lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Sequence:
MARFFRRRKFCRFTAEGVQEIDYKDVATLKNYITEAGKIVPSRITGTSAKYQRQLARAIKRARYLALLPYTDKHQ
The following text describes a protein:
Function:
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins.
Sequence:
MSVMLKQPGAFTITPHKVSLCILLKIYAPPGQVSVPFPFESVAQHNRLGLFILALTKSCDDILEPKLEELISQLRLISQNWEATWLIDQLISRLSCLSSPDDLFNFFTDIRGIIGGPDSGDIEADQVILDANSNLGIFLRRCILAFNLLPFEGVCRLLTNIGIYCKEEFSSIPPYEETSLDGSSSNLETYSEYENMDLENFFYDKVSEEIEARKEASGRVPFHLHTPNALLSLVDDIDVPADSASKQSDKLRVGSPYEDRHSNMVRDIDPSGAVFLRTNWQIQGYLQEHADTIEKNGSAVSLNGFEIVLRQLQKLAPELHRVHFLSYLNALSHDDYTAALENLHCYFDYSAGKEGFDFVPPSGNNSSGTYEIALLCLGMMHFHFGHPKLALEVLTEAVRVSQQHSNDTNLAYTLAAISNLLFENGISSTAGILGSSYSPFTSMGISLSVQQQLFVLLRGSLKRAENLKLKRLLASNHLAMAKFDLTHVQRPLLSFGPKSSMKLSTCPVNVSKELRLSSHLISDFSTESSAMTIDGAFSTAWLRNLQKPNGSNIFCQDSGSGNSSNIPQFCAQPTSIPGSVLQVLGSSYILRATAWELYGSTPMSRINALVHATCFADASSSSDAALAYVKLIQHLAVFKGYKEAFSALKIAEEKFLSVSKSQIILLKLQLLHEHALHGGRLKLAQKLCDELGALASPVTGVDMEIKTEASLRHARTLLAAKQFREAASVAHSLFCMCYKYNLQVHNASVLLLLAEIHKKSGNAVLGIPYALASLSFCISFNLDLLKASATLTLAELWLSLGSSHATRALNLVRGAFPIILGHGGLELRSRAYIVEAKCYLCDTNFNVGEDYNFVIDSLKQASEELQPLEFHELAAEAFYLMAMVYDKLGQLEEREEAATSFQKHILALNNLQDHDDPLVSIY
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVAKGKKASADAVYAKKTTRSANPFDNSTAQSSKRGNPFDVHVNKEKFKILGRICKHDRGMPGVSRAKALQKRAQTLGQQFAVKHKTNRFKDNRIGKHLSGDQLTESVMNARYLAEKMSQVRSNQKAEKFNLNDDELLTHRGQTLEEIEQYRDERSDDEELDDEALDADFTAAAHFGGEGDSAQDRQAAIDEMIVEQKRRKNEIAKEKDEVYDLTEKLDANYKLLLPLVAKVTKDEQDAKPPPDAYDKLLKEMIFEPRGSVADKLINPDELAKQEAARLEKLENERLRRMRADGEEDEEASVAKPKHRSADDLDDGYFLAGEDDEGDDTLAYDLDGNLGTHLNGKKEAVLKGDENEDDDDKEGEEEEEEDSDEESDSEVDNLSDLKESESESEPEEAPKASKKKAKKSADTIPASLDTSIPFTIKMPKTYEDFTELLSKHATAQKAIIIERIIKCNHPKLEGVNRENVVKLYSFLLQYLKDLFEDASEQDIREHFQLLSKLMPYLYELTQLNPERMSNTLLEVIKEKYEEFRKNHKMYPSLDTLVYFKLVANLYSTSDFRHPVVTPCFIFIQHVLSRSRVRTRQEISMGLFLVTVVLEFVSQSKRLVPAVFNFLQGIVHMSIPKRDVEQLEITPPFERDGPLSKLLALPANTESTKLEPQQLQPTDLVTQTITPDFKVRALDTSLLLIKEALQLVEEHVGACYLAQPFLALLSRLPLESYPEHVHQHHKDATELAEKLAAQKMKPLAPAEKKPKALRLLEPRFEAVYDDKRRPKMSKAKEERAKLLHKIKREKKGAIREIRRDTSFVQMLRLKQTLQSDKERHEKVKRIYQEASVQQGELNELSRAKKKKKF
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein; Matrix side.
Sequence:
MAGWRWLEAALPLGIIAGMLCVMGNAQYYIHKAAHGRPKHIGNDMWDVAMERRDKKLVENLSAASHS
The following text describes a protein:
Function:
Collagen VI acts as a cell-binding protein.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Membrane; Peripheral membrane protein. Note=Recruited on membranes by CSPG4.
Sequence:
MTTIKMLQGPLSVLLIGGLLGVLHAQQQEAISPQEQEAVSPDISTTERNNNCPEKADCPVNVYFVLDTSESVAMQSPTDSLLYHMQQFVPQFISQLQNEFYLDQVALSWRYGGLHFSDQVEVFSPPGSDRASFTKSLQGIRSFRRGTFTDCALANMTQQIRQHVGKGVVNFAVVITDGHVTGSPCGGIKMQAERAREEGIRLFAVAPNRNLNEQGLRDIANSPHELYRNNYATMRPDSTEIDQDTINRIIKVMKHEAYGECYKVSCLEIPGPHGPKGYRGQKGAKGNMGEPGEPGQKGRQGDPGIEGPIGFPGPKGVPGFKGEKGEFGSDGRKGAPGLAGKNGTDGQKGKLGRIGPPGCKGDPGSRGPDGYPGEAGSPGERGDQGAKGDSGRPGRRGPPGDPGDKGSKGYQGNNGAPGSPGVKGGKGGPGPRGPKGEPGRRGDPGTKGGPGSDGPKGEKGDPGPEGPRGLAGEVGSKGAKGDRGLPGPRGPQGALGEPGKQGSRGDPGDAGPRGDSGQPGPKGDPGRPGFSYPGPRGTPGEKGEPGPPGPEGGRGDFGLKGTPGRKGDKGEPADPGPPGEPGPRGPRGIPGPEGEPGPPGDPGLTECDVMTYVRETCGCCDCEKRCGALDVVFVIDSSESIGYTNFTLEKNFVINVVNRLGAIAKDPKSETGTRVGVVQYSHEGTFEAIRLDDERVNSLSSFKEAVKNLEWIAGGTWTPSALKFAYNQLIKESRRQKTRVFAVVITDGRHDPRDDDLNLRALCDRDVTVTAIGIGDMFHETHESENLYSIACDKPQQVRNMTLFSDLVAEKFIDDMEDVLCPDPQIVCPELPCQTELYVAQCTQRPVDIVFLLDGSERLGEQNFHKVRRFVEDVSRRLTLARRDDDPLNARMALLQYGSQNQQQVAFPLTYNVTTIHEALERATYLNSFSHVGTGIVHAINNVVRGARGGARRHAELSFVFLTDGVTGNDSLEESVHSMRKQNVVPTVVAVGGDVDMDVLTKISLGDRAAIFREKDFDSLAQPSFFDRFIRWIC
The following text describes a protein:
Function:
Catalyzes hyaluronan degradation into small fragments that are endocytosed and degraded in lysosomes by HYAL1 and exoglycosidases. Essential for the breakdown of extracellular matrix hyaluronan.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MAVHLLPTYALFLTLLGTIQGSRNPMVPNQPFTTIWNANTQWCLEKYGVDVDVSVFDVVANPGQTFRGPDMTIFYSYQLGTYPYYTSAGEPVFGGLPQNASLDTHLAHSFQDILAAIPASDFSGLAVIDWEAWRPRWAFNWDTKDIYRQRSRTLVQGQHPDWPAPWVEAAARDQFQEAARAWMAGTLKLGQALRPRGLWGFYGFPDCYNYDFLSPNYTGQCPPGISAQNDQLGWLWGQSRALYPSIYMPAELEGRGKGQMYVRHRVGEAFRVALGVGDPNLPVLPYAQIFYDKTNRFLPLDELEHSLGESAAQGAAGVVLWVSWENTKTKESCQAIKEYVDTTLGPFLLNVTSGALLCSQALCSGHGRCARRPSHPEALLILNPTSFSIQLTRGGGPLTLQGALSLEDRMRMAVEFQCRCYHGWKGAQCEQRGMW
The following text describes a protein:
Function:
Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
Subcellular Localization:
Cytoplasm.
Sequence:
MPLSRWLRSLGVFLLPAPCWAPRERWLGYLQRPSLAYGCPVLGAWHSARWWCQVWTEEPRAFSSSVRMNGDQKLDVHNQEKQNFIQHFSQIVKVLTEDELGHPEKGDAITRIKEVLEYNTVGGKYNRGLTVVQTFQELVEPRKQDAESLQRALTVGWCVELLQAFFLVLDDIMDSSHTRRGQICWYQKPGIGLDAINDALLLEAAIYRLLKFYCREQPYYLNLLELFLQSSYQTEIGQTLDLITAPQGQVDLGRYTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANALKILLEMGEFFQIQENYGQKDPEKVARVKALYEELDLRSVFFKYEEDSYNRLKSLIEQCSAPLPPSIFLELANKIYKRRNSCSDLSPDESPVSVYSRDLPGNEDANPQASIFPLELGSPLAPAVRSSWSFAGVPGAQRLWMAEAQSGTGQLQEQKKGLLIAVSASVDKIISHFGAARNLVQKAQLGDSRLSPDVGHLVLTTLCPALHALVADGLKPFRKDLITGQRRSSPWSVVEASVKPGSCTHSMGSLYSQVSRLAPLSSSRSRFHAFILGLLNTKQLELWFSTLQEDAGLLSLLYLPTGFFSLARGSCPSLATELLLLLQPLSVLTFHLDLLFEHHHHLPLGLQQAPAPSGPPPALQQTMQAVLHWGGRLAQTLRGTSGEATTDSSTPSTRPPPGSWWDQLTQASRVYASGGTEGFPLLRWGPRRNGTTAEGTQEAPPPTEQTTPGRSVWLGRLFGVPGCSSETDSGAFKSRRPSSWLPPTVSVLALVKRGTPPEVPPEEPVKEPACMVQADRAVRALCDHTAAGPDQLSFQRGEVLRVISTVDEDWLRCGRDGVEGLVPTAVSVADGARIKTRTMEAQPL
The following text describes a protein:
Function:
Sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in cell membranes that participates in a variety of functions. Starting from lanosterol (lanosta-8,24-dien-3beta-ol), it catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of the sterol in the form of formate, and converts the sterol to 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, which is critical for ergosterol biosynthesis. Can demethylate substrates not intrinsic to yeast, such as eburicol (24-methylene-24,25-dihydrolanosterol) at a similar rate to lanosterol, and at a lower rate the 24,25-dihydrolanosterol (DHL) to 4,4-dimethyl-8,14-cholestadien-3beta-ol.
Subcellular Localization:
Membrane.
Sequence:
MIGTIAVLVIAILVIFAFKKSPSNIPPIVETIPFIGCFYQFAKNPLQLVRNSYDRLGEIFTLHLMGFKMTFVLGPEAQALFFRGTDEELSPKEAYRFVTPVFGKGVVYDSETEIMYEQLRFVKNGLVLSQLKKAVGIIQEETEKYFETKWGDSGEIDLLYEMNKLTILTASRCLMGKSINKSLGQSGQLADLYHELEEGLNPISFFFPNLPLPSFKKRDAARAKVAAIFHSIIQERRRSTDDSVDDVLYTLMNSKYKDGSVLEDEQIVGLMIGLLFAGQHTSSITLTYTIFYLLNNLEYFDETQKDINDIVQKENQGEINFDGLKRMNRLETVIREVLRLHPPLIFLMRKVMTPMEYKGKTIPAGHILAVSPQVGMRLPTVYKNPDSFEPKRFDVEDKTPFSFIAFGGGKHGCPGENFGILQIKTIWTVLSTKYNLEVGPVPPTDFTSLVAGPKGPCMVKYSKKQK
The following text describes a protein:
Function:
Essential component of the GPI mannosyltransferase 2 complex. Responsible for the transfer of the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.
Miscellaneous:
MISCELLANEOUS: Present with 6940 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MVRPQNVHWFIATIVFFIGFVHANTESILYKVPHNFPLKKPRDSSTYARDVNLISSISLSGEAMSQITIEANTTDLELHNTTYIELADLQRDETYQIKVCWSAIHPISINNLQTITIPRFTEFQGTKSDYARILVTFQVLSDSYPSEHAMVPIQVSLITTRLGIPVDIYPTLIVMVLLVAGLVVTRAPHVLNDLLLKF
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Miscellaneous:
MISCELLANEOUS: Present with 7400 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1.
Sequence:
MKVNLMLKRGLATATATASSAPPKIKVGVLLSRIPIIKSELNELEKKYYEYQSELEKRLMWTFPAYFYFKKGTVAEHKFLSLQKGPISKKNGIWFPRGIPDIKHGRERSTKQEVKLSDDSTVAFSNNQKEQSKDDVNRPVIPNDRITEADRSNDMKSLERQLSRTLYLLVKDKSGTWKFPNFDLSDESKPLHVHAENELKLLSGDQIYTWSVSATPIGVLQDERNRTAEFIVKSHILAGKFDLVASKNDAFEDFAWLTKGEISEYVPKDYFNKTEFLLADN
The following text describes a protein:
Function:
Transcriptional activator. Binds the cAMP response element (CRE). Activates transcription through box-B element and CRE. Seems to function synergistically with atf6. Regulates FGF21 transcription.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MCSAVQEMDAESGRVFFGQQGEEEEEVMAESSLGAEGPFSYPDALCGGAEKTLEEWALDPHCGLNDSESEDILHAMINPNEVYPSSGAPLESPSESDSGISEDPRSDSPPGGEPAPGGPPCAPPAVYQVVYDISGLDGVRTEPAQRSVDVISIELDAWNSQMLIPESCIVNELPMIPAGKPGTSLPSPAGPGDSHIADNFPLYPELCLTEEEQKLLTQEGISLPNNLPLTKAEERILKKVRRKIRNKQSAQDSRRRKKEYIDGLESRVAACSAQNQELQRTVEQLEKHNMSLLAQLRRLQSLIKQTATKAAQTSTCIMIIIFSLALILFPSYSPFRWGPAAAEEPYAPRGVISRNILTDSAASHELDVGHDIEAGHDLPPSSAVGGQSDDPGPPPVLFQQPIAGPEAATPEGAVQEQSQPRNGSLKEEGRTNELAMSLAAGKGQGPASADSAKPAHADEM
The following text describes a protein:
Function:
Catalyzes three sequential steps of tetrahydrofolate biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MKSLVNLWGIYPFIRNNSLHGFAKIPRIVSTIPRQLRFSSLRHPTRQMDLIHDTVVVENLNTFAVVGQDQWKRKEPQPVQIDVYMRNNVQLAGEKDELKSTIHYGIASKLLRKEIEGSFFTTPKDLVNKIASLCFEDVIDTSHVSIKLTLPKCVLRSKNGLHYYAERERNSTSNFVDRIEFSDLELATILGIHAFERQEKQRVCLNISFANTEVEALEIARAIAEYVEQSAFLTIEALVVNLSKYLCFTKNLDDISIKAEKPSAITFANASAVQIYRTRSYFLQESLHKYESTKNKIAYLSFGSNIGDKFEQIQTALSMLHKIEGIRVLDVSPLYETEPMYYKDQPSFLNGVCKIETRMSPINLLRACQSIEQEMGRIKTILKGPRCIDLDIVLYEDCVYESEVLTIPHLGLQEREFVLRPLLALSPDLVHPYTHQPLQEALDKLPSQGIRLYSSFDNKKIINGALTMGILNVTPDSFSDGGKVSQNNILEKAKSMVGDGASILDIGGQSTKPGADPVSVEEELRRVIPMISLLRSSGITVPISIDTYYSKVAKLAIEAGANIINDVTGGMGDEKMLPLAASLQVPICIMHMRGTPETMKALSIYEKDIVEEVAVELSSRVEAAVQSGVHRYNIILDPGFGFAKTPKQSAGLLGRLHELMKKPQFKDMHWLSGPSRKGFTGYFTGDASPKDRIWGTSACVTASVLQGVSIVRVHDTKEMSKVVGMANAIRYVP
The following text describes a protein:
Function:
Bifunctional regulator of neuronal activity in the mushroom body, and possibly other regions of the brain, that acts as a signaling molecule required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Reduces neuronal excitability by enhancing Sh/shaker K(+) channel activity; possibly by stabilizing Sh/shaker to increase protein levels, accelerating its activation kinetics, slowing C-type inactivation and enhancing recovery from inactivation. Specifically affects the A-type K(+) current. Antagonizes nicotinic acetylcholine receptors (nAChRs) to reduce synaptic transmission, possibly by preventing their localization to the cell surface. Required for regulation of neuromuscular excitability and plasticity at neuromuscular junctions.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Membrane raft; Lipid-anchor, GPI-anchor; Extracellular side.
Domain:
Consists of a single Ly-6 domain, adopting a three finger fold stabilized by 5 disulfide bonds. The first loop contains a region essential for protein folding or that is required for localization to the cell surface. The second loop mediates protein-protein interactions.
Sequence:
MWREKGNAIGNWLLAITAIFGFITLIWIPQASAECQTRSIYCYECDSWTDARCKDPFNYTALPRDQPPLMTCNGCCVKMVRHQRSRYEVVRRMCTSQLQINLFMVDHVCMMESSGNGHMCFCEEDMCNSSKDLYSHGHQLHLIITIAVAVSWLMGQLLNR
The following text describes a protein:
Function:
Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MAYSEEHKGVPCGFIRQNSGNSISLDFEPNIEYQFVERLEERYKCAFCHSVLHNPHQTGCGHRFCQHCILSLRELNTVPICPVDKEVIKSQEVFKDNCCKREVLNLYVYCSNAPGCNAKVILGRYQDHLQQCLFQAVQCSNEKCREAVLRKDLKEHLSAYCQFREEKCLYCKKDVVVINLQNHEENLCPEYPVFCPNNCAKIILKTEVDEHLAVCPEAEQDCPFKHYGCAVTDKRRNLQEHEHSALREHMRLVLEKNVQLEEQISDLHKSLEQKESKIQQLAETIKKLEKEFKQFAQLFGKNGSFLPNIQVFASHIDKSAWLEAQVHQLLQMVNQQQNKFDLRPLMEAVDTVKQKITLLENSDQRLAVLEEETNKHDTHINIHKAQLSKNEERFKLLEGTCYNGKLIWKVTDYKMKKREAVDGHTVSIFSQSFYTSRCGYRLCARAYLNGDGSGRGSHLSLYFVVMRGEFDSLLQWPFRQRVTLMLLDQSGKKNIMETFKPDPNSSSFKRPDGEMNIASGCPRFVAHSVLENAKNAYIKDDTLFLKVAVDLTDLEDL
The following text describes a protein:
Function:
Required for the proteolytic cleavage of the transcription factor pacC in response to alkaline ambient pH.
Sequence:
MVYPFELPTTSHLSFQSALSSHTHPSLPQSATTARHALRLALKAHNRLPRGFQRDSHLTSVLSAINDYLPYVVALAQGLNNGKPIDTTTPSTTTHLEEIRVAQRAELEPEWRATLASSSLRRPSTNRTRGTGVQYELAFILTTLGYILSSLARSGVTRTLYASTTPSAEQRTAAVQTATKHLLQASTIHSFLSSSPYFATVSEAATLPDLAPATQAALSSLALAEATLLTVLKDDSYVVACIQARNPNDKDWMVRAPEIPKVRAHLFARLCIRAAEYAEQAATGLSSVAAEGRKAGVDEDVARYAHVLGLVARARACRFFGVDAELAGKVGEGIAWLRAAKGALGLRNTGSASAEEVTTKSRGLSKLKLGFRERREERKLEKGAGGERVDKGGLGPGDNAGREEEGRVLEMLETKWVRANDTLNTQLIPSSADYVANLPSGRDVLPPQPPYTPPSLDEERLFQMRGPPTELELNPGSDDGDSDFESQAAGDAHTPGAFPGRADNAYY
The following text describes a protein:
Function:
Has a role in cell wall biosynthesis where it is involved in maintaining cell wall strength and shape.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MFGVYFVLLFLSSALIHVANAGSNAEWRKRIIYQILTDRFAVDDGSTDNPCDPDANQYCGGTWKGIENKLDYIEDMGFNAIWISPIDKNIEGDIDGAGYAYHGYWNTDYESLNEHFGTEDDLVSLITAAHKAGIWVMLDSIVNSMALAPPLADADYSSLNPFNKESYFHPYCLIDWDITDNETNVMDCWQDSGVLLADLDVESSDVSSYLSDHFKSLISKYDFDGLRIDAVKMMNYTFFPDFVDATGVYSVGEVFSYDPDTMCSYMSVLPGVTNYFLQLYINFSFTATGAGFTLIPTYQEVMASNCSKYDSTLMLTFIENHDLYRFPYYTSDQSQIMGALSFVLIWDGIPSIFYGQEQGFNGGEDPANRPALWLTDYDQSNPYYTVIKTMVAFRKFVITQDPDWVTSTYQSIESAVDHYVGQKNDVLVMFNNMGVTNNLTIYEVETNYTANEVVSDVFGHRTLTVGADKTLTASMTNGYPLIMYPHSKMSGFTLPTVNRTVMPSTSATATTTVYTSYYSPSYSARSFTGTGSIFTISSSSRLILSFKTLVFGLGVTAMLFVLFF
The following text describes a protein:
Function:
Acts as an electrogenic sodium (Na(+)) and chloride (Cl-)-dependent sodium-coupled solute transporter, including transport of monocarboxylates (short-chain fatty acids including L-lactate, D-lactate, pyruvate, acetate, propionate, valerate and butyrate), mocarboxylate drugs (nicotinate, benzoate, salicylate and 5-aminosalicylate) and ketone bodies (beta-D-hydroxybutyrate, acetoacetate and alpha-ketoisocaproate), with a Na(+):substrate stoichiometry of between 4:1 and 2:1. Catalyzes passive carrier mediated diffusion of iodide. Mediates iodide transport from the thyrocyte into the colloid lumen through the apical membrane. Mediates sodium-coupled electrogenic transport of pyroglutamate (5-oxo-L-proline). Can mediate the transport of chloride, bromide, iodide and nitrate ions when external concentration of sodium ions is reduced.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein.
Sequence:
MVTPGDIGSFTVWDYLVFALMLLISAVIGIYYAFAGGGQKTSKDFLMGGRSMTAVPVALSLTASFMSAVTVLGTPAEVYRFGAMFSIFAITYAIVVVISSEVFLPVFYRLGITSTYEYLELRFNKFVRLLGTILFIIQTILYTGIVIYAPALALNQVTGFHLWGAVVATGVVCTFYCTMGGLKAVVWTDVFQVGIMVAGFSSVIIRAVVVQGGIGPILNDSYYGDRLNFWDFNPSPLQRHSFWTIVVGGTFTWAGIYGVNQSQVQRYIACKTRFQAKMSLYVNLLGLWAILACAVLSGLAMYSIYKDCDPWTAKFVSAPDQLMPYLALDILRDYPGLPGLFVSCAYSGTLSTVSSSINALAAVTVEDLIKPYFKSLSEAKMSWISKGTSLIYGAICIAMAALASLMGGLLQAALSIFGMVGGPLLGLFTLGIIFPFANSLGAVIGLLSGFTISLWVGIGSQIYPPLASSNLAKPLSLVGCNFTSIESNWTSTVMPMMTTLFPETQVSSRPELADSWYSLSYLYFSTLGTLVSVIVGLIVSLLSGGLKQNINRDFLLTSEDFSYLNVLFSSCKKKGQEEKVEVLNWKARSTDTYVEQGTDNPTFNHMEMTSTEKREKMNGIIA
The following text describes a protein:
Function:
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.
Subcellular Localization:
Cytoplasm, cytoskeleton. Nucleus, nuclear pore complex.
Sequence:
MSEETSVPILKASDLAEEIQTKIFELSSQAIATYKIEKDIAAFLKKELDQLYGPTWHVIVGKSFGSYVTHEQGYFIYFYIGDMAFLIFKSG
The following text describes a protein:
Function:
May bind androgens and other steroids, may also bind estramustine, a chemotherapeutic agent used for prostate cancer. May be under transcriptional regulation of steroid hormones.
Subcellular Localization:
Secreted.
Sequence:
MKLLMVLMLAALLLHCYADSGCKLLEDMVEKTINSDISIPEYKELLQEFIDSDAAAEAMGKFKQCFLNQSHRTLKNFGLMMHTVYDSIWCNMKSN
The following text describes a protein:
Function:
Functions in an input pathway to the Kai circadian clock. Senses oxidized quinones via its C-terminal pseudo-receiver domain, providing a link between cell metabolism and the clock. Affects the ratio of phosphorylated to unphosphorylated KaiC, binds quinones via its pseudo-receptor domain. Quinone-binding destabilizes the protein rapidly. Autophosphorylates, does not transfer the phosphate to its pseudo-receiver (PsR) domain. May play a role in cell division, as suggested by its polar location and increased cell length in a deletion strain (Probable); Member of the two-component regulatory system CikA/RpaA output pathway from the circadian clock, negatively regulating kaiBC expression independently of labA and of sasA. One of three clock output pathways. Dephosphorylates phospho-RpaA, enhanced by KaiB and KaiC, has only modest kinase activity on RpaA. A very robust clock is reconstituted with KaiA, KaiB, KaiC, SasA, CikA and RpaA; output is measured by transcription from an appropriate reporter.
Subcellular Localization:
Cytoplasm. Membrane. Note=Localized in tight foci at one or both cell poles. Both soluble and membrane-associated.
Domain:
The N-terminal domain is followed by a GAF (phytochrome-like) domain that lacks the conserved Cys residue for ligand binding, a histidine kinase domain and a C-terminal response regulator domain without the conserved Asp residue that is phosphorylated (pseudo-receiver domain, PsR). Autophosphorylation is dramatically reduced in the absence of the N-terminus (residues 1-183), and lacking in the absence of the GAF domain; removal of PsR increases autophosphorylation 10-fold. Thus PsR may suppress the histidine kinase domain. The GAF and PsR domains are required to complement the deletion strain. The PsR domain is responsible for DBMIB sensitivity and binds quinones directly. A KaiB mutant locked in the KaiB(fs) form binds the CikA PsR domain.
Sequence:
MLAPSSNCSLASQRLTPEGFAQLQSALQDFVATLPQAFYWDSRSLHTHLRTQTGDCAIAIAAGFQLLLLGRTAAEYCQPHPLSEPHHVSVQFGADSIQRYCQATNLPVEYQPALAQLGDLSLNPDLISQFSNLLIAAIAADRAPLAAQYPAVSVCQPLEQALHWQEEQDRLISQVSAQIRLSLDLSEILTTTIREIRQLLNADRAIIYQFKPQCLDAGLDQRWPLYIPSQSYITYEDRRNEALLSVIDPLVQPGLLITTEEWQRFQQGETLLIDSVGFYKERLPEQYSFYERVQVRSVCKIPILVQGRIWGLLVAHQCQQDHRWQPRERDILQHLAEHLSIAIYQAQLYGQLQDQTQTLENRVLERTQELIDALALAQAANAAKGEFLATMSHELRTPLTCVIGMSSTLLRWAFGPLTERQREYIKAIHDSGEHLLELINDILDLSQIEAGKAALQVRPFSLSRLATQTLNTLQEKARLGEIQLMLDLQLNNRVDVFRADPKRLRQILINLLSNAVKFTEPQGTVFLRVWREGDRAIFQVSDTGIGIPESEQAQLFQKFQQLDTSIRRQYGGTGLGLALTKQLVELHGGHIQIESTVGQGSTFTVWIPEQTLIEPVEPRPSIDNLPAGHILLLEEEDEAATVVCEMLTAAGFKVIWLVDGSTALDQLDLLQPIVILMAWPPPDQSCLLLLQHLREHQADPHPPLVLFLGEPPVDPLLTAQASAILSKPLDPQLLLTTLQGLCPPNLSEGDRPSS
The following text describes a protein:
Function:
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSSNQDVPLPFTSSRPLPSRQPTTSRPGGTLKRNKTLTRPERHVAPAPLVAPPTQSFSPTSPLPQSDGFLNIDWWRLWAYATTFWAPPVLLRWFGIKEKQSRQAWREKIALCWIAVLLGGVVGFVTMGLQRALCPADQQNQSMYQRLGDTNMTLSISGWAFNISTSITQSNVDFYSLANQMPGQDITDLFTRSVSDYPACTSSLAYSSGAFCNSTSSSSGTSCVLSSMSQETFDSLQIQNTSLLEGYSWDQVAKLENYMVIDGYVLNMSPYLSFNPTAVEGDEVDSIIRHVLSNQTGSGKDATRLFFNRQVPQDAVGCMKARYVAGRIDKITPGCFVASFFLYVSLVVILAVVLARFAMACVFNWFLSEKLVKPVTEKELGRKGINPTIMPEGANVSVNNKLGTAPWAGGGGAAEGKGGGVGPGKKLVNGKKINPLSPLPSPSHSLPNAPLITLSQIGPELFTVCLVTCYSEGPSSIRGTLESIASTNYSDRRKLIWVVCDGMITGQGEKRSTPDVCVGMLDADGRFGNPVPMGYEAVGSGQKRENRAMVYAGHYVSRNGHRTPTIIVVKCGMPQEATEKKPGNRGKRDSQLILMNFFSRVTYNDRMTPLDFDLFRKIWTLMGVTPDYFEAVLMVDADTRIYPDSLKHLVNCMHHDNMIMGVCGETRIANKRQSWVTAIQVFEYFISHHHVKAFESVFGGVTCLPGCFSMYRIKARKDGDNDWVPILVKPEIVNEYSQSEVETLHQKNLLLLGEDRFLSTIMLRTFPRRKNIFLPQARCRTVAPDTFSVLLSQRRRWINSTVHNLMELVRVRDLCGTFCFSMQFVVFMDLVGTVVLPVAICLTFALIVNSIITPPKSFEEAIPLMLLAIVLGLPAILILITTRKVVYVAWMLVYLLALPIWNFVLPVYSFWHFDDFSWGETRRVEGEIRSKGHDDSTAVFNGTTIPLRRWEDWEKSRLRKLRREEKRRKEMERQFGAGFHGDPRLGGDLRGMGMGERPWARSEYDSDNGSLYSSEEDMWGGEVGGYNEHNPAFPPPPIALPPTDDPVSNINGETLGMDEMAAILDSGFDDDPQSQSTYPPLSHPRPHAHPPPPPISRTLANAPSPVRRHQHEYNAPQPRFNRIDSPSFGSGPNSARSSPHSADAGRYAAGEYVSIDRQDTNDLDAQMPHSGGSVSSSVESRPHGVGHAKKRSGGGAGIGAGTGARGGGYGPLGPLADVNEVGRGQTRGYGGSGKDR
The following text describes a protein:
Function:
Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2. Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2: cleaves SREBPs within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Mature N-terminal SREBP fragments shuttle to the nucleus and activate gene transcription. Also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B). Involved in intramembrane proteolysis during bone formation. In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the second step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
VKMITFIIVVLLFWTALNFTDYVFKSCMLYPYISMLERNGLSLRLFRVQFYFTRFNRVVHQLGRKKPRFLYWWFTLGAVVSILSIAPAVWVLATSAMSIGVDVAACYPATYDTSMSDTIQIEHAEKTSFCVNLEKGKNVMPGINLPISDIFYYISTLVVCSIFHEFGHALAAVRENVRIQGCGLFVLGIFPGAFVDLPKDQVTVLAPWKQLKIYCAGIWHNLVAVAVALLLLTGNRFLMTPFYKEHAGVTVISVAEESGAYGPNGLLPGDHIIAVDACVVRDPATWKSCLVQAVLIPQPGYCQRKVLVQSEGTCLELHPLFYFSSECCHGQSNNSLCFSYLDHDEKREVCLPARHTLETSHGYCNSSCQTDDYYCLKPVLDNTTKLVQVKRENWPAMLFLGPPAELWHTVSVIKWVPRQKYLSVLPVHVYEVFLHYIMSFSGALALLNAIPCIALDGQWILQGLIKLLTQAFPCLRPSRKWLYLFLVLSGTFLLAINVVLGFWKLLGRR