lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Receptor for CLEC2D/OCIL. Ligand-binding contributes to inhibition of cytotoxic natural killer (NK) cells. May mediate MHC class I-independent 'missing-self' recognition of allografts, tumor cells and virus-infected cells.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Domain:
Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases leading to down-regulation of cell activation.
Sequence:
MDSTTLVYADLNLARIQEPKHDSPPSLSPDTCRCPRWHRLALKFGCAGLILLVLVVIGLCVLVLSVQKSSVQKICADVQENRTHTTDCSVNLECPQDWLSHRDKCFRVFQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKYNSFWIGLRFTLPDMNWKWINGTTFNSDVLKITGDTENGSCASISGDKVTSESCSTDNRWICQKELNHETPSNDS
The following text describes a protein:
Function:
Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity).
Subcellular Localization:
Vacuole.
Sequence:
MKLLASTVLMGAAAASIAPQQQVLKNPFQSASKPISEAWSKSMESLNHLTDSMKDMTSEAKAVWDEVSTLFPEAMDRATFFQQPKPHTRKPDTAWDYVVKGADIQNVWVENSKGEKEREIDGKLEKYNMRAKKVDPTKLGVDKVKQYSGYLDDEENDKHLFYWFFESRNDPKNDPVVLWLNGGPGCSSLTGLFLELGPASIDKNGKLHNNPYSWNANASVIFLDQPVNVGYSYSGGSVSNTIAAGKDVYALLTLFFKQFPEYAKQDFHIAGESYAGHYIPVFTHEILSHKKRNINLKSVLIGNGLTDGLTQYEHYRPMACGEGGYPAVLDSSECKAMDNALPRCQSLIQSCYDSESVWSCVPASIYCNNAMMGPYQRTGQNVYDIRGKCEDSSNLCYSALGWISDYLNQAAVQKELGVEVSSYDSCNFDINRNFLFQGDWMQPFHRLVPDILEQIPVLIYAGDADFICNWLGNQAWTEALEWPGQKGFNAAKTKDLQLENGHKTGTFKSSGNFTFARIFGAGHMVPMDQPEASLDFLNKWLNDYTL
The following text describes a protein:
Function:
Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8.
Domain:
The Asn-rich domain is dispensable for deubiquitinating and deneddylating activities.
Sequence:
MARDNENILEEWCLIESNPCIFYDMLKRMGATEISVEDVYSLSYFDDYINNKEIINMNHILGVDTYLGENNKTLDKENNVVDVIELYKNNICMEDKYNKLLKHHSYIYGIIFLFNIGKHYKNNKYIEHNVPDNLFFAKQVIPNACATQAILSIVLNKDIELNDEIKNIKTFSLNFDSSMKGLTLSNCTFLRNIHNSYKPPIYLDKEDVHHDKKKSEDSFHFVSYISFQDKVYLLDGLQSGPVLINADEQNKPNPNNNNNNKDNDNDNNNNNNNNNNNNNNNNNNNNNNNNNNIGMNGKDWIEISREHIKKEIDEICNSQTNNDVRFNIIAVMKDKEYIIQEYINIHRIVKQRVNIKLINLGENIELSDEINEDEFPLLNDIPSIENLPNNVDTLYNIVNKSTLEINYLQSLLHEQKEIKKLWNKELTFKFFNFYPFIMSSLNLMAKHKLLKDAYQKEKLKNATKS
The following text describes a protein:
Function:
Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence.
Subcellular Localization:
Nucleus.
Sequence:
MERAEALTSSFIWRPNANANAEITPSCPRCGSSNTKFCYYNNYSLTQPRYFCKGCRRYWTKGGSLRNVPVGGGCRKSRRPKSSSGNNTKTSLTANSGNPGGGSPSIDLALVYANFLNPKPDESILQENCDLATTDFLVDNPTGTSMDPSWSMDINDGHHDHYINPVEHIVEECGYNGLPPFPGEELLSLDTNGVWSDALLIGHNHVDVGVTPVQAVHEPVVHFADESNDSTNLLFGSWSPFDFTADG
The following text describes a protein:
Function:
Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone. The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA. Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E. The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Sequence:
MVFGSRPPALTEANIGDQSGKVFIVTGATSGYGLLLSTYLYQNNGTVYLAARNAKKTAEVIADLKQRFPASRGRLDSISLNLSDLSTIKKSAEEFLAKETRLHVLWNNAGVMFPPAGSTTSQGYELQLGTNNVGPHLFTKLLYPTLAATAKEAPKNTVRVVWVSSDAASWAPKPAIDFNNLDYRRNESDRSKYGRSKAGTVMQAVELARRARKDGSGIVSIALDPGIANTGLQRDMGRLMSTMVKLIANKPEIGAYTQLFAGLSPEITAEVAEKEWVVPPGKIGCPRRDLFTDTETSRKWWEWNEEQVKAYL
The following text describes a protein:
Function:
Required for efficient RNA interference (RNAi) of pop-1 indicating a role in the germline development.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MPFDLLAERKRWNAGYESIDTSSQKLTEVVTPITVTWENIEVKTRKKLFSKKQKQLLNRVSGIAKPGEMVALMGASGAGKTTLMNVLMCRNMKGLEKNGTVKVNGTKIGKEISLISGFAQQQEIFIPTLTVDEYLMIQARLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTPGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANSGRTLIHQPTAELFFQFDKIIFLSMGKTAFMGTPHESVKFFADCGHPIPKLFNPPEWIQSKLSVIPNNETKSRETIGKIIEFYEKSIIHQKSIVEIRVIATTELPPYIENPGFFAETGALLKRACLDVIRSPAQMRMKLIQKVVMGLFIGSLYWQQPLDPRGVRNTNSALYFLIAELTFSTMFGIMTFMEHELPLIAREYHDGLFYVISYYISRFLSYLPLFTIDGALMIVISYWMIGLNSTWQQVAKSILISVLVEQSATSCGLFLACLFETTSLAIAFAVPASGLFALLSGLYGNTNNFPVYIRWMQWTSWCRYGFEGLVVNQWSQVDNPKWDPFYRELILKQFSFNKDNYQLDVIGLCSIVIFFYLAGYIALFIRIRLSR
The following text describes a protein:
Function:
Potential transcription factor which binds the nonamer motif 5'-CATCCAACG-3'. Possibly involved in regulating transcription of the histone H3 and H4 genes.
Subcellular Localization:
Nucleus.
Sequence:
MSSSAMEALHALIPEQHQLDVEAAAAVSSATSGEESGHVLQGWAKRKRSRRQRSEEENLALCLLMLSRGGKQRVQAPQPESFAAPVPAEFKCSVCGKSFSSYQALGGHKTSHRVKQPSPPSDAAAAPLVALPAVAAILPSAEPATSSTAASSDGATNRVHRCSICQKEFPTGQALGGHKRKHYDGGVGAAASSTELLAAAAAESEVGSTGNGSSAARAFDLNIPAVPEFVWRPCAKGKMMWEDDEEVQSPLAFKKPRLLTA
The following text describes a protein:
Function:
Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity (By similarity). Overexpression in cultured neurons significantly inhibits neuronal transferrin endocytosis, secretory vesicle retrieval, cell migration, and oxidative stress from glutamate toxicity.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein. Recycling endosome. Endoplasmic reticulum membrane.
Sequence:
MEPRGAAAGEPEPAVSPSFQARLWKNLQLGVGKGKGGGGGRAGGPERRTAATPTPSLPPPKTTQDVGSTGSRWSGFKKRKQVLDRVFSSSQPNLCCSSPEPLEPGGAGRAEQGSTLRRRLREHLLPVAKGSSTAAGTVGVTPPGGRSPDSAPSSSASSSLSSSPQPPPRGDRIRDEGTRRGSPEAHLCHQKSSSLPGTACLEQLLEPAPPPAEPARRPAEPQSLQKGEELDCSQKINPVETSNADVPLADPGMYQLDITLRRGQSLAARDRGGTSDPYVKFKIGRKEVFRSKIIHKNLNPVWEEKACVLIDHLREPLYIKVFDYDFGLQDDFMGSAFLDLTQLELNRPTDVTLTLKDPHYPDHDLGIILLSVILTPKEGEPRDVTMLMRKSWKRSSKFQTQSLRLSDQHRKSHLWRGIVSITLIEGRDLKAMDSNGLSDPYVKFRLGHQKYKSKIMPKTLNPQWREQFDFHLYEERGGVMDITAWDKDAGKRDDFIGRCQVDLSSLSREQTHKLELQLEEGEGHLVLLVTLTASATVSISDLSVNSMEDHKEREEILKRYSPLRIFNNIKDVGFLQVKVIRAEGLMAADVTGKSDPFCVVELNNDRLLTHTVYKNLNPEWNKVFTFNIKDIHSVLEVTVYDEDRDRSADFLGRVAIPLLSIQNGEQKAYVLKNKQLTGPTKGVIHLEIDVIFNAVKASLRTLIPKERKYIEEENRLSKQLLLRNFIRTKRCVMVLVNAAYYVNSCFDWDSPPRSLAAFVLFLLVVWNFELYMIPLLLLLLLTWNYFLIISGKDNRQRDTVVEDMLEDEEEEDDRDDKDGEKKGFINKIYAIQEVCVSVQNILDEAASLGERVKNTFNWTVPFLSWLAIIALCVFTAILYFIPLRYIVLVWGINKFTKKLRSPYAIDNNELLDFLSRVPSDVQVVQYQELKPDHSHSPYKRKKNNLG
The following text describes a protein:
Function:
Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Involved in the regulation of cellulose production.
Sequence:
MTTPSWRSLRIKKYQFSLRLFLFLNAVSALFTLVFPLYQINVFCTPMIGIVVLSVLLLIWHGKYGQKRINLPFISLLFGGIWAAHIALKYPALGHYDFSFLLISLLSVLFIGSIAFAANIVAFTLYSLPPVAVCLWLNGNEQGLRILYLLTLPMVGIAIQHVIQKRYDNFAQQLMFKLLAERETLNGLSMLDPLTGLYNRRGLQNRLDTLQAPGSHEHYVLLLDIDHFKAYNDHYGHMMGDQALIRVSAAIRDAVRSRDVVCRFGGEEFLVLLTTAEPQQARATAERIRQEVYDLKIPHMFNESVATNVTVSIGIAPLTDRNIGDAIEKADKALYEAKHLGRNHILVSDDMRAL
The following text describes a protein:
Function:
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Subcellular Localization:
Cytoplasm.
Sequence:
MKPERNSLSEKIRNAEKIVIKVGSARLSGLPSEVNDFLFQLVSDIRHLRDLGKKVILVSSGAIARGRLLLSELPSTISSGDSLAEKQALAAMGQNRLVNLYDSFFSKVNLSIAQILFGVLDLESKEGYKNLKNTFTQLVEWGILPVVNENDSVATEEVKFGDNDMLSALVSLIVEADLLIILTGVDGFLKEEKVVPFLEKISKEDLGLAGGPSGPGTGGMFTKLKSAGLLSEAGIPTAILNGKKMHVIREFLEKNSIGTLVAPSGNRVFSEEDVKEIIRKNRNGNGGNSL
The following text describes a protein:
Function:
Receptor for prostaglandin F2-alpha (PGF2-alpha). The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. Initiates luteolysis in the corpus luteum (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSTNSSIQPVSPESELLSNTTCQLEEDLSISFSIIFMTVGILSNSLAIAILMKAYQRFRQKYKSSFLLLASALVITDFFGHLINGTIAVFVYASDKDWIYFDKSNILCSIFGICMVFSGLCPLFLGSLMAIERCIGVTKPIFHSTKITTKHVKMMLSGVCFFAVFVALLPILGHRDYKIQASRTWCFYKTDEIKDWEDRFYLLLFAFLGLLALGISFVCNAITGISLLKVKFRSQQHRQGRSHHFEMVIQLLGIMCVSCICWSPFLVTMASIGMNIQDFKDSCERTLFTLRMATWNQILDPWVYILLRKAVLRNLYVCTRRCCGVHVISLHVWELSSIKDSLKVAAISDLPVTEKVTQQTST
The following text describes a protein:
Function:
Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities (By similarity). Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4). Also has aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides. In addition to its pro-inflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MPEVADTCSLASPASVCRTQHLHLRCSVDFARRALTGTAALTVQSQEDNLRSLTLDTKDLTIEKVVINGQEVKYTLGESQGYKGSPMEISLPIALSKNQEVVIEISFETSPKSSALQWLTPEQTSGKQHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGEAPDPEDPSRKIYRFNQRVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFHALGGWGELQNTIKTFGESHPFTKLVVDLKDVDPDVAYSSIPYEKGFALLFYLEQLLGGPEVFLGFLKAYVEKFSYQSVTTDDWKSFLYAHFKDKVDLLNQVDWNAWLYAPGLPPVKPNYDVTLTNACIALSQRWVTAKEEDLNSFSIEDLKDLSSHQLNEFLAQVLQKAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEEAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKACMHPVTAMLVGKDLKVD
The following text describes a protein:
Function:
L-amino acid ligase, which preferentially catalyzes the formation of L-aspartyl-L-methionine dipeptide from L-aspartate and L-methionine in the presence of ATP. Less active with L-asparagine and L-methionine as substrates. Less active with L-aspartate and either L-phenylalanine, L-valine, L-leucine or L-isoleucine as substrates. Decreased activity when L-methionine is substituted with seleno-DL-methionine, L-homocysteine, L-methionine sulfoxide, L-methionine sulfoximine and o-acetyl-L-serine. Decreased activity with acetylation of L-methionine amino group. Decreased activity by modification of L-methionine carboxylate to L-methionine methyl ester. No activity when L-methionine is substituted with L-homoserine. No activity with formylation of L-methionine amino group. No activity by modification of L-methionine carboxylate to L-methionine-glycine carboxylate. No activity when L-aspartate substrate is replaced by analogs such as L-homoserine, DL-aspartate beta-methyl ester, L-glutamate or o-acetyl-L-serine. No activity when L-aspartate amino and alpha-carboxylate groups are modified to L-malate, glycine-L-aspartate, L-aspartate-glycine or N-carbamoyl-DL-aspartate. No activity with L-methionine or L-aspartate as sole substrates. No activity in presence of other nucleoside triphosphates including GTP, CTP, UTP, TTP or ITP. Involved in sulfur amino acid metabolism.
Sequence:
MTNNGNEPNLTLSDLYDKDVVYTSRPSYISNPWLKPDEHQSNFLTGRELLIANQLPVIVHEASATDKLHQLFQVIGKEVPNSIYTFNNQQSYENLIKQLAHKENKKIYFQYIHDETILNQQYYALDKTLFVALNNKARIPEWTNGKFLPKRKVVKIEQFENEIKNWEFPLVIKPGDDLPTAGGYGVMICYHDADLQKAITRIKEATAETNSLIIEQKIEEKANYCVQFAYSESLGIQYLGAATQLTDKYGFYNGNENTTNVPEHVIEAGRQIMENGVNQGFFGVAGFDLLVDEDDNVYAIDLNFRQNGSTSMLLLANELNSGYQKFYSYHSKGDNTHFFNTILKYVKEGSLYPLSYYDGDWYGEDKVKSRFGCIWHGDSKETVLENERAFLAELEHY
The following text describes a protein:
Function:
May play a role in p53/TP53-mediated apoptosis.
Subcellular Localization:
Nucleus.
Sequence:
MRYSLSPDNHLEDGIMNMANFLRGFEEKGIKNDRPEDQLSKEKKKILFSFCEVCNIQLNSAAQAQVHSNGKSHRKRVKQLSDGQPPPPAQASPSSNSSTGSTCHTTTLPALVRTPTLMMQPSLDIKPFMSFPVDSSSAVGLFPNFNTMDPVQKAVINHTFGVSIPPKKKQVISCNVCQLRFNSDSQAEAHYKGSKHAKKVKALEATKNKPKMVSSKDSAKANPSCSITPITGNNSDKSEDKGKLKASSSSQPSSSESGSFLLKSGTTPLPPGAATSPSKSTNGAAGTVVESEEEKAKKLLYCSLCKVAVNSLSQLEAHNTGSKHKTMVEARNGAGPIKSYPRPGSRLKMQNGSKGSGLQNKTFHCEICDVHVNSEIQLKQHISSRRHKDRVAGKPLKPKYSPYNKLQRSPSILAAKLAFQKDMMKPLAPAFLSSPLAAAAAVSSALSLPPRPSASLFQAPAIPPALLRPGHGPIRATPASILFAPY
The following text describes a protein:
Function:
Pore-forming subunit of the rod cyclic nucleotide-gated channel. Mediates rod photoresponses at dim light converting transient changes in intracellular cGMP levels into electrical signals. In the dark, cGMP levels are high and keep the channel open enabling a steady inward current carried by Na(+) and Ca(2+) ions that leads to membrane depolarization and neurotransmitter release from synaptic terminals. Upon photon absorption cGMP levels decline leading to channel closure and membrane hyperpolarization that ultimately slows neurotransmitter release and signals the presence of light, the end point of the phototransduction cascade. Conducts cGMP- and cAMP-gated ion currents, with permeability for monovalent and divalent cations. The selectivity for Ca(2+) over Na(+) increases with cGMP concentrations, whereas the selectivity among monovalent ions is independent of the cGMP levels.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
RFREVLVIDPSGNTYYRWLFCITLPVMYNWTIIVARACFEELQSDYLQSWLFFDYFSDGVYLADMFVRTRTGYLEQGLLVKEELKLREKYKATVQFKLDVLSVVPTDLLFLKLGWNYPELRLNRLLRVSRMFEFFQRTETRTSYPNVFRISNLVMYIVIIIHWNACVYYSISKAVGFGADTWVYPDVRDPEFGRLARKYVYSLYWSTLTLTTIGETPPPVRDSEYFFVVVDFLIGVLIFATIVGNIGSMISNMNAARAEFQARIDAIKQYMRFRNVSQDLEKRVIKWFDYLWSNKKAVDEREVLKYLPDKLRAEIAINVHLDTLRKVRIFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIVKEGKLAVVADDGLTQFVVLSDGSYFGEISILNIPGSRAGNRRTANIRSIGYSDLFCLSKDDLVEALTEYPDAKAMLEEKGKQILLKDGLLDLTVANAGSHPKDLGEKVSRVEAAVDVLQTRFARMLAEYESMQQKLKRRLAKVEESLKPLVPAQLLPDLDGDPPEPSRG
The following text describes a protein:
Function:
Converts big endothelin-1 to endothelin-1.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Sequence:
MPTQGMCAHLYVPVKRVLLELGFGSGTPGEMSAYKRATLDEEDLVDSLGEGEVYPNGLQVNLRGVRPRSGCWAERTHVEKRLLVLVVLLSLGLFMCLLALSLQYRNSHRVCLSESCISVTSSILRSLDRSADPCQDFYQYSCGGWIKGNPVPDGHSRWGTFNELWEHNQATMKHLLENSTIETNSTAERKAQRYFQACMNETKIEELGAKPLQDLIQKLGGWAITGPWDRDNFQETLQLVTAHYRTSPFFSVFVSADSKNSNSNVIQIDQSGLGLPSREFYLNKTENEKVLTGYLNFMIQLGVLLGGAENSTREQMQEILDFETTLANITIPQEKRRDEEQIYHKMAAGELKDLVPAVDWMPFLQTVFYPVAINESEPVVVYAKEYLVAVSGLINSTDKRILNNYMMWNLVRKASSFLDQRFQDAEEKLMEVMYGTKKTCLPRWKFCISDTDNNLGFALGAMFVKATFAENSKLQALKMIKEIKAAFEENLSTLTWMDDETRRAAREKAEAIYDMIGYPNFIMDPKELDKVFNDYNVTSDFYFENGMRFYNFSARVTADQLRKAPSKDQWSMTPPTVNAYYSPTKNEIVFPAGILQAPFYTSSSPTALNFGGIGVVMGHELTHAFDDQGREYDKDGNLRPWWKNASVEAFKKQTECITEQYGNYTVNGEPVNGRQTLGENIADNGGLKAAYRAYKNWVRKNGAEQLLPSLGLSNDQLFFVGFAQVWCSVRTSESSHEGLITDPHSPSRFRVIGSVSNSQEFAEHFRCPPGSPMNPRNKCEVW
The following text describes a protein:
Function:
The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MSHEVKTDPHLEKDEKDDVHVHVEVADAIDAELEQLIQTNPSKGLTDAEVEERLAKFGPNEIPESKSNPFLKFLGYFGGAISFLLEIAALVSAILGDWVDFTILIIVLIVNAVIGFHEEAKAESALDALKNTLALRCRAWRNGALVEVESVHLVPGDVIALRLGDIVPADARLLGIGVTGAATEGTLQIDQAALTGESLPVSKGKGAIVYSSSIVKQGQQLAVVTKTGLHTFIGRAANLISITTEEGHFQKIINQIGNFLIIITVVMVVIIMIVYLTVKPVINEAGHVVTEFGERFKLALKQVLVLTIAAIPVGLPTVMSATMAVGASQLAKKQVIVKRLTAIEELASVSILCSDKTGTLTLNQLSFDKPYLANRGSTNSNLAGDGTGRYTEDDLLLSAYFASEPGAPDPIEKATRDAAQERVTLLRERDVQDHNIPGYLVNEFLPFNPTSKYTEATVTDNSTGKKFRCIKGAPQVIARMCGGHDEGNTAVIDLARRGLRALGVARTIDAECKVFELVGMISLLDPPRPDSAQTIKECNEYGIGVRMITGDQLIIAKEVAHRLGMQRAILDASRLVDPNITEEALTDRCIKADGFAQVIPEHKYRVVELMQKRGLLVGMTGDGVNDAPALKKANVGIAVEGCTDAARSAADIVLLAPGLSAIVDGIKTSRSIFQRMRSYALYRIASTIHFLIFFFISMLAFDFYLPDRLIIIIAVLNDAATLVIAFDNAKISKRPDKWRLGQLISLSFVLGFLLMIISFCHFFVARALVTEPDPHIRAGIIQTIMYLQISSCPHFVIFSTRVETWFWTSIPSWKFFLAIIGTQIIAMFMSIFGASFLYATAIGWGWGVGVLFMSFVFFTVLDVFKVVIIRSWSFELTAVLWPVPSRRAKLLKRQQDAILHKRVHINIAKLRRAAVMAGVVGHWRDVTLSSKKHHA
The following text describes a protein:
Function:
Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MTMDSMLLKRNKFIYHYKNLRWARGRHETYLCYIVKRRYSSVSCALDFGYLRNRNGCHAEMLFLRYLSIWVGHDPHRNYRVTWFSSWSPCYDCAKRTLEFLKGHPNFSLRIFSARLYFCEERNAEPEGLRKLQKAGVRLSVMSYKDYFYCWNTFVETRESGFEAWDGLHENSVRLARKLRRILQPPYDMEDLREVFVLLGL
The following text describes a protein:
Function:
Involved in cell cycle. Involved in cell division. Involved in cytokinesis. Involved in flagella biogenesis and in regulation of flagella length in interphase. Involved in formation of median bodies during interphase. Phosphorylates Kin-13 in vitro. Likely regulates microtubule (MT) depolymerizing activity of Kin-13.
Subcellular Localization:
Cell projection, cilium, flagellum. Cytoplasm, cytoskeleton, flagellum basal body. Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Membrane. Note=Found in both the membrane and the cytoplasmic fractions in interphase, G1/S and G2/M phases of the cell cycle. Localizes to basal bodies, flagella, axonemes, adhesive disk and median bodies of trophozoites in interphase. Remains localization at the basal bodies in metaphase, anaphase, telophase and cytokinesis. Also localizes to mitotic spindles and axonemes in anaphase. Colocalizes with microtubules (MTs) in the basal bodies, flagella, axonemes and median bodies in interphase and anaphase. Colocalizes with MTs in the mitotic spindles present between two separated groups of basal bodies in anaphase. Colocalizes with centrin in interphase as well as during cell division. Phosphorylated form localizes to basal bodies and distinctly to the cytoplasmic portion of anterior flagella, median bodies, and flagella tips in interphase cells. Phosphorylated form localizes to basal bodies and mitotic spindles in dividing cells.
Sequence:
MSHSNAPELHPQIVDPFHNVTYRPGKLLGKGGFAYVYEFHDVNSDSSYACKITPRSALQKKKYYDKFVTEVTIHRGLVHPNICRVLNVFKDQMNYYIILEKCNGGTLTDLIRRRKHLTETEARFFSKRILNALWYLHDLYIIHRDIKTSNIFLMEDFDVKVGDFGLAVKCETPEELHWTMCGTPNFLPSEVIYSHIMKRKASGRGPDPNLDEDCVNLCHQLLPAYSGQGHSFSADMWSFGCLVFSMIYGRPPFEAADIKTTYKRIVRCDFSFPGSISVSEDLKNFIKGLLTPDPRKRFTVKECLDHSWLNPSKYFIPESLPPRIISEPYEVPPLCSASPTRNMQMTINMAKNAGGTDGRFIAATPQAIGGTEHIPTPGTANFYKPQNAILTTKSAAGISRASTAMAMQNVGSAQGVVNKYGINEAEYPQIDPPCYIMSWVDYSNRYGFAYQISNGSIGVIFNDESAAILSPNALIVDYSPSLLDAAFDRALFEEGTTILSEKKFKLLSFFRDYLENRSIVPIPAADRPKEDEELKRVIEQERMNNQEIDFKRLTKGLPLPQLFLKKWKLYDDGTLCLLFNTKVFQVNFADHSKVVVAHRSVTFMSEKREIYTYPSEYLKDDRFSFKELRRRVDRARKYYEIIKAARPVDSLAQYRYNKDSTKKSASGSSTRQLGQGGE
The following text describes a protein:
Function:
Metalloprotease.
Subcellular Localization:
Secreted.
Sequence:
MSHRLLSSFHFLLLLFSLTQSTPVDEGLFNDRMRQLDQEIEIELKKDSKERYFVEGRIEEIEEAKSKIISTIDGKTIEEEDDGYTGPYAKNLYQGDIMLTQSELPFPSIHLNSFFSDQLEQVTSKKTSRNRRQAQKNSLYPSNLWKNDPIPYTFDPRFPKSRIPAVRAAIEYWERNTCIRFAENATGKDRIRFINGNGCWSMIGKTGGEQFISIGYGCDWIGTIAHELEHAFGVWHTQARPDRGYYLAVNAWNILSYQLHNFDTQALKNVDLLGIPYEFGSVMHYFQNDFAIDRSKPTLVTRTGYERFQESMSNYLPSFYDIRLINTYYQCYDKCPSKLSCLNGGIQDVNNCDQCKCPPGYNGNNCEQITISWSYLLHVQSTTGCDKFLSIGSSPVNLNATAGSDGLWSLTYEHCAIHLQATDPKKRIELSVTTRGGFTSWNCYGAGVDIRLMKDPAMSGVRLCRPNTIFDAVYSDADHMVLSLFARVNYVDFSFSARSI
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:
Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side.
Sequence:
MAHLLKTVVTGCLCPSVSNLGSCKVLPGKKDFLRTFRTHQALWCKSPAKPGIPYKQLTVGVPKEIFQNEKRVALSPAGVQALVKQGFNVVVESGAGEASKFPDDLYRAAGAQIQGTKEVLASDLVVKVRAPMVNPTLGAHEADFLKPSGTLISFIYPAQNPDLLNKLSERKTTVLAMDQVPRVTIAQGYDALSSMANISGYKAVVLAANHFGRFFTGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAVVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEFIEAEMKLFAQQCKEVDILISTALIPGKKAPVLFSKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYVHKDGNVIFPAPTPKNIPKEAPAKQKTVAELEAEKAGTVSMYTKTLRTASVYSAGLTGMLGLGIVAPNLAFSQMVTTFGLAGIIGYHTVWGVTPALHSPLMSVTNAISGLTAVGGLALMGGHFYPSTTSQSLAALATFISSVNIAGGFLVTQRMLDMFKRPTDPPEYNYLYLLPGGTFVGGYLAALYGGYNIEEIMYLGSGLCCVGALGGLSTQGTARLGNALGMIGVAGGLAATLGGLKPDPQLLAQMSGAMAMGGTIGLAIAKRIQISDLPQLVAAFHSLVGLAAVLTCMAEYIVEYPHFAMDATSNFTKIVAYIGTYIGGVTFSGSLVAYGKLQGILKSAPLLLPGRHALNAGLLAASVGGIIPFMADPSFTTGIMCLGSVSALSTLMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTIVGALIGSSGAILSYIMCVAMNRSLANVILGGYGTTSTAGGKPMEISGTHTEINLDNAVEMIREANSIVITPGYGLCAAKAQYPIADLVKMLTEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINSDFPDTDLVLVIGANDTVNSAAQEDPNSIIAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDALQAKVRESYQK
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. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Miscellaneous:
MISCELLANEOUS: Present with 7598 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSNDPGNEVSSLYPPPPPYVKFFTQSNLEKLPKYKEKKAASAKQTAPNNSNGGSEEEITCALDYLIPPPMPKNQQYRAFGSIWQVKDQLPDLESMGLTQLYKKSTENESTNYQYKIQELRKLLKSLLLNYLELIGVLSINPDMYERKVENIRTILVNIHHLLNEYRPHQSRESLIMLLEEQLEYKRGEIREIEQVCKQVHDKLTSIQDTLRTGSQSPPSSSQ
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:
MMEVDTSYVSQTRDRTGRIDAADETELARIANLPEINMHDQEGISYTLSTALCEDFHRFERAQDGTDEIFAESFDDVSSLAYACAHDDDVRQLVTLLRWSEQAAAEGDPSGFADLCSQYDTFNTVANVKRDTTNAIQRGNGLDLGADFDSKCSGDDGALVDKVYRVGFALIRCGKYEEARELLVKTGAASLAPLLSMRRIQDDFALTPMEKENPHSKMLQKRKLFKRTITAILNKLHLHSFLAQEGSTLSAPLRMLWAALAGRVDPLLSLANKTEDRIWVLANAAVEAKLDELAGGEMMCDAPASVNSIFGEVLPHESWPYFRLYSALLRGDARDAVAHAAEFLVDYEKTDKGVPEHLLRFMAHLVIIFRNTQKLHDVTLGNRIILKYTGKLLTLSLTHLIPFYVNYLNDATGKLVTMQTMYRLKSVQSRLAFLDALAQAGQNYRQLVKEVVIKSRMDQANSASDLIDRFRWLLYRERETETDAVVEACVLLRKFLESGNDASVRALLEVCATREGSLADRVRSRGVPLTSEVRRACAEYTEFVYYLNGIDAFEAWRQAHADRVNEKRKDSTRSDATAGSSMLFSAEAALESKRAGERADRLRATESMLSAKGVDVMEMFLRHEGWRTGEVREEGANGDEEERIRSLRVLRDRYYASSLLRMAQMKAESGEEKDALECTTLVHSLALHEDISKEKLRNFLQYIHKVTRSIIN