lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in fructose transport.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain; The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain; The EIIC type-2 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Sequence:
MFKNLLRPSLFFNWSQKTFKNKFSFLKQAANALQKQAVINDNNVAFEALKKREEEITTGIITSLALPHLQSQSVIEPFVAVFKVKNLDWQSLDQKPVKLIFLIGVLVDKTNLHLDFISNFSKLMLNETFASKVLNVTSYNGLIKLIDLFNQQKVQDQPAVETKKEYDFVAVTACPTGIAHTFMAKEALEAFAKKHNLYVKVETQGTDGIQNQLTSDDINNAKGVILACDRLIDFSRFYANKNVIEVSTTKAIKKPDEVYELIKNQKGKQLANSAKPTNQTQLAESEGEFNFNNFHKRIYRAILSGVSYMLPFVVFGGILIALSFLIDINNANNAGGNFGTINPVANWLNKLGGISFSLIVPILSAYIAYALVSRQGLLPGFVVGLISSGQFLLNIVLTNGTIEWLAPSQVSSGFFGAIFGGLLSACLIIVQQNYIYKKLPQSLQGIKNILFIPLFGTLFTAGLFWVINIPLIYLNYGLSLFLNIMNSPILAPLLGFVIGLMMCFDLGGPINKAAYVFGVVSLQNQNAGTISMAAAMLSGMVPPLSIALAASIRKSCFDKQELPAAYACYLMGLSFISEGAIPFVVKKPKVMLTANLIAGAICGALTGAFALSIRAPHGGVFVFALLKTTLQGIEGATLQTGVGIGLALVCLIISMIVGSSIIIGYDLIAKHNQRKQNLNS
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.
Sequence:
MLRGEERPPERRGAGEGAGQPELRQPHFAGERGDHSLPGAVSCATYGPPGSQMANSQNGRNPRKGRILGFIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAADFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISIFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLFPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDENSRCCSIIDSFSMPMLDLDDDDDREESLMMNRLASVRKCNERQNSPVTSPGSSPLSQRRKPLPDPLQIPHLSLPPVPPRLDLIQKGVARSPCASPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPPERPPPIPPDNRISRHSHHPESVPSRDQPMPLEGWCPRDVFGTSQLVGSRTGSDTSPKPGLTAVSNINGRHNRISSEQGFMRKHRRHELPVEGAKVFSNGHLINEEYDVPPRLSPPLPGASTIPSIKCPVSSANSLSDKSRDHTDDDDEYKVPPSHSIILSSQPPHCHNIKAVARVCENGQCAGVTNGTHSATSDVKKSKHPELGDVYDAPTVPVPLPPARPPTRDNPKHSSLLNRTPSDYDLLVPPLGEDAFDSSPPSLPPPPPPPARHSITEHTKPSGSGSRPPSGHELFLHPDPHFDPMTGHVPLPPVRRVTGENVKTNRTSQDYDQLPPSSDGSQAPARPPKPLPRRTAPEIHHRKAFNSDSSTENVDAKIAKLMGEGYSFEEVKRALEIAQNNVDVARSILREFVCFPPPVSPRLNL
The following text describes a protein:
Function:
Single-stranded DNA-dependent ATP-dependent helicase (By similarity). Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA (By similarity). Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection (By similarity). Required also for telomere recombination to repair telomeric ends in the absence of telomerase (By similarity). ku70, of the ku70/ku80 heterodimer, binds to the stem loop of tlc1, the RNA component of telomerase (By similarity). Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Required for mating-type switching (By similarity).
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MSDKECTVFVLDLGKDMGTCHHGRSHSDLEWTLSYFHDELSHKFLANRKTDVVGIVGYKCDDTKNDLAEQEAYWNISVLYPIQTALFSKLQSVSQTLKPSNTMQGDLISAIVVSFDLMARHCKKNKWKKKMIVLTAARGIIDFSDYIGIAEQLLQHDVFLGVYGVDFDQEDINYSEPLKESQKKENEVRIQEFVESCHGQYCTFQQIYNNIGKPWVRKVRPVAIFRGTFSIGNRDSKDTSISIQVERYPRTRLTKPPTSSAFYENDMSKNYECLNIENSNVENKSMESDAVSTVRSYMVRDPKTNDSFEVKREDLESGYSYGRTIVPISRSDEDVLALDTIPGYEILGFIPKSSLPIYYTISDTNIIVPKDDFESKLNFSAFVQSLEREHRYALARFVSKDKGVPVLLVLMPYVEFKRHYLVDIQLPFAEDVRPYSFSEFEKLSNEEDMRQIDFAVSNYIDNMDLDSSDCGFNPPFEPENTFSMIPHRLQQAISYYANSPEGDLPQPNIYLTRYTNPPKSLLDNCILDLKLIKEKLTVNVPVKPKYSSQETAFDTGAPISEEQIEELLNSGLDEQEGEKLLVLHVSEKDPVGTFTEVLKNPFGLEDALTEMEKVIKNLIDKSKYDLALQSLQSLRLHSILEDEVERFNEYLTRLKKDVMQNNKPKENELINKIRSSGLDIILHDELTRHDNFNNI
The following text describes a protein:
Function:
Protease involved in the C-terminal processing of the chloroplastic D1 protein of photosystem II. This proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation.
Subcellular Localization:
Plastid, chloroplast thylakoid lumen.
Sequence:
MRILLCNSSSSLLLSSPSPPTPTKKSPILLTTNNNWVRKALLGAFNGALSLNILLSSPFSLAAESPLQLQSPSNPLTEQCLQEEKLEEITGPQTVTNEGIVEEAWQIVNDSFLNAGRHRWTPESWQQKREDILSTSIQSRSKAHDIIRRMLASLGDPYTRFLSPAEFSKMARYDITGIGINLREVPDESGGVKLKVLGLLLDGPAHTAGVRQGDEVLAVNGEDISGKSAFEVSSLLQGPNETFVTIKVKHGNCGPIESIEVQRQLIARTPVFYRMEQVDKGATSVGYIRLKEFNALARKDLVIAMQRLQDMGASYFVLDLRDNLGGLVQAGIEISKLFLNEGNTVIYTVGRDPQYQNTIVADTQPLVTSPVIVLVNKKTASASEIVASALHDNCKAVLVGERTFGKGLIQSVFELRDGSGVVVTVGKYVTPKHMDINGNGIEPDYENIPAWADVTRHLSQCNMNKKR
The following text describes a protein:
Function:
Intracellular monovalent cation channel required for maintenance of rapid intracellular calcium release. Acts as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. Opened by a change of voltage within the sarcoplasmic reticulum lumen.
Subcellular Localization:
Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane.
Sequence:
MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRRHPVASWLCAMLHCFGSYILADLLLGEPLIDYFSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFIMIATGWVKGSGVALLSNVEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTMFMVSCKVFLTATHSHSSPFDVLEAYVCPVLFGTGSGGDHPQDNHGAWPGGPPSGALATKSKEELSEGSRKKKTKKAD
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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; Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSQTLAAVEGSLGSIGYGLAAIGPGVGVGIIFGNGTQAMARQPEAAGLIRANQILGFAFCEALALIGLVMPFVYGY
The following text describes a protein:
Function:
Cooperates for the ATP-dependent vacuolar transport of bilirubin and glutathione conjugates.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MSSLEVVDGCPYGYRPYPDSGTNALNPCFISVISAWQAVFFLLIGSYQLWKLYKNNKVPPRFKNFPTLPSKINSRHLTHLTNVCFQSTLIICELALVSQSSDRVYPFILKKALYLNLLFNLGISLPTQYLAYFKSTFSMGNQLFYYMFQILLQLFLILQRYYHGSSNERLTVISGQTAMILEVLLLFNSVAIFIYDLCIFEPINELSEYYKKNGWYPPVHVLSYITFIWMNKLIVETYRNKKIKDPNQLPLPPVDLNIKSISKEFKANWELEKWLNRNSLWRAIWKSFGRTISVAMLYETTSDLLSVVQPQFLRIFIDGLNPETSSKYPPLNGVFIALTLFVISVVSVFLTNQFYIGIFEAGLGIRGSLASLVYQKSLRLTLAERNEKSTGDILNLMSVDVLRIQRFFENAQTIIGAPIQIIVVLTSLYWLLGKAVIGGLVTMAIMMPINAFLSRKVKKLSKTQMKYKDMRIKTITELLNAIKSIKLYAWEEPMMARLNHVRNDMELKNFRKIGIVSNLIYFAWNCVPLMVTCSTFGLFSLFSDSPLSPAIVFPSLSLFNILNSAIYSVPSMINTIIETSVSMERLKSFLLSDEIDDSFIERIDPSADERALPAIEMNNITFLWKSKEVLTSSQSGDNLRTDEESIIGSSQIALKNIDHFEAKRGDLVCVVGRVGAGKSTFLKAILGQLPCMSGSRDSIPPKLIIRSSSVAYCSQESWIMNASVRENILFGHKFDQDYYDLTIKACQLLPDLKILPDGDETLVGEKGISLSGGQKARLSLARAVYSRADIYLLDDILSAVDAEVSKNIIEYVLIGKTALLKNKTIILTTNTVSILKHSQMIYALENGEIVEQGNYEDVMNRKNNTSKLKKLLEEFDSPIDNGNESDVQTEHRSESEVDEPLQLKVTESETEDEVVTESELELIKANSRRASLATLRPRPFVGAQLDSVKKTAQKAEKTEVGRVKTKIYLAYIKACGVLGVVLFFLFMILTRVFDLAENFWLKYWSESNEKNGSNERVWMFVGVYSLIGVASAAFNNLRSIMMLLYCSIRGSKKLHESMAKSVIRSPMTFFETTPVGRIINRFSSDMDAVDSNLQYIFSFFFKSILTYLVTVILVGYNMPWFLVFNMFLVVIYIYYQTFYIVLSRELKRLISISYSPIMSLMSESLNGYSIIDAYDHFERFIYLNYEKIQYNVDFVFNFRSTNRWLSVRLQTIGATIVLATAILALATMNTKRQLSSGMVGLLMSYSLEVTGSLTWIVRTTVTIETNIVSVERIVEYCELPPEAQSINPEKRPDENWPSKGGIEFKNYSTKYRENLDPVLNNINVKIEPCEKVGIVGRTGAGKSTLSLALFRILEPTEGKIIIDGIDISDIGLFDLRSHLAIIPQDAQAFEGTVKTNLDPFNRYSEDELKRAVEQAHLKPHLEKMLHSKPRGDDSNEEDGNVNDILDVKINENGSNLSVGQRQLLCLARALLNRSKILVLDEATASVDMETDKIIQDTIRREFKDRTILTIAHRIDTVLDSDKIIVLDQGSVREFDSPSKLLSDKTSIFYSLCEKGGYLK
The following text describes a protein:
Function:
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Subcellular Localization:
Cytoplasm.
Sequence:
MAGVTAIEIPQWIQDNQGDFVPPVCNKCMFSDQLKVFYVGGPNQRKDFHLEEGEEFFFQRKGDMVLKVIEKGQVRDLVIKQGEMFMLPARVEHSPQRFANSIGLVVERERKNTEFDCVRFLVGSSNVTLFERWFFLTDVVKDLPPLIKEFYNSNEFKTGKPGKGTFACNAPYEARWTDLPVPINRKEFIYDHISEVKNGPVKIYGAPEYKTEVMLLGEGSYDLEAGAVELIIWLQENTFAVVEESGFTYALKSETMVRIKPNTKCLLNVKGGFAITIRMPG
The following text describes a protein:
Function:
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MAKPGLDLKSAKGGLSELKARLLFVIGAIIVFRAGSFVPIPGIDAAVLAELFAQQSGTILGMFNMFSGGALERASIFALGIMPYISASIIMQLLTVVHPALAELKKEGESGRKKISQYTRWGTLVLGTFQSVGIATGLPNLVPGLVVNIGFGFYFVAVVSLVTGTMFLMWLGEQITERGIGNGISILIFAGIVAGLPSAIGQTAEQARQGDLNVLVLLLLAVIIFAVTYFVVFVERGQRRIVVNYAKRQQGRKVFAAQSTHLPLKINMAGVIPPIFASSIILFPGTLAQWFGQNESMSWLSDFSLAVSPGQPLYSLLYAAAIIFFCFFYTALVFNPRETADNLKKSGAFIPGIRPGEQTSRYIDKVMTRLTLAGALYITFICLIPEFMLIAWKVQFYFGGTSLLIMVVVIMDFMAQVQTHMMSHQYESVMKKANLVNKANLDRFGR
The following text describes a protein:
Function:
Catalyzes the conversion of zeta-carotene to lycopene via the intermediary of neurosporene. It carries out two consecutive desaturations (introduction of double bonds) at positions C-7 and C-7'.
Subcellular Localization:
Plastid, chloroplast. Plastid, chromoplast.
Sequence:
MASSTCFSTTLTGRRNGFSEMIGFSVRRPMVLKDGKIQLKTQRLEVRSSLDTNVSDMSINAPKGLFPPEPEHYRGPKLKVAIIGAGLAGMSTAVELLDQGHEVDIYESRSFIGGKVGSFVDKHGNHIEMGLHVFFGCYNNLFRLMKKVGADRNLLVKDHTHTFVNKGGQIGELDFRFPVGAPIHGIRAFLATNQLKTYDKARNAVALALSPVVRALVDPDGAMMDIRNLDNVSFSDWFLSKGGTRMSIQRMWDPVAYALGFIDCDNISARCMLTIFSLFATKTEASLLRMLKGSPDVYLSGPIRKYIMDKGGRFHLRWGCREILYDKSADGDLYVTGLAMSKATQKKIVKADAYVAACDVPGIKRLLPPQWRELEFFDKIYKLVGVPVVTVQLRYNGWVTELQDLERSRQLKQAVGLDNLLYTPDADFSCFADLALASPEDYYIEGQGSLLQCVLTPGDPYMPLPNDEIIRRVEKQVLALFPSAQGLEVTWSSVVKIGQSLYREAPGNDPFRPDQKTPLKNFFLAGSYTKQDYIDSMEGATLSGRQAAAYICDSGEALTVMRKHISTNEAQEITEAGKITDELSFV
The following text describes a protein:
Function:
Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement: inhibits assembly of the complement membrane attack complex (MAC) by preventing polymerization of C9 pore component of the MAC complex. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (By similarity). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).
Subcellular Localization:
Secreted. Nucleus. Cytoplasm. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytosol. Microsome. Endoplasmic reticulum. Mitochondrion. Mitochondrion membrane. Cytoplasm, perinuclear region. Cytoplasmic vesicle, secretory vesicle, chromaffin granule. Note=Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction. ER stress reduces secretion. Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm.
Sequence:
ISGKELQEMSTEGSKYVNKEIKNALKEVLQIKLVMEQGREQSSVMNVMPFPLLEPLNFHDVFQPFY
The following text describes a protein:
Function:
[Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release; [Matrix protein p15]: Targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the pre-integration complex; [RNA-binding phosphoprotein p12]: Constituent of the pre-integration complex (PIC) which tethers the latter to mitotic chromosomes; [Capsid protein p30]: Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex; [Nucleocapsid protein p10-Gag]: Involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization.
Miscellaneous:
MISCELLANEOUS: [Isoform Pr80gag]: Produced by an upstream CUG initiation codon.
Subcellular Localization:
[Gag polyprotein]: Virion. Host cell membrane; Lipid-anchor. Host late endosome membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are probably linked to virus assembly sites; [Matrix protein p15]: Virion; [Capsid protein p30]: Virion; [Nucleocapsid protein p10-Gag]: Virion; [RNA-binding phosphoprotein p12]: Host cytoplasm. Note=Localizes to the host cytoplasm early in infection and binds to the mitotic chromosomes later on.
Domain:
[Gag polyprotein]: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus egress. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101. The junction between the matrix protein p15 and RNA-binding phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which interacts with PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in budding and possibly drive residual virus release.
Sequence:
MGQTVTTPLSLTLGHWKDVERIAHNQSVDVKKRRWVTFCSAEWPTFNVGWPRDGTFNRDLITQVKIKVFSPGPHGHPDQVPYIVTWEALAFDPPPWVKPFVHPKPPPPLPPSAPSLPLEPPRSTPPRSSLYPALTPSLGAKPKPQVLSDSGGPLIDLLTEDPPPYRDPRPPPSDRDGNGGEATPAGEAPDPSPMASRLRGRREPPVADSTTSQAFPLRAGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGDDGRPTQLPNEVDAAFPLERPDWDYTTQAGRNHLVHYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLKNKTLGDLVREAEKIFNKRETPEEREERIRRETEEKEERRRTEDEQKEKERDRRRHREMSKLLATVVSGQKQDRQGGERRRSQLDRDQCAYCKEKGHWAKDCPKKPRGPRGPRPQTSLLTLDD
The following text describes a protein:
Function:
Potassium transporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAEEGVAEAGDGPITAESPRISISSARKSSVRKGSSRSGLRRVDSLLVEAGRVKSMGAVHHGTEDLPWSVTLTLAYQTIGVVYGDLGTSPLYVFASTFPDHTPSENDILGALSFIIYTFTLIPLIKYVFIVLRANDHGNGGTFALYSLIARYAKISVSPNQVPEDQEVSSYKLAAPTKTMRRSQYLKEALNKKNWLRNVVVTIAILGTCMVIGDGVLTPSISVLSAIQGIKVNKPSLNQNVVVLVTCVILFALFSIQRFGTDRVGYCFSPIVVIWFISIALIGIYNIIMKDSTVFRAFNPYHMYEYISRNKKQGWISFGGIVLCVTGTEAMFADLGHFSVKAIQIAFTALVYPCLLIAYIGQAAYLLKHPEAVGETFYNSIPDKVYWPMFVVATGAAIIASQAMISATFSIVDQAMTLGCFPRVKVVHTSKKYAGQIYIPELNWLMMVLCIIIAAGFRDTTQIGNAYGVAVVSVFFVTTNFVTLIAIMIWQVPLWIALPCYFFMGSVELTYFSSILYKVPKGGWVPLIFVACFFSVMYTWHYGRVKKYEYEVKNKVSLDWVLGLGSNLGITRVPGIGLVYSELAQGVPTIFSHLISNLPAMHQVLVFVCIKNLPVPYVPDEERFLIRRIGPKQFRMFRCAVRFGYRDLSVGNEIDFEEQLIQNLAIFISTEVQAAQEQPMIADLAQLQRMIDAEGDGGAAPASVALDMTRRLSQGSRDDSEDSQSQSGIKAMKLPPNVDSGVEEELKVLVESKDAGVVYLLGHTEVRSRRSSSRFRKFLIDDYYHALKRNCRASTVSLAIPHERLLQVGMVHYI
The following text describes a protein:
Function:
Stimulates transcription from the HSP70 promoter.
Subcellular Localization:
Nucleus.
Sequence:
MEFKRGVPWYQLMYMKTDKIEKVPPHEVNRSFERAEKNYQNWIEKQSFDEITENILEKGTLKDKFASYKVLAQDEPLKMLEYLKTINELLAGKPRLQVDAMNCGVSIYTKFLLPKRNLRKFAVEPLKDAPENHLLLFYFEDRLKFYFDEFTKRLERAARAKQEFLRDNAIRQLGELLRLTKENSAVHLNILIDKFGDPLSAVSNIAKGTIQTVLRQHPYMCDQVVKVLQSRMNKFTEPAQKRALKFIGQINIKNGSDDTAKEVLKTARKQLMAILDKKDESNNKVITALMKSVQNCVGKCEPKEVEEIIDPLYRYIQHSSIVTTLPALRLLYVIHRAHGEIPIKFYEFFYKFFNSADLGSSNKHPQILNFLLEVLKAENDNSITCTFLHRLLHIGLHMNDMFAVSVLYFCAALFKEKPQLRSMIKKVNPDLEKKYDFRSDSPKSEGSTVTFPWILNMYMNYFHPSVVELATAIATGNEVKYDGDPFDDFAVTTQLKHIAGITEISEDDQKLVTNCFVGFDAIPDFDDEEGANDDDDAAADEAEN
The following text describes a protein:
Function:
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular Localization:
Secreted.
Sequence:
MASTTVSSTFELLFISSLLLFSQFFVSEAQGLPPVVKGLSWTFFQSSCPKLESIVRKRLERVFKDDVGQAAGLLRLHFHDCFVQGCDGSVLLDGSAGGPSEKTAIPNLTLRKESFKIIDDLRERVHKECGRIVSCSDITALAARDAVFLTGGPNYVVPLGRRDGQNFATEQATLDNLVAPTANTTTLLARLAAKDFDPTDVVALSGAHTIGISHCTSFTERLYPNQDSTMDKTFANNLKTSCPTANSNNTVNMDILSPNVFDNKYYVDLINRKGLFTSDQDLFTDRRTKNIVTSFGANQTLFFNKFVNAMIKMGQLNVLTGGQGEIRAKCSVRNKDKLLAAVVEGLEKTLAAAL
The following text describes a protein:
Function:
No glycosyltransferase or deubiquitinase activity is detected for this potential multifunctional enzyme.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MQKALKKYFVSMDEYLASIGLYRKMMARDASCLFRAVSEQLYYSQNYHQRIRKECVNFIRANRCNFEPFVEGSFEKYLERLEDPKETVGQVIIKALSLLYRRCFVIYRYPGKPPTEIAEEDNLPKILLCCSNNGHYDIVYPKSYPVDAAVCQALLYELLYTRVLGVEDDEIQAALEGFKGGGRRYRNSHSMCSEDASYDTPEDRSQSDFFREDWESRGHCRFDDRPRVGAEDQKVTEGSGKLALPYKVLKALEPELYRNVEFDVWQDSRKELQKTDYMVFAGRQYFLGDKCQVRLDPKGKYYNAFIQEVGTHSTAVTVFIEELGEKHLVSLTNLKPVNPVPAWNITPSRKGNSYSHAEQYPGELDPELRGRRRFFKKPRGVHSPAPPPPGLIYEHYRPHPPPRQPRGYGPPSSARFLNRHHLIGPDMAYYPSPSKRCYQSLDNYSFRSRRSRRQMHTLNKECLSCVPEPGEETQDMEGSITFYELEETDEGAFSPISGQAVSSPMVPGATAYWVPRVPSPIPPSGKQAMTSSEEDPDERSAGGDQGEYSEEYIYSAAEAGYQSPSVYAAAAESTTNLTIQEGSSRAGSPQEGVATYSYSQQVVVKSSVLSSSQPINSAPAAIFTSNSSSSSTGSSQTPPNSLQPNNILTPGQLPPGRPAVPWFVNELGEPVAMAPPPPYSYDPNGSDLPRDCKVLQYYYNLGVQWYQQSYWHSMVHLQQVYPHQAADAQFQSYQSTAPPADHTVPQAYPDSVRMCPHPQGDMPSNGAPLGMENPPTVVPGTVFYPVVQEQCGQPALHSTYDPYMPVLSTTYHYLTPWTPGAAPHSRFHHTTYCPSSSHPPVNYITAPGHPNHLPHSQFV
The following text describes a protein:
Function:
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPEMVPTSYYLALSGVLFALGLIGVMTRRTAILIFLSVELMLNAANIALVAFARSWGDLMGQTAVFIVMTLAAAEVAIGLAIIVAIFRGRETTNVDDLAQLRG
The following text describes a protein:
Function:
A 5'-3' exoribonuclease with a strong reference for 5'-monophosphorylated RNA and no endoribonuclease activty. Also has robust 5'-'3 nuclease activity on single-stranded DNA (exodeoxyribonuclease, exoDNase). May be involved in RNA degradation (Probable).
Subcellular Localization:
Cytoplasm.
Sequence:
MKLEIIAIGGYEEVGRNMTAVNVDGEIIILDMGIRLDRVLIHEDTDISKLHSLELIEKGIIPNDTVMKNIEGEVKAIVLSHGHLDHIGAVPKLAHRYNAPIIGTPYTIELVKREILSEKKFDVRNPLIVLNAGESIDLTPNITLEFIRITHSIPDSVLPVLHTPYGSIVYGNDFKFDNFPVVGERPDYRAIKKVGKNGVLCFISETTRINHEGKTPPEIIASGLLKNDLLAADNDKHGIIVTTFSSHIARIKSITDIAEKMGRTPVLLGRSMMRFCGIAQDIGLVKFPEDLRIYGDPSSIEMALKNIVKEGKEKYLIIATGHQGEEGAVLSRMATNKTPYKFEKYDCVVFSADPIPNPMNAAQRYMLESRLKLLGVRIFKGAHVSGHAAKEDHRDMLRWLNPEHIIPSHGDFNLTAEYTKLAEEEGYRLGEDVHLLRNGQCLSFERII