lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Most effectively accelerate the intrinsic GTPase activity of YPT7. It is also active, but to a lesser extent, on YPT31, YPT32 and YPT1. YPT6 and SEC4 (By similarity).
Sequence:
MNSLWPVSVSHTQLTSINHQVYVHPTPSSKDNIPGFLALAKPRGATTDKEILVAWIPESKLQESAADFESYVKVDIKESGTPASSSLNLAETLVSPPPSSSFSSYAFSIPISDIFSLQVKQPSLGWWWGSITIHTRSKEDQLPPLYFHDAESQSTIMEQKRRNKKFETFDSESGSSMFWGGDHFIQVLSKYANLERAESDHSFLLVNPREGDAERFGTNLTGGSEEPSQLVAGIPGRGAGGDPVDRGAQVQKAFSDIRWGLLSNLAKVTQLTRKVSQGVWDSSPQPVKQLLMKPEVKKIGDDFDSARIYLAKWALSVAEESQRAKLKVLFDDELRELVSDEGFELIDAENNPQRRNEVSLAEWNAFFDYNGRLIVTVNEVKERIFHGGLAPAVRPEGWLFLLGVYPWDSTAAERKELVSKLRVDYNRLKKEWWVQEDKERDDFWRDQLSRIEKDVHRTDRNITFFAECDAKKDGDDDNYDKDEFGFSSQINSNIHLIQLRDMLITYNQHNKNLGYVQGMSDLLSPLYVVLQDDTLAFWAFSAFMERMERNYLRDQSGMRNQLLCLDHLVQFMLPSLYKHLEKTESTNLFFFFRMLLVWFKRELLWDDVLRLWEVLWTDYLSSQFVLFVCLAILDKHKDVMIDHLAGFDEILKYMNELSMTIDLDELLVRAELLFYRFRRTVELIDRKNEDRRNSADGSEPVSITEDLRELLSRKVIVVREGERPEGVMGG
The following text describes a protein:
Function:
Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity.
Subcellular Localization:
Nucleus.
Sequence:
MKCIIPGNNVKVFGRAIHCLSKVGEDLYMEPLDTGLALRAVNSSRSAYSCFLFSPSFFLRYDDQTVTASQATQDGEETTRWRVTMKSCLAVFKSLSNLEKNVDRCNISLDTEDCRLVFQLHCRHGIVKTYNLVYQETETLQAVFSKDLCPNRITAPAKLLAEAVGSFQSSQEEVTMTVTPTQLGYKNYVDDEPDPTKVVHSELRLVPDEFTEYMIGVDTEVTFSLRDLRAILSFSDSAGLPVSIHFETPGKPIVFSVESEQTLEATFVLATLTEVSSSQLTGASQQARASQAASVSANPRQKSKSNPRKRSTAGPGPRKNKPSNNGDGRRTPNGHTTRDEYEDEFPDDLMADLLNRNERTMNQGNNTAAGPSTSSSRLDPAAPTTSNNDDTPFTASPVIPFNSALSHRFQKTVTDQSRHDDRLHPPPQPAEEEGEGERRVSPNRTLLANFMDDEDSRGSLGDVDGPSLLGDEGGGGGDDGKIDDEDDDDDDDGFNFIPATPPSKKFKSMFFGASQSQQSGSGTQRSRPPPSQPHRGGAVTVLAEDSDED
The following text describes a protein:
Function:
Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of glycosphingolipids forming gangliosides (important molecules involved in the regulation of multiple cellular processes, including cell proliferation and differentiation, apoptosis, embryogenesis, development, and oncogenesis). Mainly involved in the biosynthesis of ganglioside GM3 but can also use different glycolipids as substrate acceptors such as D-galactosylceramide (GalCer), asialo-GM2 (GA2) and asialo-GM1 (GA1), although less preferentially than beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer (LacCer).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MNVRIVRTTLLFGSMVFTMGFIMNTVISDRTKEYQRTVDKLRNLNTIKKRILEGRVLQVTPASGQEYIFSNKSIIDRKVSPKDRKVTPKSIIREDEVKTCQPKRAADRMENLFGGQFNRSLSPFATLSSIRSANSTKYPLPFGFHGTERTASDVVGKLPDTDIPADIKKLPCRRCIVIGNGGLLKGSKLGSHIDQYDAVFRLNIAPIKGYESDVGTKTTIRAVYPESSNIGSKAYTQNWTLLVVPFKANDLKWLDTIIEGRDLKKLKGFWSTTVDFVPKPRKDLRLYNPEITSELSFNLIGMKSGKGSKNVPTTGAMVIMVAIRVCDEVSVAGFGYDMKRLDTPIHYYSSQKTKAILSSFTHDIDHETKFLHKLVEQGVINDITGGLRTKL
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are usually held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis; this sigma factor does not seem to have a cognate anti-sigma factor however. It has been suggested that the sigma domains 2 and 4 may interact via polar residues in this protein to autoregulate. Positively regulates expression of a small regulon of genes.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Domain:
The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 mediates interaction with the RNA polymerase subunits RpoB and RpoC (By similarity); The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA. The domain also mediates interaction with the RNA polymerase subunit RpoA (By similarity).
Sequence:
MTATASDDEAVTALALSAAKGNGRALEAFIKATQQDVWRFVAYLSDVGSADDLTQETFLRAIGAIPRFSARSSARTWLLAIARHVVADHIRHVRSRPRTTRGARPEHLIDGDRHARGFEDLVEVTTMIADLTTDQREALLLTQLLGLSYADAAAVCGCPVGTIRSRVARARDALLADAEPDDLTG
The following text describes a protein:
Function:
Probably blocks the subsequent transfer of the phage DNA across the inner membrane into the cytoplasm. By this means, P22 excludes superinfection by the phages of the same family and also against DNA coming from oter phages.
Subcellular Localization:
Host cell inner membrane; Multi-pass membrane protein.
Sequence:
MSDSMSYAVLVAATLFLGIGLQIAWLFFSNFIKRKRLESRISEVSIAIGKNAKNPENEAYVLNYLKEKFSPERFENRITDALGLIISVIHIPLSLLITVWYFAMIAGRIFGFMNIEPVVLWVPMILQLLLSIAIFIFSVFIKIVFGRYPGEANGFNKEFIKTIK
The following text describes a protein:
Function:
G-protein coupled receptor for medium and long chain saturated and unsaturated fatty acids that plays an important role in glucose homeostasis. Fatty acid binding increases glucose-stimulated insulin secretion, and may also enhance the secretion of glucagon-like peptide 1 (GLP-1). May also play a role in bone homeostasis; receptor signaling activates pathways that inhibit osteoclast differentiation. Ligand binding leads to a conformation change that triggers signaling via G-proteins that activate phospholipase C, leading to an increase of the intracellular calcium concentration. Seems to act through a G(q) and G(i)-mediated pathway. Mediates the anti-inflammatory effects of omega-3 polyunsaturated fatty acids (PUFAs) via inhibition of NLRP3 inflammasome activation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKTNVLGSTYTLIPDAMGAWKIISLVVYGTTFLLGLPSNVLALYVIYCRAKVRVTPNLIYMINLCISDLVFVLILPLKMLAVGKGNWALPGFFCALYNLIHFGTIYASVCFLTVVGVGRFLGVVFPIQYQIYKKPCYSCLVSLVIWTIVGFHGILLFVLESTKDLSPRLFADDTLTCYSNFTEEQMTLLLPIRLELSVVLFFLPLAITFFCYAACIWVLVGSHLHVQKKRRAVRVAVATLSVFVLCFGPYNISHVVGFVLRRDLWWRSVALLPSACNAFLDPLVFYFLSTAVDDGIIQVWQSLKGKCSSLRMKISLTHGKQGNQQKALSIA
The following text describes a protein:
Function:
TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Miscellaneous:
MISCELLANEOUS: Seems to bind calcium.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Domain:
Shows a remarkable charge distribution with the N-terminus being highly negatively charged, and the cytoplasmic C-terminus positively charged.
Sequence:
MNKLITLLLAVLMIISCVYSDDVEITDDEVVQATPTSDVSFSYIFPDNQDKNFAAGSVVEVLVGFTNNADKALNITHIFASLNHPQDFSVFIQNYTRGDFGIAVEKGHHATLAYRFVPSEYLEPREFGLLISLEYQDGAQNFTQTFFNSTINITEKETSFDMDSFFLILLGLGFVGGIGYIVYGKMPKQKKVRTVSKVNKNAVRVETEDETAEWLSGTSAASSKVKSVQKVVKKNK
The following text describes a protein:
Function:
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MIKASKCNKPRALFLVRVSIPRTFIRNATSAVPTTIKLNDLASLPPITKSLPTNLPFLMPDTLQSLLRFDSEKEKQPSTDKSNDKDKPSRKEKGKDKEKENEEKKDINMDEKYEINEETDTKPTIDPNNPVSSKSNISSSSGGDNNNNNNNNNNNNDSDGKNDDGSPKDKEFLSPSDSGLHPPFLAIAMKDRPFLPGATRHLHVSDPEVIKCVNHMINSNIKSPYFVLFHVRDTNSEDAALDVIKDRDFVHEVGTLCQIIKTTGSEILVYPHYRVKLVDISTPNSRSESIEKEQDNSQTSYLKKFEVSYAVTQQLKDEPYDEQSITINAWTRRIKELYEKLAPKYDQPENKEEIMSNPSMLADFIASKVHAKPEQIQEILESSNVETKLELSLQLLQVEADADEMRQTALKNIRERTEKAYAQSLIKEYTKELLKAAGIGENSKVHKFDERIKHLKMPEEAMKAYKTEKERLGTQSDMEQNVVERYLDWLTQIPFGVYTKDSFNVKKAREILDRDHYGLKDVKDRILEFISVGKISGNVDGKILCLAGPPGTGKTSIAKSIAEALNRKYTRIAVGGVQDVHDVKGHRRTYVASIPGRIVTALTQAKTSNPLMLIDEIDKLDTTSHGGAARAFLEILDPEQNNSFVDNFIEVKVDLSKVLFVCTANYLGSIPGPLRDRMEIIEVNGYTKNDKIEITKRHLIPAAAKKVGLDEGRVVIPDETISRLIDKYCRESGLRHIKSLINRIFSKASRKIVEELEETDVDSHNKDTVEGTLVAKESEKVISDKAKIDTENSPIEYIQSNTEVKAETTTESQQEQEKEKEKDEEIKKLDLPADLKIEVKPETLKDFVGPEIYIKDRLYETLNPGVATGLAYNTSGDGDALYIESILTDSISSDLGNAGLHVTGSLKDVMKESASIAYSFAKQFMVRQFPDNRFFEAAHIHVHCPGGAIPKDGPSAGIAFTSSLVSLALNKSLPNDTAMTGEITLTGKVLAIGGLREKSLGAKRAGYTKIIFPKDCEYQLDEIPDEVKEGLTYIPVEWYSEVFEHLFQGISKEEGNSVWKEEFAKLEDKKKSKKTNTK
The following text describes a protein:
Function:
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate (By similarity). Plays an important role in maintenance of endomembrane homeostasis including endocytosis, vacuole formation, and vacuolar acidification processes. Required for development of viable pollen. Might mediate recycling of auxin transporters.
Miscellaneous:
MISCELLANEOUS: [Isoform 1]: A number of isoforms are produced. According to EST sequences.
Subcellular Localization:
Endosome membrane; Peripheral membrane protein.
Sequence:
MDSQDHKAPGFVDIVKSWIPRKSESSNMSRDFWMPDQSCPVCYECDAQFTVFNRRHHCRLCGRVFCAKCAANSIPSPSDETKDSHEEPERIRVCNYCYKQWEQGIVPPDNGASIISLHFSSSPSARSVASTTSNSSNCTIDSTAGPSPRPKMNPRASRRVSSNMDSEKSEQQNAKSRRSSDHYGHVLDSSDNQVEFFVNSSGRSDGEADDDDDYQSDFAQSYAQGNDYYGAINLDEVDHIYGSHEAHDVGVKIEPNISGFPPDQDLDSLNTETIDKTRQQENGWNDVKEGSPPCEESFEPEVVDFESDGLLWLPPEPENEEDEREAVLSDDDGDEGDRGDWGYLRPSNSFNEKDFHSKDKSSGAMKNVVEGHFRALVAQLLEVDNLPMVNEGDEEGWLDIITSLSWEAATLLKPDTSKSGGMDPGGYVKVKCIPCGRRSESMVVKGVVCKKNVAHRRMTSKIEKPRLLILGGALEYQRISNQLSSFDTLLQQEMDHLKMAVAKIDSHNPDILLVEKSVSRFAQEYLLAKDISLVLNIKRSLLERISRCTGAQIVPSIDQLTSPKLGYCDLFHVEKFVETHVSPCQVAKKMAKTLMFFDGCPKPLGCTILLKGAHEDELKKVKHVIQYGVFAAYHLALETSFLADEGASIHELPLQTPITVALPDKPSMVNRSISTIPGFTVSSAEKSPTTELRGEPHKANGDLTGNFTSSKTHFQGKLDGNDRIDPSERLLHNLDTVYCKPPETITSKDDGLVPTLESRQLSFHVEEPSVQKDQWSVLSGATEQVTDGGYTNDSAVIGNQNFNRQEQMESSKGDFHPSASDHQSILVSLSTRCVWKGSVCERAHLLRIKYYGSFDKPLGRFLRDNLFDQDQCCPSCTMPAEAHIHCYTHRQGSLTISVKKLPELLPGQREGKIWMWHRCLKCPRINGFPPATRRIVMSDAAWGLSFGKFLELSFSNHAAASRVANCGHSLHRDCLRFYGFGRMVACFRYASINIYAVTLPPAKLYFNYENQEWLQKESKEVIKKAEVLFNEVQEALSQISAKTMGAGSKGSTPNKIKLSLEELAGLLEQRKKEYKDSLQQMLNVVKDGQPTIDILLINKLRRLIIFDSYAWDECLAGAANMVRNNYLEAPKNSAPKVMGRNVSLEKLSDEKVKSIPTHVAICNDSLLQDADYETCLNQGKSFADTSGKFAIPEDVGSDRPPDCRMEFDPSEGGKDNFVESSQVVKPAHTESQFQATDLSDTLDAAWIGEQTTSENGIFRPPSRAASTNGTQIPDLRLLGSESELNFKGGPTNDEHTTQVQLPSPSFYYSLNKNYSLNSRKHIMAEDRPVYVSSYRELEWRSGARLLLPLGCNDLVLPVYDDEPTSIIAYALTSSEYKAQMSGSDKSRDRLDSGGSFSLFDSVNLLSLNSLSDLSVDMSRSLSSADEQVSQLLHSSLYLKDLHARISFTDEGPPGKVKYSVTCYYAKEFEALRMICCPSETDFIRSLGRCRKWGAQGGKSNVFFAKSLDDRFIIKQVTKTELESFIKFGPAYFKYLTESISTKSPTSLAKILGIYQVSSKHLKGGKEFKMDVLVMENLLFKRNFTRLYDLKGSTRARYNPDTSGSNTVLLDQNLVEAMPTSPIFVGSKAKRLLERAVWNDTSFLASIHVMDYSLLVGVDEERNELVLGIIDFMRQYTWDKHLETWVKTSGLLGGPKNSTPTVISPQQYKKRFRKAMTAYFLMVPDQWSPAAVVPSNSSSAEVKEEEEKDNPQAVGNKS
The following text describes a protein:
Function:
Transcription factor involved in X-chromosome dosage compensation in males, the process by which transcription of the single X chromosome in the male is elevated. Binds to the DNA sequence (GA)n. Clamp-binding promotes nucleosome depletion and chromatin accessibility, thereby allowing access to other transcription factors. Specifically binds to cis-acting elements on the X-chromosome named chromatin entry sites and promotes recruitment of the male-specific lethal (MSL) histone acetyltransferase complex, which associates with actively transcribed genes on the male X-chromosome to upregulate their expression. Mechanistically, acts by promoting chromatin accessibility at chromatin entry sites, facilitating DNA-binding of msl-2, followed by MSL complex recruitment. In addition to dosage compensation, also involved in zygotic genome activation (ZGA), a critical event in early embryonic development during which the developmental control passes from maternally provided mRNAs to the expression of the zygotic genome after fertilization. Maternally-provided protein cooperates with Zelda (zld) to activate zygotic transcription by increasing chromatin accessibility at promoters of specific genes and facilitate zld occupancy at a subset of key embryonic promoters. Also acts as an activator of gypsy chromatin insulator function by promoting binding of Cp190 to chromatin.
Subcellular Localization:
Nucleus. Chromosome. Note=Enriched at X-chromosome MSL-response elements (MREs) compared with autosomal MREs. On polytene chromosomes, localizes to many sites throughout the genomes of both males and females.
Sequence:
MEDLTKNIIFTNAINGQPATIQYQTADGTILKQPKIEGQKTEQQPTFYYTTNGNGGTVNLAQLATTDDNKTCYIAQPVGGYNYALVNGMPLNQGAALGIATVDAQGRIQIVNQNKPIAANTISNISFKCDVCSDMFPHLALLNAHKRMHTDGEQQQQQQHNAQAGGDSIAVVSAQGLVQAQNIIGNGQMGQIQIVSSDTLEPVQQSVMQQQQHESKASKCINCGSSMLQQSKRKGPKQVRCESCMQAEQTAQQQQQLFVAQDGQMAHPVQIISTTPQAQAQLQQIVAAQTGGTTPKREASSGSGHHPVKKRNSQQMTKCQKCNGSGVVLVGQHSHASHSGVGGSVKQSVTVKTENPSKPFSCNICGGLFSRYSSLWSHKKLHSGEKNYKCSICGLAFAKAVYLKNHARIHTGEKPYKCQTCGMQFSQSPHLKNHERTHSGERPYVCGVCDKGFARHATLWNHRRIHTGEKPYKCEICGSAFSQAAHLKNHAKVHSGEKPYKCEICSAAFADRFALKRHRGIHQKYGQTAPRQTSSDGMIVHKQEIPDMEDEAQQEVIIGGL
The following text describes a protein:
Function:
Cell surface proteoglycan that bears heparan sulfate. May fulfill a function related to the motile behaviors of developing neurons (By similarity).
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side; [Secreted glypican-2]: Secreted, extracellular space.
Sequence:
MSALRPLLLLLLPLCPGPGPGPGSEAKVTRSCAETRQVLGARGYSLNLIPPALISGEHLRVCPQEYTCCSSETEQRLIRETEATFRGLVEDSGSFLVHTLAARHRKFDEFFLEMLSVAQHSLTQLFSHSYGRLYAQHALIFNGLFSRLRDFYGESGEGLDDTLADFWAQLLERVFPLLHPQYSFPPDYLLCLSRLASSTDGSLQPFGDSPRRLRLQITRTLVAARAFVQGLETGRNVVSEALKVPVSEGCSQALMRLIGCPLCRGVPSLMPCQGFCLNVVRGCLSSRGLEPDWGNYLDGLLILADKLQGPFSFELTAESIGVKISEGLMYLQENSAKVSAQVFQECGPPDPVPARNRRAPPPREEAGRLWSMVTEEERPTTAAGTNLHRLVWELRERLARMRGFWARLSLTVCGDSRMAADASLEAAPCWTGAGRGRYLPPVVGGSPAEQVNNPELKVDASGPDVPTRRRRLQLRAATARMKTAALGHDLDGQDADEDASGSGGGQQYADDWMAGAVAPPARPPRPPYPPRRDGSGGKGGGGSARYNQGRSRSGGASIGFHTQTILILSLSALALLGPR
The following text describes a protein:
Function:
Essential factor involved in transcription-coupled nucleotide excision repair (TCR) which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes. Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA. It is required for transcription-coupled repair complex formation.
Subcellular Localization:
Nucleus.
Sequence:
MGLGKTIQVLSFLGSLHFSEMYKPSIIICPVTLLRQWKREAKTWCPSFHVEILHDSAHDLSSKKKQSDSESDYESEDLLDSETEGKKSSRTSKKWDPVIARVVRSNSGLLITTYEQLRLLGEKLLDIEWGYAVLDEGHRIRNPNAEVTLVCKQLQTVHRIIMTGAPIQNKLSELWSLFDFVFPGKLGVLPVFEAEFAVPISVGGYANATPLQVSTAYRCAVVLRDLIMPYLLRRMKADVNANLPKKAEHVLFCSLTKEQRSVYRAFLASSEVEQIFDGSRNSLSGIDVMRKICNHPDLLEREHSSTDPDYGNPERSGKMKVVAEVLKVWKEQGHRVLLFSQTQQMLDILERFLVTCEYNYRRMDGVTPVKQRMVLIDEFNNTDDIFIFILTTKVGGLGTNLTGANRVIIFDPDWNPSTDMQARERAWRIGQKKDVTVYRLITRGTIEEKVYHRQIYKHFLTNKILKNPQQRRFFKARDMKDLFTLNDDGNGGSTETSSIFSQVSVDVNIVGAPDSQERLSFQAPVAKDDNSKIGEADNSDPKGKAGDDNNNGELDEETSILRGLFDAHGIHSAMNHDAIMNAHDEEKLKLEEQASQVAQRAAEALRQSRMLRSREGVAVPTWTGKSGAAGGPSSAKKKFGSTVNPQLTSKSSEESLNGYDAIRGNAFPAGASAGKALSSAELLAKIRGNQEKAVSDGLVHQFGTPASTSNSRAGSVSNGNRSASSSSVVQPEVLVRQICTFIQQRGGKTTSASIVDYFRDRIPSKDLPLFKNLLKEIAILEKNPSGSFWVLKPEYQDQ
The following text describes a protein:
Function:
Involved in centrosome attachment to the nucleus. Required for zyg-12 localization to the nuclear envelope. Together with pot-1, it is required to anchor telomeres to the nuclear envelope in embryos.
Subcellular Localization:
Nucleus membrane; Single-pass membrane protein. Nucleus envelope.
Domain:
The SUN domain may play a role in nuclear anchoring.
Sequence:
MALRHTISPQFSNRHSPPVTRSVSRTGVHQPLDTSTPVTRRDSQPGTITGTIQRFHESADDSEIDLNSSKFIYKEHFSYKEITSMKKEMWYDWLEYRIRMVRRRFVPTWAQFKRTLMAVVLFAMLYKYARDCLFDGTHHNSEGSYADKDANWASEKQKFHQTISNLRAEFSAHDKQLDFKTDHLEKLLENVLEHSKGWKESAIEELKQIKLWQAEISDALQQMKKEIDDAKSTKIIHSTPEKAPETAPTASLPPSSQLQPMHITRRALLGVNVANSLIGASIDHSCSSRPVSAKDGFFYDFMSYFGTFQEGYALLDRDVLSPGEAWCTYDKRATLTVKLARFVIPKSVSYQHVRWSGIVPNHAPKLYDVVACTDSCCTKWQPLVANCEYKERDGSYDEQEQFCSVPTIQNHSPINHVQFRFRENHGDMPKTCAYLIRVYGEPVDPPKETQPMTDNGTESKLESAIVNSVSETA
The following text describes a protein:
Function:
Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Also binds to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity.
Subcellular Localization:
Secreted.
Sequence:
MGTLLWLLAFFILGVQAWDTPTIISRKEWGARPLACRALLTLPVAYIITDQLPGMQCQQQSVCSQMLRGLQSHSVYTVGWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQGYNNISLGIAFFGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLLLKEETCLDPQHPVMPRKVCPNIIKRSAWEARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDIGYHFLVGQDGGVYEGVGWHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAALEVAQDLIQCAVVEGYLTPNYLLMGHSDVVNILSPGQALYNIISTWPHFKH
The following text describes a protein:
Function:
GTPase involved in ribosome biogenesis (Probable). Binds to 23S rRNA and associates with 60S pre-ribosomes. Involved in early cotyledon and leaf development.
Subcellular Localization:
Cytoplasm. Nucleus. Note=The C-terminus is sufficient for the targeting into the nucleus.
Domain:
In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern; The DARXP motif is also sometime designated as G6 region.
Sequence:
MGKSEKTSLGRSLVKHHNHMIQESKDKGKYYKNLQKKVLESVTEVSDIDAIIEQAEEAERLYTINHSSSTPLSINLDTNSSSSVIAAEEWREQQKIEEALHASSLQVPRRPPWTPEMSVEELDANEKQAFLNWRRMLVSLEENEKLVLTPFEKNLDIWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKIMLLVNKADLLPTDVREKWAEYFRLNNILFVFWSAIAATATLEGKVLKEQWRQPDNLQKTDDPDIMIYGRDELLSRLQFEAQEIVKVRNSRAASVSSQSWTGEYQRDQAVVGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKHFQTLIISDELMLCDCPGLVFPSFSSSRYEMIASGVLPIDRMTEHREAIQVVADKVPRRVIESVYNISLPKPKTYERQSRPPHAAELLKSYCASRGYVASSGLPDETKAARLILKDYIGGKLPHYAMPPGMPQADEPDIEDTQELEDILEGSESDDSAVGDETENEQVPGIDDVLDDLSSFDLANGLKSSKKVTAKKQTASHKQHKKPQRKKDRTWRVQNTEDGDGMPSVKVFQKPANTGPLTMR
The following text describes a protein:
Function:
Pleiotropic ABC efflux transporter involved in the protection of the cells against a wide range of toxic compounds. Confers resistance to the azole fenarimol via efflux transport. May also be involved in the secretion of penicillin.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSPLETNPLSPETAMREPAETSTTEEQASTPHAADEKKILSDLSAPSSTTATPADKEHRPKSSSSNNAVSVNEVDALIAHLPEDERQVLKTQLEEIKVNISFFGLWRYATKMDILIMVISTICAIAAGAALPLFTAPSTFQRIMLYQISYDEFYDELTKNVLYFVYLGIGEFVTVYVSTVGFIYTGEHATQKIREYYLESILRQNIGYFDKLGAGEVTTRITADTNLIQDGISEKVGLTLTALATFVTAFIIAYVKYWKLALICSSTIVALVLTMGGGSQFIIKYSKKSLDSYGAGGTVAEEVISSIRNATAFGTQDKLAKQYEVHLDEAEKWGTKNQIVMGFMIGAMFGLMYSNYGLGFWMGSRFLVDGAVDVGDILTVLMAILIGSFSLGNVSPNAQAFTNAVAAAAKIFGTIDRQSPLDPYSNEGKTLDHFEGHIELRNVKHIYPSRPEVTVMEDVSLSMPAGKTTALVGPSGSGKSTVVGLVERFYMPVRGTVLLDGHDIKDLNLRWLRQQISLVSQEPVLFGTTIYKNIRHGLIGTKYENESEDKVRELIENAAKMANAHDFITALPEGYETNVGQRGFLLSGGQKQRIAIARAVVSDPKILLLDEATSALDTKSEGVVQAALERAAEGRTTIVIAHRLSTIKTAHNIVVLVNGKIAEQGTHDELVDRGGAYRKLVEAQRINEQKEADALEDADAEDLTNADIAKIKTASSASSDLDGKPTTIDRTGTHKSVSSAILSKRPPETTPKYSLWTLLKFVASFNRPEIPYMLIGLVFSVLAGGGQPTQAVLYAKAISTLSLPESQYSKLRHDADFWSLMFFVVGIIQFITQSTNGAAFAVCSERLIRRARSTAFRTILRQDIAFFDKEENSTGALTSFLSTETKHLSGVSGVTLGTILMTSTTLGAAIIIALAIGWKLALVCISVVPVLLACGFYRFYMLAQFQSRSKLAYEGSANFACEATSSIRTVASLTRERDVWEIYHAQLDAQGRTSLISVLRSSLLYASSQALVFFCVALGFWYGGTLLGHHEYDIFRFFVCFSEILFGAQSAGTVFSFAPDMGKAKNAAAEFRRLFDRKPQIDNWSEEGEKLETVEGEIEFRNVHFRYPTRPEQPVLRGLDLTVKPGQYVALVGPSGCGKSTTIALLERFYDAIAGSILVDGKDISKLNINSYRSFLSLVSQEPTLYQGTIKENILLGIVEDDVPEEFLIKACKDANIYDFIMSLPEGFNTVVGSKGGMLSGGQKQRVAIARALLRDPKILLLDEATSALDSESEKVVQAALDAAARGRTTIAVAHRLSTIQKADVIYVFDQGKIVESGTHSELVQKKGRYYELVNLQSLGKGH
The following text describes a protein:
Function:
Heterodimers with Gyc-89Da and Gyc-89Db are activated in response to changing oxygen concentrations, alerting flies to hypoxic environments. Under normal oxygen concentrations, oxygen binds to the heme group and results in low levels of guanylyl cyclase activity. When exposed to reduced oxygen concentrations, the oxygen dissociates from the heme group resulting in activation of the enzyme.
Miscellaneous:
MISCELLANEOUS: There are two types of guanylate cyclases: soluble forms and membrane-associated receptor forms.
Subcellular Localization:
Cytoplasm.
Sequence:
MYGMLYESVQHYVQEEYGVDIWRKVCHIIDCKHNSFKTHQIYPDKLMPDIAEALSACTGESFDFCMNFFGRCFVRFFSNFGYDKMIRSTGRYFCDFLQSIDNIHLIMRFTYPKMKSPSMQLTNMDDNGAVILYRSSRTGMSKYLIGQMTEVAREFYGLEIKAYVIESQNDISGGTAGPIKLTDGPLTVIVKYRLDFDNREYMAKRVNTEAHPSQLKMPTVKLDVFLDLFPFTFVLNHDMKITHAGEKIVETWIMHNPGANPKSFIGTHVMDLFQCRRPKDTTIDWDTLIQMRAVLFEFELIRTGHNRAAYDAVLNMDFENYDEMDLNEAQTMALAKAQEFSESHPVDDDESAREDEIDPATGERRSSQGLRSILLKGQMFYIKDVDSLIFLCSPLIENLDELHGIGLYLNDLNPHGLSRELVMAGWQHCSKLEIMFEKEEQRSDELEKSLELADSWKRQGDELLYSMIPRPIAERMRLSEEQVCQSFEEVSVIFLEVMNVYDEGLNSIQGAMQTVNTLNKVFSALDEEIISPFVYKVETVGMVYMAVSGAPDVNPLHAEHACDLALRVMKKFKAHDMGDVAIRVGINSGPVVAGVVGQKVPRYCLFGDTVNTASRMESSSDPWKIQLSKYTGDKVRQVGYKVESRGTVQVKGKGDMETYWLLEGPEG
The following text describes a protein:
Function:
Sugar transporter involved in the transport of UDP-galactose form the cytoplasm into the Golgi apparatus.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MKEEQTRSLFGISLSDKPTWQQFLICTSGFFFGYLVNGVCEEYVYNRLQFSFGWYFTFIQGFVYLFLIYLQGFTTKHIVNPMRTYVKLSAVLMGSHGLTKGSLAYLNYPAQIMFKSTKVLPVMIMGAFIPGLRRKYPVHEYISAFLLVLGLILFTLADAQMSPNFSMIGIMMITGALIMDAFLGNLQEAIFTMNPETTQMEMLFCSTVVGLPFLFVPMVLTGEVFRAWTACAQHPYVYGVLVFEAMATFIGQVSVLSLIALFGAATTALITTARKGVTLLLSYLIFTKPLTEQHGSGLLLIAMGIVLKMVPMDSKAPAKIPARPAVRIAGGDGDREEDEERKSLV
The following text describes a protein:
Function:
Plays a role in the recruitment of the exosome to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Nucleus.
Sequence:
MSEQAVEAFGSVEQTLAAVEEHLAVFKQTSMEDFVAPLSPLERAKVQVSLAYTINALLFVFLKTQGVSPKDIRQTHVKQELERVKAFIKKIKDAEELAKGPKLVLDKDASKRFIHNALSSDQVYVDAVNVKKDGESSKADTKTDASKIDGKGKRTASKSSGKKNKRQRKH
The following text describes a protein:
Function:
Subunit of the V0 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.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MDKHVAFMVITVFWLLFAIIGFLVSYRYEERGLIRCCVILTAVCCYLAWMVTFVMQLNPLTGPRAKQKIILGMITYWPRSIIHDEKDP