lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes.
Subcellular Localization:
Chromosome, centromere. Nucleus.
Sequence:
MSAPGMRTSDTLGCRSRLCELNHSATGPALGFFLSAEAGHRAPARTAARRSPDARAQAGTAGRSAPARSARGGGERVGAEGGEAVPGVPALPARSRSARSAPLAWLPAPRAAALPAHRARAARPRPRPPPAARRPQPGAAPAGTPEGAPGPAGSFPARRPASRFVSGGARGRGRQVPPAAGPGPPPRGGGGGAGPRGGGRARMGPKRRQLTFREKSRIIQEVEENPDLRKGEIARRFNIPPSTLSTILKNKRAILASERKYGVASTCRKTNKLSPYDKLEGLLIAWFQQIRAAGLPVKGIILKEKALRIAEELGMDDFTASNGWLDRFRRRHGVVSCSSVARARSRSAAPRAPAAPASPPAVPSEGSGGSTTGWRAREEQPPSVAEGYASQDVFSATETSLWYDFLPDQAAGMCGGDGRARRATQRLSVLLCANADGSEKLPPLVAGKSAKPRAGQAGLPCDYTANSKGGVTTQALAKYLKALDTRMAAESRRVLLLAGRLSAQSLDTSGLRHVQLAFFPSGAVQPLERGVVQQVKGHYRQAMLLKAMAALEGQDRSGLQLSLMEALHFVAAAWQAVEPSDIAACFREAGFGGGPNATITTALKSEGEEEEEEEEEEEEEEEEGEGEEEEEEEEEGEEEEGGEGEELGEEEEVEEEGDVDDSDEEEEEEEESSSEGLEAEDWAQGVVEAGGSFAGYGAQEEAQCPTLHFLEGEEDSESDSEEEDEDEDDEEDEDEDDEDEEEDGDEVPVPSFGEAMAYFAMVKRYLTSFPIDDRVQSHILHLEHDLVHVTRKNHARQAGVRGLGHQS
The following text describes a protein:
Function:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MNKLQSIQNDVLKICKVIGIIMIISLSILKIINSNQIEPYVDEIFHIPQTIKYCEFKFKEWDNKITTLPGLYILALIYSNILSMFGIGDGIWISHCSVVVLRSFNVFCLIITFFSIYEILKISTYNLLLSPASSLSSLKINQKEVIENKNSINNTIILRTIHLSIFPIFYFFHFLFYTDVVSTCSIFLTLLFSLKNKFNLSSFFGLISVTIRQTNIIWVFFITINNILKLYEENKEKQNYIFKELNLIKDIIEFIKFSIFNLLLIIKKFIGFIMVGILFLIFLYYNGSIVVGDKSNHESSFHVSQLFYFSLITMLFSLPSILISSLLKRFGNQNEGNQNENEKKILLYDPIEFLKNINFKYLIVIIIGMVLMIWKFTYTHLFLLSDNRHYTFYIWNRFIEKYSIGRYLPIPFYCYSIWFIWKVLSENRSKLWCIFYFLSTAMVLLPSPLVEPRYYIVPFFLFQLNQFHYYNNFIIQNGTIGRFFY
The following text describes a protein:
Function:
Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MEESNLFETTLYDGELFLLPSHLQRMKASAKSLGYSWPGEQYIENKLREAVQDTSMARVRWELSKAGDVTVQIVPIQTLEKAPYTLILDKQPSSTEKNPSCINKMTNRAIYIEAMNRNDAQYSKAQDVLLYNHQGFVTEATIFNVAFHRNGQWITPSLKHGLLSGTMRKNLLENGSIHEDDKGLLQKDNLKNGEQVLLFNSFRKVCKGVLIIQPEKACELLKKKDSSEKLS
The following text describes a protein:
Function:
Plasma membrane-anchored serine protease that directly induces processing of pro-uPA/PLAU into the active form through proteolytic activity. Seems to be capable of activating ENaC (By similarity); (Microbial infection) In gut epithelial cells, facilitates human coronavirus SARS-CoV-2 infection through, at least, the cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein; [Transmembrane protease serine 4 catalytic chain]: Secreted. Note=Activated by cleavage and secreted.
Sequence:
MLQDPDSDQPLNSLDVKPLRKPRIPMETFRKVGIPIIIALLSLASIIIVVVLIKVILDKYYFLCGQPLHFIPRKQLCDGELDCPLGEDEEHCVKSFPEGPAVAVRLSKDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSSKPTFRAVEIGPDQDLDVVEITENSQELRMRNSSGPCLSGSLVSLHCLACGKSLKTPRVVGVEEASVDSWPWQVSIQYDKQHVCGGSILDPHWVLTAAHCFRKHTDVFNWKVRAGSDKLGSFPSLAVAKIIIIEFNPMYPKDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQASVQVIDSTRCNADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSDQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWIYNVWKAEL
The following text describes a protein:
Function:
May be involved in regulating immune reactivity. May play a role in modulating dendritic cells (DC) differentiation and/or maturation (By similarity). May be involved in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation; C-type lectin receptor that binds carbohydrates mannose and fucose but also weakly interacts with N-acetylglucosamine (GlcNAc) in a Ca(2+)-dependent manner. Involved in regulating immune reactivity. Once triggered by antigen, it is internalized by clathrin-dependent endocytosis and delivers its antigenic cargo into the antigen presentation pathway resulting in cross-priming of CD8(+) T cells. This cross-presentation and cross-priming are enhanced by TLR7 and TLR8 agonists with increased expansion of the CD8(+) T cells, high production of IFNG and TNF with reduced levels of IL4, IL5 and IL13. In plasmacytoid dendritic cells, inhibits TLR9-mediated IFNA and TNF production (By similarity). May be involved via its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs) in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein; Extracellular side.
Domain:
Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Sequence:
MASEITYAEVKFKNESNSLHTYSESPAAPREKPIRDLRKPGSPSLLLTSLMLLLLLLAITFLVAFIIYFQKYSQLLEEKKAAKNIMHNELNCTKSVSPMEDKVWSCCPKDWRLFGSHCYLVPTVSSSASWNKSEENCSRMGAHLVVIQSQEEQDFITGILDTHAAYFIGLWDTGHRQWQWVDQTPYEESITFWHNGEPSSGNEKCATIIYRWKTGWGWNDISCSLKQKSVCQMKKINL
The following text describes a protein:
Function:
Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular Localization:
Nucleus.
Domain:
The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence:
MAEIPQSTIEDVFDDFDGRRSGILKALTTENSEQCLVGLPNGTWQVKPPARMVSPDHPRPVSGLHFGRNRMPGQVWAASIAACWDLWLLAFALYFDGRGLPKRDRINELATVCETVKEFGASNDQSAAMMLKKPGQSKSSGTHVNSSVDESRAQKDGIGAAIEDGHNDGSSSFAQSKCEQL
The following text describes a protein:
Function:
Shell component of a type 2A encapsulin nanocompartment. Expression in E.coli generates nanocompartments with an average diameter of 25 nm. They can be disassembled by treatment with 6M guanidine hydrochloride and reassembled with cargo. The nanocompartment is probably involved in sulfur metabolism. Probably allows passage of cysteine into its interior; during growth in light the physiological pH is 8-8.4, about 30-54% of free cysteine (charge -1) would be able to pass through the shell (Probable).
Subcellular Localization:
Encapsulin nanocompartment. Note=Unlike type 1 subfamily encapsulins, the nanocompartment has a raised protuberance around the 5-fold pores.
Domain:
Has 4 domains; an N-terminal arm not found in the type 1 subfamily, a discontinuous peripheral domain (P), an elongated loop (E) and the discontinuous axial domain (A).
Sequence:
MTDNAPQLALRDVAARQLANATKTVPQLRTITPRWLVRLLHWTPVEAGIYRVNQVKDASQITVACSERDESELPETFVDYIDNPREYLLSAVNTVVDVHTRISDLYSNPHDQIREQLRLTIEIMKERQESELINSREYGLLNNVAPGQLVHTRNGAPTPDDLDELLIRVWKEPAFFLAHPQAIAAFGRECTRRGVPPATVSLFGSSFITWRGVPLIPSDKVPLENGKTKILLLRVGESRQGVVGLYQPNLPGEQGMGLSVRFMGINRKALASYLVSLYCSLAVLTDDALAVLDNVDVTQYHTYRYN
The following text describes a protein:
Function:
In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis.
Sequence:
MAHKLASSLPAWQKLQQLYDTKGKQINLGQAFKADPQRFEKYSREWSSKATDARFLFDYSKNLIDDEVLEQLLALAEQAQVKEQIDAMFSGEHINTSEDRAVLHVALRDVPGDFKINEAGVDEVKPELEHMKAFSEAVRSGAHKGYTGKNIKSIVNIGIGGSDLGPVMVTEALKPYSKRELDAYFVSNIDGTHMAETLRVCDPETTLFIVASKTFTTQETITNATTARDWFLEHAKDKAHVAKHFVALSTNVKAATEFGIAEQNMFKFWDWVGGRYSLWSAIGLSIAIVIGYDNFEQLLLGAHEMDVHFKNTPLKDNLPALMALLGIWYIDFFGKHHEILLSNFFAQPEALAFGKSEAEVKQELGAEASNEFLVKSKVFEGDRPTNSILVQKITPAALGALIALYEHKIAVQGFVWSINSYDQMGVELGKVLAKKILPLLDGSDASKLDGAGHDSSTTGLIKFFLNNRN
The following text describes a protein:
Function:
Probable transcriptional factor. Binds to the promoter of the SQUAMOSA gene.
Subcellular Localization:
Nucleus.
Sequence:
MDWNMKSHQLEWGWDNNISICSCSGLEFCRHAETFINEKEVNKAENIKHIYSVVDRFSSYSLDHGSSVKSSAEESNYGIVGSVPGFVSAERKEKYSTSGTCTRPGESSIGLNLCPANNETVTNYPVLPLSSTTAKRCRGSYHLMQNPYCQVEGCNLDLTSAKEYHRRHRICEAHSKSPMVIVAGMERRFCQQCSRFHELSEFDDNKRSCRRKLSDHNARRRRSQPEANHFSSTGRPSSFHDQQSRTSGSLSGSSSSTSNSMGKSSCRPKNIRGLNTSTSDYKLDAASNLPRRAHSLLSRNSLGLYDPTHTSMEQLIMPASVGESQPFVPVTPNWQQVSSEHFPADHQVPFYSPHCFNGSA
The following text describes a protein:
Function:
Part of the nuclear inner membrane (INM)-specific branch of the ER-associated degradation (ERAD) pathway, required for the elimination of misfolded proteins in the INM, a specialized ER subdomain. Required for ERG11 degradation. Negative regulator of SPS-sensor signaling. Together with ASI2 and ASI3, prevents the unprocessed precursor forms of STP1 and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes in the absence of inducing signals. Controls amino acid permease (AAP) gene expression in response to amino acid availability, a process mediated by the transcription factors STP1 and STP1.
Subcellular Localization:
Nucleus inner membrane; Multi-pass membrane protein.
Sequence:
MSTNILQHVKQLLHNRDVFSFFHNKTGNLNYLDNTTQKPEVFVSPNSTIVSAPTLDSFQALMEKGNFTTLQLAKVGIRMFFSYSVSKYAVLCFSTAIILNRLTVMSSLRSNSTNIRLPLWSKTLLHLVATLSLVKALLQILSQFGLMHELHVSDTDFYALSVYLFVALSDCIEIFISSTTNVPSLICSDFSIWGLSLNLYIISKMPAGQQHIGDNVELLGAVFHRLVIHLVELFHIRAYRLCGEVILNAGFFTAFVTRTYLNGLDFINICLIHNYFPGFFYISTILLASIGIFLKALFTSNPFRSLYSRYKNLEKWWRSNNYNGEEEFNEIALSLCLLLTSNDYKIFKKSDNVKSVDEVAAFSNSYVVSGHLNQLQSTPEDLLSRKEMTTDSQLPGFARTYLGLFELVRTIILTYSRLLKNLLWSKNFESSIDKKPRVGKRKKRDLNKYVTEKNYKKFLYKPDVKELNIESDLRSLELLLPEDDSSKDYFPPRKIDESVSDEEFDSDMESQLIIDEEKELTHLSSNAVDSDDLEEIAWNISMWSILNYEMDVHNKVNGPLTRSQYGKRNPQGVLVDVVIERLLHHTNSRYMYKRLNMKDDDKLEFKFDFAFDSCDEVEEMDLSCLICKVNKRNIVTWPCRCLALCDDCRISLGYKGFATCVSCDSEVKGYSKLNIV
The following text describes a protein:
Function:
Transcriptional activator. Probable component of the central regulatory system controlling transcriptional responses to Pi starvation. Binds in a sequence-specific manner to phosphate starvation-regulated promoters. Required for female gametophyte development and function.
Subcellular Localization:
Nucleus.
Sequence:
MYSAIRSSLPLDGSLGDYSDGTNLPIDACLVLTTDPKPRLRWTSELHERFVDAVTQLGGPDKATPKTIMRTMGVKGLTLYHLKSHLQKFRLGRQSCKESIDNSKDVSCVAESQDTGSSSTSSLRLAAQEQNESYQVTEALRAQMEVQRRLHEQLEVQRRLQLRIEAQGKYLQSILEKACKAIEEQAVAFAGLEAAREELSELAIKASITNGCQGTTSTFDTTKMMIPSLSELAVAIEHKNNCSAESSLTSSTVGSPVSAALMKKRQRGVFGNGDSVVVGHDAGWVMPSSSIG
The following text describes a protein:
Function:
Histone methyltransferase. Methylates in vitro both 'Lys-9' and 'Lys-27' of histone H3. Required for in vivo dimethylation of 'Lys-9'. H3 'Lys-9' methylation represents a specific tag for epigenetic control for plant development and transcriptional repression.
Subcellular Localization:
Nucleus. Chromosome. Note=Associated with chromatin.
Domain:
The SET domain is required for methyltransferase activity and ectopic effect on plant growth; In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.
Sequence:
MEQGLRSDGNNPPSIDKTRVLDVKPLRCLAPVFPSPNGMSSVSTPQPSPFVCVPPTGPFPPGVAPFYPFVAPNDSGRPGESSQQTPSGVPNQGGPFGFAQPISPVPLNSFRTPTTANGNSGRSRRAVDDDDYSNSQDQNDQFASGFSVHVNNVEDSGTGKKRGRPKKPRRAQQAEGLTPVEVDVEPLLTQLLTSFKLVDLDQVKKADGDKELAGRVLLVFDLFRRRMTQIDESRDGPGSGRRPDLKASNMLMTKGVRTNQTKRIGNAPGIEVGDIFFFRMELCLVGLHAPTMAGIDYMSVKLTMDEEPLAVSIVSSGGYDDDGGDGDVLIYTGQGGVQRKDGQVFDQKLERGNLALEKSVHRANEVRVIRGVKDVAYPTGKIYIYDGLYKIQESWAEKNKVGCNVFKYKLLRVPGQPEAFKVWKSIQQWKDGVASRVGVILPDLTSGAESQPVCLVNDVDDEKGPAYFTYIPSLKYSKPFVMPRPSPSCHCVGGCQPGDSNCACIQSNGGFLPYSSLGVLLSYKTLIHECGSACSCPPNCRNRMSQGGPKARLEVFKTKNRGWGLRSWDPIRGGGFICEYAGEVIDAGNYSDDNYIFDATRIYAPLEAERDYNDESRKVPFPLVISAKNGGNISRFMNHSCSPNVYWQLVVRQSNNEATYHIAFFAIRHIPPMQELTFDYGMDKADHRRKKCLCGSLNCRGYFY
The following text describes a protein:
Function:
Forms a 40 Angstroms wide channel at the distal tip of the tail. Remains associated to the tail after DNA ejection.
Subcellular Localization:
Virion.
Sequence:
MNIYDILDKVFTMMYDGQDLTDYFLVQEVRGRSVYSIEMGKRTIAGVDGGVITTESLPARELEVDAIVFGDGTETDLRRRIEYLNFLLHRDTDVPITFSDEPSRTYYGRYEFATEGDEKGGFHKVTLNFYCQDPLKYGPEVTTDVTTASTPVKNTGLAVTNPTIRCVFSTSATEYEMQLLDGSTVVKFLKVKYGFNTGDTLVIDCHERSVTLNGQDIMPALLIQSDWIQLKPQVNTYLKATQPSTIVFTEKFL
The following text describes a protein:
Function:
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores.
Sequence:
MSRLNDPVELLQQTRSNFIIESDVSNIKEIKSNMRQLTKLMAEKQTHHNELMKQLQSQLQRQQTKVQALKKNFQEQTSQVKRVEDELNIPKLQQDIDKLVQEINQLRDTIQEGIQKVVETQKQLLNDDTDAAHTIDEEPIGKDDKIRVLKLKLFHSLDVALYNDQLLDLRNEARPLSSSSSSHNIWDEL
The following text describes a protein:
Function:
Pore-forming toxin (PFT) that consists of a crown-shaped octamer or nonamer that forms cation-selective hydrophilic pores of about 1.5 nm (inside) and 13 nm (outside). It causes cardiac stimulation and cytolysis (EC(50)=1.6 nM on erythrocytes). Interestingly, the Phe-16 is crucial for hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers. It is probable that a dimeric form is an assembly intermediate before the complete oligomerization. The formation of stable pores occurs only in vesicles composed of DOPC/SM (there is no oligomerization when the PFT is treated with vesicles of DOPC or SM alone). The transmembrane pore displays 8 lateral perforations, one at each subunit-subunit interface, partially occupied by the acyl-chain region of a bridging lipid. Each pore contains 24 lipid molecules, firmly bound to each subunit, that is, 3 lipids (L1, L2, L3, L4 and/or L5) are associated to each subunit. Lipid L1 bridges 2 subunits, whereas lipids L2 and L3 bind to sites at single subunit.
Miscellaneous:
MISCELLANEOUS: This protein has been found to bind carbohydrates, since it shows a substantial delay in elution profile in size-exclusion chromatography. The carbohydrate pocket ovelaps with the lipid-binding module of actinoporins.
Subcellular Localization:
Secreted. Nematocyst. Target cell membrane. Note=Forms an alpha-helical membrane channel in the prey.
Domain:
Composed of a long N-terminal alpha-helix and a core region rich in beta-sheet structures. Before the pore formation, the alpha-helix binds the lipid membrane, partitions into the lipid-water interface and stabilizes the monomeric molecule on the membrane. Finally, it traverses the bilayer, thus forming the transmembrane pore.
Sequence:
SADVAGAVIDGAGLGFDVLKTVLEALGNVKRKIAVGIDNESGKTWTAMNTYFRSGTSDIVLPHKVAHGKALLYNGQKNRGPVATGVVGVIAYSMSDGNTLAVLFSVPYDYNWYSNWWNVRVYKGQKRADQRMYEELYYHRSPFRGDNGWHSRGLGYGLKSRGFMNSSGHAILEIHVTKA
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which catalyzes the formation of 'Lys-48'-polyubiquitin chains. Mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus. Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation. Positively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation by mediating the ubiquitination and subsequent degradation of SMURF2. Regulates neuronal differentiation by regulating actin remodeling and Golgi organization via a signaling cascade involving RHOA, CIT and ROCK. Inhibits cell proliferation.
Subcellular Localization:
Cytoplasm. Golgi apparatus. Nucleus.
Sequence:
FICHHLCWKLNSFQREERSLCSERGASYKFNSNLEFDICSIWCSKPISVLQDYCDAIKINIFWPLLFQHQNSSVISRLHPCVDANNSRASEINLKRLQHLELMEDIVDLAKKVANDSLLIGGLLRIGYKIENKILAMEEALNWIKYAGDVTILTKLGSIDNCWPMLSIFFTEYKYHITKIVMEDCNLLEELKTQSCMDCIEQGELMKMKGNEEFSKERFDIAIIYYTRAIEYRPENHLLYGNRALCFLRTGQFRNALGDGKRATILKNTWPKGHYRYCDALSMLGEYNWALQANITAQKLCKNDPEGIKDLIQQHVKLQKQIEDLQGRTANKNPIKAFYENRAYTPRSLSAPVFSTSLNFVEKERDFRKINHEMANGGNQNLKVMDEALMVDDCDCHPEFSPPSSQPPKHKGKQKSRNNESEKFSSSSQLTLPADLKNILEKQFSKSSRGAHQDFANIMTMLRSLIQDGYTALLEQRCRSAAHAFTELLNGLDPQKIKQLNLAMINYVLVVYGLAISLLGIGQPEELSEAENQFKRIIEHYHNEGLDCLAYCGIGKVYLKKNRFLEALNHFEKARTLIYRLPGVLTWPTSNVIIEESQPEKIKMLLEKFVEECKFPPVPDAICCYQKCCGYSKMQIYITDPDFKGFIRISCCQYCKIEFHMNCWKKLKTTTFNDKIDKDFLQGICLTPDCQGVISKIIIFSSGGQVKCEFEHKVIKEKVPPRPILKQKCSSLEKLRLKEDKKLKRKIQKKEAKKLAQERMEEDLRESNPPKNEEQKETVDNVQHCQFLDDRILQCIKQYADKIKSGIWNTATLLKELLSWKVLSTENYTTCFSSRNFLNEAVDYVIHHLIQEKNRVKTRIFLHVLSELKEVEPKLAAWIQKLNSFGLDATGPFFSRYEASLKQLDFSIMTFLWNEKYGHKLDSIEGKQLDYFFEPTSSKEARCLIWLLEEHRDKFPALHSALDEFFDIMDSRCTVLRKQDSGEAPFSSTKVKNKGKKKKPKDSKPMLVGSGTTSVTPNNEIITSSEDHSNQNSDTAGPFAVPDHLRQDVEEFEALYDQHSNEYVVRNKKLWDMNPKQKCSTLYDYFSQLLEEHGPLDMSHKMFSEEYEFFPEETRPILEKAGGLKSFLLGCPRFVVIDNCIALKKVASRLKKKRKKKNIKTKVEDISKAGEYLQVKLPLNSAAREFKPDVKSKPVSGSSSAPGSEDVKPKPLSANSPKPACEVVKAKPVSDNSSRQVSEDGKPKGVSSNSPKPGSEDANYKRVSSNSPKPVLEDVKPTYWAQPHLVTGYCTYLPFQRFDNTRTSPAYINVLPGLPQYTSIYTPLVSLSPEYQLPRSVPVVPSFVANDRADKNATAYFEGHHLNAENAAGHQIASETQILEDSSLISVKSQCSTGDAHTVLSESNRKDGHCGNSNNKCEVIPESTSAVTNIPQVQMVAIQVSWNITHQEVNTEPYNPSEKQQGEISRIEKEYQVLQDQLKEAYENYEQMKLKGLEETRDLEEKLKRHLEENKISKTELDWLLQDLEREIKKWQEEKKEIQKTLKSLKKKIKKVSNANEMYTQKNDGKDKEHELHLDQSLEISNTLTNEKTKIKECIKKGKKDYEESHQRAVAAEVSVLENWKESEVYKLQIMQSQAEAYLKKLELISHDPAAYPDMESDICSWELFLSNVTKETEKAKSQFEEQIKAIKNGSRLSELSKVQISELSFPACNTVHPELLPESSGHDDQGFMTSASDVTGNQAALHRDPSVFSAGDSPGEAPSALLPGPPPSQPEATQLPGPKGAGQAALSEQSPAADQKQPVPPGCAACSSQSPKKPFNSIIEHLSVVFPCYNSTELAGFIKKVRSKNKNSLSGLSIDEIVQRVTEHILDEQKKKKPNPGKDKRTYEPSSAAHVTRSSQGPPLAVVAPSPKTKGQKAEDVPVRVAPGASSCEICHEVFKSKNVRVLKCGHKYHKGCFKQWLKGQSACPACQTCDLLSEEGWPSENREPPSCSSR
The following text describes a protein:
Function:
Essential component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MADLTPGARKPAPAELTGFRSALAHTGIPHGVLLWKPRLPSRNWLVFWSVSLSLSYAYYYDRAECKRIKQEVVERVEKYGREPMPGGSLGEPRRVVVWAGRWGGDDDADRAGRYFRKYVKPYLVAAGIDYTLPSVPLHGSITRQLHAAILLQRRQALGLAPTATPLSLPGVLDPAEAKRREVESGVVVVGRASLKEYLEGLRRGWECGVDEWAWETEVEKTLAGDGVFESVESPVEPAVETAETVVEPTADAVPKSNFGFLARPAPVTPGAPAIPAHLHTPPSPLPPTPPLLLLPFTNHLGFLQLPYMILDFFNERAKVRQGAQSALALIEGPTRDMHREDAEHWEEKSESWYNKTARQLPERLQKSRTEYYEAIKSRIDLARAYENGDREMTEEEKKANKVERIQDIQAERLKKELRWKGSEEGWEIVKPETPATWRDRWEGWLKVYQVPEDAQKGL
The following text describes a protein:
Function:
May play a key role in signal transduction and growth control. May have a role in the establishment of the intersegmental and segmental nerves.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MPRPQHHALLRAMLKLLLFASIAEHCATALPTNSSNSPSSPSPFTVASLPPTTASSSSSPAVISTSSFDRNLADLVNPEAETSGSGWESLETEFNLATTVDSSTQKTAKEPVLGTAATSIEQQDQPPDVPATTLAFANAFPVPVAGEMGNGNGNYNDATPPYAAVDDNYVPSKPQNLTILDVSANSITMSWHPPKNQNGAIAGYHVFHIHDNQTGVEIVKNSRNSVETLIHFELQNLRPYTDYRVIVKAFTTKNEGEPSDQIAQRTDVGGPSAPAIVNLTCHSQESITIRWRRPYEFYNTIDFYIIKTRLAGQDTHRDIRINASAKELETAMILQNLTTNSYYEVKVAAATFSVINPKKIVLGKFSESRIIQLQPNCEKLQPLLRQSHNDYNLAVLVGIIFSCFGIILIIMAFFLWSRKCFHAAYYYLDDPPHHPNAPQVDWEVPVKIGDEIRAAVPVNEFAKHVASLHADGDIGFSREYEAIQNECISDDLPCEHSQHPENKRKNRYLNITAYDHSRVHLHPTPGQKKNLDYINANFIDGYQKGHAFIGTQGPLPDTFDCFWRMIWEQRVAIIVMITNLVERGRRKCDMYWPKDGVETYGVIQVKLIEEEVMSTYTVRTLQIKHLKLKKKKQCNTEKLVYQYHYTNWPDHGTPDHPLPVLNFVKKSSAANPAEAGPIVVHCSAGVGRTGTYIVLDAMLKQIQQKNIVNVFGFLRHIRAQRNFLVQTEEQYIFLHDALVEAIASGETNLMAEQVEELKNCTPYLEQQYKNIIQFQPKDIHIASAMKQVNSIKNRGAIFPIEGSRVHLTPKPGEDGSDYINASWLHGFRRLRDFIVTQHPMAHTIKDFWQMVWDHNAQTVVLLSSLDDINFAQFWPDEATPIESDHYRVKFLNKTNKSDYVSRDFVIQSIQDDYELTVKMLHCPSWPEMSNPNSIYDFIVDVHERCNDYRNGPIVIVDRYGGAQACTFCAISSLAIEMEYCSTANVYQYAKLYHNKRPGVWTSSEDIRVIYNILSFLPGNLNLLKRTALRTEFEDVTTATPDLYSKICSNGNVPQHVILQQQQLHMLQLQQQHLETQQQQQQQQQQQQQQQQTALNETVSTPSTDTNPSLLPILSLLPPTVAPLSSSSSTTPPTPSTPTPQPPQTIQLSSHSPSDLSHQISSTVANAASPVTPATASASAGATPTTPMTPTVPPTIPTIPSLASQNSLTLTNANFHTVTNNAADLMEHQQQQMLALMQQQTQLQQQYNTHPQQHHNNVGDLLMNNADNSPTASPTITNNNHITNNNVTSAAATDAQNLDIVG
The following text describes a protein:
Function:
Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MNIIFLKVPSIFKKLNVGNIKILNVNQNSPSIIVNSNNTKSIKNHNYSSFTNNNNNNNKNQVNLVQNKSILSSSSSYKGNNNNNNKLSYTTSSNNNNNNKIEEIVKSTTVSPFTPLNILHPKLVGEKLYSNDNEANNNQKEFKAEISTLPNGIRVVSKQTHEGVCAIGLYINAGTKYESPQDRGVFNLLEKMTFKETKNNSTSEIIKELEEISMNAMASSSREMINVSLEVLRKDLEFVLSILSDQIKSPTYSEEELREQIEVCIRNYEMITNSSSDQLMTEILMGVAFGDAGLGNLVIATPEQYQNITREKLFDALRKYYVGKNIVISVTGAEHSQVIELVDKYFGDIPFTQKDTPSEDSIDSTITYKGGTDACVAGLIHKNHLKSQLQFLIEKQQKLKQQQQQQQPQPQNSNIDDNDNEEELLNLEIEQTKISIEQLELQQVKESSWIIAFPHSGLSTVAENKDIINGLVLQSLLGGGSSYSTGGPGKGMQSRLNLNVVYSSHRVKNCHAFLFVFNKVSLFGISLTTQSGFLQDGIELVLQELLMLRSSMTQQELERAKRSQKSQILQNLEMRSVQCDDMARHILSFGSYKSPEQICKLIDSVTLDDIKKLISKLAQSNPSVVSIVANENEPILTAEQYNQIVKQNSSTLFK
The following text describes a protein:
Function:
Maternal RNA-binding protein that is required for germ cells proliferation and self-renewal. Acts by forming a complex with pum and brat that regulates translation and mRNA stability. The complex binds to the Nanos Response Element (NRE), a 16 bp sequence in the hb mRNA 3'-UTR and prevents its translation. Controls posterior development. Rescuing factor for the abdominal defect of posterior group mutants. The other posterior group genes are not required for nanos function but rather play a role in localization or distribution of nanos protein.
Subcellular Localization:
Cytoplasm, Cytoplasmic ribonucleoprotein granule.
Domain:
The Nanos-type zinc finger is composed of two C2HC motifs, each motif binding one molecule of zinc. The presence of the zinc molecules is essential for the translation repression activity of the protein.
Sequence:
MFRSNLEGSGAAAVGVANPPSLAQSGKIFQLQDNFSAFHARGGLNILGLQDMYLDTSGANSSATLSPPITPVTPDPSTSAQSTHFPFLADSAATANSLLMQRQYHYHLLLQQQQQLAMAQHQLALAASAAAASASHQQTDEIARSLKIFAQVTTGAAENAAGSMQDVMQEFATNGYASDDLGRMSYGSAPPQVQMPPQQQHQQQQGLHLPLGRNPAQLQTNGGNLMPIPLATHWLNNYREHLNNVWRNMSYIPAAPNTMGLQAQTAATVSTNLGVGMGLGLPVQGEQLRGASNSSNNNNNNNKVYKRYNSKAKEISRHCVFCENNNEPEAVINSHSVRDNFNRVLCPKLRTYVCPICGASGDSAHTIKYCPKKPIITMEDAIKAESFRLAKSSYYKQQMKV
The following text describes a protein:
Function:
Involved in peptide utilization.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNAVTIVIASMCILAIAYRLYGTFMMVKVLKVNDDKPTPAHALEDGKDYVPTNKWVSFGHHFAAIAAAGPLVGPILAAQFGYLPGLLWLLIGAVIGGAVHDIVVLFASMRKNGKSLSEVAKDELGPVAGFCTGLSMLFIITITMAGLSMVVLHALERNPWGTFAVGITIPIAMGVGLFYKKTGNLKLASTVGFLFLMAGVFIGPWVQTTALGDFLTLDTKTLAIALPVYAFFAAALPVWLLLAPRDYLSSFMKIGVFIALIVGVFVVNPSIPFPAFTEFVKGGGPVLAGPVWPFISITIACGAISGFHAFVGSGTTPKMLNKWSDMKPVAFGAMLVECLVGIMALIAATALQPADYFAINSTPEVFRTLGMNVVHLPELSGEIGLDLEGRTGGAVTLAVGMTYIFTGMPFFSHLASYFFQFVIMFEAVFILTAIDAGTRVARYLIQDFFGEVYKPLKKTDWIPGSVFASALACLMWGYLLYSGDIGSIWALFGVSNQLMASVGLIIGATIVLKIADKRRYILTCLIPLAYLYVTVNYAGYWMVRNVYLNPEAAGYSVLNGVLSIIMLVLGFIIIVAAVKKWAQMWKDPSLRMEASIPG