lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Protein phosphatase that negatively regulates the G1-to-S phase transition to inhibit the cell cycle and establish quiescence in cells of multiple lineages including vulval, hypodermal and intestinal. Promotes nuclear accumulation and activity of the cyclin-dependent kinase inhibitor cki-1 which leads to inhibition of G1 progression during vulval tissue development. Has been shown to not be required for cytokinesis. However, in the embryo, in a contrasting study, has been shown to act as a regulator of central spindle formation and cytokinesis, and may be required for localization of the spindle component zen-4, and its interacting partner air-2 at the spindle during late cell divisions; [Isoform c]: Main regulator of cell cycle arrest in vulval precursor cells.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Midbody. Nucleus. Note=Localizes to the cytoplasm throughout interphase. As cells enter prophase, accumulates at the centrosomes. During metaphase and anaphase, localizes to the spindle, in particular spindle asters and the spindle mid zone. During late telophase, localizes to cytoplasmic aggregates. In some studies, localizes to the midbody during late telophase. Localizes to the cytoplasm in G1-arrested cells. Localizes to the nucleus or nucleolus in postmitotic cells. Some studies report no localization to centrosomes or nuclei. Co-localizes with zen-4 at the spindle, and localization may be dependent on each other; [Isoform c]: Cytoplasm. Nucleus. Note=Localizes to the cytoplasm during interphase, but localizes to the nucleus during cell cycle arrest.
Sequence:
MREDHSPRRNNTIENTLTELLPNRLYFGCFPNPDAIDKSDKSVKKTCFININNKFHYEPFYEDFGPWNLSVLYRLCVQVGKLLEVEEKRSRRVVLFCQDDGTGQYDKIRVNTAYVLGAYLIIYQGFSADDAYLKVSSGETVKFVGFRDASMGSPQYLLHLHDVLRGIEKALKFGWLDFSDFDYEEYEFYERVENGDFNWIIPGKILSFCGPHNESREENGYPYHAPDVYFDYFRENKVSTIVRLNAKNYDASKFTKAGFDHVDLFFIDGSTPSDEIMLKFIKVVDNTKGGVAVHCKAGLGRTGTLIACWMMKEYGLTAGECMGWLRVCRPGSVIGPQQPYLIEKQKFCWSLSQSNGVHLTQNKEEKRNVRRLVNQVDDINLGEERISPKSRENTRPNILRRRVQVQNGRSTAPVTIAPAGTSESRRSTKPSRVVDETALDDQGRSQGDRLLQLKAKHQHESETTSPNSSSSRRFVKSSTPQMTVPSQAYLNRNREPIIVTPSKNGTSSGTSSRQLKTTPNGNVAYRTRNSSGNTTSTLTRTGNESYRFHNSLFYEPASAVFPSMASRRSETTRYLSPTTPIKPMSPSYTDGTSPRYKARLRSENPIGSTTSTPFSLQPQITKCSLTAESKPPKRILSMPGTSKSTSSLKKIQVSRPRPYPSTGVRVELCANGKSYDIRPRKEAHVIPGAGLAANTEALLGVCKLVNTLS
The following text describes a protein:
Function:
Modulates isoactin dynamics to regulate the morphological alterations required for cell growth and motility. Interaction with ARF6 may modulate cell shape and motility after injury. May be involved in multiple neurite formation; Regulates APAF1 expression and plays an important role in the regulation of stress-induced apoptosis. Promotes apoptosis by regulating three pathways, apoptosome up-regulation, LGALS3/galectin-3 down-regulation and NF-kappa-B inactivation. Regulates the redistribution of APAF1 into the nucleus after proapoptotic stress. Down-regulates the expression of LGALS3 by inhibiting NFKB1.
Subcellular Localization:
Cytoplasm, cytoskeleton. Nucleus.
Sequence:
MMNCWFSCAPKNRHAADWNKYDDRLMKAAERGDVEKVSSILAKKGVSPGKLDVEGRSALHVVASKGNLECLNAILVHGVDITTSDTAGRNALHLAAKYGHALCLQKLLQYNCPTEHVDLQGRTALHDAAMADCPSSIQLLCDHGALVNAKDVDGRTPLVLATQMCRPTICQLLIDRGADINSRDKQNRTALMLGCEYGCKDAVEILIKNGADVSLLDALGHDSSYYARIGDNLDILTLLKTASENTNKGKELWKKGPSLQQRNLTHMLDEVNMKPNQREHQNIQDLEIENEDLKERLRKIQQEQRILLDKVNGLQLQLNEEVMVADDLESEKEKLKSLLAAKEKQHEESLRTIEALKNRFKYFESDHLGSGSHFSNRKEDMLLKQGQMYVTDTQCTSPGMPAHMQSRSMLRPLELSFPNQTSYSENEILKKELEAMRTFCDSAKQDRLKLQNELAHKVAECKALALECERVKEDSDEQIKQLEDALKDVQKRMYESEGKVKQMQTHFLALKEHLTSEAATGSHRLTEELKDQLRDMKAKYEGASAEVGKLRNQIKQNEMLVEEFKRDEGKLIEENKRLQKEFSMCEMEREKKGRKVAEMEGQLKELLAKLALSIPTEKFENMKSLLSNEVNEKAKKLVEMEREYEKSHGEIRQLKRELENSKAKFAQHVKPEEHEQLKSRLEQKSGELGKKITDLTSKNQELQKEIEKVYLDNKLLTQQVHNLTMEMKNHYVPLKVSEEMKKSHDAIVDDLNKKLLDVTQKYTEKKLGMEKLLVENDSLSKNVSHLETVFVPPEKHEKEIMALKSNIVELKKQLSELNKKCGEDQEKIDSLMSENTNLKKTMSHQHVPVKTHEEMKTTLSSTLDKTNRELLDVKKKFEDINREFVKIKDENEILKRNLENTQNQIKAEYISLKEHEEKMSTVGESLKKVQANSAEMLANYQKGQEEIVTLHAEIEAQKKELDTIHECIKLKYAPIVSFEECERKFKATEKELKEQLSEQTQKCNVREEEARKCKQENDKLKKEISTLQKDLKDKSALIENSHEMERALSRKTEELNKQLKDLLQKYTEVKNEREKLVEENAKQTSEILAAQTLLQKQHVPLEQVEALEKSLNGTIETLKEELKNKQRCYEKEQQTVTKLQQMLENQKNSSVPLSEHLQIKEAFEKEVGVIKASLREKEEESQNKTEEVSKLQSEVQNTKQALKKLETREVVDLSKYKATKSDLETQVSNLNEKLANLNRKYEEVCEEVLHAKKKELSAKDEKELLHFSIEQEIKDQQERCDKSLTTITELQRRIQESARQIEDKDNKITELLNDVERLKQALNGLSQLTYTSGSPSKRQSQLIDALQHQVQTLQQQLADADRQHQEVIAIYRTHLLSAAQGHMDEDVQAALLQIIQMRQGLVC
The following text describes a protein:
Function:
Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
Domain:
Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Sequence:
MLDTQTIAIVKSTIPLLAATGPKLTAHFYERMFKHHPELKNIFNMSNQSSGDQREALFNAICAYATNIENLAALLPTVERIAQKHTSLNIQPEHYPIVGEHLIATLDELFSPGQAVLDAWAKAYGVLADVFIQRESQIYQQSETETGGWRTLRRFRIIKKEQQSEVICSFVLAPEDGGQVLHYKPGQYLGIYIEHESLEFQEIRQYSLTTAPNGKTYRIAVKREEQGTVSNLLHRELNEGDIVRIAPPRGDFFLDVSPDTPVALISAGVGQTPMLSMLNTLYSQQHAAPVHWLHAAENGRVHAFADEVSAIAAKMPNLSRHVWYREPDLQDKHGEDYHSQGLMDLSSYQWLADDPKRHYYFCGPLPFMQFIGRQLLAQGIAPEQIHYECFGPHKVI
The following text describes a protein:
Function:
Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. The N-terminal SNAG domain competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4' (in vitro). During EMT, involved with LOXL2 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (By similarity). Associates with EGR1 and SP1 to mediate tetradecanoyl phorbol acetate (TPA)-induced up-regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3. In addition, may also activate the CDKN2B promoter by itself.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Once phosphorylated (probably on Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus to the cytoplasm where subsequent phosphorylation of the destruction motif and ubiquitination involving BTRC occurs.
Sequence:
MPRSFLVRKPSDPNRKPNYSELQDSNPEFTFQQPYDQAHLLAAIPPPEILNPTASLPMLIWDSVLAPQAQPIAWASLRLQESPRVAELTSLSDEDSGKGSQPPSPPSPAPSSFSSTSVSSLEAEAYAAFPGLGQVPKQLAQLSEAKDLQARKAFNCKYCNKEYLSLGALKMHIRSHTLPCVCGTCGKAFSRPWLLQGHVRTHTGEKPFSCPHCSRAFADRSNLRAHLQTHSDVKKYQCQACARTFSRMSLLHKHQESGCSGCPR
The following text describes a protein:
Function:
Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of chromosome segregation and cytokinesis. The CPC complex has essential functions at the centromere in ensuring correct chromosome condensation, alignment and segregation. In the complex, required to direct the Aurora B/air-2 kinase to chromosomes. Also functions in spindle midzone formation and in the formation of polar bodies during oogenesis. Required for the localization of the kinetochore component hcp-1 to chromosomes. Involved in the positive regulation of transcription. Involved in the transcriptional regulation of collagen genes.
Subcellular Localization:
Chromosome. Cytoplasm, cytoskeleton, spindle. Midbody. Note=In mitosis and meiosis, localizes to chromosomes during prometaphase and metaphase, localizes to both chromosomes and the spindle midzone during anaphase and disappears from chromosomes during telophase but remains at the spindle midzone. Persists at the cytokinetic remnant during cytokinesis. Also localizes to the chromosome of polar bodies during oogenesis.
Sequence:
MAPGTKKKSDMAKFTFYKDRLMTFKNFEYDRDPDAKCTSQAVAQAGFYCTGPQSGKCAFCNKELDFDPEDDPWYEHTKRDEPCEFVRIGKLDDSELTINDTVRLSQTAMIMTKLFEHEMMINNLSNHSSSDALFDQLKKVPNTASTTKSNSRRGK
The following text describes a protein:
Function:
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex that mediates the vacuolar degradative transport via the intracellular vesicle trafficking from the endosome to the vacuole.
Subcellular Localization:
Cytoplasm. Endosome.
Sequence:
MADSRDDLAESLQNLFTSVSSMVKSELQGTNNHLDLLEKMNLRVASEYDDMGDVAAGLRVFAEQMKSKSGGLDEFVGQMDAIEKQVSEFEAVISVLDRYVSVLESKIRAEYRHPHHQRRSNDSVVTD
The following text describes a protein:
Function:
Acts as a guanine nucleotide exchange factor (GEF) for RhoA GTPases.
Sequence:
MAEGSAERKVRMYRSVSFKRLENWNAKGFVLEGGTKLPGERDVTQPTCQKAHRPSRSLSLSRKVSKISAASKDQTSPSVRQLSQRFSSQPRDEGAQCGEENPHLNKECQEEQTLDLPCHQDQHGQDPLTVTVCDGSGKSDDLLAYVNPRASKSSGTLLDELTLNSYYSLLNQPENREIIGFEGNWPSVTEMRKLFGENSRKPNVRASSLPDYDEPRLSNQQFSYLRDATDSHRPCPVESAFPKGFNHCAADLRPKHPTLKIENSHSRNLVDSKPDINSILCMDTKDHRTNSGPKPQPPTPPPRSCIPFGLKAHTLSSGVPKQEARQQSVSLHSLHSSGKPQTAPSNVRLRFSSSEEELHSKALQLPSSPNKNEFQDRSQEVSSGSEEESNRVTLRESLRNRSFRKKKRDLEEGKSDLSGESNAKHVISDEVGQDANHSGYPLHGANIYETTSASPVSAGKMGVNAAANKPSPNLSRGISNEFPRQHLRGISEGLSPSTACHLSAASPMPTVSRVAKVNIPPFLPSPCGSRSSSRYSSTETLKEDDPFNAYSSGQSRQGGFNIYRSPSFGHNDNVRQQARSRLRVAPNVTKLKSENVHEVSSCDPESENSKYTKSMSNPDIASETLNLLSFLKSDISDLKIRNRIRECTDGDGVTARNESTHGSGGQETWVSKGRSASQSMSNSQQGNRPTLKDLTATLRRTKSFTYSEKLGSRRRVGHGSMKQSSSELSLASTGDEALLSNSKANEDGAKQGEDAASALSQDQYIQEARQVFEKISQIGSQDDYSFDQEVSTHIENKMAKGLPLDCTSHSLEKKSNTFIEKLEENMSLEELSHHEYAMTDEGIVTEVETTSGDTLYQDLGQTLTVWKSADKIQGEAHPFTVHNGEIQQSPSAVKTSFEIDSCCDVVANTCSSQVPLDTPPTPGTMRRRRKFPSLSNTGSDSSNGSSGESGSETYRSLSDPMPHRTYSITEDSKAFSVDSNLLGSLNSKTGNSESSTIAFSECTGSAASVLSFSSDGVKDYNTVIQNIVSQPGALDKVIDEKGNGKTIKKKSFSDPSRRGELSPTGLENSTEPINELSSSSEPILTEQRDESGEVEDAEEVVGRVRSQSECVLPHAEDDSGVEGNQNFSFDPKLAEVLSPRTLRRSSKKRTNRVGSQDGQQECNKPTEAFGKSRVSSKHVRHTSEPSTFIPIVSAEAKSSSHPVVKLTIPESAKLPVKPLPSLICPQLEDVSKKGTRVTGDNNMPSVGDLPRTAPSTPTTAEPKLLRLHKPHEDLTPGNRSKPYVDMRKHVFLTLLDTEHSYVESLRTLMESYMKPLKLPENSFLCDPSLVDEIFDQIPELLEHHEQFLEQVNQCVQNWGEIQTVGDVLVQSFSKEILVSIYSAYIDNFLNAKDAVRAAKEARPAFIKFLEQCTRENKEKQALSDLMIKPVQRIPRYELIVKDLLKHTPEDHPDHLCLIDAQINIKQLAERINRGMRSAEETERDIRILQEIESHIEGMEDLQAPFRRFVRQEMVVEVKAVGGKKERSLFLFTDLLICTTLKRKSGSLRRSSMSLYTAASVIDISSKYKLLWKLPLEDVDIVKGTSQASNRDSVQKIISRLDEDLSTMGQISKLSETLSFPHQSLDDVIKDMMASVHRELAEKQSLSFTMSFPPNKVELTTTKADGTESFIFEFSNPEARLHFEQGFEETKKKLVSSKNRLDPEFLKAIPIMKTRSGMQFSCASPSPPSHSCLENVHEVWVCNSDGYVGQVCLLSIKNEPSVEACIAVCSARILCVASVPGLKKNHRDRPVAMGSQSSETQSQSQEETVSQQCLHISISGSSLELSETTDSASRDLVPFDSDDTDDESSPSPSGTLQSQASRSTISSSFAEEMPSAKDTTTETTSSEEEQETSFLPIPGAFNQNRDNESPTEGQPLRRSSRSSFTRGSLEDLLSLDPEAYHSSMWLGTEDGCIHIYQSSDNIRNRKNSMKMQHSAAVMCILYLDNQVFVSLANGELIVYQREAGSFWDPQNSKSLPLGSPGGPVTKMVSVSGKLWCGCQNRVTVFNTSSLLQEHCFLIGQDQNRSVTCMVSSSAGMWISLQGSAQVRLYHSTSFEQLAEVDIAPPVHKMLAGSDAIIRQHKSACLRITALLACKDLLWIGTSAGVLLTLSFASTTSNSLKGQLSPVGLSQGHTGHVRFLTSVELPEGFDVLFPLSDQGNDQTSELERRDPARYHRPSPMTPPKSKILVISGGDGYEDFRLTSSSETVGRDDSTNHLLLWRV
The following text describes a protein:
Function:
Involved in the digestion of the blood meal.
Subcellular Localization:
Secreted.
Sequence:
MMKAPVVLLLFSTVFLAYAAAYKRFDNYKLVEVVPTSDDQLNFLKDLARDYVHIDFWRPPSFLHVKTTMMMSAETFDDFEKFVDYTLMPYEVVNHNLQQLVEEEQLAMNLARSNVGDADSYMDLNTFNNLTKIYDWLDTLPAKCPKTHTCQVYSVGESYQKTPIKAFKIMKPGSNRKSWYLDATTHAREWITTATILKIIDHLVLGKNADAKELIEKYDFYFIPIVNPDGYNFTFLENRMWRKNRRPTKAGCFGVDLNRNFAATNWGKEGSSSSECSETYKGPSAGSEPETTVVSNELKRIASHTIVMLTMHSYGNMYMLPFGNTINYTGKVCERSKDHDELMVGLNKMADATQATYNTKWLRGNGCEVIYPTTGSTDDYTKDKLAIKYSICAELRGKSFVILPSEIEPSFREVFNGIVALSRSIKY
The following text describes a protein:
Function:
Chloride channel gated by pH that facilitates the entry of chloride ions into cells upon exposure to extracellular acidic pH. Involved in acidosis-induced cell death by mediating chloride influx and subsequent cell swelling.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MIRQDLSTSYQELSEELEQVVENSEQADERDKELVQVQGPGVVPGVDNESASSSIRFSKACLKNVFSVLLILIYLLLMAVAVFLVYQTITDFREKLKHPVMSVSYKEVDRYDAPGIALYPGQAQLLSCKHHYEVIPPLASPGQPGDRNCTTQRINYTHPFSNHTMQSALIVQGPQEVKKRELVFLQFRLNQSDEDFSAIDYLLFSSFREFMQSPDKAGFMQACESAYSSWKFSGGFRTWVKMSLVKTKEEDGREAVEFRQETSVVNYIDQRPAAEKSTQLFFVVFEWKDPFIQKVQDIITANPWNTIALLCGAFLALFKAAEFAKLSVKWMIKIRKRYLKRRGQATNHIS
The following text describes a protein:
Function:
Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization.
Sequence:
MSCCFSKKLFGRRSKREDRYKVSEDAVPKPEEGGEPPKYSWDRREKVNAEDFTIANIHNTTLKKESKDGGPLQMENCTDSTILYLYQTSQVIIDDCRHCTIVLGPAAGSVFVRDCANCTIFTSCQQLRTRDCTSIRISILCPTEPIVENSSDIHFFHLAMRYPELKDQMHAVGLRPFTNRIASVHDFTPAGVNGKGNFRVTPEVVQISDGQEEILRAKGVILKPSPADFIPRFTDTTDPDPTFLYVLGKSEPVDELGDRAIELLHAIYKSGMQVMGTCDLETSTVDSKLVPFAGQAERMILFQLKGNLANLECDVEFDVMSENDLVPLRNLLIHLEGKKNG
The following text describes a protein:
Function:
High-affinity zinc transport protein. Regulates intracellular zinc levels.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSLNNLSNSYNQYLAQESHQILRHLFLNKQYSPLVKRDDDSSATVTCGGDANEFNEYGHLGYRIGAIFVILATSLIGMNLPLVLSKITKNRPNVYIEYLYLFARYFGSGVILATAFIHLLAPACNKLYDPCLDDLFGGYDWAPGICLISCWFILLLEVLLNRYVEWRFGMEIGDHHGPTLGAKQHSHSHEDGAHGVHEHPVYDIEECADGVEHECVKDDLEEVKLEPYTNTDSTDLTTKEEARSFLLKQQLTAFIILESSIILHSVIIGLTTAVSGEEFKTLFPVIIFHQAFEGCGLGSRLAGMAWGPKTAWVPWVLGVIYSLVTPIGMAAGLGVREHWDPLAHGSYAAQGVLDAISSGILVYAGLVELLAHDFLFSPERERNWYKLIYLLACSMAGTGVMALLGKWA
The following text describes a protein:
Function:
After the onset of mitosis, forms a ring-like structure which colocalizes with the medial actin ring. Appears to mediate cytoskeletal rearrangements required for cytokinesis. Essential for viability.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Domain:
The N-terminal region is in a coiled coil structure.
Sequence:
MEVNGVSQSEAAPYVTKSSVKFRDNFWGSEDAGMDALMSRTKSSLSVLESIDEFYAKRASIEREYASKLQELAASSADIPEVGSTLNNILSMRTETGSMAKAHEEVSQQINTELRNKIREYIDQTEQQKVVAANAIEELYQKKTALEIDLSEKKDAYEYSCNKLNSYMRQTKKMTGRELDKYNLKIRQAALAVKKMDAEYRETNELLLTVTREWIDRWTEVCDAFQHIEEYRLEFLKTNMWAYANIISTACVKDDESCEKIRLTLENTNIDEDITQMIQNEGTGTTIPPLPEFNDYFKENGLNYDIDQLISKAPSYPYSSSRPSASASLASSPTRSAFRPKTSETVSSEVVSSPPTSPLHSPVKPVSNEQVEQVTEVELSIPVPSIQEAESQKPVLTGSSMRRPSVTSPTFEVAARPLTSMDVRSSHNAETEVQAIPAATDISPEVKEGKNSENAITKDNDDIILSSQLQPTATGSRSSRLSFSRHGHGSQTSLGSIKRKSIMERMGRPTSPFMGSSFSNMGSRSTSPTKEGFASNQHATGASVQSDELEDIDPRANVVLNVGPNMLSVGEAPVESTSKEEDKDVPDPIANAMAELSSSMRRRQSTSVDDEAPVSLSKTSSSTRLNGLGYHSRNTSIASDIDGVPKKSTLGAPPAAHTSAQMQRMSNSFASQTKQVFGEQRTENSARESLRHSRSNMSRSPSPMLSRRSSTLRPSFERSASSLSVRQSDVVSPAPSTRARGQSVSGQQRPSSSMSLYGEYNKSQPQLSMQRSVSPNPLGPNRRSSSVLQSQKSTSSNTSNRNNGGYSGSRPSSEMGHRYGSMSGRSMRQVSQRSTSRARSPEPTNRNSVQSKNVDPRATFTAEGEPILGYVIALYDYQAQIPEEISFQKGDTLMVLRTQEDGWWDGEIINVPNSKRGLFPSNFVQTV
The following text describes a protein:
Function:
Rho GTPase-activating protein involved in the signal transduction pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MKSIFRKSVQIFKDKKDKDGVYINNSGGNNDGNGSNNGKSSPSSSLSKKDKKNKHGNNIANTDFNNEYNQGYHNGSISSNHSGQSPTLTREDSISSYNSDSTTISAASSPPIFIHNPNARKVFGVPLSQVPCRPGSNVPIIIERLVDHIEKTSLTTEGLFRIPGREVTINQYINLYNNGEDVDVSPIEPYTAAGLLKRFFRDLPVFVPQSINRRVASLFVSEDGKKKPFDMEILGNLRILVHQLPTVHFEVMQALTGLLAKIMSKSDENKMTISNIAICLVPTLNCVPAIVTYPIQYFNFFFNEIFQEHHIYHMRPYQTNLISTAIEERLEHLSHLSTQPMLIPNNNNSDVQKRYSRPASITISGLLPTQNQSPSSSTITSTTITSPHDSTTPITFTVTTTFSPQDQQNGSPSQIHQHAQQQLESGSGNQQPTNTSTNAATTTSNRDRRTYKIDPNEYAQFLEETQYNINKNYLHGGNTSNNLSQSSSNISPSTTITNNNTNNNNNNNNNINNSYGSNSSETNKLYRRSVAYTGGNIETKAAIQQIKEKIDRYSKEKKTREDKEREKLLRYSIDLERYKDRYNKEKRSSRDINKEIEREIEKRLSPRERLNLLLASNNGTMNLSSSVNSTLNRSSISGLSSLMNSANINDTSSNSGSNRRMSITQQLQMQLQQLQQQQQAYQQQQQSTTPMGLNNNTTTTSTTTNSNRYSSNRYKAVGDLASSSSSFRYSREIYDDDYYSNNNMMFNNNFNDNMSSISGSSASAFSRQRSQSCFEPESLIQQLTLQQQQYQQQQQQQSYQQPYQMNPQYSNAFIEQKLDQIRDTINNLHRDNRVSRDYTHYLREVEDLRETLQKETVTTEFFANKNQELEDKLRREEEKNKRLVEEIQLLESYFVLKEKSKLSKRLSTRSRSPTLHGSFNHNNDPLNSSSNSIHSYVSNNVNLNQQQTLNNPNNN
The following text describes a protein:
Function:
Plays a continuous role in plant development probably in the structural organization of compartments.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MKCYKSSSILSTNHHPFFYKQQPISSLQPTSIPTTISYPTRTRFSSTRIQSRLTHDDPVKQSEDLSFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEYTDRFIRVQEAYETLSDPRRRVLYDRDLSMGFSFSFSGRRQNRYDQEVVEEKSEWKAKWQTQLSGLRRRSNQKDNNTMSWAARMRRQQQESS
The following text describes a protein:
Function:
Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme (By similarity).
Subcellular Localization:
Mitochondrion.
Domain:
Forms an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 74-106, leaving each N-terminal inhibitory region (residues 26-52) accessible for interaction with an F1 catalytic domain. The inhibitory N-terminal region (residues 26-52) binds the alpha(ADP-bound)-beta(ADP-bound) (ATP5F1A-ATP5F1B) interface of F1-ATPase, and also contact the central gamma subunit (ATP5F1C). This dimeric state is favored by pH values below 7.0, and at higher values the dimers associate to form inactive homotetramer, where the inhibitory region is occluded, masking its inhibitory activity (By similarity).
Sequence:
MAVTALAARTWLGVWGVRTMQARGFGSDQSENVDRGAGSIREAGGAFGKREQAEEERYFRAQSREQLAALKKHHEEEIVHHKKEIERLQKEIERHKQKIKMLKHDD
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular Localization:
Nucleus.
Sequence:
MPSKHAKKLACEIVVDQFGEQVGKVCQTLVFKGQHSLPDLGRVTELTPPQLRNCVLVLSQHNCVQAYRVEPDAENPRTRPQVLYVALVSRILQRLRFPRMLLHVKEELGPDAEAVLEGLIEHGRLSVGQLVERASARTEDEAERSAQSEGVKEAFKQLVQARYVEKAPQAEPVLPPASEGDTKKGTRINARARAAAAKASVVESEEARAVRLSAVSDFDRFRLPSSVLGLENGAPTAAETKALSRTKRKREAELAEQAAQAAKQKADEEELVWRVNYDEFTRRFRHEAMSEFVEERMGPTAGAAVRTMLTETRGQEQSVAEKASGPVSVEAIHTILRSSPAGSALPKSSIRTALEQLAEEGSAMVTKENELGGGTYAVDMAHVVAEMRERELESVVRNRFGQGACRIFRLLRMKRMLEQKQIGEMAMIPIKDTRQLLYTLLKGHYVSLQELAKTADHVASRTFYLWRVNIPQVSEHALDEMYHGASNLRNRLQHELAQEKELLSICDDMAAGNAAGEHGSHVTLTSAQRERLEQFRQVAAVLESSLLALEKMIMLFSDF
The following text describes a protein:
Function:
Has antibacterial activity.
Subcellular Localization:
Secreted.
Sequence:
MRVLFLIFGVLYLLSTVPPARSFIYIDECPSEYYNCRMKCNADEHAIRYCDDWTICCKLKNIEIDEK
The following text describes a protein:
Function:
Has a role in a nucleosome assembly pathway that is required for the integrity of heterochromatin and proper chromosome segregation.
Subcellular Localization:
Nucleus.
Sequence:
MASFTALNIEPDDQSYDEIDNTREIQIEDALKLYTAALKLHAQGLPYYPEAAEAYKNLFQSEIFSYPEAVTEFTRLEEHPELEYVDSTIPTELDIGPAAVDGTPSTLPQILYLAHKNHGQFILDCVKARLRHSHGLMDDIGHRAALESQAKVSMDDFGRALVSDESDTELWRRAARIGAMLGSRRISRYCLEAAVEVDDDPTIAEVEPQSLEEGFAGEQLKSLLQLMSDELSLSHPIMGPFKKKTMPQFLKKHIDPYPFLPNPTSTMSRSIDFDEPLQILEGRAIINVPERSWTSIGHEICGAAQALPVVGVILALPPGEDQPFSPEPQHLESQQANDTVMAISPVAESFGNGTPTTNNSDERAGEVTSAATTKSSDAALPTRKRSQSAAGLRDTPEEDNSTHKRSRRIRNRESTAETPIDPTTQYAEQLKTFARADDDVFTFVGNMLQKLGVEDLGTREDLQVALAVDTATESNEIRNNTAVRDLRDIMKSWDDVKATVFETANAADILGASGGNANAGMSAFLEHSGSISQKVANKPPPFAEFGGISWFAQRVEKDWMPLQDVVFEWLRIVLATYLQRQWSAELKVAVVRMTSFLDADIYDRVRSELELSRSSGENSTQISELEEMVETIFELHLDVYSRITNADSMVGMDIRIMTKDRLDRWANFAAFVMRSRQHERDDELSLRYLWASVFYATVPGESSREHKVFLWTNLRDILNEAGKPPILLTNNAVIAEISTSAADREVSSLTTMEFFQNLFQPGRSDPLAIIQTLEPVLDPEATSQSAVMEIADSQDSEFSKNGENTPTILRDMWKFLDCGSTPLRLFLWQRLSEAYASIEYKTKVFSCSLKCIEILVAEFRSQDYLNCDDETRRQKMLVSFKALDHLLVPALTTALNEATTCFEIIDDRHVRSTCAALAQLSRILHAAAVFDDEMRVGSISLPQNGAYSAFGSFSNFANKLKEMQVRTWALQYAIVKEATAQNRDLFPTPDNDLADFLALVHYSLGLRKCCKASNKIFLKMMKQEMSRLKHIDKWEDYLGQVLFDLYGIKLGVGTFLLEDHGCPIESLDRRTVMNIAEQVISLANNMPMKDLMKHELKPTIEKMQTAVGQPKETPTMLHNSRNISEYLKTPIRPLDLYLAMRGESEIDSISVRTPESPLADKGWYYLLGMLALTKYRSTKRVSAGSQTDDLRFAAHFMKLQLQYTVDHWEAWYRLAQCYDLELEEEVLWSADKMNNDRPLLVRLQKCSIHCYIMALSTAMRCADGSFGTAEKLSEMYYDFGMRLYASSREPFSMEVFWVDEEKHMSGTEGMYKKMPFEEMSKYKLWRYASELFKRSLADRPDFWMNHFMLGKCQWKMVASAREEWSDKPPTNVPTMDMVLSAFVRAIETCPKPSKSSQEPILEPHYKLVSLVHKLVARGEMEFKDAAKILQDQPYGPRKGDPFVIESDEDWEIFILACFRQLRNADKPHWHHRMIARVANILYDEAKPDYVQACAARIEFRESIFTKAMSMQVWKPEVERPGRHFVYMRRYAIFMARLLFLINDKANMELLAKRVRKRAVDYYKFSDVWSECCTIYLRLIRKAANIPANVDEVFRGISQEGWDAYSQRIEDSIKDGSLSHPALDALRETIELKRLNNGLAKITPIDDMINDIWAVLYIQIVRDTPAIDVSALQQSQIDGEATARASGPMNLNHILTNTETNVSTSIPAVEPPRSRKLGINRKAVILRAEQSINRTAEAPRPVAGSRPRNAASSSVLPSNASPLIASAPRIEIPSTAPQQSTRREDSSAPGSVHDSADDESDLSDVPDMDDLDGSLIFPNLMRRNESGSGRHSPAPGNNG
The following text describes a protein:
Function:
Catalyzes an early step in riboflavin biosynthesis, the NAD(P)H-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate. The beta anomer is the authentic substrate, and the alpha anomer can serve as substrate subsequent to spontaneous anomerization. NADPH and NADH function equally well as the reductants. Does not catalyze the reduction of 5-amino-6-(5-phospho-D-ribosylamino)uracil to 5-amino-6-(5-phospho-D-ribitylamino)uracil.
Miscellaneous:
MISCELLANEOUS: The protein sequence in PubMed:16730025 comes from protein expressed and processed in E.coli; MISCELLANEOUS: Using chirally deuterated NADPH, the enzyme was shown to be A-type reductase catalyzing the transfer of deuterium from the 4(R) position of NADPH to the 1' (S) position of the substrate.
Sequence:
MVMVMEKKPYIISNVGMTLDGKLATINNDSRISCEEDLIRVHKIRANVDGIMVGIGTVLKDDPRLTVHKIKSDRNPVRIVVDSKLRVPLNARVLNKDAKTIIATTEDTNEEKEKKIKILEDMGVEVVKCGRGKVDLKKLMDILYDKGIKSILLEGGGTLNWGMFKEGLVDEVSVYIAPKIFGGKEAPTYVDGEGFKTVDECVKLELKNFYRLGEGIVLEFKVKK
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively.
Subcellular Localization:
Nucleus.
Sequence:
MIIPVCCFTCGKIIGNKWEAYLGLLQAMYTEGDALDTLDLKRYCCRCMLLAHADLIEKLLNYALLEK
The following text describes a protein:
Function:
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Complements an E.coli null mutation. Upon overexpression in E.coli has been shown to degrade endogenous sigma-32, SecY and phage lambda cII protein.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein; Cytoplasmic side. Note=Upon expression in E.coli.
Sequence:
MNRKNVTRTITAIAVVVLLGWSFFYFSDDTRGYKPVDTSVAITQINGDNVKSAQIDDREQQLRLILKKGNNETDGSEKVITKYPTGYAVDLFNALSAKNAKVSTVVNQGSILGELLVYVLPLLLLVGLFVMFSRMQGGARMGFGFGKSRAKQLSKDMPKTTFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPALEEAVDRVIGGPRRKGRIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVAVPEEDKGLRTRSEMIAQLVFAMGGRAAEELVFREPTTGAVSDIEQATKIARSMVTEFGMSSKLGAVKYGSEHGDPFLGRTMGTQPDYSHEVAREIDEEVRKLIEAAHTEAWEILTEYRDVLDTLAGELLEKETLHRPELESIFADVEKRPRLTMFDDFGGRIPSDKPPIKTPGELAIERGEPWPQPVPEPAFKAAIAQATQAAEAARSDAGQTGHGANGSPAGTHRSGDRQYGSTQPDYGAPAGWHAPGWPPRSSHRPSYSGEPAPTYPGQPYPTGQADPGSDESSAEQDDEVSRTKPAHG