lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Repair polymerase. Involved in gap-filling in DNA nonhomologous end joining (NHEJ) required for double-strand break repair. Seems to conduct DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. Preferentially acts upon short gaps formed by the alignment of linear duplexes with complementary single-strand ends. Required for filling gaps that need removal of a 5'- or 3'-terminal mismatch, however lacks nuclease activities.
Subcellular Localization:
Nucleus.
Sequence:
MSLKGKFFAFLPNPNTSSNKFFKSILEKKGATIVSSIQNCLQSSRKEVVILIEDSFVDSDMHLTQKDIFQREAGLNDVDEFLGKIEQSGIQCVKTSCITKWVQNDKFAFQKDDLIKFQPSIIVISDNADDGQSSTDKESEISTDVESERNDDSNNKDMIQASKPLKRLLQGDKGRASLVTDKTKYKNNELIIGALKRLTKKYEIEGEKFRARSYRLAKQSMENCDFNVRSGEEAHTKLRNIGPSIAKKIQVILDTGVLPGLNDSVGLEDKLKYFKNCYGIGSEIAKRWNLLNFESFCVAAKKDPEEFVSDWTILFGWSYYDDWLCKMSRNECFTHLKKVQKALRGIDPECQVELQGSYNRGYSKCGDIDLLFFKPFCNDTTELAKIMETLCIKLYKDGYIHCFLQLTPNLEKLFLKRIVERFRTAKIVGYGERKRWYSSEIIKKFFMGVKLSPRELEELKEMKNDEGTLLIEEEEEEETKLKPIDQYMSLNAKDGNYCRRLDFFCCKWDELGAGRIHYTGSKEYNRWIRILAAQKGFKLTQHGLFRNNILLESFNERRIFELLNLKYAEPEHRNIEWEKKTA
The following text describes a protein:
Function:
Ligand for members of the frizzled family of seven transmembrane receptors.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MLPLILLLLLINIFSTSESSNRVSTALRTQRKKPFAAIVFSESNYNTPFNKNPCFWLSRLKFQSKLCWRQRGLPDVLLTARNLSIISCQNQFQYDQWNCSKRDFFFKKIYRETAFMHSMAAAALTFSIARACSEGTLAGCQCGEHGKPSNSSKWQWGGCSDNIKFAKKFTRRFLQLRKKDDGNYQNAIVKYNSEVGIRIVIENVQVVCKCHGLSGSCSLKVCYKKIQAFDYVSKQLKGLYHAAIYVEHENHIRPYKSGKMGQKLVFLENSPSFCPTTVDRRCNNTENCATLCCGRGFYTTQVHEINKCMCRWRKEMFNVECKYCRENKTIFRCK
The following text describes a protein:
Function:
Supplies the nucleotide substrate for thymidylate synthetase.
Sequence:
MVPPITSDEFCETSGCFGDSANLHTTLERLKININSDAKKLVDTNGDLKKHQRFLRIAKVTSLRSKDPNTQVGCVIVDKDNCIVSVGYNGFPIGVDDDVFRWDKEDPEDNKHLYVVHAEMNAIINKRCTTLHDCTVYVTLFPCNKCAQMLIQSRVKKVYFLENRDELAFRASKKMLDHARLPYEQIVMPQEAYVIEL
The following text describes a protein:
Function:
Involved in pre-mRNA splicing and cell cycle progression.
Subcellular Localization:
Nucleus.
Sequence:
MALGRDAVQVGLEQATEERENGSSQRGPPPIIDTNDVLACRPNMAGIHEGERTGKPEPNNGQGEPAGTALVEVIKKRSQLLAQAGKRIPNPNLPIQPITSSRLVPRSALATDTDNQSVDGSQVNLIDFLSQPAANSAALGISASAPAHQPRTLMGEVPSVIKKLTANTQSVPGPPLNAPNDVHPQINITDENAELGHHPIVGSTSLPRAGLNPMADYRLAHSFFVLVLINQSNRFFSFLVEIDSPLCTDITFYPTDVEKTIATVYISSVSFEQLNTLGELFKKALAKEAAVIDMDRLKMVIERAALKTCNVMEVDAADSLSSAIISNFLCGGSSDLISDECGCVYRKYTEALRVIRRATTVPPNHKKKAISFHDESLAVQVWLFKSLKLWSFCVDLEESIGTVESTQKAYDTIFELKIANAQIVVNYGNFLEENEYWEESFKVYKRGIELFTYPIVFEIWNTYLNKFMKHYQGKKIERARDLFEQVLEKCPEKFVKPIFLLLAKRAMGVLERATEKVALHDRFEMFAYYIAKATENFGLPATRPIYEKAIKSLPNNQTAKMCLRFANLEQKLGKIDQARAIYAHSSQFCDPRTSPKFWETYHNFEIQHGSEDTFREMLRIKRAVQASFNTETSYLAAKAAAARAAGNRGGGATVSQQQDEDDETGSGDPMRRLEKDDPASSTTAGNQAFVLLKNRQAQIDRSGPLNPDQQATNNSANVDEIAINDDDD
The following text describes a protein:
Function:
Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal apoplasm and the extraorganismal apoplasm and prevents lateral diffusion (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Note=Very restricted localization following a belt shape within the plasma membrane which coincides with the position of the Casparian strip membrane domain in the root endodermis.
Sequence:
MSGSDTSGSVHVDEHGHGHGKASSSYDGAGAPAPAPAPFQGHRKAGSGSSDVPFLLRSGGSGGDGLRRCLGLIDFVLRVAAFGPTLAAAISIGTSDERLSVFTNYFQFRARFDDFPAFEFFIVANAIAAGYMVLSLPFSAATIMSSKATGVKLLLLICDTIMVGLLTAAASAAAAMVYVAHEGNLRANWVPICLQFHGFCQRTSGAVIASFLAVFVLMVLIVMAAFTMPRRTHHTAS
The following text describes a protein:
Function:
Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).
Sequence:
MSGEDSIRSFPVPDLGEGLQEVTVTCWSVAVGDDVEINQTLCSVETAKAEVEIPSPYAGRIVELGGAEGDVLKVGAELVRIDTGPTAVAQPNGEGAVPTLVGYGADTAIETSRRTSRPLAAPVVRKLAKELAVDLAALQRGSGAGGVITRADVLAAARGGVGAGPDVRPVHGVHARMAEKMTLSHKEIPTAKASVEVICAELLRLRDRFVSAAPEITPFALTLRLLVIALKHNVILNSTWVDSGEGPQVHVHRGVHLGFGAATERGLLVPVVTDAQDKNTRELASRVAELITGAREGTLTPAELRGSTFTVSNFGALGVDDGVPVINHPEAAILGLGAIKPRPVVVGGEVVARPTMTLTCVFDHRVVDGAQVAQFMCELRDLIESPETALLDL
The following text describes a protein:
Function:
Hydrolyzes purine nucleotide phosphoramidates, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate), guanosine 5'monophosphomorpholidate (GMP-morpholidate) and tryptamine 5'guanosine monophosphate (TpGd). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine--tRNA ligase, and lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)). Is essential for the activity of the enzyme D-alanine dehydrogenase (DadA) and is required for E.coli to grow on D-alanine as a sole carbon source. Is also required for growth at high salt concentrations.
Sequence:
MAEETIFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAEDGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKGL
The following text describes a protein:
Function:
ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M. May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres. Has a specific role in chromosome segregation during meiosis II.
Subcellular Localization:
Nucleus.
Sequence:
MHRQNALKLETPGTSNDSELASRQFHFPYAEAYSIQLDLMRKVFSTIEDGKVGLFESPTGTGKSLSLICAAFTWLRQNAQRHTIGTSTNDGETHGSNHGPATQQEPDWVVKHKNELRRKQHEAYELDLKDRIAAARAKQAALKKSLQDGQVLLDAQARVAKRQRRSANDDDDKDSDDDLLIDEKEGAKSARTLQMATYSKTALSETSVEIDSSLSPAVRALMQQYEQASSRGREDEDEPETLPRVIYASRTHSQLSQFVAELKKTSFGQVDIIHAETLPIRTIPLGSRKQMCINEDVQRIGRNKGSEAMNERCIELIKGKTGKTKCSSLPPFDQTGRSRILEFRDAAMAEVGDIEDLVQLGKQTNTCPYFAARSSAKQAELITLPYNLLLQKDARNALGISLEGCIVLVDEAHNLIDTILSTHSVTIDSQQIAQASEQIDTYLDKFALRLKGSNEQNLRKVRKVLSSMSAFFSKKAAEGKTNAELVLSAADLVRSLTGNLDQINLVTLETWLKETQIARKISGYADKHSKMAVQQAAASVNQHNGTRTNKSRHPPKLLLENASPDSIRSASQSAISSMHAIETFILSLANRSEDGRVVLSSATNSAGENVVRAKYQLLNPSHVFRSLVDEARSVILAGGTMEPMSDFRQQLLPFVPPDRLVTFSCGHIIPASNLMVSVLSASPKGLPFEFKFDSRDNVELIDELGRTLVNVCNIVPAGLVVFVPSYAFLDKLMARWKDAASGGLLQRLGSKKKIFIEPKTTMEVDKVLGEYTAAIRAKDVKTGVSSGGAIMFAVVGAKLSEGINFSDNLARGVVMVGMPFANMHSPELAERMKYVRELAIKHESTACVTASQKPSDPGHELYINLCMKAVNQSIGRAVRHQNDFAALILLDRRYARPEIKQRLPGWIRDQVTVADRFGSMVQQTAAFFKNRKN
The following text describes a protein:
Function:
Essential for gene silencing: has a role in the structure of silenced chromatin. May be involved in gene regulation during development. Binds RNA.
Miscellaneous:
MISCELLANEOUS: Transcription utilizes two promoters. Promoter 1 gives rise to the short transcript encoding Sas10 only. Promoter 2 generates a discistronic transcript of Sas10 and Rnp4F. The longer transcript becomes an RNA duplex which is a target for RNA editing via Adar editase; Rnp4F (not Sas10) is edited.
Subcellular Localization:
Nucleus.
Sequence:
MDSDGDDYVMSGSDQEYDDEEREILEDLRKQRKKPHDPVQEVLGFSDDDDDDDDDDEEEQQDVAELMRDSDIEGAEDDDRDLPNTMDWGSKRSTYYNTDFVDQDYSSYNAQEEEQARAEEEEAKKIQLRLAKRMSEADFQLDNVEAAPAGSSDDNELSHITKVTSDLAGLSERERRQLMHSESPEFIILTQDFQQHLDEVKNLLKPVLNYVRKHDVPMVPALQYAGLCHTVLTTYCSNVAFYLLLKARRIDVKAHPVIRRLVQLKDLIEELKPRYEEYIRPQLEALLERIEDGDAFTVLDVAQRKAKLQILNKYNDGQQASVSSDDDDNDDDDDAESKEKDLQEEAGEEEEEEDARRGITYQMAKNKGLTPHRKKELRNPRVKHRGKYRKALIRRKGAVRTVRKELQRYGGELSGIKAGVTKSVKFRT
The following text describes a protein:
Function:
ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Subcellular Localization:
Nucleus.
Domain:
The DBINO region is involved in binding to DNA.
Sequence:
MSSEEEEDKQYNIDQLLLQITQIESTRQVNPQFRKVQEPEFNLVFNLKRPPVEDLSLEEAQLCYLENKRQQVFQRKTNEVKDKKYAYAANNQSKIQNKLLMFFSKVFRDQPNMVEKFLYDKYSHKQETILEQQIHIGISSQQFEPAFQSNKLPQLGYNFEDAFKIQYTDSRMGKANIKKQRKLKNDCQASTQNDYFNTIIQQELYEDPIEIGDWKKSWAIVVRNAVKISKFKAKFRQDLREFFKRIAYFAAKEARRRNQKCQKYQKEFMEAQSYWRKRDKELIEIKKRKEKLEQERKKKEEEEREQLLQQKRLEFLMKQSDIYAHFMAKKLGITLDNQISLNTDEIDEEQALENVQKVINDNRKQLQQFDGKKQENVQIQELKLDHNDQDRDFSLIAPPSTFKGDLKEYQLKGLRWLDNLYDQGINGILADEMGLGKTIQAIALLSHISSFKSIWGPFLVIAPSSTLHNWQQEIKKFCPTLKVLPYWGQAQQRKTIRKYFQQKNFGQRESLFHIVVTSYNLVVSDNKIFNRAIKNINSQRWQILLSFNARNRLLLTGTPIQNTMGELWALLHFIMPRFFDSFDQFQEWFSKDIEAHSQDQKTLNQHQLQRLHAILKPFMLRRLKKDVENEIGQKKEVQIVCEMTSRQAVLYRNVKSKLSIKEFFRMLDSKQKVDNLMNLVMQFRKICNHPELFERKPYKSPCVFQDRQNVEVYQKNPIVQVTKRNPISFIIPKLVYDNLIKNTKCLFTAHYIYNSLKNGESTFSYLLFKHLPLSLFEKNVFDLIDLLCHKQDSSSLVNYSFSKQLQFYIPPVQSQIVSFECRSQSFYYQIQQSLYNRQALSFIKESPASFILPNSPESLIASSSKLLQLDKLLKELKQKQWRVLIFCQMTRMLDILEEYMLHKGYTYFRMDGQCQINDRRDMVNEFQQNDKIFAFLLSTRAGGLGITLTQADAVIFYDNDWNPTMDAQATDRAHRIGRTKDVYVYRLITKGTIEERIVKRAQQKQNVQSTVYSGGFQGDKFKPQEVFELLFGEQEMDETVANKFMAKGQKKKKKPVKVEQKDTQKDAQKEVVKEQKDQQEEEDIIEVDLRELEMNEKDCEDAD
The following text describes a protein:
Function:
May form a water-specific channel (By similarity). Required for prolonged spore survival on fruiting bodies.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Here, the second motif is Asn-Pro-Val (NPV).
Sequence:
MVKVVPLRFITYDPLKDPSKMIYRRPISKPVKAFKGFFSEFLGTLYLVYFCGGSVCAAFAVAGDSAARALLGGLIQGMALAALIWAVSGVSGCNLNPAVTLANLLSGRVGLIDSLYYVAAQILGCIAGAGILYGCLPNMYRIDLGVPHLAPGMNTGQAFLMEMMLTSILCLCVLGTSVFNVWDRRLNRIAPFAIGLALFIGVAIGFNFSGGALNPVRVLGPSIISGVWSHHWVYWLGPIVGAILAAFIYRCLLQERFDVIERPGYIAPLIDPSTAVSSY
The following text describes a protein:
Function:
Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which has been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42. May be involved in ribosomal large subunit assembly.
Sequence:
MDVTSRLAKRHGIASMEESIELLVGCYEQVLFGYRVHREGEQWLSSADFTHHAHTASVSVLAVNNRFVATGSRDESIQIYDMKKKGEHGALLHHNGTAMLFFKKNYLNLVDGLRWNISQTVIQNDNFGTKHQGRVVHFDKIISIMLGQVVSLSIHPSGKLALSAGTDETLRRTHYPVVSHWREICGCDT
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NSP1 plays an important role in several nuclear transport pathways including poly(A)+ RNA, tRNA, pre-ribosome, signal recognition particle (SRP), and protein transport.
Miscellaneous:
MISCELLANEOUS: Present with 2400 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Domain:
Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side.
Sequence:
MNFNTPQQNKTPFSFGTANNNSNTTNQNSSTGAGAFGTGQSTFGFNNSAPNNTNNANSSITPAFGSNNTGNTAFGNSNPTSNVFGSNNSTTNTFGSNSAGTSLFGSSSAQQTKSNGTAGGNTFGSSSLFNNSTNSNTTKPAFGGLNFGGGNNTTPSSTGNANTSNNLFGATANANKPAFSFGATTNDDKKTEPDKPAFSFNSSVGNKTDAQAPTTGFSFGSQLGGNKTVNEAAKPSLSFGSGSAGANPAGASQPEPTTNEPAKPALSFGTATSDNKTTNTTPSFSFGAKSDENKAGATSKPAFSFGAKPEEKKDDNSSKPAFSFGAKSNEDKQDGTAKPAFSFGAKPAEKNNNETSKPAFSFGAKSDEKKDGDASKPAFSFGAKPDENKASATSKPAFSFGAKPEEKKDDNSSKPAFSFGAKSNEDKQDGTAKPAFSFGAKPAEKNNNETSKPAFSFGAKSDEKKDGDASKPAFSFGAKSDEKKDSDSSKPAFSFGTKSNEKKDSGSSKPAFSFGAKPDEKKNDEVSKPAFSFGAKANEKKESDESKSAFSFGSKPTGKEEGDGAKAAISFGAKPEEQKSSDTSKPAFTFGAQKDNEKKTEESSTGKSTADVKSSDSLKLNSKPVELKPVSLDNKTLDDLVTKWTNQLTESASHFEQYTKKINSWDQVLVKGGEQISQLYSDAVMAEHSQNKIDQSLQYIERQQDELENFLDNFETKTEALLSDVVSTSSGAAANNNDQKRQQAYKTAQTLDENLNSLSSNLSSLIVEINNVSNTFNKTTNIDINNEDENIQLIKILNSHFDALRSLDDNSTSLEKQINSIKK
The following text describes a protein:
Function:
Acts as a negative regulator of abscisic acid (ABA) response.
Subcellular Localization:
Nucleus.
Sequence:
MASRDFLGAFGGGGVRGGGEGARPQAEDAAAGGAAGGESDDVELSLGLSLGGRFGTEAKRQRLARSSSIASVCSVSSLDGDDADPSPAAPLPLLRTSSLPTETEEERWRRREMQSRRRLEARRKRVERRNSMGGAPPSAPPKPGGEATATAAANGVQLRRSVGSQGSNSVNTAEQGIGGSAVCQSTDSKSPSTSDNTNQNNMLPPTKATEKPQNGTSTEQPRLRTLGSLTTRTSSCSDIRKIMMEDMPMVSSKVEGPNARRIDGFLYRYKKGEDVRIVCVCHGSFLTPAEFVKHAGGGDVSNPLRHIVVNPSPFS
The following text describes a protein:
Function:
Involved in the maturation of [NiFe] hydrogenases. Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase using carbamoylphosphate as a substrate and transferring the carboxamido moiety in an ATP-dependent reaction to the thiolate of the C-terminal cysteine of HypE yielding a protein-S-carboxamide. In the absence of any other substrate, displays carbamoyl-phosphate phosphatase activity.
Domain:
Contains a version of the YrdC-like domain which probably has a different function than that of some proteins where it has been implicated in RNA binding; Contains a unique C-terminal domain with an O-carbamoyltransferase motif.
Sequence:
MAKNTSCGVQLRIRGKVQGVGFRPFVWQLAQQLNLHGDVCNDGDGVEVRLREDPETFLVQLYQHCPPLARIDSVEREPFIWSQLPTEFTIRQSTGGTMNTQIVPDAATCPACLAEMNTPGERRYRYPFINCTHCGPRFTIIRAMPYDRPFTVMAAFPLCPACDKEYRDPLDRRFHAQPVACPECGPHLEWVSHGEHAEQEAALQAAIAQLKMGKIVAIKGIGGFHLACDARNSNAVATLRARKHRPAKPLAVMLPVADGLPDAARQLLTTPAAPIVLVDKKYVPELCDDIAPDLNEVGVMLPANPLQHLLLQELQCPLVMTSGNLSGKPPAISNEQALADLQGIADGFLIHNRDIVQRMDDSVVRESGEMLRRSRGYVPDALALPPGFKNVPPVLCLGADLKNTFCLVRGEQAVLSQHLGDLSDDGIQMQWREALRLMQNIYDFTPQYVVHDAHPGYVSSQWAREMNLPTQTVLHHHAHAAACLAEHQWPLDGGDVIALTLDGIGMGENGALWGGECLRVNYRECEHLGGLPAVALPGGDLAAKQPWRNLLAQCLRFVPEWQNYSETASVQQQNWSVLARAIERGINAPLASSCGRFFDAVAAALGCAPATLSYEGEAACALEALAASCHGVTHPVTMPRVDNQLDLATFWQQWLNWQAPVNQRAWAFHDALAQGFAALMREQATMRGITTLVFSGGVIHNRLLRARLAHYLADFTLLFPQSLPAGDGGLSLGQGVIAAARWLAGEVQNG
The following text describes a protein:
Function:
Represses transcription of the icaADBC operon necessary for biofilm production.
Miscellaneous:
MISCELLANEOUS: Binding to the ica operator DNA involves two IcaR dimers and is highly cooperative.
Sequence:
MKDKIIDNAITLFSEKGYDGTTLDDIAKSVNIKKASLYYHFDSKKSIYEQSVKCCFDYLNNIIMMNQNKSNYSIDALYQFLFEFIFDIEERYIRMYVQLSNTPEEFSGNIYGQIQDLNQSLSKEIAKFYDESKIKMTKEDFQNLILLFLESWYLKASFSQKFGAVEESKSQFKDEVYSLLNIFLKK
The following text describes a protein:
Function:
Transcription factor that binds to DNA at the consensus sequence 5'-AACAAT-3'. Binds to the proximal promoter region of the myelin protein MPZ gene, and may thereby be involved in the differentiation of oligodendroglia in the developing spinal tube. Binds to the gene promoter of MBP and acts as a transcriptional repressor. Binds to and modifies the activity of TCF7/TCF1, thereby inhibiting transcription and modulates normal gamma-delta T-cell development and differentiation of IL17A expressing gamma-delta T-cells. Required for the differentiation of Vgamma2-positive gamma-delta T-cells, a subset of IL17A expressing gamma-delta T-cells. Regulates expression of BLK in the differentiation of IL17A expressing gamma-delta T-cells. Promotes brown adipocyte differentiation. Inhibitor of WNT signaling (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MSMQSPVSVQLAPDSASTMVNCTIKSEEKKEPCHEAPQGAAPAVETQPGDPALASQDATNAKAPPQDCASPESSGSPEPKRPAASEAASGSQERLDFNRNLQEVVPAIEKLLSSDWKERFLGRSNVEAKDVKGTQESLAEKELQLLVMIHQLSALRDQLLTAHSEQKNMAAMLFEKQQQQMELARQQQEQIAKQQQQLIQQQHKINLLQQQIQQVNMPYVMIPAFPPSHQPLPVTPDSQLALPIQPIPCKPVEYPLQLLHSPPAPVVKRSGVAAHHPLQEPPQPLNLTAKPKVPELPNTSSSPSLKMNSCGPRPASHGAPTRDLQSSPPSLPLGFLGEGDAVTKAIQDARQLLHSHSGALENSPNTPFRKDLISLDSSPAKERLEESCVHPLEEAMLSCDMDGSRHFSESRNSSHIKRPMNAFMVWAKDERRKILQAFPDMHNSSISKILGSRWKSMTNQEKQPYYEEQARLSRQHLEKYPDYKYKPRPKRTCVVEGRRLRVGEYKALMRTRRQGARQSYTIPPQAGQAQVSSDILFPRAAGLPLARPLVEHYDPQGLDPNMPVIINTCSLREEGEGTDDRHSVADGEMYRYSEDEDSEGDEKSDEELVVLTD
The following text describes a protein:
Function:
Small GTPase that cycles between an active GTP-bound and an inactive GDP-bound state and mainly functions in vesicle-mediated endoplasmic reticulum (ER) to Golgi transport. The active GTP-bound form inserts into the endoplasmic reticulum membrane where it recruits the remainder of the coat protein complex II/COPII. The coat protein complex II assembling and polymerizing on endoplasmic reticulum membrane is responsible for both the sorting of cargos and the deformation and budding of membranes into vesicles destined to the Golgi.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein.
Sequence:
MFLVDWFYGALASLGLWQKEAKILFLGLDNSGKTTLLRMLKDERLVQHPPTQFPTSEELSIGKIKFKAFDLGGHRIARRVWRDYYAKVDAVVYLVDAYDKDRFAESKKELDALLMDELLANVPFLVLGNKIDYPSAVSEDELRYYLGLANFTTGKGDVSLAGTNVRPLEVFMCSIVRKMGYGEGFRWLSQYIK
The following text describes a protein:
Function:
Required for electron transfer from ubiquinol, via NapC, to the periplasmic nitrate reductase NapAB complex.
Subcellular Localization:
Periplasm.
Sequence:
MSRSAKPQNGRRRFLRDVVRTAGGLAAVGVALGLQQQTARASGVRLRPPGAINENAFASACVRCGQCVQACPYDTLKLATLASGLSAGTPYFVARDIPCEMCEDIPCAKVCPSGALDREIESIDDARMGLAVLVDQENCLNFQGLRCDVCYRECPKIDEAITLELERNTRTGKHARFLPTVHSDACTGCGKCEKVCVLEQPAIKVLPLSLAKGELGHHYRFGWLEGNNGKS
The following text describes a protein:
Function:
Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool.
Sequence:
MRINTVLFDLDGTLINTNELIISSFLHTLNTYYPNQYKREDVLPFIGPSLHDTFSKIDESKVEEMITSYREFNHDHHDELVEEYETVYETVRELKKQGYKVGIVTTKARQTVEMGLQLSKLDEFFDVVVTIDDVEHVKPHPEPLQKALELLDAKPEEALMVGDNHHDIVGGQNAGTKTAAVSWTLKGRAYLEAYKPDFMLDKMSDLLPILSNMNRS
The following text describes a protein:
Function:
Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as lamellipodial and filopodial dynamics in migrating cells. Plays a crucial role in filopodia formation, cell-substratum adhesion, and proper chemotaxis. Nucleates and bundles actin filaments. When complexed with fotH in filopodial tips, may support formin-mediated filament elongation by bundling nascent actin filaments.
Subcellular Localization:
Cytoplasm, cell cortex. Cell projection, filopodium. Cytoplasm, cytoskeleton. Note=Localizes to the leading edge of migrating cells and to the tips of filipodia. Translocates to the cell cortex in response to cAMP chemoattractant stimulation.
Domain:
The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding and actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for self-association (By similarity).
Sequence:
MSETAIFNATGQVFTYSPQTRNWVPSSNVPATLQMYFNSGANTYRVIGRAGDDPNNFLINFAVKSEVVYSRASEIFHQFTDQRTHFGINFTSKQDADTFGGGFENVLRSLKGGPQQPPPQVPKPQPQQPPQPQQPPQRPPSTVIAKPVAPQAPVAPPQAPAAAPQAPAPPAAPPAPPKPPGPPPPPPAPKPPAAGGGTGRNALLGSIENFSKGGLKKTVTVDKSAGVPTKTTPSANSAASNAGSEPSSGGSTPAPAPKSSGGGGGGDLMAEVMAKRAKMKAAASQPKEESSAPTPAPTPAPTPAPTPSSTSFKPPQSFSKPATKTAAANKPPSPSLSAPLPSTVANEDLQSLKEEILTEVRKEIQKAKDEILEAIRASQH
The following text describes a protein:
Function:
Activates the atg1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, atg13 is also required for glycogen storage during stationary phase (By similarity).
Subcellular Localization:
Cytoplasm. Preautophagosomal structure.
Sequence:
MPHYQEVDDASGDGGPMAATGPSREAVKKMDQIIQNFHTKAAIIVLGARVGLPVVFTKEGTKKVNKWFQIETDDTDAYRDELHTWRMCGGFQNRPPPLIIETYLDTSHLTSSQRLVIVDDLGKRWDALDALSNSCGSNDGRSEVILERWKIELRDIPGEQPYDFGSTLPTIYKKCIVFFRSLYSTAKLVPAWKFKKSLGKNGSPTNSLIINCRITTGDTQPRRIDGLKQPILDHSGPVTSTYVLGATDTPAGQIFAEVTYRNDCNFRVDDSESILSSRFMGADEHFFTPSLAAKGDLSRRRSTKQTEIGSLPAHKHLTDDSGPVQTYGSLSTFHGNAPPRGSSPMSALRAQRPIGSDTSSPPVGSLPYSRPSLTSKGSLKSFEGMALARRTSLSFQPFKAGSLSSSPSRATYAGETLPASPGSLPRASGISALAQARNRSSLTAGMPATLRGGPVTSDNVVPTSVSSSPKPAPIARYSSSFTHRRSRPSYGGASKLVDDDQGSSGKQSVSSSVQPGSGILAEAGAGGSSGSLQTDDDNISDFLKLLDSKKTLQSFEPSGEASKKRATAQLSKFQSMRDSHNALTDSMASSSMLQRSSSSSSRQLSSVPPMVAATSISAASSPGKPISPHTPHTPAIPSRLSANSIAEYDQPRRVTRRSRTTEARLEDVQDNDHSNDAGTNAIDIPTSPRPYYPHARRSSSVAQQHRALAIDDDLGDLPFGVHRSISLGADDREPPSLSTLLNIGQASDDVESPTGQSPSLLQPAPRISEGSTAMSRQTSSSLEAHDSEVPQLSRFSGPGSANSPYRPRIGKTGGRGVTPPQTGSFSSLLVDRGSASGSERAGGGRYSFSRGIGAYEADDEPLLFDMSEIGRDISRRSIDEPRGGYEASRGGDSGSSSRRGSRWGR
The following text describes a protein:
Function:
Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MMAASISSSPMNLPVIIGDRRPSLSLFQAQRPPTGHHRSFFSGNVALNTSSQRRPRRSCHDVVASVATTDRPVPLAGDVDRGSQPAETSGRSDDDGQLAARWREIHGSDHWEGLLDPIDAVLRGELIRYGELAQACYDSFDYDRFSPYCGSCRFPAKTFFQDVGLGGAGYEVTRYLYATSNDLKLPNFRSRKHRSAAAAADKLWSEMGTFIGYVAVSTDEETARLGRRDIVVSWRGTVTRLEWVADVTANQTRLSGMGVPCPDPDVKVEMGFAELYTGKDAACRFCRYSAREQALAEVRKQVEVYHGRGEQVSVTVTGHSLGSALAMLNAFDIAETGANASPEPELDDDGRRCRKAQAPVCVFSFAGPRVGNLRFRERFERELGVRALRVVNVHDGVPKVPGVFFNEAAFPEAVLRAVDGLGAAGVYTHLGVPLALDHRASPFLKETMDISCYHNLEAHLHLLDGFRGSGEVFQLRGRDPALVNKSADFLRDEHMVPPVWYQEENKGMVRTEDGRWVLPPRHRDIDEHPDDTDHHLQQLGLALNAST
The following text describes a protein:
Function:
May play a role in innate immunity in mouth, nose and lungs. Binds bacterial lipopolysaccharide (LPS) and modulates the cellular responses to LPS.
Subcellular Localization:
Secreted.
Sequence:
MAGPWTFTLLCGLLAATLIQATLSPTAVLILGPKVIKEKLTQELKDHNATSILQQLPLLSAMREKPAGGIPVLGSLVNTVLKHIIWLKVITANILQLQVKPSANDQELLVKIPLDMVAGFNTPLVKTIVEFHMTTEAQATIRMDTSASGPTRLVLSDCATSHGSLRIQLLHKLSFLVNALAKQVMNLLVPSLPNLVKNQLCPVIEASFNGMYADLLQLVKVPISLSIDRLEFDLLYPAIKGDTIQLYLGAKLLDSQGKVTKWFNNSAASLTMPTLDNIPFSLIVSQDVVKAAVAAVLSPEEFMVLLDSVLPESAHRLKSSIGLINEKAADKLGSTQIVKILTQDTPEFFIDQGHAKVAQLIVLEVFPSSEALRPLFTLGIEASSEAQFYTKGDQLILNLNNISSDRIQLMNSGIGWFQPDVLKNIITEIIHSILLPNQNGKLRSGVPVSLVKALGFEAAESSLTKDALVLTPASLWKPSSPVSQ
The following text describes a protein:
Function:
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
Sequence:
MFKVNNSSNHNGGGALVVSSLKQKMQTLREELERYKDLYDDKCREVNRERSLRNDAESQVMALTRRVELLEDERDEMDRRYSSVLNKLNDASKVVDEFERLKISNECFKNLDDEKISSLEDQIRTLRLAADTAEKKYDEAVRHLHMLELELGKSEERCELAESKARQLDNNLHILTSNLRSLEISEQTWRIWGEGLALWWVVFFRKLASKEDSYTSTIADLRRSLKESEMCIDVLKRELKSKQQELDKSEGKLVKE