lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways. In the hypothalamus, acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity. In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides. In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption. Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways. May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression. Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells. Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 which promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38. In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses. Increases CD4(+)CD25(-) T-cell proliferation and reduces autophagy during TCR (T-cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation.
Subcellular Localization:
Secreted.
Sequence:
MRCILLYGFLCVWQHLYYSHPISIEKIQADTKTLTKTIITRIIQLSNRNGVSTDQRVSGLDFIPGNQQFQNLADMDQTLAVYQQILSSLPMPDRTQISNDLENLRSLFALLATLKNCPFTRSDGLDTMEIWGGIVEESLYSTEVVTLDRLRKSLKNIEKQLDHIQGC
The following text describes a protein:
Function:
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor. Membrane; Lipid-anchor, GPI-anchor.
Sequence:
MKLQAVLAKTALFSAAVAKASQNTTLAQSGLPVIEVVGNKFFDSRSGEQFFIKGIAYQPSSAPQELEVGYPADTKYIDPLAEVEICKRDLPYLKKLGVNTIRVYSIDPTKPHDVCMEELSKLGIYVLIDLSEPDTSIIRETPTWDVKVFQRYKDVVDSMQKYNNVLGFFAGNEVTNDRTNTDASPFVKAAIRDVKNYIKQMGYRTLPVGYSTNDDQETRDHLADYFVCGSVSADFYGINMYEWCGHSSYGTSGYRERTNEFRNFPVPVFFSEFGCNTIRPRPFTEIQALYGTMMTPVWSGGLAYMYFEEDNEYGVVKVTKDNQVLELPDFRNLQKEFEKARPKGVKRSVYEKTYKVNSRTCPEKSATWKASEELPPTPDARKCGCLEQALPCLSLSLQDPMSYKNYFEYVCGFVNCMDINGDGSLGVYGEYSDCDTRQKLSLQLSKLYLRRKISKNECPIASNDFFFNAKSIGIPQQCQGVMEDVKVQANKKLVEPKPAAPAGKDVNAAGSSALHRLNTATLVLVSTTAFIFHLLL
The following text describes a protein:
Function:
Contributes, together with ILI5/BUL1 and BC1, to the promotion of leaf inclination and grain size by modulating cell elongation.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MEKSPPETAAAAAEVAARFRSLVDTGDIGAIRQTQHLILGRLQDSNAVLTHFNEYSEQCFAEVSNDFASKTRLLKSMKDDLDHIFLKLRSMKSRLAATYPDAFPDGAMAKTMDQRPDLESPLD
The following text describes a protein:
Function:
Guanine-nucleotide exchange factor (GEF) that acts as an activator of Rop (Rho of plants) GTPases by promoting the exchange of GDP for GTP. Acts downstream of PRK2 in the control of polarized pollen tube growth by activating ARAC11/ROP1. In association with ROPGEF4, acts as a specific regulator of ARAC10/ROP11 function in ABA-mediated stomatal closure. May play a role in the Rac/Rop-signaling pathway that controls ROS-mediated root hair development.
Miscellaneous:
MISCELLANEOUS: Plants overexpressing ROPGEF1 or ROPGEF4 are relatively insensitive to ABA-induced stomatal closure and become severely wilted during drought stress. A similar phenotype is observed in plants expressing a constitutively active ARAC10/ROP11.
Subcellular Localization:
Cytoplasm, cytosol. Cell membrane. Note=Localizes to the apical region of the pollen tube plasma membrane to activate ARAC11/ROP1 and interacts with ARAC10/ROP11 on plasma membrane in guard cells.
Domain:
The PRONE (plant-specific Rop nucleotide exchanger) domain is responsible for the GEF activity. The intrinsic dissociation of ROP4-GDP is stimulated 15-fold by the PRONE domain , whereas that of ROP1-GDP is increased 350-fold.
Sequence:
MGSLSSEEDDEVSSERCGSYSPSADISESESSSSFSCHRFDGEGASSSIPSSPRVVAGRGFYFPAPVMLPVIGGKDVVWDDKQPDNDLSEIEMMKERFAKLLLGEDMSGGGKGVCTALAISNAITNLSATVFGELWRLEPLAPQKKAMWRRELEWLLCVSDSIVELIPSIQQFPGGGTYEIMETRPRSDLYANLPALKKLDAMLIDMLDAFSDTEFWYTDRGIVLGDCDKDSYNSPASVRQEDKWWLPCPKVPPNGLSEEARKKLQQCRDFANQILKAALAINSGVLAEMEIPDPYLETLPKSGKECLGEIIYQYLTANKFSPECLLDCLDLSSEHQTLEIANRIEAAVHVWRQKNGRRHKKQAKLKLSSWGGKVKGLVNDNERNDFLVQRAETLLQSLRIRFPGLPQTTLDMNKIQYNKDVGQSILESYSRVMESMAFNITARIDDVLYVDDAMRRSISVTESLSLFSINGLNPQKAFSVQSSPHGSPFATPALSVASRSPRRAPPLYSVKRNGTREKGIVGETEKAWSYAGNLSSRRVTGVTPERD
The following text describes a protein:
Function:
Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MPLRFFHSFYRRRSQRISLQSTKIQMKQIVKILTIVFGVSALWIGLLQTSVVPENYTWLLPLYLIVSLGCYGLLMVGVGLMKFPTCPQEAVYLQQDVREAKELLQKKGVDVGSD
The following text describes a protein:
Function:
Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.
Subcellular Localization:
Preautophagosomal structure membrane; Multi-pass membrane protein.
Sequence:
MAALQTEYRRLETVEDDPPEDQDVMLHVVHDSGRARWNHIENLDEFFTRVYHYHQKHGYLCMMLAQLLELVQFLFIIFFSLFLLQCVDYSVLFQDDKTTTGTKVTIPDAIIPLEQCAKNPSSVIVICLIIAGIFWLHRLLRVLYNAFHFWEIRAFYTRALKIPSKDLVNLTWHDVLKKVQQVQREQRMCIHKAELTELDIYHRILRFKNYMVAMVNKSLLPLHHHPPFLGDTVFLTNSLKYNIEMILFWGPWAPFRNYWHLKDEYKRSSKREELARQLSKHILWIGLANLILCPFIFLWQILYSFFSYAELIKRDPSTLGARKWSQYGRLYLRHFNELDHEFQARLNRGYKPAKKYLDAFTSNVLAIICQNIAFFAGSILAVLIILTVIDEDVLTVEHVLTTVTLLGVAVTICRTFIPDENLIWCPETLIQSILAQIHYIPDSWKGQAHTYKVRDEFSQLFQYKAVYFLEELLSPIVTPYILIFKLRSRAVDIVDFYRNFSVDVIGVGDVCSFAQMDIRTHGNPKWMTGGNSEANQYNQAEDGKTELSLMHFTVTNPKWTPPQSSKCFISALKTQAQRDIKTCNRLEAENNALMTSMRSITSLEGQNSILGSLAVQHSNPPSLGTIPTPHFQPPAPLATPVSSPTPEGATSSSRPTQLVMGGITSSEGPLESDGSGLLSSLQSPDGAFLTSMQGPGLMQQSLIPTANPMVTGPSPANVTTADMNFSALYMHQLHDRSIVLPGSSSLEMQPPQHPMNQSTPWQMELPTDSIDSDDDDHPLQNMPLAPLGQLINTDV
The following text describes a protein:
Function:
[Drosocin]: Antibacterial peptide with strong anti-Gram-negative bacteria activity. Significantly contributes to antibacterial activity against Enterobacter cloacae but not Providencia burhodogranariea. Inhibitor of bacterial translation machinery that targets translation termination in a prfA- or prfB-dependent manner. Binds within the nascent peptide exit tunnel of the bacterial large ribosomal subunit, potentially interfering with nascent chain translocation that occurs post-peptide bond formation. Binds prfA/RF1 (and potentially prfB/RF2), trapping it on the ribosome after release of the nascent polypeptide chain and preventing further translation. The resulting depletion of peptide chain release factors further disrupts bacterial translation by preventing ribosomal peptide chain release and inducing stop codon readthrough. Entry into target Escherichia coli cells requires the bacterial peptide antibiotic transporter sbmA; [Buletin]: Peptide with significant antibacterial activity against Providencia burhodogranariea but not Enterobacter cloacae.
Miscellaneous:
MISCELLANEOUS: Unlike many antimicrobial peptides that kill bacteria using a lytic mechanism, proline-rich antimicrobial peptides can enter the bacterial cell to target intracellular processes; MISCELLANEOUS: 'Buletin' is named after Philippe Bulet, whose dedicated efforts in the 1980s-1990s characterized many of the Drosophila antimicrobial peptides, including Drosocin.
Subcellular Localization:
[Drosocin]: Secreted; [Buletin]: Secreted.
Sequence:
MKFTIVFLLLACVFAMGVATPGKPRPYSPRPTSHPRPIRVRREALAIEDHLTQAAIRPPPILPA
The following text describes a protein:
Function:
Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in FASLG, ITM2B and TNF processing. Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus. Also responsible for the intramembrane cleavage of Fas antigen ligand FASLG, which promotes the release of the intracellular FasL domain (FasL ICD). Essential for degradation of the invariant chain CD74 that plays a central role in the function of antigen-presenting cells in the immune system. Plays a role in the regulation of innate and adaptive immunity.
Subcellular Localization:
Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein; Lumenal side. Note=Colocalizes with palmitoylated and myristoylated proteins at the plasma membrane.
Domain:
The PAL motif is required for normal active site conformation. The catalytic domains embedded in the membrane are in the opposite orientation to that of the presenilin protein family; therefore, it is predicted to cleave type II-oriented substrate peptides like the prototypic protease SPP (By similarity). The C-terminal tail is necessary for lysosomal transport.
Sequence:
MGLLHSLHAPAAALLWSCLLGLAAAQEAILHASTNGVSSLSKDYCMYYNNNWTRLPSSLENATSLSLMNLTGTALCHLSDIPPDGIRNKAVVVHWGPCHFLEKARIAQEGGAAALLIANNSVLIPSSRNKSTFQNVTVLIAVITQKDFKDMKETLGDDITVKMYSPSWPNFDYTLVVIFVIAVFTVALGGYWSGLIELENMKSVEDAEDRETRKKKDDYLTFSPLTVVVFVVICCIMIVLLYFFYRWLVYVMIAIFCIASSMSLYNCLSALIHRMPCGQCTILCCGKNIKVSLIFLSGLCISVAVVWAVFRNEDRWAWILQDILGIAFCLNLIKTMKLPNFMSCVILLGLLLIYDVFFVFITPFITKNGESIMVELAAGPFENAEKLPVVIRVPKLMGYSVMSVCSVPVSVLGFGDIIVPGLLIAYCRRFDVQTGSSIYYISSTIAYAVGMIITFVVLMVMKTGQPALLYLVPCTLITVSVVAWSRKEMKKFWKGSSYQVMDHLDYSTNEENPVTTDEQIVQQ
The following text describes a protein:
Function:
Zinc finger nuclear factor involved in transcription by regulating chromatin structure and organization. Involved in the pluripotency and differentiation of embryonic stem cells by regulating SOX2, POU5F1/OCT4, and NANOG. By binding PBX1, prevents the heterodimerization of PBX1 and HOXA9 and their binding to DNA. Regulates neuronal development and neural cell differentiation.
Subcellular Localization:
Nucleus.
Sequence:
MEVLQCDGCDFRAPSYEDLKAHIQDVHTAFLQPTDVAEETPSQSRFSSMNSNDQPEVEYSSVKDEFAIADEIAGQNAAQLGTANYYSHSQNYYGQHMLSKPANKFFQCKFCVRYFRSKNLLMEHTRKVHGAQASAGSPGAGSMNYNIMMHEGFGKVFSCQFCTYKSPRRARIIKHQKMYHKNSLKESSTPPATSAALSESACTSVSVQDSCKELPAEVVERSILESMVKPLTKSRGNFCCEWCSYQTPRRERWCDHMMKKHRSMVKILSNLRQQPDGTSMPEGSSKGPPSPTPNSNYVPMNASGREMPNANVTNYRGSMNNSLGRSNSSSKFSSVSYPHLKHKASHNSGIVNLSDRSQYGMGDMANSSADMDTNSMLNDSSSDDELNELDSENGLNSMDHQSSGLSAEQLMGSEGHKLLETKGIPFRRFMNRFQCPFCPFLTMHRRSISRHIENIHLSGKTAVYKCDECPFTCKSSFKLGAHKQCHSGAASDWDAVNSQTESIASSLNESTVSYEGGNINGRKSGGMIDSMQQQSPQSNSQHPYKCTMCNYSTTTLKGLRVHQQHKHSFCDNLPKYEGASSNTPQDSEPDTLASPSTVKKSQTSILGLSSKNNFVAKASRKMSNDFPLDLSPVKKRTRIDEIASNLQSKISQNKQQEDSVINVEDEEDEEEDNEVEIEVELDKEEEQAEPLMDISSFTSQQMWGRDSSDTQKDSSYRNIVHEYNSTNGAEIELTISEDEEDYYCSSMGLKDQGLNSSVLGSQSSIYGSDQNNDNSDYGDSGRLYYCKHCDFSNKSARSVSTHYQRMHPYIKFSFRYILDPNDHSAVYRCLECYIDYTNFEDLQQHYGEHHPEAMNVLNFDHSDLIYRCRFCSYTSPNVRSLMPHYQRMHPTVKINNAMIFSSYVVEQQESLNAESQTLREILNSAPKSLVSSTPVARGTGVPGSFNKNSPKANSPESESQKESSVNSVVVYDCDVCSFASPNMHSVLVHYQKKHPEEKASYFRIQKTMRVVSVERGSALAQMAYEMGSPVSPKMSNLSSQLQPPPPPDLMTELYYCKHCSYSNRSVVGVLVHYQKRHPEIKVTAKYIRQAPPTAAMMRAGELPPGIHRPPASMQQHNRGNSGRAVASSENEMFFCQHCDYGNRTVKGVLIHYQKKHRDFKANADVIRQHTATIRSLCDRGQKNSPGGMHTQASNAEQEKAKLRALKCRQCSYTSPYFYALRKHIKKDHPSLKATVTSILRWAFLDGLIEAGYHCEWCIYCHAEPSGLLVHYQRRHPEHYVDYTYMATKLWAGPDPSPPAMLIPSEMKTYKCRDCIFEASSIWDITNHYQAFHPWAMNGDESVLLDIIKEKDAADKSNDASAILNSEDQMPGTQLDQDTEYAGDSNLSQDKAIQLTSVNPAISSTPYQCTVCQSEYNNLHGLLTHYGKKHPGMKVKAADFAQDIDINPGAVYKCRHCPYINTRIHGVLTHYQKRHPSVKVTAEDFVHDVEQPADMNQNDVEETSRIFKQGYGAYRCKLCPYTHGTLEKLKIHYEKYHNQPEFDVFAQSPPKFPPTMEPELVTEMKPSPEEIPPEEIIGEDIMSPSHFSSSHLVSHTVFRCQLCKYFCSTRKGIARHYRIKHNNVRAQPEGKNNLFKCALCSYTNPIRKGLAAHYQKRHDIDAYYTHCLAASRTVTDKPNKVIIPSPQKDDSPQLSEELRRAVEKKKCSLCSFQSFSKKGIVSHYMKRHPGVFPKKQHASKLGGYFTAVYADEYEKPEPSPEEKNDFEKPEVEVEVPEPVPEMEWLPFRCVKCFKLSFSSAELLCMHYTEHHSKDLKRDFTILESGIHFPDPLYQCRHCDCKLHSIAELTSHLNSHNEEFQKRAKRQERRKQLMSKQKYADGAFVDFKQERPFGSLEEISKLKERKVVGYKCKFCVEVHPTLRAICNHLRKHVQYGNGTSVSAAVKGLRSHERSHMALAMFTREDKYSCQYCSFVSAFRHNLDRHMQAHHGHHKPFRCKLCPFKSSYNSRLKTHLLKAHAGKHAYKCSSCSFSTMTVSQLKEHSLKVHGKALTLPRPRIVSLVTSHAHHASKNHTTAEEVEDCNDSSYSEPPDVQQQLNHYQLAALARNNNNISPVPDQKAEPVLNCEFCEFSSGYIQSIRRHYRDKHGGKKLFKCKDCSFYTGFKSAFTMHVEAGHSAVLEEGPKDLRCPLCLYHTKYKRNMIDHIVLHREERVVPIEVCRSKLSKYLQGVVFRCDKCTFTCSSDESLQQHIEKHNELRPYKCQLCYYETKHTDELDAHLRDEHKVSRNFELVGRVNLDQLEQLKGKEESSSSDEEEKEEEMSPKTDERESMGFSENGPPEKRFACEFCGRTFAEGSEWERHVLRHGMAVNEINQVISEDSQSKENPEENVKVPLAEEMESSMSIVVDFSHKNEPAVCIVAAADKSLQENTEAKSE
The following text describes a protein:
Function:
Essential transmembrane GTPase, which mediates mitochondrial fusion during spermatogenesis. In early spermatocytes, fusion of mitochondria give rise to two organelles named Nebenkern and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. Essential for fertility (By similarity).
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein.
Sequence:
SSMEPEMEQKVKDQHMERCVNLLVDELGVYSTAQEAWERIYHVSALEALHIRNGHIKNPSAQTKERYQEFLRFENDFSNCLAVSALKTKFGPHLLSAQKILNQLKSTLISPFIEKVSRLIDENKERRANLNAEIEEWELEMQDEREDLQYCFEELTEMTQRLGRCVLNDQIKTLIPSAVLSFSHPFHPEFPAQIGQYQRSLCAHLDNLLEDRVLQCLSIPLQRKILDMEKELGLQITEKSCDWQLIYGLDCQSYMSDFQPDLRFRFSLGFTALWHRLEGNLPLHSSPFRTQKLRNGHKKCLPLPPLVHGNHWQMLESLVKSKGSLGTVLLGAMAIRSFNWPIVMILGGLVGSFYMYEYAAWTTAAQERSFKSQYSRLLQQRLRTDVQQTVSGFELQLRQHLAKVRNCWEAQSNETLNDLNVRTAELTKQIQSMEVLQLSLKKFRDKGQLLASRL
The following text describes a protein:
Function:
Class I alpha-mannosidase essential for early N-glycan processing. Progressively trims alpha-1,2-linked mannose residues. Produces Man(5)GlcNAc(2) from Man(8)GlcNAc(2), but only Man(6)GlcNAc(2) from Man(9)GlcNAc(2). Has difficulty acting on the terminal mannose of the b-branch. Involved in root development and cell wall biosynthesis.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MARSRSISGSGVWKYLNPAYYLRRPRRLALLFFLFVSVSMVVWDRMNLAREHEVEVIKLTEEVFRLEQMLEELRGVGDGKTLMTHKDVPEDPVDIERRQKVKEAMIHAWSSYEKYAWGKDELQPRTKDGTDSFGGLGATMIDSLDTLYIMGLDEQFQKARAWVATSLDFDKDYDASMFETTIRVVGGLLSTYDLSGDKIFLEKAKDIADRLLPAWNTPTGIPYNIINLRSGSAHNPSWAAGGDSILADSGTEQLEFIALSQRTGDPKYQQKVEKVITELNKNFPADGLLPIYINPDNANPSYSTITFGAMGDSFYEYLLKVWVQGNKTSEVKLYREMWEKSMKGLLSLIKKSTPSSFTYIQEKNGNSYNDKMDELACFAPGMLALGASGYGPDEEKKFLTLAEELAWTCYNFYQSTPTKLAGENYYFSAGQDMSVGTSWNILRPETVESLFYLWRLTGNKTYQEWGWNIFQAFEKNSRIESGYVGLKDVNTGAKDNKMQSFFLAETLKYLYLLFSPSSVISLDEWVFNTEAHPLKIVARNNDQRKPTITLRQRRFGGEVKV
The following text describes a protein:
Function:
Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MFKYLSVFVIIGFIFFIQCSKNEDNDVFVPTKEWQTVRKGQKIPKGLHVRINLETGETEAKLLDEAPEDKTRALSALPPENPKSTLGEAVTDTYTPDELKKIKNEFRSYDEIKKTLGDLKLTPKMDAEIIADLLQRHQEVVDKTELLKILEDLDFLAHQYDNAREFVKQNGFREMIYKNLNSTDSEVKKETLKLMTALMQNNVNPKIHALESGAVGVLLRLVNFESDLGVKTRALSALGALLRSFPAAQRKFVESGGLSVLSKFFDSDDIKLQIKLVTMISDLLVEHEYSVVDENLSKYYVKFDLTKRILEHDWCKKLNKLLLGLLITDKDDHDSVEKCLTAMHSLRAHCGDKYEKDLITNLRKRYDSLLKSDGVEDQTFYKGLKDLCDEILYHVNNSVKTEL
The following text describes a protein:
Function:
Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme.
Sequence:
MFLTAVNPQPLSTPSWQIETKYSTKVLTGNWMEERRKFTRDTDKTPQSIYRKEYIPFPDHRPDQISRWYGKRKVEALPYKHLITHHQEPPHRYLISTYDDHYNRRGYNPGLPPLRTWNGQKLLWLPEKSDFPLLAPPTNYGLYEQLKQRQLTPKAGLKQSTYTSSYPRPPLCAMSWREHAIPVPPHSLHPLPHF
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mS41 is involved in telomere length regulation.
Subcellular Localization:
Mitochondrion.
Sequence:
MLILKRIFIIRNFIFPFSNCRYASTVPSPRSGISNTNDFFKRIGRDTAEKVNGKFESWDGLFRKSTKTMKKEGIDVRTRKYIASQRNRFKEGFIVKPYPVMVKKNGGERRKRK
The following text describes a protein:
Function:
Repressor for the homoprotocatechuate catabolic pathway hpc operon.
Sequence:
MHDSLTIALLQAREAAMTYFRPIVKSHNLTDQQWRIVRILADSPSMDFHELAFRTCILRPSLTGILTRMERDGLVLRLKPVNDQRKLYVMLTEQGQTLYARARSQVEEAYRKIEADFTPEKTQQLMLLLDDLIALGRQHPDSEAEA
The following text describes a protein:
Function:
Involved in the fatty acid remodeling steps of GPI-anchor maturation where the unsaturated acyl chain at sn-2 of inositol phosphate is replaced by a saturated stearoyl chain. May catalyze the second step of the fatty acid remodeling, by reacylating a lyso-GPI intermediate at sn-2 of inositol phosphate by a saturated chain. The fatty acid remodeling steps is critical for the integration of GPI-APs into lipid rafts.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MLASEIMVKPVTLVSVSMTKTAKIVVSLPLSGLIFTVMWSILFDLENSTATHCKVANYLPSVSAAIALTPQAYVWRFNIALHSMPRYMLLLMYWEWHYKRTVDKSKLLAPLHKLLIILAVGANFIELSALLGLTIISSTESPSAHETSFILFMIGSITCMISSCLLNTTMVIETENEKKSKNTKLFAVVIHITSFISALYFYFRHNAKCEPGVYSLFALSEYIVIISNMFFHYQHGIDFCAYKIQVNNNNDPQKIS
The following text describes a protein:
Function:
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
Sequence:
MASKHFVNDPTLLVNSALHALTLTNPSVALDEENKIIYRRPGHASQVSIISGGGSGHEPSFGAFVGEGLLAASVAGSIFASPSAEQIRRCVMSRVDAEKGILVTVMNYTGDVLNFGMAVEKAKAAGLKVEMLVVGDDVGVGRAKAGKVGRRGIAGTVLVHKITGALAATGASLENVYKVGKLTADNIASVGASLDHVHVPGRAPPNPNSEESLAFEEVEIGMGIHNEPGSGRAKVDLPELVKRMLTQLLDSKDKDRAFLNVNSNEVVLLVNNLGGVSVLELGGITAEVTSQLEKSYNIKPVRILAGTYMTSLNGLGFSISLLNVVNTNIGGPSMLQLLDASTEATGWAAPIRKETWEAKSTATRTGSAGAEEVVKPSGLKLDPATTKTALTAGLQRMIAAEPDVTRFDTVVGDGDCGIGLKRGAEAVLSTISKENLSGDAVVDLAKIVQVVENSMDGTSGALYAIFLNSLLAALRENAFTGQATPEFWAKALQSASEALSKYTPAKPGDRTVVDALHPFVETLIKTGDIKKAAEASRKGAEGTKGMKASLGRTVYIGGTGFEQVPDPGAWGLSEFFLGLAGLGDSDYELV
The following text describes a protein:
Function:
Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MEENQEQDLLYQPLPQYVSEEKEKLGLQELSCPKDKFVESFLDRHIQNFKPNEKKELKKSYLLLDLPYRQKPTVGKKKNTSHSRKRREKKVYDIPPETQKSEGRKKVYDIPPEHQKYSLYVPLHNLWLQYIKDLLQVTPTSNLNLMQKKMLKADLHGALITVCKSRCPSYVGLTGIILQEGQKVFKVITKEDKLKTVPKANSVFSVEFEGLRAKIYGNHFCTRTAQRASKKFKLPMVKQTIDL
The following text describes a protein:
Function:
Nitronate monooxygenase that uses molecular oxygen to catalyze the oxidative denitrification of alkyl nitronates. Acts on propionate 3-nitronate (P3N), the presumed physiological substrate. Probably functions in the detoxification of P3N, a metabolic poison produced by plants and fungi as a defense mechanism.
Sequence:
MSSALTDLFPYPIVQAPMAGGVSVPRLAAAVSEAGGLGFLAAGYKTADGMYQEIKQLRGLTSRPFGVNLFLPQPETADPAAVDVYAHQLAGEAAWYETELGDPDCGRDDGYDTKVAVLLDNPVPVVSFHFGVPSREVVDSLHRVGTFALVGATTADEARAVEQSGADAVIAQGMEAGGHQGTHRDNPETGGAGTGLLSLVAQVREAVSLPILAAGGIMRGGQIAAVLAAGASAAQLGTAFLATSESGAHDLHKQALTNPLFVRTELTRAFSGRPARALVNRFLREHGPYAPAAYPEVHHLTAPVRKAAAKAGDAQGMALWAGQGHRMARELPAGQLVEVLVAELAAAGTALSGLSGYATGGGAR
The following text describes a protein:
Function:
The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Sequence:
MAATTMSLSSPAFAGKAVKSLPSPSLFGEARVTMRKTAAKVKQVASGSPWYGSDRVLYLGPLSGEPPSYLTGEFPGDYGWDTAGLSADPETFAKNRELEVIHCRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQSILAIWACQVVLMGAVDGKGPLENLADHLSDPVNNNAWAFATNFVPGK
The following text describes a protein:
Function:
[Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development; [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product.
Subcellular Localization:
Endoplasmic reticulum membrane; [Sonic hedgehog protein]: Endoplasmic reticulum membrane. Golgi apparatus membrane; [Protein hedgehog N-product]: Cell membrane; Lipid-anchor.
Sequence:
MDEMLLLTRILLVGFICALLVSSGLTCGPGRGIGKRRHPKKLTPLAYKQFIPNVAEKTLGASGRYEGKITRNSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDKLNALAISVMNQWPGVKLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRSKYGMLARLAVEAGFDWVYYESKAHIHCSVKAENSVAAKSGGCFPGSATVHLEHGGTKLVKDLSPGDRVLAADADGRLLYSDFLTFLDREDSSRKLFYVIETRQPRARLLLTAAHLLFVAPQHNQSEATGSTSGQALFASNVKPGQRVYVLGEGGQQLLPASVHSVSLREEASGAYAPLTAQGTILINRVLASCYAVIEEHSWAHWAFAPFRLAQGLLAALCPDGAIPTAATTTTGIHWTYTLRAALCSRDEATSSTGMEGSSRGPPGMHRGAEPALLCSESGSSQSGDGRAWAHVHRRQPKGWITRDGFSLLAASSWKPLSPSEDRDSAWWWPRWPEHGVTTQCYSVCVDCQDESRAMALGREWRLCSGMGQPDPAEGPALEGTGVGPRMGTFAKQW