lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Neuroendocrine peptide which is produced by a subset of neurons in the hypothalamus. Activates the G-protein coupled receptors pth1ra, pth1rb and pth2r with similar affinity. Receptor binding stimulates intracellular cAMP production. Plays a role in bone mineralization by regulating expression of factors involved in phosphate homeostasis. Important for embryonic bone development.
Subcellular Localization:
Secreted.
Sequence:
MLKMQRSQQRVALMMLMVVAAVHCQESESRRAVTEHQLMHDRGRSIQSLKRLIWLSSAIEGLHTAQARTLEPDSRWRSRGAQLYSQPGREESSGGQKRALETLLSDLYRAHLTFGLGEPEK
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MVARVGAFLKNAWDKEPVLVVSFVVGGLAFSSYFSFSRSSSFPFQLSAGEKGHRIELSSHSTQRQSCPGARRS
The following text describes a protein:
Function:
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (By similarity). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (By similarity). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity). Stimulates exoribonuclease activity of Rat1, allowing it to degrade RNAs with stable secondary structure more effectively (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MPYSIPLLRPNPADPVPFYRLPHLIHTYSHLPTRAISHDDASMAYYSPAPIGCNLTEGFERRIEREDEEEHLDGLVESLEWLITRGRKGERKGGIITWRGMLTRLITMPYETRDPWEMTAIALDGSVYLELWDPPEEKAKRKREQSAWEKQGYMGYAYESFSTIPQEGRPGNGPEGWGGDVNTNVQWANVVRSAIGEIPLCIAGEVDCVKAEPGSPNPGLSGCMELKTNKVIQHPGHEAMFHKKLLKHWAQSWLLGIPEVVVGFRDDDGILRSQTTFDTAKIPYLVEVLNKPSWSPNRCLQSLHSVCSFLTKNVLPTDPLVTYPHIRGNRQAVKEAGELPPAVVWRLAFDPKKGCELHAVGEVGVVDGRWGGMLKEEYVRWRMGLE
The following text describes a protein:
Function:
Involved in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic. Catalyzes hydroxylation at the C21 methyl group of mycinamicin VIII, the earliest macrolide form in the postpolyketide synthase tailoring pathway, leading to mycinamicin VII. Uses ferredoxin MycCII in electron transfer for catalysis.
Sequence:
MVVWPMDRTCAWALPEQYAEFRQRATLVPAKVWDGSPTWLVSRYEHVRALLVDPRVTVDPTRQPRLSEADGDGDGFRSMLMLDPPEHTRLRRMFISAFSVRQVETMRPEIEKIVDGILDRLLALEPPVDILTHLALPMSTQVICHLLGVPYEDREFFQERSELASRPNDDRSMPALIELVEYLDGLVRTKTAHPDTGLLGTAVTERLLKGEITHQELVNNAVLLLAAGHETSANQVTLSVLTLLRHPETAAELREQPELMPNAVDELLRYHSIADGLRRAATADIVLGDHTIRAGDGLIILLSSANHDGNTFGAEATFDIHRPARHHVAFGYGPHQCLGQNLARLEMEVTLGKLFRRVPALRLAQEPDALRVRQGSPIFGIDELLVEW
The following text describes a protein:
Function:
Antitoxin component of a type II toxin-antitoxin (TA) system. Antitoxin that directly inhibits activity of EndoA in vitro. Upon expression in E.coli counteracts inhibitory effect of endoribonuclease EndoA. The EndoA-EndoAI complex does not seem to bind its own promoter.
Sequence:
MSESSARTEMKISLPENLVAELDGVAMREKRSRNELISQAVRAYVSERTTRHNRDLMRRGYMEMAKINLNISSEAHFAECEAETTVERLVSGG
The following text describes a protein:
Function:
Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histones. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (By similarity).
Subcellular Localization:
Nucleus, nucleoplasm.
Sequence:
MASTTTTILPKDHIKLRSTIHQKLIESGEKERLKVLLKSKLVEGGWRDEVKIACREYIKNNQNENFKIEDLIALITPIAKKKVPPQVKADLIKRIRKFLGPNIQNHHHHHIHIQSNTPNSPHH
The following text describes a protein:
Function:
Enhances the incorporation of serine into phosphatidylserine and sphingolipids.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MQSFMTGAPGHHIQSIKKSTSTRLVYVVFFLLVSIVAYILSYWTFSWFNNLDVLKICSKGDNECKGALVVYRLTFGLALYHILLGLVMINVKSAGDSRAKLQDGYWPLKILLLGVLIFVSFFIPNSFFRVYTWISIFSAAIFIFIQLVLLIECAYSLNESCVRKIEDEGHSGKKWYVLLCVLSFGSIALAVAGTVLMLVFYGRGSCSINQFYIVFNLGICLIVGVLSISEKVREYRPSSGLFQSGVVMLYCTYLIYSAINSEPPGTCSSNNTSSPKESTIIIGAVFTIISVCYSAFRSSDSTELLGNHNHYSSIPTDPNAETTGVADDECECTAYNYSFFHFTFACGAMYLSALLTNWATMTSTDITSSSTSSSNSTISVDSGMVSVWVKVVSSWVVVLLYLWTLIGPILLRNRVWD
The following text describes a protein:
Function:
Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters.
Subcellular Localization:
Nucleus.
Sequence:
MEVGDFFVGGFYGGAAGNDFSPVKMMSTERKLPENFTVDDLLDFSNEDAIINDVFLENVAGNSTDSSTVTCNSSVSGGDNHLSPVNLPHSSQFSGELCVPYDELAELEWLSNFVEDSFSTDQNLQSSLQIFATSKSLIPESSSSSTRPDSLIQSPSNSNPIFQHETPLPGKARSKRSRVAPCDWSTRLLHLNPKSAAQKKRENPNANSELPVRKCLHCAAEKTPQWRTGPLGPKTLCNACGVRYKSGRLVPEYRPAASPTFVSAKHSNSHRKVLELRRQKEFQRAQHQQLMSQTSVFGISNGGCADDFLIHHHGGPNFSHMI
The following text describes a protein:
Function:
Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome.
Sequence:
MAFRNRMYQLSNVDDADADILNSHFAPNPRGQNHTHGRRRNTLALCTTKDQMFVYGSTPAGGAEWCSEALERSRPRAAFKQQRRRHVPRWISDSFRTCLPKPSGILKEQTVNEEEGNSRHRGKYDCDERIGVAESMNYWHGIVRTEEDGSKTLFLIPESWEDVHLKEGLVAIIDLAVDRLHCSKLVLFVDKNNSSLPYLVKSLHWVGFEPLPHLNCSDHALFGMEL
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.
Subcellular Localization:
Nucleus.
Sequence:
MADENYVSGYPPPPYYYKEYQSVDIKKLMEMSNFKSTDEKSFLEHMKNSYDVIYDVDTNTYIKNIESIDNIKNCNFIMGRPPPLPLRNSYNVFGIDYELQRNIEELDSDEILYDEKKNLKEEFIRLYKIYKETFFLLFDDIVNNRKDDKSKIKHLTKIHVNLFHILAKLRHYQTINNIINVLKIQLKKRQIAIDKMKISLLNVYQYINFVQTNYGNNKMIKNEENQEKKNKKKN
The following text describes a protein:
Function:
Catalyzes the ATP-dependent unwinding of RNA duplexes with a single-stranded 3' RNA extension. Central subunit of many protein complexes, namely TRAMP-like, nuclear exosome targeting (NEXT) and poly(A) tail exosome targeting (PAXT). NEXT functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation. NEXT is involved in surveillance and turnover of aberrant transcripts and non-coding RNAs. PAXT directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor ZCCHC8, which links to RNA-binding protein adapters. Associated with the RNA exosome complex and involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA. May be involved in pre-mRNA splicing. In the context of NEXT complex can also in vitro unwind DNA:RNA heteroduplexes with a 3' poly (A) RNA tracking strand. Can promote unwinding and degradation of structured RNA substrates when associated with the nuclear exosome and its cofactors. Can displace a DNA strand while translocating on RNA to ultimately degrade the RNA within a DNA/RNA heteroduplex (By similarity). Plays a role in DNA damage response (By similarity).
Subcellular Localization:
Nucleus, nucleoplasm. Nucleus, nucleolus. Nucleus. Nucleus speckle.
Sequence:
MADAFGDELFSVFEDDSTSAAGAKKDKEKEKWKGPPGSADKAGKRLDTKLQSESASGGKNKRDLDVEGTDEPIFGKKPRIEDSINEDLSLADLMPRVKVQSVETVEGCTHEVALPADEDYIPLKPRVGKAAKEYPFILDAFQREAIQCVDNNQSVLVSAHTSAGKTVCAEYAIALALREKQRVIFTSPIKALSNQKYREMYEEFQDVGLMTGDVTINPTASCLVMTTEILRSMLYRGSEVMREVAWVIFDEIHYMRDSERGVVWEETIILLPDNVHYVFLSATIPNARQFAEWICHLHKQPCHVIYTDYRPTPLQHYIFPAGGDGLHLVVDENGDFREDNFNTAMQVLRDAGDLAKGDQKGRKGGTKGPSNVFKIVKMIMERNFQPVIIFSFSKKDCEAYALQMTKLDFNTDEEKKMVEEVFNNAIDCLSDEDKKLPQVEHVLPLLKRGIGIHHGGLLPILKETIEILFSEGLIKALFATETFAMGINMPARTVLFTNARKYDGKDFRWISSGEYIQMSGRAGRRGMDDRGIVILMVDEKMSPTIGKQLLKGSADPLNSAFHLTYNMVLNLLRVEEINPEYMLEKSFYQFQHYRAIPGVVEKVKNSEEQYNKIVIPNEENVVIYYKIRQQLAKLGKEIEEYIHKPKYCLPFLQPGRLVKVKNEGDDFGWGVVVNFSKKSNVKPNSGELDPLYVVEVLLRCSKESLKNSATEAAKPAKPDEKGEMQVVPVLVHLLSAISTVRLYIPKDLRPVDNRQSVLKSIQEVQRRFPDGVPLLDPIDDMGIQDQGLKKVIQKVEAFEHRMYSHPLHNDPNLETVYTLCERKAQIALDIKSAKRELKKARTVLQMDELKCRKRVLRRLGFATSSDVIEMKGRVACEISSADELLLTEMMFNGLFNDLSSEQATALLSCFVFQENSSEMPKLTEQLAGPLRQMQECAKRIAKVSAEAKLEIDEETYLSSFKPHLMDVVYTWATGATFAHICKMTDVFEGSIIRCMRRLEELLRQMCQAAKAIGNTELENKFAEGITKIKRDIVFAASLYL
The following text describes a protein:
Function:
Mg(2+)-dependent 3'RNA exonuclease and endonuclease that resolves R-loops via specific degradation of R-loop RNA stucture. Shows no activity against D-loop and minimal activity against the RNA strand of an RNA-DNA hybrid duplex oligomer. Has no 3' or 5' exonuclease activity, no uracil glycosylase activity, and no 5' flap endonuclease activity on DNA substrates. May have a role in maintaining genomic stability through its role in R-loop resolution.
Subcellular Localization:
Nucleus.
Sequence:
MASERGKVKHNWSSTSEGCPRKRSCLREPCDVAPSSRPAQRSASRSGGPSSPKRLKAQKEDDVACSRRLSWGSSRRRNNSSSSFSPHFLGPGVGGAASKGCLIRNTRGFLSSGGSPLRPANASLEEMASLEEEACSLKVDSKDSSHNSTNSEFAAEAEGQNDTIEEPNKVQKRKRDRLRDQGSTMIYLKAIQGILGKSMPKRKGEAATRAKPSAAEHPSHGEGPARSEGPAKTAEGAARSVTVTAAQKEKDATPEVSMEEDKTVPERSSFYDRRVVIDPQEKPSEEPLGDRRTVIDKCSPPLEFLDDSDSHLEIQKHKDREVVMEHPSSGSDWSDVEEISTVRFSQEEPVSLKPSAVPEPSSFTTDYVMYPPHLYSSPWCDYASYWTSSPKPSSYPSTGSSSNDAAQVGKSSRSRMSDYSPNSTGSVQNTSRDMEASEEGWSQNSRSFRFSRSSEEREVKEKRTFQEEMPPRPCGGHASSSLPKSHLEPSLEEGFIDTHCHLDMLYSKLSFQGTFTKFRKIYSSSFPKEFQGCISDFCDPRTLTDCLWEELLKEDLVWGAFGCHPHFARYYSESQERNLLQALRHPKAVAFGEMGLDYSYKCTTPVPEQHKVFERQLQLAVSLKKPLVIHCREADEDLLEIMKKFVPPDYKIHRHCFTGSYPVIEPLLKYFPNMSVGFTAVLTYSSAWEAREALRQIPLERIIVETDAPYFLPRQVPKSLCQYAHPGLALHTVREIARVKDQPLSLTLAALRENTSRLYSL
The following text describes a protein:
Function:
Key enzyme in the biosynthesis of O-acetylated (O-Ac) sialoglycans such as gangliosides O-AcGD3 and O-AcGD2, which affect various processes such as cell-cell interactions, host-pathogen recognition. Catalyzes the transfer of an acetyl group from a donor, the acetyl-coenzyme-A molecule (acetyl-CoA), to the C7/8/9 OH-position of a sialic acid residue. The primary site of O-acetyl group transfer on sialic acid seems to depend on cell type and can be C7, from which the O-acetyl group could subsequently migrate to the C8 and then to the C9 position, or at C9 with possibility of migrating to the C8 and then to the C7 position. Together with ST8SIA1 (GD3 synthase) it increases the levels of ganglioside Ac-O-7-GD3. Can transfer the acetyl group from acetyl-CoA to free sialate (N-acetylneuraminate, Neu5Ac) in vitro, but has preferred substrate specificity for CMP-activated sialate (CMP-Neu5Ac), resulting in the formation of 9-O-acetylated CMP-Neu5Ac (CMP-Neu5,9Ac2). CMP-Neu5,9Ac2 may be used by sialyltransferases as a sialate donor for glycoconjugate acceptors such as ganglioside GD3. O-acetylation at position C9 of ganglioside GD3 can counteract the pro-apoptotic effects of the ganglioside GD3 in tumor cells.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MAVLAYNLGKREINQYFSIKNAKLLAAAAVVLLTVFHAASRHYGSSDTCDWLLSSGRFLGDNVWQPYGCMLHKYKSTEAKFCLREKRIAFVGDSRIRQLFYSFIKMMNPEVKEVGNKHENIPFVDGDSTVNFLWYAEVNNSLKEQLMLWTEGSASKPHVIIIGAATWSIKLHNGKSEALFQYKANLTAIADTLEKLAEHSEVYWVLQDPVYEDVLSESRKMITNEQINLYNEAAVSTLNTSKKKVKFLEASRQAAMETISQSVDGLHLPESTRDVGAMVLMNSMCNKILKPIDGSCCQSAPPLSVLQKLAAAVLLVSVVCFVLLGFSSHRKSRPAPDVESGEEKKHPAAVGQLNPKGPLLAIGKMSLIMLYFYLCDRADIFMKEQKFYTHSAFFIPLIYIFVLGVFYSENSKETKLLNREQTDEWKGWMQLVILIYHISGASAFIPVYMHVRVLVAAYLFQTGYGHFSFFWLKGDFGLYRVCQVLFRLNFLVVVLCLVMDRPYQFYYFVPLVTFWFAVIYATMALWPQILQKQANGSAFWNLALLLKLLGLLLFIGFFAYSQELFEGIFSVWPLSKLFELQGSIHEWWFRWKLDRFAVVNGMLFAFIYLLLQKYQLLSEGKGEPLFSNKISNCLLFVSVVSFMTYSIWASGCKNKSECNEMHPYISVILAFILIRNIPGYARSLYSSFFAWFGKISLELFICQYHIWLAADTKGILVLIPGNPTLNIIVSTFIFVCVAHEISQITNDLAQVAIPKESGPLLKRLLGAGVFLVLVLTLSQKD
The following text describes a protein:
Function:
Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Also acts as a link between CDC42 signaling and regulation of the actin cytoskeleton. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization in the vicinity of membrane tubules by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization and dynamin may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling. May be required for the lysosomal retention of FASLG/FASL (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Golgi apparatus. Cell membrane. Cell projection, phagocytic cup. Note=Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9. Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ (By similarity).
Domain:
The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation (By similarity).
Sequence:
MDWGTELWDQFEVLERHTQWGLDLLDKYVKFVKERVEVEQSYAKQLRSLVKKYLPKRPAKDDPEIKFSQQQSFVQLLQEVNDFAGQRELVAESLGIRVCLELAKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQDINATKADVEKAKQQAHLRNHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELQVVPIIGKCLEGMKVAAESVDAKNDSKVLIELHKSGFARPGDLEFEDFSQVMNRVPSDSSLGTPDGRPELRAASSRSRAKRWPFGKKNKTVVTEDFSHLPPEQQRKRLQQQLEERNRELQKEEDQREALKKMKDVYEKTPQMGDPASLEPRIAETLGNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHTRPPDPPTTAPPDSSSSSNNSGSQDNKESSEEPPSEEGQDTPIYTEFDEDFEEPASPIGQCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGGEGYVPTSYLRVTLN
The following text describes a protein:
Function:
Involved in autophagy. May be required to recruit the atg8-phosphatidylinositol conjugate and the atg12-atg5 conjugate to the pre-autophagosomal structure (By similarity). Required for normal survival when exposed to pathogenic bacteria S.typhimurium by promoting autophagic degradation of intracellular S.typhimurium.
Subcellular Localization:
Endosome membrane; Peripheral membrane protein.
Sequence:
MKKSDSSSSLVFSGIQIEINNNYGSGSGSNNNNNNNNNNNNINNNNNPNNNPNNNGPPLRPSSEWVLLSSSQPTIATTTNLTTNAPLSDSMIMNYVGNDNLNTPITPSTSSPYLKRNNSNLNSIIENSNNSSPSNAITRNNSFNMDPNNNNNNNNNNNNNNNNNNNNGEYMNSSIVFDNNVNNNNNNPNNNPNNNVHSNSHNTNNSITHSGSITSSNSNNNNSNNNNNNNSNNNNNINNSVNSVNSLMMNSDKNCNHQFPSDDVLISNEHDIIDLALNKEFLNQYRIQTNSIFINSQHVINQDVQSYQDYESLLSSYNTILNQLLLITSSNKNNNNNNNPNNNNNNVTSPNSLLSPPSTSQLQQQQQQQQQSPSPPLNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNYYLMSTSTMSSTTTNLSTSTNSNINTNIPTNYNMSTSITATTTTTTATNTIAIGTTTTAAITTAATNSTNSNNLNLSSTNLGLDNNFLYQRILPEILSLLEKLTVFSRNNDTEIFNRLGNNVKLIFDHLNLIKNDILEANFSHLSGIFTIYNHTIISSDKTTKQFVFRFLHSLAPMTVPPAIVVTPELKKVVQKIHFSKPTFTPLCIEWKEICKYIDVLKSVSLFIAQVGQYCFLNQSIIINDELLFIPSIYVLFDNIQNLSMKEERFHIEYILHNLKFIVSKIPKQTREFTKTEIERLYSYIRGNPSYVKEILPKLLKNIYIDPYFYHLWNNHCIHLLNNNINNNNNNNTNNSSNNSNNNNNTNINIGKDIGNDLTLLLVSNKNSFLLSFDERHFSIFYSSISNSTTTTITPTITSPNNNSNRINNNNNNNNNNNNNNNNNNNINVNNNVNNNNVNNNNNNNNNNSNQYIVNYFDNTTSLLNFIESNQFKYIILSNKEVETIKFFKSVLPVTLPLPQPSSRQAILQQQQQQNYKPRILCGPCLSRFKTILDEFDNEESIENQIYSNYLNNINNNENIDPNLIDGNENKINGNDNNNNHDDDEKTNNNNNNNNNNNNNNNNNIYNNNNIEDYNNNNDNNYNFENEINDKENEFRELEKEINEIEKEEQELIKEYLELENRNQINLDIKQKLEDILKEIKLEEKTHYDLVNNYYQEYFDLKQEDEIYTNQINAIRDQLERVSQIDINKITFKIELPNTGVNGGIVGYNESSNTTISSINGFRLGTLSNLKVDWEEINSAWGETSLLLYVLASQLEFNFQNYKLIPMSSKSIIQSKNDKMSYTLYGGDNIQFSRSFLWFGASDQRFDSGMEAFLSCVNDIATFVQSKKPSINFNYRISKDKIGDSNRLLSIKIAGNSELNWTMALRFMLSNLKKILDNLDSIVESKQKQQQLQRQQSLNNL
The following text describes a protein:
Function:
Catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates. May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin.
Subcellular Localization:
Melanosome.
Sequence:
MVALTDEVDIRESLAVLPCVADEGSVAFLRAHGRVFFLLRGPPGSGKGTVMDALREYYPDARTYWSDRMFTSLMAPPRNRETVRESHRLCQEKIEAYMKENVPVIINKNTNVTVWEISPYLRLGAKYGYVTILIDINRKFLLKPQVLAVTNSKGLNAEYMNKRMSQWEDVLPMAVGWFPSARDAVLLTRRFDQLHQTLSKEADLTMNPLRSPEGFPFCLARLCWFGWEPSDRDYCRRQEVERAYGMKSTIKVFGYAILEGLVLALVQLSDDQVALCSTCSNDDGEAPSHEDDIAASFARSVSLHSWKETRCTVALEDIVDGNRTVEDLPKADKLSYLPVPRVRFIILGSTNDPFAYSRSLGGLHKRLAEEFSVSEEGVIQCEQKINVGGVDVYSTETAWLVLDDRSVELDAVFTGFYQPYSTGPRPRPVGRGRLRRPWQPRSDKW
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.
Sequence:
MASFFSRTTFRTLNTLFKATPCSKTPITAPLAQPLARRFIGTLPREQPRLRLGSTAPNFEALTTQGKIDFHQWMDGCWTILFSHPADFTPVCTTELGAFAKLKGEFAKRGVKMIGLSANDLGSHGDWIKDINEVTGSDVQFPIIADADRKVAWLYDMIDESELANLAEKGIAFTIRSVFIIDPAKKIRLVMSYPASTGRNTAEVLRVIDSLQTADKKGIATPIDWQVGDDVIVPPSVSTEDAKKKFGEVRELKPYLRYTKY
The following text describes a protein:
Function:
Has a role in maintaining cell viability during stationary phase induced by stress response. May be involved in pre-mRNA splicing.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, spindle. Note=During mitosis associates with the spindle microtubules.
Sequence:
MSLAKKIDDDEKQLVKPVNKEQTYKKPIPLEEDDYIEGLSYIIQQQYFPDLPKLKAEVVLESEEVGSFDAQNESRDEKLKYLIAKNSEDPLRKRLPSLAIHEITKAQLDGENKPISVASYQNKFTSEDNASFGELMEDESRLRAEQHKRRFGVHSQQPSNSIQTIGYSNSDAIKSIAWKEKDKSIKTWNYQPKNALMYTPETNHSSSLSQIKKQSTEIQADATGLSQSFLEAANQPSTDPIVPPSVNETDASVNGYPLVDVNFGQAVGSSSKSYFNIPERPRRERLHAMRVRDIRSHSTNTTITSVDSASTALNSYSTPNSVSRKLTNLTPAARRLVARSYLRSPLHGSSPSASRHTALRTSIPKFSWTPTPRVKSTAPTPKRV
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MVLKHSVTYNLSFFISFTFSSIFFSSLILFLVYKSVLSKLFFIKYLMLNLTKVGLRRFWSQSPRRNAPKKELSSLLESTITPKAFSKRTEEPNPIMQGTDTIPMPFYLHAKCLKNNTHITLCSPERKIIFRASGGTCGFRKGKRRGYDAAYTICSKVLEQIQVKRLGIENLHVIFHGFSQAREAVQNCLLGQEGAVIRDKIVKVMDRTPIKFGGPRGRRERRI
The following text describes a protein:
Function:
Involved in formation and maintenance of cell shape. Required for the spatial organization of components of the peptidoglycan-synthesizing holoenzyme in the periplasm and peptidoglycan synthetic activity.
Subcellular Localization:
Periplasm. Note=Localizes in helical or banded patterns along the cell length. This localization requires a normal cell shape, but is not disrupted in the absence of intracellular filaments formed by MreB.
Sequence:
MRFREGPLGDLKVPLTWTAAVALIVAAVIGVAFLLADRRETLQEQAYGVTRQTVDTVARPVSGAIAAPGRWTGLGLDYVRSYFFTAHENRRLKAELAEMRQWRDRALALQDQNDRFKSLLGLRTDPPIPMAAARVVSDSRGPFANTRLADAGSERGIVVGNPVLNERGLVGRVVGVSRGVSRVLLLTDIASRTPVMIDRTNARAILTGDGGPNPKLDYLRGVDPIQQGDRVVTSGDGGVVPRGLPVGAAVKGLDGRWRVVLFADQASIDYVRILLFKDFAQLADEKQLQARSLPPVTTEDPQTSILSNPVSRPVAPTPSPATATPSAAPAARPATTATPPQTGAPR
The following text describes a protein:
Function:
Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture (By similarity).
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MVSANGSHCPYDDSFKYTLYGCMFSMVFVLGLISNCVAIYIFICALKVRNETTTYMINLAMSDLLFVFTLPFRIFYFATRNWPFGDLLCKISVMLFYTNMYGSILFLTCISVDRFLAIVYPFKSKTLRTKRNAKIVCIAVWFTVMGGSAPAVFFQSTHSQGNNTSEACFENFPAATWKTYLSRIVIFIEIVGFFIPLILNVTCSSMVLRTLNKPVTLSRSKMNKTKVLKMIFVHLVIFCFCFVPYNINLILYSLVRTQTFVNCSVGAAVRTMYPITLCIAVSNCCFDPIVYYFTSDTIQNSIKMKSWSVRRSDSRFSEVQGTENFIQHNLQTLKNKIFDNESAI
The following text describes a protein:
Function:
Binds to and protects nitrogenase from irreversible exposure to O(2), in what is known as 'conformational protection'. Shifts nitrogenase into an inactive, O(2)-tolerant state. Exists in 2 states, an open oxidized state that binds and protects nitrogenase, and a closed reduced state that probably does not bind nitrogenase; cooperative oxidation of the 2Fe-2S clusters causes the conformation change. Does not protect nitrogenase with the vanadium-iron subunit, not clear if it protects the iron-only nitrogenase.
Subcellular Localization:
Cytoplasm.
Domain:
Has mobile N-loop (residues 59-96) that changes position in a redox-dependent manner being folded against the protein in the closed reduced state, protecting its [2Fe-2S] cluster, or away from the protein in the open oxidized state. The open form complexes with the MoFe and Fe subunits of nitrogenase protecting them from O(2).
Sequence:
MATIYFSSPLMPHNKKVQAVAGKRSTLLGVAQENGVKIPFECQDGNCGSCLVKITHLDGERIKGMLLTDKERNVLKSVGKLPKSEEERAAVRDLPPTYRLACQTIVTDEDLLVEFTGEPGGA
The following text describes a protein:
Function:
Part of the acuABC operon, which is possibly involved in the breakdown of acetoin and butanediol. Acts as an acetyltransferase inactivating acetyl-CoA synthetase AcsA via acetylation at a Lys residue.
Sequence:
MEHHKTYHAKELQTEKGSVLIEGPISPEKLAEYEFHDELTAFRPSQKQHEALIEIAGLPEGRIIIARFRQTIVGYVTYVYPDPLERWSEGNMENLIELGAIEVIPAFRGHSVGKTLLAVSMMDPQMEKYIIITTEYYWHWDLKGTNKDVWEYRKMMEKMMNAGGLVWFATDDPEISSHPANCLMARIGKEVSQESIERFDRLRFHNRFMY
The following text describes a protein:
Function:
Involved in neurogenesis. Interacts with other neurogenic proteins in the specification of the neuroblast versus epidermoblast cell fate.
Subcellular Localization:
Nucleus.
Sequence:
MGISENKACNCKADKVKGDDIFSPLKGKMKVLKKIKRRMGLASRSGSNGGGTNNLPPLLFHNVHGENIRISRDGTIARRVESFCKGIAFSSRPVKVNEKICIKFLEISNNWSGVIRFGFTFNDPSSLRYGLPKYACPDLTNKPGYWAKALPERFCSQNTVLFYYVTSTGDVHFGINGEEKGIFFSSVETRGPLWALIDVYGNSTAIEFVDIRHQLNNSRRNIASNSCENPPEDVDRIIYRMEQVHIQQRDNEDLSLPLLRYQPPQLNFNPMMLHRTRGRNVRFGSTRNNAYRTDTEFCQGYVFTARPLQLGERVVVQILATEPMFQGCLGLGLTSCDPATLQSGDLPDDSNFLLDRPEYWVLSRDFARNLNKGDEISYCISPTGEVQISRNGDSPLVVIHVDQTLRLWAFFDIYGSTQRIRVLSCPAPVSPVRNFERRIISPSATESMNSINSQSEIRRNSVMQSNSRLCCVAPADIQVQPATNGGAVLSVILPPAHANFLNQQTQTVHVNHQNSVHTQNGHGPHPSYVGPAIPISPVVAPVPNLQPTGTMISTCSSTYVEPISDSSSYSTPLGWAEVNGATVGTGTECTICYENSIDAVLYMCGHMCMCYECALQQWRGKGGGHCPLCRAVIRDVIRTYKS
The following text describes a protein:
Function:
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MQYVYIFIGGALGALLRYLISFLNTDGGFPIGTLIANLTGAFVMGLLTALTIAFFSNHPTLKKAITTGFLGALTTFSTFQLELIHMFDHQQFITLLLYAVTSYVFGILLCYVGIKLGGGLS