lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probable transcriptional factor. Binds to the promoter of the SQUAMOSA gene.
Subcellular Localization:
Nucleus.
Sequence:
MEWNTKWDWESLDISSPKKLQSTDWGIKEGEDIDGCFSLSDIGNKSSAKSSISESSLKEVVIKGSNLSFPNASVCSSDQSIGLKLGKRTYFENNLPGGNNTKTSSSSNTPVKKVKFSSQNTPIPRCQVEGCNLDLSSAKEYHRKHRVCENHSKSLKVVVSGLERRFCQQCSRFHGLSEFDGKKRSCRRRLSDHNTRRRKPQQSRNLSSSFYEGGEELSFVFNNQNRHGGHNRVTHSLGTQFPNDVSNSMPTLAFNRMMSSKGISAGVFDQGSDAGHDIRRALSLLSNDSWDSCEVDFGGLNQPMHRNGPTMAQHGVHVAHHGLPFSSPEYRWQVDHQSVVPHTHFEESHLLKAPYSSIQYGNPMDEILKPL
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin; The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Sequence:
MSFVFPSWSTAFSPAFHEDAKAMLEGALNKGDKPPVIQGKIEVVELHMGEQPPTLTLLEIGDLSIDRFRGILRLGYQGDAWLEVRCRVQANPLSHNPHLTFSTLPLSTPLLASQPLLVPMTLRLSKLHLRAILILVVSASKGITLVFKNDPLQNVDVSSTFDSVEVIRGYLQQEIEGQLREMFREHLPGIIHRLSQKWFSGSGVGGKVEMPYRDMSPVPSYAPINEEVEEEENEENHGTSPGNEESFPPRHIGPGGITLPLNNSVSQLAALSYSAHTLSPYARGHEHIAVRSFPYLGKSGAGTGSSGRASLASSSVGEGDIKAKRKRIFRIGKSKEADEKSEA
The following text describes a protein:
Function:
Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually lacticin 3147 A1 exhibits strong activity towards L.lactis strain AM2, weak activity towards L.lactis strain HP and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A2 it displays strong activity towards all three strains.
Subcellular Localization:
Secreted.
Sequence:
MNKNEIETQPVTWLEEVSDQNFDEDVFGACSTNTFSLSDYWGNNGAWCTLTHECMAWCK
The following text describes a protein:
Function:
Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Subcellular Localization:
Cytoplasm.
Sequence:
MAGNKVETFLKSELKKKNALLFVLIDSEVSNLEASAKLAKDVEKIGASAILVGGSSATDQIEMAQVVKGIKKGIKIPIILFPGNVTGVVPDADAILFSSLMNSENPYFITQAQALGAPSVLKFGLEPLPTAYLVIGDGTTAWFVGSARGIPFEKPKIAAAYALAAQFLGMRFVYLEAGSGAKSSVTPEMVKTVRQLFNGFLIVGGGIKDVKTAQNLVKAGADALVIGTFLEKGGSLKKLEEITKAIQRSK
The following text describes a protein:
Function:
Carboxypeptidase which preferentially cleaves C-terminal acidic residues from peptides and proteins. Can also cleave C-terminal hydrophobic amino acids, with a preference for small residues over large residues.
Subcellular Localization:
Apical cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MMQASITSILVVLTLVAQDRLAGGLEHKSYDYTKYHTMDEISAWMNQMQRENPDVVSTMTYGQTYEKRNITLLKIGFSSTTPKKAIWMDCGIHAREWIAPAFCQHFVKEVLGSYKTDSRVNMLFKNLDFYITPVLNMDGYIYSWLNNSTRLWRKSRSPCHENSTCSGTDLNRNFYANWGMVGISRNCCSEVYNGATALSEPEAEAVTDFLGAHQNHLLCYLTIHSYGQLILVPYGHPNISAPNYDELMEVGLAAAKAIKAVHGKSYKVGSSPDVLYPNSGSSRDFARLIGIPYSFTFELRDEGQHGFILPEDQIQPTCQEAYEGAMSIINYVHDKNFKNTAITVTATLWTTLMALWISTSHVF
The following text describes a protein:
Function:
Plays an essential role in viral DNA replication by acting as the polymerase accessory subunit. Associates with the viral polymerase to increase its processivity and forms high-affinity direct interactions with DNA. Facilitates the origin-binding protein loading onto DNA thus increasing its ability to assemble into a functional complex capable of unwinding duplex DNA (By similarity).
Subcellular Localization:
Host nucleus.
Sequence:
MALPRAMRPGGSHPNNFLFNTLPVIDNPVERQRAMAVFERESLRDAFEMLTPIAPSLKNAFLIFNEDGLLIHTSVGGEQVYIPIQTNNMESYSWKKAPPAVFLANVDGRRGLLDAFKAKTQTNVSKVVFEIENYSPSRILTQTVFSARDQTEEDTEMGSDAEGATQTVSSRLVKHEFNNYALMLPTRQPDVSMSLSKAQLNKILGVCKQAGDPITFQCLFDDTLQVRSGDRQVVFSVDYQHADNCGVESSSSLLEKMPMKTKKSAPEPIRGISGRRLFTLVLDEDTNFKQLIQKLKLKNAGAVLNFFLDPDSIPMIGLSTKQPFSVMMFFMCSYPTQPCQVGFSPAAFSSTPMGAGVKRRASEEEESDQPPKKLFPDGKLFKSNFVLLMDKTGAKIPCPEQPMHF
The following text describes a protein:
Function:
Catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine.
Sequence:
MPDYLDDLRLAHVLADAADAATMDRFKALDLKVETKPDMTPVSEADKAAEELIRGHLSRARPRDSVHGEEFGVAGTGPRRWVIDPIDGTKNYVRGVPVWATLIALMEAKEGGYQPVVGLVSAPALGRRWWAVEDHGAFTGRSLTSAHRLHVSQVSTLSDASFAYSSLSGWEEQGRLDGFLDLTREVWRTRAYGDFWPYMMVAEGSVDLCAEPELSLWDMAANAIIVTEAGGTFTGLDGRPGPHSGNAAASNGRLHDELLGYLNQRY
The following text describes a protein:
Function:
One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis and motility. In H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN and FliY.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Bacterial flagellum basal body.
Sequence:
MATKLTPKQKAQLDELSMSEKIAILLIQVGEDTTGEILRHLDIDSITEISKQIVQLNGTDKQIGAAVLEEFFAIFQSNQYINTGGLEYARELLTRTLGSEEAKKVMDKLTKSLQTQKNFAYLGKIKPQQLADFIINEHPQTIALILAHMEAPNAAETLSYFPDEMKAEISIRMANLGEISPQVVKRVSTVLENKLESLTSYKIEVGGLRAVAEIFNRLGQKSAKTTLARIESVDNKLAGAIKEMMFTFEDIVKLDNFAIREILKVADKKDLSLALKTSTKDLTDKFLNNMSSRAAEQFVEEMQYLGAVKIKDVDVAQRKIIEIVQSLQEKGVIQTGEEEDVIE
The following text describes a protein:
Function:
Involved in copper homeostasis, could be involved in both copper efflux and the delivery of copper to copper-dependent enzymes. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Functions during envelope stress responses; when overproduced induces degP through the activation of the two-component envelope stress response system CpxA/CpxR. DegP induction seems to require membrane anchoring of this protein. Structural changes and/or interaction of the CXXC motif with its environment may lead to activation of the Cpx stress response.
Subcellular Localization:
Cell outer membrane; Lipid-anchor.
Domain:
The mature protein has 2 domains, the N-terminus (residues 21-100) and the C-terminus (residues 126-236) joined by a flexible linker; both domains form beta-barrels. In the crystal structure of the soluble mutant (Ala-21) the N-terminus of 1 subunit interacts with the C-terminus of the other.
Sequence:
MVKKAIVTAMAVISLFTLMGCNNRAEVDTLSPAQAAELKPMPQSWRGVLPCADCEGIETSLFLEKDGTWVMNERYLGAREEPSSFASYGTWARTADKLVLTDSKGEKSYYRAKGDALEMLDREGNPIESQFNYTLEAAQSSLPMTPMTLRGMYFYMADAATFTDCATGKRFMVANNAELERSYLAARGHSEKPVLLSVEGHFTLEGNPDTGAPTKVLAPDTAGKFYPNQDCSSLGQ
The following text describes a protein:
Function:
DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for heterochromatin organization.
Subcellular Localization:
Nucleus.
Sequence:
MKRKDNKELICIPSSSPPSTPIREENYYLLTSSPIECSPIQQLDLSGSFKNYSTTSSRANGKKFGQLAMQSRIFFDTTDHKKYVESSYAAYDPHDQPPERDVSLKESSNKINPSNFFDSEQITKINAVKKRFPALDSEMIIATLEKFNWRENITIHKLTFQKLLGRGNSTINKSAQKLNNQPIEKSSVDKENAKRKRYVEEGTKQGQKKKPLRVIELSDEETNEDDLLGQSPTACTTDANIDNSIPENSDKIEEVSIESSGPSEVEDEMSEYDVRVLNFLNESTLQEIVEVSGCESKVVEYFISKRPFPSLEKAEALCQRNAHAATGKRKKSDGRNVGRKLVNSTYEVLQGFDAVDSLIAKCERYGAMISNTMRSWHNLFDDKKMEQFLNTSTGSISYEYNSQQPSSIASGITLKSYQIVGLNWLCLMYKAKLSGILADEMGLGKTCQVISFLASLKEKGIQNRHLVVVPSSTLGNWLREFEKFCPSLRVESYSGTQSERINKRYYLMDTDFDVLVTTYQLASGSRDDRSFLRKQRFDISIFDEGHYLKNRMSERYKHLMNIPANFRLLITGTPLQNNLKELISLLAFMLPKVFDNNMQGLDIIYKIKTTSDGDIERAYLSQERISRAKTIMNPFILRRRKENVLSDLPPKIQHVEYCHMEETQLSLYLSVLELKNLVNANRENILMQLRKAALHQLLFRSQYNLETLSLMSKRILREDAYLDANPQYIFEDMEVMSDFELHKLADQYRHLHPFALKGKPWMDSAKVKKLCSLLKKSRPNERILIFSQFTQVLDILEYVLNTLDLEFLRLDGSTPVETRQQLIDDFHTNENYKVFLLSTKSGGFGINLTCANIVILFDCSFNPFDDMQAEDRAHRVGQTRPVHVYRLITKNTIEENIRRLANTKLTLESSLTTDSEKIQKEISGELMKSLQMDGRVDTMDGSVV
The following text describes a protein:
Function:
May act in low affinity electroneutral exchange of protons for cations such as Na(+) or K(+) across membranes. May also exchange Li(+) and Cs(+) with a lower affinity.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein. Note=Tonoplast.
Sequence:
MVIGLSTMLEKTEALFASDHASVVSMNLFVALLCACIVLGHLLEETRWMNESITALIIGSCTGIVILLISGGKSSRILVFSEDLFFIYLLPPIIFNAGFQVKKKQFFRNFMTIMLFGAIGTLISFVIISFGAKHLFEKMNIGDLTIADYLAIGAIFSATDSVCTLQVLNQDETPLLYSLVFGEGVVNDATSVVLFNAIQRFDLTNINSAIALEFAGNFFYLFILSTALGVAAGLLSAFVIKKLYIGRHSTDREVALMMLLAYLSYMLAELFHLSSILTVFFCGIVMSHYTWHNVTDKSKVTTKHTFAAMSFLAEIFIFLYVGMDALDIEKWDVVRNSPGQSIGVSSILLGLILLGRAAFVFPLSFLSNLTKSSPDEKIDLKKQVTIWWAGLMRGAVSMALAYNQFTTSGHTKVLGNAIMITSTITVVLFSTVVFGLLTKPLVKHLQPSSKQSSTTALQITLRSSFHDPILHEPLLSTQGQSEYDPEQHVSFRMFWKSPSRFTH
The following text describes a protein:
Function:
Involved in a late step in sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins are targeted into the vacuole after fusion of the endosome with the vacuole. Regulates the recruitment of VPS4 to the ESCRT-III complex, probably in conjunction with DID2, and VPS4 catalyzes the disassembly of the ESCRT-III complex.
Miscellaneous:
MISCELLANEOUS: Present with 4760 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Endosome. Note=The endosomal location appears to be dependent on DID2.
Sequence:
MAPSMIPFTIKLKTCLKMCIQRLRYAQEKQQAIAKQSRRQVAQLLLTNKEQKAHYRVETLIHDDIHIELLEILELYCELLLARVQVINDISTEEQLVKEHMDDGINEAIRSLIYAILFVDEVKELSQLKDLMAWKINVEFVNGVIADHIDVPEKIIKKCSPSVPKEELVDLYLKEIAKTYDVPYSKLENSLSSSSSNISSDFSDPSGDIEDNDEEKPILALDNDDNDNADAKHPITVKKPRQNSENIKNELKIPKDIKKEVIEKKQSEKKTTKRKTKKEQENDELDELKKRFDALRRK
The following text describes a protein:
Function:
Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Binds to ERBB4 and ERBB3. Acts as a ligand for integrins and binds (via EGF domain) to integrins ITGAV:ITGB3 or ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and ERRB3 are essential for NRG1-ERBB signaling (By similarity). Induces the phosphorylation and activation of MAPK3/ERK1, MAPK1/ERK2 and AKT1, and ligand-dependent ERBB4 endocytosis is essential for the NRG1-mediated activation of these kinases in neurons.
Subcellular Localization:
[Pro-neuregulin-1, membrane-bound isoform]: Cell membrane; Single-pass type I membrane protein. Note=Does not seem to be active; [Neuregulin-1]: Secreted.
Domain:
The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization; ERBB receptor binding is elicited entirely by the EGF-like domain.
Sequence:
MSERKEGRGKGKGKKKDRGSRGKPGPAEGDPSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPENIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNEFITGMPASTETAYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLIKCAEKEKTFCVNGGECFTVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFYMTSRRKRQETEKPLERKLDHSLVKESKAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRQKLHDRLRQSLRSERSNLVNIANGPHHPNPPPENVQLVNQYVSKNVISSEHIVEREVETSFSTSHYTSTAHHSTTVTQTPSHSWSNGHTESVISESNSVIMMSSVENSRHSSPAGGPRGRLHGLGGPRDNSFLRHARETPDSYRDSPHSERYVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVSMPSVAVSPFVEEERPLLLVTPPRLREKKYDHHPQQLNSFHHNPAHQSTSLPPSPLRIVEDEEYETTQEYESVQEPVKKVTNSRRAKRTKPNGHIANRLEMDSNTSSVSSNSESETEDERVGEDTPFLGIQNPLAASLEVAPAFRLAESRTNPAGRFSTQEELQARLSSVIANQDPIAV
The following text describes a protein:
Function:
Exonuclease that cleaves single-stranded 3' overhangs of double-stranded RNA. Has no activity with 5' overhangs. Has negligible endonuclease activity. Can bind ATP, dATP and AMP (in vitro); the nucleotide occupies the predicted substrate binding site.
Miscellaneous:
MISCELLANEOUS: Member of the DEDD group of RNAses that are characterized by the presence of four acidic residues in the active site. These residues are conserved even when the proteins have highly divergent sequences. Has high structural similarity to RNase T despite very low sequence identity.
Sequence:
MRYFYDTEFIEDGHTIELISIGVVAEDGREYYAVSTEFDPERAGSWVRTHVLPKLPPPASQLWRSRQQIRLDLEEFLRIDGTDSIELWAWVGAYDHVALCQLWGPMTALPPTVPRFTRELRQLWEDRGCPRMPPRPRDVHDALVDARDQLRRFRLITSTDDAGRGAAR
The following text describes a protein:
Function:
Acts as a ventralizing factor during embryogenesis. Inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling.
Sequence:
QDTYRRRPKLNTIILNSQKSKSAGIKGTDHHAWKTYLSLFKKTIGKIATCLELRSAALQSTQSQEEFKLEDLKKLEPILKNILTYNKEFPFDVQPIPLRRILAPGEEENLEFEEDEEGGAGAGPPDSFSARVPGTLLPRLPSEPGMTLLTIRIEKIGLKDAGQCIDPYITVSVKDLNGIDLTPVQDTPVASRKEDTYVHFNVDIELQKHVEKLTKGAAIFFEFKHYKPKKRFTSTKCFAFMEMDEIKPGPIVIELYKKPTDFKRKKLQLLTKKPLYLHLHQSLHKE
The following text describes a protein:
Function:
Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells (By similarity). Plays a role in the early development of the nervous system and is required for proper patterning of the neuroectoderm during gastrulation. This involves the correct speciation of the neuroepithelial domain and adequate development of the non-neural ectoderm (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm.
Domain:
The C2H2-type zinc finger 5 is required for nuclear localization.
Sequence:
MATQMVNQSTGNSLFCTSTYSNISLDNDMYGLHDLSKADMAAPRLIMLANVALTGELSSGCCDYTPEGERQMAELTTVNDNSFSDSEGDRLEDSPSMDIQSHNFIMEMEPAECSKEGTSENDGTLLSNTLEVEVQKDKRTPSPTDDKYKCVKSKPFRCKPCQYKAESEEEFVHHIKIHSAKIYVDNDSNKKAQGNEADSSISEESDVSKGPIQCDRCGYNTNRFDHYLAHLKHHNKAGENERVYKCTICTYTTVSEYHWKKHLRNHYPRILYTCSQCSYFSDRKNNYIQHIRTHTGERPYQCILCPYSSSQKTHLTRHMRTHSGEKPFKCEQCSYVASNQHEVTRHARQVHNGPKPLTCPHCDYKTADRSNFKKHVELHVNPRQFLCPVCDYAASKKCNLQYHIKSRHSGCTNITMDVSKVKLRTKKGDIGVADVDANKQTENGNIIDKSVEETVKAEKRESCGKAKKSIVNLVDGQVAKKRRLSSTQKKIKTSDARPEKILDKSRKSSCVKRKSDLLENSNDTQTSTV
The following text describes a protein:
Function:
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Subcellular Localization:
Mitochondrion.
Sequence:
MNQLLNNLKFHKPFFKLNTAQIEILKDPVDFYVNLHKGIKNAQKRIVWSTLYIGNGNMEEFLIESLSNQQRRFEQLRISLLMDYYRGTRRDKKDHTTPLDHYLYLRMQNLYAQNMKLGLMRHPFLPQLANMFEESASREIFNVHHMKWYIFDNRVILTGANLQEQYFINRQDRYMVFHEANEIADYLDDAQSALLQHAYYVDFDSNSKFDPLRAQPFKRQQYFKEFHQTWKIFKFSYKEAAEIKSDDEEYKEQQQAKVQNKEEENDDTQQEQEEEELSQEEMLQFYEKDLIVEQKIQERKEQAKLILNKSFNKGDVQNIINRLEKALYKDEERELDEGEECTVLITLHIPYLQTDEDKLVFMRILEHLDQFTQVTWASGYMNFTKTIINFVNNCKTDIKFVTASPGANGFHKAGKAKSFIPLLYRNFELAINKPIFEYKKNGWTFHTKGFWAELQDGSTMTIIGSSNYAERSEKRDNEIQAYIFTQCPMFKQDLKKEQNQLFNYAEKITKEEILNDPEIKINWKIKLLSKIFKSMM
The following text describes a protein:
Function:
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Subcellular Localization:
Cytoplasm.
Domain:
Lacks the C-terminal regulatory region which is replaced by HisZ.
Sequence:
MLTLALPKGRLAEESIDLMISKGWLSSKPDPNSKELIYNDPKGKIRILLVRSQDVATYVEQCAADAGISGWDVLKEGGYDLATPLDLKIGKCRLSLAAPNGFTLEAHHRKIRVATKYPNLAREFFFLKGLSCEIFKLYGSIELAPLVGLSDCIVDLVSTGGTLKANGLKELDIILESSARLVFNRSSLYGKRKEAVEFMDSLSKI
The following text describes a protein:
Function:
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Sequence:
MRRAYRLRRPEQFRRVRQEGRTFTSPWLILTVAPARRRTLRCGFVVSRRVGGAVQRNRARRRVREAVRLLLPRLTAGYDMVFTIRTPEVIDAPFTQLQDDITALLRQACLLPAPTNETVSPVSDTPLPQHERGSQ
The following text describes a protein:
Function:
Involved in the breakdown of putrescine via hydrolysis of the gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate.
Sequence:
MSRLPLIGVTACTKQIGLHPYHIAGDKYLRAVVNGAGGLPLIIPALGESIDQAALLDSVDGLLFTGSPSNVEPRHYSGPASEPGTLHDSDRDATTLPLVRAAIDAGIPVLGICRGFQEMNVAFGGSLHQKVHEVGTFMDHREPADQPLEVQYAPRHAMHVQPGGVLAGIGLPSEFQVNSIHGQGVDRLAPGLRVEALAPDGLVEAISVEGAKAFALGVQWHPEWQVLTNPNYLAIFQAFGKACSKRAGQR
The following text describes a protein:
Function:
Cell surface receptor that plays important roles in innate and adaptive immunity by amplifying inflammatory responses. Upon activation by various ligands such as PGLYRP1, HMGB1 or HSP70, multimerizes and forms a complex with transmembrane adapter TYROBP/DAP12. In turn, initiates a SYK-mediated cascade of tyrosine phosphorylation, activating multiple downstream mediators such as BTK, MAPK1, MAPK3 or phospholipase C-gamma. This cascade promotes the neutrophil- and macrophage-mediated release of pro-inflammatory cytokines and/or chemokines, as well as their migration and thereby amplifies inflammatory responses that are triggered by bacterial and fungal infections. By also promoting the amplification of inflammatory signals that are initially triggered by Toll-like receptor (TLR) and NOD-like receptor engagement, plays a major role in the pathophysiology of acute and chronic inflammatory diseases of different etiologies including septic shock and atherosclerosis.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
TCSDKIWEIQAAAEVFEEKCTLAEGQTLKVSCPTNTNIYSNSQKAWQRLKDNGEVQTLAITEGSSQVRVGKYFLEDIPSEGMLQIQMANLQVEDSGLYRCVILGPSDPIILFHPVRLVVTKNSLGTPASDEYPCQVSVQNPTPLPVTTKLRPRPRPRPKPVTQPIPTSADRLSSPGFTVTPTNVTHVNRAPGISIIIPAACGLLSKTLVFIGLFAVTHRSFAS
The following text describes a protein:
Function:
The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MNPIWIPILKNSKIRMKNNEHHSENRGIPGMNQSGSVNTSQQRIPPQAVSSHTLKLKDFCHIFSTGELYNPEQLNYGVEAFEAYKNGCLSEDLKEEHRKVTEAELVIFQFPLYWYSMPAILKGWMDRVLVQGFAFNIPKGSGSGLLKNKKALLSFTTGGNQAMYTKEGISGDISYVLWPMQFGILQFCGFDVLAPQICFAPEYAPLEERRQMLTSWEKRLKTIWEEKPIPCILA
The following text describes a protein:
Function:
Reversibly inhibits the activity of ATP2A2/SERCA2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Binds preferentially to the ATP-bound E1 conformational form of ATP2A2 which predominates at low Ca(2+) concentrations during the diastolic phase of the cardiac cycle. Inhibits ATP2A2 Ca(2+) affinity by disrupting its allosteric activation by ATP. Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Sarcoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. Membrane; Single-pass membrane protein.
Sequence:
MEKVQYITRSALRRASTLEVNPQARQRLQELFVNFCLILICLLLICIIVMLL
The following text describes a protein:
Function:
Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MALIDPSFHPGPTLIVGDGNFSFSLCLAKALHENVDIYATSLDTKEQLETNEFALQNLQELSSFPNVKAFHGVDATKLEKQFKSLQFPRIIFNFPHTGGKVKISNCRKLLERFFICASNHLTPTTGVVCVSLCQGQGGTPCDVPQRDYGNTWKVVEQAAKAGLILMDVLPFRGSDYPIYNSAGFKGHLNKGFSTTRGLTHLFSHGTPLEPIPSVESFEDLSVNGSRKAAQHCLGSTHPVAKLKSKIENCLQHCDIPGTSINGFCKLKRIATTNKSDADNSYNKACCQDLSHLCQDIDCCQTDDNFDGTLFKDLPSAIQYCLKAQHSPFVISGTETDFNVPVTSCTYPITHKMVICRTRPKESELNEELDLAQKFITNKICPTLTLSEDQISCQKSPGLDFNKTQMSSFKPSDYHALRKRRRELFEWRPSGDQVNKVWIPSDVCCKDENNLCTSCTLETNYFKCSDKIENLVTTESKRELCSNGLLVISCGILSAKDGINAGWLIIVHLDALLMALHNIPDIRLLWSKEEKFLGQPFGQEDQYTPFNLYPPVFLHDISFWLSNDSTEKAFLETIFHTTQNCVCDVWFRERYRDPVSGAISYNYRMMYSRCDGALSHMQTVEIQNLLRRVLMKKKFILS
The following text describes a protein:
Function:
Putative transcription factor.
Subcellular Localization:
Nucleus.
Domain:
The homeodomain differs form the typical one by having namely 4 instead of 3 extra amino acids inserted in the loop between helix 1 and helix 2.
Sequence:
MSSLSKPNRQFLSPTTNNQDTGREQTIACARDMVVLYNECLKNHAVSLGGHALDGCGEFTPKSTTILTDPPSLRCDACGCHRNFHRRSPSDGFSQHRSPPSPLQLQPLAPVPNLLLSLSSGFFGPSDQEVKNKFTVERDVRKTAMIKKHKRTKFTAEQKVKMRGFAERAGWKINGWDEKWVREFCSEVGIERKVLKVWIHNNKYFNNGRSRDTTSSMSLNLKL
The following text describes a protein:
Function:
Responsible for addition of the terminal mannose residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. Implicated in late Golgi modifications (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MKFHLKRYVIVTSILLSFFLLFRRQFLPLTQRQPNPINNELVSFDLIKQRNKFENPIYAKWKLSSSSPLETDLTTRCNDYFQQLLTQENFQINYHDSGYKTEPFVYKRKKWLKERIRSLRKQYKFDKNKDKYDFDQIAKQEFSIVSKNQSIHELNIYQHFSHTRIFGKCFATNNNNNNNNGVINMENPQSNQLCKSFVQKLYPWMSGNLPIFERNKERSPPQLDDSTDCIIEQIYKNSKGKGKGIIIPLMTQDKSNNQIQNIGRLIKVLRGLNNTLPIEITFMELITPEAKQQLYDIATSDSQMYPTKQDIAFVDLSPTTTNQVKGSISDSSIITLSSIFTSFEEFIILNQHIIPLIELTKFFNNERYKLHGTYFFKSPSKLKYRTTKFNIGFHEIASFIKNQLIPNKFDKHYFNLYQKGSENGDEVTIDRFFNYQFNNLIDSSLIIFNKSKTLSGLLISGNFEFLYHDDLFNIRINNTPTKTKMDYLWLGQYISGINEQIIFNFNYAIMPGILTPSQNLPKDSIECLEICSSSWGQLSDIDDISLLYITSHQLQNWLNHQKFFESLLKDKYEFKFNELVDNFLITNTNTNTNTNTNTNGNTNDKDSTKLTMGRIDLSIFEKIKTQPLKIETIIRPPTLIEPINVLGYNEPDQAWVHQDDFDRIGQNGQGQGQGQGHPFYCVYSSIGDPLKEGIRGLSINVEQSLQKKYKKLIEIWLQD