lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.
Subcellular Localization:
Endoplasmic reticulum membrane.
Sequence:
MHSSKPLDRPLLHPQQSYSSANHNSVLNRRRSGSKGSTTSNGSVSSFQHQQNDDPNSPLSGSISTSMNTALAGPKHSFIDASSKDNTAGNSAASLAGSVTTTTGTTSRFANAPPPRMLSRRPPPSTGSFARPPTSTSGSAAQRHSSMASNTKRNPIDATGVGRVVSGSTQFSTETGSLGSVDGAKKTVTTSNITSNHASFFDSFGLGSTTTVHNTKTSQDHTVPTNGSHSPTRVTNVKPPTGPLQKNMNAQKLIDEFGFDQISSSQPVDHNVSLTRTAGVQYHQESSKHNHQQPKVISPKPPSPLPNQTFQSGIPLLNASVTVAGPPLKSPAYTKDEHHHQLQQSQPKVNESTVSASFEPPPLHNMSTTVTTQEIKPKTTYSSSPPIETAVFNVVSESSGPAIVPLEHEVSDVQQPENASFFDEHHRNLDLQDENPFNAAMQSNSVVHGVSSQSIQTNSKHSNQLALSPNRSSPVDMSANPNGKNLGPKNGVVMQNDTEINHHTFDDIDTRDRPAGFYDFALGGTLFTNSTHHAPNDSLQFNPNHNDVGAFRATHSSDVQNLNDLDDLVLGSVPLADVNKQQSSHTAGIPYSDSNVAYPMSVTSQSLVNHFIPSDISTSNAEFSHQVQQQPAFESNTIDQYGSSMQPHNQQNQNQDFQRLYNNAHADDGSMEGIASNDDTMIDSQQHFATDFDSNTHNGVGYEDYATVHGSATLFQQSVEQHQTIQPDSFDTHSQSLTERNDLHSFGHLSSADIQQHENILPMPIVHSVSNYEGTAHTTENDGYMSAPIVEPPIPIAWADESQRESLSTSVEHNSLADLADSASNPFGFGNQYNGIDPFGFVQGNVQPINNAIYDQPTDNTMYGQTVDNTMYDQTVDNTMYGQTVDNTMYGQTVDNTMYGQTVDNAMYDQPADNAMYAQIHDPNQQQFYGQDQPNNFDQQQQNFDQRLGYGEPQQFPNHSQGLDHQQFYDQQQSFVPNLQHQDLYQQQTLDSQQQSFDQQLVYDQENHQQQNMPDQQNQVEYNQSTNTQGQNENAYGWDGAFMQHQNVQQPVDKKIQDPYSFSTHDHLVRQPSPSHVEQYHHDFPSEPYNPSAHMPLSEASAVQSKSSRLSPAPPLSTTSVTSGYSKSNNHMAQNALSTSPVLTNAFEHTPVSTTRQCPSCLCECKATAKFCGECGLSLKQIAHATEHEKSVVEYAPNPAQTGYATDHTYQQSDYSQVNNETGVSYQFVPDVGVSGSSNMPHFDEHQQQQNYAEPAQLYHGQQSQYSYNGYDQQEHSNYDYSNNTYTDPHAQHAQAISQSPVQAQQPQKPLEFSDPLRRHRGHVFASFGFGGKLVVMRPRRQVLYLTSNTGLPTVTEKSYPGPILTINVKSILYSGITKEIEVAFEGKGPLVCSRNIWNKKKLISHLDNCFLNSENTVAYQSQKTLLWKMARLALEQDGVMLGSGNQATELSTAQQIRTILDTKSTKPNSGQHNDPHFEMHAMLLEGDRKGACQIATANLMWPHALIISSHVDRQTYADVTMQFSRSGLQTPATKPPHGVPLPGINVIYGLFAGAGPNAIYEFLPGPFGPENMPPEEYIDRWRFILSVILANRTPGDTDAILALGDQLATYGLVNEAHTCFLAVGAGRMLTGSDTLNSGNSKIIMLGANHVSQPTTFFKDIDAFHITETLEFALTLGSGGISNGFPHFQAYKFWYATYLSDLGFQNLAFKYTEGIEHFIKTFKNGSPYFHQTFCNKLCQFTDQLLTSMSSFESKAAAKDADDASSGGWLRKISSNLTGAALGRGLEQFMNNAVGVEDDITQPVKPQGPMYPTTSHTDGLLSTQSSSIPSQPSLAGNMSEVTTTLSTTTEFFSMMPQIPIVKLRHTQSNPTHLSTSMTSTSSIGVPSTSNVVMPFVSSAANDIYQHHPSNVSSTGEHAPLGSVSYPTYGMTQPDLHQTSQLPPMNAGHGPYASSFSHTSPALSYHADPTETRQELQQPSYMEQNQYEMQTGEFTGNYDYAANYDTSAGYPQTTSYDQSTEYAANAVHEQGANYEQNASAGYGGAEVYEQNANYGSYADTGDQTTNTMHAQDQQHSQNNGYYNSYHDQDTQQQFQNETHWSSYQDNQNGLQQHQADTQWNNYTEDPQTFQPSQNDSQSISAANNQESRDDKPPNDTHWSSYQKNDYSSNGIHEDTNHNQPPLTGPFFGASQELPGQTLQNVSKKAVDNSSFVPSFPLAFPPPANSTAGALPAFSPVVPPEPDAVDDFGFDNKSIRKAKSAFVLRPSSPLKAGENAPSEPVRRNSGSEQPTEKDKTSPTPAGTPDPAGGARNSRTILSYFGSMFGRPSKPDDKDSATQAFLPSGNALVFDKDLKKWVTKGGEPVGGPEKQLAPPPIKHMAETGAPTEMKPAMGAPTLGSAETPPGPMGPTLNSKPSTGSLGASRRSARSRYVDVINPNAAKESVPAINLALPTRFGMPSEQSQPKIMMPPFQQQANGSTSSFYDDFVKSNDSAAMETQPTSNDQSVTRDNQQDLPVLDGQHLASTEKQHQPPFMARMADVPARISSVPPLDTSHPQPPSARSSSSLSNHPQNIASANRSFHSLSSQPLSTVYMSNSGVQQPHHPSTFSEVNSSGEFQTQPGMTRLTPRLANRVVSNSRQGTPPSDL
The following text describes a protein:
Function:
Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles. Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity. Involved in membrane trafficking and Ca(2+)-dependent membrane fusion. May play a role in the assembly of the V-type ATPase complex. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). In islets of Langerhans cells, may regulate the acidification of dense-core secretory granules.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Single-pass type I membrane protein. Note=Not detected in trans-Golgi network.
Sequence:
MMAATVVSRIRTGTGRAPVMWLSLSLVAVAAAVATEQQVPLVLWSSDRNLWAPVADTHEGHITSDMQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAISTLTTYLQEKLGASPLHVDLATLKELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLKSEDVPYTAALTAVRPSRVARDITMVAGGLGRQLLQTQVASPAIHPPVSYNDTAPRILFWAQNFSVAYKDEWKDLTSLTFGVENLNLTGSFWNDSFAMLSLTYEPLFGATVTFKFILASRFYPVSARYWFAMERLEIHSNGSVAHFNVSQVTGPSIYSFHCEYVSSVSKKGNLLVTNVPSVWQMTLHNFQIQAFNVTGEQFSYASDCAGFFSPGIWMGLLTTLFMLFIFTYGLHMILSLKTMDRFDDHKGPTITLTQIV
The following text describes a protein:
Function:
Serine/threonine protein kinase that plays a role in viral propagation by phosphorylating various viral and cellular substrates including the viral p6.9 protein or host histone H1. Participates in nucleocapsid assembly and polyhedra formation.
Sequence:
MATTNATLQTLVQFYENCKNVKTRYKIINGRFGKISILSHKPTSKLYLQKTISAHNFNADEIKVHQLMSDHPNFIKIYFNHGSINNQVIVMDYIDCPDLFETLQIKGELSYQLVSNIIRQLCEALNDLHKHNFIHNDIKLENVLYFEALDRVYVCDYGLCKHENSLSVHDGTLEYFSPEKIRHTTMHVSFDWYAVGVLTYKLLTGGRHPFEKSEDEMLDLNSMKRRQQYNDIGVLKHVRNVNARDFVYCLTRYNIDCRLTNYKQIIKHEFLS
The following text describes a protein:
Function:
Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
Subcellular Localization:
Bacterial flagellum basal body.
Sequence:
MFEKTHFMKTQDLLERGMNNSIFKRKVISDNIANADVPHFKRSEVIFESMIKRAIESEKIEAIKEVPTQISDERHIQFFKPLDYREVQPKANTDYLTTMRADGNNVDVEKEVVEASNSQMQYMMMAERINQNYRELKQVMRMA
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MTAPVSTLASQKVLLDRDTLTEAEKWRYVVDNTLKKGSLGFLTGAALSLVVFRSVPVRVAATAFGCGFGIGKSYIDTRYILGHDVSVETVWTAEVLRKGFRGSTGVSDRESSGS
The following text describes a protein:
Function:
Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function; May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, invadopodium. Cell projection, podosome. Cleavage furrow. Cytoplasm, cytoskeleton. Midbody.
Sequence:
MILTMETDFDKENLVRYKTPRLLQRRRTLSFQKEFSFEDKEELANSTKDIDASLLAVLPKVSELRKLFEPNRPDTLEMKRKERIARRLEGIENDAQPVLLQNCPGLVTHRLLEEDTPRYMRATDPYSPHFGRSNEEETSDSSAENQPRSRYQAESAGGKTKPPSYSPLVMDPQGVESKAERIARYKAERRRQLAEKYGLSIDSDVDSEYSSKYARTKKEQDVPEKRIMKSEKKEDESRDFSSLYSSKMESKEMRSAASDSKEYSVQERESSPEREKLRLNEDSEKKSPDLSSIRYDTPCASENSTSFSFLGHDSPLSEVPSSPKQIRRASLSSPKQMVTTQSSHSLSDTRVGAGKTKPDWFLQKDSDGEPASLINWPSRVKVREKLVKEENTRGSPELVTDNVSQRKIRPVPVNFVPLQSETSAFHRVSSQPLGLLCRPVHGYIQPAGIAHTAKLVASEERESHFEPANANFLTRFPLDASVDSGKTDLPQVHEPLKFSYSSLENEQERQPILPSAIHRQGKSRESRTREGDAEILPVNKPKSMEPERDLERLKQRMPGTWKKTHESTERSEKVMYLQSAKGNVQVREEIPVRHKVLTRSLSDYTGSPKLEVFKSKEHVAKNEVEFRSTEGKIPNGEITMVDTKVSVAQLRNAFLETANASKKPELESHFEMPTSGTDLCGSAEHERGSRRPRRYFSPGENRKTSERFRTQPITSAERKETDRSAFSPEMIATDDEEKLDERAKLSVAAKRLLFREMERSFDGKGIPKPRSRNTAVERRLRRMQDRSRTQPITTEEVVIAATLQASAHQKTSAKEEIKEAKDALEQDQPAEPDSSTLTLAEKMALFNKLSQPVTKVVSTRTKGDIRQRRSNARYQTQPVTLGEVEQVQSDSGKIAPLSPTIVTSVSTMVSALSPVYSKDLHVKAAEEEPASEIAKPDFRHHSLVDNVDTSLKNILKTELWQPSVEVRESKRQSRECEEAEPKGFVKREENGLKKHSSFKEEPPHPVSDKTEDYNKEIKYAFPRKSSMELFSPQPHSEPAEQKELVSNILQEKREAKGQLFEDVMECEGTGARLTQQREHDAPISELVGTAATKSFSQSAAVVSCRQQETSELLEEKQNSRESKAEITEDTLDASSKTMSIKERNSDRMGAKATDKDWLALLKKSGEEDWKNRLNKKQEFGRVSVVERSPPLQEMEQLFTKKEEGGIADDNAMSKLFWEPVYASTYPPALPAAHKLHPFVPNVQVSNSSLRKPSPLAFERHPWRWKRASDGGENQMTIEERKQLISVREEAWKAKGKGAANDSTQFTVAGRMVKKGLASPTAITPVASPFCNRLKSTTPISKPLEEIEARPDMQLESDMKLDKLETFLGRLNSKVGGMQETVLTVTAKSVKEVMKLDDDETFSKFYRVNYPTSLLPLELDEDFDAIFDPDAPKLISSVAEHKRAVRPMRRAQASRNPLKMLAAREDILHEYTEQRLNVAFMESKRMKVEKMSANSNFSEVALAGLASKENFSSVSLRSVNLTEQNSNNSAVPYKKLMLLQIKGRRHVQTRLVEPRATSLNSGDCFLLLTPHYCFLWVGEFANVIEKAKASELATLIQTKRELGCRASYVQTIEEGINTHTHAAKDFWKLLGGQTSYQSAGRPEEDEMYEAAIIETNCIYRLVDDKLIPDDDYWGKMPKCTLLNSKEVLVFDFGSEVYVWHGKEVTLGQRKVAFQLAKHLWNGTFDYANCDINPLDPGECNSLIPRKGQGRPDWAIFGRLTEHNETILFKEKFLDWTELKKPAEKNSSESPLKEETKSDAKPYDIMRMVPLPETTVGTVLDGMNIGRGYGLIEGEDRRQFEIITISVDVWHILEFDYSRLPKQSIGQFHEGDTYVVKWKYLVSTSVGSRQKGDLQTRVVGKEKCVYFFWQGRHSTVSEKGTSALMTVELDEERGAQVQVLQGKEPPCFLQCFQGGMILHSGRREEEEENTQSDWRLYCVRGEVPLEGNLLEVACHCSSLRSRTSMIVLNINKALIYLWHGCKAQPHTKEVGRTAANKIKEQCPLEAGLHSSSKVTIHECDEGSEPIGFWDALGRRDRKAYDCMLQDPGKFNFTPRLFILGSSSGEFLATEYIYPSRDPSVVNSMPFLQEDLYTAPQPALFLVDNHHEVYLWQGWWPVENKIAGSARIRWASDRKCAMETVLQYCKGKNVKKPPKSYLIHAGLEPLTFTNMFPSWEHREDIAEITEMDAEASNQIILVEDVLAKLCKKLYPLADLLARPLPEGVDPLNLEIYLSDEDFETALQMTREEYNALPSWKQVNLKKAKGLF
The following text describes a protein:
Function:
Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
Sequence:
MRGDFYKQLTNDLETARAEGLFKEERIITSAQQADITVADGSHVINFCANNYLGLANHPELINAAKAGMDSHGFGMASVRFICGTQDSHKALEQKLASFLGMEDAILYSSCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAELEARLKEAREAGARHVLIATDGVFSMDGVIANLKGVCDLADKYDALVMVDDSHAVGFVGENGRGSHEYCDVMGRVDIITGTLGKALGGASGGYTAARKEVVEWLRQRSRPYLFSNSLAPAIVAASIKVLEMVEAGAELRDRLWANARQFREQMSAAGFTLAGADHAIIPVMLGDAVVAQKFARELQKEGIYVTGFFYPVVPKGQARIRTQMSAAHTPEQITRAVDAFTRIGKQLGVIA
The following text describes a protein:
Function:
Alpha-fucosidase involved in degradation of fucosylated xyloglucans. Hydrolyzes alpha-1,2-linked fucose. Active on cotton xyloglucan oligomers but not active on paranitrophenyl-fucoside.
Subcellular Localization:
Secreted.
Sequence:
MRKTTLFLAVTFATSNAQGRALRSSSPATYGTTDGSDYILKTGYLIGNGKLGVIPFGPPDTEKLNLNVDSLWSGGPFEVENYTGGNPSSPIYDALPGIRERIFENGTGGMEELLGSGNHYGSSRVLGNITIALDGVEAYSKYKRTLDLSDGVHRTSFTIANRTTAALKSSIFCSYPDQVCVYHLESASDARLPKVTISIENLLVNQSLLQTSCESEAKRAVLRHSGVTQAGPPEGMKYAAVAEVVNPRSSVTTCLGEGALQISSRKKQLTIIIGAATNYDQKAGNAKSGWSFKNAKDPASIVDGIASAAGWKGYQRLLDRHVKDYKKLMGDFSLELPDTTDSASKDTSELIEKYSYASATGNPYLENLLLDYARHLLVSSSRPNSLPANLQGRWTESLTPSWSADYHANINLQMNYWLADQTGLGETQHALWNYMADTWVPRGTETARLLYNASGWVVHNEINIFGFTAMKEDAGWANYPAAAAWMMQHVWDNFDYTHDTAWLVSQGYALLKGIASFWLSSLQEDKFFNDGSLVVNPCNSPETGPTTFGCTHYQQLIHQVFETVLAAQEYIHESDTKFVDSVASALERLDTGLHLSSWGGLKEWKLPDSYGYDNMSTHRHLSHLAGWYPGYSISSFAHGYRNKTIQDAVKETLTARGMGNAADANAGWAKVWRAACWARLNDSSMAYDELRYAIDENFVGNGLSMYWGASPPFQIDANFGFAGAVLSMLVVDLPTPRSDPGQRTVVLGPAIPSAWGGGRAKGLRLRGGAKVDFGWDKRGVVNWVNIVKRGKGTSRVKLVNKEGDILAEM
The following text describes a protein:
Function:
GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. Catalyzes, on the cytoplasmic face of the endoplasmic reticulum, the addition of the fourth and fifth mannose residues to the dolichol-linked oligosaccharide chain, to produce Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide. Man(5)GlcNAc(2)-PP-dolichol is a substrate for ALG3, the following enzyme in the biosynthetic pathway.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MDLGIMSAHDQLVVCLCEITRLLWMLLLPLAVLCALSIAVLVLLVLGVRLWLQGIRNARRARDGCPTVAFFHPYCNAGGGGERVLWCAIRALQSRYQDINVVVYTGDLGVSGRLILEGARRRFNIALPRPVHFVFLQHRLLVEPGLFPHFTLLGQSVGSIFLGWEALMEFVPDLYIDSMGYAFTLPLFRYLGGCRVGTYLHYPTVSTDMLSVVRERNPRFNNPDYISNSLFLSAFKVVYYFLFALLYGMAGSCSDLTMVNSSWTLNHILSLWRSPNRTCLVYPPCDVGAFLDIPLEEEDGGGRKSHSLVSVGQFRPEKDHQLQIRAFKKVLDRRRAALGGEEALKLVLIGGCRNQEDEERVLMLRGLCQELGVADKVEFKLNISFEDLKKEIGEATIGLHTMWNEHFGIGVVECMAAGKVVLAHNSGGPKLDIVVPFEGGQTGFLASDEDSYADAIERILALPAADRLRIRRNARQSAARFSDEEFQACFLAAMEPVMVMLDR
The following text describes a protein:
Function:
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Miscellaneous:
MISCELLANEOUS: Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequestering undecaprenyl diphosphate, thereby reducing the pool of lipid carrier available.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MEQFYYVLKYLILGLFQGLTEPIPISSSGHLVLAQHLLGLKIEGFSFELLVNSASLLAVLLIYRNDLIRLTKNGLSYIFTRAEDAKSDFFFIIYLVIATIPAGVIGVLFKDYIDQYLKGVKMVGISLLITAVGLWIIRNLRGRKNDGDLSMKDAIIVGLAQACALIPGISRSGATIVAAMLLGMKQETALRFSFLLYIPVSLGGLLLSITDIANDPNLDTLFVPYVVAFIATFIMTYISLKWFMNIMAKGNLKYFSFYCIIVGVLTLIFL
The following text describes a protein:
Function:
Component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway.
Miscellaneous:
MISCELLANEOUS: Present with 361 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MRPRRRGLAYHHTKPKGQLSQGHYPTTSNDGQRRKVGNSEAFQSFDIWKNLDRIRSTKKNAGQFIKGSLLILPMRTEDKQQFDECMDELHKYISKDILRCYPQKEQKDEGMLFYIVLKDFNILDSCFVLSVLLAFQKRLWMAPSEKSYFRVPKNINLTGSFYLPKNIETGRGHIITSYRREQPSSSIVEVGFNVVPDFQQFQVKACHVSKFMNELSNFFSQVEFGKCEANVINYFKREYNRTYSQISLALYELPLIGDGLFDIKSYISKTRPIIETSKAQMIKHISEMKAYNEISGLQGDQFPRQQRPLSNSPSSNSISSSQTIEAGATSYQTQPQRHAVNKPSNVLNSSNRHSGPKTFEDGRYSEGNKPGFMTQDEIKQHCIGTIKASMDAVKKKSSYQILKTYVRCPRQNYIDIVYQNLNDLRSKTNCNIVVLNLNNLHESQMWLESLNTTNYTIFAQAPHPSTIRVISIGGVGEYIVKALELILNILEH
The following text describes a protein:
Function:
Scaffold protein which plays an important role in the activation of the JNK pathway composed of mlk-1, mek-1 and kgb-1; by bringing together mek-1 and mlk-1, promotes mlk-1-mediated phosphorylation and activation of mek-1 which in turn phosphorylates kgb-1. In addition, negatively modulates the activation of the insulin/IGF-1-like signaling (IIS) probably by inhibiting the insulin receptor daf-2. Positively regulates the activity of the transcription factor daf-16/FOXO by both inhibiting IIS and activating the JNK pathway. Plays a role in maintaining gonadal basement membrane integrity through activation of the JNK pathway components mek-1 and jnk-1. Involved in the response to several environmental stresses including heavy metal ions (Cu(2+) and Cd(2+)), heat, oxidative and protein misfolding (ER) stresses. Plays a role in gonad and germline development following the L1 diapause. Plays a role in life span and egg laying. Plays a role in axon regeneration after injury.
Subcellular Localization:
Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Note=In intestinal cells, enriched in the nucleus.
Sequence:
MLNVEPSFAEELRSSGVSLSATYLGSVPVVESINVMVSEMRVQVVSECIQHVAATVGVTAAREINPVVSRVIGEVKKENFPVDINISSKMIKIIKQSRLIQRHPFSFFSFGAQGQKGTDTELMFGYIAKNKDGTDRRCHVVFIEDVHKLIDVLTTAINVNTFDAQANASTSNDGFTVPAPPMRHRSSLHRQSFVSNCRAPTVTEDVVGKVWYHGNLSREDAQALLKTEGDFLVRQSDHTPGKYVLSGRTAENEHKHLILLDNHNRVRTRDRTFSNISELIDYHVNNGMAVRSEGRDRETSLNLIRPVPCPGSDDIE
The following text describes a protein:
Function:
Transcription activator that binds to the DNA motif 5'-CACGTGG-3' in the promoter of iron (Fe) deficiency-inducible genes as well as of genes involved in iron homeostasis, thus contributing to basal tolerance to iron deficiency, iron uptake from soil and iron transport, particularly during seed maturation and germination. Promotes the accumulation of mugineic acid family phytosiderophores (MAs). Required for ethylene-mediated signaling during iron deficiency responses. Improves growth and yield, especially in calcareous soil with low iron availability. Promotes iron concentration in shoots and grain.
Sequence:
MGWPPEDMAAQDLQCEDHFVCCTSKETDVSCQSLGFSSRPLEREIVDQDELHYYTLIAMDSSSSTKKLCHNAYERGRRKKINDLYASLRALLPESDQSKNLSIPLTISRVLKYIPELQRQVERLQQRKEEILLALSRPEEQSHCGDIVVYRPMVSAACLSNREVMVQVCLLSSHFSISFSKILRLLKREGLHLVNASTYTTHDGRCFCSLHIEARETFDTECRIFCDTLLKEIKEQAELGSRITWNM
The following text describes a protein:
Function:
Binds anionic lipids and gangliosides at acidic pH.
Sequence:
MKTLLLFAAVCVAVTYSQVLEPCMAPDLWEARVSRIDPEKRFSERARMSYDATNRRVRRIEEVNLLEDKEFYDVLYIHNTEPGTEYRLNLKTKECQKREMSNAWRPFQVPPNSTFLGESYIGTGAVPGAGVLTELWSNTFEDGDKYFGVYTVEGCIPIQEEFYSNRTGLVSTFFFDVTAGISDPNVFIPPRECM
The following text describes a protein:
Function:
Required to trigger chlorophyll degradation during leaf senescence and fruit ripening. Binds directly PSY1 to regulate the accumulation of lycopene and beta-carotene in the maturing fruits.
Miscellaneous:
MISCELLANEOUS: Plants silencing SGR1 exhibit a stay-green leaf phenotype during leaf senescence, and a red-brown fruit phenotype in mature fruit. Plants silencing SGR1 exhibit altered development of fruit pericarp cells.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MGTLTTSLVVPSKLNNEQQSSIFIHKTRRKCKKNQSIVPVARLFGPAIFEASKLKVLFLGVDEEKHPGKLPRTYTLTHSDITSKLTLAISQTINNSQLQGWYNRLQRDEVVAEWKKVKGKMSLHVHCHISGGHFMLDLFARLRNYIFCKELPVVLKAFVHGDENLLRNYPELQEALVWVYFHSNIQEFNKVECWGPLRDATSPSSSSGGVGGVKSTSFTSNSNKKWELPKPCEEACACCFPPVSVMPWLSSNLDGVGEENGTIQQGLQEQQS
The following text describes a protein:
Function:
Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Miscellaneous:
MISCELLANEOUS: Present with 3290 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
Domain:
The flexible SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC4, forming a V-shaped heterodimer.
Sequence:
MKVEELIIDGFKSYATRTVITDWDPQFNAITGLNGSGKSNILDAICFVLGIASMSTVRASSLQDLIYKRGQAGVTKASVTIVFDNTDKSNSPIGFTNSPQISVTRQVVLGGTSKYLINGHRAPQQSVLQLFQSVQLNINNPNFLIMQGKITKVLNMKPSEILSLIEEAAGTKMFEDRREKAERTMSKKETKLQENRTLLTEEIEPKLEKLRNEKRMFLEFQSTQTDLEKTERIVVSYEYYNIKHKHTSIRETLENGETRMKMLNEFVKKTSEEIDSLNEDVEEIKLQKEKELHKEGTISKLENKENGLLNEISRLKTSLSIKVENLNDTTEKSKALESEIASSSAKLIEKKSAYANTEKDYKMVQEQLSKQRDLYKRKEELVSTLTTGISSTGAADGGYNAQLAKAKTELNEVSLAIKKSSMKMELLKKELLTIEPKLKEATKDNELNVKHVKQCQETCDKLRARLVEYGFDPSRIKDLKQREDKLKSHYYQTCKNSEYLKRRVTNLEFNYTKPYPNFEASFVHGVVGQLFQIDNDNIRYATALQTCAGGRLFNVVVQDSQTATQLLERGRLRKRVTIIPLDKIYTRPISSQVLDLAKKIAPGKVELAINLIRFDESITKAMEFIFGNSLICEDPETAKKITFHPKIRARSITLQGDVYDPEGTLSGGSRNTSESLLVDIQKYNQIQKQIETIQADLNHVTEELQTQYATSQKTKTIQSDLNLSLHKLDLAKRNLDANPSSQIIARNEEILRDIGECENEIKTKQMSLKKCQEEVSTIEKDMKEYDSDKGSKLNELKKELKLLAKELEEQESESERKYDLFQNLELETEQLSSELDSNKTLLHNHLKSIESLKLENSDLEGKIRGVEDDLVTVQTELNEEKKRLMDIDDELNELETLIKKKQDEKKSSELELQKLVHDLNKYKSNTNNMEKIIEDLRQKHEFLEDFDLVRNIVKQNEGIDLDTYRERSKQLNEKFQELRKKVNPNIMNMIENVEKKEAALKTMIKTIEKDKMKIQETISKLNEYKRETLVKTWEKVTLDFGNIFADLLPNSFAKLVPCEGKDVTQGLEVKVKLGNIWKESLIELSGGQRSLIALSLIMALLQFRPAPMYILDEVDAALDLSHTQNIGHLIKTRFKGSQFIVVSLKEGMFANANRVFRTRFQDGTSVVSIM
The following text describes a protein:
Function:
May function as a sodium/calcium exchanger (NCX) and participate in the maintenance of calcium homeostasis. May play a role abiotic stress responses.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSTRRQHRRGFPLVPLLLSLLAAAAYGRLISDGAPSAPLLSVIRLSGSPPAAAAGKAAEEKCEQSYGFLPCTTTVLGNLFLVLTYGFLMYKAATYLSTGSELLLEIMGPGLVGGLLLPILGALPDALLVLVSGLSGSKEEAQSQVLIGMGLLAGSTVFLLTLLWGTCVVVGKCDLGPNREAVDVTDTKGFSLTGTGITTDVQTSYAARIMGLSVIPFIIAQFPKMLKTHHGQRLAMLLALIVSFLLVLSYCLYQVFQPWIQRRKLAYAKHKHVISGILKHAQLQSLGRLLNDDGTPNEDVIRKLFHKIDMDESRSLSRAELHALIIGINFEEVEFDRTDAVDKVMADFDTSRNDIVEEEEFVQGMKKWLNEFKRNMPAGGAFSSKFNEYHERTRQEHDQLIDRSDEAVESVENPGWCITKAVALLLLGAAIAAAFADPLVDAVHNFSNATHIPSFFISFIALPLATNSSEAVSAIIFASRKKQRTCSLTFSEVYGGVTMNNTLCLGVFLALIYFRNLTWDFSSEVLIILLVCVVMALFTSFRTTFPLWTCLVAYMLYPFSLVIVYILDYVFGWS
The following text describes a protein:
Function:
Primarily acts as an independent SigF regulator that is sensitive to the osmosensory signal, mediating the cross talk of PknD with the SigF regulon. Possesses both phosphatase and kinase activities. The kinase domain functions as a classic anti-sigma factor-like kinase to phosphorylate the anti-anti-sigma factor domain at the canonical regulatory site, and the phosphatase domain antagonizes this activity.
Sequence:
MTRTWQISDVTDAAVARVAAARLATAFGVPPVERARLTASLGAQLRLCLTKGGTWRLALETGTVSRPAPQAAERVLHAVVTPSPEAAAAGQPPWRVTVPCPEADDVGAIADAGAVADDPVELAQALLGADEDTALVLERLTEQEGLVDFHREELQQTNQGVVALHAELDAAGRAQREAFAAERKARTEAEHARRRLTFLADASAVLTASLDHHEIVRRLPELLVPEYATGVDIWLFDQDGDRPGPAHAAAAVVAARTGRPQYAAAHPGGLPGVDDQPPSALAPDRPLLCIPLPTRQAPLGVVTLSPPGDRWDPDDAVMLVELTRRASIAIDHAQRYQHNRDIAETLQRALLTELPAPPGLALAARYLPATHGLNIGGDWYDAFRQPDGGVIAVVGDVTGHGLRAAVMMSQLRTALRAYAVDGGSPGQLLTRLHTFLHHLQPDLFATAVIARFHPDDPTVTWAAAGHPPPVLRTPDGGVRTLDAKPGAMLGIPMRQEIADHTVPMAPGSTLALYTDGLVERRARGIDPGIARLADALASFGPAELDTDLEGSADGILRPMLSDSERDDDVCLLLCHLRGTG
The following text describes a protein:
Function:
Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. DmsC anchors the DmsAB dimer to the membrane and stabilizes it (By similarity).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MNTGLYELPLVFFTVLAQSAVGAWLVFTFVLLNEKNTKSRTYIHKVMFVILALLGIGFIASIMHLGLPIRAFNSLNRVGSSMMSNEIAAGAIFFTLAGFYWLIAILGKMPVSLGNVWRIVTALIGILFMYVMNQVYHITSIPTWNNALTSWSFYLTVVLGGLTLSYALLIPNKQREYQLQHLPSLFAIGVSLVAIVAIYQGFNLHNIHSAIQNAADLVPNYAIMTVTRLCLLSIVAFLLFRVKNIGLLGISVLLTLVAEGIGRVLFYGLHMTYGMTIGG
The following text describes a protein:
Function:
Catalyzes the isomerization of L-erythrulose-1P to D-erythrulose-4P. Involved in the degradation pathway of L-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source.
Sequence:
MPDARALGAAQLWIGTSWKMNKGLAESRGYARELAEYVAAKPPAGVQPFIIPSFTALTTVRDALGDDSPVLLGVQNAHWEDHGAWTGEVSVAQAKDAGAQIVEIGHSERREHFGETVETTRLKVAAALHHGLVPLLCIGESAENKQAGESSRFILEQAAGALEGLTDEHLARVLIAYEPIWAIGENGRPATVEELRQPFDDLAREYGCRTMGLLYGGSVNTDNAEDLLGIDHVTGLFIGRAAWQLPGYVRILEMAAAHPKAKA
The following text describes a protein:
Function:
Alpha-1,2-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is essential in fungi (By similarity).
Miscellaneous:
MISCELLANEOUS: May be used as a target for the development of some new fungicide, due the fact the presence of a fourth mannose in GPI-anchor proteins is essential for viability in fungi but not in mammals.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MIKINFNWRTFYLLTIVFRFVFTLSDSYIHPDEHFQSLEVLTNRILNYSTNIPWEFQDDPARSLAPLYFIYGPLLYFIKFFKLNLTALQIWYIARLQISILSWIITDFCLYWMLPSKPERIKAIFFTSTSYITLVYQNHLFSNSIETLLLLVTILLIDDLRYVQESKDQDVQNLNKNKNLFYTGVLISLGIFNRITFPAFLILPGWFVMKYVLKHYVSGLYLVMGFFSTTALLILVDTILFGNINNVVAEPFNVSSYIIAPLNNLLYNARYENLAQHGIHPYYTHILVNMPQILGPGLIFFVSKSYTKTTPFLTVISGLLFLSVIPHQELRFLIPLLPLACCSFDFTLKWVQPWMLYTWYIFNIFMSILMGKLHQGGVVPVLDHIKSEASVQVWWRTYTPPSWILGSNSTETTHLGEKLNDNKFINIVDCMGADSKEVQQILQTISTNKPVYLITPIASFKHFDESRFSPVWNYTFHLDLDHLDFADIQPGLGVYQLL