lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Melittin: Main toxin of bee venom with strong antimicrobial activity and hemolytic activity. It has enhancing effects on bee venom phospholipase A2 activity. This amphipathic toxin binds to negatively charged membrane surface and forms pore by inserting into lipid bilayers inducing the leakage of ions and molecules and the enhancement of permeability that ultimately leads to cell lysis. It acts as a voltage-gated pore with higher selectivity for anions over cations. The ion conductance has been shown to be voltage-dependent. Self-association of melittin in membranes is promoted by high ionic strength, but not by the presence of negatively charged lipids. In vivo, intradermal injection into healthy human volunteers produce sharp pain sensation and an inflammatory response. It produces pain by activating primary nociceptor cells directly and indirectly due to its ability to activate plasma membrane phospholipase A2 and its pore-forming activity. In the context of inflammation and cancer tests, is highly cytotoxic to normal cells, highly induces calcium signaling and almost completely prevents cAMP production. In addition, prevents LPS-induced nitric oxid (NO) synthesis but does not affect the IP3 signaling and pro-inflammatory activation of endothelial cells. Also shows significant antiproliferative activity on the breast cancer cell line MDA-MB-231; Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin; Melittin-2: Has strong hemolytic activity.
Miscellaneous:
MISCELLANEOUS: N-formyl-melittin major has 80% of the activity of melittin; MISCELLANEOUS: Melittin: The secretion of this protein into venom follows a seasonal pattern. This variation is synchronized with phospholipase A2 variation, i.e. their production increase in the same months; MISCELLANEOUS: Melittin-S: The secretion of this protein into venom follows a seasonal pattern, the maximum secretion occurring during the (southern) winter months; MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at 56-Leu-Pro-57. The trans conformation is the major form. The trans conformation is required for an alpha-helix; MISCELLANEOUS: The derivative MelP5 is amidated.
Subcellular Localization:
Secreted. Target cell membrane. Note=Alpha-helical peptides form toroidal pores in the prey.
Sequence:
MKFLVNVALVFMVVYISYIYAAPEPEPAPEPEAEADAEADPEAGIGAVLKVLTTGLPALISWIKRKRQQG
The following text describes a protein:
Function:
Acts as actin nucleation factor that directs the formation of actin cables and polarized growth in pollen tubes.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MGRLRLAFLAISLVVFVCVSEEIFSRGGLNLLRFSVYGEDVAEQTWIHQNPRRKLISYPKKFSVSAPNLAFGPAPSFAPGPGPSFAPGPAPNPRSYDWLAPASSPNEPPAETPDESSPSPSEETPSVVAPSQSVPGPPRPPPQREKKDDILMKLIIAVASTAVLTFVFVALMFLCCFKRNCNNAVGSRDGPRDEGPLLRLSTGSTENSPTVASTSRKMFSVASSKKRSFLSRVSLKRNGHEFSTAESSSAAGLPPLKLPPGRSAPPPPPAAAPPPQPPPPPPPKPQPPPPPKIARPPPAPPKGAAPKRQGNTSSGDASDVDSETGAPKTKLKPFFWDKMANPDQKMVWHEISAGSFQFNEEAMESLFGYNDGNKNKNGQKSTDSSLRESPLQYIQIIDTRKAQNLSILLRALNVTTEEVVDAIKEGNELPVELLQTLLKMAPTSEEELKLRLYSGDLHLLGPAERFLKILVDIPFAFKRIESLLFMISLQEEVSGLKEALGTLEVACKKLRNSRLFLKLLEAVLKTGNRMNVGTFRGDAQAFKLDTLLKLSDVKGTDGKTTLLHFVVLEIIRSEGVRALRLQSRSFSSVKTDDSNADSSPQSVERYRSTGLQVVTGLTTELEDVKRAAIIDADGLAATLANISGSLTNAREFLKTMDEESDFERALAGFIERADADFKWLKEEEERIMVLVKSSADYFHGKSAKNEGLRLFAIVRDFLIMLEKVCREVKETTKTTNHSGKKESEMTTSDSNQPSPDFRQRLFPAIAERRMDSSDDSDDEEDSSPS
The following text describes a protein:
Function:
Dephosphorylates a number of phosphatidylinositols (PIs) like phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), but also phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Specifically functions within the early endocytic pathway and actin organization.
Subcellular Localization:
Cytoplasm, cytoskeleton, actin patch.
Domain:
The SAC domain is capable of hydrolyzing phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Sequence:
MKILLSKQQTRKIAIVSETHGLVFRPINSKNSRRSTCAVELVPKAELNGNGFRRLSNHEIYGFIGLIEIEGLMFIATITGKSKVAQPIPNKTVNKIYAVDFFCLNNSKWDFMDIDSSGYPIVTNDGDFAISSPPSISTHSSRSSLRSSSSRSLNAQEQAPKHPCHELRKLLSNGSFYYSTDFDLTCTLQKRGFTEHSLSFDDFDREFMWNSFLMDEIITYRDRLDVTAKELLDQRGFLTTVIRGFAETIFSYINRLKVGLTIISRQSWKRAGTRFNARGIDDDGHVANFVETEMIMYSSQYCYAFTQIRGSLPIFWEQDTSLISPKIQITRSVEATQPTFDEHFIRLFKKYGPVHIINLLSTKSSEIQLSRRYKEQLKNSEKMKIGRDVFLTSFDFHRETSQDGFAAASRIIPKIRNTILDAGYFSYDVKEGRLISEQDGVFRTNCLDCLDRTNLIQQTISLAVFKLFLEDFRLVKPSSFIDDNEFVQKVNALWADNGDQISQIYTGTNALKSSYSRKGKMSFSGALSDATKSVSRMYINNFVDKGKQQNIDTLLGKLPHQQVVELYDPICEYVNERLLESEEKFTTHSNINLFVGTFNVNGNSRRADLSKWLFPIGDKFKPDVVVLGLQEVIELTAGSILNADYTKSSFWETMVTDCLNQYEEKYLLLRVEQMSSLLILFFARSDRAYNIKEVGGSTKKTGFGGITGNKGAVAIRFDYGATSFCFVNTHLSAGASNIDERRNDYNNIYRNITFPRSKTIPHHDSLFWLGDLNYRITLTNDEVRRELRAQKDGYIDRLLQYDQLTQEINEGVVFQGFKEPTLQFRPTYKYDYGTDNYDTSEKARTPSWTDRIIYKGENLHPLAYSDAPLKISDHKPVYAAYRANVKFVDEKEKLNLVEKLYAEYKNTHPEALTTGPDELSHARMEKQKESIPLDATVQSAGIKLIDLDDTSSCVSPLLSGPSPQPSVVGPGGLSNVSPDKSKLNVLPPPPPTSRHNKEPSSKLLSPTKEISIVSVSPRKGESNLPALERHSTPKPLPPVPALSLSKPVSLQKSSSELQHAKETIDNGKIVPRPCPPIRRKSSTAPDEISTSTKNSGVSTTEDPEPAKASTKPEKPPVVKKPHYLSVAANKLNTSQEHSIKVSPSNSKSEEELPCKKKSKPKVPAKNPELEKLSVHPLKPCDPN
The following text describes a protein:
Function:
Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol-disulfide oxidase activity. May function as an important antioxidant, and may be involved in the responses to viral infection.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MQTSLANIVLFSSLQVLLSLTCFQEVVEAASGKGFGDNIHWRTLDDGKKEAEASGLPIMLIIHKSWCGACKALKPKFAESKEISELAHNFVMINLEDEEEPKDDAFSPDGGYIPRILFLDPSGKVHPEITNKNGNPNYKYFYSNAEQVISGMKEAQEKLTGDAFKQRHTGDEL
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 2 (EFT1/EFT2) at 'Lys-613' and methylates elongation factor 3A (YEF3).
Miscellaneous:
MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MFDPLDLYTPDDIQVEALQFNLAEREPKDPCSPQRDEILTAVDEEESDDDDTIIDNLDLPSVKYAPPEVILCILILLKPDRQVNFNQETGKNKSVLEVCKSHGLEPDLLKRLLTWYTEEWPNKRLNSLEKICNKIPMLRFTVSKELLLGYYTSVLKKYNNSCGLNEEIIQELLKELSSRISENCGRTAQPSIVRYFELRNLSTSIPLHEPSLTADNLGWKTWGSSLILSQLVVDHLDYLHTTNVNMLANSDIKQIKVLELGAGTGLVGLSWALKWKELYGTENIEIFVTDLPEIVTNLKKNVSLNNLGDFVQAEILDWTNPHDFIDKFGHENEFDVILIADPIYSPQHPEWVVNMISKFLAASGTCHLEIPLRAKYAKEREVLKLLLKESDLKVVEERHSEGVDDWGAVKYLYRQIVRN
The following text describes a protein:
Function:
May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Cell projection, dendrite. Cell projection, dendritic spine. Early endosome membrane; Single-pass type II membrane protein. Postsynaptic density membrane.
Sequence:
MEGDREDRKWTEELEVSYKHWRTSPRGGPGERVFCKQNGLIDTHRVGAEPTEALVSAYTIPYCQGHEGLKEHSGPPQLLNPGALLPHQAASDPSFRPASGLLLCREGLLQMWGEAGGGDCCETTFIEGHGHDTTNSATCSPKEVLLYADAKFLEFSGEGAIIPSLSYDIDDDDDFQELESDYSSESESEDAFLLLPPRDHLGLSVFSMLCCFWPLGIAAFYLSHETNKAVSKGDFHLASSSSRRALFLAVLSITIGTGGVGSPRTGL
The following text describes a protein:
Function:
Transcription factor involved in RNA polymerase II (RNAPII) transcription regulation. Involved in transcription elongation. May function at post-recruitment and elongation steps of transcription. May be recruited by BZR2/BES1 to target genes and promote their expression during transcription elongation process. Required for brassinosteroid (BR)-induced gene expression. Required the for regulation of numerous nitrogen-responsive genes in roots. Acts in roots to repress NRT2.1 transcription in response to high nitrogen supply. This repression is associated with an IWS1-dependent increase of trimethylation on 'Lys-27' H3K27me3 at the NRT2.1 locus.
Subcellular Localization:
Nucleus.
Sequence:
MGFEDDPYRDVDGEPIVDFDDFGNDREPSTEPLQDFDEDLADDIGDWDGEGSQTPVYDNDKVAKPRKRLVKKSSSERVTIDVPELIDEDVDDAEFDEFMGGRGGGSTDYDDKVGRKRKKEKERSSSGSGKEKRHKFPNRGERKSEEIDEMWKSIAHNPENDEEGVRTMDDDNFIDDTGLDPSERYGGDAGDRSPTHYPQAEEGEDEDEVNNLFKMGKKKKKTERNPAEIALLVENVMAELEVTAEEDAELNRQGKPAINKLKKLSLLTDVLGKKQLQTEFLDHGVLTLLKNWLEPLPDGSLPNINIRAAILRVLTDFPIDLDQYDRREQLKKSGLGKVIMFLSKSDEETNSNRRLAKDLVDKWSRPIFNKSTRFEDMRNLDEDRVPYRRPPVKKPSNKATMESRDGDFDLEIRERKTGLTSGQSSRGDRQMTMRPEATPLDFLIRPQSKIDPDEIIARAKQVSQDQRRVKMNKKLQQLKGTKKKRLQATKVSVEGRGMIKYL
The following text describes a protein:
Function:
Plays an essential role in chain termination during de novo fatty acid synthesis.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MLCAYFRLTVNSLLFLIWTDFSKVGGESSIQGLITSAASNIHQVQCFHLTIMAASSNIMTSKFFMAISPSSWNSTNKSKICLQQIDTSSNTNGKMVKFTRDSSLKVKLQAQALLTNDSRATSMIESLKDEEMMTSPPATMEHLTTEGRLINDGLVFQQNFSIRSFEIDSEYKVSARAIMNYLQESSLNHRKKMGMSSDSLVGVTPEMIKRDLLWIFRGMCIEVDRYPSWADVVQIYHRIYTSGRTGLRLEWIVNDSKTGETLVRASCLAVMMNKKTRKTCKFPEEVKQELKPYLTTDAEPLFEADKILCPQVGKMDNIRTGLTSYWHDLDFNYHVNNAKYLDWILEGTPTSLIHSHELSRVSLQYRKECLKDDVIQSLSRVVTKETGLSTNNQEIELEHVLRLESGPELAGARTAWRPKSICRQTIN
The following text describes a protein:
Function:
Required to maintain the structure of the centrosomal microtubule organizing center (MTOC) during mitosis. May have a preferential role in regulating neurogenesis. Required for germ cell mitosis and oocyte differentiation.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, microtubule organizing center. Cytoplasm, perinuclear region. Note=During interphase in syncytial embryos distribution is cytoplasmic. On entering mitosis, moves to polar regions of the spindle immediately surrounding the centrosome. At telophase, migrates to microtubules on the spindle side of both daughter nuclei. The nuclear-cytoplasmic distribution could be regulated by the availability of calmodulin. In the fat body, localizes to a perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs).
Sequence:
MSAFEITVTPSRLKQKKRAEGREPAVVVMAPFSAKAIVQFEDVPITKTARRQVRVLNPSDDDIEVKVMKAIREEHNLSLEWMEHTVPARDEVSMELVWSPVLEVACKETLQLIDNRNFRKEVMIILKSKSNQPVKNPRKFPTVGKTLQLKSPTGAGKTMKSVVSAAVQQKKRMSAAAAPPSKQTWRVTAPSRPAAWAHPPPQAPLVEKNVYKTPQEEPVYISPQPRSLKENLSPMTPGNLLDVIDNLRFTPLTETRGKGQATIFPDNLAAWPTPTLKGNVKSCANDMRPRRITPDDLEDQPATNKTFDVKHSETINISLDTLDCSRIDGQPHTPLNKTTTIVHATHTRALACIHEEEGPSPPRTPTKSAIHDLKRDIKLVGSPLRKYSESMKDLSLLSPQTKYAIQGSMPNLNEMKIRSIEQNRYYQEQQIQIKAKDLNSSSSSEASLAGQQEFLFNHSEILAQSSRFNLHEVGRKSVKGSPVKNPHKRRSHELSFSDAPSNESLYRNETVAISPPKKQRVEDTTLPRSAAPANASARSSSAHAWPHAQSKKFKLAQTMSLMKKPATPRKVRDTSIQPSVKLYDSELYMQTCINPDPFAATTTIDPFLASTMYLDEQAVDRHQADFKKWLNALVSIPADLDADLNNKIDVGKLFNEVRNKELVVAPTKEEQSMNYLTKYRLETLRKAAVELFFSEQMRLPCSKVAVYVNKQALRIRSDRNLHLDVVMQRTILELLLCFNPLWLRLGLEVVFGEKIQMQSNRDIVGLSTFILNRLFRNKCEEQRYSKAYTLTEEYAETIKKHSLQKILFLLLFLDQAKQKRIVKHNPCLFVKKSPHKETKDILLRFSSELLANIGDITRELRRLGYVLQHRQTFLDEFDYAFNNLAVDLRDGVRLTRVMEVILLRDDLTRQLRVPAISRLQRIFNVKLALGALGEANFQLGGDIAAQDIVDGHREKTLSLLWQLIYKFRSPKFHAAATVLQKWWRRHWLHVVIQRRIRHKELMRRHRAATVIQAVFRGHQMRKYVKLFKTERTQAAIILQKFTRRYLAQKQLYQSYHSIITIQRWWRAQQLGRQHRQRFVELREAAIFLQRIWRRRLFAKKLLAAAETARLQRSQKQQAAASYIQMQWRSYQLGRIQRQQFLRQRDLIMFVQRRMRSKWSMLEQRKEFQQLKRAAINIQQRWRAKLSMRKCNADYLALRSSVLKVQAYRKATIQMRIDRNHYYSLRKNVICLQQRLRAIMKMREQRENYLRLRNASILVQKRYRMRQQMIQDRNAYLRTRKCIINVQRRWRATLQMRRERKNYLHLQTTTKRIQIKFRAKREMKKQRAEFLQLKKVTLVVQKRRRALLQMRKERQEYLHLREVTIKLQRRFHAQKSMRFMRAKYRGTQAAVSCLQMHWRNHLLRKRERNSFLQLRQAAITLQRRYRARLNMIKQLKSYAQLKQAAITIQTRYRAKKAMQKQVVLYQKQREAIIKVQRRYRGNLEMRKQIEVYQKQRQAVIRLQKWWRSIRDMRLCKAGYRRIRLSSLSIQRKWRATVQARRQREIFLSTIRKVRLMQAFIRATLLMRQQRREFEMKRRAAVVIQRRFRARCAMLKARQDYQLIQSSVILVQRKFRANRSMKQARQEFVQLRTIAVHLQQKFRGKRLMIEQRNCFQLLRCSMPGFQARARGFMARKRFQALMTPEMMDLIRQKRAAKVIQRYWRGYLIRRRQKHQGLLDIRKRIAQLRQEAKAVNSVRCKVQEAVRFLRGRFIASDALAVLSRLDRLSRTVPHLLMWCSEFMSTFCYGIMAQAIRSEVDKQLIERCSRIILNLARYNSTTVNTFQEGGLVTIAQMLLRWCDKDSEIFNTLCTLIWVFAHCPKKRKIIHDYMTNPEAIYMVRETKKLVARKEKMKQNARKPPPMTSGRYKSQKINFTPCSLPSLEPDFGIIRYSPYTFISSVYAFDTILCKLQIDMF
The following text describes a protein:
Function:
Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Along with RAD10 forms an endonuclease that specifically degrades single-stranded DNA.
Miscellaneous:
MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSQLFYQGDSDDELQEELTRQTTQASQSSKIKNEDEPDDSNHLNEVENEDSKVLDDDAVLYPLIPNEPDDIETSKPNINDIRPVDIQLTLPLPFQQKVVENSLITEDALIIMGKGLGLLDIVANLLHVLATPTSINGQLKRALVLVLNAKPIDNVRIKEALEELSWFSNTGKDDDDTAVESDDELFERPFNVVTADSLSIEKRRKLYISGGILSITSRILIVDLLSGIVHPNRVTGMLVLNADSLRHNSNESFILEIYRSKNTWGFIKAFSEAPETFVMEFSPLRTKMKELRLKNVLLWPRFRVEVSSCLNATNKTSHNKVIEVKVSLTNSMSQIQFGLMECLKKCIAELSRKNPELALDWWNMENVLDINFIRSIDSVMVPNWHRISYESKQLVKDIRFLRHLLKMLVTSDAVDFFGEIQLSLDANKPSVSRKYSESPWLLVDEAQLVISYAKKRIFYKNEYTLEENPKWEQLIHILHDISHERMTNHLQGPTLVACSDNLTCLELAKVLNASNKKRGVRQVLLNKLKWYRKQREETKKLVKEVQSQDTFPENATLNVSSTFSKEQVTTKRRRTRGASQVAAVEKLRNAGTNVDMEVVFEDHKLSEEIKKGSGDDLDDGQEENAANDSKIFEIQEQENEILIDDGDAEFDNGELEYVGDLPQHITTHFNKDLWAEHCNEYEYVDRQDEILISTFKSLNDNCSLQEMMPSYIIMFEPDISFIRQIEVYKAIVKDLQPKVYFMYYGESIEEQSHLTAIKREKDAFTKLIRENANLSHHFETNEDLSHYKNLAERKLKLSKLRKSNTRNAGGQQGFHNLTQDVVIVDTREFNASLPGLLYRYGIRVIPCMLTVGDYVITPDICLERKSISDLIGSLQNNRLANQCKKMLKYYAYPTLLIEFDEGQSFSLEPFSERRNYKNKDISTVHPISSKLSQDEIQLKLAKLVLRFPTLKIIWSSSPLQTVNIILELKLGREQPDPSNAVILGTNKVRSDFNSTAKGLKDGDNESKFKRLLNVPGVSKIDYFNLRKKIKSFNKLQKLSWNEINELINDEDLTDRIYYFLRTEKEEQEQESTDENLESPGKTTDDNALHDHHNDVPEAPV
The following text describes a protein:
Function:
Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching (By similarity).
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MASKEATVYVVDLHESMGREMARGHDSKEVTDLNWGLQYIYSEISNKILSGRKTDVVGLVGVHTDTTQNMFEEESGFEHIDIITPIQQFNLDTLLEAKKQLVPNSDNKGDLISGIVVAVQMIKLYTKALKYIRNIVVLTNGQGNMNLGDSGGIIKQLNENRIILKVMGVDFDDEEVDYFEEDKPEHKRENELKLKEFVDRCEDSVFATYKEARDSLDIPKVKAVNPVRAFQGNLVLSDPEQQPPQRVMSIGVEVFPCTRRATAMTASSYAMSKIEPATISTPSQNNLQAVKWDRQYYVNDESGIGGKKELDRDTLENGYRYGSEIVYITKEEEEAIMFPTSASLQVIGFVNKKSVPPYMLMGHTDYIIGQRGNNRDAVAISAFARALFETDNFGLARYVNKDGKDPQIVVLMPYIRAELEGLVFCQLPFAEDERKFILPSLTSLETRSGNKTVTTHSRLLPTKEMLDAMDDYVDAMDLSKLKGEDDEPWLTMEECFNPSIHHIRNVVKECAVSQDYGKIPEPLPILTRFSQPAEELTEEAKPQLELLKHLFDIKEQFREAKKRKTEVTVGQTGLDLDALLEGELEVKLESSQTLSSNVKSEPGRQTASQSSQNSQQLSLDPENICPDFIRTLNKIDTKATSDEEFRSGATNLYKQTITLLEEKLESSKGNDAYNEIIGVLQTMREQADEMEIPDVFTAAKGQFVSKLERGDLGGQKNVLVAQINSI
The following text describes a protein:
Function:
Has a role in a nucleosome assembly pathway that is required for the integrity of heterochromatin and proper chromosome segregation.
Subcellular Localization:
Nucleus.
Sequence:
MPTFQAINVEPEENVDEEIDTTKQIQVDDALKLFQNALKLHAQGPRFFDEASDAYNALFESEIFRYPESKTEYERTEERPDGTLVVEPTLAQGLEVGAADVDGIASTLPQTLYLSFKNHGQFIVDRIKHKARASKLGSDFDYDDAAIQHDAKKALDEFSAALDYDPSDADLWRKTARIAAFLKSARISRYSLEAAVELDDDPAVTDFEPPSLAEGFAGEQLKRQLEVLDDKMALSHPIMKSFREKGLPKFLERYLDPIPSLPDYAKTIAAPRPDSDEVGQPRLVMNIPSYSWTELGIALVHFVAEHGFSGQAVAIQLPEGIVEDEDVQMEIDKQLQPPEESTQEEEAAVVAEVTSAEKSGAQDTEEAESIVRETKVTIVEEARAAQPTKDRTSSLPTRKRSQSAAGIPDPGDEEKGETKRSKRTRRRETAPEEAMDSATLLATQLQPFQAADQNLFQMTKNFLENLGVTDRDTLDRITEILDSCASDDRTSKIQNPATTDLREAILHFDEETASILLDGRESPPLSLSAFLEHSKSPSQRAIEPPQFDDVRNIRGFVMRMNSGWNTIQDVVYEYVKSLAESYSTEKWSDQMKVAIVQVISRLDEGIYDRVVYDLEQWQLSDASGHQPSPDIVDLVYMLFELHLDVYERITNPNSVVEQITRTKARIRLGRWWDLATQVSRRRYFGTDDALTLRFLWAAVVFITVTEGVPREHILNCWHSLRDHLATTTVPDIVLPNNAVMPEISVAAADREVSKLTTMEFFLGLFQEEQDNPVSVIDTLEPVLNPESVCINSQAAPNPTEDAMDEDTEPAGNIKSVKDCASQGLQDLWNFIEKSSTDLRLLLWSRLGDAYGKIKYTTKQFSCFLRSIETIVHDFERKDYVNTPQAARKELFMTMLKALDDQIIQSLHLALNHNNSFDIIDEEHIKTTSAALAKVSCLLHVAAMYEDEASVGIIQPPATGSLAASFLNRLREMQVRTWSLQYTVLKMGINLHPDIFLTPENDLADYLAAVHQVLGLRKYCKSSNKIFLKMMRVELLKLKNIENWEDYLGQVLYDLHGLKLGVGIWDVQEHDCPPEKLEKRQALAMVEKISLLAHRMTMKDLLKSDLKNTVESMQQAIGSAKSTAQMMHNHRNFNEYLKTPIHPLHLYKALTGNVDLDAVTINTPDSAPAKHGWFFLLGMIALTKFKGVDLNRRQTPGALDDLRIAVTFLRLQLQYTPDRWDAWFRLAECFDYELDDMVLWTADKMNKDRADLVKFQRQSIHCYTLALSHSYASTSDPNVYALSGGDTEALYDLYHEFGMRMYASSREPFAMEPFMHSDQHRFFIEISGNGTYKEILHNQMSDYQVWKFAASLFRKAMAGKPKDWKNPYMIAKCLWKMYQKPEDELDEKNRHGRPTVQAVIKALEKTVEVVRTLPKPRHGQDPILEPHYKILSVINKLVTRGDLPHQEAADILQRQPLAPGRGERVTLEKDEDWHEYMLRYMRHLRDKDKSNWQHRMIIRHARLLFDGDEIGDEEDETKKEASKEAASKAFAVLRENMFTKTMVMNVWKCDAERPGRHHVYTEQYIRYMARLLAVMNDRANLEAVLRRIRKKGVDFYHFSELWQHGVQIYLKMIRKAFNIPANDEDPFKNVAPEDFEAVAEKIAEWVITPEAESHAALNAMKEAIELKKLNANLMKAGPIDDLINDCYSIIHHEMVPEQTASETPQGGDEHSRAGEGELPTKPAAEGEEPKSMTLSILPALQERERAAAAAAASGSLRAPSEQPDKMSEKQLSFNGDITHRGRKLGVRRPDVLRKAEQAVLRAAEGPPKALSGITRSSRKGSVSSGSGKKGQTTRDEGADDDNDETDEDITRHDDEDITMKDADDEDNNRPRSRRSRRGQDDTQMADDEHEEEAMSSPPGSVHDSADDESDLSDVPADYEDDIPPSLLFPNLRRSVDASAAGGAVAASATTPLTPGRPTIYSSSSESGSSSADEKAQSEPKRTPRKPSWHKSQATKAQHERPGSSSIDQHKATEGGSIGPMRWGLKTGRPRNGSGTSASAVVHGVPGTEDVEDAEEDEVEEEVEDEDEDEGEHEDAEETVGEVGETEEEGDEDVDVDEEMEDGEGEEDVEEGEEDHEDDEDVEAEEEDEEEAEEAEEDVRPGEHKDDVEEGTEGEEEGEEGGEEEEEEEGVEDAEDEEGDEEEEEADEEEGDEEEGEGEEEEIGDEDTDDESEHDSSTRGN
The following text describes a protein:
Function:
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Subcellular Localization:
Cytoplasm.
Sequence:
MEKKETKSESEKTNKQDNKNTKSQKKENLNLVNSDKKIAELENEISNLKDLYLRKQAEFENFRKRLEKEKDNFVKFANETIMKDVVNFLDNLERAINSSKKSKDFDNLLTGISMIENEILSIFDKKYNLKKFGENGENFDPSRHEAISIEEKEGLKNPEIVEVYQKGYCYNDRILRTAKVKVAQSKN
The following text describes a protein:
Function:
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Miscellaneous:
MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSDPLQQVCDLIKGDLSLERVRDIKEQLLKEKSVVEYQLNKESDKYYGEVEESLKLLNLSKNSVTSIKQQINEVNKLGNDNRFAINRYDILFRATKLYETVNTTSSIYDRIYNFVALMEHIERLLVAELAEDALETGCPHLLEIHFLLTSARDFQEQVVVMAKEATEDAQRTVMKLFSRLSGIISKFDKLLDGLTYDIVEMARAEQISLAIRLFKIYDLEEREDLRIEAIRNIIKKKEIEIEKSSIKKLPNSKNTARLQDETPKVIEYPTNKGLYQEIMSGTISTRTAPRGYKHFLINGINNSISEMFGEMREKYVGDQKFDVLDNMDWIFNELIIVKEHIANCCPPHWNIFEVYFDQYYKELHSLITDLVESEPETIIILDILAFDKTFQDTLKQDFGFTKSEVKSVIGDKEKETLFKDYLNLIVVKMTEWIGNLEKAEFDVFLERSTPPHSDSDGLLFLDGTKTCFQMFTQQVEVAAGTNQAKILVGVVERFSDLLTKRQKNWISKISEEIKKQINYNHKYDIDPESITPEDECPGGLVEYLIAVSNDQMKAADYAVAISSKYGKLVSKVYEKQITNHLEGTLDGFAEVAQCSSLGLITLMFDDLRKPYQEIFSKTWYMGSQAQQIADTLDEYLLDIKPQMNSVLFVNFIDNVIGETIIKFLTALSFEHSFKNKNNKFLEAMKRDFEIFYQLFVKVLDGNESKDTLITQNFTVMEFFMDLSCEPIDSILDIWQKYLEVYWDSRIDLLVGILKCRKDVSSSERKKIVQQATEMLHEYRRNMEANGVDREPTLMRRFVLEFEKQ
The following text describes a protein:
Function:
May play a role in the immune response.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MGALLWSLLLLLQEAKGFSGDDEDPEEVIGVLQESINLSLEIPSNEEIKHIDWLFQNNIAIVKPGKKGQPAVIMAVDPRYRGRVSISESSYSLHISNLTWEDSGLYNAQVNLKTSESHITKSYHLRVYRRLSKPHITVNSNISEEGVCNISLTCSIERAGMDVTYIWLSSQDSTNTSHEGSVLSTSWRPGDKAPSYTCRVSNPVSNISSRRISVGSFCADPGYPEKPSMLCLLVKSLFLLLLLAILTVGLCLFRAQKSYETPRVRKLKRNRIKLRKKGKSGPTPV
The following text describes a protein:
Function:
In complex with CCZ1, is required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis. The MON1-CCZ1 complex acts at the fusion of vesicles with the vacuole, through its regulation of the SNARE complex during the coordinated priming and docking stages of fusion, and particularly at the stage of tethering/docking.
Subcellular Localization:
Endosome, multivesicular body membrane; Peripheral membrane protein. Prevacuolar compartment membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein.
Sequence:
MTSESEPNTSLPFSPIQQTLPATPSRSTSQVSMVSAEALLSHSSPTKQLTPSHRSSLPSALPYNTLLNAPAGSPALRARASTASSSRAPSVLDDARVEHNDSETQVLEITPPMDNYELDGGSDHTSLPSDASSIKGKEKQRSNDRNEIETVGAGGEMALPSGDARKGLKELVRRSTTADKGYGGHDHRRLSEKLSQNENLQILITQSDKMSYSPRLYYVLTNAGKPVFCSHTRPSEDDVTNLMGVAQALISIFADDDDRLRYIIKGNHRVAFLLKAPLYLFCVSDWGEPEHVLRLQLEYIHLQILSVVSSTQLLRLFQRRSNADLSTLLEGTEPFLSNLIDCSQYDFSFLTSTLQPLRMAPALRDTSAAALMPPSKFKDLLYVLLIAGGHIVTVLRPRKHSIHPSDLHLLLNTIASSSALRTTETWLPICFPKFNPSGFVHAYISYVLEDVGLVFVSADREAFEDLRVWKDMVLEKLEQDKTLSRIQEAIPLHPYTISSVGCPGLRHFIYKSRQHVQITQPIWEAPYEDGSTNQKRLVTTYQKLHDAVHAKSGQASALKLVYISTEHEACLVWATKPFELYITVSPQLSKSAVVAAANNVAKWVLAEEGRIFLKDAPVF
The following text describes a protein:
Function:
Guanine nucleotide exchange factor for Arf6. Regulates axon growth and branching by inhibiting microtubule polymerisation at the cortex. Together with shot, promotes axonal microtubule bundle integrity. Required for normal ethanol-induced tolerance and preference. Probably by activating Arf6, counteracts ethanol-induced sedation.
Subcellular Localization:
Cell projection, axon. Cytoplasm. Cell membrane; Peripheral membrane protein. Cytoplasm, cell cortex.
Sequence:
MSEELKVVLRRSEQHSGFGFSLLGTTGPPHVIYDIVENSPAADCGAVEAGDVILKVNGTDVHRYTTKEVLKCLRLSEQLVTLELKRDPKLKARIKEQLANTQSPHYVDIESPNIYDYHSSSTNSSPNHRPNAGGKGAATTPSQTGLRYKSPTHLPSLRQNSSPLLASGSTTTTTTATHTHSHSRNSSASSTKIKVVETSITTSTTNVVGLTSPTGSVGGGVGGEATSPTFRPSRIPQALTKCAVPKPVPVLHSPQNKRPRPSQIPTKAANGNGNGHTAHLPPQSLQHSNSYSGSPVTRQRFADREPEREPEPNSAPPQPAKAPRFEAYMMTGDLILNLSRTPQTSNPLPAQAKKIDSLRDSPSRLVNPRINGALAPRASGESSPTSSSSVDSPTNTSSDSVKREAKLLQKQQQQQQQTYQQQQQRDSINNSYNRKDSLTNDTLLMCEELEPDEEGEYVLEEDNKQQRQRQQQQRYRQQQNQQRYEYYQNEDELEEQEEVEEEREEDQTHYDITNIETYQSGVGRGDDDDSDRQCLVDDDDDDDAYDDEENDAGDEDYSTNSLGSGSAKQRLRALKQRTATRQQQRNRDAVDCAGRSGSGSSSTTVKSEAGGLGLDETSFSVPTSPISLSTPLIDKETANSVPTSPEPSSLVPESSSGAGAGAVVVRRHNGHVVRKCDAAGFRTSKSEDHLQQIQREGIAAVIPIDIDEDVNSSLNTLLDTRQDSEDSQSMATVIVNNSSLASNNNEGEQTDNRSSSSSSNSSDNNNCSSNTGEPATSETATATATIITATSTRTMNCSSKLNYILCKKASDRDRIVWTYNAPLQPHQLAALQRQQQQQEQQFQQQQQQLHQQHLQQQQQLQQQHQQQQQQQQQQQQQQLYGQQSHSNSHSSSISSSPQHSAVGSPASPTSVSSSVMSSSGSKGALGLGSSSNGPMAAVQQQQLREREQGGQVAQPPSGIPGLLSCPGGGCGNNGGGGGIGGGGNNDQSVSEAISNISSPDYQDDDNLLSSRDILGGMVLSDPSDSDSTILVSDAAAHQRQQLKQQLRAQQQQQRERERDRDRDREQSEHKVVIQVRGLDSNSSGGNGTNGRSEEDVVTLTDEPLGTMTVGMRDASPPVSDDGSDVESLHSYHYSPKAVDMPSAIRLAKRLHSLDGFKKSDVSRHLSKNNDFSRAVADEYLKHFTFEKKSLDQALREFLQQFSLSGETQERERVLVHFSKRFLDCNPGTFNSQDAVHTLTCAIMLLNTDLHGQNINRKMSCAEFVDNLADLNDGENFPKDVLKSLYQAIKTKPLEWALDEEAGDLQQQRANNSALGNVGLNPFLDPPELATAVEYKKGYVMRKCCYDSSFKKTPFGKRSWKMFYCTLRDLVLYLHKDEHGFRKSQMSDNLHNAIRIHHALATKANDYTKKQHVFRLQTADQAEYLFQTSDSKELQSWVETINYVCAAISAPPLEGGVGSQKRFQRPLLPSKQSKLMLKEQLDSHEVQLAQLDQELNEHKKGPIPSKGLALQNYKEKESYLQYELRRYRTYVSILSAKMLADQQQLELQAQQPSPASHEEEADTFPVGTTACTPPTPQSINQKDQQKEQQQQQPTNRKEKKKK
The following text describes a protein:
Function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MDMVDRTSRRGYRDWFVQRITALLSGIYAVFVIVFLLVHHPISYPQWHALFSHLIMKIFTLIVIFSILWHAWIGMWTIFTDYVKNKPIRLALETLVCLLLVGYFVWAIEFLWIAR