lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May be essential for spermiogenesis and male fertility probably by regulating the manchette dynamics, spermatid head shaping and sperm flagellum assembly.
Subcellular Localization:
Cytoplasm.
Sequence:
MSLPKTPSTPLNSASTSESKKLVSVATEGTRGLPELKEKKNMVDRSKPLPTSLLNEFIPKEVLLSLTYAANAGPCPENLLPPKKIKTPKGTLPRLVDHVWHHPVRRNKFKYLIDHPVSLTGAGRDISFLYDVKYTKGQTREKAVCPPHLARSLQSHDGVIVPHKPKTLTDTLIPEEFHIVSSTGVSGLECYDDKYTTLLTDSENRLLLFPSMKPNKRVEVAQLNDVMDTMLERAGVENQEYTGPTKMHKLLHILKKEQTIYNTIFHELIRQVSVDCADRGELLSKVRERYVQMLDQIARQMIDFYKDLVTQRVMDQRILEELYNFKHVIEELTRELCLVRAHDVKLTKETEKAHKDLAQALLDAEKNAKMVEEYHDLYTLQRERMENDMKQLMAERDIWSSATYELALKVIERNRVILARRLYLNEKGWNKYTKHLIILLANKDTEDLALLQKLTQKWRNLVNKFKQEVEEMEESTRETLKIVEKGLTKWQESFNEKDILSPNNGNVFDSVILDFKQWQKMLNEKKEEFTGDVLLSKYDTLKIIKHLQENWTDIGLGIFNRHKSLEGELPSERQYMEEIIKNIQKLYKEYEIRINGDNGYSKILPILISSLDFCSFKLENLEFPDTPLEEWQEIDEKINEMKLQLDLLLNLTGIVPQHIDMDSVSVLQAYIFNMIQQWLLKIGNEINNGNIELQRHMDELHISMIQWMVNLLILMIPNFTDQDCLLKLEEESAEKHDIGVARLELDAIELTRKLYQYSRYLSSSCEGMVTAMALSKSTTSHRNATEDLYEVDKLKKECYEWINTCSCLLSNIKGRKITLLTYEEIEQLLEEEAVKEFIEPEMDESLLCSRRILLP
The following text describes a protein:
Function:
Involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. May transfer phospholipid across the periplasmic space and deliver it to the MlaFEDB complex at the inner membrane.
Subcellular Localization:
Periplasm.
Sequence:
MFKRLMMVALLVIAPLSAATAADQTNPYKLMDEAAQKTFDRLKNEQPQIRANPDYLRTIVDQELLPYVQVKYAGALVLGQYYKSATPAQREAYFAAFREYLKQAYGQALAMYHGQTYQIAPEQPLGDKTIVPIRVTIIDPNGRPPVRLDFQWRKNSQTGNWQAYDMIAEGVSMITTKQNEWGTLLRTKGIDGLTAQLKSISQQKITLEEKK
The following text describes a protein:
Function:
Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins.
Miscellaneous:
MISCELLANEOUS: Defined as class III fido-domain containing proteins, in which the inhibitory helix is present at the C-terminus of the Fido domain.
Sequence:
MPSENPIGKTMKSIDEQSLHNARRLFESGDIDRIEVGTTAGLQQIHRYLFGGLYDFAGQIREDNISKGGFRFANAMYLKEALVKIEQMPERTFEEIIAKYVEMNIAHPFLEGNGRSTRIWLDLVLKKNLKKVVNWQNVSKTLYLQAMERSPVNDLELRFLLKDNLTDDVDNREIIFKGIEQSYYYEGYEKG
The following text describes a protein:
Function:
May play a role in mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MSSSRSGEHRRNYAQGRNYESSRSRGDQRDRDYREYRRNYRDERSSRRYEDSQRRDYSPARRRDRYERHRESVREESPRRPVEHERNWQPELKHGRERFRERDYEGRRDRKERRDGVSPFSPEGEGLERKREHEKLQAPSPKEEEERPVDQGDKMDGVKEDKDGSLEVGKSHDAMTRTKSAEEEIVEQEDEATAEMKRIMGFSGFDTTTGKKHGDVGQVYKQKKTKYRQYMNRPGGFNRPLDNE
The following text describes a protein:
Function:
Component of neuronal acetylcholine receptors (nAChRs) that function as pentameric, ligand-gated cation channels with high calcium permeability among other activities. nAChRs are excitatory neurotrasnmitter receptors formed by a collection of nAChR subunits known to mediate synaptic transmission in the nervous system and the neuromuscular junction. Each nAchR subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, cation permeability, and binding to allosteric modulators. CHRNA4 forms heteropentameric neuronal acetylcholine receptors with CHRNB2 and CHRNB4, as well as CHRNA5 and CHRNB3 as accesory subunits. Is the most abundant nAChR subtype expressed in the central nervous system (By similarity). Found in two major stoichiometric forms,(CHRNA4)3:(CHRNB2)2 and (CHRNA4)2:(CHRNB2)3, the two stoichiometric forms differ in their unitary conductance, calcium permeability, ACh sensitivity and potentiation by divalent cation (By similarity). Involved in the modulation of calcium-dependent signaling pathways, influences the release of neurotransmitters, including dopamine, glutamate and GABA (By similarity).
Subcellular Localization:
Synaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MGFLVSKGNLLLLLCASIFPAFGHVETRAHAEERLLKKLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPQEYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFYDGRIKWMPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLVSMHSHVDQLDYWESGEWVIINAVGNYNSKKYECCTEIYPDITYSFIIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIIITVFVLNVHHRSPRTHTMPDWVRRVFLDIVPRLLFMKRPSTVKDNCKKLIESMHKLTNSPRLWSETDMEPNFTTSSSPSPQSNEPSPTSSFCAHLEEPAKPMCKSPSGQYSMLHPEPPQVTCSSPKPSCHPLSDTQTTSISKGRSLSVQQMYSPNKTEEGSIRCRSRSIQYCYLQEDSSQTNGHSSASPASQRCHLNEEQPQHKPHQCKCKCRKGEAAGTPTQGSKSHSNKGEHLVLMSPALKLAVEGVHYIADHLRAEDADFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAGMI
The following text describes a protein:
Function:
Transcription factor involved in regulation of the aflatoxin biosynthesis gene cluster. Binds with its co-regulator aflS to AFLR1 elements (5'-TCGSWNNSCGR-3') present in the promoters of the aflatoxin cluster genes. The ratio of the expression data between aflS:aflR plays a crucial role in the regulation of aflatoxins production. A high ratio, produced at a range between 17 and 30 degrees Celsius, corresponds with the production profile of aflatoxin G1 biosynthesis. A low ratio, produced over 30 degrees Celsius, is related to aflatoxin B1 biosynthesis.
Subcellular Localization:
Nucleus. Endosome.
Sequence:
MVDHISPRASPGPIRSSQTRRARKLRDSCTSCASSKVRCTKEKPACARCIERGLACQYMVSKRMGRNPRAPSPLDSTRRPSESLPSAGSEQGLPAHNTYSTPHAHTQAHTHAHSHPQPHPQSHPQSNQPPHALPTPNGSSSVSAIFSHQSPPPLVETQGLGGDLAGQAQSTLSSLTVDSEFGGSLQSMEHGNHADFLAESTGSLFDAFLEVGTPMIDPFLESAPLPPFQARYCCFSLALQTLTCLFPHAPLGCQLRLTDGEDSSCNLMTTDMVISGNKKATDAVRKILGCSCAQDGYLLSMVVLIVLKVLGWYAAAAGTQCTSTAAGGETNSGSCSNSPATVSSGCLTEERVLHHPSMVGEDCVDEEDQPRVAAQLVLSELHRVQSLANLLAKRLQEGGDDAAGIPAHHPASPFSLLGFSGLEANLRHRLRAVSSDIIDYLHRE
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Sequence:
MASTIPRVSFNLRVNDGKRCRIRVEEEEIHQTKMSSEEEPTPAILRNLFELSIDSGSHITIEVADKESHPTKTKKQDQSKEARSPIQKEKLEHTIVNKAEVPFDCRGPRVFFDITIGGVKAGLIVMELYSDVVPMTVENFRALCTGEKGKAPNGKSLHYKGSSFHTVIPGRFCVGGDCTGGESIYGGKFIDENFKERHKGFGVLFMSNGGERDNNCSKFAISTNRDTGLDGKYVVFGRVVEGLDVVRAIENVGSPYGEVLKPVLIADCGQI
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MSSSTSVQGEIMDLDLNQEPDSPPGLITEISPWLNELETAHERIEDRLRQLEAIVSRIRERAATVTTTTTTATPSPAPALIPPRDSTAGVIHERSRERLVENDKTYLIAKALNMERTTSVPGGYFDCNICLEKAEDPILTCCGHLFCWGCFYQLPFIYLNIKECPVCDGEVTDTEVIPIYGNGDDDNDGSSKAKREECGIRLPPRPNAKRVESIRQKIITRGNPFIPGPETLEHIRRTIDSIGGLQALAEGHEFGLTNIVTNNRVVQNQHNRLRLLSSFPGLVVDSSEMPPPTSDDAVVAAAFDVDSFVDTTTPSLRTNRRRSSRIAEISPSPSPAVRASIRRNQSGSAAGSSSSPRDFAVAGFGFGSREVATSDSSSSRRRTEDVNNGPRTRSRRRLG
The following text describes a protein:
Function:
Involved in aerobic respiration where it is required for assembly of respiratory chain enzyme complexes III and IV. Also has a role in mitochondrial gene expression. May be part of a mitochondrial membrane-associated RNA-shuttling system, delivering NAM1-associated transcripts to the translation machinery.
Miscellaneous:
MISCELLANEOUS: Present with 3430 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MWKFNKKLARLTYRLYSSSGPSSPLHGKKKLPQNLKFVVLNPTQSGLVKNDQKQPRHRPSKKRSHKETGDNNLDFGSKLLVFEKQNSLDSALNSIRLKKPTSASLPSLEYNALLQSLTSSYNRYQLREFISTHQPDSSSHLTHWKKSKLSQYIIEKIWNCQPISTPTTPTGIKSTSLTFQFDSPREIFLLLITQNGKILTNFNKLGLTFIISIQDNELTVKGSPSLLKYAEISLNKIWSNITHENVRMYSLMPSKDVINLIQKETHTFFEYLPDLQMYKISALSTKKISMAKVFLLNAVASNPNTTQHHHTIASPALKTELYPFNNTLENLDWLNKSQDWARLQSVVPKNCTDLMTPTENATPELTDAQVSQFESSLSKNIPSLSPSDSISQSLSITLGHSLQSASFSSIFQPLIHKSFISKLLNLPMYKESSSSAVPVPVPLDQHLITNAHQSFIQLNFTPVPPTSGSSSSPFLQIWFEIDEFDNIVTTSMRPLLKLQENSVILRTPQCQTDYKITSDYIQDLLPDFDQTNPDAWLSEQKGLQEFLLKSHWKLNKYQNLMKKINISLPDNLIQQYQLTDVLTHRVLNLRFPTNTAQDDKYIIQYSDISRGFLNNGSYRQLDFINVNPSETSLKTFINDVLSF
The following text describes a protein:
Function:
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Subcellular Localization:
Cytoplasm.
Sequence:
MSADSPSSPASSQAAEVQVRLPDGSLKTQPADATAMDVAKEISEGLARSVVAAEVDGTIVDSFRPLGEIADDENVVPLRLLTTRDESALDVLRHSAAHVMARAIMRIYKGVSLAFGPTTSGGFYYDFDMPEKISEDDFPKIEAEIKKIIKAKEPFERFVLERDEARKLCDDLDQDLKVEHIETGLGDQATVSFYRQGEFVDLCRGPHIPHAGMIKAIKLLSVAGAYWKGDASGRQLQRVYGTAFFDKKELASYLEQIEEAKRRDHRVLGKQHGLFAINPEVGQGLCLWLPKGARVRVTLEDFLRRELLSRGYDPVYSPHIGRVEMYETSGHFPYYRDSQFAPLFGSEVGGLLDAWSTRLDKDDLSKDDEDKLIAAAEVFGVKLPDYKPSASNDAKKDVLHRWQLNHERYLLKPMNCPHHCQIFGAQPRSYRQLPLRLFEFGTVYRHEQTGELNGMMRVRGLTQDDAHIFCTADQVEEEFRATIELTKFVLESVGLDDYRVQLSLRDPDSSKYVGSEENWDHAEGALRGVLEQSGLSFNEEPGEAAFYGPKADFMVRDCIGRSWQLGTVQLDYNLPERFKLEYKGNDNATHRPVMIHRAPFGSLERFTGMLIEHFAGAFPMWLSPEQIRVLPLSDKSVEYATAVAKQLDEAGFKVTVDASDGKVQAKIRNAQIDLVNYMAVVGPKEAESGQVALRDRIEGDLGSMPIKEAIARLQKEVETRQVRQAVKGSTVSIAETGGAATDY
The following text describes a protein:
Function:
Regulates mitochondrial small subunit maturation by controlling 15S rRNA 5'-end processing. Localizes to the 5' precursor of the 15S rRNA in a position that is subsequently occupied by mS47 in the mature yeast mtSSU. Uses structure and sequence-specific RNA recognition, binding to a single-stranded region of the precursor and specifically recognizing bases -6 to -1. The exchange of Ccm1 for mS47 is coupled to the irreversible removal of precursor rRNA that is accompanied by conformational changes of the mitoribosomal proteins uS5m and mS26. These conformational changes signal completion of 5'-end rRNA processing through protection of the mature 5'-end of the 15S rRNA and stabilization of mS47. The removal of the 5' precursor together with the dissociation of Ccm1 may be catalyzed by the 5'-3' exoribonuclease Pet127. Involved in the specific removal of group I introns in mitochondrial encoded transcripts.
Sequence:
MFQVITLSACFNPARLIRSSTSSSKLVLADGQPRKLCCCPFKPATHRRASSAQASLMPSQPKVKNPSASSVFSPAINLSVSPRGSKDDDQNATTKGSESIGEEQVPSNEAGPSTQIDTDLLLKELISLKENAGRASKSSIHKRVKYHWEQWNEFLNTPKGKRLDQNTILNITHEFLFLHPSKILTIFGDAEQAQRFHERFPSSKFDARIFKSIGLATLKYQNWTVLKRLLSRQRNLRRSDFLSIIRIASRKILFSSSLKTQNARIEVLLQLSEAITDSFNQETDCMKCMTQSIEILCDALLRMSCHEPAAAMVLQVLRQHPNFSKSFASEFLHRLMSTCASHQHLSIAHDLLAELPPELQTLDQFKACMSVWDRRTPRPLLHSACSVWDALVSHPHIVPDHDAHNLYLSLKSRLGHVEDLTRIIHNMERRRILMDGGKQKTYGILLHSIGRRRGLQSAYEALPELVSKGYIPDEYTSNILLSAKKTIHDAESYPWNESASRAEREERLLETMEKIQKANMKSDEVTRNILVRSFLSRSPYHSKEDISNIKHVSLDQSNPTHGATLDRQQFRRFRKPLYSMLCSAFRRANYLDELEQLKIEWKRESSKARSKSTQNPQKS
The following text describes a protein:
Function:
Required to protect lysosomal transporter MFSD1 from lysosomal proteolysis and for MFSD1 lysosomal localization.
Subcellular Localization:
Lysosome membrane; Single-pass type I membrane protein; Lumenal side.
Sequence:
MKASPTLWFALAALAMTAQGGWVRNPGRPADMTTSVEIAMGSLDAQPGTLFLAVASQDFTYFALNFDDHVDPGAVAINWTLFRNPTITPALVAEAITIKSGNRLQYGQAFVLDALLEFNDTKVEALHREMPLSLRSSAWTVKPGATSDTLTFNTSFTRDCSVNVSLLMHTGKGYAAVAPAIPIMPNASDINLILLGCNATIKNSRFGTRNHVYTSRTVRSTIAPLSRERHFSNLMPFLQTVLATDMKLKTEMSIDDEHSPAVFKLSILGTEKAPQAPSNQVTHGYLAFKPVVYGSASRGSSNMTSVQTNVSSLVPVDNATLPSSLFGGAGEGSELILLFGSKGDGWENASSYYMSAVLGTGDHGSNQFSFALLMTTIVSFGVPFIAFIVGGVYAVWKRSRLQRANYHQIN
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Nucleus.
Sequence:
MYGGEEEDYEKEEEEEITQEDAWAVISAYFEEKGLVRQQLASFDEFIQNTMQEIVDESADIEIRPESQHNPGRATEYSETTYKINFGQIYLSKPMMTESDGETATLFPKAARLRNLTYSAPLYVDITKHVVRKGDDGDEDGDREDLPKVFIGKVPIMLRSNYCTLFQNSDKDLTELGECPYDQGGYFIINGSEKVLIAQEKMSTNHVYVFKKRQPNKYAYVGEVRSMAETQNRPASSMFVRMLSRAGAKGGSSGQYIRATLPYIRTEIPIIVVFRALGFVADKDILEHICYDFSDTAMMELLRPSLEEAFVIQNQQVALDYIGKRGSTVGVTREKRIKYAKEILQKEMLPHVGVGEFCETKKAYFFGYIIHRLLLCALGRRAEDDRDHYGNKRLDLAGPLLGGLFRMLFRKLTKDVRGYLQKCVDNGKEINLAYAVKAKTITSGLKYSLATGNWGQANTAGVRAGVSQVLNRLTYASTLSHLRRLNSPIGREGKLAKPRQLHNSHWGMMCPAETPEGQACGLVKNLALMAHITVGSAANPILEFLEEWSTENFEEISPAVIPQSTKIFVNGCWVGIHRDPELLVRTLRQLRRQVDVNPEVGVVRDIRLKELRLYTDYGRCSRPLFIVEKQRLLIKKSDVRALQLKEASESGWHELVAKGFIEYVDTEEEETTMISMTISDLVNARNNPEEAYSKTYTHCEIHPSMILGVCGSIIPFPDHNQSPRNTYQSAMGKQAMGIYVTNYQLRMDTLAYVLYYPQKPLVTTQAMAHLHFRQLPAGINAIVAIACYSGYNQEDSVIMNQSSIDRGFFRSIFYRSYRDEEKKQGTLVKEEFERPNRENTTGMRHGSYDKLDDDGLAPPGTRVSGEDVIIGKTTPLPQDETGSQAQRYTKRDQSTCLRHSESGMIDQVLLTTNADGLRFVKIRVRSIRIPQIGDKFSSRHGQKGTVGMTYTQEDMPWTQEGITPDIIVNPHAIPSRMTIGQLIECIMGKVAAHMGKEGDATPFTDVTVDNISKALHKCGYQMRGFEVMYNGHTGRRLYAHIFLGPTYYQRLKHMVDDKIHSRGRGPVQILTRQPAEGRSRDGGLRFGEMERDCMIAHGAAHFLKERLFDQSDAYRVHVCEICGLVAIANLKKNTYECRGCKNKTEIVQVHIPYACKLLFQELMSMAIAPRMFTKEEKKKVVHKKVP
The following text describes a protein:
Function:
Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNEGSNSRLERILVIALVVIFGSGAWVSVSGIWTELPILIATGLPEKYRITSIVNILIQFAVVGMIAFLICNKLSASTRLYRPEIPVNYAITFMGTIATFLLIFFWDSKTYLSGQPHSVAFLCLVFFVALVDITSNVTFVGFMSLLKPNLLNWFWIGEGMSHVLPAFVVLIQQSGGSKDTCVANYTFINETMIGNSSVTYNCTSWQEVVPQFLFEPDEYFSFLFVVMISCHIAFICLNTLPCARREYTPQRDGHHLKRDGCGGLFKSLSSADEETDLLRLTPVVSSNGNDTSISNTENNDSNNELTEKHLTKKQVAFLYTIFFLNFLMAYGIMSPILGYSGSAYGHATFQLLVPLEQIAVAFAYFLFLLKPIYSFNAVAVSLVVAFFGYTYALVVASTSPYPPFGGLVAGKVLIVLNAVITSVSSRYCHASTVWILRNNADGRKHLIISGAIGQAGVILGSSTMFILINFYNIFEANHDSNTCPTNATCTMII
The following text describes a protein:
Function:
Inhibits cell growth rate and cell cycle. Induces CDKN1A expression as well as TGF-beta expression. Mediates the inhibitory growth effect of EGR1. Involved in the maturation of snRNAs and snRNA 3'-tail processing.
Subcellular Localization:
Nucleus speckle. Nucleus, nucleolus.
Sequence:
MSLNVPIIDVHRENFKDFWPAINLAIQTASYIAIDTELSGLGNRRKLMAKSIEDRYKSIAEVAKTRSILSLGLSCFKIQEEEDHHTGPAGETPGPGPTSQKFLAQTFNILTLCNEDYMVEPGALQFLVGHGFDFNKQYSCGVPYCRGPDRKEDKSWPTLRLLFNNILASKKPLTLHNGLVDLVFLYQNFYTDLPPSSAQFIADLYEMYSGGIIDTKYVAEYEARMPSSYLEYVFRKSQRDNAIRKTKGLHHASVVFCQYSPEMNAVEYQSYLLPPDFEERQNGGTPGNKSTEICEIYAAHGCCGKGIHCPKSHDPNAILDAEEIIVEDKRKRKRRRRNRKNRNQEVDVVDGETDKKKMKEREGEGEEKQKEGNMNGGGAAPEGNEAVSEESVPVVDGDKPSDFTEANDTEGATESGPLPNGADGPKRTEPKGIVPKKSGSHRAGFDAFMTGFATAAFIARFGSTDTPEGAIQLQNSTTRQKQGGQLTSRVGQLDQAESCMERHGIGHLTNKLYLSGKDYPLAVAKSSFTKTSTLHKDKMDMIIKLMAS
The following text describes a protein:
Function:
Involved in cytokinin biosynthesis. Catalyzes the transfer of an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP and ADP.
Sequence:
MEILLAYRWGELKKSGENGKKRRQEEEGWEKTDTEQIRSAGANPVGHLFSSLVLREQRWNSMLRSCKADRCSSFFRMPSYPLFLIQFWFPRVPSVPCRLLPPLVDVPAVARMVYKDKVVFILGTTGSGKSKLAIALAKSFRGEVVNSDKMQVYDGLGVITNKVTEEESGGVPHHLLGVVHPEADFTASHFRREATRAVESILGRGGLPIVAGGSNSYIEELVEGVGGEFRSRYDCCFLWVDVELPVLHEFVSSRVDKMVEQGLVKEARAAFRPDGDYSRGIWRSIGVSEMDGYFRSGDSAGDGETKARMLEAAVDAIKANTCRLACCQLQKIRRFCAMGWDVHRIDATEFFQRRGRGSEEELWEEVVGEPGAAITRSFLASKNQNNELDATANAATF
The following text describes a protein:
Function:
Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the matching and maintenance of pre- and post-synaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses. Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post-synaptic components. On the one hand induces accumulation of synaptic vesicles in the pre-synaptic part by binding with NRXN1 and in other hand induces clustering of GRID2 and its associated proteins at the post-synaptic site through association of GRID2. NRXN1-CBLN1-GRID2 complex directly induces parallel fiber protrusions that encapsulate spines of Purkinje cells leading to accumulation of GRID2 and synaptic vesicles. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). NRXN1-CBLN1-GRID2 complex mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (By similarity). Essential for long-term maintenance but not establishment of excitatory synapses (By similarity). Inhibits the formation and function of inhibitory GABAergic synapses in cerebellar Purkinje cells (By similarity); The cerebellin peptide exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release.
Subcellular Localization:
Secreted. Postsynaptic cell membrane.
Sequence:
SGSAKVAFSAIRSTNH
The following text describes a protein:
Function:
May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids.
Subcellular Localization:
Membrane; Peripheral membrane protein.
Sequence:
MSKNSEFINLSFLLDHEKEMILGVLKRDEYLKKVEDKRIRKLKNELLEAKRRSGKTQQEASRVCVHCHRNLGLIFDRGDPCQACSLRVCRECRVAGPDGSWKCTVCDKIAQLRIITGEWFFEEKAKRFKQVNVLGTDVVRQSILRRSPGAEEVQSQEQTRQDAEKSDTSPVAGKKASHDGPKRKGFLLSKFRSATRGEIITPKTDTGRSCSLDLDGQHFRSLKSPPGSDRGSTGSSDLNDKEPGPRTPKSSRSNGVTPGTQSSPAPSTRTVTSVISREYGFENSMDLAAIEGTSQELTKSHHRNTSGTPSIAVSGTSLSSDQSRSELDLSESFTEDSEDTVSIRSKSVPGALDKDSLEETEQSIDALVSSQLSTNTHSLASGLSTTSLNSMMSVYSETGDYGNVKVSGEILLHISYCYKTGGLYIFVKNCRNLAIGDEKKQRTDAYVKSYLLPDKSRNNKRKTKIRTGTNPEFNETLKYTISHTQLETRTLQLSVWHYDRFGRNSFLGEVEIPFDSWNFENPTDEWFVLQPKVEFAPDIGLQYKGELTVVLRYIPPEENLMLPPEQLQGNKTFKKGKKKESPVISGGILEVFIKEAKNLTAVKSGGTSDSFVKGYLLPDDSKATKHKTLVIKKSVNPQWNHTFMFSGIHPQDIKNVCLELTIWDKEAFSSNIFLGGVRLNSGSGVSHGKNVDWMDSQGEEQRLWQKMANNPGTPFEGVLMLRSSMGKCRL
The following text describes a protein:
Function:
Selectively catalyzes the oxidative deamination of acidic amino acids. May play a role in the egg-laying events and early development of the worm, in addition to quality control of the germ cells.
Subcellular Localization:
Cytoplasm.
Sequence:
MANIIPKIAIIGEGVIGCTSALQISKAIPNAKITVLHDKPFKKSCSAGPAGLFRIDYEENTEYGRASFAWFSHLYRTTKGSETGVKLVSGHIQSDNLESLKQQQRAYGDIVYNFRFLDDRERLDIFPEPSKHCIHYTAYASEGNKYVPYLKNLLLEQKIEFKQQEVTSLDAVADAGYDVIVNCAGLYGGKLAGDDDTCYPIRGVILEVDAPWHKHFNYRDFTTFTIPKEHSVVVGSTKQDNRWDLEITDEDRNDILKRYIALHPGMREPKIIKEWSALRPGRKHVRIEAQKRTSVGNSKDYMVVHHYGHGSNGFTLGWGTAIEATKLVKTALGL
The following text describes a protein:
Function:
Aquaglyceroporin that may modulate the water content and osmolytes during anhydrobiosis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Sequence:
MGAFVNTKVYIENKNIRDWLSEALSMFMYMSLLLGSAATGHFSGREDDALFGVIFQGFSITFGIYIGGAMSGAIINPALTLAVALLGKISWRKCIVLQSAQYIGSFIASAVVYLIYNDSLDAFGAGANFTATEPGVFRKDVAGIWSTFPKTYLKERGAIFNQIFCSMLLTFGFLAISDYKNFRPSKGLFPIAVGLLVMTVFLAFSYSTGAAMNPARDFSPRLWSLIIGYGIEVFSYNQYEWFWIPWLMPYVGAMLGALIYQLLIGAQWSKGQKGESKHKDP
The following text describes a protein:
Function:
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1.
Subcellular Localization:
Cytoplasm, P-body. Nucleus. Note=Shuttles between nucleus and cytoplasm.
Domain:
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex; The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Sequence:
MDFNVGVFSEKSSILIDGGDRFGVSAIHWDLQEELLWVGNQGGHVTSYYGSSLHKYTSFQVHASQEVRQMISFDAGLLIVTPNTLRCQQRRGVPLFTYSSSTCEDLQCLLQTGPTTVLLGGHQPLVIEFDLVTAKETTKFDVGEKGCAILRRHPRFICSGDASGCVSLRDPRTLREEHKFVAHTESLSDFDVHNNLIVTCGFSSRQGGVVSDRFLKIYDVRMLRALSPVPVVGEPFLLRFLPAFSSQLAVISAMGQLQVLDAAAPASSALQLFQVNNEGAMCMALEVSSSCQCLAVGDAGGYVHTFASNASALFNSFSRPTEFADPVESLPVSIAMDDTTTPLTSIPFPLERNSPLLSDWPEQFTRRRFRKVPPIDHAILSNMRMVGTIGYAPSPADHRPNQVAYSAEKRTQRGQKHSGTDSTHSKEDTECYQVWKRYRHIEMTYRYTKGGLDENELARYNSTPLCGLDNTLPYSYANSLLQVLYFIPELRHCLLEHSCNREFCLACELSFLFHMLDVGRNQDPTGTPVTVQPSNFLRAFRTLPEASAMGLLMAENHPEIKIKSTLPRLAQSWARFILQQLSSETLPQSKITKESTAITTNLVEFNGEGAENSSKPERDVSPSEVGLSPVSPICKLFGVEQEQISRCTKCGSENSKTSPVLLSSLTLQDVEDEHSFEHVLEKSFDVASVTPAWCEVCQKYQATQQRRRCLTLPPVLALSCANDTYKGFRFWSDQLQCFLDPELFDGSDLTEGASVQSGQGKPCRYGLECTRPNCKFGHGGQPLRHSASFTGISSNHWVPSQLRFKVQPEGGLVCLKPDQNQEGFLSYSLVAAVCWIDESKLDAKHHGKWHLVSTIQIPPGYSSSETSSEENNSSTWYVFNDFAVNPINPEEAISFFPDWKLPCLLFYSKNEKTNCSILTDRPLSNPITADVFKEDKSLAQKSECLQRISFLPLATDEMPGNGDLVAMDAEFVTLNQEEAELRSDGKSTTVRPSQMSVARVTVIRGLRSNGLSWTSIEYSSQGNMEGLPFIDDYIATQDQVVDYLTKFSGIQPGDLDVASSSKHLTTLKSTYLKLRFLVDNGVTFVGHGLKNDFRVINLLVPSNQVIDTVHLFHLPHQRMISLRFLAWHFLNLKIQSVTHDSVEDARTALRLYRRYQELKAKGDEFFNESLQELYNVGRRLQWMVPGMDEE
The following text describes a protein:
Function:
Role in flagellar biosynthesis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Bacterial flagellum basal body.
Sequence:
MTPEVALDLFREALWLTAMIVGVLVVPSLLVGLVVAMFQAATQINEQTLSFLPRLMVILLTLIVLGPWLLRQLMEYTQTLIGNIPLLIG
The following text describes a protein:
Function:
RNA-binding nucleolar protein required for pre-rRNA processing. Involved in production of 18S rRNA and assembly of small ribosomal subunit.
Sequence:
MANRGGIALSNGDNERPSHSSHASSPWGNSIWNSTNTSSSLGFAFGNAKRDSSRPRENGNYDLTDGKTGSGSLVADSETEWRPSRPTWTDAGSSNNVHVRSSGVSPARKRSIAQTLPTQQYSDTSSTFYTGPRNSIVGTGPVSKPPKPLLDPTSTNFTSSRQVESLNASFSNFGFSQPDITQRPDTAVNSWPDSASVHSPNEDRRSVAPSEYFAPSSGAPSRNGSLPPSRHGAEPNQFNSMDAFSRLSQAAPRQASSFSYANGRSFQERSGSIQSDSFHTLNRMAMDQEQDARLAHRQSFSTNGQNMNYTHSGSEPHVARDSYPDVQLPTRTDDPRYRNGTYTPDSFANGHISDPTLQFQGFEFDNSRNAPNGSGVRQSPYHSQLHTPPVYDRLNPYSTGEQALSHPNNLALFQNKLAGYQIQQERRNYIPHSQFQQQQFQHILPATQLRHPYQYSYAVPNGVPMSAIPPHMAMATMQPMMPVQTPRGPREQQTTEGTTVQGAKLVEFRKESKTSKRWELPDIYDDVVEFAGDQHGSRFIQQKLETANSEVKERIFKELESNSLQLMQDVFGNYVIQKFFEHGDQTQKKILASKMKGHVSALANQMYACRVVQKALEHVLVDQQASMVKELEKDVLKTVKDQNGNHVIQKVIDRVPMEHIQVIVESFRGHIGVLAVNSYGCRVIQRLLEKVPEPQRRFIMTELHARGADLITDSYGNYVTQHVIEHGLPEDRAKIVSLITAQFLTFSKHKFASNVVERCLVCSDDEQRRELVNAFIAKNERGENNLLNLLKDGYGNYVIQKLLETLNRDDYNVFVAALKPELEKAKKLISGKQIVSVEKKMYRYDRVDSPTMPRDTNESNEAPPTPALSDSAQSPQTSSIPSTNTSTVDDPVHSATQSSQKETAIPISGVSIHETTS
The following text describes a protein:
Function:
Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Subcellular Localization:
Cytoplasm.
Sequence:
MIAPKGLQWPGVSSTRYTSSTQSPLSSSDSRWTQLISAPCHFSLPVFISTLKTLSLHPEKLFPAVLQGDILPLHQSSTTDRLSKDAEDEIRTTIPGLELIERIRTRLVPNQPQRHIKLDQTSSFYRFSQSPEGAPQENSDTTTENDCGLVIFIPEINSIEHIPYYYPQANRIAFLWDPSNINDGSEEKSGVRARISVHYLQTKSPSLMSHAPTNAHLPLAHPALGAMISRLNRPKRRSPLATISQESDVDRCQRLGVVDGSQLESGGIARSTKELENDLYKQCQHLLEKVCKYGHDHFADSPVLHPRNGVIKPPESFESIYLLLKNRHCHLNPSFSKTDMAKHRLTKLQAAPSDEWGIPANNISEWGQRDVAVAAYLMLLWKDMYPERPSANDQGKGENGKEWDTWGRPEGGFIDLGCGNGLLVHILISEGYIGKGYDLRPRPSWNMYPSKTKDALVKQSLDLPGWFPRTEDEWELGSWVTREKCVVRDGAFIIGNHCDELTPWLPLLSIIPSPPVPYISLPCCLHTLDSIYSHLNFASPSQSSNQCISLPAELDPTKSLYDSYIAWLGWYSLGCGWECDIDKVGHGMAIGKGWAIIGRKRWASAEDDAKCRAWVLAEVEVVRRRGRFKVKENEDDDHAK