lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Acts as a membrane anchor, bringing other regulators of programmed cell death (PCD) to the plasma membrane. Negatively regulates hypersensitive cell death.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Domain:
The LITAF domain is stabilized by a bound zinc ion (By similarity). The LITAF amphipathic helix region (68-90) is necessary for plasma membrane localization; Both N-terminal (1-47) and C-terminal (114-134) domains are sufficient for the interaction with MIEL1 or with the N-terminal domain of LSD1; The LITAF domain (48-113) is not involved in the interaction with LSD1.
Sequence:
MAKEGTTVIGVPYYAGQNPYQAGIVPPNAIYGDPLGAPIQQTIYRDTPAPFNCLYCGNTGLTNLRSKPGVAAVVACMMPFMLGFCFLCPSMDCLWNKQHHCPQCGNKVADFEKSDPCLVMDPPQWKQPSFALPA
The following text describes a protein:
Function:
Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing.
Subcellular Localization:
Cytoplasm.
Sequence:
MAAAPHRAQVPADSTAPLQTGPVLENNPSKSANAKDQILSGTENVTTGNARGASSLRSPNGPPEKASSVGKAGEQPYLYQQNVYAPQPQPLYPGGYMNPSGQWEEYPHYVNMEGLHSVSPGIYNDNQSLMLSAGYANNPQMMYGAYSPVSTAGDGQQYFPVHYSFSNPYYQPPASPSMGYSNSATGMSQGDPMLQQEYFLPDGLLYSPTPGYHQPFSSFDRALTQPNNAPGLFGQGSLPLASGMHHGSMYGPGSYKGRQYGSKFGGTTPSWSSAGRRFGTFDLSGNQQRGSMSFGSHNGSLEFMNEQNRGPRATKPKIQDTENSGDEKSEKTVPLIDSELYNRSDFITEYKDAKFFVIKSYTEDHVHRSIKYNVWASTASGNRKLDSAYRAAREKEEHCPIFLFFSVNGSGQFCGVAEMIGPVDFDRSVNYWQQDKWSGQFPVKWHIIKDVPNNLLRHIILENNDNKPVTNSRDTQEVKLEQGLQMLTIFKSHEAETTIVEDFDFYEQREKALQENRRQQHAASTDTQKLVDTKAQDAVADISDAFAKAVQLKNTENSGTTPKTEGASAEKGSAATAKVEGSANLNTGPVEESS
The following text describes a protein:
Function:
Attenuates Hha toxicity and regulates biofilm formation. Binds to various coding and intergenic regions of genomic DNA.
Miscellaneous:
MISCELLANEOUS: Hha and TomB may form a type II toxin-antitoxin (TA) system.
Subcellular Localization:
Cytoplasm.
Sequence:
MDEYSPKRHDIAQLKFLCETLYHDCLANLEESNHGWVNDPTSAINLQLNELIEHIATFALNYKIKYNEDNKLIEQIDEYLDDTFMLFSSYGINMQDLQKWRKSGNRLFRCFVNATKENPASLSC
The following text describes a protein:
Function:
May be implicated in the adrenocortical zonation and in mechanisms for repressing the CYP11B1 gene expression in adrenocortical cells. This is a non catalytic peptidase C1 family protein (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MWGCPLGLLLLLLAGQAALEARRSRWRRELAPGLHLRGIRDAGGRYCQEQDMCCRGRADECALPYLGATCYCDLFCNRTVSDCCPDFWDFCLGIPPPFPPVQGCMHAGRIYPIFGTYWENCNRCTCHEKGQWECDQEPCLVDPAMIKAINRGNYGWQAGNHSAFWGMTLDEGIRYRLGTIRPSSSVMNMNEIYTVLGQGEVLPTAFEASEKWPNLIHEPLDQGNCAGSWAFSTAAVASDRVSIHSLGHMTPILSPQNLLSCDTHHQKGCRGGRLDGAWWFLRRRGVVSDNCYPFSGREQNDEASPTPRCMMHSRAMGRGKRQATSRCPNSQVDSNDIYQVTPVYRLASDEKEIMKELMENGPVQALMEVHEDFFLYQRGIYSHTPVSQGRPEQYRRHGTHSVKITGWGEETLPDGRTIKYWTAANSWGPWWGERGHFRIVRGINECDIETFVLGVWGRVGMEDMGHH
The following text describes a protein:
Function:
Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and host cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter.
Subcellular Localization:
Secreted. Host cell membrane. Note=Secreted as a soluble precursor.
Domain:
The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation.
Sequence:
MQKIKLTGLSLIISGLLMAQAQAAEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPGYNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPVPLAADSKVRRARSVDGAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ
The following text describes a protein:
Function:
Polycomb group (PcG) protein. While PcG proteins are generally required to maintain the transcriptionally repressive state of homeotic genes throughout development, this protein is specifically required during the first 6 hours of embryogenesis to establish the repressed state. Component of the Esc/E(z) complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3, leading to transcriptional repression of the affected target gene. The Esc/E(z) complex is necessary but not sufficient for the repression of homeotic target genes, suggesting that the recruitment of the distinct PRC1 complex is also required. Required for the correct spatial expression of the homeotic genes of the Antennapedia and Bithorax complexes.
Subcellular Localization:
Nucleus. Chromosome. Note=Associated with chromatin. Colocalizes with many PcG sites on polytene chromosomes. It also associates with many unique sites on polytene chromosomes.
Domain:
The PHD-type zinc fingers mediate the interaction with E(z); In contrast to vertebrate homologs (PHF1, PHF19 and MTF2), the Tudor domain does not bind H3K36me3.
Sequence:
MMNNHFHLQHDHPPQNVAHPFMQQPSTAVPSAPPATYGYLAQPAGQQPQWMTTTYQILPPSVGPATVAKRYYATTGPQTTHPTHPSTIQITNSFAQQSTPPKQQAATSCSPFKANNIRIISTAPSVYSLNKPPQEAHSTYAPVQSYYLPSGGGQTAGQINLLAASGTGKQLQPPPLVPVTNSTSPPSTVVLDRINICINNHYTETPTSLSSSLTTAQQPSPIIPAIQHKAILPLIDSSTADSSSCSSSSVSSSSYSGTATTSAAVVIVDEPDSTTTTPQTPPTTPEAMSSPGKSSPSPPLLATQSLLKGVNSMKPSFKTVEAAPPTPPTPPSPPPPPPAPPVAAPSPAVTYALQEDVFIKCNDGRFYLGTIIDQTSDQYLIRFDDQSEQWCEPDKLRKLGGGSSITAGGGGASTTESTNTSPSGPMCVACKRSDIEDVVEICERCGRGYHRGCTVEIVTGSGIWSCKRCAKPMKMQQPVSHKITKPAGICRQLPYHADKLSWDEKHRVNEEQIYCYCGKPGKFDHNMLQCCKCRNWFHTQCMQNFKKKLLRGDMFFVFCCTVCNNGIEFVRRMQIEWVDVLHIALYNLRKHQHQKYHHLLNDIWPFILEQRHQLPICEKWRTLPETALMERLKQTLKDYSDRFVCGREFKRAPAFYALRHSGPPHIPKVFLEPHEELSDELLEKRFKLMLMPEEPDEGANELPKRVPKDVYEFNTDEDDPVETSEDEIPIKQIIEKAKKQAAQKADKHDELPLKPDLADDNANDGDPGKLPAPIPPLLDANSSRKRKAFRLSKRYDNSRNHCDLSSDENSSSSRGTSSLDLIIPPPVNFLGRNNPFLMATPKKASQGRSISVGTGVGVNGIINSIFKLKGTSKEQPRMVRTIKRRLSAKDITIGPNQEVRRRRTRRLTTAIEVISTTTINPIPSHYLPIYAKDLQPPAPPMGKPTHGRLLRQRPQKQSPSQSRRNSTSSTATSSSSNGIGAPGHSMLDLKQSVNKYFGGAMNRIDAGEPFAIRAKRRMGNGQVQYLVEWGGDTATTAIGLLGN
The following text describes a protein:
Function:
Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element.
Subcellular Localization:
Nucleus.
Sequence:
MNPQANDRKEFQGDCSATGDLTAKHDSAGGNGGGGARYKLMSPAKLPISRSTDITIPPGLSPTSFLESPVFISNIKPEPSPTTGSLFKPRPVHISASSSSYTGRGFHQNTFTEQKSSEFEFRPPASNMVYAELGKIRSEPPVHFQGQGHGSSHSPSSISDAAGSSSELSRPTPPCQMTPTSSDIPAGSDQEESIQTSQNDSRGSTPSILADDGYNWRKYGQKHVKGSEFPRSYYKCTHPNCEVKKLFERSHDGQITDIIYKGTHDHPKPQPGRRNSGGMAAQEERLDKYPSSTGRDEKGSGVYNLSNPNEQTGNPEVPPISASDDGGEAAASNRNKDEPDDDDPFSKRRRMEGAMEITPLVKPIREPRVVVQTLSEVDILDDGYRWRKYGQKVVRGNPNPRSYYKCTAHGCPVRKHVERASHDPKAVITTYEGKHDHDVPTSKSSSNHEIQPRFRPDETDTISLNLGVGISSDGPNHASNEHQHQNQQLVNQTHPNGVNFRFVHASPMSSYYASLNSGMNQYGQRETKNETQNGDISSLNNSSYPYPPNMGRVQSGP
The following text describes a protein:
Function:
Specific functional receptor for IL17C. May be signaling through the NF-kappa-B and MAPK pathways. May require TRAF3IP2 /ACT1 for signaling. May be a crucial regulator in innate immunity to bacterial pathogens. Isoform 2 and isoform 4 may be either cytoplasmic inactive or dominant active forms. Isoform 3 and isoform 5 may act as soluble decoy receptors.
Subcellular Localization:
[Isoform 1]: Cell membrane; Single-pass type I membrane protein; [Isoform 2]: Cytoplasm; [Isoform 3]: Secreted; [Isoform 4]: Cytoplasm; [Isoform 5]: Secreted.
Sequence:
MGSSRLAALLLPLLLIVIDLSDSAGIGFRHLPHWNTRCPLASHTDDSFTGSSAYIPCRTWWALFSTKPWCVRVWHCSRCLCQHLLSGGSGLQRGLFHLLVQKSKKSSTFKFYRRHKMPAPAQRKLLPRRHLSEKSHHISIPSPDISHKGLRSKRTQPSDPETWESLPRLDSQRHGGPEFSFDLLPEARAIRVTISSGPEVSVRLCHQWALECEELSSPYDVQKIVSGGHTVELPYEFLLPCLCIEASYLQEDTVRRKKCPFQSWPEAYGSDFWKSVHFTDYSQHTQMVMALTLRCPLKLEAALCQRHDWHTLCKDLPNATARESDGWYVLEKVDLHPQLCFKFSFGNSSHVECPHQTGSLTSWNVSMDTQAQQLILHFSSRMHATFSAAWSLPGLGQDTLVPPVYTVSQARGSSPVSLDLIIPFLRPGCCVLVWRSDVQFAWKHLLCPDVSYRHLGLLILALLALLTLLGVVLALTCRRPQSGPGPARPVLLLHAADSEAQRRLVGALAELLRAALGGGRDVIVDLWEGRHVARVGPLPWLWAARTRVAREQGTVLLLWSGADLRPVSGPDPRAAPLLALLHAAPRPLLLLAYFSRLCAKGDIPPPLRALPRYRLLRDLPRLLRALDARPFAEATSWGRLGARQRRQSRLELCSRLEREAARLADLG
The following text describes a protein:
Function:
Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. Recruited to the 19S regulatory particle of the 26S proteasome through its interaction with 19S component PSMD2/RPN1. Once recruited, dephosphorylates 19S component PSMC2/RPT1 which impairs PSMC2 ATPase activity and disrupts 26S proteasome assembly. Has also been reported to stimulate the proteolytic activity of the 26S proteasome.
Subcellular Localization:
Nucleus.
Sequence:
MNECPPRAAPPPSGRVQLGGGGGRACAVPAGAWPSPAAWRAFWAVRPITAASGPPSSRQIRPPSLLRSAPPGAVSGPRRPPSSRRLPVDGRHFRRAPAALPVDGRHFRRAPAALPAGGRHFRWAPAGPLGLQWPAPVGTRLRFFWQYNHWSYASRMSLSLIIKWGGQEYSITTLSEEDTVLDLKQSLKTLTGVLPERQKLLGLKVKGKPAENDVKLGALKLKPNTKIMMMGTREESLEDVLGPPPDNDDVVNDFDIEEEVVEVENREENLLKISRRVKDYKVEILNPPREGKKLLVLDVDYTLFDHRSCAETGVELMRPYLHEFLTSAYEDYDIVIWSATNMKWIEAKMKELGVSTNANYKITFMLDSAAMITVHTPRRGLIDVKPLGVIWGKFSEFYSKKNTIMFDDIGRNFLMNPQNGLKIRPFMKAHLNRDKDKELLKLTQYLKEIAKLDDFLELNHKHWERYLSKKQGQ
The following text describes a protein:
Function:
Acts as an acyl-protein thioesterase that hydrolyzes fatty acids from acylated residues in proteins. Regulates the mitochondrial S-depalmitoylation of the nucleophilic active site residue of peroxiredoxin-5/PRDX5, a key antioxidant protein, therefore modulating mitochondrial antioxidant ability. Also catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, an active metabolite of the immunosuppressant drug mycophenolate.
Subcellular Localization:
Mitochondrion.
Sequence:
MHKLYNKTQDKFIVYDNYRIINTNIPSVIFLHGLMSSMKSTKAIYLIDYCKKNNYNFIVFDNFGHGNASGQFEDQTISDWLEGVSLILDKLIDKEAILVGSSMGGWLALLAALRFPDKIKGLVCVAPAPDFTENIWQNISLNDQNKMQKEGILEVSGKNCEHKYPISYKLIEDAKKHLLLTKKQIDINTPLHIIHGMLDEDVPYNVSVKLLEKITSKQIVMKLIKDGHHNLSREEDLKVMTNSLEEVISLSNIK
The following text describes a protein:
Function:
Probable O-linked N-acetylglucosamine transferase (OGT) involved in various processes such as gibberellin (GA) signaling pathway and circadian clock. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by adding O-linked sugars to yet unknown proteins. Acts as a repressor of GA signaling pathway to inhibit hypocotyl elongation. Functions with GIGANTEA (GI) in pathways controlling flowering, circadian cotyledon movements and hypocotyl elongation. Acts as a light-regulated promoter of elongation via its interaction with GI. Acts as an activator of cytokinin signaling. Required with SEC for gamete and seed development. Its OGT activity has been proved in vitro but not in vivo. Possesses O-fucosyltransferase activity on specific serine and threonine residues. Mediates O-fucosylation of the DELLA protein RGA, a repressor of the GA signaling pathway. O-fucosylation enhances RGA activity by promoting RGA binding to key transcription factors in brassinosteroid and light-signaling pathways. Regulates root hair patterning upstream of the transcription factor WER, independently of DELLA proteins and GA signaling. Involved in abscisic acid (ABA) signaling partly through functional ABAR. Mediates O-fucosylation of CPN20 that may depress ABA responses during seed germination and seedling development. Involved in the modulation of the pace of the circadian clock by mediating O-fucosylation of APRR5, one of the core circadian clock components. O-fucosylation promotes APRR5 proteolysis.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The TPR repeats mediate protein-protein interactions and are essential for its function. Expression of such repeats in plants accelerate flowering.
Sequence:
MVGLEDDTERERSPVVENGFSNGSRSSSSSAGVLSPSRKVTQGNDTLSYANILRARNKFADALALYEAMLEKDSKNVEAHIGKGICLQTQNKGNLAFDCFSEAIRLDPHNACALTHCGILHKEEGRLVEAAESYQKALMADASYKPAAECLAIVLTDLGTSLKLAGNTQEGIQKYYEALKIDPHYAPAYYNLGVVYSEMMQYDNALSCYEKAALERPMYAEAYCNMGVIYKNRGDLEMAITCYERCLAVSPNFEIAKNNMAIALTDLGTKVKLEGDVTQGVAYYKKALYYNWHYADAMYNLGVAYGEMLKFDMAIVFYELAFHFNPHCAEACNNLGVLYKDRDNLDKAVECYQMALSIKPNFAQSLNNLGVVYTVQGKMDAAASMIEKAILANPTYAEAFNNLGVLYRDAGNITMAIDAYEECLKIDPDSRNAGQNRLLAMNYINEGLDDKLFEAHRDWGWRFTRLHPQYTSWDNLKDPERPITIGYISPDFFTHSVSYFIEAPLTHHDYTKYKVVVYSAVVKADAKTYRFRDKVLKKGGVWKDIYGIDEKKIASMVREDKIDILVELTGHTANNKLGTMACRPAPVQVTWIGYPNTTGLPTVDYRITDSLADPPDTKQKQVEELVRLPDCFLCYTPSPEAGPVCPTPALSNGFVTFGSFNNLAKITPKVLQVWARILCAVPNSRLVVKCKPFCCDSIRQRFLTTLEQLGLESKRVDLLPLILFNHDHMQAYSLMDISLDTFPYAGTTTTCESLYMGVPCVTMAGSVHAHNVGVSLLTKVGLGHLVAKNEDEYVQLSVDLASDVTALSKLRMSLRDLMAGSPVCNGPSFAVGLESAYRNMWKKYCKGEVPSLRRMEMLQKEVHDDPLISKDLGPSRVSVTGEATPSLKANGSAPVPSSLPTQSPQLSKRMDSTS
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:
MNSTSTSSYEHDVPVKYIRTLDARLLPPRVGHNWLDAAFRSVQGKPQQLEEEFRGKRAFMPPGVYDHTPPEGLGLTARQLMQALSTRRKDGPAPDGRPIFTTLSDKVLRFYAFFSEKAPEGCCEEYWHRCVVINFYPEDDTVLIQEPPIPNSGLPGGTFLKRQKVRADPRQREQFPSDEFLTINHFNVGYSVRINCVEFFLYDCDAFTRDFLTEIGVDVGEPMQYPDSSFMSQWKHQQEQRATTNYGIVSNNYYRDDAVRAARFVLDAGKVLRFYGLLDERDKTTGGAVRKLEVLYFVEDDSIAVVERPTTNEAVPALFLSRGWLPKAGSIEKTLEFTFAHRVNGMREPYVGPGGCYTARDLGVGATINVLGRGVFLYDCDDFTRSYYKETFGVELAEAIDGLSQYGLPSKPDVVSFRSNATPASAPATVAPKVVETNVIIKKGDVLRFLLRLSAPCTSAERMRRFTLTHYTATGDSMVYESPIKNSGYVGGCFSSRSRIPNPAGGPGAYYTHEDFKVGSIIVINAHKFEVMNMDEHTANFLACKGETALNEEQLRLLVDAFRLFLRTRFHSFRDAFLGFDRDKDSVISVTEFVDHVTHLQITDRRMDAQALFDSICQNPETGYLTLETFVDWINQKGSESCGDAKSSQPINIDERALMRKALCQLCERLEARCLNSLQMFRLASTMPRAYSGRRADCYSLTNPHRDAYITPVQLRRCIEEVLGGNPSPRELDALLFFFFPALPPEEYRVKRDISLEHSLDLKAFQKKYHEMCTLQQLS
The following text describes a protein:
Function:
Receptor for prokineticin 1. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase. May play a role during early pregnancy (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
METTVGTLGENTTNTFTDFFSARDGSGAETSPLPFTFSYGDYDMPSDEEEDVTNSRTFFAAKIVIGMALVGIMLVCGIGNFIFITALARYKKLRNLTNLLIANLAISDFLVAIVCCPFEMDYYVVRQLSWEHGHVLCASVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLRPRMKCQTAAGLIFLVWSVSILIAIPAAYFTTETVLVIVESQEKIFCGQIWPVDQQFYYRSYFLLVFGLEFVGPVIAMTLCYARVSRELWFKAVPGFQTEQIRRRLRCRRRTVLGLVCVLSAYVLCWAPFYGFTIVRDFFPSVFVKEKHYLTAFYVVECIAMSNSMINTLCFVTVRNNTSKYLKRILRLQWRASPSGSKASADLDLRTTGIPATEEVDCIRLK
The following text describes a protein:
Function:
Possible adhesion molecule with a role in early hematopoiesis by mediating the attachment of stem cells to the bone marrow extracellular matrix or directly to stromal cells. Could act as a scaffold for the attachment of lineage specific glycans, allowing stem cells to bind to lectins expressed by stromal cells or other marrow components. Presents carbohydrate ligands to selectins (By similarity).
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MLAGRGARAGGGLPRGWTALCLLSLLPFGFTNTETVITPTTVPTSTEIMSAVSENTSKREAITLTPSGTTTLYSVSQDSSGTTATISETTVHVTSTSEITLTPGTMNSSVQSQTSLAITVSFTPTNFSTSSVTLEPSLLPGNGSDPPYNSTSLVTSPTEYYTSLSPTPSRNDTPSTIKGEIKCSGVKEVKLNQGICLELNETSSCEDFKKDNEEKLTQVLCEKEPAEAGAGVCSLLLAQSEVRPHCLLLVLANKTELFSKLQLLRKHQSDLKKLGIRDFTEQDVGSHQSYSRKTLIALVTSGILLAVLGTTGYFLMNRRSWSPTGERLGEDPYYTENGGGQGYSSGPGVSPEAQGKASVNRGPQENGTGQATSRNGHSARQHMVADTEL
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MIRKIVTSLKQFRRTYEDQKLGRQLVGTDPHGNLYYQYYDQNGKPTRRMSERTDKMAPFVDPLWEEWIRHIRDKPYTEEERMELEKQQRAYKTKVNEYEQKDAEMMQQFKKSNKTWNANKK
The following text describes a protein:
Function:
Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Sequence:
MNSLLLLSIGATLLPIVWTAVPTASISAHVLDISGGSPAKGIQILAYIQKNDAWTNIGAQFTQDNGRVDWVSPNFTLIAGTYRLVYVTKPYYTDKGIDSFYPYVEVVFDIRDPTQHYHVPLTLSPWGYSTYRGS
The following text describes a protein:
Function:
Histone methyltransferase.
Subcellular Localization:
Chromosome, centromere. Nucleus.
Sequence:
MVRVGLSSAPGVNLTEQIDNVFDQLINKIEHADFDTRPFLKQLNVLGRYEPIKRNVYCTKRRIEDYGISCHCKPSPGSSVVCGRDCHCGMLFSCCSSQCECDDTCTNKSFQHRPLKKTKLIKTEKCGHGLVAEDEIKKGEFVIEYVGEVIDDRTCENRLWTMKRLLDTDFYLCEVSSNMVIDATNKGNRSRFINHSCEPNTAMQKWTVDGETRVGIFALRDIKIGEELTYDYNIMYRFVQFGAAQVCHCGSSNCRKMLGTTKYSGSSQNHHAKKKKRKTSCENCIQQFLRLWHPHKKMYVGCWIIDFDQETKMHTLKFNDLHTEKFNLKEEEWHFLEVDFDED
The following text describes a protein:
Function:
Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs; Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MRPPRGGGFRGGRDGGRGGRGGRGRGGGRGGGGGFRDEGPPSEVVEISAFLHACEGDAVTKLTNEKIPYFNAPIFLQNKTQIGKVDEIFGPINESYFSIKMMEGIVATSYSPGDKFYIDPNKLLPLARFLPQPKGQAQAAARGGRGGGRGGGRGGGRGGGGFRGRGGPRGGRGRPPRGGRGGGFRGRGRF
The following text describes a protein:
Function:
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules via their alpha domain, in particular TRAV27. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of pro-inflammatory cytokines. Also causes the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death.
Subcellular Localization:
Secreted.
Sequence:
MINKIKILFSFLALLLSFTSYAKAEDLHDKSELTDLALANAYGQYNHPFIKENIKSDEISGEKDLIFRNQGDSGNDLRVKFATADLAQKFKNKNVDIYGASFYYKCEKISENISECLYGGTTLNSEKLAQERVIGANVWVDGIQKETELIRTNKKNVTLQELDIKIRKILSDKYKIYYKDSEISKGLIEFDMKTPRDYSFDIYDLKGENDYEIDKIYEDNKTLKSDDISHIDVNLYTKKKV
The following text describes a protein:
Function:
Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3). Plays a role in the recycling of transferrin receptor to the plasma membrane.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side. Early endosome membrane; Lipid-anchor. Note=Enriched in endosomes that are in close proximity to clathrin-enriched regions at the cell surface.
Sequence:
MASLDDPGEVREGFLCPLCLKDLQSFYQLHSHYEEEHSGEDRDVKGQIKSLVQKAKKAKDRLLKREGDDRAESGTQGYESFSYGGVDPYMWEPQELGAVRSHLSDFKKHRAARIDHYVVEVNKLIIRLEKLTAFDRTNTESAKIRAIEKSVVPWVNDQDVPFCPDCGNKFSIRNRRHHCRLCGSIMCKKCMELISLPLANKLTSASKESLSTHTSPSQSPNSVHGSRRGSISSMSSVSSVLDEKDDDRIRCCTHCKDTLLKREQQIDEKEHTPDIVKLYEKLRLCMEKVDQKAPEYIRMAASLNAGETTYSLEHASDLRVEVQKVYELIDALSKKILTLGLNQDPPPHPSNLRLQRMIRYSATLFVQEKLLGLMSLPTKEQFEELKKKRKEEMERKRAVERQAALESQRRLEERQSGLASRAANGEVASLRRGPAPLRKAEGWLPLSGGQGQSEDSDPLLQQIHNITSFIRQAKAAGRMDEVRTLQENLRQLQDEYDQQQTEKAIELSRRQAEEEDLQREQLQMLRERELEREREQFRVASLHTRTRSLDFREIGPFQLEPSREPRTHLAYALDLGSSPVPSSTAPKTPSLSSTQPTRVWSGPPAVGQERLPQSSMPQQHEGPSLNPFDEEDLSSPMEEATTGPPAAGVSLDPSARILKEYNPFEEEDEEEEAVAGNPFIQPDSPAPNPFSEEDEHPQQRLSSPLVPGNPFEEPTCINPFEMDSDSGPEAEEPIEEELLLQQIDNIKAYIFDAKQCGRLDEVEVLTENLRELKHTLAKQKGGTD
The following text describes a protein:
Function:
May act as a component of the auxin efflux carrier.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MITLQEFYTVMSAVVPLYVAMILAYGSVRWWKLLTPAQCSGINRFVAIFAVPLLSFQIIAHNNPYDMNPRFVAADVLQKLIVLAVLASWSRLKKFSSSVRSTSDTKSKDLDWAITLFMVSTLPNTLVLGIPLEVAMYGEKPAELVVQAVVLQCIVWYTLLLFLYEYRSAKNLILEQFPGPSAANIVSFRIDPDVISLDGEQQQIKTEAEIGQDGKIHVQVKRSPPPQPPPLPPTSSMYREYDSSSISLLRSPGLVSPLSSKAGTPRASDLTGVEIYSVQSSRNMTPTGSYTDLGLMTGTHGSSPHLRPSSNNPGLSIETSTTLSSNELPHYSNHSSNMHTPREPPSEEQSNMFAYTPGRHHYSPSPKTTTGPAAHDELQKQVPRSPGPLERLFVGNQVFSPMKLAEAARKMDYQQQQYESREMQMLVWSSSNSPASDRGCYETRKLTSHKNLSIQIPSNSTPLHPCMAKDFSFVDNVLFQREDTTPLSEKNLKSESHLPCKVPFTPPKLVDSDSSAPTQMPPPTVMTKLIVRMMWKKLIRNPNTYASLLGLAWALISFRWNVGMPKILEHSITILSDAGLGMAMFSLGLFMALQSSLIACGTTMAVVVMIIRFVTGPAIMSATSIAVGLRNVQLRASIIQAALPQGIVPFVFAKEYNVHPDVLSTAVIFGMLISLPINLLYYVLLGL
The following text describes a protein:
Function:
Secreted protein cleaved by KEX2 in 8 similar peptides (ECE1-I to ECE1-VIII). Stimulates biofilm formation; [Candidalysin ECE1-III]: Acts as a cytolytic peptide toxin that directly damages host epithelial membranes, triggers a danger response signaling pathway and activates epithelial immunity. Probably acts similarly to cationic antimicrobial peptide toxins, inducing lesions after binding to target cell membranes and causing an inward current associated with calcium influx.
Subcellular Localization:
Secreted; [Candidalysin ECE1-III]: Host cell membrane; Single-pass membrane protein.
Domain:
The N-terminal alpha-helix of peptide ECE1-III allows insertion of the toxin into host epithelial cells membranes.
Sequence:
MKFSKVASFAFLALSSQAALIQHDVIIENIKRDAVLAGSAENNIASSAFTKRESEVDSSEDVQLEKRISFAGIVSSIINQLPSIIQIIGNIIKAGLVKRDDIDDAFALVLAEYPHIVSVFEDAFGDFTEAKRDEAASVGTQILGSFPSILTQVVNGFSKVLDFANSDTFSTGLSILSNFTSIASSFASSLSSVVQNGKRDGVEDIVSMVVRQIPDLIVEASTPFVTNAEKMKRDADVAASLVDNLVKKGLSTAIDTFGAATVASVVSKRQVSSFLSKVLSKA
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MSRILKSLSRSYSTTSPRLYVDVVQGLYISSLKSYKPKAVPSETAAEVKEWSMPSAPTAPKYDVDFTSALNSYKYEGETIPTKAAGESNKFDFLESYENEKEH
The following text describes a protein:
Function:
DNA-binding protein that plays a critical role in nucleoid compaction, genome replication and DNA replication and transcription. Binds to both ssDNA and dsDNA with a binding site covering about 15 nucleotides. Displays DNA-supercoiling activity only when associated with the viral DNA topoisomerase 2.
Subcellular Localization:
Virion.
Sequence:
MAKVPPKPPTKTQIIANIAEETELTKKDVAAVLDSLAAEIEKSLQKGGPGQFAIPGLCKIVLKDVPAKPKRKGRNPANGEEIWLAPKPASKKLTIRPLKGLKEMI
The following text describes a protein:
Function:
Probably plays a role in host phagosome maturation arrest.
Sequence:
MPVEETSTPQKLPQFRYHPDPVGTGSIVADEVSCVSCEQRRPYTYTGPVYAEEELNEAICPWCIADGSAASRFDATFTDAMWAVPDDVPEDVTEEVLCRTPGFTGWLQEEWLHHCGDAAAFLGPVGASEVADLPDALDALRNEYRGYDWPADKIEEFILTLDRNGLATAYLFRCLSCGVHLAYADFA