAHPLRFPGARPIRSAAAVSALIWMLELAANAPPLLGEAIHRDRYNHTFCYESYPLSGRGAALANVGRVLAGFLLPWGVMMLCYAGLLRALRGSASCEQRERRRVRRLALGLPCVALLCYGPYHALLLLRSLVFLVGGGSVDAGGGCALEERLFPAYHASLALATLNCLADPALYCLACPGARGEVAKVVGGVVAWAMGKERRAWGERGGNGRGCGEGEEVGMVELRGNGREFVV
The following text describes a protein:
Function:
Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can also use unsaturated fatty acids. Catalyzes a key reaction in unsaturated fatty acid (UFA) synthesis, the elongation of the cis-3-decenoyl-ACP produced by FabA. Can use acyl chains from C-6 to C-14. Has an absolute requirement for an ACP substrate as the acyl donor, and no activity is detected when both substrates are based on CoA.
Subcellular Localization:
Cytoplasm.
Sequence:
MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAMRGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVMRKLKD
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MPKVTSKLTSSGKKKKKTVCCKYCDKEFRFPCLLVTHLRTHTGEKPFKCDICEKSFHSRPILKAHKESHKEQKPFKCSICEKSFHYIFAVKRHEKIHTGVRPKYKCEICDKYFTQNGNMYRHMLLHNRDKLYECNLCEKGFMQHKELRAHYSEHNKKPFQCSECDKAFFRETTLKRHQLTHKNNKPYQCSICDKYFKSKSHMKRHMVIHYRKKPYECKLCPKGFTQYKDLKRHYTKHNSMKPYKCDKCDKAYLQEAALTVHKRTHTGDKPHKCNICMKSFGYISNMKRHEKTHLTKTNNK
The following text describes a protein:
Function:
May directly or indirectly regulate the accessibility of the key branch point intermediate, monoacyl phosphatidylinositol tetramannoside (AcPIM4), to the elongating alpha-1,6 mannosyltransferases which could regulate the lipoarabinomannans (LAMs) biosynthesis.
Sequence:
MGVPSPVRRVCVTVGALVALACMVLAGCTVSPPPAPQSTDTPRSTPPPPRRPTQIIMGIDWIGPGFNPHLLSDLSPVNAAISALVLPSAFRPIPDPNTPTGSRWEMDPTLLVSADVTNNHPFTVTYKIRPEAQWTDNAPIAADDFWYLWQQMVTQPGVVDPAGYHLITSVQSLEGGKQAVVTFAQPYPAWRELFTDILPAHIVKDIPGGFASGLARALPVTGGQFRVENIDPQRDEILIARNDRYWGPPSKPGIILFRRAGAPAALADSVRNGDTQVAQVHGGSAAFAQLSAIPDVRTARIVTPRVMQFTLRANVPKLADTQVRKAILGLLDVDLLAAVGAGTDNTVTLDQAQIRSPSDPGYVPTAPPAMSSAAALGLLEASGFQVDTNTSVSPAPSVPDSTTTSVSTGPPEVIRGRISKDGEQLTLVIGVAANDPTSVAVANTAADQLRDVGIAATVLALDPVTLYHDALNDNRVDAIVGWRQAGGNLATLLASRYGCPALQATTVPAANAPTTAPSAPIGPTPSAAPDTATPPPTAPRRPSDPGALVKAPSNLTGICDRSIQSNIDAALNGTKNINDVITAVEPRLWNMSTVLPILQDTTIVAAGPSVQNVSLSGAVPVGIVGDAGQWVKTGQ
The following text describes a protein:
Function:
May play a role in the regulation of membrane traffic through the trans-Golgi network.
Subcellular Localization:
Golgi apparatus, trans-Golgi network.
Sequence:
MASSAEITLLKYIRDATEPFAFEPNLALNLEIADLINQKKGNLPRVAAFAIVRKINDRNPTVAYLAVNLLDICVKNCGYAFHLQIATKDFLNELVRRFPEHPRMGINKIQQLILRLIEEWRLTICKDSRYKDDFGFIRDMHILLGYNGYKFPEISKDDITVLSEKNTLKSIEELEREDREAMSAKLQELIRRGTPTDLAEANKLMKIMAGYDTQRKKEYRDRVIASLEKLKRKATLFGEMLAGITETDQLSAGDVYDELATSLQEASIKLERILKDDFEDENDKQQVASLYEYVTNLTNQYKCIKNRDVEGAANFRKTANEVEMVSAKSNSDLLIDLNFQPDTNSEINHTTDLVGSPASQTATPPIHLSSLAPSASSQPSALSPEPTLSNILHKFAYFTLRYASKEFQQNKLSLVLKLSNDSTKLIDNFQLFIAVPKVYKLQLEPQSGSMLPAGAVEGITQQVSVYGPLNPSKGLPVRLKVTYKIDGVLKEEFEQSVIPL
The following text describes a protein:
Function:
Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MESLKRWNEERGLWCEKGVQVLLTTVGAFAAFGLMTIAISTDYWLYTRALICNTTNLTASGDDGTPHRGGGGASEKKDPGGLTHSGLWRICCLEGLKRGVCVKINHFPEDTDYDHDSAEYLLRVVRASSIFPILSAILLLLGGVCVAASRVYKSKRNIILGAGILFVAAGLSNIIGVIVYISANAGEPGPKRDEEKKNHYSYGWSFYFGGLSFILAEVIGVLAVNIYIERSREAHCQSRSDLLKAGGGAGGSGGSGPSAILRLPSYRFRYRRRSRSSSRSSEPSPSRDASPGGPGGPGFASTDISMYTLSRDPSKGSVAAGLAGAGGGGGGGGAVGAFGGAAGGAGGGGGGGGGAGAERDRGGTSGFLTLHNAFPKEAGGGVTVTVTGPPAPPAPAPPAPSAPAPGTLAKEAAASNTNTLNRKTTPV
The following text describes a protein:
Function:
Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells.
Subcellular Localization:
Cytoplasm.
Sequence:
MFSRHFAAFFRFNRYVAQKYSSFIAAGFSNRFSLKVATLLPLVVLRSADCRQKEDQEVKRPVRRRTMSKVKYETSLEGRAQLYLNAMKVRWDQLHKVPGLFSYQLEKSPQSRKIPGYWGFYAELNSDRNRKRRRPQTIESLNPTFKHMMFNFNKVDAQEVIMTIDDAHGSPEVQMIINKSPITKYHTLICPEVGKNHTQRITRDALQFCITFMRNIDDKDMRMGYNSPGALASVNHLHFHLLHMPQDLYIDHVPLDELAGGYVYRLSRRAPTEGICIVFNENDSDEQVAEKVDQLYMLAMWMCKNNMPHNLFLTQDRRPGKSGNIKVFVFARSEYCVNKDLAEFNVGFCELAGYIPLPDADKMENLTELQVLFRIRTITGNAPKAVYEQITSMVEGQEYYLWDQPLTI
The following text describes a protein:
Function:
Oxidizes mannitol to mannose. Provides the initial step by which translocated mannitol is committed to central metabolism and, by regulating mannitol pool size, is important in regulating salt tolerance at the cellular level.
Sequence:
MAIDATKLVVFPKKAFGWAARDSSGVLSPFHFFRRETGEKDVAFKVLYCGICHSDLHIMQNEWGKTTYPLVPGHELTGVVTEVGSKVKKFKVGDKVGVGYMVDSCRSCENCADDIENYCTKYTQTFNGKSRDGTITYGGFSDSMVADEHFVIRIPDSLPLDGAGPLLCAGVTVYSPLRHFGLDKPGMNIGVVGLGGLGHMAVKFAKAFGAKVTVISTSPKKEKEAIEHLGADSFLVSRDPEQMQAATSTLNGIIDTVSASHPVVPLIGLLKSNGKLVMVGAVAKPLELPIFSLLGGRKSIAGSLIGGIKETQEMIDFAAKHNVTPEIEVVPIDYVNTAMERLVKGDVKYRFVIDIGNSLKPSP
The following text describes a protein:
Function:
Cytochrome b subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of ubiquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. The cytochrome b subunit contains two ubiquinol reactive sites: the oxidation (QP) site and the reduction (QN) site.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSTAANEPSRSRGKAPAGERVADWADGRLGIYSLAKANMRKIFPDHWSFMLGEVCLYSFIIIILTGVYLTLFFHPSMAEVEYHGSYVPLQGQMMSEAYASTLDISFDVRGGLLIRQIHHWAALIFLAGMFVHMMRVFFTGAFRKPREVNWLFGFLLLVLGMFTGFTGYSLPDDLLSGTGIRFMEGAILSVPIVGTYISFFLFGGEFPGHDFVSRFYSIHILLLPGIMLGLLVGHLILVFYHKHTQFAGPGKTNKNVVGMPLLPVYTAKAGGFFFLVFGVISVVSAIATINPIWAIGPYRPDQVSTGAQPDWYMGFSEGLIRVMPGWEINAWGHTLVLGVFVPLLIFPLVLAAIAVYPFIESWVTGDKREHHILDRPRNAPTRTAFGVAWLTVYFVLLIGGGNDLWATHFHLSINAITWFVRIAFFVGPVVAFIATKRICLGLQRRDKDKVLHGRESGIIKRLPHGEFIEVHEPLSQEQLHTLTAHEQYQPAEIGPTVDENGVERKVSGTQKLRAKLSESYYGEESQIPKPTVEEYKEITSGHGHH
The following text describes a protein:
Function:
Repressor of jasmonate responses.
Subcellular Localization:
Nucleus.
Domain:
The jas domain is required for interaction with COI1.
Sequence:
MSNLELAVLPKLVHDDDTKLPVSQREKGESEQLTIFYAGIVHVYDNIPAEKAESIINLARESCSQLSGSTVAKEIKSTHKSQVPSVCKFQADLPIARRKSLERFFEKRHNRITSKQPYASPAITQSEDKCDDESMMASGEGSPRASREVTMDALLSTTKLNQPIQIDDVEGEGPYGGEGLYEATLFVEFVCNRKGAYGGGHRGRRGGIGPAPYGRGWGHKASEYPNQRNIVLMEGDPYFVRVKMTKSDVSEGTLQEDDGDDGEPERVVEEGKVNVPCGLMRKTPHDDAWPEEGEVLISL
The following text describes a protein:
Function:
Repressor of the mexAB-oprM multidrug resistance operon. Also represses its own expression. Many variants lead to increased expression of the mexAB-oprM operon.
Sequence:
MNYPVNPDLMPALMAVFQHVRTRIQSELDCQRLDLTPPDVHVLKLIDEQRGLNLQDLGRQMCRDKALITRKIRELEGRNLVRRERNPSDQRSFQLFLTDEGLAIHQHAEAIMSRVHDELFAPLTPVEQATLVHLLDQCLAAQPLEDI
The following text describes a protein:
Function:
May be involved in cell wall biosynthesis.
Subcellular Localization:
Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Sequence:
MEKAWWRSRMWTATATAVVILLPSFALLGYMESEHALLSQTSSVLEGIVSSSYGYAAGALPTSGGGATAVGPVQDLIARLRERTRLALASSADEPYSEEEQQIWAVRNPCVARDALPARYKRRTFAQDPAPNAAWARVFHEYSNLHRACTRRIGNLSRAFYSDASDAVPPGCQFVIGESYTGLGNKMLVLASTLMYAVLTGRVLLAPANTLIPAVFCEPFEGSSWRVDDDGMTNLKAGGPWTEVAGSFGWVDEQAAENVSRLLTRVKVHNGWQPVNRFYCDSEQAFLSQVPWMQIGACLHFLPRLFAVPKFRPVMEALFPDRMALTHLLRSALLPSDAVWERVLNVDEVYLEHTERQIGVQVRYFDQRIRDRINSRVGDCCLENDLLPAVQPFPSPAAATNANQSAPTTANVRTARSGHQHSRITKVFIASLLPDVHDYLNQRYLRQRTVGEVAVGLVQLTHESSQRTGVEVDSEALVEMLCLSFSDHLLVTPQSTFGGVAQAYGALKPWFINYDRDPSIPPSVNCQRGQSVDVCYQGGPRGYDCKHDPGLKGHNLFDDLPYLQPCLGIDTSGIQIITSHDSL
The following text describes a protein:
Function:
Serine/threonine-protein kinase that may function as a signaling receptor of extracellular matrix component. Binding to pectin may have significance in the control of cell expansion, morphogenesis and development.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MIWLHGLLDELAKKQEMRILHSDSHSAIFLAKNSVFHSKSKHIQTKYHFIRYLIEDKLVILEKIYGSKNPADMLTKGVTIEKLKLCTASIAATVNGQAKEGCLDRCEAVIIPYPFGTDEHCYLSPYFWVTSNHSSNPPKLLLGKPSPEGNNVQVLDISLEGELLILNYVSHDCYDSLGEADSLYSYDSYLKPGQFNISSTKNKFTMVGCDTFAWFKGQRGHESYRTGCMSICDNITDVQNGSCSRNGCCQTSIPDGLSAIDLTLGSFNNYSEIWEFNPCGYAFIVEESNFNFSSNDLRDLKSKTELPMVFDWALDKETCQVDVNDQTNNACKGNSTCNKRITGWGYLCNCSEGYQGNPYLEPGCQDIIECENSILNKCENPETCINTQGNYTCSCPMWYHGDGKIDGQRCIPNRLQMIHVAMGQKNCKFSNLYLKLVVAFQCASNVEHLENLVFIFFYSKVLELIYSSLKYCLISLINICIGIALVVLVAGSTWLYWALKKRRFVKLKKKYFQQNGGSELRQQLSGQGSTERIKFFTSEELEKATKNYDESNIIGRGGFGTVYKGTLTDGRIVAIKKSKMVERIQGKGFINEVGILSQINHRHVIQLLGCCLETQVPLLVYEFINNGTLSDHIHDENKASAIMWETRLRIAIQTAEALYYLHCVASTPIVHRDVKSSNILLDEEYNAKMCDFGASRLVPLDQNQLSTAVQGTPGYLDPESLQTNRVTEKSDVYSFGVVLVELLTGKKALFFDRPKEQRILTIFFLFPLKDDSLFQVLEDCIVNNGNHKQILKVAQLAQRCLSINGEDRPTMKEVMLELEMIRMIGENAEQNPEENTYLLGESYAHYYLGGGESSIATHSMTGSFLLPI
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAKSASNKKSIPTTSSSSTATSAASSSVVLKEVKSTLTTTINNYFDTISAQPRLKLIDLFLIFLVLLGILQFIYVLIIGNFPFNSFLGGFISCVGQFVLLVSLRLQINDSTTTTTDKESDDQLELDEDKIENGTTGGGNGRLFKEITPERSFGDFIFASLILHFIVIHFIN
The following text describes a protein:
Function:
Acts as a transcriptional repressor.
Subcellular Localization:
Nucleus.
Sequence:
MQNSLSVPPRDEGESNIPSGTIQSRKGLQNKSQFRTIAPKIVPKVLTSRMLPCHSPSHSDQVNLGPSINSKPLGMSTQNYALMQVAGQEGTFSLVALPHVASAQPIQKPRMSLPENLKLPIPRYQPPRNSKGSRKKPILIFPKSGCSKAPAQTQMCPQMSPSPPHHPELLYKPSPFEEVPSLEQAPASISTAALTNGSDHGDLRPPVTNTHGSLNPPATPASPTPEEPAKQDLTDLSGKAHFVSKITSSKPSAVVSEKFKEQVYLAKTMTSLSPAILGNAVQLISSVPKGKLPIPPYSRMKTTEVYKIKSDANIAGFSLPGPKADCDKISSTTEGFNAATKVASKLPVPQVSQQSACESAFCPPTKLDLNHKTKLNSGAAKRKGRKWKVPDEILAFQGKRRKCIINKCRDGKERVKNDPQEFRDQKLGTLKKYRSIMPKPIMVIPTLASLASPTIQSQMLGGLGQDVLLNNSLTPKYLGCKQDNSSSPKPSSVFRNGFSGIKKPWHRCHVCNHHFQFKQHLQDHMNTHTNRRPYSCRICRKSYVRPGSLSTHMKLHHGENRLKKLMCCEFCAKVFGHIRVYFGHLKEVHRVVISTEPAPSELQPGDIPKNRDVSVQGMEGSLERENKSNLEEDFLLNQAGEVKLQIKCGRCQITAQSFAEIKFHLLYVHGEEIQGRLQEGTFPGSKGTQEELVQHASHDWKRHPERGKPEKVHSSSEESHACPRLKRQLHLHQNGVEMPIENEGPQSGTNKPRETCQGPECPGLHTVLLWSRSGFNCLLCAEMLGQKEDLLHHWKHQHNCEDPSKLWAILNTVSNQGVIELSSEAEK