lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MASGFLPPYIIPGQEPGTTAEERQEIYKYLHWTRLGQAGQESCVAKTILSGAMGLGLGAMFSLMSSSFAYEDPLRRDPNFDTMKFDKKARVMFKEMGRGMWSTGKGFGKVGALYAGLECCVESYRAKSDLWNSLVGGGLAGGMLAWQSGMKAMLFGAAGFAAFSGAIDAYMRKEPPDDD
The following text describes a protein:
Function:
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity).
Sequence:
MARITTEDCTGKISNHFDLTLVAARRARQLENGNTPLVDDVRNNKPTVTALREIAAGHIGTELLTRNK
The following text describes a protein:
Function:
Transcription factor involved in the regulation of the insulin signaling pathway. Consistently activates both the downstream target Thor\d4EBP and the feedback control target InR. Involved in negative regulation of the cell cycle, modulating cell growth and proliferation. In response to cellular stresses, such as nutrient deprivation or increased levels of reactive oxygen species, foxo is activated and inhibits growth through the action of target genes such as Thor. Foxo activated in the adult fat body can regulate lifespan in adults; an insulin peptide itself may function as one secondary messenger of insulin-regulated aging. Also regulates Lip4, homolog of human acid lipases, thereby acting as a key modulator of lipid metabolism by insulin signaling and integrates insulin responses to glucose and lipid homeostasis (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Note=When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation (By similarity).
Sequence:
MMDGFAQDWPTLTHTDNGLAMDQLGGDLPLDVGFEPQTRARSNTWPCPRPENFVEPTDELDSTKASNQQLAPGDSQQAIQNANAAKKNSSRRNAWGNLSYADLITHAIGSATDKRLTLSQIYEWMVQNVPYFKDKGDSNSSAGWKNSIRHNLSLHNRFMRVQNEGTGKSSWWMLNPEAKPGKSVRRRAASMETSRYEKRRGRAKKRVEALRQAGVVGLNDATPSPSSSVSEGLDHFPESPLHSGGGFQLSPDFRQRASSNASSCGRLSPIRAQDLEPDWGFPVDYQNTTMTQAHAQALEELTCSVADELTLCTQQQQQGFSAASGLPSQPPPPPYQPPQHQQAQQQQSPYALNGPAPGYNTLQPQSQCLLHRSLNCSCMHNARDGLSPNSVTTTMSPAYPNSEPSSDSLNTYSNVVLDGPADTAALMVQQQQQQQQQQQQQQQQLSASLEGQCLEVLNNEAQPIDEFNLENFPVGNLECNVEELLQQEMSYGGLLDINIPLATVNTNLVNSSSGPLSISNISNISNISNLSNLSNISNISSNSGSSLNLNQLQAQLQQQQQQQQAQLQQQAQQQQQPHQQHQQQLLLNNNNNSSSSLELATQTASSNLNARVQYSQPSVVTSPPSWVH
The following text describes a protein:
Function:
Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
Sequence:
MGYSSAKPSLNNCSEPEQVVRLRAQLLEWYGRMGRDLPWRRTRDPYAIWISEIMLQQTQVKTVLPYYQRWLAALPTVAALAAAELEAVLKLWEGLGYYTRARNLHKAAQVIVKEHGGVFPETAQQLQQALPGIGRSTAGAIASSAFGRCEAILDANARRVLGRLFAVGDPPARAEAKLWEISQRLVDPQAPHNFNQALMDLGATVCTARSPLCLLCPWQVDCLGRRSGDPTHFPVRPARAVRSEIAGVSVAIECQGKFLLVRRPERGLLAGLWEFPFVESVGGGEPEETVRVAFGNRLESLERLGQVEHEFTHRHLTAQVLRAQWIAAPAALPKVFDCREHTWQPPECWLKFPMPGYVHKICKLLKEALPKVSVD
The following text describes a protein:
Function:
Mediates a low-level metal ion resistance, probably by efflux of cations from the cytoplasm into the periplasm. Also mediates resistance to cobalt, cadmium and zinc via regulation of the Czc system. May repress expression of the Czc system by an export of the inducing cations. Binds and transports zinc. Can also bind cobalt, copper and nickel.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MGAGHSHDHPGGNERSLKIALALTGTFLIAEVVGGVMTKSLALISDAAHMLTDTVALAIALAAIAIAKRPADKKRTFGYYRFEILAAAFNALLLFGVAIYILYEAYLRLKSPPQIESTGMFVVAVLGLIINLISMRMLSSGQSSSLNVKGAYLEVWSDLLGSVGVIAGAIIIRFTGWAWVDSAIAVLIGLWVLPRTWILLKSSLNVLLEGVPDDVDLAEVEKQILATPGVKSFHDLHIWALTSGKASLTVHVVNDTAVNPEMEVLPELKQMLADKFDITHVTIQFELAPCEQADAAQHFNASPALVGSKSLAAGGN
The following text describes a protein:
Function:
Mitochondrial protein-lysine N-methyltransferase that trimethylates ATP synthase subunit C, ATP5MC1 and ATP5MC2. Trimethylation is required for proper incorporation of the C subunit into the ATP synthase complex and mitochondrial respiration. Promotes chronic pain. Involved in persistent inflammatory and neuropathic pain: methyltransferase activity in the mitochondria of sensory neurons promotes chronic pain via a pathway that depends on the production of reactive oxygen species (ROS) and on the engagement of spinal cord microglia.
Subcellular Localization:
Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MFGGGGDACTMKRKELQEGKDAKDDAFASSDANHFEKRNWGLLIPGVVGGTLVALYAVATPFVTPALRKICLPFVPATSTQIENVLKMLQRRSGSLVDIGSGDGRIVIAAAKEGFRAVGYELNPWLVWYSRYRAWREGVHHTAKFYISDLWKVSFSQYTNVVIFGVPQMMLQLENKLQLELEEDTRVIACRFPFPHWTPDHITGEGIDTVWAYDSKSFQGSGKRCPEILSQRKKTHNRNISLSVKCEDLRLALLTSLY
The following text describes a protein:
Function:
Involved in regulation of invasive growth.
Miscellaneous:
MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MGSISRYLLKKAADGLKDEQRLKIEMSDSKSVPECFHFNRERRMPIAEINGEDGFFMFPSQQSLENFENTKKYSNELSPDAIGIPLFQIINCTLPFGKRGHSNTVVGNVPYYKIFKFILRTADEPPPYTVAKIVCSNNGLILYKVPLYDIYKNVSQANVTYSFVGTTSTEPNLLAMAHREGHRDLDTKVNNLNLRWHVTYSPVVTNDHYKLILLADYEVNRLDEDVIRAAKNKMSIDQKDQKVQRFVAAHYTREFETSLFRWVAQEGHLILGEYSTDQGSFGLNNIPPLTEELGCQSLLIHYIEYMKRQRKKIAKEARRQNKRNVANTTNMNMNLM
The following text describes a protein:
Function:
Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA.
Miscellaneous:
MISCELLANEOUS: Present with 5260 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLLVRTTSLNVSRMPVPCLARGIGILKGKYRLANLMNAQPSVRHVSSEIQQKDQQAGESNTATDTGVIHKSDEETLIYFDNVYARTTSVWNPTLWYNLLLRNQSRDAVREKIRNLASPPNNPIYGLELKSTIPVKRDGGVFATFVVPPKYTKAQVNSLIQQNTARESSKNLLSYFTRASAFPVKGSPWIEDLRRLPSTTIVIKFQGPALTEEEIYSLFRRYGTIIDIFPPTAANNNVAKVRYRSFRGAISAKNCVSGIEIHNTVLHIQYENIRRGHLVSNFFTNHTRIAIPVLFALLSIFAVLVFDPIREFSIEQKITHKYSLSWDNKFWKQLKTLTSSTMTSIKYYWGGPDDNHQRKHLWEERIEKVNDLKMWLEENNNTFVVIRGPRGSGKHDLVMQHTLQNRANVLYLDCDKLIKSRTDPMFLKNAASQLGYFPIFPWIDSVTGVLDLTVQGLTGQKTGLSETKESRFRNMLTTSLMSIRRIALKNYKAFVSTGDGTVNVKEEDYLQQHPEAKPVIVIDRFEGKSEINGFVYKELSDWAAMLVQMNIAHVIFLTETVASNQRLSESLPNQVFKNLILSDASKENSRNYVLSQLEDYLYYNKKSKGENVKEPESEKETAENNDSDSEADTSVKKAEVILNEKELQEIDASLEPLGGRMLDLQAFVRRVKSGEEPSEAVDKMIEQASEQITQMFLSDKIDSNKSAQAWELIELLSANPVIPFHEIVNKPLFKAAPETGIMELENNGLITVSRDRGVLQEIRPAKPLYRAAFTYLINDPELAKVLKTRYLLKVVGFETGRIKKWEEELKPLGKVPDQKLFKTRLDYLSGKINASNAVITKCEEEIKNLSK
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Sequence:
MKIAIAGSGALGSGFGAKLFQAGYDVTLIDGYTSHVEAVKQHGLNITINGEAFELNIPMYHFNDQPDESIYDVVFLFPKSMQLKEVMEDMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGELVDEGKENVIKVADLLNEAELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNVDEVFEYLVDLNEKVGAHYPSMYQDLIVNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKESQRHAQD
The following text describes a protein:
Function:
Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MVAFSALSGVSALSLLLCLVQHAHGVSLKVSTQGGNSSSPILYGFMFEDINHSGDGGIYGQLLQNPGLQGTTPNLTAWAAVGDATIAIDGDSPLTSAIPSTIKLDVADDATGAVGLTNEGYWGIPVDGSEFQSSFWIKGDYSGDITVRLVGNYTGTEYGSATITHTSTADNFTQASVKFPTTKAPDGNVLYELTVDGSVAAGSSLNFGYLTLFGETYKSRENGLKPQLANVLADMKGSFLRFPGGNNLEGNSAENRWKWNETIGDLWDRPGREGTWTYYNTDGLGLHEYFYWCEDLGLVPVLGVWDGFALESGGNTPITGDALTPYIDDVLNELEYILGDTSTTYGAWRAANGQEEPWNLTMVEIGNEDMLGGGCESYAERFTAFYDAIHAAYPDLILIASTSEADCLPESMPEGSWVDYHDYSTPDGLVGQFNYFDNLYRSVPYFIGEYSRWEIDWPNMKGSVSEAVFMIGFERNSDVVKMAAYAPLLQLVNSTQWTPDLIGYTQSPDDIFLSTSYYVQEMFSRNRGDTIKEVTSDSDFGPLYWVASSAGDSYYVKLANYGSETQDLTVSIPGTSTGKLTVLADNDPDAYNSDTQTLVTPSESTVQASNGTFTFSLPAWAVAVLAAN
The following text describes a protein:
Function:
Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. May have a role in synapse differentiation and growth.
Sequence:
MAATPAPAVTPAATATSAAAKIPVNPVSPEEETLLRGLNKLRNEEKLTDVTLIVEEHRFKAHRVVLAASSDYFCAMFADCAMIESRKDEINLYGIKARAMGSIIDYIYTSMLELNYDNIEEILAAATHVQVREVIDRCTIFLGAKIEMENCLAIAGMADIYGIMDLSERAYRYMCAHFEEFATTSDFKEMKVDQLRFILSSNYPIDVAEQDLVRLVCSFAIEQQLNESALGDLLRLIKWQHISYKSVDELRNMNCSLDKGKQLPLPTSYYNRIKQEHMGHLLNGVVSLKDQSLPQGPTNMRGMELCLLKIGGFEWNGLTNVIMCFSPKKMNWYELTAIPHIDQCNFGTAVLNNKLFIVGGAYDVFLKEYIHPFGFCYCPLRNTWMTIAPIQQDRCRFSLNAVGTQHLYAVGGILDDDNEEALRMISNVERYDIAKNVWTYMPSLQENRSQHAGVVVGDKLYISGGVHLANILASMWVFDTKTEVWQELASMPTPCCDHVLVAVDNRIYACGGWHESLTEWRVLVEHIYAYDIETNTWSVETKIPAPKFYTGVTAMGRTIFFVGGLDSTESIDRASAETMAYDLDTKEWWHEKDSWDSPNDVWESTCVAIYVPNCDA
The following text describes a protein:
Function:
DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Subcellular Localization:
Nucleus.
Sequence:
MAAAASVAPVTEPAKVAEVEDPASDAEREADVAAAMATAVELVSKPAVIDDEFSLAPQADDDAAANATSASHSPSAFAAGRASQQQQQELLQSAGVSKVASSASGGSSASGSGNHAGSSGGSSGGKGGKGANSKDTLFFPDYRERVVQIFEQLTQINSALGERFKSQLYGRTVECFKRGDKVFQLLPPNLLPLPEEDPKKKAIIEALYKDDPAAQKKRVEEVERNRAKRSLVLSSDNLIPGLGTKLREKVIEILVTGGLEELHRQEAKPIIRAIRELTQVHGVGPRTAIDYFKKYGISTVAQLRDYAIKAGELDMSNKDSGKPSNLVVCADKSKFHLNDAQRLGLVYYEDMCHRIPHEEGRLHEAFMKLRMRKYLGKDYELVVCGSYRRQVESAGDIDVLITHRRSAAEGGGGSSSSSGGRPLLPPSKVLGAFLAGLKADKYIEATLAQGPTKFMGLCRLRATVTESVSAATGKGKAAKANGKAPTKFRARRLDVRYVDSDSFPAAMLYFTGSKNFNVIMRSEAIKKHCVLNEYGLFRKPTRKQMQHYGVVQKNPDMSFHDMITRLARFDLSAIKDEENELANGSSAEAGGGASGATAAGSGASGDADGAASKKVTAALTKIKKKGRGKTKQELAELHEMAKIVERQRVKACTEREIFEALGMDYVPPKDRSV
The following text describes a protein:
Function:
May be a male specific regulatory factor.
Sequence:
MNFIQIAVLFVLVAVALARPQEDPANLPAPEAAAAPPAAAAAPPAAAAAPPAPPAPPAAAPQAAPAGGSGRKKNVNHNVITIG
The following text describes a protein:
Function:
Immediate early (EI) protein that plays many roles during productive infection including regulation of host cell cycle progression, regulation of viral gene expression or nuclear export of intronless viral RNAs. Acts as a transcriptional transactivator via interaction with the cellular transcription elongation factor SUPT6H and as a nuclear RNA export factor via interaction with UAP56, a component of the cellular mRNA export machinery (By similarity).
Subcellular Localization:
Virion tegument. Virion. Host nucleus. Host cytoplasm. Note=Shuttles between host nucleus and cytoplasm.
Sequence:
MELHSRGRHDAPSLSSLSERERRARRARRFCLDYEPVPRKFRRERSPTSPSTRNGAAASEYHLAEDTVGAASHHHRPCVPARRPRYSKDDDTEGDPDHYPPPLPPSSRHALGGTGGHIIMGTAGFRGGHRASSSFKRRVAASASVPLNPHYGKSYDNDDGEPHHHGGDSTHLRRRVPSCPTTFGSSHPSSANNHHGSSAGPQQQQMLALIDDELDAMDEDELQQLSRLIEKKKRARLQRGAASSGTSPSSTSPVYDLQRYTAESLRLAPYPADLKVPTAFPQDHQPRGRILLSHDELMHTDYLLHIRQQFDWLEEPLLRKLVVEKIFAVYNAPNLHTLLAIIDETLSYMKYHHLHGLPVNPHDPYLETVGGMRQLLFNKLNNLDLGCILDHQDGWGDHCSTLKRLVKKPGQMSAWLRDDVCDLQKRPPETFSQPMHRAMAYVCSFSRVAVSLRRRALQVTGTPQFFDQFDTNNAMGTYRCGAVSDLILGALQCHECQNEMCELRIQRALAPYRFMIAYCPFDEQSLLDLTVFAGTTTTTASNHATAGGQQRGGDQIHPTDEQCASMESRTDPATLTAYDKKDREGSHRHPSPMIAAAAPPAQPPSQPQQHYSEGELEEDEDSDDASSQDLVRATDRHGDTVVYKTTAVPPSPPAPLAGVRSHRGELNLMTPSPSHGGSPPQVPHKQPIIPVQSANGNHSTTATQQQQPPPPPPVPQEDDSVVMRCQTPDYEDMLCYSDDMDD
The following text describes a protein:
Function:
Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGCTTNHSVIVPVFALISMFSLSSWINVVGLWVELPIMVQKLPERWNLPSYMTLVIQCCNIAPAIYTLAGKIKCRKKQNSSNSGCSDAKRDVALPMIIILISISSALLNSFFWDRTAYIGRAERSVALMFFLSLSSVASCLSALVYLPYMARYPSVYLSAFYFGQGLSGLLPGLIGLGQGLGGNPTCANVTVWNSSCLNATFSNCSSEDVKYLLKPVYPQPKFSVQIFLILISLLLVVSFLAFYLLNFSRLNQYQLRKNASSDNVATVSGDDKTNADVDRKNNGLVSNNHHRSSGDNKEVRAAAAADVEDESKLISPSPSSQYTLSASETNSNASTSAVVVKNLAEPQLSKSHLAFYLSSIVAINMATNGIIPATQSYTCLPYSNVVYTLTVRLSSVVGSLSSLSSMFIPKPSIKVFFFMILTALSVVVFHVVIAVLSPTPPLVNTVYGPILIVCTALIMTSLFSFAKVTAASRMHAYGGRRALKWCGAVTQLGSFLGAMLAFALINWTSIFTSISPCSAEH
The following text describes a protein:
Function:
Calcium-binding protein which probably acts as a calcium sensor and modulator, contributing to cellular Ca(2+)-mediated signaling. Activates endogenous kinase(s) in a Ca(2+)-dependent manner. Plays a role in regulating actin cytoskeleton dynamics. Regulates the association of actin filaments in a bundle but not actin polymerization and/or nucleation processes. Required for host cell phagocytosis and macropinocytosis.
Subcellular Localization:
Cytoplasm. Cell projection, phagocytic cup. Cell projection, pseudopodium. Note=During host erythrocyte phagocytosis, co-localizes with F-actin to the phagocytic cup. Leaves the phagocytic cup before the formation of phagosomes. Co-localizes with FAK in the pseudopodium.
Domain:
The N-terminal domain (EF-hands 1 and 2) is required for localization to the phagocytic cup, G-actin binding and activation of kinases; The C-terminal domain (EF-hands 3 and 4) is required for G-actin binding but is dispensable for localization to the phagocytic cup and activation of kinases; The central linker region between EF-hands 2 and 3 is required for the interaction with F-actin.
Sequence:
MAEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDADGNGEIDQNEFAKFYGSIQGQDLSDDKIGLKVLYKLMDVDGDGKLTKEEVTSFFKKHGIEKVAEQVMKADANGDGYITLEEFLEFSL
The following text describes a protein:
Function:
Needed for the assembly of the mitochondrial F1-F0 complex at high temperature.
Subcellular Localization:
Mitochondrion.
Sequence:
MSTPTTVYRSLLRQLREMNVIYKTSTLKQKKGFTKTQKDFLVYTKACLRNNKVEQLSKFQEVVAFLKSGNQHELLFNRHHPLANVNELEKVKLAARRVGLESPE
The following text describes a protein:
Function:
Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MALLRGLLVLSLSCLQGPCFTFSPVSAVDLPGQQPVSEQAQQKLPLPALFKLDNQDFGDHATLKRSPGHCKSVPTAEETRRLAQAMMAFTTDLFSLVAQTSTSSNLVLSPLSVALALSHLALGAQNQTLHSLHRVLHMNTGSCLPHLLSHFYQNLGPGTIRLAARIYLQKGFPIKDDFLEQSERLFGAKPVKLTGKQEEDLANINQWVKEATEGKIEDFLSELPDSTVLLLLNAIHFHGFWRTKFDPSLTQKDFFHLDERFTVSVDMMHAVSYPLRWFLLEQPEIQVAHFPFKNNMSFVVVMPTYFEWNVSEVLANLTWDTLYHPSLQERPTKVWLPKLHLQQQLDLVATLSQLGLQELFQGPDLRGISEQNLVVSSVQHQSTMELSEAGVEAAAATSVAMNRMSLSSFTVNRPFLFFIMEDTIGVPLFVGSVRNPNPSALPQLQEQRDSPDNRLIGQNDKADFHGGKTFGPDLKLAPRMEEDYPQFSSPK
The following text describes a protein:
Function:
Membrane-associated protein that warps the membrane surface to access and bind aromatic isoprenes with high specificity, including ubiquinone (CoQ) isoprene intermediates and presents them directly to Coq7, therefore facilitating the Coq7-mediated hydroxylase step. Participates in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular Localization:
Mitochondrion.
Sequence:
MSDNNNNNNNNNNNNNNMDNNNSDTFLKIWRNQYLQNQIFKSIEILNYEELLKNDNLMYIGNRKKIGEIRTLGFLVKRKLWRILKIMIENDEYLVFTEKSVKKFLRNCGDAQLMKLVLIKKKSEIECLVNAYRFLIDEHLMWQLELVDKELSEGSRYEYIPGTILDTAIRSGSLEAIKYVYDNISQEYDQDIAIYNCFYGNNHLRCPDKTIPFLQEYCNFKIRSNIHSSLCIPWVDVKRNIKNEDFKRELFEKKYILDYNPISILELQNALVDPETIQLEMEIFYKKNPTWEVPAGLYERTLSKDELIDIFYMDLLAKHLFSGNQFDSSTKTRVFTHYLFDHKKSRDLTKLYPLVTNGPSRFLIPYAIKMFDIELLKQVLEDPILPFFEPGFPIIEFFLIPSNPHNKPLNLNEFIGSFFTDPILLQTNNTNPFKTYALLSIIQLYPMNAIREAFHTFNQLIQQHGEHTRPANIPINHRRIETTNKDTNHLKELQQFLNENYHLLVNGPPNESLKIYMETPNSNISQHKKNDNDFIFCNNQLSDYEQVLLKNDMIQFFKILNQIKQYQPSFVPTFHQYIIKSLAKFSSTQTIKTLIQDFNSFNNQFDMTLLLKASYNKGNYQVTNYLIETICSNQLNEDNINKNDLILSFDEIIVGNSSSLCPFSKGDTQTIQYMLSNEYYKNNFKSLSNFELMINKLLTTGNLKCYQELLKLDLLPPLESLSNGVSEGNFEISTKLFNGLVNSGRVTILNHFLKLNQIPLEAIPPIFNHQLYHFNLFESHHFLRYHFNEIIDKNDSVSIQNNQNPQCNIM
The following text describes a protein:
Function:
Catalyses the transfer of galactose onto proteins or lipids.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
KSTKVKLLKLTCCVFLVQIGLLLIGVTCFRYASSRPEPYPALQRLVNHVDRFLWSRFHLDSISVELEGDDVVGYLPSTSKVASDDATLDFCDPSAAKLIGALMFPLPPTPPPSYDVISKNNLQVTPGGSYRPPKCRARYKVAVIVPFRDRENHLKHLLSHLHPILQRQQIEYTIYVIRQVHGSLFNRAILMNIGFAQALLEDDYDCYIFHDVDLLLENDHCTYHCPKISDHDRSNPRHLSMSVDKFHYDEATKMEVFGGVSVFTKEQFLSVNGFSNLYWGWGAEDDDLFLRTWRRGYKIDRSETEKCTYRMIAHSHDGENPMS
The following text describes a protein:
Function:
Attaches the virion to the host receptor LamB, inducing viral DNA ejection. During tail assembly, initiates distal tail tip assembly by interacting with gpI, gpL and gpK. During virus entry to host cell, binds strongly to host LamB in an irreversible attachment. The binding induces structural changes in the tail leading to viral DNA injection through LamB trimeric pore.
Subcellular Localization:
Virion. Host cytoplasm.
Sequence:
MGKGSSKGHTPREAKDNLKSTQLLSVIDAISEGPIEGPVDGLKSVLLNSTPVLDTEGNTNISGVTVVFRAGEQEQTPPEGFESSGSETVLGTEVKYDTPITRTITSANIDRLRFTFGVQALVETTSKGDRNPSEVRLLVQIQRNGGWVTEKDITIKGKTTSQYLASVVMGNLPPRPFNIRMRRMTPDSTTDQLQNKTLWSSYTEIIDVKQCYPNTALVGVQVDSEQFGSQQVSRNYHLRGRILQVPSNYNPQTRQYSGIWDGTFKPAYSNNMAWCLWDMLTHPRYGMGKRLGAADVDKWALYVIGQYCDQSVPDGFGGTEPRITCNAYLTTQRKAWDVLSDFCSAMRCMPVWNGQTLTFVQDRPSDKTWTYNRSNVVMPDDGAPFRYSFSALKDRHNAVEVNWIDPNNGWETATELVEDTQAIARYGRNVTKMDAFGCTSRGQAHRAGLWLIKTELLETQTVDFSVGAEGLRHVPGDVIEICDDDYAGISTGGRVLAVNSQTRTLTLDREITLPSSGTALISLVDGSGNPVSVEVQSVTDGVKVKVSRVPDGVAEYSVWELKLPTLRQRLFRCVSIRENDDGTYAITAVQHVPEKEAIVDNGAHFDGEQSGTVNGVTPPAVQHLTAEVTADSGEYQVLARWDTPKVVKGVSFLLRLTVTADDGSERLVSTARTTETTYRFTQLALGNYRLTVRAVNAWGQQGDPASVSFRIAAPAAPSRIELTPGYFQITATPHLAVYDPTVQFEFWFSEKQIADIRQVETSTRYLGTALYWIAASINIKPGHDYYFYIRSVNTVGKSAFVEAVGRASDDAEGYLDFFKGKITESHLGKELLEKVELTEDNASRLEEFSKEWKDASDKWNAMWAVKIEQTKDGKHYVAGIGLSMEDTEEGKLSQFLVAANRIAFIDPANGNETPMFVAQGNQIFMNDVFLKRLTAPTITSGGNPPAFSLTPDGKLTAKNADISGSVNANSGTLSNVTIAENCTINGTLRAEKIVGDIVKAASAAFPRQRESSVDWPSGTRTVTVTDDHPFDRQIVVLPLTFRGSKRTVSGRTTYSMCYLKVLMNGAVIYDGAANEAVQVFSRIVDMPAGRGNVILTFTLTSTRHSADIPPYTFASDVQVMVIKKQALGISVV
The following text describes a protein:
Function:
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Acts redundantly with BOP2. BOP1/2 promote leaf and floral meristem fate and determinacy in a pathway targeting AP1 and AGL24. BOP1/2 act as transcriptional co-regulators through direct interaction with TGA factors, including PAN, a direct regulator of AP1. Controls lateral organ fate through positive regulation of adaxial-abaxial polarity genes ATHB-14/PHB, YAB1/FIL and YAB3, and through positive regulation of LOB domain-containing genes LOB, LBD6/AS2 and LBD36. Promotes and maintains a developmentally determinate state in leaf cells through the negative regulation of JAG, JGL and class I KNOX genes. Is also involved in nectary development, formation of normal abscission zones (AZs) and suppression of bract formation, probably by regulating the cell wall disorganization.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes.
Sequence:
MSNTFEESLKSMSLDYLNLLINGQAFSDVTFSVEGRLVHAHRCILAARSLFFRKFFCESDPSQPGAEPANQTGSGARAAAVGGVIPVNSVGYEVFLLLLQFLYSGQVSIVPHKHEPRSNCGDRGCWHTHCTAAVDLSLDILAAARYFGVEQLALLTQKHLTSMVEKASIEDVMKVLIASRKQDMHQLWTTCSYLIAKSGLPQEILAKHLPIELVAKIEELRLKSSMPLRSLMPHHHDLTSTLDLEDQKIRRMRRALDSSDVELVKLMVMGEGLNLDESLALIYAVENCSREVVKALLELGAADVNYPAGPTGKTALHIAAEMVSPDMVAVLLDHHADPNVQTVDGITPLDILRTLTSDFLFKGAIPGLTHIEPNKLRLCLELVQSAALVISREEGNNNSNDNNTMIYPRMKDEHTSGSSLDSRLVYLNLGATNRDIGDDNSNQREGMNLHHHHHDPSTMYHHHHHHF
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MAAEMLLEPNRGSVTFEDVAVYFSWEEWALLDEAQRCLYHDVMLENFALTSSLGCWHGAEDKGAPSEKSISVEGVSQIKTLKADSCPQKGQPFEKCGPVLRDNFHLPEHQEAHLEQKPYTCGNQFYIAANLQQYQGQHIREIPIRTSVDTALIIKSCRTHLSGESFFSEGIRKDDLASMGFFHQPVTHTNENSNNSNECEAVFHSGERHQNWGEGKKILNCTDTLVEDQRVLTREGLYECSKCGKTSTRRWNLIQHQKVHTGERPYECHECGKSFTRSNSLKTHRKVHTGEKPYEYKECGKSFSQRSNLVQHQKGHSGERLHQCGECGKSFSRSSTLIHHRRLHTGERPYECSKCGKSFKQSSSLSSHQKIHTGERPYECRECGKSFSCKSNLIIHLRVHTGERPYECQECTKSFSCKSNLINHLRVHSGERPYDCAECGQSFTQRSILIQHQRIHTGERPYECHECGKSFSRKFSLIYHRKGHTGERPHQRKERGKSFNCKSNLNEHQKIHPGERSHESGDSGKSFSQSSSLIQH
The following text describes a protein:
Function:
Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MNRLLRVIPRARLLHTTPRLYQASNFAMPAMSPTMTEGGIVSWKVKEGDEFSAGDVILEIETDKAQIDVEAADDGVMAKIYKKDGDKDIQVGDTIAVIAEPGDDIKTIDIPAPVESDGKPAPKEEAKEEVKEAPKEEAKAPAPKAPSTPKEAPKTESSSAPSSSGYSAPANPAQTLLPSVSSLLVANGISKEDAFAKIKATGPHGRLLKGDILAYLGKVPEGSPGAVADEINKRSHLDLSNIKPAKKSDAAAPTGAAKAGDAAAPATKAAPEPVIFTSFLDVAHFEPEDQLELQRIVKQAIKLAKYDAVELAKPRRSANVDPDFEAIIGPAKGTKFYDVNVIYPKSTKRALSNGADLYDILSDRKPRKAAVQVPSNTVQVDVTVNDKVPGAEKRAKLFLNRLEYHLTVEE
The following text describes a protein:
Function:
May play a role in cholesterol transfer to late endosomes. May play a role in modulating membrane acid-sensing ion channels. Can specifically inhibit proton-gated current of ASIC1 isoform 1. Can increase inactivation speed of ASIC3. May be involved in regulation of proton sensing in dorsal root ganglions (By similarity). May play a role in protecting FBXW7 isoform 3 from degradation.
Subcellular Localization:
Membrane; Single-pass type III membrane protein. Late endosome membrane. Membrane raft. Cell membrane; Single-pass type III membrane protein. Cytoplasmic vesicle.
Sequence:
MLGRSGYRALPLGDFDRFQQSSFGFLGSQKGCLSPERGGVGTGADVPQSWPSCLCHGLISFLGFLLLLVTFPISGWFALKIVPTYERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVELAVEAVLQPPQDSPAGPNLDSTLQQLALHFLGGSMNSMAGGAPSPGPADTVEMVSEVEPPAPQVGARSSPKQPLAEGLLTALQPFLSEALVSQVGACYQFNVVLPSGTQSAYFLDLTTGRGRVGHGVPDGIPDVVVEMAEADLRALLCRELRPLGAYMSGRLKVKGDLAMAMKLEAVLRALK
The following text describes a protein:
Function:
Bifunctional nuclease with both RNase and DNase activities. Involved in basal defense response. Participates in abscisic acid-derived callose deposition following infection by a necrotrophic pathogen.
Sequence:
MMLRAQFRVRTMDGFRVLRDERNARGLIPNLGGCFSIHFGFKRSLRLQCRGGRKSILIYCKSSRGNSSNGGGQSTNAYDDHDHDFLQASVLISETLLHYRMLRQGFQEDMRWRLPGRWNPFDVLSQESRPDMSFIGYEFLRRFQSPTIFLKVSCDGDFLLPIIVGASIGEFAIEKLIDNFREGDHNGDCPDQFQLVSNLVEKLGYEVKMVRITERVVNTYFARVYFSKLGENEILSIDMRPSDAINVANKCKAPIHVSKQIVFTDAIRISYGMGRVHDRKTTYDVSLDSPADGPDSLSEELDIVKNMNLAIQEERYGDAAMWRDKLMELRQSSHEQ