lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Orphan nuclear receptor that binds DNA containing an extended core motif half-site sequence 5'-AAGTCA-3'. In males, plays an essential role in the migration of the linker cell which guides gonad elongation during the L3 and L4 stages of larval development by negatively regulating the expression of netrin receptor unc-5 at the mid-L3 stage. Involved in the regulation of non-apoptotic cell death in the linker cell, acting upstream of or in parallel to transcription factor hsf-1. Represses hypoxia response genes, fmo-2 and acs-2, in both normoxic and hypoxic conditions, probably acting via repression of nuclear receptor nhr-49.
Subcellular Localization:
Nucleus.
Sequence:
MMTAVSQMSVPSSRILLDVDCRVCEDHSSGKHYSIFSCDGCAGFFKRSIRRHRQYVCKNKGSPSEGQCKVDKTHRNQCRACRLRKCLEIGMNKDAVQHERGPRNSSLRRQQMMFDHGSSPNSPEMGSESDAIILPTSSMNRDTVAGTAARIFFALVGFCQNPLNGVPKERQMTMFQQNWAALLVLHATETRAITSKQIRTETISGSSEQRNAVANAFEIIERLQLDNREYMMLKHFTMWRDTPSAIQIVFQLASIQNFTHRTEPTRYIQCINAIAAIPTTSIIDVLFRPSIGSASMPRLIQDMFKPPQQPTPTSLFPMANFNLNFLLKQEKTETEEGEDIEEEDDATSSNQFDENSSTDDRSVGELDPVQLFLALNSSTQPSSASSPSSSRPRHSIRSITELLSIQEEESVNVEEV
The following text describes a protein:
Function:
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The complex plays an important role in the uptake of multiple carbon sources present in different host niches.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MGDRAPASQLMEGAYRVLMKRNSVYVAFILVGALAGERVINYSIDKVWEANNKGKRFEDIPNLGQKTGDDE
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC).
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane.
Sequence:
MEVDPSPSPPPSRPPPLPGYFDPESSGRREEYRRYRKRLSSSNVSPLLGSSLSKSSEARLLYDGDSIPRRPNAGLLLEDIKQEAEDYSNFEGLDGSRMFSSAKRRAPFDGGSASDAAYSSGRQAVRQTLKPVKMEDDMYAPHEGETSFSMFASLLDSAIQGLMPFPDVILQFERTCRNASESIRSSATGKLRVVEDKLMQQKAQLLLDEAASWSLLWYLYGKGNEELSGELFVSPTTSHQEACRFVAADLTAQLCLRIVLWLEGLASEALDLEKKVRGSHVGSYLPSSGVWHRTQRYLKRNNNDSTIVKHVDFDAPTREGAQLLPDDKKQDELLLEDIWTLLRAGRLEEASELCRSAGQAWRAATLCPFGGIDMFPSLDALLKNGKSRTLQAIELESGIGRQWRLWKWASYCASEKIAEQDGGRYEMAVYALQCSNLKRILPICTDWESACWAMARSWLDVQVDLELSQYQTSRPDEKQLDDDMNGAQSSVGPESWPYHVLDQQPRDITALLQKLHSSDLVHETVSRACREQHRQIEMNLMSGNISHLLDLLWSWLSPAEEDQNIARPLDDPEMIRFAAHVVLVLRYIFISDEMEDELEEKLVAVGDLIINMYVRYLFSEDQEELVGVYASQLQRDLCIDLFVEMMELRLNSSLHTMYKLFLSAVEYLPFSSGDASKACFEEIIERVLSRSRQTKPSKYDEDFSDVAHQHHLQSLQKAMVIQWLCFTPPPSIPDFQMITGKLLIRALMHSNTLFREFSLISMRRVPELPAGPHKLLAILAEPLKQKENLFSLEDQEVSDNLQEFEDWHEYYSLDATYRNWLKVEMQNDAVSPEMLSAEENDQAVAAAKETLELAFLLLKKDERPWLDAVESSPFESSDPIFLELHASAMLCLPSGECMLPDATSCTALTSALYSTASEEDVLHRKLKVDIQVSSRDPCCIEVALSCLAAEGDGYGLHEANDGGLLAAIMAAGFKGELSRFQPGVSMAISRLDAWYSDGNGSVESTAAYIIRGLCRRCCLPETILRSMQACISLSAAGDSLDDCDKLIELVGSSESGMIHLFSQQQLQEFLIFERECLICKMELEEEQQLPSDG
The following text describes a protein:
Function:
Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Participates in the regulation of the ubiquitin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May be indirectly involved in PIS1 gene expression.
Miscellaneous:
MISCELLANEOUS: Present with 2770 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The OTU domain mediates the hydrolase activity and the interaction with CDC48.
Sequence:
MKLKVTGAGINQVVTLKQDATLNDLIEHINVDVKTMRFGYPPQRINLQGEDASLGQTQLDELGINSGEKITIESSDSNESFSLPPPQPKPKRVLKSTEMSIGGSGENVLSVHPVLDDNSCLFHAIAYGIFKQDSVRDLREMVSKEVLNNPVKFNDAILDKPNKDYAQWILKMESWGGAIEIGIISDALAVAIYVVDIDAVKIEKFNEDKFDNYILILFNGIHYDSLTMNEFKTVFNKNQPESDDVLTAALQLASNLKQTGYSFNTHKAQIKCNTCQMTFVGEREVARHAESTGHVDFGQNR
The following text describes a protein:
Function:
Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans.
Subcellular Localization:
Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Sequence:
MMLNFLPVRKFKRNGRYIVFGAVLTVALLAAYLEFRATNEWSSSEVTIRGESVVWAKAAAAQRSVKEDHFSENQEKDKWTPKNTQQTWRTEYKGQANLHVFDDWCGSSIAQLRKNLHYPLYPHSRTTVKKLAVSPSWTNYGLRIFGYIHPYTDGDFLFALASDDNSEFWLSDDDNPDNLKLIAYVGKTGREWTAPGEYGKYASQISDLVPLQANKKYFFELIHKQNGEGTDHVEVAWQLKVTGSGFAIIDSKFISLYTNESSLRAGDVSHIPQTAASHVTPPPRSLQTPPHGVDMLRPDPRDSFHQIPLLDQVRLHGVLPDCIYNPSYIIKGYPLVRYQGLQFVYLTYVYPNDYTRLTHMESENKCFYRANPYYMERYGFSNYIQMDVPEKEELSLKFKGDSMFGKAANIGRNKDKDFQKSRENGEKQQIDGMEKKKKVLSDYGDDYDDYSMNRRRKLFSVQKHSVIRRKRNDGELNIRNEQENQPKEIQKLPEEAHNEPQPRRKKKRRLPQQQNLEDQQHPQNAPSEVKSYNQGVKQAYTVDKIPEQQNPERFQEKTQRRFKEKHLQADGSMVKNDRIHRLKAHYVNSSNVNPNPAIVRDVPIEKVREAIDLKEKSIKKPAMLNEVEIEHPESNGMDNRKVFLGEHVYKARKNSSNVVELKKHRVKNATYEYLHGGEVKADAMKKPKYREQKVDRVVVVDNRIVEYNNKAHNNIAVLQKPHQNMLYNQTSEHKDQAFNNRWGHANEDRNGVEKPIQDNAMHVKETEDNGDEEDAWVNQGLSEEEDYELVHRPAFDVEVKWNQTFHAKLLDLHSMRSDWIDLKCNVSGNLMLSESEALSVVDAFMKELNKKYPRQFSLDRIVNVEKKPDYNRGSRYLLELDLLEASGRHLRLGQYVFVKRTDDWGSQRKQKPQDTKLQLCNPYTFYWNPTATVHFIIPVKNQARWVKQFISDMEEIYRITGDQNFNIIITDYESTDMNIEEELLNSYIPRYQYLRLSGNFERSAGLQAGIDLITDDNSIVFLCDLHIHFPPGFIDTVRKHCVERRMAFAPIVMRLNCGATPQEPDGYWEVNGFGLLGIYKSDLDRIGGMNTKEFTDRWGGEDWELLDRILQGGLEVERLYLRNFFHYFHSKRGMWNRRTLRNT
The following text describes a protein:
Function:
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular Localization:
Nucleus.
Sequence:
MASQASRRFHEAGVGSRTGLRLSAVARDQDGFEDLEAFYKASQAALDHQKQQHPDELEDDDEDYDSFDEATFNRRRQAASSSSMMDIQNSSAPSPRSLLRSSRGSAAVASVSSPERAGQAHGNITLADDDDQLDLPELSTGSRSFNLVTMASNDANDDEEPEQRLRAPSTPQRGLSERKAGTLPNAKRKGKEPVTARRNIQLSDSDDDDILASIQQRLESAYDDEQDQWPMSEDEIVPVKPSPAKMTTAAASSHTKPRKRSRMTKGTADERPAVSAPSGASSKRPKKAKEPTNESSVVTAPPAASSKNKPERPPKSRAVEKEPEPEPELAFGLDEDEPEPAHFAARSSSISTPPPAAKQLPKRKRGEPAKKSSAEQPAAASRVPQKASTTSTGVGRPAASSEKHKATKPKKVADEVVERVRLQPREATVINENGVRRSTRQRFAPLEYWRGERIRYGRPSLPSGTTPDDLCGSQGRGEDEFEEDPSMMLVRRRVPVLDIKEVIRVPRAPGEGTFSGTTMRARTTTRRKVERKSEERAPRLTPQTRVPEDEDEYARLDPTADTIYVEDGWDEETVETGMVIKDEASAEVEVSVVRTKATHRPIPVANQRFRFEKFFNSGGVMATGILHLPPGASKPTKSAKDNSFVFCVLQGALRASVHRKSFIIGPKGVFQVPAGNTYSLENICQREVHLFFAQCIKTKIANAGDLTMFTQMSDTSYGTPGFKAGLYSHDQRGGRDDQRLEDEMRKTTESAAGESMQLQQQRGNGKVLDHRPVLTARSDADDSDEDDFELSRRVKSAKRVFRKL
The following text describes a protein:
Function:
Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases, methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residue. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin, thereby promoting filament repolymerization. Plays a role in innate immunity by reducing oxidized actin, leading to actin repolymerization in macrophages.
Subcellular Localization:
Cytoplasm, cytoskeleton. Nucleus.
Sequence:
MGKEHSPPSERDSAVFAWVCGFGSLSPERLELRTTFVSPSTTGVYACAKCGYELFSSRSKYAHSSPWPAFTETIHTDSVAKRPEHNRPGALKLQGLRAVCSRPVASARELPPQAIGRDWPSGANVGNRTGFLYGLQDKGVLWQVWQRVGPRVPERWPQAGAVPILNIQQLAEVCP
The following text describes a protein:
Function:
FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monooxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Sequence:
MTVHYVHEGPEPQESRYSIPQHTTWMDPNNRRLRVITIGAGFSGILMAYQIQKQCANIEHVVYEKNHDIGGTWLTNRYPNAGCDVPSHAYTYRFALYPDWPRYFSYASDIWEYLDKVCAAFKLRQYMQFRTEVIKACWNEEEGQWKVRLRRQRPGQEPEEFDDHCHILLNACGVLSNPKWPDTPGLHDRFKGRVIHTAAWPDDYGEVQWNSDRVAVIGSGASSIQAVAGIQPHVGHLDIFVRTGVWFGVLAGNTGAPTKIYSEAERAQFRSNPSALVEHTKSIEAEVNGMWGAFYRDSMAQKGASAFFRQRMASIIKDDRLAKGFTPTFGFGCRRITPGDPYMHAIQQANVDVHFTAVASCTEDGIVGADGIERLVDTIVCASGFDNTYRPQFPIIGRRGVDLRDKWKTNPEAYLGLAVPDMPNYITFIGPSWPIQNGSVMAPLHSVSEYAIQFLKKMQNENIRAWAPRQQITDRFNEHVQEWVKHTVWSDQCRSWYKNNETGRVNAIWPGSSLHYQAVIERPRYEDFEISYADANPWAHLGMGWTMLDRAGGKQADVSPHLCLENIDPVWFKSIGGDVDILRKQLEKGHTLPNNASHAEA
The following text describes a protein:
Function:
Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. Cleaves 16S rRNA between adenosine-1492 and guanosine-1493 (E.coli 16S rRNA numbering), releasing a 49 nucleotide (nt) 'colicin' fragment. Inactivates 70S ribosomes or 30S subunits by endonucleolytically cleaving 16S RNA at a specific site about 50 nt from its C-terminus. Produces 5'-OH-guanosine and a 2',3'-cyclic phosphate adenosine. Mixing a susceptible (e.g. strain K12 / A19) and colicin E3 producing strain results in total protein translation inhibition within 11 minutes. Its activity is inhibited by cognate immunity protein Im3; Uses BtuB, the vitamin B transporter, as a receptor on the outer membrane; binds via the receptor (R) domain. Then the translocation domain (T) probably 'fishes' for its outer membrane translocon protein, OmpF (Probable). The N-terminal 83 residues (T83) can bind to and occlude OmpF channels. A complex of the cytotoxic C-terminal 96 residues (C96) plus the immunity protein does not occlude OmpF; upon complex separation from the immunity protein C96 becomes disordered and is able to bind OmpF. The N-terminus probably binds TolB and then reinserts into an empty pore of trimeric OmpF; the rest of the protein is pulled through OmpF and crosses the inner membrane, where the cytotoxic fragment is probably released by protease FtsH (Probable).
Subcellular Localization:
Secreted.
Domain:
Has 3 domains, the translocation (T) domain, receptor-binding (R) domain and the cytotoxic RNase (C) domain. The R domain forms a 100 Angstroms-long antiparallel helical hairpin with the T and C domains forming globular domains at each end; the Im3 immunity protein binds between the T and C domains and probably blocks access to the 16S rRNA substrate. The hairpin motif interacts with BtuB, but BtuB does not translocate the toxin. The disordered N-terminus of the T domain (residues 1-83) binds to and occludes OmpF trimers when added from the trans- but not cis-side. Does not undergo major conformational changes in the T.thermophilus ribosome; however the 10 N-terminal residues (residues 456-465 in the whole protein) which form an alpha helix in complex with Im3, elongate to contact uS12 and may be part of the mechanism of 16S rrRNA recognition.
Sequence:
MSGGDGRGHNTGAHSTSGNINGGPTGLGVGGGASDGSGWSSENNPWGGGSGSGIHWGGGSGHGNGGGNGNSGGGSGTGGNLSAVAAPVAFGFPALSTPGAGGLAVSISAGALSAAIADIMAALKGPFKFGLWGVALYGVLPSQIAKDDPNMMSKIVTSLPADDITESPVSSLPLDKATVNVNVRVVDDVKDERQNISVVSGVPMSVPVVDAKPTERPGVFTASIPGAPVLNISVNNSTPAVQTLSPGVTNNTDKDVRPAGFTQGGNTRDAVIRFPKDSGHNAVYVSVSDVLSPDQVKQRQDEENRRQQEWDATHPVEAAERNYERARAELNQANEDVARNQERQAKAVQVYNSRKSELDAANKTLADAIAEIKQFNRFAHDPMAGGHRMWQMAGLKAQRAQTDVNNKQAAFDAAAKEKSDADAALSSAMESRKKKEDKKRSAENNLNDEKNKPRKGFKDYGHDYHPAPKTENIKGLGDLKPGIPKTPKQNGGGKRKRWTGDKGRKIYEWDSQHGELEGYRASDGQHLGSFDPKTGNQLKGPDPKRNIKKYL
The following text describes a protein:
Function:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (Probable). Represses chlorophyll biosynthesis and photosynthesis in the dark. Is recruited by PIF3 to the promoters of chlorophyll biosynthetic and photosynthetic genes, and represses their transcription by histone deacetylation. Involved in the repression of hypocotyl cell elongation to promote photomorphogenesis. Is recruited by HY5 to the promoters of a subset of cell wall organization and auxin signaling-related genes, and represses gene expression by decreasing the levels of histone H4 acetylation in a light-dependent manner. Promotes abscisic acid (ABA) signaling. Is recruited by MYB96 to the promoters of a subset of Rho GTPase (ROP) genes, which repress ABA signaling at the early stages of signal transduction. Represses ROP expression by removing acetyl groups of histone H3 and H4 from the cognate regions, particularly in the presence of ABA. Represses the plant response to elevated ambient temperature by directly repressing warm temperature-responsive genes.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Shuttles in and out of the nucleus upon light exposure. In the absence of light, is exported out of the nucleus, and upon further exposition to light is imported to the nucleus.
Sequence:
MVVETIERSCEGSKRRHVNGGDIAVPCSGEECSNGDINVAPGVSAKRARVSREMTFEDIYGADALLNDDDDEDDDCDWEPVQAPMEFVKWCCVNCTMSNPGDMVHCCICGEHKESGILRHGYLASPFFKDTGLIEVEEKYGGSSSATSSTAVGFDERMLLHSEFEVKAQPHPERPDRLRAIAASLATAGVFPGRCLPINAREITKQELQMVHTSEHVDAVDTTSQLLYSYFTSDTYANEYSARAARLAAGLCADLATDIFTGRVKNGFALVRPPGHHAGVRHAMGFCLHNNAAVAALVAQAAGAKKVLIVDWDVHHGNGTQEIFEQNKSVLYISLHRHEGGNFYPGTGAADEVGSNGGEGYCVNVPWSCGGVGDKDYIFAFQHVVLPIASAFSPDFVIISAGFDAARGDPLGCCDVTPAGYSRMTQMLGDLCGGKMLVILEGGYNLRSISASATAVIKVLLGENPENELPIATTPSVAGLQTVLDVLNIQLEFWPSLAISYSKLLSELEARLIENKKNQMKRKVVRVPTWWKWGRKKLLYNFLSARMISRSK
The following text describes a protein:
Function:
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MFGISFSELLLVGLVALLVLGPERLPGAARTAGLWIGRLKRSFNTIKQEVEREIGADEIRRQLHNEHILSMEREAQKLLAPLTGQNPPQETPPPAAESPAPSVPTPPPTSTPAVPPADAAAPPAVAASTPPSPPSETPRNP
The following text describes a protein:
Function:
Non-catalytic component of DNA polymerase alpha, which in a complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase. POL12 may play an essential role at the early stage of chromosomal DNA replication by coupling DNA polymerase alpha to the cellular replication machinery (By similarity). Interacts with MCM10.
Miscellaneous:
MISCELLANEOUS: Present with 11200 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSGSIDVITHFGPDADKPEIITALENLTKLHALSVEDLYIKWEQFSNQRRQTHTDLTSKNIDEFKQFLQLQMEKRANQISSSSKVNTSTKKPVIKKSLNSSPLFGLSIPKTPTLKKRKLHGPFSLSDSKQTYNVGSEAETNEKGNSSLKLEFTPGMAEDAVGDSAPLSHAKSSDAKTPGSSTFQTPTTNTPTTSRQNVPAGEILDSLNPENIEISSGNPNVGLLSTEEPSYNQVKVEPFYDAKKYKFRTMRQNLQEASDVLDDQIESFTKIIQNHYKLSPNDFADPTIQSQSEIYAVGRIVPDSPTYDKFLNPESLSLETSRMGGVGRRVRLDLSQVNELSFFLGQIVAFKGKNANGDYFTVNSILPLPYPNSPVSTSQELQEFQANLEGSSLKVIVTCGPYFANDNFSLELLQEFIDSINNEVKPHVLIMFGPFIDITHPLIASGKLPNFPQFKTQPKTLDELFLKLFTPILKTISPHIQTVLIPSTKDAISNHAAYPQASLIRKALQLPKRNFKCMANPSSFQINEIYFGCSNVDTFKDLKEVIKGGTTSSRYRLDRVSEHILQQRRYYPIFPGSIRTRIKPKDVSTKKETNDMESKEEKVYEHISGADLDVSYLGLTEFVGGFSPDIMIIPSELQHFARVVQNVVVINPGRFIRATGNRGSYAQITVQCPDLEDGKLTLVEGEEPVYLHNVWKRARVDLIAS
The following text describes a protein:
Function:
May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Single-pass membrane protein. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein.
Sequence:
MHFNLFKKAEAPPPETHTMPTSTEPPVVSQDNSTAVAGSGDKSADTFRKIQQELMNQINKIPLPPWALIAIAVVAGLLIITCCFCICKKCCCKKKKGKKEKGKGMKNALNMKDMKGSGGQNAKDDDDDAETGLTEGEDKEEEEKEEEKLGKLQFSLDYDFQNNQMQVGIIQATELPALDMGGTSDPYVKVFFLPDKKKKHETKVHRKTLNPIFNETFTFKIPYQELGGKTLCMSIYDFDRFSKHDIIGEVKVPMNTVDLGQPIEEWRDLQSAEKEEPEKLGDICISLRYVPTAGKLTVCILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTVKKKTLNPYFNESFSFEIPFEQIQKVQVVITVLDYDKLGKNEAIGKIFVGCNASGTELRHWSDMLANPRRPIAQWHPLKPEEEVDIALGSKK
The following text describes a protein:
Function:
RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis. Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. M6A demethylation by FTO affects mRNA expression and stability. Also able to demethylate m6A in U6 small nuclear RNA (snRNA). Mediates demethylation of N(6),2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N(6)-methyladenosine at the second transcribed position of mRNAs and U6 snRNA. Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping. Also acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs. Has no activity towards 1-methylguanine. Has no detectable activity towards double-stranded DNA. Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single-stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine. Ability to repair alkylated DNA and RNA is however unsure in vivo. Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation. Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells (By similarity). Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs (By similarity).
Subcellular Localization:
Nucleus. Nucleus speckle. Cytoplasm. Note=Localizes mainly in the nucleus, where it is able to demethylate N(6)-methyladenosine (m6A) and N(6),2'-O-dimethyladenosine cap (m6A(m)) in U6 small nuclear RNA (snRNA), N(1)-methyladenine from tRNAs and internal m6A in mRNAs. In the cytoplasm, mediates demethylation of m6A and m6A(m) in mRNAs and N(1)-methyladenine from tRNAs.
Domain:
The 3D-structure of the Fe2OG dioxygenase domain is similar to that of the Fe2OG dioxygenase domain found in the bacterial DNA repair dioxygenase alkB and its mammalian orthologs, but sequence similarity is very low. As a consequence, the domain is not detected by protein signature databases.
Sequence:
MKRVQTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLVFREAGSIPEELHKEVPEAFLTLHKHGCLFRDLVRIQGKDVLTPVSRILIGDPGCTYKYLNTRLFTVPWPVKGCTINYTEAEIAAACQTFLKLNDYLQVETIQALEELAIKEKANEDAVPLCMAEFPRAGVGPSCDDEVDLKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGSEDESDDESSFEGRDPDTWHVGFKISWDIETPGLTIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLALQNVLNDSDNGDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYKICTDWWCEPMTQLEGLWKKMESVTNAVLREVKREGLSVEQRSEILSAVLIPLTMRQNLRKEWHARCQARVVRTLPAQQKPDCRPYWEKDDPSMPLPFDLTDVVSEIRSQLLEARS
The following text describes a protein:
Function:
Inverting glycosyltransferase that catalyzes the transfer of one glucose moiety from UDP-glucose to an asparagine residue in peptides and proteins containing the NX(S/T) motif, resulting in their modification with a beta-linked 1,N-glucose. Likely acts as a key component of a general protein glycosylation system. Also accepts UDP-galactose as a substrate donor, albeit with low efficiency. Cannot use UDP-GlcNAc or UDP-GalNAc as substrate donor.
Subcellular Localization:
Cytoplasm.
Sequence:
MENENKPNVANFEAAVAVKDYEKACSELLLILSQLDSNFGGIQEIEFEYPVQLQDLEQEKIVYFCTRMATAITTLFSDPVLEISDLGVQRFLVYQRWLALIFASSPFVNADHILQTYNREPNRKNSLEIHLDSSKSSLIKFCILYLPESNVNLNLDVMWNISPELCASLCFALQSPRFIGTSTAFNKRATILQWFPRHLDQLKNLNNIPSAISHDVYMHCSYDTSVNKHDVKRALNHVIRRHIESEYGWKDRYVAHIGYRNNKPVMVVLLEHFHSAHSIYRTHSTSMIAAREHFYLIGLGSPSVDQAGQEVFDEFHLVAGDNMKQKLEFIRSVCESNGAAIFYMPSIGMDMTTIFASNTRLAPIQAIALGHPATTHSDFIEYVIVEDDYVGSEACFSETLLRLPKDALPYVPSALAPEKVDYLLRENPEVVNIGIASTTMKLNPYFLEALKAIRDRAKVKVHFHFALGQSNGITHPYVERFIKSYLGDSATAHPHSPYHQYLRILHNCDMMVNPFPFGNTNGIIDMVTLGLVGVCKTGAEVHEHIDEGLFKRLGLPEWLIANTVDEYVERAVRLAENHQERLELRRYIIENNGLNTLFTGDPRPMGQVFLEKLNAFLKEN
The following text describes a protein:
Function:
Required for polar body extrusion during cytokinesis in embryo development. Affects cortical granule size. Has roles in meiotic chromosome segregation, osmotic barrier function and polarization in conjunction with cpg-2. Binds chitin.
Sequence:
MTLKPVLLAFLVASAYAQYGVAGMYENLPLETTTLDGSGDGSGADNGFVSGADAVAIDTDCSTKEDGLYAIGGCSPQFLTCSGGISRIMDCPADLIYDPRIVACEYSYNVPQCGGVPQDVTSTQEAYPSEETTVNPYAPVEEATTTPAEDVTVPEETTTEAYAPVDDYSTTTPAEDVPVPVETTASPYAPIVPYTTGAPAADEPVTRSAVTKSCVGKADGFYSFGECSDHYTACSNGYLIPMQCPARLAFDEARVICDYVMNVPECTNGSGNDEGSADETTPESSGEMPYSNGYGYEETTTVAEDVPSTKDYAEPIAAAYVARYPSEKTTAENVPTTTIGYEPEVVETTAPYVEETTTTVGYKPEVEETTTEAEVPTTTVGYEPEIVETTAPYVEETTTAADVPSTTAVYEPEVVETTTEAEVPTTTTVGYEPEVVETTVPYVEETTTAADVPTTTVGYEPEVEETTTEAEVPTTTVGYESEVVETTAADIPTTTIGYAPIVVESTTAADVPTTTVPAETTTEVPACVEGATAIEPCSQHYKNCVNGQEAIFICENGLFFSPEQARCAPADQIAECHQTTVQYY