lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cell projection, cilium.
Sequence:
MLAGALAVVGLVLLGLHAARGRDHLPFAAVLAGAVVAVLVLAVLCNRADFHQDQLGLACYALMAVLLAVQAAGILLPPPPPHSASDGLWWTVFCVYTVYTLLPVRMRAAVLSGLLLSAIHLGLALRARAHDRALLRQLVSNVLIFSCTNLVGACAHYPAEGSQRQAFQETRQCIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAVSVPTSLPPSLLSLLLPSLPPSVCPCRPLTFPCRPLLPSTARNLPLLQSFCPCPPSRPVSSPAAFCHPLPSSYLPVPSPDGFCLPLSPSATLCRPLLSSVCPCRPLPVPAPSVAPFCPLSVSATLCRPLPVPASLCPSLPSVTPSRPLPPSAVLLPSPAIPCHPLPPSVSPCRLLSLLDFPCRLPLPLPSPASLCRPLPPSLCPCLPLPSPPASCCPLPPCWLPQGSCPGRGLVGQEPGLRAAGPPEAPPPPPPPSASLPSDARLCAGQQGAGHGHPAGRRPKRRCVPGWSRAPPPPQENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANQMEAGGAAGRIHITKATLNYLNGDYEVEPGSGGERNAYLKDHNIETFLIVRCSQKRKEEKAMIARMNRQRANSIGHNPPPWAADRPFYSHRGGGHQVSKEMKRMGFEDPKDKNTQENMNPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEQKYSKQVDGRFGAYVACASIVFLFICLVQMTVVPHSRFMLGAYLAAALMLTAVVFVSGVYTCTTLCPAPLQSLSRKIVQSRRNSTAVGVCTISLVFLSAFVNMFTCSRVDLLSCLAAEHNVSRNEVNACHVLASEFNFTLGAELTSCGSSQPQCHFPEYFTYSVLLSLLACSGFLQMSCPGKLALLLVAEAVYVLIVEGPAAALFDNADLLNAAADVLDFQNGTMECHPQETKVSLKIVTPLVISVFVLALYLHAQQMESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKAGKTHIKALADFAMKLMDQMKHINEHSFNNFQMKIGNGATGGLGWGLGVAGLSAWGPGMEVYR
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MEVDGETQIEELECDIRTLRKQLKAKVQQLKTLKKHFQKNCINKLNNNEIARYSRQIILSEIGVQGQLKLKRSSVLVVGAGGLGCPSALYLAGAGIGRIGILDYDEVELTNLHRQLLHTECSVGLTKVESVRSYLEELNSQIEIVTHHIQLTSDNALQTLESYDIVVDATDNVATRYLLNDACVLLKKPLVSGSALQLEGQLTVYNFNGGPCYRCLFPNPPPPETVTNCGDGGVLGAITGVIGALQALETIKIILGNSGVLSGRLLLFDGHQSTFRNLKLRPKKADCAVCSDNPSLTKLIDYEQFCSMKATDKDSHLNLLAPHERITVQEYKSLAESNVPHLLVDVRGANQFEICQLPASINVPIDDILKNRRTAEVTQLAATGGPVFVVCRRGNDSQLAVRHLSQLFQEQGLAPPRDIVGGLHAWTHNIDPEFPIY
The following text describes a protein:
Function:
Involved in vesicular trafficking at the Golgi apparatus level. Involved in endosome-to-Golgi trafficking. Mechanistically, captures transport vesicles arriving from endosomes via the protein TBC1D23. Recognized vesicles are then tethered to the trans-Golgi before subsequent SNARE engagement and vesicle fusion. Selectively regulates E-cadherin transport from the trans-Golgi network in tubulovesicular carriers.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle, acrosome. Golgi apparatus membrane; Peripheral membrane protein. Golgi apparatus, trans-Golgi network membrane.
Sequence:
MFTKLKKRIEEENQTELNIGIPTSLPSPTPTHSRRASESGVNTPVRSTCSEASDSDREQKTKEKEDLERRLRESEHRVELLASQRENREELESFQSQEMAKVKHLLLCSQQELRAADEKLRQRSEECRLAQERVLELERASQKVQGDQGRNKELLKEKATLDAEVDRLKQEALQNSGRISQLECTLGNLTDEHDGLKHTHDLYKSRTTSLLAEKDSSICTLEDRVQTLEKRLDGAGLTGDEQVQSLVQERKVLEKKLDESRQHLSEVKSSWSEKINNLETQIFNLNQKMAEDAQECRRMEREVEELALKLKTSEQHGWVLEEQLQQKTAELAALHRSKEEELRRQRSQQDAQLDELRLQVAALRSDLSQAHKDRDREAQEAQARINALETSQTEFVEREIETEKQVTALENAGRQLKVAQLEKELSVVTESEASLKLTIKRVKAEIKAMAEEVDELRLRNASLSGENERLKQEAGESRLQGDEERRDFERELEGLRAALREATSKLQSLESQASASAESSVSQEELRAKVAQLEDQLLERNKAMKLQQQRISDMKKTIQRELKCQQNTGGEGIQSNDTVPEHGNIASAGDAVATRGSANATSARPGNHCLEGSKLEEDINFKYLKHVVFKFMTSKEYEAQHLIRAVSVLLRFTADEEQLIREHLDWKSSWFGSRPHPHHQPLPPHLPQPHHASHRHQPQQHQHRSSVALGAHSKAGTRPS
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Sequence:
MKSMTGLILASSLSLALSACDGSGDEQTPSIPTPDPTPPTLAADVCYLMSTTKGDITLAIDLTNTPITGKNFKQYVDKSFYNGTLFHRTINNFMIQGGGFTTGLQSKPTNAPIKNEASVGISNKRGTIAMARTPVSDSATSQFFINVLDNPQLDASASSYGYAVFGKVVEGMDVADQISIVPTKTSNGFSDTPVKEILINSVKETTCPAA
The following text describes a protein:
Function:
Transcription activator. Binds to 5'-CAACTGTC-3' and/or 5'-TAACAAA-3' motif in target gene promoter (e.g. alpha-amylase) to promote their expression. Positive regulator of abscisic acid (ABA) responses leading to growth arrest during seed germination. Promotes the expression of aleurone-related genes (e.g. CP1, CP, GASA1, BXL1 and BXL2) in seeds. Together with MYB33 and MYB65, promotes the programmed cell death (PCD) leading to vacuolation of protein storage vacuoles (PSVs) in the aleurone layers during seed germination. Maybe involved in the regulation of leaves lamina morphogenesis. Involved in pollen grain development. Together with MYB97 and MYB120, functions as a male factor that controls pollen tube-synergid interaction in fertilization. Required for pollen tube growth arrest and sperm cell release in the female gametophyte, probably via the regulation of pollen tube-specific gene expression.
Subcellular Localization:
Nucleus. Note=Detected in the vegetative nucleus of mature pollen grains and pollen tubes.
Sequence:
MDGGGETTATATMEGRGLKKGPWTTTEDAILTEYVRKHGEGNWNAVQKNSGLLRCGKSCRLRWANHLRPNLKKGSFTPDEEKIIIDLHAKLGNKWARMASQLPGRTDNEIKNYWNTRMKRRQRAGLPLYPHEIQHQGIDIDDEFEFDLTSFQFQNQDLDHNHQNMIQYTNSSNTSSSSSSFSSSSSQPSKRLRPDPLVSTNPGLNPIPDSSMDFQMFSLYNNSLENDNNQFGFSVPLSSSSSSNEVCNPNHILEYISENSDTRNTNKKDIDAMSYSSLLMGDLEIRSSSFPLGLDNSVLELPSNQRPTHSFSSSPIIDNGVHLEPPSGNSGLLDALLEESQALSRGGLFKDVRVSSSDLCEVQDKRVKMDFENLLIDHLNSSNHSSLGANPNIHNKYNEPTMVKVTVDDDDELLTSLLNNFPSTTTPLPDWYRVTEMQNEASYLAPPSGILMGNHQGNGRVEPPTVPPSSSVDPMASLGSCYWSNMPSIC
The following text describes a protein:
Function:
Catalyzes the second reaction in the biosynthesis of heme A, a prosthetic group of mitochondrial cytochrome c oxidase (CcO). Heme A is synthesized from heme B by two sequential enzymatic reactions catalyzed by heme O synthase (HOS) and heme A synthase (HAS). HAS catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8, in a reaction that involves matrix ferredoxin and ferredoxin reductase. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Domain:
The N-half (TM1-TM4) and C-half (TM5-TM8) domains are connected by an intracellular loop. Each domain is formed from four-helix bundles and they align in a pseudo twofold symmetry manner. The N-half domain is the substrate heme O binding domain and the C-half domain is the cofactor heme B binding domain.
Sequence:
MQRLLLPSLRALTGSRNVGLLVPRVASRTQCGSSCGSQRPLRPGQYSTITEVALQSGKGTVSLPSRAAERAVGRWLLVCSGTVAGAVILGGVTRLTESGLSMVDWHLIKEMKPPTSQEEWEAEFQKYQQFPEFKILNHDMTLAEFKFIWYMEYSHRMWGRAVGLAYILPAAYFWRKGWLNRGMKGRVLALCGLVCFQGLLGWYMVKSGLEEKPESYDIPRVSQYRLAAHLGSALVLYCASLWTSLSLLLPQHKLPETRQLLWLRRFAGGTAGLVFLTALSGAFVAGLDAGLVYNSFPKMGESWIPEDLLTFSPVLKNVFENPTMVQFDHRLLGVTSVTAITVLYFLSRRIPLPRRTKMAAVTLLALAYAQVALGISTLLMYVPTPLAATHQSGSLALLSGALWLMNELRRVPK
The following text describes a protein:
Function:
This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
Sequence:
MIEREINSVNDNPLIDVSRNKAIHGGNFQGTPIGVSMDNTRLALGSIGKLMFAQFSELVNNYYNNGLPSNLIAGRNPSLDYGFKGAEIVMASYCSELQFLANSVTNHVQSADQHNQDVNSLGLISARKITEAVDILKLMSSTYLVALCQDIDLSHLEENLKSVVKTTVSQVAKRTLTIGAIGELHPARFCEKELLRVNGESEKNVNSSIFQKIGAFEDELNVLLPKEVETARAVLESGNPSIPNRITECRSYPLYRLVRQQLGTELLTGEKFRSPGEEIEKVFTAMCNGQIIDPLLECLKSWNGAPLPIC
The following text describes a protein:
Function:
GTP-binding protein that functions in the development of root systems, which are mediated by auxin. Acts as a cell cycle regulator during root development. Proteasome-mediated degradation of the protein is necessary for the transition of metaphase to anaphase in mitosis.
Miscellaneous:
MISCELLANEOUS: Overexpression results in reduced growth of the primary root, an increased number of adventitious roots, a helix primary root and a delayed gravitropic response of roots in seedlings.
Subcellular Localization:
Cytoplasm. Nucleus. Note=During mitosis, associates with mitotic spindles.
Domain:
D-box [RxxLxx(L/I)xN] is the common motif recognized by the E3 ubiquitin ligase APC specifically acting during transition from metaphase to anaphase.
Sequence:
MSGVWVFKNGVVRLVEKQQATAGTAVAGGRRKALVHTPSGQVVSSYAALEARLTALGWERYYEDPSLFQFHKRGSLDLISLPADFSAFSSVHMYDIVVKNRDSFRVVDA
The following text describes a protein:
Function:
Putative mannosidase involved in glycoprotein quality control since it is involved in the targeting of misfolded glycoproteins for ER-associated protein degradation (ERAD).
Miscellaneous:
MISCELLANEOUS: Present with 71 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MSIARLVYSLFRRVRSVLLLFITISLLFYYTFQNEIDILNSYALNDSLPSINNYEHNTEGSSKLDPPDLSSTGSDRIATDKENGNVAVDLSDPATLREKNKYFPLLLKGSSHQIGSNLPISSLLTYKEKYPVLFEYSSPSLTSISQNDVHKIQPAMQLPPDVDMIKQIKDIFMKSWNQEQLLLKSNLRRESTWPIDLIDSLDTLYLCGETKLFQDSVNIIEDFDFRVPPLAMEVIDIPDITTRVLEGLLSAYELSMDKRLLNKAKHVADFILRSFDTPNRIPILKYFWKSDLRNRFPDRTVPSGQLTTMALAFIRLSQLTRLNKYFDAVERVFTTIRQSYNEFDMEFMLPDVVDASGCQLLTQEEIENGAHLKGSSIMKSINENFKFVHCQQLGKFLNPPIDDNSLQEQSQYQAYRINEKTVPILENLFKINDLFQSSYDILDGSSKNANAATMDPSIGSEVEAVDEIIEKRNFKDGTKKDSTKNTVGDKSLIDSQTFLTNSISNIFKFMTFRPMLPKQTENKKFNFLNSILTKSQFMPTTNELDVTIRKSYDVSLYSCRLGGILGLSSRVPHRGGVNTKYILPSSLLEMSEIITESCFMLMEEFDGLLPQKFELDPCTDETNGNCEFNGETKSRMIANGEYETFENDLDVGIKVSNYGKGGNDQKAKRNVLSKDGITETQNIKGDTVGSSKSIAEIDGDEVTQIRRVFTLGKDIKPHITTDDTMGSQWKNHPDWPFWVNKVESRRLLDSNIIESIFYMYRISGEQKWRSMGKQSFGILMQELMELNSGAKGLWQIKEFYENGEKVNNDLPSYWFSRTLKYYLLLFSDGDKVSLDKHILTQGGHIIKKK
The following text describes a protein:
Function:
Putative phospholipase.
Subcellular Localization:
Secreted.
Sequence:
MLVVLLFISLSLATTSSITISLYHVGEDWTIKYVSDTEAVAIATYVTSKEAKGYNELSVHTNKKYSDKEQMFATGFADGFFSGNNINFHKENMNAWYLDHYLGKAKDYPKSLYKYLQDNIDYINTQIKANPEDQYWVSVDLIMEQVRGVTAGHNFAVKASESMTFYDMFFYESFGDLLDLTAVLPADDEVNGIERPKWFIKYANNDIDWHLNWKLRTKCSGLIRYVKENHDIYVSQVAWFMYGAMNRVMKHFDINLNNEYLSAKKVSFSSYPGFVFSFDDFYMTSNDLAIIETTFTNFNTTLNQYIHSNTLLDWIRIVLAVRASKNGKEFHDIFEKQNSGTYNNQWIVVDYKLFNSVESGIPEGTLTVSEQIPGYVFYKDFSTSLESTGYFGSFNVPEIQKTIDMSNTTANAQGNKAFWNSPTECCRAKIFEKYAPKVMNMNDMKKMMKYNDYKNEPLSKDPTTELQDPGATIAARYDLRPSELKPLPFGQMDAKICDKSGFETLQFHVQAGPTHDNQPYLDLEVYEKQGWFVPDKGVLKVWNFDWEEFIPK
The following text describes a protein:
Function:
Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
MSILEEIKKEVRVLCWIMTSPSSLRPKATHVKQTWXPRCDVTLYMSTQADPEFPAIGLDVSEGRDYLWNKTRTAFRYVYRHHFQDADWFMKADDDXYVIVDNLRYFLRDKNSSAPLYYGHHFTPYVKQGYMSGGAGYVLSREALKRFAEADNYRCSKQDYKAEDVGMGFCMQSLEVIAXDSRDSLNRSRFLPLSLVDFVNITYRTGITSTGSTKYPENYRKNPFGFQTIERFKLKNRLYSSSSSSSSSNAGSTATQLLHNNSCIGNRSINNFTPAAARTLSTTSNSSNCSNRYSSGSSCCSDYLISCHYVTSYDMHLLDFVVYHLRSANDNKRHVYKIGNNRTLPL
The following text describes a protein:
Function:
Restriction of 5-methyl and 5-hydroxymethylcytosines at the specific DNA sequence 5'-C(me)CGG-3'.
Miscellaneous:
MISCELLANEOUS: Encoded by the SOS-inducible cryptic lambdoid prophage e14. UV treatment leads to prophage excision and reduced levels of McrA.
Sequence:
MHVFDNNGIELKAECSIGEEDGVYGLILESWGPGDRNKDYNIALDYIIERLVDSGVSQVVVYLASSSVRKHMHSLDERKIHPGEYFTLIGNSPRDIRLKMCGYQAYFSRTGRKEIPSGNRTKRILINVPGIYSDSFWASIIRGELSELSQPTDDESLLNMRVSKLIKKTLSQPEGSRKPVEVERLQKVYVRDPMVKAWILQQSKGICENCGKNAPFYLNDGNPYLEVHHVIPLSSGGADTTDNCVALCPNCHRELHYSKNAKELIEMLYVNINRLQK
The following text describes a protein:
Function:
Metalloprotease with endopeptidase activity. Specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues (By similarity). Mep72 appears to be a secreted biofilm-specific regulator that affects the processing of a very specific subset of virulence factors exported by the type III secretion machinery as well as flagellar proteins. Binds directly to ExoS and PcrV and affects the processing of these proteins in the biofilm secretome, but contrary to expectation, Mep72 seems to protect these targets against proteolytic processing/degradation.
Subcellular Localization:
Secreted. Note=Is secreted through the type II general secretory pathway (Xcp system) and undergoes processing during export.
Domain:
Has a tridomain structure comprised of an N-terminal metzincin protease-like domain and two tandem C-terminal carbohydrate-binding domains.
Sequence:
MKKSLLCSTLALAVASAAQAAPKTVDIMVLYTPAATQTANGRDIDARIASYIEFANTAYEKSGVNLRLRLVHKQRLDWADYPTVTGANLDRFMRDPQVQRLREQYGADLVSLVNRSQNSGNGYITCGIGYMGSGDKNSGRFHGNAKDIAYNLTGVDCGLNTFAHEAGHNMGLRHSYEQDLESSYYDPRYAHSGTYEWSRGYGVQGRFATVMAYPHAFGTNKQAPFFANPRLVNAECANQPCGREEHADAVRALNSMATQIADFRPTKVPGTVNPGSGGDTPTPPDLPWCTKAKLGGLLGDGEFASMEGWRAWSGNAQLSLVNVAKGCRDNALLVDVRGFDLLVRPIAPLRAGSGYRLSGKVMLKAANTRETVRMALLSERADGALAYNPAQSVELSVSGNEFSRLEKTFDYRPAADQRNLYVAVWSDSGASLLVDEMNLQEAQAAPPSVPPAPKRIAYDFESGIGGWSGVHASARATRVASAGRLALEAYQRRYAGTGASTSLLGNLEAGRTYAFSADVRVGDGRGSQAMTYAYLYLESQGRPGEYLPLGYKVVENGRWASLRGQVQLPKGPIKRAELMILSGNQQESMFIDNVQLLQK
The following text describes a protein:
Function:
Probable transcription factor that may function in the maintenance of the proper function of the central cell in pollen tube attraction.
Subcellular Localization:
Nucleus.
Sequence:
MVPKVVDLQRIANDKTRITTYKKRKASLYKKAQEFSTLCGVETCLIVYGPTKATDVVISEPEIWPKDETKVRAIIRKYKDTVSTSCRKETNVETFVNDVGKGNEVVTKKRVKRENKYSSWEEKLDKCSREQLHGIFCAVDSKLNEAVTRQERSMFRVNHQAMDTPFPQNLMDQQFMPQYFHEQPQFQGFPNNFNNMGFSLISPHDGQIQMDPNLMEKWTDLALTQSLMMSKGNDGTQFMQRQEQPYYNREQVVSRSAGFNVNPFMGYQVPFNIPNWRLSGNQVENWELSGKKTI
The following text describes a protein:
Function:
Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MLTPFCSSHHLQEKMNSCQSNPTKMDNSENVLFNDQNENFTLVAPHPSSSYLTRDQEHEIMVSALRQVISNSGADDASSSNLIITSVPPPDAGPCPLCGVAGCYGCTLQRPHREVKKEKKYKGVRKKPSGKWAAEIWDPRSKSRRWLGTFLTAEMAAQSYNDAAAEYRARRGKTNGEGIKRRWR
The following text describes a protein:
Function:
Essential protein. Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites (e.g. psbA and psbD) and are then released. Essential for blue light-mediated transcription of psbD, which encodes the photosystem II reaction center protein D2. Plays a role in reproduction. Required during female gametophyte development.
Subcellular Localization:
[Isoform 1]: Plastid, chloroplast; [Isoform 2]: Mitochondrion.
Sequence:
MGVVSISSSAARSPLGLGNDLLTHRSSLKKPSIVAFKADDSSNSALIIPPREQVLIPAEKHNEKKREVTRRKPCKTPKKPLSLEHNSAPSCSLGVDYNEAAARLESIYKLSPATTTLVEDDVEDGGSKAKVSRRRKRKESGEEKKVVVRNNVKKEKRMSLDKRIALKRNVQEKPVVASVDKKVTKRQQEEEKIERLVRDYSASNDIVSLDWKKMKIPPVLSSTEHAWLFKLMQPMKALLEVKDVLQKSLGREPREAEIAGEINMTAGEVKKKIEIGRAARNKLIKHNLRLVLFVMNKYFHEFTNGPKFQDLCQAGMRGLITAIDRFEPKRKFRLSTYGLFWIRHAIIRSMTTSNFTRVPFGLESVRVEIYKAKTELWFEMGRPPTEDEVVERLKITPERYREVLRAAKPVLSLNSKHSVTQEEFINGITDVDGVGANNSRQPALLRLALDDVLDSLKPKESLVIRQRYGLDGKGDRTLGEIAGNLNISREMVRKHEVKALMKLKHQARVDYLRQYIV
The following text describes a protein:
Function:
Probably plays a role in germ plasm formation, positioning and maintenance.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Unlike the transcript, the protein is not exclusively localized to germ plasm but is also present in the nuclei of early oocytes, of later stage primordial germ cells (PGCs) and of some somatic cells, as well as in their cytoplasm.
Sequence:
MALKAEDSFDIYSQLIQSFCRYAENTTVSESQSPAFNAQKEFQTCQDHACCTHSEAHTHILMQQWQLLEEQWEYIDHLKTDVAALKQLLHGFMNSLSGTDSGMEGTNHFLPPHQNPTLLKDEEIVASALNRPSVDINGFEENITTGAQIHAAFTKSPKKMPATSTPRKSEVLWSCSPTLATDGYFMLPDIILNPLDGKKLVSMLRSSNYEPHRFAELLFQHHVPHSLFQLWANKVNFDGSRGKLGLPRNLMIDILHQTSKRFVLGPKEKRKIKTRLNLLLRTRQDRAWWDVGL
The following text describes a protein:
Function:
Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSDKPDLSEVETFDKAKLKKTNTEVKNTLPSKETIQQEKEHNERT
The following text describes a protein:
Function:
Recruits the lipid transfer protein VPS13 to endosomal and vacuolar membranes.
Subcellular Localization:
Endosome membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein.
Domain:
The PX domain binds phosphatidylinositol 3-phosphate (PtdIns(3)P) which is necessary for peripheral membrane localization.
Sequence:
MPHIQFLPPEPVVLVSRVADDPDPAGPGLHVAKVAVGDCTIVDARTPCAPLQGRFAVWTVALQLHSPDTPRSLTLRKRYSDFVRFRERLLLCLPPPLRRAVPPLPPPVPWYDAWRYSDVNLDRAWLAARRAGLERFLQQVLLNRALVAAAPVVVRGFLEPPAAHRWVPVRA
The following text describes a protein:
Function:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Subcellular Localization:
Nucleus.
Sequence:
MHNPGADGTQVSPGAHGPSLPGTGCPRPRTDTPGPQPQPMDLRVGQRPLVEPPPEPSLLALQHTQRLPHHLFLGAVQPQRSVEPMRLSMDTMPELQVGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALEKTVHPNSPSVPYRTLEPLETEGAARSMLSSFLPPVPSLPSDPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPVLGSEALLGQRLRLQETSLAPFALLPTITLGLPAPARADGDRRTHPTLGPRGPVLGPHAPLFLPHGLEPEAGGPLPSRLQPILLLDPSVSHAPLLTVPGLGPLPFHFAQSLMTSERLSGSGLHRPLSRTRSEPLPPSAPLGALQPRLERLKPHVQLIKRPAKPSEKPRLRQIPSAEDLETDAGGLGPVGEDGLEHRESSHGQHEARGPVPLQQHQQVFLWEQQRLAGRLPRGGAGDPVLLPLAQGGHRPLSRAQSSPAAPASLPTPEPPSQARVLPSSETPTRTLPFTTGLVYDSVMLKHQCSCGDNSRHPEHAGRIQSIWSRLLERGLRSQCESLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQGKAGKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRTVVMPIAREFSPDLVLVSAGFDAAEGHPPPLGGYHVSAKCFGYMTQQLMSLAGGAVVLALEGGHDLTAICDASEACVAALLGNKVDPLSEEGWKQKPNLNAIRSLEAVIRVHSEYWGCMQHLASCPDSWVPRVPGADAEEVEAVTALASLSVGILAEERTSVQLVEEEEPMNL
The following text describes a protein:
Function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
LDSIICGVCCFTLLINLTSCFDWASSVAQLKAVAKTEQVLVSRLQNFINNKTEELGRIQNYVDALRKVSDKISSSKEEYISHPINQYHLIQRFAKEWTKVGDLLQMFNETGFELTQNISRMRKLYPTDNDLNPAAAGIERLQRVYELSIDELIEGNVKGINTRNSINVNDCFLIGKISCKSFKCDACKIWMQRALKLKADETFTNDEALAYEAVCRAKRGNLTHAFAITEDLLTRDPFNDILLGNMLYYRFVLGKLNILYPCFITIKVDYPHLFIFHKDENAEDEIKQYNQICQGKFKLPHKVSKNLRCYLYTNKNDPRLRIKPVKVEELCNSPHIVQFYDVINNDDIETIKKMSKKHLSRALVTGPNNTGIVEDIRTSKVAWFKKNDFTAVKKLYTRISEMTGLSEETFEDLQVANYGLAGEYQPHFDYTEDPSIYKREDGAEVGNRIATMLLYLNDVKEGGRTAFIEPKIVAKPIKGSAVFWYNLYPSGLGDPRTRHASCPVVIGNKWASNVWVHEVQQEFKRKCGLRQDAD
The following text describes a protein:
Function:
Alkaline phosphatase with broad substrate specificity. Has phosphatase activity towards nucleotide phosphates with a preference for ATP. Active towards a great variety of phosphomonoesters with the exception of 2',3'-cyclic AMP and myo-inositol hexakisphosphate.
Subcellular Localization:
Periplasm.
Sequence:
MLTPKKWLLGVLVVSGMLGAQKTNAVPRPKLVVGLVVDQMRWDYLYRYYSKYGEGGFKRMLNTGYSLNNVHIDYVPTVTAIGHTSIFTGSVPSIHGIAGNDWYDKELGKSVYCTSDETVQPVGTTSNSVGQHSPRNLWSTTVTDQLGLATNFTSKVVGVSLKDRASILPAGHNPTGAFWFDDTTGKFITSTYYTKELPKWVNDFNNKNVPAQLVANGWNTLLPINQYTESSEDNVEWEGLLGSKKTPTFPYTDLAKDYEAKKGLIRTTPFGNTLTLQMADAAIDGNQMGVDDITDFLTVNLASTDYVGHNFGPNSIEVEDTYLRLDRDLADFFNNLDKKVGKGNYLVFLSADHGAAHSVGFMQAHKMPTGFFVEDMKKEMNAKLKQKFGADNIIAAAMNYQVYFDRKVLADSKLELDDVRDYVMTELKKEPSVLYVLSTDEIWESSIPEPIKSRVINGYNWKRSGDIQIISKDGYLSAYSKKGTTHSVWNSYDSHIPLLFMGWGIKQGESNQPYHMTDIAPTVSSLLKIQFPSGAVGKPITEVIGR
The following text describes a protein:
Function:
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKKKNIILISVLLGALLLLTGCSMDPSQNTDGFFSTYLIQPFTSFIMFVAKFVGGNYGIAIIITTLLIRALIMPLNLRTAKAQMGMQSKMAVAKPEIDEIQARLKRATSKEEQATIQKEMMAVYSKYNINPMQMGCLPLLIQMPILMAFYYAIRGSSEIASHTFLWFNLGSPDMVLAIIAGLVYLAQYFVSMIGYSPEQKKQMKIIGLMSPIMILFVSFTAPSALALYWAVGGLFLAGQTLLTKKLYMNKHPEIKVMEQEEKEFEQIVEEQKKEK
The following text describes a protein:
Function:
Repressor of jasmonate responses.
Subcellular Localization:
Nucleus.
Domain:
The jas domain is required for interaction with COI1.
Sequence:
MAAVLLSDIMAQNNNNNSNASDDVKPTILHDFLGRGCAPVTKIAAASDVASASSPSASVSGGGGGGRGGGPVSTTSDLGSERQAGLHLEGVPFYGQKTDFSTSQIRYSGTKRSNSDSIFMAPSREAIPQLRPDFPETSHLMKMLRNVGGERHRWPHEDESFMGMHQMRPTSSSSSLMLQQQQQQPGKPDHANSSKWERAIPVNVGPVLQYPPPAAAQVVQYKYQPVQNRFKDANSNMNVNVNVGPSLISQSAADEGSRTGIKGSGILSSSGNGGGGGGVAEPGGSKQKSVIGNTDSGSTPTRQMTIFYGGQAHVFDDVHPNKADVIMALAGSNGGSWSTSFLPNPPVKPSGGQVMKDGEQKSEEKQ
The following text describes a protein:
Function:
Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
Subcellular Localization:
Mitochondrion. Nucleus. Chromosome.
Sequence:
MKRRCTSNNESPKIDAGLEAKYWKLKVSNVVTSVETASKECSDNDNNVCSLINWDEEWHDMHCNTVHQHFTLDLSTWKRCSVLTIDQLENGTIKVSLQDSHSEEKAICQLFPPWNMIQCITHGLIVSVLAMKVSPSSSHFVVNADFGFFVTDPDRLVSGTTVVGSLFCHRRGVLQELFRMSESENTQMVIGTVVHYIFQRCLLDKSCKLLTHVETIAKKVMKTKKVISSLYEVNLSTKEAFSLLGPYLKEIETFLNKHFNHRSIQTDTETIAICEVNDIEENIWCHHLGVKGRIDATVSVSSDATKKTFEIMPLELKTGRASYSFEHLGQLALYQMMMNLVGHEVNAGLLLYLKEGKCSRVTANRNMKRDLIILRNEVARSLSKWMVKDNITQKGSLAMKPTLPDPINNERACTKCPYNTVCITLLKSEREGTVTNYGLSILAEEACGHLRTKDVDYFIQWSGLIYLETHDETVQSRNVQNMWNSSPKERAETGRCIYGLILVSPVRIVDDLYFHTFKLEAASSTLPKALDTFQVGEYIICSTSKRIAVASGYIISHASNEIVVSFERDLSTNYGAETFILDQNTLYKSTFNLSNLALLLFNDDRCSQYRRIIIDREKPTFSDGFLSKSMIPKAKEILKKLNRHQKNAALKAAATKSYCLLKGLPGTGKTQTIVGLIRLLSLLGQSILLTSSTHSAVDNVLKRLLPFQDLKFIRLGSIDRIDPAVASSAEAIVTEHCDSPEKLSEVYEQYKIVGVTCQGTGHPLINKRLFDFCIVDEATQVFQPSLIRPLLRSKRFLLVGDPEQLPPVIKSVEARSLGACESMFHRLDQEGSFYILPTQYRMNRVLTKLANEFAYNGKLICGNDIVENNTINLPNLENIRRIYEVERWLLKMISNQIDLSVVLVDTGNTYQMNLNYRKLNEISTSITDDQSKNAMNCTNVSEIAIVVYVSWAFLQAGVEPESIGIIAPFRAQVELIRKLMKKLFEKQKYTRHSSSSNHNVIYTKENVEQLNHTCNIEVNTIDQFQGKDKKIILFSCTKSSNLSDDIWINKGKERSSHGYEILSDKSRLTVAITRAKEKLIIIGDRLTLDSYAPFKKLFNVASKISNISLREKKDGFEWNALLEFLISLSD