lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Binds lactose. May play a role in fruiting body formation.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Secreted, cell wall. Endomembrane system. Note=Detected in extracellular matrix, cell wall and cytoplasmic membrane-bound bodies.
Sequence:
MLYHLFVNNQIKLQDDFKAEAVATIRSSVFNSKGGTTVFNFLSAGENILLHISIRPGENAIVFNSRTKGGAWGPEERVPYAGKFKGPNPSITVLDHGDRFQILFDNATAIYYTKRIKENAAAIAYSAENSLFSSPVTVDIHGLLPPLPPA
The following text describes a protein:
Function:
Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endomembrane system; Multi-pass membrane protein.
Sequence:
MVTPSFIVGIIGNVISILVFTSPIKTFRQVVKRKSTENYKGIPYVTTLLSTSLWTFYGLLNPNGLLVITVNGAGAIFQAIYVILFLVYAPMDKKVQTGTLVAIFNVGFLGLVIAVTLLAMHGSLRLTFVGILCVVLTIGMYAAPLSAMRRVIKTKSVEYMPFLLSFFLFLNATIWTIYSVLVKDFYIGVPNATGVVLGSGQLIVYAIYKNKSVLPEKSIEKIDEEEGSAHLVKAAGGVIEMGGLEVEDEEANYLKNRSLRKGRSLSKPSHVDRQHSI
The following text describes a protein:
Function:
Iron-sulfur subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSRADDDAVGVPPTCGGRSDEEERRIVPGPNPQDGAKDGAKATAVPREPDEAALAAMSNQELLALGGKLDGVRIAYKEPRWPVEGTKAEKRAERSVAVWLLLGGVFGLALLLIFLFWPWEFKAADGESDFIYSLTTPLYGLTFGLSILSIAIGAVLYQKRFIPEEISIQERHDGASREIDRKTVVANLTDAFEGSTIRRRKLIGLSFGVGMGAFGLGTLVAFAGGLIKNPWKPVVPTAEGKKAVLWTSGWTPRYQGETIYLARATGTEDGPPFIKMRPEDMDAGGMETVFPWRESDGDGTTVESHHKLQEIAMGIRNPVMLIRIKPSDLGRVVKRKGQESFNFGEFFAFTKVCSHLGCPSSLYEQQSYRILCPCHQSQFDALHFAKPIFGPAARALAQLPITIDTDGYLVANGDFVEPVGPAFWERTTT
The following text describes a protein:
Function:
Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src-family tyrosine kinases. Represses BCR signaling during development of immature B-cells.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MAKPILEGAARPSALLAPRRPTIQVPGRAVELKQRAGPCCQALWVDWGPPSVTVSVGDKVSLPCRHNSNSTNITWWRVPQGNSTWPPVMDLSELGPKGELIIQQVNKSHRGMYRCEVNEGQRIQRSCGTYLRVRDPLPRPFLDMGEGTKNNIITAEGIILLICAVVPGTLLLFRKRWQNVKFGADVQDDYDDENLYEGLNLDDCSMYEDISRGLQGTYQDVGSLHIGDVQLEKP
The following text describes a protein:
Function:
Has a role in transcriptional regulation. Acts in parallel with the Ras/MAPK and the PI3K/PKB pathways in the control of cell identity and cellular growth. Essential for regulation of the cytoskeleton and cell growth but not for cell proliferation or growth rate. Required specifically for the microtubule-based basal transport of lipid droplets. Plays a partially redundant function downstream of Raf in cell fate specification in the developing eye. Pair-rule protein that regulates embryonic cellularization, gastrulation and segmentation.
Subcellular Localization:
Nucleus.
Sequence:
MKRSDIESSGSESDAENTSESESESEESDIDETPPPSPPPPKKKSYSLMNQIRKVQKEMPQMAPSTPPIRGPPSVENPLSNSRLDPNEGSKHPEQSAESGDDNDNFSKYNNSQPPTFTDFHQLSESSHESKASPSSVKSKGGSKSSTKPLGSSKPTVKRPQSRTDNSSSSKASSAKDTSSSPRVKPESNSKESTKAKSSKQSSKSASSGQNKKSPGPGAGAKSSSKSQEKKPGQRAKTSEKKKNIKPIIKSNQFVSDSDSEDERTPLRPSSKAAINTSTSSSGSSSSSNLDTSYPVRQTKVEPDSGKRMPGVKKGDNKYIVKPEPLDTYEHRRPPFDDFAHMDPIVSPIRADFIDEQSRPLDRHPEIKFDKDGKPSVFVRLKRELFDHLPKSSVIKFEQNVPGTSTQKRKDSNDPPEKPSAIVKPVKRKQTELEKEKSGRPENKRSRIENKSPRRMREEALRGVRDEPTEALEPFVSSESSLDRRQSSDRRGSVSSMTSQQSSHSSRRTKNDCDPHHPSSRSKRDSSRSRDFASQRLHDWTSPERHADRSVEMPHNVALGGGEADPAASSHRNGGLSHSHSHSLPPHAHHSTASHPHRGVEGEDWRVFPPAESYQGYGEEAQSRHRLELDERQFTADDYLAEGKKLKHLADTQVDKHAKALTYFEAVVYLTSCGNVFELDPLVPDDKAVTMYSDTCEIIRYILKLKGIHNGQEGNSNDNKLAVLCYRCQALLNMHMFKLKRQSAMNLSRALTEHLKGTSSKPQPPLQQNPSSWNSSSRYTGTPSPVSPTPSAAGSVGSACSMGSQGSTSSDLVPSQTSGGGPAPPSGPGAKLCNGLNPQSSTVAMPQHIVRIMSQFLTYSNYSLYSIQYWEQADILTEENKDFFRDLARECGELTLHSSTRDLVHYVRRGLTNLRRL
The following text describes a protein:
Function:
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence:
MTITISAVILAGGKARRMGGQDKGLQILGKQSLIEHIINRLQPQIHQISINANRNQTEYAKFGFPVFSDELPDFQGPLSGMLTALEKTKSDFILFTPCDTPFFPMNLLDKLKSAVKNDRTLIAYACDEEREHPVFCLMSVQLKEKLRHYLASGERRLLQFMKENGGISVKFTQEEGNFENFNTLDDLKKTVI
The following text describes a protein:
Function:
Protein component of the posterior mating plug.
Subcellular Localization:
Secreted.
Sequence:
MKMILALVVLGLVLVAAEDKYTTKYDNIDVDEILKSDRLFGNYFKCLVDNGKCTPEGRELKKSLPDALKTECSKCSEKQRQNTDKVIRYIIENKPEEWKQLQAKYDPDEIYIKRYRATAEASGIKV
The following text describes a protein:
Function:
Catalyzes the formation of 41 N(4)-acetylcytidine (ac(4)C) sites in RNA, almost always on the middle C of a CCG motif. Modifications are found mostly in tRNA, with small amounts found in rRNA and mRNA; Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Subcellular Localization:
Cytoplasm.
Sequence:
MIFDIVKRDVEKARSARHRRLIVLVGRDDRRLAEAAGEALRGYEAAGGRGTGLYMFQPEFADANKRMNYLRDLIEGSSLEVEFRPYKDTPRILGTTYDFAVLDLVNDLKPNDVGRLGGVVRGGGIYVFLVPPLDVWKKYITKFQATLLVPQFTPNDIKHRLKDRFWQSLYSHKGVIIYDVDRDVLLKSFGIEDVQPHEPKKPEPPEKAVLPLKIYRLAATQDQVEVLKLFEVFYHKPKKKQALVIIADRGRGKSAALGLGLAGIGHKLRKAKARVQIVVSAMEYSNLETLLEFALKGLEALGYKPGVEREGGEIRAIKASGIFIDVVTPYMLLKRENADIVAIDEAAGVPLPVLYAVHKKFNRLVFATTIHGYEGAGRGFSIRFLKYLKEARDTDVYLYEMEEPIRYGRGDPVEEWLFDAFLLNAEPAKIEAEDLEYVKRQEVLYLKEEDILKSEEVFRQFFGIYVQAHYRNEPDDLGMLLDAPHHTARALALPNGKIVVSVELAYEGGLDDLSIDQALRGLKLPGNIIPDRFLKYWRLPEFAKLRGWRIVRIATHPELQDMGLGTLMLKKIEEEARELGMDYVGVGFGVYDRLLKFWVRNGYVPIHLSPERNPSSGEYSVLLVKPLNEKAEAYVKYANIEFRRRLIHSLMGPYGDLLPTEVQLLLEDWGWDIDSPPALSKNQLDRLIAYAYGPMTYENVTDAVYMLATQYFYSSKGRRPALPDVAIRILISKVLQAKPWKEAAEAAGVRRGDLMLILREVVKVLLFYYYGGEFEVPLFVVGTVKGRD
The following text describes a protein:
Function:
Probable serine endoprotease which cleaves preproteins at paired basic amino acids. May process FMRFamide-like (flp) and neuropeptide-like protein (nlp) neuropeptides. In muscles, involved in neuronal retrograde signaling by regulating presynaptic activity and localization of synaptic vesicle fusion protein unc-13 at the neuromuscular junction (NMJ). Acts in the intestine to regulate anterior body muscle contractions (aBOC) and the expulsion steps during the defecation motor program (DMP). Probably by regulating DMP, required for fatty acid uptake by intestinal cells and therefore regulates the levels of triglycerides in the intestine. Plays a role in locomotion.
Subcellular Localization:
Secreted.
Sequence:
MKLIFLLLLFGVSPIVCQDFEDGVFLAKITSIDEHDARKIGRRFGFEAQWKLQSYTDVYVGRRLRRRKRGIEDEIVAEMMLSQQVQFIEKLQGFRRYKRAPMTNKGYPVHVWNLTPSLYIREAWEDGFNASRVTVAVVDDGVDIKHVDLKSAFSPRVSFDFVRFGDLPTPKNSKEFEHGTQCAGLVAMEGQQCGLGVGHGATLGAIKLLGQDFLNDALEGDALAFQKDLIDIYSVSWGPKDDGKSAEKPAKFTEEAIKNGALHGRNGKGNIFVWASGNGGVNGDNCAYDGYVSNEYTLSFGVIDASGAPAAYGEGCSSVLAAVSGGDAMIQTTGLESTCSSISGSSASAAIASGIISLVLDANPTLSQRDIQHLIARTSNASAIRDVELYENSAGLNFHPKVGFGLLNAQKLVVMAATWENVAPQVTCEKMNLANGIIDNSDCDVTKVERVIVSGSIIHPHRGQVQIRLESPRGTISELLPLRPKDTSRDLLDWNFVSVNFFGENSRGIWKLHVTSEEDDVDFRVEMKMFKVVGTMS
The following text describes a protein:
Function:
May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Subcellular Localization:
Endoplasmic reticulum. Golgi apparatus, cis-Golgi network.
Sequence:
MSRSLNRKQDIYRIDWQLPAVSSSASAHHINRDLFVLSYGALVAQLCKDYERDEDVNKYLDAMGYNIGIRLIEDFLANTGIKKCRSYNETVDVIAKVAFKTYLGITPTLIGGNDGGNSFSLILDTNPLDDYVEELPPGRSSLSYCNLLSGIIRGALEMIHLPADVSFIQDRLKGDDVTEIGITFLQKSNERKSKRNK
The following text describes a protein:
Function:
Participates in the control of the reentry into the cell cycle following pheromone treatment.
Miscellaneous:
MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
Sequence:
MNASGRSHSKGPIIRSVSLEDLKRNSSFKGNLKYKDEVTSHKEPQVGTLSNEELLKDLDNMLRGKLNMGRNSFHADKRNKSDGNISALTFKARSGLEGDIRTIDIQQDSSDENDNFKFSDDGVNKDRNNEKDNNTDNAVEFQDDAEEAEEENEDESFANVDELDGFDLNKVSDGKHVPINEKGEVDYNMPVDKEFQKSLDQCAASLEERSSAPYALQRAVDWELKMFYSLEDELSEWFCSSDYMHFGQTQTLFKQKITQPQLFFDDENYAASVVECLIEDIPNSLASNLLALSYISMGCFAFTNSKSEHTKIIRRNNLMLVPHIQEIVHAFKKIAISCRDDNRNLKKQTILLFHSSTILYFICSICIEGRGENPEAVNVVIDAFEKTDLLEFLTKYIENWRWNSRLAMRIRNMISLLFKLIVLQFGDSSVYKQTKSSIYNLHGLTYPSKHPEKLSISPLHYQAFREDITSRFPDYNMPSSGLPKDVDKSESLSQFLEIPRPKSKNPLNMALIVPEKHIATPAPSPPSSPQLMHLGEGPRPRKSFQTNMAYPCLYPSDNEGSEDDTLEDRIDLNIERKPDNDIVIPFSTEEAARILSESLEIKLSTKQLWYERDLFMITERGWKQQLENEPYDYAALNHDANSSKEEKSAICIMQRIDKYYKSCLSSFNSLVFVLLQTMESSLTNNFHRKSEVSDKNLLNMLTPQLEIVRAKELSLKSAAGILHALLKWFKLSHILKFEHLAVVIHDSRYINTCASILSKYSEVYPERVFNKYVQTPNSFWKECSLSNESYRESYSVDDSGEVDTEIMPSFAYLLRILRKVTGNKTQRLKELPLSIGILFKRYYRLFNLDMYHPILKITRELTPFKNKRWKSEHMELISGVYLYEKLELTDNWVTGKDISGELSDACGQEIALRALLQFYNFQHYEISMEDLGYGHRNSSSQDLLNKESEYLNI
The following text describes a protein:
Function:
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Sequence:
MTTMIVASVATGALATIARWLLTRRSVILREVGPETTPAAPARTAELGLSGAGPTVVHFRAPGCAPCDRVRRGVGDVCADLGDVAHIEVDLDSNPQAARRFSVLSLPTTLIFDVDGRQRYRTSGVPKAADLRSALKPLLA
The following text describes a protein:
Function:
Selectively regulates proliferation and morphogenesis of neural-crest derived pigment cells.
Subcellular Localization:
Secreted.
Sequence:
MHTKVLQQGLWALLLWPHLFTVSVPLDCRDDQASLARCPSISQEKLLDRVIHHAELIYRVSEESCSLFEEMFIPLPLRLQSNQGGYACITKALPIPSSKSEIQQLSDKWLLHSVLMLVQSWIEPLVYLQMTLDRYDHAPDMLLNKTKWVSEKLISLEQGVVVLIKKMLDEGAMTTTYSEQGAFQYDVQLEMLEYVMRDYTLLTCLKKDAHKMETFLKLLKCRQTDKYNCA
The following text describes a protein:
Function:
May be involved in cell wall biosynthesis. May act as a fucosyltransferase.
Miscellaneous:
MISCELLANEOUS: [Isoform Short]: Unstable and lacks the key conserved region and thus would presumably lack the catalytic activity.
Subcellular Localization:
Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi.
Sequence:
MGVFSNLRGPRAGATHDEFPATNGSPSSSSSPSSSIKRKLSNLLPLCVALVVIAEIGFLGRLDKVALVDTLTDFFTQSPSLSQSPPARSDRKKIGLFTDRSCEEWLMREDSVTYSRDFTKDPIFISGGEKDFQWCSVDCTFGDSSGKTPDAAFGLGQKPGTLSIIRSMESAQYYPENDLAQARRRGYDIVMTTSLSSDVPVGYFSWAEYDIMSPVQPKTERAIAAAFISNCGARNFRLQALEALMKTNIKIDSYGGCHRNRDGKVDKVEALKRYKFSLAFENTNEEDYVTEKFFQSLVAGSVPVVVGPPNIEEFAPASDSFLHIKTMEDVEPVAKRMKYLAANPAAYNQTLRWKYEGPSDSFKALVDMAAVHSSCRLCIFLATRVREQEEESPNFKKRPCKCSRGGSDTVYHVFVRERGRFEMESVFLRGKSVTQEALESAVLAKFKSLKHEAVWKKERPGNLKGDKELKIHRIYPLGLTQRQALYNFKFEGNSSLSSHIQNNPCAKFEVVFV
The following text describes a protein:
Function:
During neurogenesis, plays an essential role in axonal guidance and outgrowth by regulating the polarization of both microtubule and actin cytoskeletons. Establishes the asymmetry of axonal and dendrite microtubules and the polarized sorting of neuronal proteins. This is achieved in part by regulating the localization of kinesin-like protein unc-104. In neurons without a distal microtubule-organizing center (MTOC), also controls the organization of microtubules in dendrites. During the dorso-ventral axonal guidance and outgrowth of VD neurons, required downstream of Rac GTPases ced-10 and mig-2 to inhibit growth cone filopodial protrusion mediated by the unc-6/netrin receptor unc-40-unc-5. Specifically, regulates growth cone filopodial protrusion polarity, and thus migration, by promoting F-actin polarization and by restricting plus-end microtubule accumulation in the growth cone. Probably downstream of mab-20/Sema2a and mab-20 receptor plx-2, regulates the guidance of DD/VD neuron axons by modulating fln-1 interaction with F-actin which results in the remodeling of the actin cytoskeleton. In hermaphrodites, involved in sex myoblast (SM) migration by regulating the gonad-dependent repulsion of SMs; [Isoform a]: In neurons, required for the polarized sorting of axonal proteins. In PLM neuron, regulates innexin unc-9 gap junction turnover by suppressing unc-9 transport out of gap junctions. Plays a role in locomotion and egg-laying; [Isoform b]: In PLM neuron, regulates innexin unc-9 gap junction turnover by suppressing unc-9 transport out of gap junctions; [Isoform c]: In PLM neuron, regulates innexin unc-9 gap junction turnover by suppressing unc-9 transport out of gap junctions.
Subcellular Localization:
Cell projection, axon. Cell projection, dendrite; [Isoform a]: Cell projection, axon.
Sequence:
MFPFLAPIRSANHVEQQGTKYYVEITFLADSPYSRAPSSTGTEKSVIPTLRNLDDLETVSNKSRSSEGVNKLGSRPNSRSSAIVKKTSVSSLPTSARSEGKSSPIPVKDAIPAPARHKNKGLEMSSAMMELFGGGGSTSPAPSKRENPADAPSDRVVSNAKLSQPGPEWFEGFEQMDMTDIELPPDPNCPAEKVLRGEKSTPDFDSDWQEAKEDVLDPQSYPKSFNPAESLPGPDIGAGVDDEEEPEAEAQEMEEPQYESKVDEKDDDDNGSSSSKKGHPSEDGDSTRNGETPTDRRNSGAIEETADGESSAQSAAEKKNSGDDGNGGGGEMSILLVKNAQIVNDDAIFVADILIEDGIIQNVAPNLEAPEGAEVLDAAGKLALPAGIDVYTQVTDSSVDDLSTGCKSAIAGGTGTIVEVVRPRGAESVVSAVKRVKNQLEKSGISCHVALSVAITDFCEQEMSELVKNEGINSFVLDGVSLTDDKLLELFEHVKRLGALIRVVPENKSIVAMLEKKMLKLGVTGPEGFPQSRPESLEADRVSGVCVLGNLASCPISIVQVSSADSLAAIEKARASGALAHAEIASAAVTADGSALFSQDLRFASAHLTDVPLRRGAPDRMIGALSTQPLVVCTSGHRPVNSATRVAAKDFAIAQKGSTGAEERMAVVWERAVRSGRIDAMRFVAVTSTNAAKMFNMYPKKGRIAVGADADLVIWDASGKRVLESSRAQSSQENSMYDGLTVHSVVTATIVGGKIAYQNGEVREAPVAGGFLRLSPNSPYLFSMVGQRDKFANVERVEREASSQQQKPQQNGHHKNSGDFDRNRTKVMESSIDFGGSAANRPRNPPGGRTTGFW
The following text describes a protein:
Function:
G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase. HTR1D is coupled to G(i)/G(o) G alpha proteins and mediates inhibitory neurotransmission by inhibiting adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPHSNKSSELSPGGSSNTSWVPWAAPSTVHSLQISLAVVLSTITLATGLANVFVILAIARTQKLHTPANYLIGSLALTDLLVAILVMPISIAYTVSRRWAYGQVLCDVWLFSDITCCTASILHLCAIALDRYWAVTDALAYSRRRTAGRAAAMIAAVWLLSVCISLPPLFWRQARATAELADCTVNTDQLSYTIYSTCGAFYLPSALLLALYGRIYAAARSRVLRPSALAGKRFTTAQLIASSSGSSPCTLGAGIPTGRPGPTRPVRVRLAGRGRRGLSSARERRATKTLGIILGAFIGCWLPFFVASLVLPLCQGACPLPPALFDFFTWLGYLNSLINPVVYTAFNEEFRQAFQKLVRFRKWA
The following text describes a protein:
Function:
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Subcellular Localization:
Mitochondrion.
Sequence:
MTDELIAYIGVRGPITVAEFMRRVLRDGRYGYYTSKGSRREQVIGAAGDFITAPEVSQLFGESLLVWLMTQYQSLGSPAKIQLIEIGPGKGTLICDIVRSGEKRHKVCVGVHLVEVTNGMRSRQKESIRNLQKETSVNVISFEWHDVLSSVPIHDDSGDPIPTFVICQELVDALPIHSFQKIEGNLWRERLVDVAIRDDSEASDAAKDVHLAVAPPSDDNHASTSLNSLPVGSIIEACPEGLILVQDIADRIQNCNGGAALIIDYGENGASGGDTLRGFWRHTQVHPLSRPGEVDVTADVDFGALREAVNRRVTFEDSFERKRKENAYKRKGKTLEEDANENDKPDNKSTPPITRQYEAYGPITQGQFLASMGIVERVERYIEDDDTTDEQAYELFSALERLVGSDEMGERYKVLAIAAAKKDGLFPPPGF
The following text describes a protein:
Function:
May be involved in several stages of intracellular trafficking (By similarity). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)).
Subcellular Localization:
Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
Domain:
The PX domain mediates specific binding to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)).
Sequence:
MLEVHIPSVGPEAEGPRQSPEKSHMVFRVEVLCSGRRHTVPRRYSEFHALHKRIKKLYKVPDFPSKRLPNWRTRGLEQRRQGLEAYIQGILYLNQEVPKELLEFLRLRHFPTDPKASNWGTLREFLPGDSSSQQHQRPVLSFHVDPYVCNPSPESLPNVVVNGVLQGLYSFSISPDKAQPKAACHPAPLPPMP
The following text describes a protein:
Function:
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MWPFSRQQNVSRILPIVPTAPRRFPVWFPAVLVLVLIALDQWLKAWALAHLQLNAPAIPVIPGVLDWELTFNTGAAWSMFSGSAVPLALGRILVGLGILSYLLWKPQGRFLTVVLSMIAAGAIGNSIDGLQRGQVTDMIHSPLLSAVTEAINGTRFPIFNIADMCVVGGTILLLVASLLPERKREKAVPEA
The following text describes a protein:
Function:
Involved in protein precursor import into chloroplasts. Part of the motor complex consisting of a co-chaperone (TIC40) and a chaperone (HSP93) associated with the import channel (TIC110). Causes the release of bound transit peptides from TIC110 and stimulates ATP hydrolysis by HSP93. Involved in reinsertion of proteins from the chloroplast stroma into the inner membrane.
Subcellular Localization:
Plastid, chloroplast inner membrane; Single-pass membrane protein.
Sequence:
MESLVLASSCSASPRLPLLSAASRPSRPLSAAPLSAGAGRRGARRPRLVVSAASRGSRNVSDGFNTKGFASISSSTSTENTSTGTGTVPPMPPPSSYIGSPVFWIGVGVALSAAFSMVSSMVKKYAMEQAFKSMMTQAPQNTFGANSPFPFSMPPQAGSTAPSSYPYSGPRKNTPKGATVDVSATEVAATGSSEAADVAETSKPSKKFAFVDVSPEELQKQKELQSSLQTVDVKSDSTESETKGDTEQVPTNGAAFKPSEDSSTWTTESSKSGPMLSIDTIEKMMEDPAVQKMVYPYLPEEMRNPDSFKSMLQNPMYRQQLEDMLNNMGASPGQWDNRMVDHLKNFDLSSPEVRQQFAQVGMTPEEVVAKIMANPEVAVAFQNPKIQTAIMDCSQNPLNIVKYQNDQEVMDVFMKISQIFPQING
The following text describes a protein:
Function:
Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate (By similarity).
Sequence:
MYWVNGQRRNEVPIHDRSFQYGDGCFTTILTKEGQVQQWSSHKARLQACLDILHIPEPNWDRVWQGLQSMILPQEKAGLKIHISRGLGGRGYSPTQVSESIVTISAFAFPAHYQAWRDKGLAVGICQQRMGLNPLLAGHKHNNRLEQILLKREMDNAGWDDGVCLDINGKVIETTAANIFWCRDGTMFTPCLRHAGVAGVARRQILELAQQQEIPIVIDEFTLEDLLSAEEVFITNALLEVAPVTQIGQQRLTIGSMTRRFQESSNS
The following text describes a protein:
Function:
Essential transporter for growth and development under abiotic stress. Mediates shoot branching by promoting the outgrowth of lateral shoots. Required for salt tolerance via Na/K homeostasis, at least partly by regulating SKC1/OsHKT1;5. Necessary for hypodermal suberization of roots, which contributes to formation of the apoplastic barrier.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSSSSDHAIDVQTVDQDQDQNQNQPFVLRFTNLTYSVSTAVDSVFSSRKPESKSLGGGMKKTLLNAVSGEGRKGEIVAVLGASGSGKSTLIDALAGRISRESLQGSITLNGEQLHGRMLKVISAYVMQDDLLFPMLTVEETLMFAADFRLPSSLSKVEKKARVQTLIDQLGLGNARNTIIGDEGHRGVSGGERRRVSIGVGIVHDPIILFLDEPMSGLDSTSAFMVVNVLQKIARAGSIVMMSIHQPSSRILGLLDHLIFLSRGNCVFTGTPDDLQPFFSDFGYPIPENENRTEFALDLIRGLEVAIPPGTNRLVEHNNSWKSTTVADSEEQSGMNSTLKDAISETIGRGKLASNPFWYEMGVLTRRAYKNTKRTPELFAARLATVMVTGIILATVYWKLDMTPEGSQERLGFFAFAMSVTFYTCSDTLPVFLQERYIFMRETSYNAYRRSSYVLSNSMVAIPFLVVLSLAFATTTFFAIGLYGGATGFGFYFLITLASFWAGSSFVTFLSGVVSNVMLGYTVVVAVLAYFLLLSGFFISRDRIPNYWIWLHYISLVKYPYEAVLHNEFDFAGRCFARGIEVFQNTAVGGASEKMKVALLGDMASTLGIGEITANTCLITGPDILRQQDITQLGKWECLLVTVAFGIFFRILFYCALLLGARNKRK
The following text describes a protein:
Function:
Subunit j, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary 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 (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain. Minor subunit required to maintain the ATP synthase population in the mitochondria (By similarity).
Subcellular Localization:
Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MLQSLIKKVWIPMKPYYTQAYQEIWVGTGLMAYIVYKIRSADKRSKALKASSAAPAHGHH
The following text describes a protein:
Function:
[Antimicrobial peptide 1]: Has antifungal activity. Inhibits spore germination of F.graminearum (EC(50)=4.5 uM), F.oxysporum (EC(50)=8.5 uM), F.solani (EC(50)=4.0 uM), F.verticillioides (EC(50)=8.1 uM), P.infestans (EC(50)=16.3 uM), P.betae (EC(50)=6.0 uM), P.debaryanum (EC(50)=12.0 uM), P.ultimatum (EC(50)=14.4 uM), B.sorokiniana (EC(50)=18.2 uM), A.alternata (EC(50)=16.0 uM) and A.solani (EC(50)=14.0 uM). Does not destroy spores but rather inhibits hyphal growth during germination. Does not affect spore germination in A.niger, C.graminicola, D.maydis and T.album. Does not inhibit trypsin; [Antimicrobial peptide 2]: Inhibits spore germination of P.infestans with an IC(50) of 24 uM. EcAMP2 has no activity against F.graminearum, F.oxysporum, B.sorokiniana and A.niger at concentration up to 32 uM. Has no antibacterial activity; [Antimicrobial peptide 2.1]: Inhibit spore germination of P.infestans with an IC(50) of 24 uM. EcAMP2 has no activity against F.graminearum, F.oxysporum, B.sorokiniana and A.niger at concentration up to 32 uM. Has no antibacterial activity; [Antimicrobial peptide 3]: Has antifungal activity. Inhibits spore germination of F.graminearum (IC(50)=5.5 uM), F.oxysporum (IC(50)=9.6 uM), B.sorokiniana (IC(50)=15.0 uM) and A.niger (IC(50)=22.4 uM). Has antibacterial activity. Inhibits P.syringae (MIC=4.5 uM), C.michiganensis (MIC=2.1 uM) and E.carotovora (MIC=9.8 uM). Does not inhibit trypsin.
Subcellular Localization:
Secreted.
Sequence:
MGKGSSGGGAWWAFLLLAGVLLAVAATAAGAEEDVATEVAAAADRDPKEDLRWCRKGCQWQYGQDTRQRKECERDCRQRHREQEQDADEEDGSGRGSCRSQCMRRHEDEPWRVQECVSQCRRRRGGGDDDVAVDACEGADRCRERCERRHRGDWQGKQRCLMECRRREQEEDVDDRCPCPCRRQCERHGDPATRQRCVEACQRRREEERRHGGGDADEEGSRGGRCERKCRRHSDWQTRQRCLQQCEQRERQEEGGRDDAGDGKDTYCADRCQSMCRQRHRGDREMQRRCARKCEREEGCPRRRDATADADEAEEDDGNDRCSQQCQHHRDPDRKQQCMRECRRHQGRSDDDDTRAGEDDS
The following text describes a protein:
Function:
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins.
Subcellular Localization:
Nucleus.
Sequence:
MAAEQKATTEEVKMDLFEDDDEFEEFEINQDWVENEEQVKEVGLQWEDDWDDDDVSDDFSHQLRKELETISADKK
The following text describes a protein:
Function:
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen. This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis. May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis. May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation. May play a role in the regulation of cell morphology and cytoskeletal organization. Involved in phospholipid biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MTPRRSPFLPTPFESILLSIYPATLLLGSIFSVLSPDVRASEYSAALQSHTPSTAPSYFAKKSNIFNQWFVKKGWAWITASYFFFLLTHPSTGPPGVLTVTPRRLRGFLRYAVVTTWWIFVTQWFFGPAIIDRGFIITGGQCDMVDAAEKGHVDMDDTRQFLTGVACKAVGGKWRGGHDISGHVFLLVLGSMFLFQEVLHVVLRSSGIKEERTIVMEDGAIKSADVEAPPQNEAEGLNQDGWLGLSVRIILGVAGLSLFMLAMTAMYFHTWFEKFTGLIVAFGGVFVVFWLPRLNPAVRSVLGMPGI