lhallee/plat_data huggingface dataset:
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:
MRTGEPLPEVGDVLAALATGLWHWDTATGEVTVDGEAARLLGLPTGPATLTEAQVRARLHPVDWNEITGVVQLAVAEGTLAEVRIRIMDERGHVVRVVRSRSKPSFDTVRKAYVLTGTLQEVAEPRPGTPAGRSAVTGEWRRSREAFLLDAGRALAEARSTEEVLRVAAGLSMPGFSPDGLAVFGVSGDRLTVIGHHGQPENEANPFVDMSLETDYPAAEVVRTGRAVYLSSPQQYRSRYPMTWSLAERFGRRSWAYLPLTVAGRTMGAWMAAFAYPVAFTPDERSVLTTVARMLAQALSRAGAAENQRELAEGLQRSMLPMLGPEIPGMDIAARYVPTGGGLQVGGDWYDMIPLPGGRFALVIGDVQGHDVRAAGLMGQLRIALRAYASEGHRPDAVLARASHFFHGLATAEDDPGDLRFATCYYAEVDPATGTVESARAGHLDPVVRMADGTALILATAGGLPLGIDPDTDYPTTRLALEPGDTLMLCTDGLVETGGHDLQSGWHRLRVILEEHVGGLEELADALVQAVHGPSSHHTVGPLADRREDDIALLLLCRQGEGCGCGESTATRAPVRRTMLTVAQAEPARIATARQHLRDLLHDWPGEEQRDAAVLLLSEMLTNVLVHTDTDALLVAEVAGEPGERRIRVEVTDNGDDLPHKRRPGEMASSGRGLMLVELLADAWGVAPRGEGKSIWYELYESAAPVDGAGPASGPEAAVETP
The following text describes a protein:
Function:
Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis.
Sequence:
MLDYRQKIDALITKIEKARTAYSRHHIVKIVAVSKNASPEAIQHYYNCSQRAFGENKVQDLKTKMHSLEHLPLEWHMIGSLQENKINALLSLKPALLHSLDSLKLALKIEKRCEILGVNLNALLQVNSAYEESKSGVVPEEALEIYSQISETCKHLKLKGLMCIGAHTDDEKEIEKSFITTKKLFDQIKNASVLSMGMSDDFELAIACGANLLRIGSFLFKE
The following text describes a protein:
Function:
Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.
Miscellaneous:
MISCELLANEOUS: Present with 3930 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Domain:
The N-terminus is dedicated to mating-type repression.
Sequence:
MAKTLKDLQGWEIITTDEQGNIIDGGQKRLRRRGAKTEHYLKRSSDGIKLGRGDSVVMHNEAAGTYSVYMIQELRLNTLNNVVELWALTYLRWFEVNPLAHYRQFNPDANILNRPLNYYNKLFSETANKNELYLTAELAELQLFNFIRVANVMDGSKWEVLKGNVDPERDFTVRYICEPTGEKFVDINIEDVKAYIKKVEPREAQEYLKDLTLPSKKKEIKRGPQKKDKATQTAQISDAETRATDITDNEDGNEDESSDYESPSDIDVSEDMDSGEISADELEEEEDEEEDEDEEEKEARHTNSPRKRGRKIKLGKDDIDASVQPPPKKRGRKPKDPSKPRQMLLISSCRANNTPVIRKFTKKNVARAKKKYTPFSKRFKSIAAIPDLTSLPEFYGNSSELMASRFENKLKTTQKHQIVETIFSKVKKQLNSSYVKEEILKSANFQDYLPARENEFASIYLSAYSAIESDSATTIYVAGTPGVGKTLTVREVVKELLSSSAQREIPDFLYVEINGLKMVKPTDCYETLWNKVSGERLTWAASMESLEFYFKRVPKNKKKTIVVLLDELDAMVTKSQDIMYNFFNWTTYENAKLIVIAVANTMDLPERQLGNKITSRIGFTRIMFTGYTHEELKNIIDLRLKGLNDSFFYVDTKTGNAILIDAAGNDTTVKQTLPEDVRKVRLRMSADAIEIASRKVASVSGDARRALKVCKRAAEIAEKHYMAKHGYGYDGKTVIEDENEEQIYDDEDKDLIESNKAKDDNDDDDDNDGVQTVHITHVMKALNETLNSHVITFMTRLSFTAKLFIYALLNLMKKNGSQEQELGDIVDEIKLLIEVNGSNKFVMEIAKTLFQQGSDNISEQLRIISWDFVLNQLLDAGILFKQTMKNDRICCVKLNISVEEAKRAMNEDETLRNL
The following text describes a protein:
Function:
High affinity carnitine transporter involved in the active cellular uptake of carnitine. Also transports organic cations (By similarity).
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MADGNTRFTVDEALVAMGFGKFQIYVLAYAGMGWVAEAMEMMLLSFVGPAVQSLWNLSARQESLITSVVFAGMLIGAYSWGIVSDKHGRRKGFIITAVVTFVAGFLSAFSPNYMWLIILRCLVGLGLGGGPVLASWYLEFIPAPSRGTWMVVFSAFWTVGTIFEASLAWLVMPRLGWRWLLAFSSVPSSLLLLFYRWTSESPRYLILQGRKAEALAILEKIARMNKTQLPPGVLSSELETELEENKNIPTENTHLLKAGESGEAVAVSKIVLKADKEPGFSLLALLSPTLMKRTLLLWVVFFGNAFAYYGVVLLTTELNNSHNRCYPTEKQLRNSNDVNYRDVFIASFAEFPGLLISAAMVDRLGRKASMASMLFTCCIFLLPLLSHQSPFITTVLLFGGRICISAAFTVVYIYAPEIYPTAVRTTGVGVGSSVGRIGGILCPLVAVGLVHGCHQTIAVLLFEVVILVSGICVCLFPFETSGRDLTDSISASKEPPSASV
The following text describes a protein:
Function:
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation (By similarity).
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MRLTISRKFSLVFLTLILINLLVGGIGVLNMQHIIQKTDEINTKWIDGIKGITSINYVTEHLSSKEKDFLIYTDKSKMDTLDQEMNQIMEDINQKLDNYEKTISTDKEQKLFEQLQTKVNTYMDIHAQIIESGRTNDMDKARGLLVQTEASFEDMKKTITQLVDLNQEGSNTAVKETKAVYHKGLIYTALLVAASILISIFIWLYITRNIVKPIIRMKESANHIAEGDLSNDMEALNSKDELGDLNEALQKMVGNLRDIVGYSKDISSRVLSSSQVLATATNETRSGSKHITETMNEMAEGSEQQAQDAVTIAESMNEFTESIDKAYNHGITISDTSQNVLELAVSGNENMATSLQQMKTIHHIVEEAVHKVRSLEQHSQDINKLVQVINGIAEQTNLLSLNAAIEAARAGESGKGFAVVAEEVRKLADGVSDSVQDITRIVNGTQQEIHTVITYLESSFTEVEKGTENLTDTGQAMQHIKQSVTHVADSIKEVTDGLKQLTNQSITINQSIENIASVSEESAAGIEETFSITEQSAHSMDQVLLNAEELEQLANELNEKMGQFTI
The following text describes a protein:
Function:
Serine/threonine-protein kinase involved in vacuolar processing and morphology.
Subcellular Localization:
Vacuole membrane; Peripheral membrane protein.
Sequence:
MISIVLELFQNLCCCRGFSDATIRVNDKRYRIQRLLGEGGMSFVYLVQLSKNSLIIDNGIATPELYALKKIICPSVESISNGMREIENYKRFQSPYVIKSIDSQVMQEKDGSKTIYIVLPYYSLGSLQDSINRRLLEGTFVSEAECVRIMLGVTRGLLCLHDPASRQDNATSRVNVDAVSMTYSDETAMLLEDTPLEMDMLSSNSAGSIAYAHRDITPSNILFSSDGLPVIGDLGSCSQADITIENRHQLSELQEWVNDNCTLPYTPPELLNLKLNQVLSSKVDIWSLGCTFYTLMFGISPFEREEQIHGASLTYAINTGKYSFPRNSRFSEGLLSVIKKCIQVDPIQRPTTSQLLNLLQDLDT
The following text describes a protein:
Function:
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity.
Sequence:
MDYVLISVPTKAFNRQVGTLSELIALSDDLAKHDQFVMSVTVKLANILKDLAATPADAERTMQVDGRSLPEATEHFSWDMARYNVKQLPRELAQQIIQDTQDVEVKLKTKSQGFNKIKGNLQAIERKSNGSLLIKSLANVVKPEHVVRDSEFLVTLLVVVPKLVAEDAEYGLYTVTVFRKIVEDFKQNAREKKFVVRDFEFDAEEIAKDEHELNELRTNMVKQQALRVFVESVLRFGLPPDFTATLLKINNGNTRKVRQILGEEYAALDRANAAGADVVDIPGVTNQGEYYPYVSFDVELAHFVDKR
The following text describes a protein:
Function:
RNA-binding protein that regulates the translation of specific target mRNA species downstream of the mTORC1 complex, in function of growth signals and nutrient availability. Interacts on the one hand with the 3' poly-A tails that are present in all mRNA molecules, and on the other hand with the 7-methylguanosine cap structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding ribosomal proteins and several components of the translation machinery. The interaction with the 5' end of mRNAs containing a 5'TOP motif leads to translational repression by preventing the binding of EIF4G1. When mTORC1 is activated, LARP1 is phosphorylated and dissociates from the 5' untranslated region (UTR) of mRNA. Does not prevent binding of EIF4G1 to mRNAs that lack a 5'TOP motif. Interacts with the free 40S ribosome subunit and with ribosomes, both monosomes and polysomes. Under normal nutrient availability, interacts primarily with the 3' untranslated region (UTR) of mRNAs encoding ribosomal proteins and increases protein synthesis. Associates with actively translating ribosomes and stimulates translation of mRNAs containing a 5'TOP motif, thereby regulating protein synthesis, and as a consequence, cell growth and proliferation. Stabilizes mRNAs species with a 5'TOP motif, which is required to prevent apoptosis; (Microbial infection) Positively regulates the replication of dengue virus (DENV).
Subcellular Localization:
Cytoplasm. Cytoplasmic granule. Note=Colocalizes with RPTOR and PABPC1 in cytoplasmic granules that resemble stress granules.
Domain:
The C-terminal region mediates interaction with the mRNA and polysomes. It is required for translational repression of mRNAs with a 5'TOP motif; The N-terminal region mediates interaction with PABPC1.
Sequence:
MATQVEPLLPGGATLLQAEEHGGLVRKKPPPAPEGKGEPGPNDVRGGEPDGSARRPRPPCAKPHKEGTGQQERESPRPLQLPGAEGPAISDGEEGGGEPGAGGGAAGAAGAGRRDFVEAPPPKVNPWTKNALPPVLTTVNGQSPPEHSAPAKVVRAAVPKQRKGSKVGDFGDAINWPTPGEIAHKSVQPQSHKPQPTRKLPPKKDMKEQEKGEGSDSKESPKTKSDESGEEKNGDEDCQRGGQKKKGNKHKWVPLQIDMKPEVPREKLASRPTRPPEPRHIPANRGEIKGSESATYVPVAPPTPAWQPEIKPEPAWHDQDETSSVKSDGAGGARASFRGRGRGRGRGRGRGRGGTRTHFDYQFGYRKFDGVEGPRTPKYMNNITYYFDNVSSTELYSVDQELLKDYIKRQIEYYFSVDNLERDFFLRRKMDADGFLPITLIASFHRVQALTTDISLIFAALKDSKVVEIVDEKVRRREEPEKWPLPPIVDYSQTDFSQLLNCPEFVPRQHYQKETESAPGSPRAVTPVPTKTEEVSNLKTLPKGLSASLPDLDSENWIEVKKRPRPSPARPKKSEESRFSHLTSLPQQLPSQQLMSKDQDEQEELDFLFDEEMEQMDGRKNTFTAWSDEESDYEIDDRDVNKILIVTQTPHYMRRHPGGDRTGNHTSRAKMSAELAKVINDGLFYYEQDLWAEKFEPEYSQIKQEVENFKKVNMISREQFDTLTPEPPVDPNQEVPPGPPRFQQVPTDALANKLFGAPEPSTIARSLPTTVPESPNYRNTRTPRTPRTPQLKDSSQTSRFYPVVKEGRTLDAKMPRKRKTRHSSNPPLESHVGWVMDSREHRPRTASISSSPSEGTPTVGSYGCTPQSLPKFQHPSHELLKENGFTQHVYHKYRRRCLNERKRLGIGQSQEMNTLFRFWSFFLRDHFNKKMYEEFKQLALEDAKEGYRYGLECLFRYYSYGLEKKFRLDIFKDFQEETVKDYEAGQLYGLEKFWAFLKYSKAKNLDIDPKLQEYLGKFRRLEDFRVDPPMGEEGNHKRHSVVAGGGGGEGRKRCPSQSSSRPAAMISQPPTPPTGQPVREDAKWTSQHSNTQTLGK
The following text describes a protein:
Function:
ATP-dependent DNA helicase essential for viral DNA replication and recombination. The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ssDNA for both leading and lagging strand synthesis. Interaction with the primase allows the primase to initiate lagging strand synthesis and fully activates the helicase. Loaded by the helicase assembly factor on replication forks that begin at discrete replication origin sequences, as well as on forks that are created during recombination.
Sequence:
MVEIILSHLIFDQAYFSKVWPYMDSEYFESGPAKNTFKLIKSHVNEYHSVPSINALNVALENSSFTETEYSGVKTLISKLADSPEDHSWLVKETEKYVQQRAMFNATSKIIEIQTNAELPPEKRNKKMPDVGAIPDIMRQALSISFDSYVGHDWMDDYEARWLSYMNKARKVPFKLRILNKITKGGAETGTLNVLMAGVNVGKSLGLCSLAADYLQLGHNVLYISMEMAEEVCAKRIDANMLDVSLDDIDDGHISYAEYKGKMEKWREKSTLGRLIVKQYPTGGADANTFRSLLNELKLKKNFVPTIIIVDYLGICKSCRIRVYSENSYTTVKAIAEELRALAVETETVLWTAAQVGKQAWDSSDVNMSDIAESAGLPATADFMLAVIETEELAAAEQQLIKQIKSRYGDKNKWNKFLMGVQKGNQKWVEIEQDSTPTEVNEVAGSQQIQAEQNRYQRNESTRAQLDALANELKF
The following text describes a protein:
Function:
Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity. Stabilizes AZIN2 by interfering with its ubiquitination. Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol. Probably plays a key role in spermatogenesis by regulating the intracellular concentration of polyamines in haploid germ cells.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MPCYRSRPSAFSLSYIKRGKTRNYLYPIWSPYAYYLYCYKYRITLREKMLPCYKSITYKEREDLTLRPRSCLQCSESLAGLQVVRSTEQGDHNQFKELYSVGKLTVLATDPLLHQDPVQLDFHFRLTPQTSTHWHGLLCDHRLFLDIPYRALDQGNRESLTATLEYVEEKTNVDSVFVNFQNNRNDRGALLRAFSYMGFELVRPDHPALPPWDNVIFMVYPLERDLGHLPSEPP
The following text describes a protein:
Function:
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins.
Sequence:
MDAKQIEAVAASYPSPPGIKHTFGTAGFRANADTLDRVFFTVGLLAVLRSKKLAGQTIGVMVTASHNPAQDNGIKLVDPQGEMLASSWESHATVLANSADLPSSLTQIIDSETIDFKQPAKLILGHDTRPSCARLIKAFKDAVKALDPSAQILESGLKTTPQLHYLVKCINDGGVYGAPTEEGYYKKLSDAFIALNAETKTPYTLMVDCANGVGGPKLESMQAYLKDSPLRLKLSSTDVNSSEKLNKDCGADYVKTTQSAPSGVSLEPLARACSFDGDADRIVYYYYSEKKSFRLMDGDKIATLVASYIKQLVELESAEIKDHLRIGVVQTAYANGNSTRYIKDQLGLAVTCTPTGVKHLHHAAQTFDIGTYFEANGHGTVVFSEALLKRLPASSKLLSLAGLINQTVGDSMSDMLLVETILNARGWGMAEWDAKYEELPNRLVKVIVSDRHAFVTEDAERVLVKPDGMQLKINQIVANYPSARSFVRPSGTEDCVRVYAEAGTKEATDELAYKVAGMVFEFCGKGEKPKEFL
The following text describes a protein:
Function:
Receptor for retinoic acid that acts as a transcription factor. Forms homo- or heterodimers with retinoic acid receptors (rars) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes.
Subcellular Localization:
Nucleus.
Domain:
Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Sequence:
PFLSLSLCFLLPLHVDCRSPDSSSLSSSPTLRGTPPPEPSAPLHPSMIGSAMTTSIGGLGSPFPVISSSMGSPGLPATPSIGYGPVSSPQINSTVNLSGLHSVSSSDDVKPPLGMRVVPGHPHGALMPGKRLCAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLTYTCRDNKDCIVDKRQRNRCQYCRYQKCLATGMKREAVQEERQRGKDKDGDGDLVCGGANEDMPVEKILEAELAVSRSRTKASTGGGSGTGAARIYSQRLGSVLSNPKGLSLLASHSSLPSVLCRVLTELVSKMRDMRMDKTELGCLRAIILFNPDAKGLSNPGEVELLREKVYASLESYCKQKYPEQQGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMS
The following text describes a protein:
Function:
Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
Sequence:
MRRGLVIVGHGSQLNHYREVMELHRKRIEESGAFDEVKIAFAARKRRPMPDEAIREMNCDIIYVVPLFISYGLHVTEDLPDLLGFPRGRGIKEGEFEGKKVVICEPIGEDYFVTYAILNSVFRIGRDGKGEE
The following text describes a protein:
Function:
Inhibits the vertebrate potassium channels Kv1.1/KCNA1 and Kv1.3/KCNA3 in vitro with an IC(50) of 5.3 nM and 50.0 nM respectively.
Miscellaneous:
MISCELLANEOUS: Negative results: is a weak beta toxin because it has no effect on Nav1.2a/SCN2A voltage-dependent sodium channels when perfused at a concentration of 100 nM, but when added to the extracellular bath solution at a concentration of 1 uM it shifts the voltage of activation toward more negative potentials. Has no effect on the Nav1.5/SCN5A voltage-dependent sodium channel. Administration to mice produces no toxic effects.
Subcellular Localization:
Secreted.
Domain:
Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Sequence:
MMKLMLFSIIVILFSLIGSIHGADVPGNYPLDSSDDTYLCAPLGENPFCIKICRKHGVKYGYCYAFQCWCEYLEDKNVKI
The following text describes a protein:
Function:
Needed for flagellar regrowth and assembly.
Sequence:
MMLIKNTPRAGAVKLRVHQFPPLRKVRQVAPSAADQTLDPAEYQKQLMAGFQEGISQGFDKGLAEGKEEGYQEGVRLGHDDGLKKGRIEGRQSELASFNDVIKPFSGYITQLHTYLETYEQRRRDELLQLVEKVTRQVIRCELALQPAQLLTLVEEALAALPMVPQQLKVYLNPAEFGRINDVAPEKVQAWGLAADPDMVGGECRIVTETTEIDVGCQHRLDQCIGALHSSFLTEPHHE
The following text describes a protein:
Function:
Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Sequence:
MIYTVTLNPSIDYIVRLDQVKVGSVNRMDSDDKFAGGKGINVSRVLKRLNIPNTATGFIGGFTGKFITDTLAEEEIETRFVQVAEDTRINVKIKADQETEINGTGPTVEPVQLEELKAILSSLTAEDTVVFAGSSAKNLGNVIYKDLISLTRQTGAQVVCDFEGQTLIDSLDYQPLLVKPNNHELGAIFGVKLESLDEIEKYARELLAKGAQNVIISMAGDGALLVTSEGAYFAKPIKGTVKNSVGAGDSMVAGFTGEFVKSKDAVEAFKWGVACGTATTFSDDLATAEFIKETYGKVEVEKR
The following text describes a protein:
Function:
Involved in protein export. Participates in an early event of protein translocation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSTLLNVLLFLSAFILIVLVLIQPDRSHGMTASMGLGASNTIFGINKDGGPLARATEVVATLFIICSLLLYLTR
The following text describes a protein:
Function:
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Sequence:
MRTFLGISIPEEIKEQLTSICYGLSDIRWVPKENFHITLVFLGEQSSECLDILSDFCSEISFTEFDLSLKSVGTFGKQKSPSILFAAVKPSIELSQLHKTLDSGIRKLGFSIDRQNYQPHLTIGRFKNSNETRVIMYLEEFANFVSSNFKVSEFHIYSSKTFSNGPVYSIEESFSLLPSYKI
The following text describes a protein:
Function:
Plays a role in the formation of lipid droplets (LDs) which are storage organelles at the center of lipid and energy homeostasis. Regulates the morphology, size and distribution of LDs. Mediates the formation of endoplasmic reticulum-lipid droplets (ER-LD) contact sites by forming a complex with RAB18 and ZW10 (By similarity). Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through FYVE-type zinc finger (By similarity).
Subcellular Localization:
Golgi apparatus. Golgi apparatus, Golgi stack. Endoplasmic reticulum. Preautophagosomal structure. Lipid droplet. Mitochondrion. Note=Resides predominantly in the cisternal stacks of the Golgi. Colocalizes with TRIM13 on the perinuclear endoplasmic reticulum. During starvation conditions, localizes to omegasomes which are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Localizes to lipid droplets in the presence of oleic acid (By similarity).
Sequence:
MSAQTSLAEKGLNPGLMCQESYACSGTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRLKAGHVPYCDPCKGPNGHSPGVRQRAAVRCQTCKINLCLECQKRTHSGGNKRRHPITVYLVSKVQESLEGEEMDEETKRKKMTERVVSFLLVDENEEIQVTNEEDFIRKLDCKPDQHLKVVSIFGNTGDGKSHTLNHTFFYGREVFKTSPAQESCTVGVWAAYDPVHKVAVIDTEGLLGATVNLSQRTRLLLKVLAISDLVIYRTHADRLHNDLFKFLGDASEAYLKHFTKELKATTARCGLDVPLSTLGPAVIIFHETVHTQLLGSDHPSEAPEKLIQDRFRKLGRFPEAFSSIHYKGTRTYNPPTDFSGLRRALEQLLENNTTRSPRHPGVIFKALKALSDRFSGEIPDDQMAHSSFFPDEYFTCSSLCLSCGAGCKNSMNHGKEGVPHEAKSRCRYSHQYDNRVYTCKACYERGKEVSVVPKTSASTDSPWMGLAKYAWSGYVIECPNCGVVYRSRQYWFGNQDPVDTVVRTEIVHVWPGTDAFLKDNNNAAQRLLDGMNFMAQSVSELSLGPTKAVTSWLTDQIAPAYWRPNSQILSCNQCATSFKDNDTKHHCRACGEGFCDSCSSKTRPVPERGWGPAPVRVCDSCYDARNVQLDVTEAQADDEGGTLIARKVGEAVQNTLGAVVTAIDIPLGLVKDAARPAYWVPDHEILHCHNCRKEFSVKLSKHHCRACGQGFCDECSHDCRAVPSRGWDHPVRVCFNCNKKPGDL
The following text describes a protein:
Function:
Required for DNA transformation. Positively regulates genes required for DNA transformation (late competence-specific genes) in association with CRP. Required for expression of the late competence-specific gene, com101A. Required for expression of the dprABC operon.
Sequence:
MNIKDEHIDSVCSLLDQLVGNVSFKNLFTGYGLFHKEETMFAIWQNKKLYLRGEGVLAIQLTKLGCEPFTTNELNKRFVLSQYYALSDQILRSNRLCRKLIILSIKQILEQKLECTLRKLNRLKDLPNLTIKHERALIKVGITNVAMLREIGAENALVELKKSGSGATLDFYWKLVCALQNKNSQMLSQAEKERLLKKLNEVWRKNGLKGYRKLDDE
The following text describes a protein:
Function:
Plays a role in myoblast fusion; probable mediator of endocytic recycling for membrane trafficking events during myotube formation.
Miscellaneous:
MISCELLANEOUS: [Isoform 1]: Gene prediction based on partial mRNA data.
Subcellular Localization:
Cell membrane. Membrane; Single-pass membrane protein. Note=Colocalizes with EHD1 and EHD2 at plasma membrane in myoblasts and myotubes. Localizes into foci at the plasma membrane (By similarity).
Sequence:
MLRLVVQSAKIDPPLAPLPRPCMSIDFRDIKKRTRVVEGNDPVWNETLIWHLWNRPLENDSFLQVTLQDMGSQKKERFIGLATVLLKPLLKQPSEVLFVKDLTLLNHSMKPTDCTVTLQVAHMSNQDIEKTGAEDHLGITAREAASQKLMVPGSTAHRALSSKPQHFQVRVKVFEARQLMGNNIKPVVKVSIAGQQHQTRIKMGNNPFFNEIFFQNFHEVPAKFFDETILIQVVNSSAMRYKAEIGRFQTDIGFIYHSPGHTLLRKWLGLCQPNNPGSGVTGYLKVTIYALGVGDQALIDQKLLYGTDDTDIQIFKSAVVPINMAYLQLFIYCAEDLHLKKHQSVNPQLEVELIGEKLRTHMQTQTDNPIWNQILTFRIQLPCLSSYIKFRVLDCRKKDCPDEIGTASLSLNQISSTGEEIEGVYSGFLPCFGPSFLTLHGGKKAPFRIQEEGACIPDSVRDGLAYRGRVFLELITQIKSYQDSTIKDLSHEVTRIEKHQNRQKYGLCVIFLSCTMMPNFKELIHFEVSIGHYGNKMDLNYKPLVSSTPYSPVIYDGNIYHYVPWYNTKPVVAVTSNWEDVSFRMNCLNLLHFTRDRLKANLDTLKSTRNPKDPALLYQWEKLLRELAEDCKRPLPCMTYQPKATSLDRKRWQLRSLLLQELAQKAKQAKPKDMVATAEDWLYRLNTVLPEPQMGLPDVMIWLVAKEQRVAYAQVPAHSVLFSPAGALHSGRLCGKIQTLFLQYPEGEGQKDVLPAHLRVCMWLGNVTDSKDLQLLRQGDTAVYAEMYENQAKYKDQWGQQGLYHCPNFSDVMGNKTLPMTDFQPPLGWHWQDSWTVEPQRRLLLDIDINKSQVLEEVYENQGRDTRGAWGPAAIPNTDVNGQPMEARENVKCPQGWHFKKDWVVELNHAVDSKGWEYGVGIPPSGLPQVWSPVEKTYHSCRRRRWARVRFRNHGELSHEQETLSFLQLGLAKGEEEGWEYDTFGSKFHLNPQPQSRFRRRCWRRRLAPNKDKGIAPIFLLEGSLAMDLKYHAGKEEDSKTWPWGLDRQFRDPQRQDTRPPNLPFIYCTFNKPHYYQLFCYIYQARNLVSNQILTFQGPFIRVVFLNHSQCTQTLRSSAGPTWAQTLIFQHLLLYENPQDTKESPPLVVLELWQRDFWGKESLWGRSVWPPMVWLDLQDRILPPMRWHPLVKELGKEEGEILASCELILQTEKLGEKQLPILSVPWKNGAYTLPKSIQPTIKRMAIEILAWGLRNMKKASSPQLLVEFGEESLRTEPIRDFQTNPNFPESESVLVLTVLMPTEEAYALPLVVKVVDNWAFGQQTVTGQANIDFLQPYFCDPWAQDYMHPKLPTLSEKKHQDFLGYLYRKFWFKSSKAEDEYEHEVDWWSKLFWATDEHKSLKYKYKDYHTLKVYECELEAVPAFQGLQDFCQTFKLYQEQPKLDSPVVGEFKGLFRIYPFPENPEAPKPPLQFLVWPEREDFPQPCLVRVYMVRAINLQPQDYNGLCDPYVILKLGKTELGNRDMYQPNTLDPIFGMMFELTCNIPLEKDLEIQLYDFDLFSPDDKIGTTVIDLENRLLSGFGAHCGLSKSYCQSGPFRWRDQMPPSYLLERYAKRKGLPPPLFSPEEDAVFYNGKKFKLQSFEPKTPTVHGLGPKKERLALYLLHTQGLVPEHVETRTLYSHSQPGIDQGKVQMWVDIFPKKLGPPGPQVNINPRKPKRYELRCIIWKTANVDLVDDNLSREKTSDIYIKGWLYGLEKDMQKTDIHYHSLTGEADFNWRFIFTMDYLAAERTCVQSQKDYIWSLDATSMKFPARLIIQVWDNDIFSPDDFLGVLELDLSDMPLPARHAKQCSIRMMDADPKWPYFIQYKHFSLFKKKTVTGWWPCQVLDGGKWRLSGKVKMSLEILSEKEALIKPAGRGQSEPNQYPTLHPPLRTNTSFTWLRSPVQNFCYIFWKRYRFKLIAFMVISIIALMLFNFIYSAPHYLAMSWIKPQLQLYPPIKIFNIINSLNTSNASSSILPTQDPNLKPTIDHEWKLHPGPTNHLSDIFPELPAPGD
The following text describes a protein:
Function:
Has dual calcium-independent phospholipase and O-acyltransferase activities with a potential role in glycerophospholipid homeostasis and remodeling of acyl groups of lipophilic alcohols present in acidic cellular compartments. Catalyzes hydrolysis of the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 or A2 activity) and transfer it to the hydroxyl group at the first carbon of lipophilic alcohols (O-acyltransferase activity). Among preferred fatty acyl donors are phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols and phosphatidylserines. Favors sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of phosphatidylcholines, phosphatidylethanolamines, and phosphatidylglycerols (By similarity). Among preferred fatty acyl acceptors are natural lipophilic alcohols including short-chain ceramide N-acetyl-sphingosine (C2 ceramide), alkylacylglycerols, monoacylglycerols, and acylethanolamides such as anandamide and oleoylethanolamide. Selectively hydrolyzes the sn-1 fatty acyl group of truncated oxidized phospholipids and may play a role in detoxification of reactive oxidized phospholipids during oxidative stress (By similarity). Required for normal phospholipid degradation in alveolar macrophages with potential implications in the clearance of pulmonary surfactant, which is mainly composed of dipalmitoylphosphatidylcholine (1,2-dihexadecanoyl-sn-glycero-3-phosphocholine) (By similarity). Involved in the first step of bis(monoacylglycero)phosphate (BMP) de novo synthesis from phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) (By similarity). BMP is an important player in cargo sorting and degradation, regulation of cellular cholesterol levels and intercellular communication. At neutral pH, hydrolyzes the sn-1 fatty acyl group of the lysophosphatidylcholines (By similarity).
Subcellular Localization:
Secreted. Lysosome. Membrane; Peripheral membrane protein.
Sequence:
MGLRRGPCPAALLPGGFLFLLLLADPALLAGRRPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKRTESYFTLWLNLELLLPVIIDCWIDNIRLVYNRTSRATQFPDGVDVRVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVDWGYIRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKNKYIQAFVALGAPWGGVAKTLRVLASGDNNRIPVIRPLKIREQQRSAVSTSWLLPYNYTWSPEKIFVHTPTANYTLRDYHQFFQDIGFKDGWLMRQDTEGLVEAMVPPGVPLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGDGTVNLQSALQCQAWRGHQEHQVSLQALPGSEHIEMLANATTLAYLKRVLLGP
The following text describes a protein:
Function:
Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes.
Subcellular Localization:
Nucleus.
Sequence:
MEIPKLLPARGTLQGGAGGIPAGGGRVHRGPDPPAGQVPTRRLLLLRGPQDGGPGRRREEASTASRGPGPSLLAPRPDQRSGGGGGGGDDFFLVLLDPVGGDVETAGSGQAAGPVLREEAEEGPGLQGGESGANPAGPTALGPRCLSAVPTPAPISAPSPAAAFAGTVTIHNQDLLLRFENGVLTLATPPPHAWEPGAAPAQQPGCLIAPQAGLPHAAHPGDCPELPPDLLLAEPAEPAPAPAPEEEAEGPAAALGPRGPLGSGPGVVLYLCPEAQCGQTFAKKHQLKVHLLTHSSSQGQRPFKCPLGGCGWTFTTSYKLKRHLQSHDKLRPFGCPAEGCGKSFTTVYNLKAHMKGHEQENSFKCEVCEESFPTQAKLSAHQRSHFEPERPYQCAFSGCKKTFITVSALFSHNRAHFREQELFSCSFPGCSKQYDKACRLKIHLRSHTGERPFLCDFDGCGWNFTSMSKLLRHKRKHDDDRRFMCPVEGCGKSFTRAEHLKGHSITHLGTKPFVCPVAGCCARFSARSSLYIHSKKHLQDVDTWKSRCPISTCNKLFTSKHSMKTHMVKRHKVGQDLLAQLEAANSLTPSSELTSQRQNDLSDAEIVSLFSNVPDSTSAALLDTALVNSGILTIDVASVSSTLAGHLPANNNSVGQAVDPPSLMATSDPPQSLDTSLFFGTAATGFQQSSLNMDEVSSVSVGPLGSLDSLAMKNSSPEPQALTPSSKLTVDTDALTPSSTLCENSVSELLTPTKAEWNVHPDSDFFGQEGETQFGFPNAAGNHGSQKETDLITVTGSSFLV