lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (By similarity).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MRMNKRTLLFVSLVSAAFLGCQIFFGYRDLKSCQDLAEKQRAISEQILASTEQLSVVPWTASLEESESVNQYAIRLGNRLLLLTKGGSHPEVYSRGTYWSLIEQTSTFGGILVSLYGETGQEVLSKGSSVYLPNQRDAFPVLVAEFRSNQEPLVFLGEYKDGKIANKAGAIYGTSLVFLNTGNGFVPLGIYNSKEECVESLDLPMARAVVFADKENPTASGSYYMLSNEYMQIVVSQESGAIEGINLPFASDQEENKSIVNEIGFDRELAINSPSEASFPGVETIDSQRQNIANVVGGYYPLLRRGTLSDVKKRVPAQYQALNIVSGRELASPVATGFRVVSFDNKTLILESGDGGIRRTYSLGEQPYAFELEIQTTQGREDLWITSGVPEVEIMSNAFVPAVKYHAVKKNKSDLFNVKLPKAKDSLLVRNNATPQWILNSNGYFGVILTPRIPIPAGYASSFIPGNVVPTRLSQLPPKDQAYPASKYPGYTAMLPLPKEAGRYQFMVYAGPLADPTLKALDRANANSKGETPEYVDAIAFRGFFSFITEPFAALLFVIMKFFKFLTGSWGISIILLTIVLKLLLYPLNAWSIRSMRRMQKLSPYIQEIQQKYKREPKRAQMEIMALYKMNKVNPITGCLPLLIQIPFLIAMFDLLKSSFLLRGASFIPGWIDNLTAPDVLFSWETPIWFIGKEFHLLPILLGVVMFAQQKISAVKRSGPASDQQRQQEAMGTMMALLFTFMFYNFPSGLNIYWFSSMLLGVIQQWVTNKILDEKHLQHEVIINKKR
The following text describes a protein:
Function:
Putative phospholipase.
Sequence:
MISSLLFSYGISAISYKAVNASCNIADGNPTFAEGIDPNAAAWAYWEDSLNETGWYKLHIKGNSKYTDSEIMKCAGYLEGYVSHDRINNHFNLIFDIQEWTRNRKYPDKIYQYLSSNLRYVRQSIEAYSATSKFWQEIAFIMNQFDGLVAGYQAIDGDATMNELDLWFLQSEGDMFDISEMYPDVKQPKEKTYPGEHCTGLVRLLPDYSDIFFSHDSWSDFRELHGELKEYDLPIKAFKAKKISLSTRIGKLSSYDDFYINDQGLFVLETTMTNFNDELYEQSKPQSLFTWMRAVHATWCSDSGKEWTDNFGQHNSGTYNNQYLIVDSKKFKRGEKPTTDLLWIIEQMPGTFEKADITGDLLRDGYFPSINTPYFDRLFELAGYPAKIASWGDDGNYWDYKTSSRYIIMAREAPFIKDFEQFKSFMRYSNWKRDPYAHGDAGQMIIARYDLRDLPNPHFVKRMFGGLDTKALRLTEATTSMMFHALASPECLHNPVFNFNDWDVKHDGLPDKWNHTWQVFQSIDGDKCMVHGSNKTSCFQQEGCGFCMSSQMCYSGYKDSPYVMECDAGWEVPQPPQPWAKPTIIAVTVIVVIFVLSVYAIHFMNNKKN
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. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). Required for activated transcription of the MtnA, MtnB and MtnD genes.
Subcellular Localization:
Nucleus.
Sequence:
MSGSNAKSSGTGFGSHIPSIEEKNKQIQQETMMEKLRAKYRNKPKSYEEIKKSVRMYFIEKHYPLDPLCKATLQSALDKLQHYIKVTSRHGLVERLESLSRQLGLKFMEDQQLLFISTDMFYVEILLDAAGSLSDVKVHHECKIEQQSSELVACLKSGDFADFTVQLEGLSSIYQLNAEPKVKKKAFVALQAMETDIQSLYQLHLQGHSGDSYSLMTSSSVGLVLPRRGGHPMRLTYFCPPLHLPEGDPKLASGDFTIDQVMRSSYGLSATINLEGSSANKLQTLPTVTLVRDAQTGLEVPTYAQLNQNNSLLMPATFVLRLNKPMPVCLESLKALGLPGLDSVATPPGPPTTVLNLIVQTASKQAIKNTQRGLYVNLPKETHCYFFTDNRKLQGTLVSSLPFTEPAQVPRIVAFLKKQALFYTLLASCVREQQKQYNDMDSTVILEVTAVSFNQITVELQHPYEESLATVDFLLEDGQPTCSVYCLTNEYELLSQKLTRTARKVVSIPMVIYKLLKCWDEEHEFKLHGAIGPGSGSGAIGGGGMSGGGPVSGVGNNFSQFSMDTPTPSDGSLPGGGFANINNLKMDAKSRSLADAFAASTSAAAAIAGLINLKRETDPQSGSSASGTTVSGSSSSSGSAKTSDHDIADKYKNIWKDKTPNLKHCVSITPIPGDGKSGSAGGVSGVEVQRTGGIEIIPLNAQAAIAGGGVTASSSATPTTITITPITGKDPSKDSTKKSTAASAGVGVAAKRPHESSTSSSSTSGCSGSGSSMSSSASSGSSDTQKEKKRKKKRDDSPMGPPEKIYSRQNSPAGGADASATGGVVRKFSSPSSSPKAGGGGQGLMAGVPTARPSPKHSPVYSSPKHNTASNSPKSPFGTHSPKHGSSGKPSMSTLKSAATAATILSPKGDKSSSAVGNTSSGPSASSGSSGATGLVRSFASVGAPPPPPPIPPLASSSGSISSSQSLKKEKTSSASGSSSTSSSATAGVASGGGISPASVAAAVAALKSSQQQMKSVASLSHLAAGGGLGSYAAPSGAGASGAAAVVVGAGAGAGAGASGLELSALRKGMAGGAVSLMTSTAALAPTIPAPTTTVAAGSAASLVSPVSAVVGQGQETAGAAAAATLATATILQQQPQPGAAPTSSCLTTSGGSSDSAGSINPAGASTEYMVKPSSQEGLKLTINKTGSSKSSGTGSGSSSSSGLQAKAKSSSSGATSFAGSTGSTKKQHTGLKPGVNSGPASKKATAAVSSATASSSKHFFQKANSSGNLSSKLSGSGSGGGIPLTKSNSTNSFQEHNAPRRRPSMGALASGSSGGGSGQRKLGSASGGGSGSSGSVSPALSGSMSQPPPRFDHHTDMMTILQYASPTMAASMEGFIKGLHNKFQIPKLSQRGSGGNTTSGRSTPSGSSEPALAGTSSSILGPIASSTGLTEPEAKPPVPPSQSGNEGLLNLSSTAGTPSADGIDEELLASLAGE
The following text describes a protein:
Function:
Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Subcellular Localization:
Cytoplasm.
Sequence:
MTSGRSTRVTMFESQASMGEPSNEDLSSTDDVRTDAPLAYAKYVTFDQSLPLERGGELPEIRCCYETWGTLNDDGSNAVLVCHAVSGDSHAARHDEDDQPGWWDGLIGPGLPIDTDRLFVVCPNVLGGCRGSTGPGDADPTSPDGKPYGANFPRITIGDIVEAQKLLADHLGIRQWRAVVGGSLGGHQVLQWINRYPDAAKTCVAIATSPRLNSQALGFDVIARNAIQTDPHYAGGQYYDKDQRPDTGLAIARMLGHITYLSVEAMEAKFDPDRHDPRQIASQFEQRFSIGSYLAHQGQKFTTRFDANSYVTLSMAMDLFDLGGTRLKLMETFDEATCDFLLISFSSDWLFPPAQSREIVNALTALDKRVTYAEITTNAGHDAFLIAKDIATYGPLIRERLRDTETHPAVPSDITLNVDEESILEIIPAGSSVLDLGCGNGQLLAAIRDRHRTPGPPTTEHRLMGVEVAQENLLATAMRGIDVIDYDLNHGLPAFIDDQFDYVILNATLQAVENVVELLNEMLRVGRHAIISFPNFAYRQLRDHYVTHGRSPKAPGEFDFDWHNTPNRRFPTIADVRDLLGQLNVVIDEEVFWDVDQGQRIEPDNDPNLNADTAVIAFHRENR
The following text describes a protein:
Function:
Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Sequence:
MTHQSRAVLSLFPCFRSSFVVRTLLLSKLFDCMWIVNQGGNHFVKEMSLVTWQVFAAFGTFKGGRACERCATEYQVSATPLLTERSSIICGRPAIYGILGMRMNLYTSYLLSQAKGYIKWYWLTIRSNLIPSWVKFNTGNGADFRRKEVELMLQAGYITVGLGPHRLQAETEIIALLATLVMWSDSQETTA
The following text describes a protein:
Function:
Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner (By similarity). ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates (By similarity). Confers salinity and drought stress tolerances by maintaining both photosynthesis and antioxidant machinery, probably via an increase in plant hormones levels such as gibberellic acid (GA(3)), the cytokinin zeatin (Z) and indole-3-acetic acid (IAA).
Subcellular Localization:
Nucleus. Mitochondrion matrix. Mitochondrion matrix, mitochondrion nucleoid.
Sequence:
MAVAAALLRRRALYSALASPSWLHDTSSCYICSISGTHSLVNHPNLRLQRGYHNSGKFDLTDLTHPHIWYPNAREKKRNVFLHVGPTNSGKTHNALKRLEASSSGVYCGPLRLLAREVAQRLNKANVPCNLITGQEREEIEGAKHSSVTVEMADMTTEYQCAVIDEIQMVGCRSRGFSFTRALLGLCSDELHVCGDPAVVPLIQRILEPTGDVVTVQYYERLSPLVPLKTTLGSFSNIKAGDCVVTFSRRSIYMLKRRIEMGGKHLCSVVYGSLPPETRTKQATMFNDQDSNLNVLVASDAIGMGLNLNISRIIFSTLEKFDGICNRELTVAEIKQIAGRAGRYGSKFPVGEVTCLNSDHLPLLHSALKSPSPIIERAGLFPTFDVLSLYSRLHGTDFFQPILERFLDKAKLSPDYFIADCEDMLKVAAIVDELPLGLYDKYLFCLSPVDIRDDISTKGLIQFAENYAKKGIVRLKEIFTPGTLQVPKSHNQLKELESIHKVLELYVWLSFRLEDSYPDRELAASQKSICSMLIEEYLERSGWQQNGRKDFLQKPKRLHQEYDASQLRKYFQEIDVRSK
The following text describes a protein:
Function:
Periplasmic acid trehalase that catalyzes hydrolysis of the disaccharide trehalose and required for growth on trehalose as carbon source. Growth on trehalose is strictly respiratory (By similarity).
Subcellular Localization:
Membrane; Single-pass type II membrane protein. Vacuole lumen. Periplasm. Note=May exist in the periplasm either as a membrane-bound or as a free protein (By similarity). Vacuolar localization is dependent on the multivesicular body (MVB) sorting pathway. Vacuolar localization appears to be associated with its degradation.
Sequence:
MKRIRSLWFNAEASYSNLNNSPSLRNKNSTGNNSRSKNYRSFSRFDLINSILLLMMLFLLAIFVTALYLTKSSRLTYSHASRAALFNPLGVISPSLGNHTLNYDPEARESSKKLYELLSDFNTAYYDDENMILGSNLFSKNTYSRQPYVANGYIGSRIPNIGFGYALDTLNFYTDAPGALNNGWPLRNHRFAGAFVSDFYCLQPKLNSTNFPELDDVGYSTVISSIPQWTNLQFSLVNDSKWFNPQNVTLDDVTNYSQNLSMKDGIVTTELDWLNSQIHVKSEIWAHRHIHPLGVVSLEISLNTDHLPSDFDSLDVNIWDILDFNTSHRTVLHSTGTDEKNNAVFMIVQPDNVPSSNCAIYSTCTVKYENSTNPINSSESFEEKDVSSNIYNVILTEDQPKIIVHKYVGIMSTEFNKNKEQQDNTNIGLAKMIALNSKGNYEKLLSSHKRAWYDLYNDAFIEIPSDSLLEMTARSSLFHLLANTRDYNVSSDRGLPVGVSGLSSDSYGGMVFWDADIWMEPALLPFFPNVAQNMNNYRNATHSQAKLNAEKYGYPGAIYPWTSGKYANCTSTGPCVDYEYHINVDVAMASFSIYLNGHEGIDDEYLRYTTWPIIKNAAQFFTAYVKYNSSLGLYETYNLTDPDEFANHINNGAFTNAGIKTLLKWATDIGNHLGEVVDPKWSEISKDIYIPRSSSNITLEYSGMNSSVEIKQADVTLMVYPLGYINDESILNNAIKDLYYYSERQSASGPAMTYPVFVAAAAGLLNHGSSSQSYLYKSVLPYLRAPFAQFSEQSDDNFLTNGLTQPAFPFLTANGGFLQSILFGLTGIRYSYEVDPDTKKINRLLRFNPIELPLLPGGIAIRNFKYMNQVLDIIIDDHNGTIVHKSGDVPIHIKIPNRSLIHDQDINFYNGSENERKPNLERRDVDRVGDPMRMDRYGTYYLLKPKQELTVQLFKPGLNARNNIAENKQITNLTAGVPGDVAFSALDGNNYTHWQPLDKIHRAKLLIDLGEYNEKEITKGMILWGQRPAKNISISILPHSEKVENLFANVTEIMQNSGNDQLLNETIGQLLDNAGIPVENVIDFDGIEQEDDESLDDVQALLHWKKEDLAKLIEQIPRLNFLKRKFVKILDNVPVSPSEPYYEASRNQSLIEILPSNRTTFTIDYDKLQVGDKGNTDWRKTRYIVVAVQGVYDDYDDDNKGATIKEIVLND
The following text describes a protein:
Function:
Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation. The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen. PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase. The VTC complex also plays a role in vacuolar membrane fusion.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Domain:
The SPX domain has very high affinity for inositol polyphosphates. SPX domains may integrate inositol pyrophosphates (PP-InsP)-dependent signaling to adapt cytosolic phosphate concentrations to different metabolic situations.
Sequence:
MRFSDSIEAGIYEPWRDKYMNYPELKHLLKTEEEAPSWGENDESKFVSVMDAQLEKVYAFHLEILKELNESVDWVKSKVSASQEPDGPPISKEEAIKLLERLDSCTETVKKLEKYTRLNLTGFFKIVKKHDKLYPGYSLRPVFQVRLRACPLGSVQFNPLLAEIFSLYNTLRDGLSAPSNSVQVKPKHEHNVDYNSSMYRRRTFRFWVHPDNVMEVKTYIMRHLPVLYYSGKQGFDKDQNGVSGILDPISTCLYLDNSNFDLYSQNLERSEQAYSLRLHWYGKLTPKTDIIVERMVRQGSTLSHSEDRFTIREKKVRELLSGRYDFRKVEDDHSTTASDQKKKLIEDVEQLIVDNHLQPVLRSVYTRTAFQIPGDDEVRINLDSDWVMIREDSLDIERPCRDPEDWHRHDIDDADFPYKHLRKGEYSRFPYSVLEIRECVRYDEDEPLWISELRNSHLISEIDGFSKYEHGVAILFEKYVSLLPMWVFSMDQDIRKDLQEVYSHPEGSAGSRNVYIKRRNQRVLKQNMTPEPSQPSPLVNRLKANEMHPVSEEPEDNREVYRNEHGDHFNFRSIPGLLKPSTYGSFKHHGKTFVTPPHIKKPEIPLRVSGPIKVEAKVWLANERTFLKWLHVVVLLGSLALALYNSAGERLGQAFGVVYTLLAIFIGFYAWKLHAKRSQMIKSRSPAPMTDYWGPLIVGTALAISLIVNMSFALKDAVYQNLIEPDRLLVKLFT
The following text describes a protein:
Function:
Calcium channel that probably plays a role in the regulation of calcium homeostasis. Uptakes calcium ions and mediates calcium flux in proteoliposomes in a pH-dependent manner. When expressed in E.coli in the presence of high extracellular calcium concentrations, shows calcium-leak activity, increasing intracellular calcium concentration. It can also mediate Ca(2+) flux from the endoplamic reticulum (ER) when expressed in permeabilized mammalian cells. Calcium transport activity is also detected in ER-like lipid vesicles.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
BsYetJ in nanodiscs is structurally different from those crystallized in detergents. In lipid nanodiscs, BsYetJ conformation is pH-sensitive in apo state (lacking calcium), whereas in a calcium-containing solution it is locked in an intermediate state, inert to pH changes. When crystallized in detergents it shows a pH-sensitive conformational equilibrium between a rather flexible pore-open state seen at lower pH and a pore-closed state seen at higher pH. BsYetJ appears to be a lipid-sensitive membrane protein: differences in membrane lipid composition lead to changes in functional sites.
Sequence:
MQATVHESKQSIMQRILTVFVFTLLIATVGLFIGQFVPVALMLPLSILEVAMIILAFWMRRRKAVGYAFVYTFAFVSGITLFPIVSHYASIAGAYVVLEAFGSTFVIFAVLGTIGAKMKKDLSFLWSFLLVAVLALAVVGIFNIFSPLNSAAMMAYSVIGTIVFSLYILYDLNQIKHRHITEDLIPVMALSLYLDFINLFINLLRFFGILSSDD
The following text describes a protein:
Function:
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Probably changes conformation upon binding to the ribosome (maybe in particular due to interaction with L24), exposing a hydrophobic crevice that is probably important for its chaperone activity.
Subcellular Localization:
Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.
Domain:
Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence:
MAELISKEGNKVEFKVSVPAAEVNRAYDQVWAGLARDVRVPGFRPGKAPRKVIENRVGKGYVESQVRDRLLETHYSQGLRELGLNLVDATVDPQDVQSGQAFEFTVKGETYPEVKLGDWQGLKVSAQAPEITDEVLEQTLSDLRERNASFEKAERPIEAADQVTIQELGEGDSEEGGSYPIYLDMAEEHVRNALLGKSAGDVVDITVPAHQHGDHEHAEHTVRVKVVEVSSKKLQDLNDEFATSLNYESMDKLRTDLREELERRAQQEGDNLRREELVGHLVEGMTVEIPQALIDRRREGMMSEIQDDLRRQGVQWKEYEAFMQEQGKLDEFEADLTKNAETRVRRDLALEQLATDLNAQVNEAEFNQTLMNLAQANGMNVQQLVQQLGQDGVQSYYISLLRERGLQRALAQLSGEGQSTEAASPKATGTEAAGTEQSEPAQTETAQNDAGQTETAQSEGEQQSE
The following text describes a protein:
Function:
Involved in mRNA splicing where it associates with cdc5 and the other cwf proteins as part of the spliceosome; Involved in mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MEKEKLTNRTSTHKFNETDRETNHSRRHRHHHSRHRESKHGRHDRSERPSSREAGDRSRHERFSKEPLEVKKLPVENEYFDSKFASASSMPSSKDNPQNNDFTNSLQGLDFGTFGSRIQREPIDRKSNKPGEIFVGATLQNESSTSTEHKDIEQLETEINESGINYKIGDNGSRWRMMKLKRVFDMAQDQRRPVEEVALERYGSLKEFDFALEERDELELRKRTRKVQKEVPTGELYEKRCADEFKTRKDSGNGATYYKVIPDPSVNKDTPTESDLNRLKADLLRAQLKKDPNYESLEREYQKACDDFENSLHPSENSNSQATIPSKKRNFDDPTIDEMVQEEKLLNKQRKYGQNYEYAKQIAKDKTYSNNLDYLDENAGKLSNRMKRGDVSLAQISSGGDLKKINHVLDTCPLCLNYETQPLAPVISLSHRAYVSLPTQPELAKYHCLIVPTGHRINTLSCDEDEWDEIRNFMKCIALMFDSMNLGVIFYENAPSPQRYMHTAIECIPVSKRILSLAPAYFREALSTSDEEWSQHRKIIDTLEGSKKYGKWAFRKMMVKELGYFHVWFSIDGGYGHVVEDEKAWGRHDQVPRQVFASMLNLPPEVIRRKGSWTGKKDPREDMFRSRFEKFDWTKGLID
The following text describes a protein:
Function:
May play a role in myoblast differentiation. When unphosphorylated, associates with an ELAVL1-containing complex, which stabilizes cyclin mRNA and ensuring cell proliferation. Phosphorylation by AKT2 impairs this association, leading to CCND1 mRNA destabilization and progression towards differentiation; [Isoform Ptx2c]: Involved in the establishment of left-right asymmetry in the developing embryo.
Miscellaneous:
MISCELLANEOUS: [Isoform Pitx2Cbeta]: Produced by alternative initiation at Met-35 of isoform Ptx2C.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
METNCRKLVSACVQLGVQPAAVECLFSKDSEIKKVEFTDSPKSRKESASSKLFPRQHPGANEKDKGQQGKNEDVGAEDPSKKKRQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERNQQAELCKNGFGPQFNGLMQPYDDMYPGYSYNNWAAKGLTSASLSTKSFPFFNSMNVNPLSSQSMFSPPNSISSMSMSSSMVPSAVTGVPGSSLNSLNNLNNLSSPSLNSAVPTPACPYAPPTPPYVYRDTCNSSLASLRLKAKQHSSFGYASVQNPASNLSACQYAVDRPV
The following text describes a protein:
Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Sequence:
MAETRFKFGYWKIRGLGACCRMLLWYCGERDFEDRMYEQGDPPALSRQEWYDEKYTLGLDFPNLPYLFDRVKGLGLTQTMAILEHVSRELKPELLTGSGRDAPRLTMVLNFVMDLHSNLSSYFYRASEDEAKRMREEVFPTQLALLEKYLEKAEGPFLGGHLTYADFYVAEELDHAVELIPGFLDEFPSVKAYWERFFALPEIVAFRASPHHCTLVNNKVAKMNNFVFPAPAAASE
The following text describes a protein:
Function:
Plays a role in vesicular protein sorting. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. Required for the auxin-carrier protein PIN2 sorting to the lytic vacuolar pathway and the PIN1 recycling to the plasma membrane, thus influencing auxin transport orientation. Also involved in the efficient sorting of seed storage proteins globulin 12S and albumin 2S. The VPS29-VPS26-VPS35 subcomplex may be involved in recycling of specific cargos from endosome to the plasma membrane.
Subcellular Localization:
Cytoplasm. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Prevacuolar compartment membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side. Late endosome membrane; Peripheral membrane protein. Note=Colocalizes with and mobilized by VPS38/USL1 at late endosomes, probably in a PI3K complex-dependent manner.
Sequence:
MVLVLALGDLHVPHRAADLPPKFKSMLVPGKIQHIICTGNLCIKEIHDYLKTICPDLHIVRGEFDEDARYPENKTLTIGQFKLGLCHGHQVIPWGDLDSLAMLQRQLGVDILVTGHTHQFTAYKHEGGVVINPGSATGAYSSINQDVNPSFVLMDIDGFRAVVYVYELIDGEVKVDKIEFKKPPTTSSGP
The following text describes a protein:
Function:
Required for mother cell-specific ho expression. Might be required for the transport of factors (such as ASH1) that promote HO repression from the mother cell into its bud.
Miscellaneous:
MISCELLANEOUS: Present with 3410 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MPLCEKGNDPIDSSTIDSLCAAFDKTLKSTPDVQKYNDAINTIFQLRQKSESGKMPADLTNSEALKDRQKIEEILTRSYQDHSESRVHLSKLIQNDIPFALNLFEILSRSSIHVFVGCFSNKDATIALLNELQIRIHYGEDTHVTYLLSIILQLLNKFKYNFKEVRFLVKELILRISEDEVKSMMLIIFAELQSSFQKDFDKAVVDFMSSLIVEAEIDVGNDPLSIIVKTLSELYPSLTTLCSEIFLTKGLSKLFKKRVFEEQDLQFTKELLRLLSSACIDETMRTYITENYLQLLERSLNVEDVQIYSALVLVKTWSFTKLTCINLKQLSEIFINAISRRIMPKIENVNESAVKLEEVPKVEMSVEALAYLSLKASVKIMIRSNESFTEILLTMIKSQKMTHCLYGLLVIMANLSTLPEESNGSSQSINDLKNYADLKGPGADKVGAEKESKEDILLFNEKYILRTELISFLKREMHNLSPNCKQQVVRVIYNITRSKNFIPQCISQGGTTIILEYLANKQDIGEPIRILGCRALTRMLIFTNPGLIFKKYSALNAIPFLFELLPRSTPVDDNPLHNDEQIKLTDNYEALLALTNLASSETSDGEEVCKHIVSTKVYWSTIENLMLDENVPLQRSTLELISNMMSHPLTIAAKFFNLENPQSLRNFNILVKLLQLSDVESQRAVAAIFANIATTIPLIAKELLTKKELIENAIQVFADQIDDIELRQRLLMLFFGLFEVIPDNGTNEVYPLLQENQKLKDALNMSLKRGDSGPEFSAAIPVILAKIKV
The following text describes a protein:
Function:
Forms a strong non-covalent specific complex with biotin.
Subcellular Localization:
Secreted.
Sequence:
MGSGAFTLALVLALSTCVTPVERKLSGLWRNEQDSLMEISALADDGGFQGEYLTRVTLAGGCTRISPLRGAQQQPSEVAWPTFAFTVWWDTFSNATTAFAGQCFVDASGREMLSTTWMLREAVGSLEEDWKATRVGRNVFTRKRTPKGKILHSLSPSCEDAALPVL
The following text describes a protein:
Function:
Rhamnosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the addition of a rhamnose to the galactosyl-undecaprenyl diphosphate intermediate.
Sequence:
MKITLIIPTYNAGSLWPNVLDAIKQQTIYPDKLIVIDSGSKDETVPLASDLKNISIFNIDSKDFNHGGTRNLAVAKTLDADVIIFLTQDAILADSDAIKNLVYYFSDPLIAAVCGRQLPHKDANPLAVHARNFNYSSKSIVKSKADIEKLGIKTVFMSNSFAAYRRSVFEELSGFPEHTILAEDMFMAAKMIQAGYKVAYCAEAVVRHSHNYTPREEFQRYFDTGVFHACSPWIQRDFGGAGGEGFRFVKSEIQFLLKNAPFWIPRALLTTFAKFLGYKLGKHWQSLPLSTCRYFSMYKSYWNNIQYSSSKEIK
The following text describes a protein:
Function:
Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes.
Subcellular Localization:
Nucleus.
Sequence:
MKIKQENITNTTSINTSNVNDKPKPKRKKTSRACNHCHKAHMTCDSGRPCKRCIQRGLDSTCEDAPRKRKKYLQDVPNSSLMSNHSMNSSDNLDSNGVSPMQPTLSQPMPPVQESSLPTNIPNQSQVPSQSPNTASQKQLSYSPPLASTYSPNHKTYSATLFQHSATSPELMQTVPEYFPELYNQHYQPSANPNQKRRTNFLSTAADLEYSTLSNILQENFGHHTTSNEGTPNSHNFSPALSPHNMPTNNTNAPSTSTQLLTNDQQRQATSFNNHTKHNTPSPLNTSHTKLYEDARYPKCDETINQYFLGDTDSGKMVVFPDVLTAIENMKNNDPAVYLERNSKSALSFVMSIQHENNSNGGKEDQLFKEPEEIYEKVKKPFSYTPGYHSLIAYLRKRFTKPMLVKMAESMATYRPSFIACTNSLKEHDLIFMEQCFQRTLLTYDNYIKISGTPTIVWRRTGEVAYVGNEFCVLTGWPKEELIGKDKRKFIVELLDDKSVLQYFQVFSRIAFGDFLGATMTECTLLTPNPNVKIRTGCMWTLKRDVFGIPMMIVGNFLPIL
The following text describes a protein:
Function:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MSDWEASDHEEAANAGISVAAGVSAIKKNKWADEDADEDVKDDWEASESEDEKSKNEPAKPKGPVRNKGITKMKIAEKEAEEALRLAEQEALAQQAADPVLRKKLEQTRTIQSDMENARGLFGDAVVSNPNSSEDPMKMDPKTKADFESMSSALAQLIVSKHGNKPLYPLFVEHFFRQLSEPLSDVQTRKTASILTTIANEKQRAAKDAKKGKGKLKPTLGGGVVSGASKGGRGVNADLEVYDQALDDEFDDFM
The following text describes a protein:
Function:
Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles (By similarity). Also exhibits lysophospholipase activity (By similarity). Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates (By similarity). In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MGNPLQISIFLVFCIFIQSSACGQGVGTEPFGRSLGATEASKPLKKPETRFLLFQDENDRLGCRLRPQHPETLQECGFNSSQPLIMIIHGWSVDGLLENWIWKIVSALKSRQSQPVNVGLVDWISLAYQHYTIAVQNTRIVGQDVAALLLWLEESAKFSRSKVHLIGYSLGAHVSGFAGSSMDGKNKIGRITGLDPAGPMFEGTSPNERLSPDDANFVDAIHTFTREHMGLSVGIKQPIAHYDFYPNGGSFQPGCHFLELYKHIAEHGLNAITQTIKCAHERSVHLFIDSLQHSDLQSIGFQCSDMGSFSQGLCLSCKKGRCNTLGYDIRKDRSGKSKRLFLITRAQSPFKVYHYQFKIQFINQIEKPVEPTFTMSLLGTKEEIKRIPITLGEGITSNKTYSFLITLDKDIGELILLKFKWENSAVWANVWNTVQTIMLWGIEPHHSGLILKTIWVKAGETQQRMTFCPENLDDLQLHPSQEKVFVNCEVKSKRLTESKEQMSQETHAKK
The following text describes a protein:
Function:
Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7. Through ARL14 activation, controls the movement of MHC class II-containing vesicles along the actin cytoskeleton in dendritic cells. Involved in membrane recycling. Interacts with several phosphatidylinositol phosphate species, including phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 4,5-bisphosphate.
Subcellular Localization:
Cell membrane. Cell projection.
Sequence:
MAEEVTAVLRMSKDGTTFGFLLRQIDIGEHVIYKIIENTPADMCAKVEIGDIVMKINGVDVTGLATKDVVKCVRVSPNPMTLQLRKDPQVKSRVYEMIKSTSPERVLHHQLHQQQTPPAQGPEEFTVVLRRKQEDTRLGFVVRATDLLDHVIVEIRQDSPAALCGKVEVGDVFLKINDTDAQQYSPRDVLKCLGLATEPITLRMKRDPWIKKYLREQYQHEEQQLVLSDDSIESQSYKVRSDNTNGSSPSLPASRLAQPKRSKLLSLDSEPNLNSPNAARTPGNGNPYAVRECLSESACRPSRIPQAIAHSNWSAPQSPSRGRKPPRAPQIPTARSDLLKHQRFVMTGESQFESRYYDTTTTTTTTAVIKEPPESVRDSPTNQRFGGVGGKRKNAPLVNYDTLSSSTSRSDENSNSSCLMEDNANNDPTQPPSPASPLSPTDATAAAAASDNNGGKLNANHGSNGNNNLPEPGKPANRSNGEGGTDGGASGNQNAYSGNATTAGDDAAAGREGVAWAKDCDSSAGGGGGGGGGGTRTNSEATARQRHTGAGSRSRGDPSEISYSVPTSPTTYSVGGGGGGGGGGGGGGPGGGSEYHHHHHHHHHLLSSGGGEQYRNNNEMGINSLPTSPEYGGAAGGGGGVGGGGGQQVFRYGAGSVTEHSSNGGCGGGGGSGGTGDMSSGELTANTNMSSGSGPASGMVRKCDAAGFRTSRSEDHLQQTQRDGGIGAVVSIDIDEDVNSSLNTLLDTRHDSQEYAISERERFLWSYNAQPAPKTTAAGGGGGTEGATGHASEPGGAASVVSPQSYSSSVSSSPQRSASDSPASPTSVSSSVMSSSGGSREHSHNGHAGGTNSSSIANNLPGGNHYHQQQQQHSHHQHHSQHHHHHNNQQQQQQQQQQHHHHQQQHSSGVGQQQQPGYGGGGGRDHSVSEAVSNISSPDYQDEHDLLSTKDLMAMAISDPSDSDSTILISENTHRCDLPLSHSDRDHKLVIQVKSGELGGAADCGRHLTDAEEDYDGARCLALLKEAERSELDSFDAMDCDGMMLQMPGPNSGLVPAGHAGDGMLAYGGSVTRESSPPVSDDGSDVDSLHSFHYSPKAVDLPSAERLAKRLYYLEGFKKSDVSRHLCKNNDFSRAVAEEYLKFFFFECLTLDKALRLFLKQFSLTGETQERERVLVHFSKRYLDCNPRSFNSQDAVHTLTCAIMLLNTDLHGQNIGSKMTCAEFIDNLSDLNDGENFPKNVLKQLYYSIKEKQLEWALDDETDPKSGNRNGDGNGNGGNGNGLGGSLGGNGGGGGDGGPTGGSLQGPPVGPNPFLEAPPMFAAVEYKKGYVMRKCCYDTNYKKTPFGRRSWKMFFCTLRDLVLYLHKDEHGFRKNQMSDNVHNAIRIHHALATRASDYTKKQHVFRLQTADQSEFLFQTSDSKELQSWIDMINFVCASFSAPPLEGGVGSQKRFQRPLLPCTHSRLLLRDQLSSHERQINKIMTMLEEHKMTTAPPKGLALQNYKEKEVYLQYELKRYKTYYNLLSSRLTMEPQDFTNQHQVSAAALNDTGERRDDSTCSTMLPLGGGGGGGGGGYEYGANSHPGPGQQRTATNAGNLMPNFIQQHQGQGGGPGLNATGRSGLSPPDTTALGQLPRVATESTNSL