lhallee/plat_data huggingface dataset:
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. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I 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:
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:
MWLDDVASELSFTQGLLLGQLSIVILIGAFIKFFIFGDPPSPDVSAALRATERRSRTLAHKRSLLTLRSSTPRHASQSLNRKRSSVLRNPAPLTTNAILSKTYYNVDSHQPESLDWFNVLIAQTIAQFRADAQHDDAILTSLTKALNGGNRPDFLDEIKVTELSLGEDFPIFSNCRVIPVDEDGITLGREGGAAGREHGRLQARMDVDLSDFITLAVETKLLLNYPKPLVAVLPVALAVSVMRFSGTLSISFVPGSPLNGSPTTLAFCFLDDYRLDLSIRSLVGSRSRLQDVPKIAQLIEARLHTWFDERCVEPRFQQIELPSLWPRKKNTRGGEDLDTGSEAGGIGRARSRDVERDLREEARKEVEAETGVRVGRSKLGVSLDVPDVGLDGGSEEGLRFRRRSRGRGDEYAMPGSMPGLSMA
The following text describes a protein:
Function:
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Subcellular Localization:
Cytoplasm.
Sequence:
MTTIVSVRRDGHVVIGGDGQVTLGNTVMKGNAKKVRRLYNNKVIAGFAGGTADAFTLFELFERKLEMHQGHLTKAAVELAKDWRTDRMLRKLEALLAVADETASLIITGNGDVVQPEDDLIAIGSGGPYAQSAARALLENTELGARDIVEKSLSIAGDICIYTNRFQTIEELTY
The following text describes a protein:
Function:
Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Domain:
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence:
MNVDASSLRNFKDFLQLYNQMTERCFYKCIEHTNSRELSPNEIECTEKCATKFIRFNNKLMMNFVRRQNDIMTRRMKEAEQMMENNQEVSVSNS
The following text describes a protein:
Function:
Required for protein transport between endoplasmic reticulum and Golgi apparatus.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MFGFGNILYVTLLLLNAVAILSEDRFLGRIGWSQSAALGFGDRQDTIKSRILHLIRAIRTVMTFPLIAINTIVIVYNLVLG
The following text describes a protein:
Function:
Ferric reductase involved in adaptation to iron starvation and which is most likely part of the reductive iron assimilatory system (RIA), a siderophore-independent high affinity iron uptake mechanism.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLLVSCLIILLHLQNALSQIIPPNERCVTAVYTAYEYLSFSGQPNKGLWAPRCRNRLHVLSIYAASDLYCSDAEREAGFAQLDDQCRQYAGVDLIPRQEFAPNLTHEAISQMRVVEFGELPKKGPLDTPILISKSYYSRVFRTIDAWQFELWSHYAFGYLGYAYWTVVIAAGALHKLVLHAISVKRAPSLPPFPFLLLIYYWIQTNLIIPAPLASSRRRLLWWTFPGRIHAIVVLLFWILSIVLCLIGYRTFSDNIYWPDISAQLLRYVADRTGILSFANVPLLWLFAGRNNIFIWATGWSYSTFNIFHRHVAWIATLQAVVHTILYTVLFIQSGNAWKKMQKPYLLWGTLAMLAMILVFPFAVDWFRRRTYETFLVLHILFSVVALVGCFYHVIIFEDHEYWFYLWPAVVIWVSDRVLRLIRIVYCNLHVQLGSRSRFQCTECVAAYDKDADIIHLELTPGSGLQPAPGQYYFLYQPFRLTGWESHPFTLGYWSYNDGAPSTQCRSLKRDTTTDVSEIPLLPDTPSSGSDYGSIDTSTDPPERKLALRFWIRPYDGWTRHLRDQCLQSPTRIIQPNILLEGPYGEQCPLWKYESVLLIAGGTGIAAAVPYIQDHILRSSTGQTSTQSIHLVWTARQPALLRDIAGRELKQALSRKDFRVSFYVTSESASQGAIMDGVEFACGRPDLQAIITAHAEEARLGSSSVLVLVCGPSGMAGLARAAVHQAMRWGCRSLRYVEESFDW
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Sequence:
MNGLPILDISGLCKSYGAVRAVDWVDLHVDRGEICGLIGPNGSGKSTFFDCVTGLARPSAGAVKLDGQDITGWSLNDIAREGRMLRSFQKTVVFSALDIEENLVIAGQMFTFPGIWSTFGIGAAARNRVAALRERARELIRIAGLWDVRFQPAGKLSGGQQKLIQFASMLMPEPKLILLDEPMAGINPKLIERVVESIRLANTSFGVSFLIIEHNIDVVTSLCKRVVVLDQGRKLAEGTPDEIVRNQAVREAYLGG
The following text describes a protein:
Function:
Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.
Subcellular Localization:
Periplasm.
Sequence:
MQPTHTLTRLTVIGKLIIASSFFLSLAVQAQQCGQTAPLINERLSYMKDVAGYKAENHLPIEDRIQEEKVINSAMAQAESLGLNGESIKPLMVAQINAAKAIQYRYRADWLSQPEPGWQPKPLDDVRANIGELSTKILEQIAEELKTCKPAEMGDKAHFINTIRQHNLTSADVEAIFSTFNQVKLK
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MREMIWKVIVIFFVKVVKGVIINEIIEGELSIEKINPTFSYSIDFTSDEPIRQYTMLIGKEILNKQEIILELPNITSGIINCIENHIGFTIKRTKTKGLLNEYIMRYQGNLCPMSFYKTIICIINVYCLQSQIISKAPFYQVITNINNNIQRFILEDYVGTKDHWFFIDFYSFIDPIQIESIQKFISIEKNNQYFIEEHFINVKNIGNELDGPFERIQYEEFINESICLKKLQLKLPLESQIDKYYDSTGIIYGYSSKINKNNNIVTIQPRYPLLGGWSTSFSINYHYKFISNNLSILEIPLITNSFPIGVLNYSISIKLPFGMNIKNYWFNPAFNNIFSFKENHALGPFSSQKIQVELNNIVLDQNQIYLMIEYGSVDSYYQVFIKIILLTSLLVIITLINYLTL
The following text describes a protein:
Function:
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MAVALILLLIAIGSVLFHLFSPWWWTPIATNWGYIDDTINITFWITGFVFTAVILFMAYCVFRFHHKEGRQAAYNPENKKLEWWLSVGTGVGVAAMLAPGLVVWHQFVTVPADATEVEIMGQQWQWSFRLPGKDGRLGTSDVRNISPENPMGLNRDDPHGQDDVVIENGDLHLPIGKPVKVLLRSVDVLHDFYVPEFRAKMDMVPGMVTYFWIRPIRTGTFDVLCAELCGAAHYQMRAKVIVEAESDYHAWLEQQKTFAGLSGRNAVVRAKYNSGDD
The following text describes a protein:
Function:
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase 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 the initial step of dolichol-linked oligosaccharide biosynthesis, transfering GlcNAc-1-P from cytosolic UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol embedded in the cytoplasmic leaflet of the endoplasmic reticulum membrane.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSSWRTKREKGHSSGRHQSKVGVALICSSSLVDGICWACYHHHTKAPHSYVGAAVLYLGWICNLYMGMLAVFCTHSINIHAGLNGLEAEQTVVISAAVLIHNIMQIGKSSDPEYQQAHAFSIYLVLCLLTTSLALLSYNWYPSSDSVGDTYTLLEWLWLYFLAIHSATLLLFFLPQVLNFLYSCPQIFKIIPCPRRPLPRFDPQTGLLTGTKDGNLLYGRCTENILCIILLIFQAFSCLLCFCSRHVLAGWYKRGVTANSVKREREQGLKHMNELVAARHKAVHAAEAKRNHQAATIAQQADDIRESSRTVSSFFFWRRCLNKIYNITAFSLAKTFFGILVC
The following text describes a protein:
Function:
Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein. Membrane raft; Single-pass membrane protein.
Sequence:
MQSKFWFEFLQTLPTLPGDTVPVMAIQASPGETSGELIIAQAPNQTLDNNNSALGGLSPLLFFPVVIIAVIFLILVTIFLYTRFYVIAPNNEALVRTGGVFKKEQMVILHGGCIVIPGFHEITRVSLREISIDVVRAGNLAVRTQDYMRANMRVTFYVCITPNRNEILTAAARLSKKGQISEADIKDALEKRADDAIRAAAKKKKLAELDSDKLGFADEVLNLIQGDLRKVGLTLNNIAISEIEESDTYDENNFFDAQGVRLRTETIQRSIQQKREVELTTRVAIEQGELEAEKKSLAIKREQEDANITQQKEIELLKLAQRKELESQEAQQQREIQEAKDKEEAKKERNKILQEQAVEEERIQKELAIQNSQIASAIALEERNKELKVAQALQKQEAEVAEIQRKKTIEASQLQAKAEIALAEQKTQITEQTAAIAIANKQKERLEAEALRAEAESGVITAQEVEAAERAQKLAVIVAQQDAQQHRIAEQNVVEIDVFRRRRQAESARQAAELEAESIRTLADANRHKAMAEAEGQKAIIEAHNSLSNANRTAELLKTIWPELVTQLPDLIKALAPQPGVLGESRIYSFPGLSGSNGNGSNSGDINKLLLSTSGLTLLNGLLNEGKLSTVVDQVKSLLQDPPSVSPPSAAVSEDDWPDLAPPTETNFSPEEI
The following text describes a protein:
Function:
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MTKEFHHVTVLLHETIDMLDVKPEGIYVDATLGGAGHSEYLLSKLSEKGHLYAFDQDQNAIDNAQKRLAPYIEKGMVTFIKDNFRHLQARLREAGVQEIDGICYDLGVSSPQLDQRERGFSYKKDAPLDMRMNQDASLTAYEVVNHYDYHDLVRIFFKYGEDKFSKQIARKIEQAREVKPIETTTELAEIIKLVKPAKELKKKGHPAKQIFQAIRIEVNDELGAADESIQQAMDMLALDGRISVITFHSLEDRLTKQLFKEASTVEVPKGLPFIPDDLKPKMELVSRKPILPSAEELEANNRSHSAKLRVVRKIHK
The following text describes a protein:
Function:
Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
Subcellular Localization:
Host cytoplasm. Host nucleus. Note=Predominantly found in the host nucleus.
Domain:
The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Sequence:
MHGPKATLQDIVLHLEPQNEIPVDLLCHEQLSDSEEENDEIDGVNHQHLPARRAEPQRHTMLCMCCKCEARIKLVVESSADDLRAFQQLFLNTLSFVCPWCASQQ
The following text describes a protein:
Function:
Promotes the exchange of Ras-bound GDP by GTP.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAERVKILKPGLTNRSRSASIDMIVMDEIAKNNPIYTNDNSNNNNNDETSSNISGSNSIQNLSLNNLNNLSGGGGGSNSNSVNNTISERNPDSPRFRSNTGNLQTMMMVSNGNIIGSIQSPSPPISPRAQMTAPNLSKFLDQHTPPPSPKPEHLSGHLRIQQQHHSGIYRNLSFSSVNSSTSFGDFKRSTNLFQPPQSQSQQQQQLQLQQQQQQSMPNLSLGNNINSNNNNNNGSENNDISMEIKDNTSGIDTSVKSFSPRKKRKKENKIIRRIRRWMTWVISSNIWLTIMIISIIFVLFIDDIIGASGSPSSNAIDYSIMAVKCSIIGFFSIDIILNLFCFQQEYFPGTIVFWLDLISLISIVTDIHHFQNYYANLVLSITVNTRIIRICGSFIRISLISTLYNRFLRKQTLPSEGLEVEASKLGDKLIRLTTNKIVLLALAVLFATQLLVYESDTPTQYIQSTISSFEYLSSTYGLQSPEFTGVFNNYQLNNEKLLFTQISNQKIFNLPDKINSLQERSILKYNYLNSIIWIDNSYYIKYSCILHLCLTVFVILVLITINLLIVNDAHWLVINPLENVLTIVKLLSKQNSMIKQGGGGSGIVGGFSNNTINSNSNLNSNSNLNSNSNSNLVRNRVESIGNKSDTADTTSSSGIDNEEPDEADFLLGMLNEIDDSLQAAKEKVEEESIQNSILKKDIEDLYVEKYILQVHLRSIVRKINFHDPIGHYLKNRQLLLMQSNATFNTLEQDSEDDIRFKLNDDGLPDLNVIQYATIDKLIEKLTMAEAHDLKFANVFLLTYRKFLSPVELMERLTIRFCVTPTMELPEKLLASKEQVEQWRKTKQEQIRTSVFNTIKLWIGIYNWDFYENPDLYELFNNLVNKIMPFCKMEKHATYIDSIHKRKMATYIQDPPYIPIEPLTQEEIAETMVLEDRLLFNFDISDIAIQITLMEFDLFKNIKSKEFLNLAWTHKTEKTRLSPNIVRFIEHFNSVSFWLQTCIVKSGKIKERVAVLKKVIALADVFVQLNNYYGAMEVLSSLESSAVSRLHKTWEQVPQSSIQSLQSLQKLLSPQENFKNYRERISKCGSCCIPYIGLYLSDLTFIHEGNPDYYQQSQLINFSKLREVAITINTIKQFQNIFYYYEKNQNIRSQMNFKSPGADIIWKMSLSCEQRNK
The following text describes a protein:
Function:
Catalyzes the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Key transducer of G protein-coupled receptor signaling: activated by G(q)/G(11) G alpha proteins downstream of G protein-coupled receptors activation (By similarity). In neutrophils, participates in a phospholipase C-activating N-formyl peptide-activated GPCR (G protein-coupled receptor) signaling pathway by promoting RASGRP4 activation by DAG, to promote neutrophil functional responses (By similarity).
Subcellular Localization:
Cytoplasm. Membrane. Nucleus. Note=And particulate fractions.
Sequence:
MAGARPGVHALQLEPPTVVETLRRGSKFIKWDEEASSRNLVTLRLDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDTRLEEKLMTVVAGPDPVNTTFLNFMAVQDDTVKVWSEELFKLAMNILAQNAPEHVLRKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALICGLNFNRSESIRPDEFSLEIFERFLNKLLLRPDIDKILLEIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRSSQARLLIEKYEPNKQFLERDQMSMEGFSRYLGGEENGILPLEALDLSMDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGEALLIDPLDKYPLSAGTPLPSPQDLMGRILVKNKKRHRPSTGVPDSSVAKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKTSLEPQKSLGEEGLNRGPNVLMPDRDREDEEEDEEEEETTDPKKPTTDEGTASSEVNATEEMSTLVNYVEPVKFKSFEASRKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDLPMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIVDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGRFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYTEASDYIPDDHQDYAEALINPIKHVSLMDQRAKQLAALIGESEAQASTEMCQETPSQQQGSQLSSNPVPNPLDDSPRWPPGPTTSPTSTSLSSPGQRDDLIASILSEVTPTPLEELRSHKAMVKLRSRQDRDLRELHKKHQRKAVALTRRLLDGLAQARAEGKCRPSSSALSRATNVEDVKEEEKEAARQYREFQNRQVQSLLELREAQADAETERRLEHLKQAQQRLREVVLDAHTTQFKRLKELNEREKKELQKILDRKRNNSISEAKTREKHKKEVELTEINRRHITESVNSIRRLEEAQKQRHERLLAGQQQVLQQLVEEEPKLVAQLTQECQEQRERLPQEIRRCLLGETSEGLGDGPLVACASNGHAAGSGGHQSGADSESQEENTQL
The following text describes a protein:
Function:
Has a role in sister chromatid separation.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Cytoplasm, cytoskeleton, spindle. Note=Spindle pole body during metaphase and spindle microtubules during anaphase.
Sequence:
MELDDFNSRILSQIFDKSWKVRFEAYESLLHALNRALDDSDVCFQPWIHDPALWKQGLCDSNVPTQEHAVKSLRCFLDKSRQKGVNSAKSFVVAPLLEKCLPSPRQSIRDASHQALLILAKSDALDYVLEGLFSAARVKHPKQAVASIKELNSLLENFGIPALSPIPFYKLIPTLFAQSDKNIRQEASNLSITLYAWVGNAFKTHVFPQLKQIQVSDLEASFQNVTSRTTTGGHISNSLNTQEVVLPSFSSNAKPKPHLSSKSSSQGNTLQRSTSSFSTPNRKVSQPSDFSASPSRSIVSPAKNIVGSTPVDVLSKLTPEFHTALSSPKWKDRKEALESMVPVCSNPVYQEGDYSELLRVIAKSLKDANVVVVGVAALLLTHIAKALRKGFLPYTGIVLPSLFDRFKERKSSLVHSLLDAANAIFESCGLNDIMDETLEFLKHKNPQVKTETLRWLNRCLQLTDVCPPRASLETLCSLCVTLINDTFEPVRMATTNVLATLVQIFSQPVLSKYIVGLDPKKLPKILELSKDITVNAHPNQPSRPRLPRVASPLKTSPVKLAVTPQAPSPLPSSNPSQASLTEESLSTRSSPTKPSTTSLRSQSLVNRFASSTLKAPSSSSKGVSNAASSKQSFPSSPSISKKLETSRLSTKKLPGSTMKAASALKEYPQQQSMKSGGEKQDNLVTITMSEKVELDLLREEKAIRQVQEAEDALERERLFREINDLQIQNAEMKEQVYEKESTISQKEVEITSLRNEKDRLSTRLQQVLLELEKQHETNEEAMDIDLKVPESGAIGRVTTRATATTAMDESGNAGMVSSGIHSVSTKPSSYGTRRSLAGSMLQKPTQFSRPSFMFSPEARDNWRESHDLSSHLWEQIQRMKKA
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MGNEKGTEKILNLILEIIWLLTGEECVVVKKNGEQITDGVNQIHIPKMDPPPNSSARNRAPHLPITEVPLGYEGVSVCLSPEGWKYTARHKGSAGADPDVAVNNTNSELRVEEILMEPDTSADCNRNTPEIHRWSAPNYTDGDNVAPHNYQVQPAAMMVPHNYKEEEIPTEISVGESADRIIPPKSPILQYQTVQGAEQGLTQNYQIEPPDTISQQERCDDDVVLPQHCREDAQCKMEEEEIYAEPAGLGNQLNTSPTYHPNLVHETDLSQNAKQYQREHCASGKPHNLVVDTGFHSEEFQNPAAFPRGHAGRSQALNRSLQGSPCAQPITSVKQKHAVDRREFRNNLEFTLHLKSHSREPMGSGSSESFANHSGFALQTMQRGQCVRAVLTRTKMAAQQCIQAANKGYVCPTCGKGFSQKSDLIVHQRIHTGEKPFVCSDCGKSFTQRGHRTSHMRSHTGEKPFSCAECGKRFTRKSTLIVHQRSHTHSKYACSDCGACFTKHAVLAAHQKTHIK
The following text describes a protein:
Function:
Can cross-link actin filaments into both network and bundle structures. May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, stress fiber.
Sequence:
MEELIVELRLFLELLDHEYLTSTVREKKAVLTNILLRMQSSKGFEVKDHAQKAETNNLPAPPQMPLPEIPQPWLPPDSGPPPLPTSSLPEGYYEEAVPLSPGKAPEYITSNYDSEAMGSSYESYDEEEEDGKGKKTQHQCHHEEASMDLVKDAKICAFLLRKKRFGQWTKLLCVIKDTKLLCYKSSKDQQPQMELPLQGCSITYIPRDSKKKKHELKITQQGTDPLVLAVQSKEQAEQWLKVIKEAYSGCSGPVDPECSPPPSASVPVNKAELEKKLSSERPSSDGEGVVENGVTTCNGKEQAKRKKPSKSEAKGTVSKVTGKKITKIIGLGKKKPSTDEQTSSAEEDVPTCGYLNVLSNSRWRERWCRVKDSKLILHKDRADLKTHIVSIPLRGCEVIPGLDSKHPLTFRLLRNGQEVAVLEASSSEDMGRWIGILLAETGSSTDPGALHYDYIDVEMSANVIQTAKQTFCFMNRRAVSTSPYLGSLSNGYAHPSGTALHYDDVPCVNGSLKNKKPPASSNGLPVKGRAPSSQQKKVESAGGVKRTASNAEQYKYGKNRVEADAKRLQSKEEELLKRKEALRNRLAQLRKERKDLRAAIEVNAGRKTQVALEDKLKRLEEECKQREAERVSLELELTEVKESLKKALAGGVTLGLAIEPKSGTSSPQSPVFRHRTLENSPISSCDTSDAEGPLPVNSAAVLKKSQPSSSSSPCRGHVLQKAREWELKNGT
The following text describes a protein:
Function:
Alcohol dehydrogenase specific for ethanol. Acts mainyl as a mitochondrial formaldehyde dehydrogenase and has no effect on ethanol production. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all. The role of ADH4 in yeast metabolism is not yet known, but ADH4 is not responsible for the production of ethanol during growth on glucose nor responsible for the oxidation of ethanol to acetaldehyde.
Miscellaneous:
MISCELLANEOUS: While ADH4 is expressed at only low levels in laboratory strains, it is often highly expressed in brewing strains; MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion.
Sequence:
MSSVTGFYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAKKRLGEIALHFGASQEDPEETIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKAYEY
The following text describes a protein:
Function:
Required for secondary wall formation in fibers, especially in short days conditions. Promotes indole metabolism and transport (e.g. tryptophan, neoglucobrassicin and auxin (indole-3-acetic acid)). May prevent salicylic-acid (SA) accumulation.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein. Note=Also detected in transvacuolar strands.
Sequence:
MADNTDNRRSLWGVPEKLQLHIAMLTLQFGYAGFHVVSRAALNMGISKLVFPVYRNIIALLLLLPFAYFLEKKERPAITLNFLIQFFFLALIGITANQGFYLLGLDNTSPTFASSMQNSVPAITFLMAALLRIEKVRINRRDGISKILGTALCVAGASVITLYKGPTIYTPASHLHAHLLTTNSAVLAPLGNAAPKNWTLGCIYLIGHCLSWSGWLVFQAPVLKSYPARLSVTSYTCFFGIIQFLIIAAFCERDSQAWVFHSGWELFTILYAGIVASGIAFAVQIWCIDRGGPVFVAVYQPVQTLVVAIMASIALGEEFYLGGIIGAVLIIAGLYFVLYGKSEERKFAALEKAAIQSSAEHGIERAPVSRNSIKSSITTPLLHQSTDNV
The following text describes a protein:
Function:
Regulates the transcription of genes required for cell separation.
Subcellular Localization:
Nucleus.
Sequence:
MSLSYLSSSSQKSFESFRQEESPACNHSYQRDYETFGDSKHTSFSSFAPFENEVSLNQAVIPSPPSHLQNFQDQFDYSSVLKTPFNPLLEANSAYFLSNQISLPDSHSYASSFDASLSPPSSPLTCVSQIHTEQNFNNNDAFSLTNSQQAFSEIGYDASNWIDELDSQQQVLSFPEFDIPEIKTETCSNKDHLENFDYLSSSIPETSGPASSVLPSSSQLESFNEFMFLPSSPPGLDEINGAPSFEELNFQISQPSPAHPVDLSSPETAPNISPVSPFAQLVKLEPTSPQKPSFALDSSFSHLDVCRHTDNQKAFAKLSSPAEYVSEFEKFSSVCDHGLDISNANINNTLTQQFALSAPYESCIVTKKPEPCITVKEEEQLAPKIESADLSITPQVTEHDSKPPVRISYDHRCKTRKQSTRICRIPPETMASLYCGPEADGKYVCLYNGCNKRIARKYNVESHIQTHLSDRPYRCDLCKAGFVRHHDLKRHLRIHENGRPYVCECLKRFNRLDALNRHKQRNICVGGVDRRQH
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MDLGSMTSAAKVLNVAQPALSQHIASLEADFKCKLLDRSARGVKPTEAGRILYRYSKSIQRQIEEARRTILDNKPELTGNVTIGLAPLSSAALLATPLLTQIRERYPGIVPHIYDSSGVMLSEMMLKGSMDMAVLYGERPVTGLDYKPLMREYFYLVAPRGMYPEQMPPEEVSAAEVAQFDLLLPYRESFLRQTVERVCAEVGLRPRIVAEIHSQSTLSSAIAAGVGAAVLPMSIAKELPNLDELCIRRINAPSASQQMSLCISDNAALSDAAFAVYKILLEIIVKTWGPFEAQLGSVAIASGGPASPPDEPKDEP
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 homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome.
Sequence:
MSSSIVLSNNNSNSNSMSMIGQSPPCCSDVPNTPASEEMTRMVKNVVASWEWVPLGKDKVGIIIPADQDHRQVHKSRFVDLLEFCDETMKVKEVIAVFGRADLTVAAGFPRTLRYVGFRVVAPENFPPTLDATTHFAMTYVV
The following text describes a protein:
Function:
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Sequence:
MRIYDPFRKKWIEEEIETPFPSKGLVATFPFVDLHVHVRLNGGEDYSSLEEASLVGGFFKVVVQPNTKPLIDSKEVLERHLDLSKNRAVEFLFAVSPFGSIEAEGERVVGFSTDGIEYDYPTLVETMKKKKKALWFDHSQMYEVDGIFYEGAPLPFQKRPRSNEAIAIARTVLTGLEYGFERFHIQHVTTKYSVEVISFLKNLAKVSCEVTPHHLFFCYEDIKNTNFKINPPLGSPEDRRALIEAVKKDVIDVLATDHAPHHEKPDDFLTAPYGSTSIEIAFPAYYTALGDLELVVKKLTKKPLEVLGVEARLTEDTLVFIDPEAEFIVDAKKFKSKGKNSMFDGVRLKGKVVALKLKGRWVMIDGEVIADQKEND
The following text describes a protein:
Function:
RNA helicase.
Subcellular Localization:
Cytoplasm, cytosol. Cytoplasmic granule. Mitochondrion. Nucleus.
Domain:
The helicase domain is involved in the stimulation of RELA transcriptional activity.
Sequence:
MAAETGSGKTGAFSIPVIQIVYETLKDQQEGKKGKTTIKTGASVLNKWQMNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLMKGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEEEFKFPPKDGFVALSKAPDGYIVKSQHSGNAQVTQTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSVPDTVHHVVVPVNPKTDRLWERLGKSHIRTDDVHAKDNTRPGANSPEMWSEAIKILKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLEQYFIQQGGGPDKKGHQFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAISLVATEKEKVWYHVCSSRGKGCYNTRLKEDGGCTIWYNEMQLLSEIEEHLNCTISQVEPDIKVPVDEFDGKVTYGQKRAAGGGSYKGHVDILAPTVQELAALEKEAQTSFLHLGYLPNQLFRTF
The following text describes a protein:
Function:
Transfers mannosyl residues to the hydroxyl group of serine or threonine residues.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Endoplasmic reticulum.
Sequence:
MPSLEPWLWGDSCSWLGMLAMLRLRLHKSNMDFTCLFCCSLAFVLYLNTLGAGFVYDDRRAILANADVSGGTPWQRSFSNDFWGTPLTDSGSHGSWRPLCVLSFRLNYLIGGGFAPWGFHLVNNLLHCVATALVVRVARTLLASVWAVLAAGALFAAHPIHTEAVAGVVGRADLAACVCYLLTYLSYLRHMRWRESGDPRQWLALGATLILAAAGLLCKETAITALLVCALFDVMRGLSGQVDKQRLRSVCIVLGALFCMAYCRLVIVPGPQTAFSSADNPIARTPSAWTRLLTFLYLPVFNLRLLLQPNVLSFDWGMDALPRVTSLWDRRNAQSACFYSVLVGVAWGSCRQLLSGSKEVTHCGVSSTFPQYHIQKVASRKSRSKRKRLANNTKYQAFEAAYHQQQQEALPCRDCNNNNSSGYVYEGSSPVAQAPAQAPHLVSSAFRGSRSSSSCSNSTNSSSSSSSSSSSSSSSSSSLSGGFQCSSKDYALEGMSPANRHACVLIMSLSFLALPFLPASNLLFYVGFVVAERLLYLPSVGFCLLVGYGVSKLMSCNQRTRNILLLSFSLLLAAMSLRTLRRNADWRDEESLYRSAIAINPPKALGNLGSVLSSQGRYEEAKQVLQEAIRFRPNMADVHFNLGILHQNQQVYPAAVECFQRAIKFRPNLAVAYLNLGISFIALGKRQQAIEILQAGSNLDGAAVRDRTAHDQARSSAYLQLGALYVEQGKLQRALAIYREALSSLPGLPQQREILYQRIGDVLGRLQQWDEAERHHRAALELQPNQVAAHLSYGITLARNSSRASEAEMWFKRALKLAPEQASVYHHYAEFLSLQSRHHESAIYHRRAAELAPNDYTLVVAAATAMRLLDRKVDAEMWYRKAVALRPGDAHAHTNLGAILHLLGRTNHAAASYKAALRLQPGDAITLGNLAKLGVTNV