lhallee/plat_data huggingface dataset:
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. Regulates motility patterns of both 9+0 and 9+2 motile cilia through differential localization and recruitment of axonemal dynein components. Required for centriolar satellite integrity and non-motile cilium assembly (By similarity). Required for motile cilium formation (By similarity). Through its role in the beating of primary cilia, involved in the establishment of organ laterality during embryogenesis. Required for sperm flagellum biogenesis and is essential for male fertility.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton. Note=In tracheal cell cilia, localizes prominently to both centriolar satellites and axonemes. Tightly associated with microtubules in tracheal cilia. In embryonic node cells, localizes to the base of the node cilia at the centriolar satellites and, to a lesser extent, to the cilium axoneme. Localizes to centriolar satellites through G1, S phase, G2 and mitosis (By similarity). Enriched on the spindle poles in mitosis (By similarity). Relocalizes from the centriolar satellite to the ciliary transition zone upon ciliogenesis (By similarity). In skin fibroblast cells, locates predominantly to the centriole with much lower levels associated with the actin cytoskeleton (By similarity). Localizes to the sperm flagellum and manchette.
Sequence:
MYSQQFGTVPREFKGPTPKAVIIRAKPPKAQRAEQHLKRIQRSYHKYHTTLASIKSNEENRLKCDWIQRNNHKTFDSLVQARVQDAMQGFVINTEERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIAHQQQAREAEKEEERQEFEAGLAANKACLDKIQRILSENQALSQNVHPMRRGYPDKPPL
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:
MARLAALLVSLAMLMAAVTAARVERAGAGFYTPPSPSTCGLKIGYYHDKCPHAEAIVKGVVAAALHRDPGVGAGLIRMLFHDCFVEGCDASVLLDPTPANPQPEKLAPPNNPSLRGFEVIDAAKDAVEAACPGVVSCADIVAFAARDASFFLSDSRVSFDIPSGRLDGRYSNASRALDFLPPPTFNLGQLVANFAAKGLSVEDMVVLSGAHTIGLSHCSSFVSDRLAVASDIDPSFAAVLRAQCPASPSSSNDPTRRRRRCASTDYRQRQRAAGRRGGPVGQLPRGQRAAERSGVLARGQGGATASCTRREARRRPRGQRAGRRNGIGGSSARRREAETAASQHEHQAAEALHGGYTTTRTRRWLDASMNVGGVIASCTSTASPDTARDGIGNERSRRRSSMVRTSSGRPWSPRGQLRTAILLDCAR
The following text describes a protein:
Function:
Aldo-keto reductase that catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP) to L-glycerol 3-phosphate (L-G3P). The physiological role of Gpr is the detoxification of L-GAP, which may be formed via non-enzymatic and/or enzymatic racemization of D-GAP. Also contributes to cellular methylglyoxal detoxification by catalyzing the NADPH-dependent conversion of methylglyoxal to acetol. However, the catalytic efficiency of methylglyoxal reductase activity is more than 2 orders of magnitude lower than the L-GAP reductase activity. In addition, exhibits activity with glyoxal and probably plays a significant role in detoxification of glyoxal in vivo. Shows broad specificity and can use aromatic aldehydes such as 4-nitrobenzaldehyde and benzaldehyde, D,L-glyceraldehyde, phenylglyoxal, isatin and the model substrate 4-nitrobenzaldehyde.
Sequence:
MVWLANPERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAEENFGRLLREDFAAYRDELIISTKAGYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGNKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDDRVTSVLIGASRAEQLEENVQALNNLTFSTKELAQIDQHIADGELNLWQASSDK
The following text describes a protein:
Function:
Acts as a transcriptional activator of a number of genes encoding proteasomal subunits. Binds to a PACE (proteasome-associated control element) DNA sequence 5'-GGTGGCAAA-3'. Its expression is in turn regulated by the 26S proteasome, thereby providing a negative feedback control mechanism. Required for normal growth at low temperatures.
Subcellular Localization:
Nucleus.
Sequence:
MASTELSLKRTLTDILEDELYHTNPGHSQFTSHYQNYHPNASITPYKLVNKNKENNTFTWNHSLQHQNESSAASIPPQQTYHFPIFNKYADPTLTTTTSFTTSEATANDRQINNVHLIPNEIKGASETPLQKTVNLKNIMKVSDPYVPTRNTFNYDVKISNDFFDNGDNLYGNDEEVLFYEDNYNPKMQWSLQDNSAAINNEDARAIFNNEFDSDDDDISDDEEDEIEENCLQQEQHQEEPLLSLDVTPISMFGSDQKTGRAKSSSHLFNEYSYVDSNMDSISSVVSEDLLDERGHEKIEDEDEDNDLDEDDIYDISLLKNRRKQSFVLNKNTIDFERFPSPSTSANVPSTATTGKRKPAKSSSNRSCVSNSNENGTLERIKKPTSAVVSSNASRRKLINYTKKHLSSHSSTNSNSKPSTASPSAHTSSSDGNNEIFTCQIMNLITNEPCGAQFSRSYDLTRHQNTIHAKRKIVFRCSECIKILGSEGYQKTFSRLDALTRHIKSKHEDLSLEQRQEVTKFAKANIGYVMG
The following text describes a protein:
Function:
Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MTDPHVASHEQEVAGRPSTGLLSRINAPVARVGMYLSVTGLLVIVTIVFYQVFGRYVLNSSPTWTENLALVLILYVTLIGAAVGVRDAGHIGMDSLLVMLPDNVREKIELVIHVLVAVFGVAMAYNGWILGASVGTVKIPNLGLPEVIRYVPLIASGVLIVSFSIEHIIALLRGEEVVPSWN
The following text describes a protein:
Function:
Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid. Involved in coenzyme Q (CoQ) biosynthesis, catalyzing the last step in the tyrosine to 4-hydroxybenzoate (4-HB) pathway. Oxidizes 4-hydroxybenzaldehyde (4-Hbz) to 4-HB, the aromatic precursor for coenzyme Q.
Miscellaneous:
MISCELLANEOUS: Present with 2930 molecules/cell in log phase SD medium.
Subcellular Localization:
Lipid droplet. Mitochondrion outer membrane; Single-pass membrane protein. Endosome membrane; Single-pass membrane protein. Cytoplasmic granule membrane; Single-pass membrane protein.
Sequence:
MSNDGSKILNYTPVSKIDEIVEISRNFFFEKQLKLSHENNPRKKDLEFRQLQLKKLYYAVKDHEEELIDAMYKDFHRNKIESVLNETTKLMNDILHLIEILPKLIKPRRVSDSSPPFMFGKTIVEKISRGSVLIIAPFNFPLLLAFAPLAAALAAGNTIVLKPSELTPHTAVVMENLLTTAGFPDGLIQVVQGAIDETTRLLDCGKFDLIFYTGSPRVGSIVAEKAAKSLTPCVLELGGKSPTFITENFKASNIKIALKRIFFGAFGNSGQICVSPDYLLVHKSIYPKVIKECESVLNEFYPSFDEQTDFTRMIHEPAYKKAVASINSTNGSKIVPSKISINSDTEDLCLVPPTIVYNIGWDDPLMKQENFAPVLPIIEYEDLDETINKIIEEHDTPLVQYIFSDSQTEINRILTRLRSGDCVVGDTVIHVGITDAPFGGIGTSGYGNYGGYYGFNTFSHERTIFKQPYWNDFTLFMRYPPNSAQKEKLVRFAMERKPWFDRNGNNKWGLRQYFSLSAAVILISTIYAHCSS
The following text describes a protein:
Function:
Positive brassinosteroid-signaling protein. Transcription factor that bind specifically to the DNA sequence 5'-CANNTG-3'(E box). Can bind individually to the promoter as a homodimer or synergistically as a heterodimer with BZR2/BES1. Does not itself activate transcription but enhances BZR2/BES1-mediated target gene activation.
Subcellular Localization:
Nucleus.
Sequence:
MELPQPRPFKTQGRKPTHDFLSLCSHSTVHPDPKPTPPPSSQGSHLKTHDFLQPLECVGAKEDVSRINSTTTASEKPPPPAPPPPLQHVLPGGIGTYTISPIPYFHHHHQRIPKPELSPPMMFNANERNVLDENSNSNCSSYAAASSGFTLWDESASGKKGQTRKENSVGERVNMRADVAATVGQWPVAERRSQSLTNNHMSGFSSLSSSQGSVLKSQSFMDMIRSAKGSSQEDDLDDEEDFIMKKESSSTSQSHRVDLRVKADVRGSPNDQKLNTPRSKHSATEQRRRSKINDRFQMLRQLIPNSDQKRDKASFLLEVIEYIQFLQEKADKYVTSYQGWNHEPAKLLNWQSNNNQQLVPEGVAFAPKLEEEKNNIPVSVLATAQGVVIDHPTTATTSPFPLSIQSNSFFSPVIAGNPVPQFHARVASSEAVEPSPSSRSQKEEEDEEVLEGNIRISSVYSQGLVKTLREALENSGVDLTKASISVEIELAKQSSSSSFKDHEVREPVSRTRNDNVKQTRKPKRLKTGQ
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MTEEAQQNPEQTEQKTEQTVTVEEITEGLFSESTIDAFELNPRLISALKKMKIDKFTNIQTESIPPIISGSDVLMRADTGSGKTLAYLLPIMHRLATDFPRDTNPIRRDMGCLAIVIAPTRELCLQIETVVQDLRSQMNFVISGSLLGGEKVQSEKKRLRKGINLLIATPGRLLYHLQNSQNLYVNNLKFLVLDEADRLLDMGFGKKVAEIIEIINQAQNKVDDNPVHQTILVSATLPKELHSLTEIALYKPTEVGIMQDEKFSIPQTLLQRFVTVDAKWRLVALATLLKRYMIEEPETKAIVFLSCCKSVDFHASFFSFFNFMTPEERAQKKIPQRNYKGPNPNAEENKPTIRDTHASTDNDEVGAFSQFFNCPVFRIHGNVDQIERSKTISKFTAAKSAIMFCTDVAARGLDIPNISVIIQYDPPVDTEDYVHRVGRTARIGHDGISYLFLQQNELGFIDLLRDRKVQIKPYKYEELQRKGVAAMLGDNPNLCFAAMRKETFECVKTNDLEMAAGQAWAASIAAYTSHHKTTRSIFRAQALHLGHLATAFGLEKTPAEIKEMLHEDRDLQESINKPTEKKEMLPAFEERTSEFL
The following text describes a protein:
Function:
Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (Probable). Has a higher activity with long-chain diacylglycerols like 1,2-di-(9Z-octadecenoyl)-sn-glycerol compared to 1,2-didecanoyl-sn-glycerol. Specifically expressed in brain, it regulates neuron-specific morphological changes including neurite branching and neurite spine formation (By similarity).
Subcellular Localization:
Postsynaptic cell membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Cytoplasm. Note=Translocation to the plasma membrane is induced by phorbol esters.
Sequence:
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDFEGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPNVKSKPALLSGGLRMNKGAITPPRSSPANTCFPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIIGQMMHVAEYLEWDVTELNPILHEMMEEIDYDRDGTVSLEEWIQGGMTTIPLLVLLGLENNVKDDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCARAPPSCIKTYVKSKKNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQTTLHNKCASHLKPECDCGPLKDHILPPTTICPVVLTMPTAGTSVPEERQSTAKKEKGSSQQPNKVTDKNKMQRANSVTMDGQGLQITPIPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGLHFFRDVPDFRVLACGGDGTVGWILDCIEKANVVKHPPVAILPLGTGNDLARCLRWGGGYEGENLMKILKDIESSTEIMLDRWKFEVTPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFHIMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLQGIAILNIPSMHGGSNLWGESKKKRSHRRIEKKGSDKRPTLTDAKELKFASQDLSDQLLEVVGLEGAMEMGQIYTGLKSAGRRLAQCSSVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPMLMGPPPKTGLFCSLIKRTRNRSKE
The following text describes a protein:
Function:
Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MWVLLTSVFWLLRCLAFSEGRILPHTGEQCPSLQHEGINTDGNSNSTGFNLVRRFSLQKMSSVKKIRNPKGPIIMRLGGAKLVEPTSQVFPHGVPDEFTLVISLLLKKQTTDEDWYLFQISDQMGYPQVSLSINGVDRSLEFRSKGRDKEYVSCTFAGHGVYSLFDNGWHKIVLSVQEKMVSVHIDCSFISSKPIEPRGALASEGHTFIGLDAANGVPVHFDIQKFLLYCDPLMAMQEGCCEILPSGCNPEAPKTRRNVEVAESVQNANLIDIPHKTKQQGYTRCFCLEEALERRGGKVSSGMPIELPAECASCAFQLPERNVTVGPPGPRGLKGERGQSGTYGPKGEKGERGADCVRTSAQGPLQCAEGTKGEKGERGQEGPRGYEGPSGQDGEKGQKGERGDLGLKGSVGLPGRDGRPGEICVMGPKGQKGATGIVGPEGLAGEPGPPGKPGPPGTGLPGKPGDPGGPPGPPGEKGTTGTPGRDGAVGKPGKPGIPGHKGEKGDQCEPCASVSTDGTNVISMPGQKGQKGEMGIPGTGEPGKAGIKGESGIKGEQGSSGINGIKGEKGESCTSCPTLSPGMASIQNIPKGLKGEPGEPGVGLTGLPGKTGVPGSSGPKGEKGDFGPHGPPGTHGLPGDQGRIGPAGTKGEKGEPCTMCSSLPAEVTKPDTVIAIPGPPGQKGEPGESGNGIPGKNGKQGELGMKGQKGATGAAGDPGIPGSTGLPGLAGQPGIQGFEGPKGQKGDACDSCPMIGGGDSNGSGIPGKKGEQGPPGIGQPGKPGQSGLPGIQGPQGIKGAQGEPGPPGEGKRGPQGESGERGLPGKTGPPGPQGSPGFVGSKGEKGSTGQKGASGAPGNSGTGVMGPPGRDGTSGQPGIPGRDGVPGERGEKGDAGVCSCPPGPWMDPEIFGRPDSPNKWNGDVWPFGIQGPPGPPGPPGPPGLPGLQGVPGHNGMPGPPGVPGELGPLAAESNIDILKNICGDCASGQNTHPPPIAMKGQKGEQGLPGIPGTEDCERCRPEKEDEVGDEPDHGCAGGPGQPGAPGLPGHDGLPGPRGPPGLPGASGPPGFPGTLGTPGLPGMQGERGPPGPHGEKGELGPPGLPGYPGTMGSPGLPGSKGERGYHGPAGEKGESGPPGIPGVPGPAGPAGPRGERGTSGSFGEKGDQGFSGPPGFPGPAGPPGFPGKTGSPGPPGPTAEKGSEGLRGSPGQPGSSGPPGPPGLQGPPGIEGLDGKDGKPGLRGEMGPPGPPGHKGIPGFKGKTGHPGLPGQKGDCGPPGPSGITGRPGAEGDPGPMGPPGRPGPSGNLGAAGPTGPPGNPGPPGMGLKGDRGPPGDRGQLGLPGEPGTPGHPGPAGEMGSDGPMGKEGPSGRPGAPGSPGEKGETGMPGSSGPPGERGRPGPPGTSAAYTKSESLGIVGPRGPPGERGSSGSPGPAGAPGSPGLPGTPAESISYDEIKRMIRQELIKIFDERMAYYTTRMQMPLEMASSPGRPGSPGKDGSPGRPGPPGSPGLPGQMGREGRQGAPGMRGEPGSKGEKGANGIGVMGDVGPPGSPGPQGPPGYGKLGLPGPMGQQGIPGIPGSPGAKGYPGKDGRCNPSDCHGMMGVQEYHPKSMKGPG
The following text describes a protein:
Function:
Involved in the biosynthesis of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacterial cell wall. Catalyzes the transfer of the first two galactofuranosyl (Galf) units from UDP-galactofuranose (UDP-Galf) onto the rhamnosyl-GlcNAc-diphospho-decaprenol (Rha-GlcNAc-PP-C50) acceptor, yielding galactofuranosyl-galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-GlcNAc-PP-C50). Thus, GlfT1 is the initiator of galactan synthesis, while GlfT2 continues with the subsequent polymerization events.
Subcellular Localization:
Cell membrane. Secreted, cell wall.
Sequence:
MTHTEVVCAVVVTHRRRELLATSLDAVVSQDRKPDHLIVVDNDNDPQVRELVTGQPVPSTYLGSRRNLGGAGGFALGMLHALALGADWIWLADDDGRPADTTVLSTLLSCAHTHSLAEVSPMVCNLDDPQRLAFPLRRGLVWRRLTSELRTDSSSSSGDLLPGIASLFNGALFRADTVDAVGVPDLRLFVRGDEVELHRRLVRSGLPFGTCLTASYLHPCGTDEFKPILGGRMHTQYPDDETKRFFTYRNRGYLLSQPGLRKLLPQEWLRFGWYFLVSRRDLAGLREWIRLRRLGRRERFQR
The following text describes a protein:
Function:
The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side.
Sequence:
KPIPYSDLTVGVLKETYPGEQRVSIAPESAKMLVDAGLSVIVESGAGEHAAFSDAAYVNVGCIVLPKESVYAQADIITKIRPPDEYEVPKLAKKTFVGMISPSINTDLYNELTEQETNVFALDCVPRMLSRAQTYDVLSSQANIAGYRAVIEAANNFPRFFAGQMTAAGKVPPAKVLVLGVGVAGLAAIQTAKNMGAIVRAFDVRAVTKEQVESMGATFLEVPLKEDGAGAGGYAKEMSDEYKAAQAQLMLEQARDVDVIITTALIPGRKAPVLVNQDMLDVMKPGSVLVDLAAANGGNVAQTEANKVITTENGITIIGYTDLPSRLASTSSTLFGNNVAKFLLSIGPQTTKQQGVFQIDMEDDAVQNMLISYNGEARWPDKITPYNPPPPPTLTSEVIEKTEDELMHELNEKQRASFVKNAGIASIAAFALLAFGYNTDSPESISMLTTFALAGLAGYQVVWGVAPALHSPLMAVTNAISGMTALGGMMLLAQGARESSGIIPDSPAHWAGAVATLLSFINISGGFLITGKMLDLFRRPEDAKDYFELYALPASFLIAGLGASYFSGDMETVSGSVAIASAVCCIAAIAGLADQKTARTGNILGIAGVTFGLAATTAEMSAAGAGASAFEQVGLLGGIGSVIGASVASVVGPTELPQTVAAFHSLVGVAAMAGAAGEYLGNSHVGQLDGGTLASIYAAVFIGGITFTGSLIAFGKLSGMMKSNALALPGRDQLNLVMVSVIALGLAAFVNPDLGALAGIDRLSPESLQLASLSMAAVLSSVLGLHLVASIGGPDMPVVITVLNSYSGWALCAEGFLLGNALLAQVGALIGFSGAILTWIMCEAMGRSIVSVIFGGAGTSVAKVSGEAAVMEGEITIGSVDNMMESLLEAKNIVIVPGYGLAVAQAQFAVADIAKKLIGMGKNVRFGIHPVAGRMPGQLNVLLAEANVPYDIVFEMDEINDDFDDTDVTIVIGASDTVNSAAQDDPTCSIYGMPVLRVWKSHLVFVLKRNVGSTGYAGMENPILYKDNVEVVLGDAHETCEALRSAI
The following text describes a protein:
Function:
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit; With S5 and S12 plays an important role in translational accuracy.
Sequence:
MANQPRPKVKKSRALGIALTPKAVKYFEARPYPPGEHGRGRKQNSDYKVRLLEKQRLRAQYDLSERQLVRAYERASKTNMKTGEALVIELERRLDALVLRSGIARTIYQARQMVVHGHIQVNGQKVDKPSFRVRPDDVVQVRERSKEKTLFTIAREGGFAPDGETPRYLQVNLKALAFRLDREPNRKEIPVICDEQLVVEYYAR
The following text describes a protein:
Function:
Component of the cytosolic Fe/S protein assembly machinery. Required for maturation of extramitochondrial Fe/S proteins. May play a role in the transfer of pre-assembled Fe/S clusters to target apoproteins (By similarity).
Sequence:
MSALLSEDYLNDYISPALACTKPTEIKKEKFVTEDGEFQVGVEPQELEKVTISLSDCLACSGCITSSEEIMLSQQSHSVFLDAWRELGFDKCGSAGDAQCTNKLVVSISPHCRASMARYYGVDVDAADYAILRVFKEVFHATSVIGDGAGRLLSVKRVVEELMERRKASQGTALSSICPGFLIYTEKTKPKLVPMLLNVKSAQQVTGALFKEIALEEGYDVDTSLKDGKRTNVQYHLTIVPCFDKKLEASRPDGEGEVNCVITPREVLAMLGEMGVSFRKYLGDWASLDKQLQQSQLGMLRAEMSPAGWDPLLHWSIPANGDGYSDGYAYQYACTVRDAHVASGCAAQVVSVPGKNADVLEYRVVEPSSEGGKVIARACVLSGFRNIQNLCRKLDPSGHKKRSVRRVAALRSRGRKDSSSEDSTGTPSAISNALGGTANPAECDYVEVSACPSGSINGGGLLMELAPEREEMGETPLPSSTIGGNARRRQQQLQELQAMYKAQIRITDETPTSLPPAALPPLPPQYTMQYTFYIQEEDPAKPDIVTVGNTW
The following text describes a protein:
Function:
Catalyzes the oxidation of L-galactonate to D-tagaturonate. Required for growth on L-galactonate as the sole carbon source. In vitro, can also use L-gulonate.
Sequence:
MSTMNVLICQQPKELVWKQREIPIPGDNEALIKIKSVGICGTDIHAWGGNQPFFSYPRVLGHEICGEIVGLGKNIADLKNGQQVAVIPYVACQQCPACKSGRTNCCEKISVIGVHQDGGFSEYLSVPVANILPADGIDPQAAALIEPFAISAHAVRRAAIAPGEQVLVVGAGPIGLGAAAIAKADGAQVVVADTSPARREHVATRLELPLLDPSAEDFDAQLRAQFGGSLAQKVIDATGNQHAMNNTVNLIRHGGTVVFVGLFKGELQFSDPEFHKKETTMMGSRNATPEDFAKVGRLMAEGKITADMMLTHRYPFATLAETYERDVINNRELIKGVITF
The following text describes a protein:
Function:
Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation.
Subcellular Localization:
Cytoplasm. Cytoplasm, P-body.
Sequence:
MSWASAEDIYLSTSLASYLDKKLLVLLRDGRKLLGTLRSFDRFANAVLEGACERLIVGEIYCDIPLGLYIIRGENVVLIGELVCITLSLSFSFSLSHTHAIFFKMIFFLLSIPARAYLLIDFVLIDKDVDKEELPPHMTRVPEAEIRRV
The following text describes a protein:
Function:
Catalyzes the hydrolysis of ester bond in chlorophyll to yield chlorophyllide and phytol. Shows a preferential activity toward chlorophyll a. Does not seem to be required for chlorophyll degradation during senescence. May modulate the balance between different plant defense pathways.
Miscellaneous:
MISCELLANEOUS: It has been proposed that some chlorophyllase might be transported to vacuole via the endoplasmic reticulum where they might be glycosylated (Probable). Unlike CLH2, the expression of this protein is dependent on the presence of a functional COI1 protein. Plants silencing CLH1 exhibit reduced size, and decreased levels of chlorophyll and chlorophyllide. Plants silencing CLH1 exhibit enhanced resistance and salicylate (SA) levels, and decreased jasmonate levels (JA) upon infection with the bacterial pathogen Pectobacterium carotovorum. Plants silencing CLH1 exhibit enhanced susceptibility to infection by the fungal pathogen Alternaria brassicicola.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MAAIEDSPTFSSVVTPAAFEIGSLPTTEIPVDPVENDSTAPPKPVRITCPTVAGTYPVVLFFHGFYLRNYFYSDVLNHIASHGYILVAPQLCKLLPPGGQVEVDDAGSVINWASENLKAHLPTSVNANGKYTSLVGHSRGGKTAFAVALGHAATLDPSITFSALIGIDPVAGTNKYIRTDPHILTYKPESFELDIPVAVVGTGLGPKWNNVMPPCAPTDLNHEEFYKECKATKAHFVAADYGHMDMLDDDLPGFVGFMAGCMCKNGQRKKSEMRSFVGGIVVAFLKYSLWGEKAEIRLIVKDPSVSPAKLDPSPELEEASGIFV
The following text describes a protein:
Function:
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Sequence:
MAKEFVNSKLQPGKVVVFIKPTCPYCKKTHELLSRLPFKQGSLEFVDITATGDDVSKIQDYLQELTGARTASSSLGSEASRGMPSQPDRLHQFWCWVG
The following text describes a protein:
Function:
May function as an adapter protein.
Sequence:
MERMWRKVNHSLRNTSKSQAQQAAGGDGIIGGPATGATAATPQSTDTISSAGGFGDGQLVVAVQGLASGGIGASITASGGSNATGRRLASSGGGGGCNKSLSQHVLQTRTASSERRRRRRRKSRPRRGGGMGVTSCVGDPGGDNMSSSGGFYTLKEHQHYRPSHHHGGGVSVGVGGGSSRRLFATSAPSGTVMMYPNPQRGTALAPSVGSGTGHANTAGLGGGGGGGAGGAGGGATGSGTGGQPDISLRQRAVAKLRMFNFHLNWDLHMTHCKPCGPRLSGSGGNIITRRLCRNRRREDNELYRSNSFKFERFERKECLEELSNTLQKQIAICDDYSLPVDFVKKRPSSFDPCLAEAIPANPEHWIAPSPQTEFLPFGEAQQALQLQPAAAAATAAATTSAAAAANATAAAPQLPPPLPVPVATLPNQAATAAAAATAAILATHQQQQQQQHQHLSNNNNNGGSTHGQQHTHSNNNNTLPVGAQQQQQQQHQQQRATLQHPPLPNSNIKQASVKLIEGYSDPKDTRNHKKVYHKKAKKRSTTGHKRHQQQQQQQQPHQQQLQQQQQQTLPTPRSAQQQQQLQQKLQQRHSTYNNNNGNSRKDKRNSQYNSDSSAPKSSDDEADIDEEVEQQPLPVPQAPVQSASQPAAGLNSPDSISDDLVRPLPPQLQRSPRKLTVAPAEHNKRQPSPYYYSDLLKSRDKDKDKDKDKDKDKDKDKDKDKDKDKERDKDREDFKLKCRQSTASEPPQQTQTQLGGYRKSSSLDVPPAEEQPEAESHEEEDPRTGQDSQSTPKRYSFTEEGVHIIRCETPSTSTSEESDCSECLKRREWHARALALVRKTCNVQPRNQNPTGSELQLQLQHCDAGEGELLKCCPPPPAPAENQSQVQPMPPHRLLGPAAVCGACITSAPASSLAGGRGSELGDDLEEEYFRPRSIFYVHPHGVHECIECAQPAQPATVPAPTLSNPSLDIYGDDEDEVDGDEDEDEEDDSEDIMGSRRRQIYETAFDCKIAKSDDDLDEVDRITNCSVLLQLSNGNGGDISKVTGSSKTRAECKRAKNSKNQALQEQTGEAHVQVHHVEAELGKLQLSQVDQQNQNQNQSQNQQHGVSATGSGASASSTQQLPVRGYTPSPPSTAPLPMKFPGKHDRYLNMNSIRSAPNLPAANPAHPRLRDLRLPIQSMRHQCGGSSNDNSLTDSAYVNPPSTNSNSNAASASASASVSATGSAAPRRPRSFVLESGRVLELRRSAQGHQGGQSTHHHHHHHHHAPGSRRNRHGQSQGQTTGGGHNYSSTESIATSSSGGSMESLRSSTSEGNRSTSSSESRHSSSLSSHSSESGSGGSGGSGGSSVAYPLRPAPLLLHSKLHILSPISDKSSQEPASASASEQSQQPSQQLAPMASQEDDSTTSGAPAGNQVQVNASLKQPRSNRGAPNKALLQLADELLGSDSGISLHSREDGKPQALALQRLTLPKLQLIGAEGTTTSATASGAGGSSATGGSSGAGGSGSGSVVASGSTGIQQDLRDLPFDMPKLRRRKTLQQEAACTSGSATSVDLGELPFDMPKLRRRLRANQAEINNLLMHSTESSGISQASSSHSMRDDQKMSSKLDTALFRQNLTLNLNESRQATKQFGSLDLRGLNSNKELNMNLSQGYVTAVDLIDVTIPLERQGWYHGAITRIEAETTLRPLSEGSFLVRNCESTKQDYSLSLKGAKGFMHMRIQRNETGQYILGQFSRPFETVPEMIRHFCLNRLPVRGAEHMCLIEPVIAQLL
The following text describes a protein:
Function:
It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains, called bisecting N-acetylglucosamine (GlcNAc). It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. The addition of this bisecting GlcNAc residue alters not only the composition, but also the conformation of the N-glycan. The introduction of the bisecting GlcNAc residue results in the suppression of further processing and elongation of N-glycans, precluding the formation of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is unable to use the bisected oligosaccharide as a substrate. Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location. Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation. In brain, addition of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal targeting in response to oxidative stress and further degradation which increases its location to early endosome and the APP cleavage (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MKMRRYKLFLMFCMAGLCLISFLHFFKTLSYVTFPRELASLSPNLVSSFFWNNAPVTPQASPEPGGPDLLRTPLYSHSPLLQPLPPSKAAEELHRVDLVLPEDTTEYFVRTKAGGVCFKPGTKMLERPPPGRPEEKPEGANGSSARRPPRYLLSARERTGGRGARRKWVECVCLPGWHGPSCGVPTVVQYSNLPTKERLVPREVPRRVINAINVNHEFDLLDVRFHELGDVVDAFVVCESNFTAYGEPRPLKFREMLTNGTFEYIRHKVLYVFLDHFPPGGRQDGWIADDYLRTFLTQDGVSRLRNLRPDDVFIIDDADEIPARDGVLFLKLYDGWTEPFAFHMRKSLYGFFWKQPGTLEVVSGCTVDMLQAVYGLDGIRLRRRQYYTMPNFRQYENRTGHILVQWSLGSPLHFAGWHCSWCFTPEGIYFKLVSAQNGDFPRWGDYEDKRDLNYIRGLIRTGGWFDGTQQEYPPADPSEHMYAPKYLLKNYDRFHYLLDNPYQEPRSTAAGGWRHRGPEGRPPARGKLDEAEV
The following text describes a protein:
Function:
Subunit 8, 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 (By similarity).
Subcellular Localization:
Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MPQLNTTTWPTIITPMLLALFLITQLKLLNSHLHPPTPPKFTKPKLHAKPWGPKWTKVYLPHSLPPQY
The following text describes a protein:
Function:
Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
VVRDEPTNNIPDTIFTKLGQQLHRRSQHPIGILKNAIHNYFDSNYENKFDKFDDLCPIVTVKQNFDDVLVPADHVSRSYNDTYYIDPQTVLRCHTSAHQAELLSKGYTQFLVTGDVYRRDSIDSTHYPVFHQMEGVRVFSPNDWESSGQDGTAYAAEDLKEMFGRIGTPLICTLELLGAVEMRWIDTYFPFTDPSFELEIYFQEKWLEVLGCGVTEQEILKRSGNSNNVAWAFGLGLERLAMVLFDIPDIRLFWTTDERFTSQFSEGQLGVKFKPFSKFPPCYKDMSFWINESFTENNLCEVIRGIAGDLVEEVCLIDNFTNKKGMTSHCYRVAYRSMERSLTDEEINELQWKVREQVESKLNVVLR