lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. In the DCX complexes, acts as a scaffolding subunit required to stabilize the complex.
Sequence:
MEEDKGEILGNFPSFNAMNFTKFDPQSNDKKKKKISVYLSTEESKPQQVIKKDRSSILLRYLYQQLDKKKHENLKHKINTGDSQASADGNPPDDEPRRKIFKPSHSKDDVTSTSFSEKT
The following text describes a protein:
Function:
Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSRGWDMVLSRIAIMAPSMVELMFTLTVQSRAVASTHDYSCSLFASLGPQISWRTVFIVEYFGPLVIPILFLYPLRPYLYYNFDNIPQPTDIQRLVCALLVVHFLKREYETVFVHRFSNATMPARNIVKNSGHYWLLAGCNIAYWVFRPDSSAATGRVSPALVYTGLALYVFGELANLNTHLVLRNLRRPGTTERGIPSGFGFSAVTCPNYFFEVVSWVGVYLVSGLSWSVLFFIAVAAGQMALWAKKKERNYRKEFGDKYKRKRYAMIPGLI
The following text describes a protein:
Function:
Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
Sequence:
MSQDSNAKINYLLNIINSQRKPPIINNPSISSNTNRVRTKTKTRTRTSPNSKTKIKTKTMNTMKTNNRNSILTETEELFTNESQIIESFNSNCTIVDSNSDFHDKLHVYKSPIIDITKYFSPTVESQMDLELIILNEYYLKTHQHHQEQQNDEDEDEDEDDELNYFYIDAHLKYILSSLIDPMPSGYQVLDVNHSWMIYWLLNSYYLIQNPTMEINQSILDLIVNKITKCINYGDSLSGVPFDGIGGGNNQLGHLASTYAAILTLILTDQYELLDNLRELIRDWLLTLKKRSSCGSGASFIMHENGEMDARSTYCALIIINLLNLTNYEENSSSPEELDPLIDGVENWLNSCQTYEGGFSNIPNTEAHGGYTYCALASYFLLYDNRKQFSSGSTSSSSRSRSNIDWEKLLEWSVHRQHELEGGVDGRTNKLVDACYGFWIGGLSPLLQLIIMNSSQGQGQQQEVKVFDEEKLRQYLLIIAQDESGGFKDKPGKQVDYYHTNYSLSGLSILEHSYKFSQDDEGRSLAFQIDVEREEEEGGGGGGGDNFTNPIHPVFGIPIKFVKKCHDYFKLKPISKPKKRAEQKR
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase component of the peroxisomal translocation complex. The two types of peroxisomal matrix targeting signals, PTS1 and PTS2, are first recognized in the cytosol by their receptors PEX5 and PEX7, respectively, which then carry the cargo to the peroxisomal membrane. The peroxisomal targeting signal (PTS) receptor-cargo complexes interact with peroxisomal membrane protein (PMP) components of the docking complex. They have then additional downstream interactions with the translocation complex, leading to the transport of fully folded and oligomerized cargo into the peroxisome matrix. The peroxisomal translocation complex forms the retrotranslocation channel with each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 and PEX20 through the peroxisomal membrane (By similarity). Specifically catalyzes monoubiquitination of PEX5 and/or PEX20 at 'Cys-6' and 'Cys-8', respectively, a modification that acts as a signal for PEX5 or PEX20 export from peroxisomes to the cytosol, thereby promoting PEX5 and PEX20 recycling.
Subcellular Localization:
Peroxisome membrane; Multi-pass membrane protein.
Domain:
The three subunits of the retrotranslocation channel (PEX2, PEX10 and PEX12) coassemble in the membrane into a channel with an open 10 Angstrom pore. The RING-type zinc-fingers that catalyze PEX5 or PEX20 receptor ubiquitination are positioned above the pore on the cytosolic side of the complex.
Sequence:
MPNRLIPLANPANRVLQLDAKLLDNEISDMLYRQLSGAFNSNRLPSWLGRIHSNYASELKLLLELLIFKVTVWNKHSSYGLTLQNLVMYDGGVHNKKFRSKQQSELRVTKKILLLSSVLLGYFVKKIQSYVYSFEDYDLETDGEDLSTLERIRLKTIKLLKSQISTLEKAHSVLSLVNFVTFLVSGSFPDLTTRILNIRFKPLVTTQVAFASNPETISYEFQNRQLVWNTLTEFIVFILPALSVPKFTKSLVSSITGTSPKSSQVTDEDLKVFSSLPERVCAICFQNSQNSDSGAQNDISLNDTLVTNPYETTCGHIYCYVCILSKLQIFKEEGKNLPKSDPNKYWHCLRCNEPASWCRVYTGDVEDALRQKAVEEVTEDEDASSEDEEKRDQDSEGAKTVSQSFHHVNGSDYQTASFIEQAELNENEYTDGSEVEIYDAEDEYTDEEVDDDSPGFFVGAL
The following text describes a protein:
Function:
Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
Sequence:
MTIANSTDFMVENAVCDFPSTPEEERRIVSELTTESEDNLKEGNLYFVISKRWYTRWEKYVEQPTTNGCESPRPGPIENSDIIENTTSSDDPQLRRLLVEGEHYVLVPQQVWNRLAEWYSGGPPIPRKLICQGFYSRSFSVEVYPLCLLLTDARDDSITAIRLGKQASIKELYEKVCAMTEVSQEKAHIWDYFGKRKGQLLDPSSNKSLEESSLHMDQDILLEVDGSSSSHIAMSSAGNELALVPLEPSRSLVTIAGGPTLSNGHSTTSKFSLFPRITSEDDGCDSLSILGKGERGGLAGLSNLGNTCFMNSALQCLAHTPPIIEYFLQDYSEDINRDNPLGMCGELAIAFGELLKKLWSSGRNAVAPRSFKTKLARFAPQFSGYNQHDSQELLAFLLDGLHEDLNKVKRKPYIELKDSDSRPDEEVAEELWNYHKARNDSVIVNVCQGQYKSTLICPVCGKISITFDPFMYLSLPLPSTLTRQITVTLFYCDGSHLPMPYTVTVPKYGSCRDLITALGTACCLTNDESLLLAEIYDHKVFRYFENPLESLNLIKDDEHIVAYRMKQMQKGSGKAKLEILHGGQERAVLESVRGRDVKLFGTPFVTYVNTERLSGPDIDAVISGFLSPLHRVQASSKIHNGVENGHLPNADTVEASGSITSPDTEIEDACDRELSFRIFLTDERGLDFKPLKSDSSLKPGIVTRVLVEWNEGEHENYDSSYLNDLPEVHKTSFSAKKTRQEAISLFSCLEAFLAEEPLGPDDMWFCPGCKEHRQANKKLDLWKLPDILVFHLKRFTYSRYLKNKIETFVDFPINDLDLSKYVKNKNGQSYLYELYAVSNHYGGLGGGHYTAYAKLIDDNKWHHFDDSHVSSVNESEIKNSAAYVLFYRRVGSKIESQTAEVSMADMD
The following text describes a protein:
Function:
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
Subcellular Localization:
Cytoplasm.
Sequence:
MHLNAIAISAFRNIDHVEISFDRRFNVLHGANGQGKTSVLEAIYLLGTMKSFRMAKAHDLIAWNAPHSLVRGDIDKAGVRREIALYLGREGRKARIDRKPVTKLADFFGAVNAVVFSPEEIGMARGGPELRRRYLDRAIFNGDLGYLLLHHEYHRLLKQRNALLRRGERDGLEVWTIQLAEAGARLMVKRRAYLSQIEPLVRQFYRDIAGAGQEVGLAYRCHGLASAEGERDCAAALRELMAAHEAEELRRGATGVGPHRDDVDFILNGRVIRHHGSQGEQRSFVLAVKMAEIEYLERLNGAPPVLLLDDISSELDPERNANLMTFLRGKRMQVFITTTDVSTLRLEGIDTHASFRVSRGTVTPV
The following text describes a protein:
Function:
Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (By similarity).
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein; Periplasmic side.
Sequence:
MNLNRYVIAGGLSLAFHALLLITTDEAQVFAMPAGNPTQSVSINMVSMPKVAPAQPEQTQTEQSKPESVKPTPVQEVVKTPPAKPKVKPHKPKPQTVKKPVPAEQVPSKSVAKPQPEKVERTAETAQKPAPTPNQQPSQPTAASQGITSQPILVDKPALVSAQVQPRYPRIARKRGIEGTVMYEIWLDAQGNQIKQQLLSSSGTEALDQSALEAIKQWKFSPHILDGVPVAHRIHIPIRFKLEG
The following text describes a protein:
Function:
Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MPDERTTGREGVGAAVLAAGFGERLRECGRPKPLARVAGLTLLERTVRTLRAGGLEGEIVVVVGHRGEEVAGHCKARGLPVRVVENPDYPRGNGTSVLAAMRFLPERFVVAMVDHIHTPESVRRLLRCEGDFVAAVDTRPVYADPGEATRVRLEGGRVVEFGKNLPRYDGLDAGLFLCSRPALERLREASGGERLSWNDLKRAWLASGGEVVACDLAGAPWTDVDTPQDLRLSEEMVLGWAASGNDGPVSRHINRRISRRITRRLLDTPLSPDQVSLLSFALAALGAGLLAAGRLRLGGALVQLASIVDGCDGELARARLESSPRGAVFDATLDRWADALIISGLALGAGTRLAAAAGYPALAGALLVSYTRARWEAALGRMPSRFTGLGATRDVRLAVLALGGLLGAPGAALLATGALGNAEALRRLLALKRGRS
The following text describes a protein:
Function:
Fatty acid desaturase that introduces a cis double bond at the 5-position in 18-carbon polyunsaturated fatty acids.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
The cytochrome b5 heme-binding domain acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome.
Sequence:
MMETNNENKEKLKLYTWDEVSKHNQKNDLWIIVDGKVYNITKWVPLHPGGEDILLLSAGRDATNLFESYHPMTDKHYSLIKQYEIGYISSYEHPKYVEKSEFYSTLKQRVRKHFQTSSQDPKVSVGVFTRMVLIYLFLFVTYYLSQFSTDRFWLNCIFAVLYGVANSLFGLHTMHDACHTAITHNPMTWKILGATFDLFAGASFYAWCHQHVIGHHLYTNVRNADPDLGQGEIDFRVVTPYQARSWYHKYQHIYAPILYGVYALKYRIQDHEIFTKKSNGAIRYSPISTIDTAIFILGKLVFIISRFILPLIYNHSFSHLICFFLISELVLGWYLAISFQVSHVVEDLQFMATPEIFDGADHPLPTTFNQDWAILQVKTTQDYAQDSVLSTFFSGGLNLQVIHHCFPTIAQDYYPQIVPILKEVCKEYNVTYHYKPTFTEAIKSHINYLYKMGNDPDYVRKPVNKND
The following text describes a protein:
Function:
Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. Its dissociation from the complex determines the transition from state pre-A1 to state pre-A1*. Inhibits mRNA translation in a cytoplasmic polyadenylation element (CPE)-dependent manner (By similarity).
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice site.
Subcellular Localization:
Nucleus. Nucleus, nucleolus. Chromosome, centromere. Cytoplasm. Cell projection, axon. Cell projection, dendrite. Cell projection, filopodium. Note=Translocated from nucleolus to nuclear foci in response to UV damage (By similarity). Detected in axons, dendrites and filopodia. Colocalized with EIF4E in neurites.
Sequence:
MAALGVLESDLPSAVTLLKNLQEQVMAVTAQVKSLTQKVQAGAYPTEKGLSFLEVKDQLLLMYLMDLTHLILDKASGGSLQGHDAVLRLVEIRTVLEKLRPLDQKLKYQIDKLIKTAVTGSLSENDPLRFKPHPSNMMSKLSSEDEEEDEAEDDQSEASGKKSVKGVSKKYVPPRLVPVHYDETEAEREKKRLERAKRRALSSSVIRELKEQYSDAPEEIRDARHPHVTRQSQEDQHRINYEESMMVRLSVSKREKGRRKRANVMSSQLHSLTHFSDISALTGGTVHLDEDQNPIKKRKKIPQKGRKKKGFRRRR
The following text describes a protein:
Function:
Cyanamide hydratase involved in the detoxification and/or utilization of cyanamide, a toxic nitrile compound distributed widely in the environment.
Miscellaneous:
MISCELLANEOUS: This enzyme is highly specific for cyanamide.
Sequence:
MSSSEVKANGWTAVPVSAKAIVDSLGKLGDVSSYSVEDIAFPAADKLVAEAQAFVKARLSPETYNHSMRVFYWGTVIARRLLPEQAKDLSPSTWALTCLLHDVGTAEAYFTSTRMSFDIYGGIKAMEVLKVLGSSTDQAEAVAEAIIRHEDVGVDGNITFLGQLIQLATLYDNVGAYDGIDDFGSWVDDTTRNSINTAFPRHGWCSWFACTVRKEESNKPWCHTTHIPQFDKQMEANTLMKPWE
The following text describes a protein:
Function:
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane.
Sequence:
MSSARVPPQQQQQQQQQQAPEFYGPDTPTFDLSWDYNYDNALAAPPNNVPPVVHSGENRIITAQPQSQQRERDGVSLRIPSPPPGDAIRSVNSPFLTPFSPRAGLDFLYGLPSVFIQQSYELNELLSGVASDNRFTVRGPSNEALYGASETSDPKDRFWGSLRPFSLSLVDRSHQEVLLFRKNLGCGVFCCFCKNQFLEVWAAPGELIGCIQQDYGVLSQEIVLLNSDINTMFRIPIPFLNALRMPKETHFRVLDRDRMTQKGTITRAWNVNTASYTNNIYYSDPTMDVKFKSLFIAAAFMLEYLYFQSNCC
The following text describes a protein:
Function:
Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate. Does not display threonine synthase activity like the paralog protein ThrC.
Sequence:
MGRFILKCLKCGREYSQEYRLTCENDDSFLRAEYLEKKLELRKQPGIGRFHSWLPVQEELTTEAGPITYKSEALARELGLSNLYIGFSGYWPEKGAFIKTCSFKELEAHPTMQLLKESGGKAIVLASAGNTGRAFAHVSALTGTDVYIVVPDSGIPKLWLPEEPTDSIHLISMTPGNDYTDAINLAGRIAKLPGMVPEGGARNVARREGMGTVMLDAAVTIGKMPDHYFQAVGSGTGGISAWEASLRLREDGRFGSKLPKLQLTQNLPFVPMYNAWQEGRRDIIPEIDMKDAKKRIEETYATVLTNRAPPYSVTGGLYDALVDTDGIMYAVSKEEALDAKALFESLEGIDILPPSAVAAASLLKAVEAGNVGKDDTILLNIAGGGFKRLKEDFTLFQIEPEITVSNPDVPLEELKL
The following text describes a protein:
Function:
Important for the overall degradation of proteins in lysosomes.
Subcellular Localization:
Lysosome.
Sequence:
MTGLWLLALPLITSAMGASEHDEVQFKFWMTQHKKEYSMMEYHQRLQIFTENKKLIDKHNEGNHSFTMALNQFSDMTFTEFRKAFLWSEPQNCSATSGNHLSSKGPYPDSIDWRKKGNYITPVKNQGACGSCWTFSTTGCLESVTAIATGKLLSLSEQQLVDCAQDFNNHGCNGGLPSQAFEYIMYNKGLMTEQDYPYTAMEDKCMYKPSLAAAFVKEVVNVTAYDEMGMVDAVATHNPVSFAFEVTSDFMNYHQGVYTSTECHSTADKVNHAVLAVGYGQENGTPYWIVKNSWGSKWGMDGYFLIERGKNMCGLAACASFPVV
The following text describes a protein:
Function:
Transcription factor that may play important roles in patterning the embryonic brain.
Subcellular Localization:
Nucleus.
Sequence:
MATTASNHYNILTSSPSIVHSEPGSMQQATAYRDAQTLLQSDYSLQSNSHPLSHAHQWITALSHGEGGPWSSSPLGEQDIKPAVQSPRDEMHNSSNLQHQSRPPHLVHQTHGNHHDSRAWRTTTAAHIPSMATSNGQSLIYSQPSFSVNGLIPGSGQGIHHHSMRDAHEDHHSPHLSDHGHPPSQHQHQSHQSHHDHSDEDTPTSDDLEQFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLNKWLEEADSTSGSPTSLDKIAAQGRKRKKRTSIEVSVKGALESHFLKCPKPAASEITSLADSLQLEKEVVRVWFCNRRQKEKRMTPPGGPLPGTEDVYGDTPPHHGVQTPVQ
The following text describes a protein:
Function:
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MYPKLLTIPQFQFLKYKIGPIVIYSWGTFVALGFLIGILLAMRWAKRENIDPDHVLNVAVWSIISSIIGARAVYVIKYWNAYKTNPITILHLWDGGLIFFGGFLVALVVVLLYLKRYKIDYWKFLDILAPAVAIGSAIGRIGCFLNGCCYGYETPLLWGVKFPNVYGYRHATELYYTIAFLIVFIYLLRVKSRKTFDGEVATNFFIYYSFAFFLVEIFRDNPRNFLYLTGSQTVSLLLIAFGIYAYRRRRAGRPIIPEQCLFWKIMTTKPKVSKKR
The following text describes a protein:
Function:
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) (By similarity); Confers high-level resistance to the antibiotic mupirocin (pseudomonic acid A), an Ile-analog that competitively inhibits activation by Ile-tRNA synthetase, thus inhibiting protein biosynthesis.
Subcellular Localization:
Cytoplasm.
Domain:
IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)) (By similarity).
Sequence:
MTDNAYPKLAGGAPDLPALELEVLDYWSRDDTFRASIARRDGAPEYVFYDGPPFANGLPHYGHLLTGYVKDIVPRYRTMRGYKVERRFGWDTHGLPAELEVERQLGITDKSQIEAMGIAAFNDACRASVLRYTDEWQAYVTRQARWVDFDNDYKTLDLAYMESVIWAFKQLWDKGLAYEGYRVLPYCWRDETPLSNHELRMDDDVYQSRQDPAVTVGFKVVGGQPDNGLDGAYLLVWTTTPWTLPSNLAVAVSPDITYVQVQAGDRRFVLAEARLAAYARELGEEPVVLGTYRGAELLGTRYLPPFAYFMDWPNAFQVLAGDFVTTDDGTGIVHMAPAYGEDDMVVAEAVGIAPVTPVDSKGRFDVTVADYQGQHVFDANAQIVRDLKTQSGPAAVNGPVLIRHETYEHPYPHCWRCRNPLIYRSVSSWFVRVTDFRDRMVELNQQITWYPEHVKDGQFGKWLQGARDWSISRNRYWGTPIPVWKSDDPAYPRIDVYGSLDELERDFGVRPANLHRPYIDELTRPNPDDPTGRSTMRRIPDVLDVWFDSGSMPYAQVHYPFENLDWFQGHYPGDFIVEYIGQTRGWFYTLHVLATALFDRPAFKTCVAHGIVLGFDGQKMSKSLRNYPDVTEVFDRDGSDAMRWFLMASPILRGGNLIVTEQGIRDGVRQVLLPLWNTYSFLALYAPKVGTWRVDSVHVLDRYILAKLAVLRDDLSESMEVYDIPGACEHLRQFTEALTNWYVRRSRSRFWAEDADAIDTLHTVLEVTTRLAAPLLPLITEIIWRGLTRERSVHLTDWPAPDLLPSDADLVAAMDQVRDVCSAASSLRKAKKLRVRLPLPKLIVAVENPQLLRPFVDLIGDELNVKQVELTDAIDTYGRFELTVNARVAGPRLGKDVQAAIKAVKAGDGVINPDGTLLAGPAVLTPDEYNSRLVAADPESTAALPDGAGLVVLDGTVTAELEAEGWAKDRIRELQELRKSTGLDVSDRIRVVMSVPAEREDWARTHRDLIAGEILATDFEFADLADGVAIGDGVRVSIEKT
The following text describes a protein:
Function:
Part of the yadCKLM-htrE-yadVN fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches.
Miscellaneous:
MISCELLANEOUS: The operon is cryptic under classical laboratory conditions, but is functional when constitutively expressed.
Subcellular Localization:
Fimbrium.
Sequence:
MKTIFRYILFLALYSCCNTVSAYTSFIVGNNAGVDNYRGPSTAAQMTFNYTSTASNLVFYKPTQLGPTGVKMYWSYLDTGTGGGILYCNTSGRANPGPITIENAMVYSGKDYGGHKLFNTSVPGLYYTMLISRVWSAYDTITDIQSPGIYIGDPSNQEFFFSVTDSDLQTKGCNKADDYDKFWAIGGIVHNITVEFYTDTNFDPTLNQQVQLSSSSNYLYSFKAYSPGTKVVDHSNHIYVNFTLNNVKLTLPTCFTSILTGPSVNGSTVRMGEYSSGTIKNGASPVPFDISLQNCIRVRNIETKLVTGKVGTQNTQLLGNTLTGSTAAKGVGVLIEGLATSKNPLMTLKPNDTNSVYIDYETEDDTSDGVYPNQGNGTSQPLHFQATLKQDGNIAIEPGEFKATSTFQVTYP
The following text describes a protein:
Function:
A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity). Identical to MRCH which is implicated in the formation of both melanin in the cuticle and ommochrome in the epidermis of armyworm species; Diapause hormone (DH) is responsible for induction of embryonic diapause; The three SGNPS are far less active than DH in inducing diapause eggs. Beta-SGNP expressed higher pban activity than PBAN-I, but alpha- and gamma-SGNP were far less active in pheromonotropic activity.
Subcellular Localization:
Secreted.
Sequence:
MYKTNIVFNVLALALFSIFFASCTDMKDESDRGAHSERGALWFGPRLGKRSMKPSTEDNRQTFLRLLEAADALKFYYDQLPYERQADEPETKVTKKIIFTPKLGRSVAKPQTHESLEFIPRLGRRLSEDMPATPADQEMYQPDPEEMESRTRYFSPRLGRTMSFSPRLGRELSYDYPTKYRVARSVNKTMDN
The following text describes a protein:
Function:
Binds cholesterol and may regulate the distribution and homeostasis of cholesterol in hair cells (By similarity). May play a role in angiogenesis (By similarity).
Subcellular Localization:
Lysosome membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein. Note=Localizes to the stereocilia and the apical region of hair cell, apparently around and just below the cuticular plate. Co-localized with cholesterol in the stereocilia.
Sequence:
MKGDMDLSVLPNNNHPDKFLQLDVKSLMRSSTLLQASLARFPGGNYPATQHWQNLVYSQREKTIATQRIKGFGVENPVLPESPPASMSSVMKNNPLYGDITLEEAMEERKKSPSWTIEEYDKHSVHTNLSGHLKENPNDLRFWLGDTYTPGFDTLLKKKKKRNKRSKLCHMGLILLLVASILVTIVTLSTIFS
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Sequence:
MTTTPIADQAAVLAEGMADQTPSEALEAFGAEQAELDAAGVPSGIATAGSLMPDASLLDVHGNATTLQQVREGRPAVVVFYRGAWCPYCNLALRTYERELAPRLAERGVSMIAVSPQRPDGSLTMAQTNDLSYDVLSDPGNHIGRALGIVTRPTDRVQHAQASLGLDLTEVNADGTPDILMPTVAIVDAEGVLRWIDVHPNYVTRSEPARILEALARAVR
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular Localization:
Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MEADPLYHVKQLFYQASYQACISEASEYPHTPSDDPSSLHRALYIARSHLALPSPSPSSAHAILAPFLSLSPVPLSARAVDAFASIHEAEEDAREEKVEEVRDLVLECEGGNDEEEEKTVRAIAASVFILVGENEEAVATLTEGAAKDDLECIAILVQLLLSLNRRDLAQATYNSAKKFGSDSMLIQAMEAWIGLKTGSQPLHQSYYFYEELYQLPNGRTAPVLASHAAAHLLLGHVDEAKADIVEASQSKAGQSSSDVLAVGASVGAEGFAEKLVTTAKQHPYALDLIEKNKLFDEAAAKYAVSA
The following text describes a protein:
Function:
Dual metabolic roles of gluconeogenesis and glyoxylate detoxification.
Sequence:
MGYSDKHKLKTSNLQLPVRLLLGPGPSNLHPRVNQQLISSMVGYTDASYYKVMDETMELMRYLFQTDNHFTIPISGAGTAAMETCVSNLIEPGDKVVCLVSGFFSDRIYQMAVRYGGNILKVDKQWGQWFALEEIESALVQHKPSLLTLVFGETSTGVKQQMEGVGELCKKYNCLLMVDCVAALGGVPVFVDDWKIDACYTGTQKCLSGPPGISPLTFSNAACHKIATRKTPVANWYLDCNLLGGYWCPEFNLADGTIAKEEKSTIPKRYHHTTPANLLYSLREALVLLVEEGLDNVWKRHQDAAILLYAGLESLGLKPFVPQLNEAPEKGGRLFSLTTVNIPDGVDGKMVMKYLLDNFNIEIAGGIGAFAGKVWRIGLMGQNANPGNIKLLISSLSDALKVNGFNC
The following text describes a protein:
Function:
Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subcellular Localization:
Secreted.
Sequence:
MAPTPPYNIQGKRTLLATVVLLWTFVACVEGRPGCPSCRMPPLEPSAEKAFLVEVAKQQILQKLNLSQRPNITHPVPRAVVANALRRLHLGKGRMDGPGLSSRWEKPEPDEQGYEIISFAETEPSGLLQFQLTQTKGQDMHILQAHLWLYLKVHRNITLQVYLAGHERVALAEQQLGSKGSSWHTFSLMPGMQNFFQHKEKALQLELQCKGCHPNITALVTTTGSSHQPFLVVKAKVREPSHQITKRSLSCDQNSAVCCRKDYYVDFRDIGWNDWIFKPEGYQINYCMGECPMHLAGTPGIAASFHTTVFNLVKANNIQTAGRSCCVPTQRRALSLLYFDPNSNLIKTDIPDMVVDACGCS
The following text describes a protein:
Function:
The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-dependent activation of SMT3 and formation of a thioester with a conserved cysteine residue on AOS1.
Miscellaneous:
MISCELLANEOUS: Present with 18800 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MPRETSLVTIIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNNSKLVPYQGNVMDISTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECTKKETPKTFPVCTIRSTPSQPIHCIVWAKNFLFNQLFASETSGNEDDNNQDWGTDDAEEIKRIKQETNELYELQKIIISRDASRIPEILNKLFIQDINKLLAIENLWKTRTKPVPLSDSQINTPTKTAQSASNSVGTIQEQISNFINITQKLMDRYPKEQNHIEFDKDDADTLEFVATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVLNLLKYAPTTKYTDLNMAFTAKASNLSQNRYLSNPKLAPPNKNCPVCSKVCRGVIKLSSDCLNKMKLSDFVVLIREKYSYPQDISLLDASNQRLLFDYDFEDLNDRTLSEINLGNGSIILFSDEEGDTMIRKAIELFLDVDDELPCNTCSLPDVEVPLIKANNSPSKNEEEEKNEKGADVVATTNSHGKDGIVILDDDEGEITIDAEPINGSKKRPVDTEISEAPSNKRTKLVNEPTNSDIVELD
The following text describes a protein:
Function:
Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope.
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Multi-pass membrane protein. Note=Central core structure of the nuclear pore complex.
Sequence:
MSASSSSNACKLLLLGRCLRAVLLSVAIQFLLLTVFLLFVNFQLLHPLAWVTGTLRLVASWYTWFASIPLVASVVLYGVILCQQHLSERRYCPTRYRWLLHYGPRKVLFLFAHLLVGLLTAWLYTGYLHTDYQHLKYKCYGQDCISAYNVYLLGIGMTAGCYYFVSVHMRKEISIEFPIVEQSRAEKMRELLYASLAKSLLSSLLPTISYTAVFCLFGPMVCHRLSHILSVDMDERLDGFFGVVTNVRLLFYGYLLTAQILSNMHLMRCFYGILLSEDLPLVVTKPRAAFAHEQDITLVAGLGVFNVYVVQCLAAHHFYKLALRKNSPQRAEIFQLTEPGNRPASWRSLCDQCLSILGSFTEELTESMQKISILKCAQSLPMPKITESLTTSLMAEKVLLRQYNQKHGIRPIVSPSREVAVESPADGIRHFPNWCERVSTQLEQSLQRLLQRVPGIVYLFNEPEGAKTTFLLANSLPVVYMTQALAQVCAASLKEDPYGVVQNDLPAIIKAINKLRNELDKLSSVIGNIRISSSSFNVLRCAVRRSLYAICLSFCDYLDDLLPPGEELRQLQDLVCQE