lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May have a specific role in modifying the cell-wall structure, specifically during seed germination, thus facilitating radicle protrusion.
Subcellular Localization:
Secreted, primary cell wall.
Sequence:
MRVPLIDFLRFLVLILSLSGASVAADATVKQNFNKYETDSGHAHPPPIYGAPPSYTTPPPPIYSPPIYPPPIQKPPTYSPPIYPPPIQKPPTPTYSPPIYPPPIQKPPTPTYSPPIYPPPIQKPPTPTYSPPIYPPPIQKPPTPSYSPPVKPPPVQMPPTPTYSPPIKPPPVHKPPTPTYSPPIKPPVHKPPTPIYSPPIKPPPVHKPPTPIYSPPIKPPPVHKPPTPTYSPPVKPPPVHKPPTPIYSPPIKPPPVHKPPTPIYSPPVKPPPVQTPPTPIYSPPVKPPPVHKPPTPTYSPPVKSPPVQKPPTPTYSPPIKPPPVQKPPTPTYSPPIKPPPVKPPTPIYSPPVKPPPVHKPPTPIYSPPVKPPPVHKPPTPIYSPPVKPPPIQKPPTPTYSPPIKPPPLQKPPTPTYSPPIKLPPVKPPTPIYSPPVKPPPVHKPPTPIYSPPVKPPPVHKPPTPTYSPPIKPPPVKPPTPTYSPPVQPPPVQKPPTPTYSPPVKPPPIQKPPTPTYSPPIKPPPVKPPTPTYSPPIKPPPVHKPPTPTYSPPIKPPPIHKPPTPTYSPPIKPPPVHKPPTPTYSPPIKPPPVHKPPTPTYSPPIKPPPVHKPPTPTYSPPIKPPPVHKPPTPTYSPPIKPPPVHKPPTPTYSPPIKPPPVQKPPTPTYSPPVKPPPVQLPPTPTYSPPVKPPPVQVPPTPTYSPPVKPPPVQVPPTPTYSPPIKPPPVQVPPTPTTPSPPQGGYGTPPPYAYLSHPIDIRN
The following text describes a protein:
Function:
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Gon7 likely plays a supporting role to the catalytic subunit pgp2 in the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators (By similarity).
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MNNLELTYKCETDTTRPFLKSLPVGFEPVEVDDYYISLKEQVRAMQDHCNEEFTKKMQTEGKNDVPEEKPIIL
The following text describes a protein:
Function:
Rhomboid-type serine protease that catalyzes intramembrane proteolysis. Required for correct root growth, floral development, fertility and photoprotection. May be involved in TIC22 processing during its import and in AOS accumulation in the chloroplast membrane.
Subcellular Localization:
Plastid, chloroplast membrane; Multi-pass membrane protein. Note=Localizes probably to the inner membrane.
Sequence:
MVSVSLSHHNLWPPESGSTAFRGFATAASVHACHHVSRHLRLDFHLRSSLKKLQHFSDDARMKFARYQRVFVFNGANFLKSRVDIRLSQSSPFVCFFNGGESRLNPRGGEEGSSNPETSKRNTVNGRRWTNVLLAINVIMYIAQIASDGKVLTWGAKINSLIERGQLWRLATASVLHANPMHLMINCYSLNSIGPTAESLGGPKRFLAVYLTSAVAKPILRVLGSAMSYWFNKAPSVGASGAIFGLVGSVAVFVIRHKQMVRGGNEDLMQIAQIIALNMAMGLMSRRIDNWGHIGGLLGGTAMTWLLGPQWKYEYTTRDGRRVFMDSAPIPLLLRWRNEQRRL
The following text describes a protein:
Function:
Component of the 39S subunit of mitochondrial ribosome. May have a function in the assembly/stability of nascent mitochondrial polypeptides exiting the ribosome.
Subcellular Localization:
Mitochondrion.
Sequence:
HYSGSPFSALHCFLRCNGVRPDEVAAARSPLPPGNGRPHSHPACSGSEEGISRRFPVPEGVRAVAPAPVPAAACTSEKPNWDYHAEIQAFGPRLQETFSLDLLKTAFVNSCYIKSEEAKRQKLGIEKEAVLLNLKDNQELSEQGTSFSQTCLTQFFEDAFPDLPTEGVKSLVDYLTGEEVVCHVARNLAVEQLTLSADFPVPPAVLRQTFFAVIGALLHSSGPERTSLFIRDFLITQMTGKELFEIWKIINPMGLLVQELKKRNISVPESRLTRQSGSTTALPVYFVGLYCDKKLIAEGPGETVLVAEEEAARVALRKLYGFTENRQPWDYSRPKEPMRAEKTIAAS
The following text describes a protein:
Function:
Plays a central role in chromosome cohesion during meiosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. May act by protecting centromeric rec8 from separase degradation during anaphase I.
Miscellaneous:
MISCELLANEOUS: 'Shugoshin' means 'guardian spirit' in Japanese.
Subcellular Localization:
Nucleus. Chromosome, centromere. Note=Localizes to the centromere. Bub1 is required for centromeric localization. At the onset of anaphase I, it is degraded.
Sequence:
MNFQFINSNINNEDKLPMESLKKKFLKQNREIIKINTQLSIKIRESENEIQDLIQENFTLKSYLVKLEARFRNQSQTEDLLKNFFPEIQTIHKKISQVQSLLKIIEKKCSSDFLEANVKSQFTTCENKDSKEDYQILHNKRLEYVSFNDELKSLETGQPLYCFQDFQKKVHGPPALSEKPGKCILKDKTNAHVNKIPQDEVNYSLPQKNITIFSKELKENEFESINEGETEEEKAKTSNVCVCIPCKSAEQITDLKGQATGDSSPCDFEESQPRINGREKLRRSVKVINYAIPSLRTKLRRDFDLPSDRKRKRHPRGKA
The following text describes a protein:
Function:
Regulator of short-term neuronal synaptic plasticity in the dentate gyrus. Associates with AMPA receptors (ionotropic glutamate receptors) in synaptic spines and promotes AMPA receptor desensitization at excitatory synapses.
Subcellular Localization:
Cell projection, dendritic spine membrane; Single-pass type I membrane protein.
Sequence:
MKGIRAIFYYFLVDLLTLLCWAQGKGGQHFGSTVVVSDVNLSNHGDQGSSEPPQTAEGCRGYFDVMGQWDPPFNCSSGEFLYCCGTCGFRYCCKFKQAKLDQNTCTNYDRPVWLQPGKTPPKIVDPAHDPTRDKTNLIVYIICGVVAVMVLVGIFTKLGLEKAHRPQRENMSRALADVMRQQGHCGTEHMERDTNLVVHVQHYETMPARSSANNLHSSKINNVVPTSPHLPQMAHPHSYPTMGQISNPYEQQPPGKELNKYASLKAVAEKGNDDFYSKRRHLAELAAKGSLPLHPVRVDKERSYSPEGGTLKVNGQKAKANKIHTHPLASTYNPDYKTWDHSEHSLRRQAYATKKHCPVESVNEPLQSQNQHFKHSQPYFVTNSKTEVTV
The following text describes a protein:
Function:
Forms serotonin (5-hydroxytryptamine/5-HT3)-activated cation-selective channel complexes, which when activated cause fast, depolarizing responses in neurons.
Subcellular Localization:
Postsynaptic cell membrane; Multi-pass membrane protein.
Sequence:
MFAFVKCKENLFTSLLLTLQDEKSQTVALQVLIRMSWRNELLSWNPSEFCGIDILNIPRSMVWIPDIAIKEDASDTGSVQEDPFLKLDPSGLLSGTSRQQLTYTCQLDLFRFPFDQQSCSLEFYSLSHNSRSLKLATTGNGTAFTIVSKKIKTTEGEWTLVELQVTEDAASTLQRVGSSLQYTVVLKRRPFLYIINLILPLMFLLFLDLASFFISESKLSFKVTVLLSVFVLLLNLQTILPSTEEHMPMLAIYCVSVFTLVFFGVLEAVLVSFLIEMDDSLREEAKGAVRAEVDNQPKAQRPTEPTEETDETEENQPDDQNLLKLILDKVQLTLLEVLRERQDKRKPGCFRKLAKLIDVVFFAIYLTTIIISLIVLFVIWIGK
The following text describes a protein:
Function:
Receptor which may mediate L-selectin-dependent lymphocyte rollings. Binds SELL in a calcium dependent manner. Binds lymphocyte.
Subcellular Localization:
Apical cell membrane; Single-pass type I membrane protein. Basolateral cell membrane; Single-pass type I membrane protein. Endosome, multivesicular body membrane; Single-pass type I membrane protein. Note=Exclusively localized on capillary endothelium. Transcytoses across the cytoplasm in the capillary endothelium.
Domain:
Ig-like V-type domain mediates binding to lymphocyte.
Sequence:
MRPLVLLWGCLVLPGYEALKGPKEISGFEGDTVSLRCTYVEKMKEHRKYWCRQGGILVSRCGDIVYANQDQEVTRGRMSIRDSPQELSMTVIMRDLTLKDSGKYWCGIDRLGRDESFEVTLIVFPGKRDNAVPAGTCCPSSPTPSFQPLTPTRSLQPKAKAWQTQLPEPRSSRPVVWLPLTTPQDSRAVASSVSKPSVSIPMVRMMAPVLILLSLLLAAGLIAFGSHMLRWRKKAWLATETQKNEKVYLETSLPGNGWTTEDSTIDLAVTPECLRNLNPSAVPSPETQNLSQSTEEEEAARSLDDDKEDVMAPPPLQMSAEELAFSEFISV
The following text describes a protein:
Function:
May be involved in neurite outgrowth.
Sequence:
MGTVPHPLGPAKLSLVTAPEDKDHLGDLPPAKHQPKAHTAEKASNGFPCTTLGSAASCTCDLKHTNTQRLEDDSLLSGLSSQAAEGPQAAVEPAPVAVACSAGCGPDMMPAPQSSQQFMQGGQMRVNALVQVEDSAMKPQRAEEQPVLQMTQCSSPSTPVGGNESCPTSQASLLQRGEEGGKAEEAGAQPASPARETTTDPGRDPQEAVDAKSRAAVTEQLHPADQSETEQSSQLPAQLCHEGTHPVHDAGVEPGNLGPTHLSKFRETGTMTVQSECSMLTQEAASRTWRDAEVQAVATVESKSASTSPSILAAFLKGNPPPEDKEELHIIYQGSGGLSQSKLVDSFSSQQKSPCSPGIVLKSTVGMAVAATAQSQPAGLPGVSPHVVSEASADNAKPTLPLSSAAATSQGTPVGAAEGTDAASGGKGNAALPVDAAALPKSVPVQQLTIHPHQQPAAGKENTAPAAGTENNVQCLVHEAGSSQLPLLCHTQGETKQNEVLGSSEQCQSATKVEVIPQSAAKLKEENVMVLDAQGVVNTSSEPVSRKAHTGEAGGEQQSRGQGEARQAAEASKLQVEAMAVPGCSSGHVSPHTEASTDPQQQGLQAKETRPEIHATTCPSSAQALPNHGENKKQPTPAMEAKVQVKQSKHIRDVVWDEQGMTWEVYGASLDPESLGIAIQNHLQRQIREHEKLIQAQNSQNRKSISSDTSSNKKLKGRQHNVFQSMLQNFRRPNCCVRPAPSSVLD
The following text describes a protein:
Function:
[Gasdermin-like protein het-Q1]: Gasdermin-like protein involved in heterokaryon incompatibility, a process that ensures that during spontaneous vegetative cell fusion, only compatible cells from the same colony survive (non-self-recognition). In P.anserina, the het-q locus exists as 2 incompatible alleles, het-Q1 (this entry) and het-Q2 (AC P0DW09). This form constitutes the precursor of the pore-forming protein: during the allorecognition process, it is cleaved by het-Q2, releasing the N-terminal moiety (Gasdermin-like protein het-Q1, N-terminal) that binds to membranes and forms pores, triggering cell death; [Gasdermin-like protein het-Q1, N-terminal]: Pore-forming protein that causes membrane permeabilization and cell death. Released upon cleavage and maturation by het-Q2 and binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering cell death (By similarity).
Subcellular Localization:
[Gasdermin-like protein het-Q1, N-terminal]: Cell membrane; Multi-pass membrane protein.
Sequence:
MPTKTSQHAFAGSERWVVPRYSSKPGTLIRLGSVLTDPEDLESSLNLDSIPPIPPHLLRDATPEVRMSVQTELSKSDSTLAKAAPALEGILTLGGGVEASRSQGVSSSLNISGTVKATVFRADKSYMDVLLKDKNVISYAKRGLGKPMFVVVGVATAGRVEMKETRHVTRKAGVSGKVGVEVIGEGEVGLERERSDKSCNEVRGEGGLDFAYRVREFGYSRVRGTVKDKGDWTGKVLFAGGKGPVVEKGGEVVPVFKEFKEGEVKLRATGSFDVAAKA
The following text describes a protein:
Function:
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MLSNIIPLSIGAALGATARWLLNLAVPASIPPATGNLFANWIGAFLIGIFAETVNHPQWKLLLITGFLGSLTTLSGFSLETVTLLQLNRPASALANIFLHTAGSLLLTWLGLKIGAAVK
The following text describes a protein:
Function:
Probable ligand for lin-12/Notch and glp-1/Notch receptors and involved in the mediation of Notch signaling. Involved in the lin-12/Notch pathway signaling of cell fate in vulval precursor cells (VPCs) and in the postembryonic mesodermal lineage (M lineage), acting redundantly with dsl-1 and apx-1. Functions in uterine cells to promote basement membrane mobility during tissue remodeling. Required for oocyte growth control, acting redundantly with apx-1, perhaps signaling via the glp-1/Notch pathway. Plays a role in Notch-dependent induction of left-right asymmetry in interneurons and motoneurons. Involved in maintaining the developmentally arrested larval state known as dauer, probably signaling in the glp-1/Notch pathway. Required for normal sleep bout quantity and arousal thresholds during the transition from the last larval stage to adulthood in well-fed animals.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Domain:
The N-terminal region and DSL domain may be involved in interacting with Notch receptors.
Sequence:
MIAYFLLLLTCLPVLQARVEVHQEFISSKRVSVRFEIVTESHSPNRPVTFDLFPRGPKTNIILLDTFNPVFNFSIQLVQPFTGQPLGDRIYRKVQFSGTNQPWINDTFTTTSGISLSVATEVTCARNYFGNRCENFCDAHLAKAARKRCDAMGRLRCDIGWMGPHCGQAVDPRKCSCENDGICVSSMIHPSQPNQTSSNEQLICECTNGFTGTRCEIFGFNQFQLTAPRPDACSVKDACLNGAKCFPNGPKVFCSCAVGFIGEFCEISLTTTTPTTVEITVSTSGYSSAVYITVALFVIFSIIIGCFKYKFKPMRQQALARGQVPEPYKMPETKSMLIDPEASEAQKKVFTIEGSVQKIDEEVRYTSAPRKYESNNEYAVIQKSTPPPPSLSPPSIPACHYV
The following text describes a protein:
Function:
The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity. Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3. Has cholesterol transfer activity.
Subcellular Localization:
Lysosome.
Sequence:
MQSLMQAPLLIALGLLLAAPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVVGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSGGKRLGCIKIAASLKGI
The following text describes a protein:
Function:
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MLGLTRPELRLALLAVAVRLALLLGATGGDLLLPDYDTSKTLPAELLQPVQPAAFHQSHSADGLQEPWMGDGQPQAGAAAAGATQSARPWLLRGWLVWDAVFFVDIAARGYVYEQYYAFFPLMPALLSRAPPELFALLAVALNAAASVAGVVMLYRLGASLICDPELSAAACLFFILSPAAVFHAAPYTEAAFAAATLAVLCCLHCRGIGGGSSSSRSRSRDGIGGLEGAVSAARGSRDQRRGGLKSGGPGFSLARLMAATAAVAVSCGLRSNGVVNAGYVGHYSLRHAVALWPKSKARALWTALLGVVAAAVSVTPLVLFQAAAYEAFCRRDAHGAAHVSSAAPAGAYDAGVGSSSSSSTGSTGGGGGGSTGPYDWPRPWCSSRVPYVYGFVQLLYWNVGFLRYWTLQQAPNFLLAMPVLLLSAAGLFEYSRANAGHMACLGLMPPGRTHSDGVAAAAEDTAAEALGKSNWRSGLSKSEGEAQLASVRGAMGEHSTGQLRRRLGLGGASDAGAKVAAAGGTSSYQGEAPGRELYMSDGSRHAGYFSPELAVTMFPWAFSLLVAVTTMHVQVSTRFLLSSCPPLYWYMAHLWRRGMGRRLGNEVGGRRPRRAEPAAAGEAATEAATMGGGGSGPAAPGGPSSAGGSGWSSWLAMALWRWCLVYVALGCVLFINFLPWT
The following text describes a protein:
Function:
Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA.
Sequence:
MRSRIPLLLAVLAAACLRFGSAEADPLPAAVVELVKAGSVSSIQDLQFLLFSESIEVEPDSHHDNDSSNRLPRSLLDAQPAQQAICKVRTEVIEVTRSMLDRSNADFLLWPPCVEVQRCSGCCNTKTLQCVPVLTHTRYLQVMKIQYVKKRPLYDKAVVSVLDHVECRCQPAPRPAHRRKSSSQKLDARDRSEKSRPKEDLHRRDELKHNQRLNLEDLLSHSWLPQDRFSESPDTVHFGRDAWTRNETQYGGGKSHHRHPVDVRKHSTTNDTSTQGTMAPIPNHTEQEETDTSLRNITQIESQNYTNRNITNQTSEFNNGVSETTNQTFKHQSNLTQLNEQLRTMNRTYSNATETANLNRGDVFVSVEESVKKLRGETTDVEKVKVDEAEDLLLLHKLMDEEKHKPHLKVQQTNVQPDKKLQQLHHKQQQHTYTTTQRTGTTSPPLHHQPPHKPPRPPPQPPKKRRKQRNRISKSAMRALLM
The following text describes a protein:
Function:
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Subcellular Localization:
Cytoplasm.
Sequence:
MHMPKGFLSFGINIGIKDDTKDFGVIYSEIPCKATAVFTKNNFPGAPVIVGKEHVRSGVLQAIVINSKNSNVATGEKGIQNSREICKIIGESLGIKETLVLPSSTGVIGVPLKMEIILPACKKAKSLLKPGNLEEVAEAIMTTDTRKKISSRNIKTKSGQGTIYGIAKGAGMIEPNMATMLCYILSDVSLPEGTDLYSILKSSVDQSFNCLTIDSDTSTSDTVALLCNGLSGESSVQDFSKALTEICIDLTKLIATDGEGATKLIELTISGAKSEAQARKIGKSILNSPLVKTAIYGGDPNWGRLIMAVGKVFDEPIPFEGLQIYFGTLPVKEANPETLKKLSEYLKNNTEISLNVVLNVGTISMKFWGCDFTEKYIEENAYYTT
The following text describes a protein:
Function:
Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MTVLAPWALWEKTKDVMVLEQQYQSMCTWIAAIPENMKRHRHLCDPVVLQFAVAVRESNPWAVMTAYHKINGVHCSEDPRLIRDIPRSEWKYDGLVLCDWWGIYSTSELINAGMDLEMPGPTDWRCKILAWATRSRKVSIETIDSSVRRVLKLVNRVLAAQSEPVKDSDTEKNRALLRETTAVPVVLLKKNEANVLPLVKDSKTRYALIGDHWKNPAVAGDDSSEVTPYYVSTPYSAFVEAVGEDSFICAMGCYSHKFAPLLYSTITQPGSDAHGMLLEFFNKDPNGSSDAELLYTTTTEKTDLKFADSLPPDTVPEYTSSGSAPSRGSRWGCAGWIREAVEIARQVDIPVILTGLSADYEYEGIDRKSLGLPGRVDELIERVTEANPKTIIITEAGTATTMPWADKTPTVIHSWFGRQETGHGIVDILFGDVNPSGRLPLTFPRNLEVPPVYESDPKHIMTISVSLKNTGQCPGAEIVQVYVKDVSSSVQRPRKELKSFKKVHLAPGENMKIEVTS
The following text describes a protein:
Function:
Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.
Sequence:
MAAYRCPVCDYVYDEANGDAREGFPAGTGWDQIPDDWCCPDCAVREKVDFEKIGG
The following text describes a protein:
Function:
Histone demethylase that specifically demethylates 'Lys-10' of histone H3 (H3K9), thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate (Probable). Probably involved in regulation of chromatin structure, promoting expansion of euchromatin. Negatively regulates rhino-dependent piRNA production capacity of several genomic regions; may help define the frontiers of piRNA clusters by regulating histone methylation levels. May be involved in regulation of behavior and circadian rhythms.
Miscellaneous:
MISCELLANEOUS: Shares a promoter with CG8176, which produces a bicistronic pre-mRNA encoding both genes. Alternative splicing results in mature mRNAs encoding either Kdm3 or CG8176. Efficient production of mRNAs encoding Kdm3 requires the splicing factor hfp.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MSQKELAALVATRTSRKRTISSTSFSISTRTDPKSIIEIHIFNDSLPIKRACCEVENPTLKAEQRVQQEEESLGQVPPLTEEEQQRHDEFRNSGSIFLQDLPCFKLQQAQPIAGSSPIPKCRECRRRNLATTEGEPSSVSDVYCRFYEFRRLQFNENGELCVVGFPNPYSEPSPEDIAIWQPDKNTPPTSGYMDIQVCRYILLHAGDQFCYIWHQEAEALSLHQNTDGTIAWKKAVKGTREICDVCDTTLFNYHWTCRKCGFGVCLDCVKDRKEGLRLRRAENAAQKGCDEYHWLLCSDPSGPQEHVLTELMLTQIIAGDALNVLGRLLHEVRTLWQVPQVCGCLLSKQAIEDAQSKEVIQDMIKESQLKQHTSYSSLASEQKVHQQQRLDQLHATKLEFARELGVDYVPGRVWTKETLGKDPITTAFDNLKHINFLRKGLAGLRRFLPPRTMTFAYSTQLAPGVPHEFLCDGRLLRLTDAMHPDNRVLFQEVWKCGQPVMISEVARSLNLDLWHPQAFCRDFGDKPNDLINCLNGNLVPNQPMRHFWEGFQCMTKRLPDAYGKPMLLKLKDWPPGDDFAEILPTRFADLMKGLPMPEYTLRTGNLNIASCLPKMFVPPDLGPKMYNAYGSALHPDKGTTNLHLDISDAVNIMVYVGIPQDGDTRPQMAATQKAIEIGGCDYITRARCQSPDVLPGALWHIFPARDADKIRDLLNRVTLEKGFRLEPDHDPIHDQNWYLDDKLRARLFKEYGVEGHPIVQCLGDAVFIPAGAPHQVQNLHNCIKVAEDFVSPENITHCYHLTHEFRRLSHSHTNHEDKLQIKNIIYHAIKDCCTILTRAVDERLNAELTKLNAD
The following text describes a protein:
Function:
Possesses 5'->3' exoribonuclease activity. Acts as an endogenous post-transcriptional gene silencing (PTGS) suppressor.
Subcellular Localization:
Nucleus.
Sequence:
MGVPAFYRWLAEKYPMVVVDVVEEEPVEIEGVRVPVDTSKPNPNGLEFDNLYLDMNGIIHPCFHPEDRPSPTTFAEVFKCMFDYIDRLFIMVRPRKLMYMAIDGVAPRAKMNQQRSRRFRAAKDAADAAAEEERLREEFEREGRRLPAKQQSQTCDSNVITPGTEFMAVLSIALQYYIHQRLNYDPGWKKIKVILSDANVPGEGEHKIMSYIRGQRNLPGFNPNTRHCLYGLDADLIMLALATHEVHFSILREVVFTPGQQDKCFLCGQVGHLAANCEGKAKRKAGEYDEKGEAIVPKKPYQFLNIWTLREYLEYEFRMPNPPFQIDFERIVDDFIFICFFVGNDFLPHMPTLEIREGAINLLMAVYKKEFPSMGGYLTDSCTPDLNRVEHFIQAVGSYEDKIFQKRARLHQRQSERIKREKAQAKRGDDLDPHVRDDLIVPVANFRGSRLASGAVPSPYEQNGSRRERNSQALKAPRVSSSGSSIAAAIVEAEKDLEAQELENKENLKSMLKDALRGKSDVFNSENPEEDKVKLGEPGWRDRYYEDKFGARTPERMEEIRRDVALKYTEGLCWVMHYYYEGVCSWQWFYPYHYAPFASDLRSLSQLNITFELGLPFKPFDQLMGVFPAASAHALPLKYRQLMTDPNSPIVDFYPTDFEVDMNGKRFSWQGIAKLPFIDEDRLLAEIKKVEHTLTPEEARRNSTMCNMLFVNGSHSLSPYIYSLSSKFGHLPDKDLGGIKEKLDPSASGGMNGYIALCCGDLSPPVFRSPVDGLEDIMDNQVICSIYKLPDPHKHIARPPVGVIIPKKSVEAGDLKPPPVLWHEDSGRRPHDNNHRGPYDKSNRSNPSGSLSGRQLGEAAHRLVVNSLSNRGGGQHNSPSMPYQTIMSGMNYPNGRHHMGNHGVPPRMEQPAGRSGWHVPGDNMANGQAAYDQYQPERSGPSWHERDNRGGQRYNPYARENRQDSSGRVQPHGYYQNRGNSQSAASSAGPGLSGQHPPAYAGGYSGGYQPTPHGPQQWQQRPYGGGAPPTRPNSHQSQNRYGSLDRSSNKRSSGHGRH
The following text describes a protein:
Function:
Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.
Subcellular Localization:
Secreted.
Sequence:
AEMQVSVALLYSSAVLLLLQGCCTAARAWKVLKNDATEVIPEYSEDAQQPEPEQQTNNTMNRAKHGGRTLSANTHSYGASELSCRELRSTRYITDGPCRSAKPVKELVCSGQCVPSHLLPNSILRGKWWRHSHSDYRCVPAHSRTQRVQLQCPNGRSRTYKIRVVTSCKCKRYTRHHNQSEAKEAPARPRRNRKHTRQPQDRSKTSNTPEIGNSY
The following text describes a protein:
Function:
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Sequence:
MHLIVTEKNIAARRIAAILAPKSPKKERVSGVDVYRYELGKGKSRQETAVVGLSGHIVGIDFQKEYNNWQKVDARALIDAEITTTPINRKIVTALRTLGKEADRVTIATDYDREGELIGVEALNIIKKVNPEVPFDRVRYSAITPKAIDAAFTNPTSVDFDLADAGHSRQVIDLVWGAALTRYISLAAGRLGKMFLSVGRVQSPTLSLVVDREKERNIFVPTPYWEIHVELETKAGETFSAQHSTRRFLDKEEATAVFKKLGKKAELKEIEKGTKSDLPPTPFNTTGFISAANSIGLSPANAMRIAESLYTNGYISYPRTDNTVYPETLDLRAQIEIFTEGPFKEFADALLEKAELVPTRGKKETTDHPPIYPASLAKESELKEEEWKVYELVVRRFFATFAGPSTWETMRLRLEINAEEFRANGARLLEPGWRWYYPYNVPEDRLFPELSEGEILKVIKKEMLDKETQPPGRYGQGRLINIMEELGLGTKATRHEIISKLYSRAYIHGNPVQPTNTSFAVVETLEKYSPTITKPDMTKLLEENMDLIAEGKIKEDTVLEESREMLQQVFSELDKNRDKIIESLQAGLREDKIIGNCSLCGNELMIRRSKRGSRFIGCSNYPNCTFSLPLPKSGQIVVTDKQCETHGLHHIRIINAGKRPWDLGCPQCNFIEWQKTQKEKQAQQPKKEKPKTIKDIEGVGKATAGKLEEAGITSVEALAEADPIELAKTIKTSVKKVKTWQISCNGGIVEDL
The following text describes a protein:
Function:
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Sequence:
MFRVQTLNQIAEKGLQVFTEERYEVGDRINHPDGILLRSYSLHQEEFSKDLKAIARAGAGVNNIPVERCTEKGIVVFNTPGANANAVKELIIASLIMSSRNIINGVSWTKNLEGEEVPQLVESGKKQFVGSEIAGKRLGVIGLGAIGALVANDALALGMDVIGYDPYISVETAWRLSTHVQRAFSLDEIFATCDYITLHIPLTNQTKGIIGEHAVEKMKRGMRLFNFSRGELVDEKVLQKALEEDIITHYVTDFPNENVIKMKNVTATPHLGASTSESEENCAVMAARQLREYLETGNIRNSVNYPNVELPYIGKKRITIMHQNVPNMVGQITGCLAEHHINIADMTNRSKHSWAYTMIDIDNGIDDIIKENIVENISKITGVVAVRMIV
The following text describes a protein:
Function:
Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs.
Subcellular Localization:
Cytoplasm.
Sequence:
MAAPQTVQRGIVKSVLSGDAVIIRGQPKGGPPPEKQLNLSNIVAPKMARRANPNVEASVETKDEPYAWEAREFLRKMVVGKEICFTVEYKVPGTGREYGCLYVGKDPQTGKNVTEALVNEGLVEVRRGGIKPSDDQAKLCDLEDTAKSNSKGKWAADAQSHVRDVAWTLENPRNFVDAHHNKPVKAIVEHVRDGCTLRAFLLPSFQYITVMLSGIKCPMFKREGDKEVAEPFADQAKFFVESRLLQRDVEIIMEGVSNQNILGTVIHPNGNITEFLLQEGFARCVDWSMGVVTTGAEKLRSAEKAAKEKRLRIWKDYTPSQASIAITEKQFTGKVIEINNADRLVIKTPENQIKEVTLSSIRPPRMTDDGGPKDNTKRIRPLYDVPYMFEAREFLRKKLIGKKVNVSVDYIRPGSDGYPERTCATVTIGGINVAEALVSKGFVTVVRYRADDDQRSAHYDELLAAEARAQKNAKGLHSKKEVPIHRVADLSGDTNKARQFLPFLQRAGRSDAIVEFTASGSRVRLYLPKETCLITFLLAGISCPRVPRSLPSGTTEGEPFGEEALSFTKELCMQREVEVEVENIDKAGNFIGWLFVDGVNLSVALVKEGLSKVHFTAERSQYYHTLVSAEEEAKKEKIKMWANYEEPKDIVVVEEAERNVNYKDVVVTEVGEEMKFYAQHVETGPHLEKMMEELRTEMTDTPPLQGAYTPRKGDLCAAKFVDEEWYRARVEKVSGNQANVLYVDYGNREVIPAARLAALPSSFHSLPIQAHEYQLAFITVPEDPEAKKDAQEAFLKDVLNQQLALNVEYKNQGQDMVIILTSDKNTDIGLGLVKDGLVMVETRREKRLQKLVNDYKKAQEAAKNARLNLWQYGDFTADDAVEFGYKR
The following text describes a protein:
Function:
Interacts with MMS4 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably occurs approximately half a helical turn upstream of the free 5'-end in these structures. May be required in mitosis for the processing of stalled replication fork intermediates arising spontaneously or subsequent to treatment with DNA damaging agents such as methylmethane sulfonate (MMS), camptothecin (CPT) or UV. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). This involves consecutive cleavage of D-loops and nicked Holliday junctions leading to sister chromatid crossover. In contrast to MSH4-MSH5 dependent crossover, double Holliday junctions do not seem to be involved. Spore formation and viability are severely impaired in deletion strains.
Miscellaneous:
MISCELLANEOUS: Two distinct classes of meiotic crossovers have been demonstrated in budding yeast. Class I crossovers exhibit crossover interference and require MSH4 and MSH5 for their resolution, while class II crossovers exhibit no crossover interference and require MUS81 and MMS4. While class I crossovers represent the majority of crossovers in S.cerevisiae, they are virtually absent in S.pombe, which lacks orthologs of MSH4 and MSH5; MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MELSSNLKDLYIEWLQELVDGLTPKQEQLKIAYEKAKRNLQNAEGSFYYPTDLKKVKGIGNTIIKRLDTKLRNYCKIHHISPVEAPSLTQTSSTRPPKRTTTALRSIVNSCENDKNEAPEEKGTKKRKTRKYIPKKRSGGYAILLSLLELNAIPRGVSKEQIIEVAGKYSDHCMTPNFSTKEFYGAWSSIAALKKHSLVLEEGRPKRYSLTEEGVELTKSLKTADGISFPKENEEPNEYSVTRNESSEFTANLTDLRGEYGKEEEPCDINNTSFMLDITFQDLSTPQRLQNNVFKNDRLNSQTNISSHKLEEVSDDQTVPDSALKAKSTIKRRRYNGVSYELWCSGDFEVFPIIDHREIKSQSDREFFSRAFERKGMKSEIRQLALGDIIWVAKNKNTGLQCVLNTIVERKRLDDLALSIRDNRFMEQKNRLEKSGCEHKYYLIEETMSGNIGNMNEALKTALWVILVYYKFSMIRTCNSDETVEKIHALHTVISHHYSQKDLIVIFPSDLKSKDDYKKVLLQFRREFERKGGIECCHNLECFQELMGKGDLKTVGELTIHVLMLVKGISLEKAVAIQEIFPTLNKILMAYKTCSSEEEAKLLMFNVLGDAPGAKKITKSLSEKIYDAFGKL