lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum. Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway. Binds cholesterol via its SSD domain.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MVEMGEAAEYGMVSKMREMVSRMFYNYGLFCSNYPIALIVFSVVIAVLCSLPCFFAVPLTLTAPYQYTTPLKGFPDTARKFYTKQLPDNKTAIDHSKRPQWFSRPPVGYVLQVVINASVSPWQPGLTYGDDVRGPLSKAFELDKEIKSFSSKSNVLLRSSCLYVSDVADHVKGVMPEHSCLVVSPANVWQGSFDRFQEDPYPGRSVFMGNFYDKPALHDLLLGVQAKYTGLQKYNIHSVSPQISFAVTVVFHTYNDSFIEELKSHLEERFNMGSPSLDWNTGEFLILHIYYKSLINSDDFMPAAIIYALLMFYIYFSVRKIEMVKSKWGLALSATVMLVLSCTMSAGLCIQYGVEPTLNEGEVFPYIIILIGLENILVLIKSVTSTPMDLPVELRIAQGLSKEGWSISKNMWTEILIVVIGLFTFVSAVQEFCLLALVAMFSDFFLQMMFFVSILALDFRRLEISDLYKSGMMQTLQDSPDGARPSRTHHRSFLSPFWGQPIEEPAPTPRIPRRLRVFNFLASIRIIQKIIKFTLALWIIVTCLFIYKAGIINFFLVSNIYGSPLEPSTTHSAPTPLDPTLPLVPPLNDPYHTLDKTGQVPDPDASDKVNDPSLPVLKAGDSPKASDQKGDDKVKDKTKSGSDGSDGSLLDLKPCHGSDCSDKLSLWVRQRGLWKLSAWHWPALFNMYNISLADRYVSILPPIKLNIHISPEEAVALRKDSETKRYGSSPGVGQIIGSYEGLHEADRWDYYVTMMLGIISGASSVILMMLLCKCATLVRSRQARYKPGRRADIVKRVQGPCEAVPLHLTGHEQEVECFVTGGRWVVSACIQGDIRIWDPNEGRCEHFIPRTRYRLNNKSSSLPRQPISPTQPLKTPNHSSVPSSPFSPLYTDPPQTTEGAAPNSARDLNTHFCSEVIMPRPGSSKDLSSHFSGSHEAGIPRPGSSKDLSSHFCASQEGGMPRPGSSKDLAGMHFSMDGYYANGEQVYSAARHPSQSSSRSSGVASCDDDPYLQQHTKSRTHSTVSADFSQVDMFGSPQEREGVVDPAGVGGGHCAPHGGGGGDGAGVCSTVWCLACKDELVAAGCSDGSVELWSSENGQLLAWSPYKGDQSQPGITGVCFCRNLLVVARLGGSLDFLQISGFNGVGVTVSYDSYYQYPPVVHLTLLKTVQAHQQPINTIQANEAQLITASQDYTLKVYSLDDLSCRFTLRGHAGSVTSLYVDKDPFISMASGSTDGLVRLWDTSRGDMLKALKGPTSTVLSITCTSQHVLCVSLDNKLCVWTRLQGWMLHVIQLDGGCSSSVATLNDKLMITGAQGYLVVWDIVSGEPIRELNLGDKHVRVKNILPVDNSPTIVCDFGSELRLIQFPPSLEKID
The following text describes a protein:
Function:
Stabilizing subunit of the ethanolamine phosphate transferase 3 and ethanolamine phosphate transferase 2 complexes that sequentially transfer an ethanolamine phosphate (EtNP) from a phosphatidylethanolamine (PE) to the 6-OH position of the third alpha-1,2-linked mannose and the second alpha-1,6-linked mannose of the alpha-D-Man-(1->2)-alpha-D-Man-(1->6)-2-PEtn-alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol (also termed H6) intermediate to generate a 6-PEtn-alpha-D-Man-(1->2)-6-PEtn-alpha-D-Man-(1->6)-2-PEtn-alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol (also termed H8). Participates in the tenth and eleventh steps of the glycosylphosphatidylinositol-anchor biosynthesis, in association with PIGO and PIGG, respectively.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MKDNDIKRLLYTHLLCIFSIILSVFIPSLFLENFSILETHLTWLCICSGFVTAVNLVLYLVVKPNTSSKRSSLSHKVTGFLKCCIYFLMSCFSFHVIFVLYGAPLIELALETFLFAVILSTFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFVGAWLGALPIPLDWERPWQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN
The following text describes a protein:
Function:
Required for cell fusion, independently of fus1. Appears to have a role in transporting proteins that are involved in mating. May act as a scaffold to retain cell fusion proteins in the cisternae of the Golgi. Degraded at the onset of mating and this leads to release of cell fusion proteins.
Subcellular Localization:
Golgi apparatus.
Sequence:
MDDTNQFMVSVAKIDAGMAILLTPSFHIIEFPSVLLPNDATAGSIIDISVHHNKEEEIARETAFDDVQKEIFETYGQKLPSPPVLKLKNATQTSIVLEWDPLQLSTARLKSLCLYRNNVRVLNISNPMTTHNAKLSGLSLDTEYDFSLVLDTTAGTFPSKHITIKTLRMIDLTGIQVCVGNMVPNEMEALQKCIERIHARPIQTSVRIDTTHFICSSTGGPEYEKAKAANIPILGLDYLLKCESEGRLVNVSGFYIENRASYNANASINSVEAAQNAAPNLNATTEQPKNTAEVAQGAASAKAPQQTTQQGTQNSANAEPSSSASVPAEAPETEAEQSIDVSSDIGLRSDSSKPNEAPTSSENIKADQPENSTKQENPEEDMQIKDAEEHSNLESTPAAQQTSEVEANNHQEKPSSLPAVEQINVNEENNTPETEGLEDEKEENNTAAESLINQEETTSGEAVTKSTVESSANEEEAEPNEIIEENAVKSLLNQEGPATNEEVEKNNANSENANGLTDEKIIEAPLDTKENSDDDKPSPAAAEDIGTNGAIEEIPQVSEVLEPEKAHTTNLQLNALDKEEDLNITTVKQSSEPTADDNLIPNKEAEIIQSSDEFESVNID
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.
Sequence:
MELELGQNWDRCLADVVVKIGTAFRSGMGLGMAYSNCHAPYLLHGKYVKEQEQ
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
ISPYFCVVKAIQKDPLSNALLQPSSLHLFVLLPLHHQLIISFSPDQRSRVQSVGRSRMSESRDSGVGSKSRRPALLVEGLKLTQIKGGKQSTVSSSITVTQTVSEQTPFLCRKPPFSCKHCGKTFTMKGNLKIHIRTHTGEKPFECGECGKCFRHRSHLRTHSRTHTGEKPFPCNRCERSFYQKSHLRDHMKSHSEECVHHEALNVGEYRARNSSRCEQAFSQ
The following text describes a protein:
Function:
Regulates synaptic membrane exocytosis.
Subcellular Localization:
Synapse.
Sequence:
MFNGEPGPASAGASRNVVRSSSISGEICGSQQAGGGAGTTTAKKRRSSLGAKMVAIVGLTQWSKSTLQLPQPEGATKKLRSNIRRSTETGIAVEMRSRVTRQGSRESTDGSTNSNSSEGTFIFPTRLGAESQFSDFLDGLGPAQIVGRQTLATPPMGDVHIAIMDRSGQLEVEVIEARGLTPKPGSKSLPATYIKAYLLENGACVAKKKTKVAKKTCDPLYQQALLFDEGPQGKVLQVIVWGDYGRMDHKCFMGMAQIMLDELDLSAAVTGWYKLFPTSSVADSTLGSLTRRLSQSSLESATSPSCS
The following text describes a protein:
Function:
Facilitates degradation of misfolded endoplasmic reticulum (ER) proteins through the recruitment of components of the proteasome and endoplasmic reticulum-associated degradation (ERAD) system (By similarity). Involved in ER stress response.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSSLSGHASTIQPSCLGFCGRTVLVGNYSEDVEATTTAAGSTSLSRCGPCSFGYRNNAMSICESCDTPLQPYDWMYLLFIALLPLLLHMQFIRIARKYCRTRYYEVSEYLCVILENVIACVIAVLIYPPRFTFFLNGCSKTDIKEWYPACYNPRIGYTKTMRCTYEVVFPLYSITFIHHLILIGSILVLRSTLYCVLLYKTYNGKPFYAAIVSVPILAVIHAVLSGVVFYTFPYILLIGSLWAMCFHLALEGKRPLKEMIVRIATSPTHLIFLSITMLMLSFGVIAIIAPLDIPYRWSFLCIVPVPFIFYMATIPFSNPTTTMRLS
The following text describes a protein:
Function:
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Subcellular Localization:
Chromosome, centromere, kinetochore. Nucleus.
Sequence:
MPINSRRQTLGAVSAKPPMPSSMSRPTTTASTTTTPSTSSLASDASRKKIPRSRKSMIPRMAGSENAVNQQQQQQQHVMSAASPSAKSKGSRIAAPSPSRVPKSSSRPPAAAAAAAASSRKSLGGPIILSSATPSKNRRVSLAPSSSATHSSSQYTTTDPRDIKDKSYLNNSIRKMVSYLKSHGYDSSPLNVKQLVNGPSGRDFNHFMTFLLRRVDPTFNSTYGGSIATTSTTGAAKRSDDPPIKFEDEVSMAFRTLGYPFPISKTGIVAVGAPHTWPALIAAIDWLIDVLVLVEGEERMEWEVEMSVVNGEGGGGGEEVVEEEQLYSLESNALRAQHQFDAFLRKSMVAFMNDDNEECDELEGELLEVWNGDNEKVDGYLAGLDEECGRMREEMKRLEREGQGLSEAHQKREEYATDIEKFLTLIEQLNEHQAELQQKVSTLTSEKTTMEQQMKECDTKITQLKDTIGSQELSVDDVRKMERQKVRVEEQLQQKRDVLDGHENALKEAQEKWLKCFQLLQQTVDEYNSKGTSLELIPENAKLAKGQKLEIRLDEERALDGIVEMMGGVDVANVVKPYVQKLTEDYKSEAFNEKERVVELKENIESMESLSEQLAEDIEDIKQKITSCQEESTAEQEKLESEIKSKRRQLELLQTKITTLNDPKGTEATIEKYNAQYKQLQALQLKQDKENTAKKNAVAEEIRNAVEKAQKHQDFVKKAISEMNGYLKKKEEECMKLELLDS
The following text describes a protein:
Function:
Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly. Plays a role in positioning spindle poles during mitosis, specifically at prometaphase.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton, spindle. Note=Localizes at the central spindle.
Sequence:
MSKKLKEQAANDASEGDAIKVFVRVRPSESHDADAAFGQCLEVRLPDTIIMHSKPEPKVFTYDHVTAANTTQESVFTAVGKRIIESCVGGFNGTIFAYGQTGSGKTFTMLGPCEDGDNFHHEMRGVIPRSFEYLFSLVNREREKHGDRYEFLCRCSFLEIYNEQIYDLLDPASLGLHLRENMKKGVFVDGLIERAVASASEAYGVLQAGWHNRRVAATSMNRESSRSHAVFTVSIESKEKKAGVSNIRVSQLHLVDLAGSERQKDTKAIGVRLKEAGSINKSLSILGNVIMALVDIAHGKQRHVPYRDSKLSFLLRDSLGGNAKTYIIANVHPDAKCFGETLSTLKFARRAKMIKNRAVVNEDTQGNVMHLQAEIRRLREALCMKGAEGSIPRGPSESGDSQMSNSSTESNGPVSGQQSGSSSSSKWKKYFLEAMSLRDIVEVEKREMREKVSSLEELCSKRDQVISSNKMIIKFRNSTIDMLQKTKNKALLKEDRDLLNENLKKEIEQLQEQLEHNPFVMRYVVENQSLRAQNKKLKMMEAVRSGEAMAATKAEELETLFLELREGLSKNRRYSSTPVDGEKVPTSTLVILKSQIKKLQDELENAKQEHAEQEEMTRTTRLDLESELAAYKKANLDMEKTLQGMKIKNRMDRDAMNDIHMQTIKSITTPKKVTYQLRSRTVLRTAGEETPGGPGFAGLSDNGSPLRSHSTNSLPPSGDILVTNSSPAMSEEGIIDEEMPEHVIEQCNEALTIELQKLQDKNANLQQQLEEHESQKHKMLQNSSKLDHQLQQITELYSTESQAWQEHEKDLTTRLAEATIQISTLQRDYEMTRGEAEDFKVMLQAADKEIGQEKKQKSKVTQDWDRVRAALDAQVVRLENEMCGQSRELENLTEDREQLQDAYNTLQAEHEFQQQREADLENRLKGKKAEITQLQEEIQKHLEKLDSERDKSMRLTAELRQGDNTKKDLLDAQELIDQFREERDDLLHRLDTEALKLSSSKEDLETVNSALTAIKKTDVEQKEALSSLMAALQGQKGMVKDKEEQLASMQMQLEDTRGQVSLLEAALEEGKASGAGLQSQIAALEDRMHAQAGEYQEQIEQMRADAMDANQHQKELLKELEKQSEELTQLHKQMKEKEEEYETKESEHKDTIESLEEQLEEVKTNLSTVVVELDEPESKKRKMADAQAMEIESLRDSEKRFKELSSVYDNMRDQMNEEIRSLKMKADELEDVRISKEILQAQHTALTYEIEQVRNEMAEKESSLKDEVNHLKRDMERQKTVLASMLRDKDEAVEKLYTVQTTLDQVKANEEILQENMDQVMEELDRTSALESTHFKEKEDIKSKLEEEREEKSKLTKDLTRLKEVYEEAEKKITELGGHQNPKQKIHHLQAVKSENYFLKEEVESLEKQLGKAQSDSEQMKRDYEALQKRLTSSSAEPPEEAGATTCIRCLPHSKRIMQTQTA
The following text describes a protein:
Function:
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster. Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin.
Sequence:
MTLPVLIIGAGLSGLTTARLLTNAHIPCIVFEASPPSRTQGYAISLRDWGFNALLRALGNLPLSSLTRAVAPDRHIGGWGWLDQSWRNNQTGEIIMMPPKESKEKPTILRANRNALRQWIADAGVGEDEEIDVRYGHRLVGVQLLREGGDGNVVTAEFANGATYTGSLLIAADGVHSTVRTLILPAVKPEILPVLVYHGDFKLSREEYECVIRPHAGESTIVAGVGDGFNTPLTVCDVTSTTVHMDWTYSRPSIGDNDPLYNPNITSEEAKVIPEALIEEINAKKLGEPWSLFLNGEAMRRHRVFNWLTRCVSMERSDVNSCTGKGVVFVGDSWHAMPIFGGEGGNHAIFDGIELAKMLEVAWGRSKEDVQAAIGKYYDKSWRRCNDAVRRSKQRFYQLHRPISEWIEIAEKQKMRA
The following text describes a protein:
Function:
Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A; Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
Sequence:
MGTPQKDVTIKSDAPKTVLLEKHAQYIESYGAKKDDYEYCMSEYLRMSGIYWGLTVMDLMGELQRMNKEEILAFIKSCQHDCGGFSASIGHDPHLLYTLSAVQILTLYDSLSTVDSNKIVDYVQSLQKEDGSFAGDKWGEIDTRFSFCAVATLALLGRLDAVNIEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITDQLHQVNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRLFVLACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEERIKPVNPVFCMPEEILQRINIQPELVS
The following text describes a protein:
Function:
Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MENMAEDLRQKAMALEIYNQQLQMIQSEITSIRALKSEIMNSIKTIENIKADEETLIPVGPGVFLKAKIVDDKALIGVKSDIYVEKSFNEVIEDLKKSVEDLDKAEKEGMKKAEELAKAITALRKELQTEIQKAQQAQDKKQ
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Miscellaneous:
MISCELLANEOUS: Present with 2491 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MEKESVYNLALKCAERQLTSMEFSNLYKEFFNEKFPSLIQEEEEDTTTTANINEVKKASDLVDTPSNNTAATADTTHLHEALDIVCSDFVKILNLEKPLILADYIVEVLLVNYNSDMIKCFLPKLNSVRNSLLLAHFFSKSCSFFAKLSDTLIIDQVRKDLGNVIVPNILSLDMNSMNKELIAIVSKLLQTTLKLSPSPILLTSAGCKNGSFTLLNQLSQTNKLLFKRVSQTFEAKLHFKDTKPFLNKDSTNEFVGSPSLTSPQYIPSPLSSTKPPGSVNSAAKYKDMKLLRYYKNIWLNNKIINWEISNPDFLSKYSAITSSIFQESFNSVQNLDQLLTDLIETSFTCFAQFVSNKQYHQANSNLTLLERKWVIFITKHLPLLILENSSRSPRVVTNALDNIDEKVVKAIRIYFTEKDDNKTNNEDLFDDYPSTSLDIRHDFIKGLIMLNLQPASVINNYLREDQMIDTSILPTRDDLFVRNLQGIQEVVHNTNSFIISSLDTLELESITESITHDSSNGLFQVLHNFESVAPTKQREIVKAFLSIFEDAIKELNYNRIAKICALLFFNFSHSLTTILSFSSPAALMKTLIKFVDLSRNGRNGSNGNDESSEYETINISLSFSWAILLIINLTQTYGISVVDVALKYPELSIKNSFIINFISNLPNVSDKYYLEESNVNDSDMLTKSHNTVQSWLCDLFVNGSITDQLIQNIETRQLANLIPFIVKQVLLSVEIGVLTDISSLIGGFEYFLQPLLLVGLIKTFYWLEQFLSCVKNDTISEDILQGIFNLLNTLFNPVTLNEDSKAFHTAVLRLNAIPLLKVLRKFRVQSQSNYGIYSSDAQGDPNLEPLIAKLVAVLNVSPVYDVDPRIINSENDYSRKQLGYGKFLILNENPINKIMTNQINSFWSLHSSTYYNLDYLFELIELVTPKSFLFDVLKTLEYKLATYGVPGSENKRGSLDSEHVFDYFFYFLVLYDVKTAEEASQLIEYMENDAKKSKGDVDIKGEDLHEKNDSAEVRQETQPKAEATQDDDFDMLFGENDTSTQAYEEEEENEDNDGNNRTNNVPMIKAEETPSKTNKISILKRHSFAVLLHERKLLNDLALENGEITKTENEKFISYHDKYLCMLKTCVF
The following text describes a protein:
Function:
Regulator of mitochondrial fusion: acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of pld6/MitoPLD dimers. May act by regulating phospholipid metabolism via pld6/MitoPLD.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein.
Sequence:
MAFQRAEGMSIIQALAMTVAEIPVFLYTTFGQSTFSQLRLSPGLRKVLFATALGTVALALAAHQLKRRKHKKKQITADNGGLKLGGVPGSVLPVRRSSSAKKGYSRSRVQSPSSKSNDTLSGISSLDPSKHSSSSHSLASVVAVNSSSINAAPAGPWESPEMDETLEEGDSNAENLYIQGMELFEEALHKWEQALNVGQRCRSNTPASQVNDLLNQSCSEGLSEDSQSGHFAGKLEALLYRAYNLQEEFGTSIPPDDLLMDLEGSLIFPLVESRRALMMDDEGSSTSEDSFFSAAELFETLQLNEVPFLPTKPAAAYEEALKLVHTGEVACRTLRTELLGCYNDQDFLAKLHCVRQAFEVLLLDDGNQLFFGEVGKQMITGLMQKAEKNPKGFLENYEEMLRYALKQDTWATTQRELKGRGVVCMNFFDIALDFILMDAFEDLESPPSSVLAVLRNRWLSDSFKETALATACWSVLKAKRRLLMVPDGFISHFYSVSEHVSPVLAYGFLGPKEHLTEVCNFFKNQIVQYLKDMFDLDNVRYSTIQSLAEDILHLSRRRSDILLGYLGVETVREMNGAVPVQTTEAELDL
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MELFTINRYDETKLNEDAEKAQEELILQKLQARKEKKARLRTAQTAVELQETANQSSESPVNTVAHESSDETVNGGARADGTENGEQSDEERTETQSGMEQDADESASNNDNEEKVQKTAGAKQLGDFIVLGGDKLHRLKQTDEVLPPWLSHPTIIQHDLSAKGPSIKQQSYLDDRIKANLKSMGFKRLFPVQEKVIPWILEAHQKPAPFWPRDVCISSPTGSGKTLAFAVPVVQLLLKRVAPAIRALVILPVQELAEQVFQVFRQLCDGTNIHPVVLSRGMQLEVEQQKLVKYCNGEYMPKVDIVVTTAGRLIEHLHSTKGFTLRHLRFLIVDEADKVMNQIQNDWLYHLNKHVKHESDEYLLGRTADLLSQSELFDRARQPHKLLFSATFKRDAEKLKTLKLFHPKLFTAVIDPQERTMMAQSTATTQAAEPRRGNFAGQYTTPAELKECICLTEQRSKPLTLYGLIRENGYRKFLVFTNGINTSHRLSFVLQRLFGTDMVIEEWSSSLSPATRKSVLNRFSLGKVNGIICTDALARGIDIENIEVVISYDMPNHIDKYIHRIGRTARAGLRGTAITLLAEDEKKKFNALLKEANKRELETMEVSPSLEEEFAAKYANVLNDLREALELETEVINKIRKGISIGNITRVNLLTKLKDQVDLTYSTEIIKTLKILPKSWTNEEIEQRAMQGMPKKNKRKAENIGGDQPNADGGAVEVEVGTETTANGKVKGDRKKRKLNAAPAVAGKESTGNGTPPTTGDSGATKQAAKRKRKKAKLSSGVANGTSIANGNVVKSVKSPEKKGKVKKNRWRSNAPKSGADKPAK
The following text describes a protein:
Function:
P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation also seems to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in phospholid transport across membranes and in acrosome formation.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle, acrosome membrane; Multi-pass membrane protein.
Sequence:
MKYVKAFVSEISWDCSWYCSAMQERRNEDRQKEEEERILQANNRRFNSLFEYPDNSIKTSKYGFFNFLPMNLFEQFQRLANAYFLILLFLQLVPQISSLAWYTTVIPLIVVLSITGVKDAIDDVKRHRSDQQINNRSVSILVNGRVEEIKWRNVQVGDIIKLENNHPVTADMLLLSSSEPYGLTYIETADLDGETNLKVKQAISVTSAMEDNLELLSSFNGEVRCDPPNNKLDKFSGTLSYLGNTYLLNHERLLLRGCVIRNTDWCYGLVVYTGQDTKLMQNSGRSTFKRTHIDHLMNVLVVWIFMFLGGMCFLLSIGHGIWENSRGYYFQAFLPWKHYITSSATSSALIFWSYFIVLNTMVPISLYVSVEIIRLGNSYYINWDRKMFYAPKNMPAQARTTTLNEELGQVQYVFSDKTGTLTENVMIFNKCSINGKTYGYSYDDNGEYVPKSPKDKVDFSYNHLADPKFSFYDKTLVEAVKSEDPLVYLFFLCLSLCHTVMSEEKVEGELVYQAQSPDEGALVTATRNFGFVFCSRTPETITVIEMGKIRVYRLLAILDFSNERKRMSVIVRTPEDRVMLFCKGADTIIYELLHPSCASLSEVTMDHLDDFASEGLRTLMVAYRELDKAYFQTWIKKHGEAWLTLENRERKLALVYEEIERDLMLLGATAIEDKLQRGVPETIVTLSKAKIKIWVLTGDKQETAVNIAYSCRIFKDEMDGVFMVEGTDRETVLEELRTARKKMKPESLLESDPINMYLARKPKMPFKSLDEVANGNYGLVISGYSLAYALEGSLEFELLRTACMCKGVVCCRMTPLQKAQVVDLVKRYKKVVTLAIGDGANDISMIKAAHIGVGISNQEGMQATLSSDFSFCQFHFLQRLLLVHGRLSYNRMCKFLSYFFYKNFAFTLVHFWYAFFNGFSAQTVYDIWFITFYNLIYTSLPVLGLSLFEKDVNETWSLCYPELYEPGQHNLYFNKKEFVKCLLHGIYNSFVLFFVPMGTVFNSERNDGKDISDFQSFSLLVQTTLIGVMTMQIALRTTSWTMINHTFTWGSLGLYFCILILLCSDGLCLRYPSIFNFLGVARNSLSQPQIWLCLILSTILCMIPLIGYNFLRPLLWPINADKVLNRIHFCLKHPIPTQVQTKIKHPSLRRSAYAFSHKQGFGALITSGKTLKSSALAKSKRFL
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER).
Subcellular Localization:
Cytoplasm.
Sequence:
MPQHLVSPEEFLTKLGQCFSDPSSSSSVWLTHKRLTYSDDADVQMNDEERENNSEGPEHEVLIRCTQGNNKFSARIPASSLPSFHAAYGSLLKTSMAPLMRKRDKKKEKARAEALTKKRKELYVEVVIGNEGKRGKGRRQRQRKIAAQKKKETEREKLEIRQAQQKASGDL
The following text describes a protein:
Function:
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Sequence:
MNINEILKKLINKSDLEINEAEELAKAIIRGEVPEILVSAILVALRMKGESKNEIVGFARAMRELAIKIDVPNAIDTAGTGGDGLGTVNVSTASAILLSLVNPVAKHGNRAVSGKSGSADVLEALGYNIIVPPERAKELVNKTNFVFLFAQYYHPAMKNVANVRKTLGIRTIFNILGPLTNPANAKYQLMGVFSKDHLDLLSKSAYELDFNKIILVYGEPGIDEVSPIGNTFMKIVSKRGIEEVKLNVTDFGISPIPIEKLIVNSAEDSAIKIVRAFLGKDEHVAEFIKINTAVALFALDRVGDFREGYEYADHLIEKSLDKLNEIISMNGDVTKLKTIVVKSSG
The following text describes a protein:
Function:
Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MKNIVKLFLWFLLAILNIALFWAGVFLFQNEYYELSIVLFSLLVLIDFFIINPRGYPYRYTIPALILLFVLVLYPIYFTFKVAFTNYGTGHFMSRQEAIERLLYDPNFSYVVDSTPVSYKVFVVYDGLSPTDDFLILFKTGDTIFLGERPKPVVARGQEVLLSQFNLVPITGETISLNGDTFRIVPWPADLSEINLVVRGEKTYKSFYSPDDEILRLNAPYFKSRIAQGYLVNAEYVLPDGKKLALRIAPDGEWRFMYVERLYRLAYKEIYDGVKMKITTTVVNNLTGREVVEREGAFYDVDENGNETFLVGFIDFVGWKNFLRIVKDPKVSGPFFRIFLWTFVWAVLSVVLSLAVGLPFALVLNNPRLKGRNLYRTLLIIPWAIPVFISALVWRNGLLNESYGVINKFLLPLFGLEPIKWFNDPFWARVGVLLVNVWLTFPYMMTISLGALQSIPPELYEVAAIDGAGRFRRFVHITFPLLMTIIAPLLVSSFAFSFNNFTIIYLITGGGPPIPNSTTPTGYTDILISYVYKLAFEGGQGQDFGFASAISILIFFLVGGISFVNFKLSGAFEEVSR
The following text describes a protein:
Function:
Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.
Subcellular Localization:
Mitochondrion. Peroxisome.
Sequence:
MATAMTVSSKLRGLLMQQLRGTSQLYFNISLRSLSSSAQEASKRAPEEVSDHNYESIQVTSAQKHVLHVQLNRPEKRNAMNRAFWRELVECFQKISKDSDCRAVVVSGAGKMFTSGIDLMDMASELMQPSGDDAARIAWYLRDLISKYQKTFTVIEKCPKPVIAAIHGGCIGGGVDLVSACDIRYCTQDAFFQIKEVDMGLAADVGTLQRLPKVIGNQSLVNELTFSARKMMADEALDSGLVSRVFQDKDAMLNAAFALAADISSKSPVAVQGSKINLIYSRDHSVDESLDYMATWNMSMLQTQDIIKSVQAAMEKRDTKSITFSKL
The following text describes a protein:
Function:
Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor; Necessary for the splicing of pre-mRNA. Has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns.
Subcellular Localization:
Nucleus.
Sequence:
MSATPPDLLSLAASREVSAAVAVAASANGGSGRSADKERSRSRDRGRDKDKDRDKDRKKRDKDSRDRDSRRRDDRGDRDRDRERDRDSRSHRSKSRNYDDGDRRRKRSRSRDRDRDRKRDRDRDSRSRRSSSRGGRDDYDRSRRRRSRSRSYERRRNDRGSQRDQRDQHSQRSSRERTHVNPFDTSNSRNSLNQDHDQSRIPSLFDRQQGLETIREEGREQRFDLTQTIQELMGNAGGNKGFASFFNSQNSNDSTSNGAFDNSADSAAERKRKRKSRWGGSENDKTFIPGMPTILPSTLDPAQQEAYLVQFQIEEISRKLRTGDLGITQNPEERSPSPEPIYSSDGKRLNTREFRYRKRLEEQRHQLIVKMQTVNPEFKPPADYKPPVTRVSDKVLIPQEQHPDINFVGLLIGPRGNTLKAMEKDTGAKIIIRGKGSVKEGKVGRKDGQPLPGEDEPLHAFITAPNPEAVRKAVDKIKDVIRQGIEVPEGHNDLRRMQLRELAQLNGTLRENDIQRCTCGSTDHKSWQCPDKPIITNTIVCTSCGGTGHLTKDCRNKRPGSGVPGMACEDSQAKIDEEYMSLMAELGEGPPPPSASAKTDPPASNGPQLHRASYSIFDKKPSQMQAIQSPPSSSSRDHQRDLGGWGAAAHEHGMGMEHGMGLDQHGHGLAAMDHGMSLGMEHAMAAYVPAPPGTQAPPPMPPPLMPWMSAPQPPPPATEPLNPPIPGTLPPLIPPPPGTSAPPMPPWGGGAYSGWGGGYAPPPPPPCAPPPPALSLSQPPPPPPPSA
The following text describes a protein:
Function:
Co-chaperone required during oogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with Hsp83/HSP90 and is required for the biogenesis of all three piRNA major populations.
Subcellular Localization:
Cytoplasm.
Sequence:
MARLMKPISLSQLTQEGFQFEIDTSYIEDPSSDPEDTPDILEKKIENSNKECLGIFDEDVYEEGEPFEIIARKMCNLTPNGKIKKRVIREGNGEKPQEFAKVKINYNAYLEYEESPFDSTYVRNKPLNFTIGNGKVLPGLDFAVQSMTVNEKSQFLIDPEYAYGRSCLIGRVPPNATVLFEIELISVVNCGAAVTYETLPEELQSSFTEIHKYCVALCERGKKSFKDRDYKHAIKNYNTAATKLEKTVLGGKDEIELQRELLLKLYTNLLICYARSGEPRKGCFNAKKVYDLTEDGELMKIPIKVYFNHAKCLRILSDYDKAKEVLDKAYKAEPKNPEIANEMLNLSRDRTEHKDKQMAFAKALVNN
The following text describes a protein:
Function:
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Sequence:
MQQQFLYLSSAEAQLSLGLGEEKTTERLFFAVMADAATATHAAQIGSALLQAGLVEGKPLAPERLHVTLHHLGDYAGGLPPSLVARASQAAERVAQQPFEVEFDRVGTFGGRRSQLPCVLRGEEQVRGLYDLQGALGRQLAHVGIAGDAQYTPHMTLLYCNQSLPQRRCDPLLWTVTNFALVRSFLGQSRYQIEGRWLLR