lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSSSLYLINPIEKSSENITGETNLLEHFNLYKTLNEFNSKHLSSTYKSYVKNLPGDNYIKREKSKHSSSSSSNNNNNSNNNNNSNNTNASGQQDVNMGVPPQQQQQQQQQQQQQQPQQPQQPEPPKPPGGLTRLVEGNFFDENQQELILLSLDDSQLRSAFTLLDGGYQRPDKDKKRDKKHRDKKKRKHRDGSSSSSTSGEKKKSKKDRPDGSHHHSNSNNNNSGNSMNSNNMNNNNLNHNNNNNMNHNNMNHNNNMNHNNNMNNNMNNNNNNNNNNNNNNNNNNMNNNNNGGNITVEH
The following text describes a protein:
Function:
Transcription activator that binds to 5'-TATCCA-3' elements in gene promoters. Derepress weakly the sugar-repressed transcription of promoters containing SRS. Contributes to the sugar-repressed transcription of promoters containing 5'-TATCCA-3' elements.
Subcellular Localization:
Nucleus.
Sequence:
MEQHEEAAERKPSPPVIFRLFGVEVRGGGGGVDEEEYEEEEVEGGLFIKKSSSMPNLTSIDPLPVPADGGKRRASDDSELASGQQKRRRRKVQERKKGVPWTEEEHKKFLEGLRQLGKGDWRGISKNFVTSRTATQVASHAQKYFLRQTNPGKKKRRASLFDVVAECSDDQLPSPQSVGTKPPTQDIIHTDRGDVPILSYPVARGFRGDSVQVDELTEYVKRLKAAEDMSLSMISGLEMASSSISSLELSIAPPHCAIEAAIKVL
The following text describes a protein:
Function:
Probable aminopeptidase.
Sequence:
MIPEKKSIAIMKELSIGNTKQMLMINGVDVKNPLLLFLHGGPGTPQIGYVRHYQKELEQYFTVVHWDQRGSGLSYSKRISHHSMTINHFIKDTIQVTQWLLAHFSKSKLYLAGHSWGSILALHVLQQRPDLFYTYYGISQVVNPQDEESTAYQHIREISESKKASILSFLTRFIGAPPWKQDIQHLIYRFCVELTRGGFTHRHRQSLAVLFQMLTGNEYGVRNMHSFLNGLRFSKKHLTDELYRFNAFTSVPSIKVPCVFISGKHDLIVPAEISKQYYQELEAPEKRWFQFENSAHTPHIEEPSLFANTLSRHARHHL
The following text describes a protein:
Function:
Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine.
Sequence:
MMKVRPVERRDLADIFELAGKTGVGMTSLPQNEQHLAARIERALNTWQGSLDPGEQGYLFVLEDSEQQKVVGVSAIEVAVGLNDPWYNFRVGTLVHASKALNVYKSVPTLFLSNDHTGYSELCTLFLDPDYRKDKNGPFLSKVRFLFIAAFRQYFSRKVIAEMRGYTDEQGRSPFWESVGRHFFSIEFAKADYLSGTGQKAFIAELMPKHPLYVDFLAEEARAVIGQVHPHTAPARAVLETEGLQYQGYVDIFDGGPTLEANTDDVRVVRDSSKRTVVIKDYDIEDYDIDPNGRLYLVANDHYHHFRAILMNTHLSDERLRLTPESAEALGVAAGDSVRIVSLFAPETKR
The following text describes a protein:
Function:
Phenol 2-monooxygenase; part of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite. The products of the cluster lead to a brown coloration and are important for growth and conidiation. The nonribosomal peptide synthetase-like protein fsqF, which lacks a canonical condensation domain, is required for addition of a serine-derived dehydroalanine moiety to activated tyrosine but is not essential for the subsequent steps leading to isoquinoline formation. A different enzyme, most likely the ATP-grasp enzyme fsqD, is responsible for activation of tyrosine (Probable). Three additional enzymes encoded by the fsq cluster, the N-methyltransferase fsqC, the phenol 2-monooxygenase fsqG and the FAD-dependent oxidase fsqB, catalyze the formation of the isoquinoline ring system in the fumisoquins. FsqB converts the fspF thiolation domain-bound (2S,4S,5S)-2-amino-6-(3,4-dihydroxyphenyl)-4-hydroxy-5-(methylamino)hexanoyl into isoquinoline. The cyclization most likely proceeds via a two-step mechanism, beginning with FAD-dependent oxidation of the methyl group to an iminium species followed by electrophilic attack on the deprotonated phenol (Probable).
Sequence:
MSNASDHVDVLIIGAGPAGLTTANSFNGSNCRVRLIDWKPAPLETGRADGLKSISLEVLDSFGIGDRVLNDCQPCEEIVLWNPGKDGVIARTMTIPDKVEELGQIERVMVENLYRHKTVQVNWNTQPVRLHIAPVTKDEPEAHPLTITVQNKETLGQETIRAKYVVGADGAHSWLRKYLNIGFSGDVTDSTWGVMNLVPKTDFPDIRKVFVVHSRAGTVMGVPREDKLVRLYISMDGGNRHTSIDAKSITAENLLQAARAILAPYRLDAARIPWWSAYCVGQRVADEFARHNRIFLAGDAVHTHSPKAGQGMNTSIQDGYNIGWKLRYCLEQKASPALLSTYQTERRPIAQALIDFDRKYLESFTRRDITHQEFLEAYLAGQRFTTGIQIQYPPSLIVTAKHLHAPSHPLATNLAPGKRLPDFQMVNQSDAVPIQAYHRFTSDGRFRLLVFPGDISQALAFGRFSRLGDWLTSHLPPSSGLEIITIHGARRADVELMDLHPAFRPWSDEEGWNYWTVYADDDSYHKGHGHVYERCGISKEDGVLVLLRPDGYISLIASFDETHELIDFFDGLQSGPRTVPQPERRANL
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MRRVLAIVALLALASSAFAEIKLQQVDRKINLNSQFARISEAVKAKNVGDKPVSDVVFCQLLNGDAVVSLYKVVNADTKAELTVSPTTVEGAPAGAACFSAKLAAPLAAGDTASLTVTAVLAKAQVPYPKEISQTEGQLMLYKDNLYVLSPYAVSAQTTEVTTPSSSVKSYTDSEKPVSKSDNKIKYGKYDLIKPWTLQELSVHFENNKPFKHIVTYVKEIEVSHWGNIYVEEKYEIKNAGARHSGSFSRLKYAHSYNGKANSFRDVRAVLPPSARSLYYVDLIGNISSSNTRKTVQATVVDIDLRYPLMGGWKVDFTLGYSVPLTGFLFHTKGGRRKLTMDLASPLEDVFVEDMVVRVVLPEGSSKLQAVLPYDMDQSTDVKYTYLDTTGRPVLVLHRRNVASPEHSAKFSVEYSFAATSILREPLLLVSVFFCLFAAVIAYNRLELVITRDDKWAAARDREVLATYMEQIQAALEDEASLMAGFEAATRAVRDTEDVDAAQRKRAAVEKGCKDLEDKVKPLLAAVESRSARVAGQVREVLDKSKALQARYGRQLAERVELVKKGSTMGEISRKLAPGQEALEAARRELKNAIDTVFGAY
The following text describes a protein:
Function:
K(+) channel that conducts outward rectifying tonic currents potentiated by purinergic signals. Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties. Contributes most of K(+) currents at the plasma membrane of resting microglia. Maintains a depolarized membrane potential required for proper ramified microglia morphology and phagocytosis, selectively mediating microglial pruning of presynaptic compartments at hippocampal excitatory synapses. Upon local release of ATP caused by neuronal injury or infection, it is potentiated by P2RY12 and P2RX7 receptor signaling and contributes to ATP-triggered K(+) efflux underlying microglial NLRP3 inflammasome assembly and IL1B release (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Each subunit contributes two pore-forming domains 1 and 2 which assemble to form a single pore with M2 and M4 transmembrane helices lining the central cavity and M1 and M3 facing the lipid bilayer. The transmembrane helices are bridged by the selectivity filters 1 and 2 that coordinate the permeant ions. Up to four ions can simultaneously occupy the selectivity filter and at least two elementary charges must translocate across the filter to convert it into the open conformation.
Sequence:
MAGRGFSWGPGHLNEDNARFLLLAALIVLYLLGGAAVFSALELAHERQAKQRWEERLANFSRGHNLSRDELRGFLRHYEEATRAGIRVDNVRPRWDFTGAFYFVGTVVSTIGFGMTTPATVGGKIFLIFYGLVGCSSTILFFNLFLERLITIIAYIMKSCHQRQLRRRGALPQESLKDAGQCEVDSLAGWKPSVYYVMLILCTASILISCCASAMYTPIEGWSYFDSLYFCFVAFSTIGFGDLVSSQNAHYESQGLYRFANFVFILMGVCCIYSLFNVISILIKQSLNWILRKMDSGCCPQCQRGLLRSRRNVVMPGSVRNRCNISIETDGVAESDTDGRRLSGEMISMKDLLAANKASLAILQKQLSEMANGCPHQTSTLARDNEFSGGVGAFAIMNNRLAETSGDR
The following text describes a protein:
Function:
Gamma subunit of a guanine nucleotide-binding protein (G protein). G proteins are involved as modulators or transducers in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of cAMP phosphodiesterase. Required for the control of pseudohyphal and haploid invasive growth.
Subcellular Localization:
Cytoplasm.
Sequence:
MFYLSDIEEEASAGAEPTYNFWEVLLFSNTQENLVTVVGELHTLTDRVVHYKIEPESREVTATTLPSLLALLLEKRNQARRLYRDVLSMKMSELDWDIDDLFTQLQEELTRTDDTLSMYPRRRFYH
The following text describes a protein:
Function:
Inhibits bovine, insect and wheat chymotrypsins. Inhibits bovine chymotrypsin with Ki of 0.6 nM. Does not inhibit human or wheat alpha-amylases, bovine pancreatic trypsin, or trypsin-like activity isolated from wheat.
Subcellular Localization:
Secreted.
Sequence:
TSIYTCYEGVGLPVDPLQGCHYYVTSQTCGFVPLLPIEVMKDRCCRELAAISSNCRCEGLRVFIDRAFPPSQSQGGGPPQPPLAPRCPTEVKRDFARTLALPGQCNLPTIHGGPYCVFP
The following text describes a protein:
Function:
May play a role in organizing the actin cytoskeleton of the brain cells.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSGSGRKDFDVKHILRLRWKLFSHPSPASSSPAGGSCLQQDSGGGSFEHWGPSQSRLLKNQEKGSVSAFWKKPSSSSSSSSSSSSSASSSPFNPLNGTLLPVATRLQQGAPGQGTQQPARTLFYVESLEEEVVTGMDFSGPEDKGLALKELQAEPASSIQATGEGCGHRLTSTNHSLTPQSDLDSSSSEEFYQAVHHAEQSFRKMENYLKQQQLCDVILIVGNRKIPAHRLVLSSVSDYFAAMFTSDVCEAKQEEIKMEGIDPNALWDLVQFAYTGCLELKEDTIENLLAAACLLQLPQVVEVCCHFLMKLLHPSNCLGIRAFADAQGCIELMKVAHSYTMENIMEVIRNQEFLLLPAEELHKLLASDDVNVPDEETIFHALMMWVKYDMQRRCSDLSMLLAFIRLPLLPPQILADLENHALFKNDLECQKLILEAMKYHLLPERRTLMQSPRTKPRKSTVGTLYAVGGMDNNKGATTIEKYDLRTNLWIQAGMMNGRRLQFGVAVIDDKLFVIGGRDGLKTLNTVECYNPKTKTWTVLPPMSTHRHGLGVTVLEGPIYAVGGHDGWSYLNTVERWDPQSQQWTYVASMSIARSTVGVAALNGKLYSVGGRDGSSCLSSMEYYDPHTNKWSMCAPMCKRRGGVGVATCDGFLYAVGGHDAPASNHCSRLLDYVERYDPKTDTWTMVAPLSMPRDAVGVCLLGDRLYAVGGYDGQTYLNTMESYDPQTNEWTQMASLNIGRAGACVVVIKQP
The following text describes a protein:
Function:
Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ13 has a very low single channel conductance, low sensitivity to block by external barium and cesium, and no dependence of its inward rectification properties on the internal blocking particle magnesium.
Subcellular Localization:
Cell membrane. Membrane; Multi-pass membrane protein.
Sequence:
MRTDTTESNNTKSSTPLLTQRYLRMVTKDGHSTFQMDGAQGQGLAYLRDAWGILMDMRWRWMMLVFSASFVIHWLVFAVLWYVLAEMNGDLELDHDSPPDNHTICVKYITSFTAAFSFSLETQLTIGYGTMFPSGDCPSAIALLAIQMVLGLMLEAFITGAFVAKIARPKNRAFSIRFTRSAVVTHTEGKPYLMFQVANTRSSPLTSVQISAILYQEQENGQLHQTSIDFHLDSITLDECPFFTFPLTYYHSIIPPSPLAALLQREAAHHFELVVFLSAVQEGTGEICQRRTSYLPSEIMLYHRFAPVLARSAKGEYQIKMENFDKTIPELPAAADSMNPMRTAKEIRINGQHVDSFQLSETGLTE
The following text describes a protein:
Function:
Probably part of the ABC transporter complex YdcSTUV. Probably responsible for energy coupling to the transport system.
Sequence:
MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGLMAEKLCGMTGSFALRPEHIRLNTPGELQANGTIQAVQYQGAATRFELKLNGGEKLLVSQANMTGEELPATLTPGQQVMVSWSRDVMVPLVEER
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:
MEKASALWSSWLVVTMILTIFLATNAQATNYPTHPNLTEDFYLRTCPQARIIVFNVLVRQLALNKNLPAQLIRLFFHDCFVRGCDSSILIESTPGNVAELDGFPNRNSVKGLDVIALAKEKLEESCPGIVSCADIIALAARDILQLSRGLYFPVPLGRRDGSVSLASEANANLPSPFANYTQLVTSFANQGLSEEDLVVLSGAHTIGVSHCGVVYRRLWNFSPTIQTDPALSPAYAAKLKALCPIDQPQSQTEIELDSSMGGNFFDSNYYDNVLNGEAAFISDSALITNPSAAALVRTLGRFPTVPFFEKFGVAMVKMGLINVKTGSDGVIRKVCSKI
The following text describes a protein:
Function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Sequence:
MVTPGSGAAIGVFVSCGNRFEVTMNEQAQPAGGDPLFNPLSPDFIRNPYPHYDRLRAIDPIHVTPFGQFVASRHADVSLVMRDKRFGKDFVERSKRRYSEKIMDEPVFRSMSHWMLQADPPDHTRLRGLVVKAFTARRVEDMRPRIQEIVDEAIDAVIDRGHMDLIEDFAFRLPVTIICDMLGIPEDHREVFYKSSRDGGRLLDPVPLTPEEIAKGNAGNMMAQMYFQQLFELRRRNPADDLTTQLVQAEEDGNKLTNEELTANIILLFGAGHETTVNLIGNGLLALHRNPDQLALLKARPELMVNAIEEFLRYDSSVQMTGRVTLEDIDDLGGRKIPKGETVLCLLGSANRDPAVYPDRPDRLDVTRPNVKPLSFGGGIHFCLGAQLARIEAEIAIATLLRRLPDLRIDDVENPEWRPTFVLRGLKSLPASW
The following text describes a protein:
Function:
Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues, with a preference for phosphotyrosine as a substrate.
Sequence:
MSWRYALLTDRYSSSIGDRYSPHYYQSPSRLETSEQTTGRQLQRVLHYSMAPSRALPGLRRAECAIHDVDCDEVYPGIYIGDAAAAKNKTYLRLMGITHVLNAAEGCRYGQVDTGHSYYRDMPSIRRSHKDCVFRYMGFPMVDAPTTDISRYFYVASKFIDSAISSGGKILVHCLVGMSRSATCVLAYLMICRKMSAVDAIRTVRMRRDIRPNDGFLQQLADLDMELKRKNLYPY
The following text describes a protein:
Function:
Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme (By similarity). Important for proper ciliary and flagellar beating. May act in cooperation with CFAP45 and axonemal dynein subunit DNAH11. May play a role in cell growth and/or survival (By similarity).
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, flagellum axoneme. Note=Located in the proximal region of respiratory cilia.
Sequence:
MDNKISPEAQVAELELDAVIGFNGHVPTGLKCHPDQEHLIFPLGCTILIQAINTQEQNFLQGHGNNVSCLAISRSGRYIASGQVTFMGFKADIILWDYKKRELLARLSLHKGKIEALAFSPNDLYLVSLGGPDDGSVVVWSIAKRDAICGSPAAGLNVGNATNVIFSRCRDEMFVTAGNGTIRVWELDLPNRKIWPTECQTGQMKRIVMSIGMADDDSFFYLGTTTGDILKMNPRTKLLTDAGPAKDKFSLGVSAIRCLKMGGLLVGSGAGLLVFCKSPSYKPIKKIQSQGGITSITLRGEGHQFFVGTEESHIYRVSFTDFKETLIATCHFEAVEDIVFPFGTAELFATCAKKDIRVWHTSSNSAHRIGVTAIATTSDCKRVISGGGEGEVRVWQIGCQTQKLEEALKEHKSSVSCIRVKKNNEECVTASTDGTCIIWDLVRLRRNQMILANTLFQCVCYHPEEFQIITSGTDRKIAYWEVFDGTVIRELEGSLSGSINGMDITQEGVHFVTGGNDHLVKVWDYNEGEVTHVGVGHSGNITRIRISPGNQYIVSVSADGAILRWKYPYTS
The following text describes a protein:
Function:
Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MEMENLATRLSCRTEHEPFHPPISQKIHFQPDLSFRHFSYTTTLMGILQGNCALGNWRSQSSILPVSHGNTSSIVKPVPPAFIGAPMENSKAFIIKDLALFGVLKTALAPFERVKLLMQNQNHLIKSSQLPKPYNGILDCFARTIRNEGVLSLWRGYTAMTLADVSLKVMRFAIFRYALSREDFQWTYPRLLVLDSVVIVTNQLLFYPFLYAGARMANDVKAIGSMGNWQFNGIVDVFRKTLKSDGIAGLYRGFNIRLAEFGMMGAVSAGLKPWKQHYSSLLQNNVFWRHMVEFGFGICANMAIYPLDTVNKRMMMTSGAVKYKSTRQAIAQIMKTEGLKSFYSGAGAEILSCAVYKGTVLLIIYVADVIRAAKEKNDYCSRSTMEGSLRQMTRH
The following text describes a protein:
Function:
Inositol phosphosphingolipids phospholipase essential for the coordination of cell wall formation. Responsible for the hydrolysis of the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol phosphorylceramide (M(IP)2C).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSVEKAPELRVLSFNCWGLRFVSKYRTERLKAVGEKLAKCDYDIVLLQEVWSIYDFQEIRNLVSCNLVYSRFFHSAAMGAGLAMFSKFPIIESSMNKYPLNGRPQAFWRGDWYVGKGVATASLQHPSGRIISLFNTHLHAPYGKGADTYLCHRLSQAWYISKLLRAAVQRGHIVIAAGDFNIQPLSVPHEIITSYGLVNDAWLSVYPDQVEHPPNRFSMNDKELVEIAGTTCDSRLNTWRENISSKDMDDFVAKRLDYVFHSPSTCEAKNAKVVFLERVPKLDCSYSDHFAIETVLSIKLQPIPVQETRVSYSIIDDTLGITYQYMARERLHMRLRIAHLLISIPLIIGVHVAIAWCDPAWLKVIILFFTVMLTIAAVVNGFCIGLLFGRWEFNGLLEFVAELKEQKLLCKQYLVDHPLPFAKS
The following text describes a protein:
Function:
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Sequence:
MARVRIRQHVNPLSEKYRQVLACPDWATVYDDVQRPLHLDIGCARGRFPLKMAQQHPDWNFLGVEIRQPLVLEANETGDRLGLKNLHYLFGNINVEPEKFFSAFPPTLQRVSIQFPDPWFKQRHNKRRVAQPELVTAIANALPPGGEVLLQSDVEPVAQDMRDRFAENDNFVFTHDTPWLAENPLGVPTEREIACFNLQRPVYRCLLQRTP
The following text describes a protein:
Function:
May be involved in the regulation of spermatogenesis and sperm maturation.
Subcellular Localization:
Cytoplasm.
Sequence:
MVKGGKAPKGKKITLNVAKNCVKITFDGRKRLDLSKMGITNFPKCILRLTDVDELDLSRNMIRKIPESISKFQNLRWLDLHSNYIDKLPESIGQMTTLLYLNVSNNRLTTNGLPVELNQLKNIRTLNLGLNHLDSVPTTLGALKELHEVGLHDNLLTSIPNSISKLPKLKKLNIKRNPFPKTEESDIFLDTIKRLDNLYLVEDKDLCSNCLKKCQQARDKLNKIKNMATATPRKAIFSNLVSPNSMAKDSQEDWRIRSTSL
The following text describes a protein:
Function:
Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MENQVLTPHVYWAQRHRELYLRVELSDVQNPAISITENVLHFKAQGHGAKGDNVYEFHLEFLDLVKPEPVYKLTQRQVNITVQKKVSQWWERLTKQEKRPLFLAPDFDRWLDESDAEMELRAKEEERLNKLRLESEGSPETLTNLRKGYLFMYNLVQFLGFSWIFVNLTVRFCILGKESFYDTFHTVADMMYFCQMLAVVETINAAIGVTTSPVLPSLIQLLGRNFILFIIFGTMEEMQNKAVVFFVFYLWSAIEIFRYSFYMLTCIDMDWKVLTWLRYTLWIPLYPLGCLAEAISVIQSIPIFNETGRFSFTLPYPVKIKVRFSFFLQIYLIMIFLGLYINFRHLYKQRRRRYGQKKKKIH
The following text describes a protein:
Function:
Regulates the formation or stabilization of cell-cell contacts at several stages of epithelial morphogenesis. In early embryonic development, required for proper ventral closure of the epidermis. During male tail morphogenesis, regulates precursor cell sorting and allows the formation of distinct sensory rays. Seems to control cell-cell contact formation through 2 parallel pathways, one involving efn-4 and one involving plx-2 and unc-129. Involved in axon guidance. Probably by binding receptor plx-2, regulates fln-1-mediated remodeling of the actin cytoskeleton and thus axon guidance and/or fasciculation of DD/VD neurons.
Subcellular Localization:
Secreted.
Sequence:
MKAWILLLVLTRCSWGLISADNTFSDRTIGEFRELLINTKDGALFAGSEGAIFRLWAYNINDTGENVFSKKQLILSETEESECCSTASDEKLCRPSTRFLAFTNNKDSIYVCSSVGMRPEIRVLDSISLQDQQEPRTEIGICVVDPTFNSTAVVVDNGNPEDASSVYSGIRTGMGGENHLIYRPPLTKNGKQLHASIRTIYSDNKWLNEPQFVGSFDVGQHVLFFFREIAHDNSFGERIIHSRVARVCKKDIGGRNVLRQVWTSFVKARLNCSVSANFPFYFDHIQSVKRVDKHGETFFYATFSTSETAFTSSAICMFQLSSINHLLDTGLLMEETANGQFAVTADEIPAHRPGTCSSNSHSISDTDLHFAKTHLLVSDSISGGTPILPLRDHVYTQILVDQLNNQNVIFAFDSSQQKMWKISHWKEGNEWKWNLIETQTLKTSGFRINDVALLPGEFFFATSKAGVHQFSVARCQELPSCALCSMDPYCSWNAVNSKCALKTKTNEKSVGWISSSWAGRISPECSAVEKLQVKDVYLGDGFKIQGARGGTWQKDGRDLEESQRHVATSQGELVILNVDVEDAGTYECTRNGVILMRARVVVHENCARPTSVAEYRSCQREWCKKADAYKAALNIWSDSNKKNVQCKANGPSINGL
The following text describes a protein:
Function:
NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. Reduces ketopantoyl lactone (2-dehydropantolactone), isatin and camphorquinone. Does not act on menadione, p-nitrobenzaldehyde and pyridine-3-aldehyde.
Sequence:
MTQSNLLPKTFRTKSGKEISIALGTGTKWKQAQTINDVSTELVDNILLGLKLGFRHIDTAEAYNTQKEVGEALKRTDVPREDIWVTTKYSPGWGSIKAYSKSPSDSIDKALAQLGVDYVDLFLIHSPFFTTEQTHGYTLEQAWEALVEAKKAGKVREIGISNAAIPHLEKLFAASPSPEYYPVVNQIEFHPFLQNQSKNIVRFCQEHGILVEAFSPLAPLARVETNALAETLKRLAEKYKKTEAQVLLRYTLQRGILPVTTSSKESRLKESLNLFDFELTDEEVNEINKIGDANPYRAFFHEQFKDL
The following text describes a protein:
Function:
Transporter involved in riboflavin (vitamin B2) uptake. Also transports FMN and FAD.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLPSFTRKPADHPIGYLVALSGLLMQLMSYGIDNSYSIFSEDMHNDPSLGFPSITAISLGNSVSLGLSPAFGVLAGFCVDRLPPRFMMALSTILLFTGLWISSTLAANIYVVTFTYCLFASIGTACMLSPGAAATSSWFNRYQGLAMGINFAGGGIGSAIIPPLAGKWVVAYGWRKAFQLMSIFCAIGVLATALSARRREPKRDDSSADDETREGNKSGNGSLVRRSNEPATVGGEGAANNGHNEGKEDVREMGRKNGSHTNTSKVPPNGRGVGTNQQNGNDGEGLDVTEQSQRNNTFASAIDVDMDTSMDADEPQVIRSLHTHKLTPWELFLSMFTLPFMGNFLCWFIYSWAFYSLIYAAVPYISSMGKPGTVYAGVPPIPTDVAATLFTFYGVFQVVGSVLVGWLASLVTAEFAYVFCATVGGIGCGLLALGRSYVAFALLLCIIGFCMAGMFAVMPTLIATHLYGPNLGFYFGAVFLAGVVGGFVAPPMQATIQLRNNGSYAFVCVVMSVSMTLSALVCYATLWRSKRSGIVLAARKTKLVEIM
The following text describes a protein:
Function:
Possesses 5'->3' exoribonuclease activity. Acts as an endogenous post-transcriptional gene silencing (PTGS) suppressor.
Sequence:
MGIPSFFSWLVGKYPKIVGTIIDVYSASSSEEDEEEEKEEEEEEKGGEEEVDEDDDEEEIIYDNLYLDMNEIIHKCFRLNNGLVYNWFFAYLDRLFRIVRPRRLLYLAVDGVAPMSKMTKLRQRYFKTAKYRADSEAEAILLTEIFRAQGKEVMPRDTYELENPVVKMPGTEFMEKISAALEYFIRERLNTDPEWKDIKVILSDANVPGEGEHKIMSFIRAQRSMENYDPNTRHCLHGHDADLIMLALASHEVHISILREFDNPNGRIPARFYQFVDIWILREYLELEMKTPGCKQDTERLIDDFIFICFLTGNDFIPQIPSLEINEFAVDLLIEVYKTTFNKMGGYMVNTDKIKDKYGAYLEVSRLEKFFHELSLCEEKILLKRYELQEKLLCKIQSEAAVKEWAKGEDRGEKKTSFAQHFFYPVETSLERKSDDVVRKNTRELWRTVSDIFCNKDDLFKNGACKQDKIRPGWKSRFYREKLGAETSKEVGRLQTEMVQKYLEGLCWMLQCYFYEVPSWTWCYPFYYAPFASDFKCLSQFNISFTVDKPLRPFDQLMAVLPPQKNVLSCALPKCYSKLIGCEESKIQMSHPTEFEIDPDGKRFLSQGIAKLPFIDKELLLSATKMVEKDLTEDEMARNNARQERIFLRNSQSLANTAAFVATISDNAQKKLWIDTSEIGGWFSPDEKEVESSALRKNKVQHAWSWIRDPHMTVPHITSPVSLCECLLRSAMFFNPEAVKPISRLLDNVIVPDKTITEADIRKRPMWHTYPGPRPRRPHVTHKPDTHWKASSPATPREEHKLAGEGWLGRGKGSAAATAETRQIGPSGYGRGSQGADMAQRQSRGSRFDGGDEWAGGGGGGAVKRPETEGRPVGLWARGGGRRGSGPARRGSTF
The following text describes a protein:
Function:
Mitochondrial transporter mediating uptake of thiamine diphosphate into mitochondria. It is not clear if the antiporter activity is affected by the membrane potential or by the proton electrochemical gradient.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MIITTSNDEDKKTNVFVELAAGSFSGALTRFIVAPLDVVKIRLQLQRTQLNNNSNNNNKIIGKENVNYRGIINTMSKVIREEGIRSLWKGNFSAELLWVTYAAIQFSTYNEIIGILDPEYRKHQQRTDKDKPNYKPSSSITMIGGASAGILSTIVSYPFDIIRTNIVNNHNKTNFKQTFKTIIARNGGYSNLFSGINSSLFQIVPQMGFQFTFYETFKFISNKYTSSVNNNNNNPLNQFTCGLLSGAISKFLVLPFDVVKKRLQVNEKVGYGMKSCFRDLYFNEGGVKAFFKGGTPGIVKAGLAAALSFTFFEQSKRILLNKQ
The following text describes a protein:
Function:
Regulates intracellular cholesterol distribution from recycling endosomes to the trans-Golgi network through interactions with RAB11 and OSBP. Functions in membrane tethering and promotes OSBP-mediated cholesterol transfer between RAB11-bound recycling endosomes and OSBP-bound Golgi-like membranes.
Subcellular Localization:
Golgi apparatus, trans-Golgi network. Recycling endosome.
Sequence:
MAAMAPGGGGGGVNPFLSDSDEDEDEVSATDERRAGLRLGAGGGLDPGSADSLSPQDPVALGSSARAGLPGEAAAAALGGPGETPARLSIDAIAAQLLRDQYLLTALELHTELLESGRELPRLRDYFSNPGNFERQSGTPPGTGAPGVPGAAGLGGAGGREPSTTSGGGQLNRAGSISTLDSLDFARYSDDGNRETDERVAVLEFELRKAKETIQALRANLTKAAEHEVPLQERKNYKSSPEIQEPIKPLEKRALNFLVNEFLLKNNYKLTSITFSDENDDQDFELWDDVGLNIPKPPDLLQLYRDFGNHQVTGKDLVDVASGVDEDELEALTPVLGNLPSTLETPQTVENSLLVQKLEDKISLLNSEKWSLMEQIRRLESEMDFLKNEHFASPVVCDSVQPSLDQSPHKDSEDSGQNSVINSLDKGENKDVHLSKSDEVDSTVPKETFPHSFPRREREGIPSSSPSSKNTVHFDKPNRKLSPAFHQALLSFCRMSADSRLGSEVSRIADSEASVMLMLGRCLPHIVPNVLLAKREELIPLILCTACLHPEPKERDQLLHILFNLIKRPDDEQRQMILTGCVAFARHVGPTRVEAELLPQCWEQINHKYPERRLLVAESCGALAPYLPKEIRSSLVLSMLQQMLMEDKADLVREAVIKSLGIIMGYIDDPDKYQQGFELLLSALGDPSERVVSATHQVFLPAYAAWTTELGNLQSHLIPTLLNKIEKLLREGEHGLDEHKLHMYLSALQSLTPPLFASVLQNAPFSSKAKLHGDVPQIEVTRFPRPMSPLQDVSTIIGSREQLALLLQLYDYQLEHAGTTGWESLLWVVNQLLPQLIEIVGKINVASTACVHEFSRFFWRLCRTFGKIFTNTKVKPQFQEILRLSEENIDSSAGNGVLTKATVPIYATGVLTCYIQEEDRKLLIGFLEDVMTLLSLSHAPLDSLKAAFVELGANPAYHELLLTVLWYGVVHTSALVRCTAARMFELLVKGVNETLVAQRVVPALITLSSDPEISVRIATIPAFGTIMETVIQRELLERVKMQLASFLEDPQYQDQYSLHTEIIKTFGRVGPNAEPRFRDEFVIPHLHKLALVNNLQIVDSKRLDIATHLFEAYSALSCCFISEDLMVNHFLPGLRCLRIDMEHLSPEHEVILTSMIKECEQKIENKTVQEPQGSMSIAASLVSEDAKTKFLNKMGQLTTSGAMLATVFQRKK