lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC). The repeat domain in Nup98 has a direct role in the transport (By similarity).
Subcellular Localization:
Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Nup96 is localized to the nucleoplasmic side of the nuclear pore complex, at or near the nucleoplasmic basket.
Domain:
Contains G-L-F-G repeats.
Sequence:
MFGGQFGSFGAKPAATASPFGAPSAAPTTSLFGSTAPSSGFGGFGSTAQTTQPTTGGFGGFGGFGGATTTQQPAASPFGGGGTGGSGLFGSSAQTTTQQPGASPFGGGFGTTTTTTTQQPGASPFGGTGGGLFGSSAQTTTQQQGASPFGGFGGATTTQPSLLSGATGGFGGFGGSTTSGTQLGGGGGATSGAFGGSSSPFGGSGGATTSSPFGGGGGSFGATTQKQYGTPIPYQQTTIEGNTFVSISAMPQYNDRSFEELRFEDITHRKDIVYKTGGGSGGGNSLFGSTPTTQPSSPFGAQTTTQTTGGLFGGQTTTSPFGGQTSATPGSSLFGSTQPTQQQTSGGLFGSVQPTQQQAGGGLFGSMPSTGGSSLFGSTQPTQQQTGGAQPTQSLFGGQTQTTTSPFGSQTSTPFGQPQQTNTGSGLFGAQQTQQTNTGGGLFGAQPTQQTSGGGLFGTQPTSGTGLFGTSPTAGGTGLFGTTQPTSQGTGLFGTTQPTTQGTGLFGTSPTSGTGLFGSTPTSGTGLFGSTPTSGTGLFGSAQPPQNQQSQTSLFGNTGTGATNTGTGLFGSAQPSSNPGGGLFGSAQPSTTTGGLFGSNQPTAQPTTSLFGNTTGSVGGLGATPNITSGLFGSNPAQTGGLFGSTQPTTQTSLFGNTGSTGGLGAQNGGGLFGNLSQPTATAGQGLSGGLFGNLSQPTATAGQGLSSGGLFGNTLLGQPSTQGLSSALPTLGLGLMGGQPQQTQQLPQGSLMLQQTQQPLQQQPLQQQQQPLQQSTIQLNNQINSASPYFPISSPAPFATFVKDLTSTSKVVSPPSYTQRSLSHHGYIPKSTTKLVPRRGPNNVDLGFSVIQNQNGLFPIDKFITKHSKSLNINTTNETEDTLRSLNTKSSSLFNNNNNNNNNNNNRNVNTNVNDYQNNGLPSSSLYNSNINQLSNNNNNNNNIYNNNNNNNINNNNNNNNISTQFNLRNNQSSSDNLNNDKSLSSSSSNKSQQQQQKEQKEEQPPKPIKEKEFINPNAPKLTRDGYQCVPSIKELSKKTDKELSSVQGFTISRDGCGSIYFPGSTNLVALDLDDIVDIEPREVSVYKDEETKPEIGYGLNRDAVVTLENCWPKNKNGEVVKEDGTILDKYENALKKVSAKSDCGFVSYSRSNGTWVFTVKHFSKYSAPDFDEDDQQMQQQTQQKQQQTQPSKVTFQQPSTKLTKPKFTANLDNFDSDSETSSGDENQDEMVPQKKTPFIKRVSNRESGLFDTPSVVPMSEKIETTPSKIARVSEPTSQSSRMSNNALKFSTFNPQQQQLQSSRFKSTGLSILSNPVKNLIQSDVNNEQSMFSNTTTTSTTRIQPLPSQQHLVQPIPTTISLNKNYFSKVRIDPQVYDRIVPKEESITNQYRMKNERLNHSTQDVSLFMRRSFRVGWAPGGKLISITKSSFKNLLIKKLPTDTKEDKKESIIKFLKNHHSHSSLVPENLKSIGWFSISNVQEQIESQLTLNVPSSQSVYYNRIWSLISNLWGNVLKGNGSKYINTNYSEDTIRKLNLNQWLKDVIAPLLRDEMDSLRKKTNSNYLEQIFSYLSAKQIKEASDLANENKDFRLATMMSQIWSSSESGKELILKQLTTYHSNGSDEFINEKRLEILHLIAGSVNKIYKNLNDWIRCFAVSFWFKYSLEYSIEDSVENFERSFNAHRSVYPLPPYLIKSTSTNSKQIEEQQHYYDICFLLLKLFAVNRGSSHFDKFKNIFYPENIGQDLLDYHLSWNLYTVLKSIPSLNKQPDLVNASNLHSSFALQLERLGLWQWSIYVLLHTPDQSNHVREEAVKSLIARAAPVITSEDRVFLTTKLHIPEIWIDEAKAWYSGYDCNNDIYDQIDALFKSYQYTKIHDIIFSNIGPNYIIQKRYHSLKDLLIRLEPHSSFISTWRYGGSIFLEFADICIQYKEILSQLSNTAEEIQRTKYYVNLKDITTRIVNILSDISKITQSSEIKNTSASYKQSLSFMSEALITKASLLRDLPESIVKLVSTNNLVSTLNSLPLTQDYRSKNLESLTDQIQDTLLNSIYQ
The following text describes a protein:
Function:
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
Sequence:
MANTTGRIPLWLIGTVAGILVLGLLGIFFYGSYSGLGSSL
The following text describes a protein:
Function:
Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm. Acts as coreceptor of TREM2 for SEMA6D in dendritic cells and is involved in the generation of immune responses and skeletal homeostasis.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MYVPTGPERLGPGTQSIMPLASLSPRAPLPLLLLLLLGGTPRAGGGPQPPFRTFTASDWALTHLVVHEQTGEVYVGAVNRIYKLSGNLTLLRAHVTGPVEDNEKCYPPPSVQSCPHGLGSTDNVNKLLLLDQAANRLLACGSASQGICQFLRLDDLFKLGEPHHRKEHYLSGVREPGSMAGVLIAGPPGQAQAKLFVGTPIDGKSEYFPTLSSRRLMANEEDAEMFGFVYQDEFVSSQLKIPSDTLSKFPAFDIYYVYSFRSEHFVYYLTLQLDTQLTSPDAAGEHFFTSKIVRLCVDDPKFYSYVEFPIGCEQAGVEYRLVQDAYLSRPGRALARQLGLAEDEDVLFTVFAQGQKNRVKPPRESVLCLFTLRAIKEKIKERIQSCYRGEGKLSLPWLLNKELGCINSPLQIDDDFCGQDFNQPLGGTVTIEGTPLFVDKDDGLTAVAAYDYRGRTVVFVGTRSGRIRKILVDLANPGGRPALAYESVVAQEGNPILRDLVLSPDRQYLYAMTEKQVTRVPVESCVQYTSCELCLGSRDPHCGWCVLHSICSRQDACERADEPQRFAADLLQCVQLAVQPRNVSVTMSQVPLVLQAWNVPDLSAGVNCSFEDFTESEGILEDGRIHCRSPSAREVAPITRGQGDQRVVKLYLKSKETGKKFASVDFVFYNCSVHQSCLSCVNGSFPCHWCKYRHVCTHNAADCAFLEGRVNVSEDCPQILPSTQIYVPAGVVKPITLAARNLPQPQSGQRGYECLFHTPGSPARVAALRFNSSSLQCQNSSYSYEGNDVSDLPVNLSVVWNGHFVIDNPQNIQAHLYKCPALRESCGLCLKADPRFECGWCVAERRCSLRPHCPADFPAAWMHARHGSSRCADPKIFKLSPETGPRQGGTRLTITGENLGLRFEDVRLGVRVGKVLCSPVESEYISAEQIVCEIGDASTVRAHDALVEVCVRDCSPHYRALSPKRFTFVTPTFYRVSPARGPLSGGTWIGIEGSHLNAGSDVAVSVGGRPCSFSWRNSREIRCLTPPGQSPGSAPIVININRAQLTNPEVKYNYTEDPTILKIDPEWSINSGGTLLTVTGTNLATVREPRIRAKYGGVERENSCLVYNDTTMVCRAPSVDNPARSPPELGERPDELGFVMDDVRALLVLNTSSFLYYPDPVLEPLSPTGLLELKPSSPLILKGRNLLPPAPGNSRLNYTVLIGSTPCALTVSETQLLCESPNLTGQHKVTVRAGGFEFSPGVLQVYSDSLLTLPAIVGIGGGGGLLLLVIVAVLIAYKRKSRDADRTLKRLQLQMDNLESRVALECKEAFAELQTDIHELTNDLDGAGIPFLDYRTYAMRVLFPGIEDHPVLKEMEVQANVEKSLTLFGQLLTKKHFLLTFIRTLEAQRSFSMRDRGNVASLIMTALQGEMEYATGVLKQLLSDLIEKNLESKNHPKLLLRRHTEARAGVGYNWGAWLQPDAACHLQECAGEPLFMLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIDYKTLTLNCVNPENENAPEVPVKGLNCDTVTQVKEKLLDAVYKGVPYSQRPKAGDMDLEWRQGRMARIILQDEDVTTKIDNDWKRLNTLAHYQVTDGSSVALVPKQTSAYNISNSSTFTKSLSRYESMLRTASSPDSLRSRTPMITPDLESGTKLWHLVKNHDHLDQREGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDEQADQHQIHDADVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKSSITDACLSVVAQTFMDSCSTSEHKLGKDSPSNKLLYAKDIPNYKSWVERYYADIAKMPAISDQDMSAYLAEQSRLHLSQFNSMSALHEIYSYISKYKDEILTALEKDEQARRQRLRSKLEQVVDTMALSS
The following text describes a protein:
Function:
Binds together with bS18 to 16S ribosomal RNA.
Sequence:
MLVNSYELMVILRPDLNEERVSQEVTKYQEFLTNNAAEEVSVKVWGKRRLAYQIRRFNDGIYVLFNFNGEGQQIALIERDMRLNDNVMRFLSIKLTPEKPEKEKKAKAVAVEA
The following text describes a protein:
Function:
Specifically methylates the cytosine at position 1962 (m5C1962) of 23S rRNA. Methylation occurs before assembly of 23S rRNA into 50S subunits.
Subcellular Localization:
Cytoplasm.
Sequence:
MSVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPSESIDIAFFSRRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPECSIYDRSDVAVRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQHGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALMGGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKDINMLAIQLLNEGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM
The following text describes a protein:
Function:
Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes. Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting center near the SNRPN promoter, where it might function as part of a complex with RB1 and ARID4A. Involved in spermatogenesis, together with ARID4A, where it functions as a transcriptional coactivator for AR (androgen receptor) and enhances expression of genes required for sperm maturation. Regulates expression of the tight junction protein CLDN3 in the testis, which is important for integrity of the blood-testis barrier. Plays a role in myeloid homeostasis where it regulates the histone methylation state of bone marrow cells and expression of various genes involved in hematopoiesis. May function as a leukemia suppressor.
Sequence:
MKALDEPPYLTVGTDVSAKYRGAFCEAKIKTAKRLVKVKVTFRHDSSTVEVQDDHIKGPLKVGAIVEVKNLDGAYQEAVINKLTDASWYTVVFDDGDEKTLRRSSLCLKGERHFAESETLDQLPLTNPEHFGTPVIGKKTNRGRRSNHIPEEESSSSSSDEDEDDRKQIDELLGKVVCVDYVSLDKKKALWFPALVVCPDCSDEIAVKKDNILVRSFKDGKFTSVPRKDVHEITSDTTPKPDAILKQAFDQALEFHKSRTIPANWKTELKEDSSSSEAEEEEEEEDDEKEKEDNSSEEEEEIEPFPEERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAGYNVKCAYKKYLYGFEEYCRSANIEFQMALPEKVVNKPCKECENVKEIKVKEENEPEIKEIKIEDEENIIPKEEKPTDDDIERKENIKPSLGSKKNVLESIPTQSDQEKEVNMKKTEENENLEDKDEETTGMDESLSIKVEAEEEKAKSGDETNKEEDEDDEEAEEEEEEEEEDEEDDDNNEEEEFECYPPGMKVQVRYGRGKNQKMYEASIKDSDVEGGEVLYLVHYCGWNVRYDEWIKADKIVRPADKNVPKIKHRKKIKNKLDKEKDKDEKYSPKNCKLRRLSKPPFQTNPSPEMVSKLDLTDAKNSDTAHIKSIEITSILNGLQASESSAEDSEQEDETGAQDIDNSGKEDSKIDHLTHTRNDLLAKEEQNSSSLLEENKVHADLVMSKPVSKSPERLRKDMEGLSEDTDYEEDDEITKKRKDVKKDTTEKSSKPQVKRGKRRYCNTEECLKTGSPGKKEEKAKNKESLCIENSSNSSSDEEEEEKSKTKMTPTKKYNGLEEKRKSLRTTGFYSGFSEVAEKRIKLLNNSDERLQNSRAKDRKDVWSSIQGQWPKKTLKELFSDSDTEAAASPPHPAPEEGPAEGSLQTVAEEESCSPSAELETPPPASADSKPAEEKTAEIGDKKAEFPSSGSNSVLNTPPTTPESPSSVTVTEAGQQQSSVTVSEPLAPNQEEVRSIKSETDSTIEVDSVAGELQDLQSEGNSSPAGFDASVSSSSSNQPEPEHPDKACTGQKRGKESQGGGSSSKKQKRSHKATVVNNKKKGKGTNSSDSEELSAGESVTKSQPVKSVSTGMKSHNTKSPARTQSPGKCGKNGDKDPDLKEPSNRLPKVYKWSFQMSDLENMTSAERITILQEKLQEIRKHYLSLKSEVASIDRRRKRLKKKERESAATSSSSSSPSSSSITAAVMLTLAEPSMSSASQNGMSVECR
The following text describes a protein:
Function:
Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Sequence:
MNYLKDPYVVNNEHEINRNNCYLHEEEKKYINVEEKHFINVQQKDFINVQQKDFINVKQNEFINVKQNEFINVEQKDFLNVEQKDFLNVEECIPQNNNLSSRKRYINYNNISGPYNIHNNFYNHYKKQKKHYNATNFYAKNNLFSHNQQNGVYHMNINNRNVSNNGCVMNKITKSFEKKKQKKSSSHGLYKHVNDTTTCLLDNQIYEHNNLYLNTDSFVDCEQNKNDSKKHRNNKHVRDSEYVYNSEFAQNSDQRVSSLSCENKPINNPVKRSFILNDKNVGSGYFLNETIVENMNYHNNKYEDNKNHVSNQFINDTYCNNNNNNNIYVKNETCYNFLPNNDTERNEMNSTHAIEREEDIIKHITKYNEEGKRRKKKRNMDILSKDEILKDAVEYFKKCSSRNIDNVNYDSSYEEDMKIKNLHHKENMCYVCKEKEHIYKCPYCEICTCSLVCSKNHKKMFKCTQKLKKNLKIKNVSKGNFDESILYKDFLYLQNIETIIRGNYKYIKVKNYETTNIWLLHNKMLIKLLKKRKIILLKAPIFTKIHKENKTFIYNHILFWTIKITFVNLNIRILHHEINENLTFLQIIQYLCSKIEKLQTKIFIYLQNVKSIYVSLNNEQPNKARKNLNHHQNKNTNNDNNNACDMKKYCSVQQVLRKSLCGKSFYEYPHFDIEILYEDNKPIVNPLYELEHKKEEDNQQNCQQEGSIGNTIRMREGGEDNKEGDEDNKEGDEDNKEGDEHNKEDDKDNKENDENNDEGDENNDEGDEDNDEDDEDNDEDDEDNDEGDEGNDKGDEYNDEGDENNDEGDEDNDEDDEDNDEDDEDNDEGDEGNDKGDEYNDEGDEYNDEGDEYNDEGDEYNDEGDEYNDEGDEYNDEDDNDMNNNDKNNM
The following text describes a protein:
Function:
Vacuolar Fe(2+) uptake transporter.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MGVGAVQENVKTMILTVSAGLFAGACSMAIGEFVSVYSQLDIERAQMKRDKATRGQKREHEEGNKKQLPNLFQAAVASTFSLGAIVPILAAAFIANHKLRLAMIVAAVSLASLAYGAIGSFLGKSPMVKSCARVLIGGWMSMAITFGLTKLIGSTGLEI
The following text describes a protein:
Function:
Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases. The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage. Within the MRN complex, rad32 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Rad32 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR. It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation, which is required for single-strand invasion and recombination.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MSRRQRLSEVEEQGVDDYDENTIRILIASDNHIGYAERDPIRGNDAIRTFNEILGIAREREVDMILLGGDLFHDNKPSRKALYQTMRALRLNCLGDKPCELEVLTDMSMITGDTAVCNINYQDPNINVAIPVFSIHGNHDDPSGEGHYCALDILQVAGLLNYFGRVPENDNISIAPILLQKGYTKLALYGLSNVRDERLYHTFREGKVKFMRPDLYRDEWFNLLTVHQNHSAHTDTGYLPESFIQDFYDFVLWGHEHECLIDGSYNPTQKFTVVQPGSSVVTSLCQGETALKHVGILNIKGKEFNLEKIRLRTVRPFVMKDVVLSEVQSIPPMVDNKSQVLQYLIGEVDNAIKEAQEQWLQSQSDIPENERGEAPLPLIRLRVDYSGGYQTENPQRFSNRFVGQVANVNDIVHFYQKRHYKRTAKDKALLAAPGEEIKLDSLRVETLVKQYLDTNRLECLPEQKLGYAVAQYVEKDDKDALKDFVENYVKKQVSVLVQKRVTEENLEDEIKHIMDGMGNLAHMKRKGSPEVPTSMDERSEQHDLFKDAPAHDETMEEMPLFLPSQSQSIFETEHNDVHEEPKQRTSTRQRKNAATKAAAPNTRSSTTTSTKRRTLPSTMTGTRRGRSGSRASQQSKLSFGKSQTNTRQNASSRNPEDDEILEL
The following text describes a protein:
Function:
Plant defense peptide (Probable). Disrupts membranes containing phosphatidic acid (PA) via a PA-dependent oligomerization process.
Subcellular Localization:
Vacuole.
Sequence:
KDCKRESNTFPGICITKPPCRKACIREKFTDGHCSKILRRCLCTKPC
The following text describes a protein:
Function:
Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
Sequence:
MDIEDQVAPALAHAQSTSPLLTNVRVMMVTMGCGHNAAESDIIASALQTAGAVITHSNGKYITPESARDVDVLYINSCTVKNPSEDKAFVHVQKGLEVGTVVVLGGCVPQSYGTVNDELRKASAAKQLIISGVLTQQWLAALPRLLREAIDLHILNNSHLLQPALRMTQPSDKAGVPAAISYVTKEATKDVEVEYLKCTPVHRANPIIDIISTGSGCMGSCTYCKTCHSRGRLRSVPLDTLLARIRSSLADPIIRELWLTGEDTLAWGRESDATFAVLLQEVQKLFETENPTHKMLKIGMTDPDSVINQEDSLISFMRCKYVYKFLHLPVQSGSDRILTLMRRHYDIETFLRSCSKLQSAVPDLCLDTDIICGFPGETDEDHAQSLNLFRNLKEDAPRFQVVNITQYYARKNTPAASMEQVPASKKRERTREMSEVVKNSFRRDQYHGQVHDIMVLERLQTENHGRQYGGKTYNNLTVAIEAVDQEVPIKLGSYVRVRITGSTRVALIGSVMTYHSSPVIVRRVE
The following text describes a protein:
Function:
Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MGRSGAGSPRELPASCCRCDADIACFAATDGKLLSSDVTHYVIPDWKVVQDYLEILEFPELKGIIFMQTACQAVQHQRGRRQYNKLRNLLKDARHDCILFANEFQQCCYLPRERGESMEKWQTRSIYNAAVWYYHHCQDRMPIVMVTEDEEAIQQYGSETEGVFVITFKNYLDNFWPDLKAAHELCDSILQSRRERENESQESHGKEYPEHLPLEVLEAGIKSGRYIQGILNVNKHRAQIEAFVRLQGASSKDSDLVSDILIHGMKARNRSIHGDVVVVELLPKNEWKGRTVALCENDCDDKASGESPSEPMPTGRVVGILQKNWRDYVVTFPSKEEVQSQGKNAQKILVTPWDYRIPKIRISTQQAETLQDFRVVVRIDSWESTSVYPNGHFVRVLGRIGDLEGEIATILVENSISVIPFSEAQMCEMPVNTPESPWKVSPEEEQKRKDLRKSHLVFSIDPKGCEDVDDTLSVRTLNNGNLELGVHIADVTHFVAPNSYIDIEARTRATTYYLADRRYDMLPSVLSADLCSLLGGVDRYAVSIMWELDKASYEIKKVWYGRTIIRSAYKLFYEAAQELLDGNLSVVDDIPEFKDLDEKSRQAKLEELVWAIGKLTDIARHVRAKRDGCGALELEGVEVCVQLDDKKNIHDLIPKQPLEVHETVAECMILANHWVAKKIWESFPHQALLRQHPPPHQEFFSELRECAKAKGFFIDTRSNKTLADSLDNANDPHDPIVNRLLRSMATQAMSNALYFSTGSCAEEEFHHYGLALDKYTHFTSPIRRYSDIVVHRLLMAAISKDKKMEIKGNLFSNKDLEELCRHINNRNRAAQHSQKQSTELFQCMYFKEKDPATEERCISDGVIYSIRTNGVLLFIPRFGIKGAAYLKNKDGLVISCGPDSCSEWKPGSLQRFQNKITSTTTDGESVTFHLFDHVTVRISIQASRCHSDTIRLEIISNKPYKIPNTELIHQSSPLLKSELVKEVTKSVEEAQLAQEVKVNIIQEEYQEYRQTKGRSLYTLLEEIRDLALLDVSNNYGI
The following text describes a protein:
Function:
Ligand-activated Ca(2+)-permeable, nonselective cation channel involved in pain detection and possibly also in cold perception, oxygen concentration perception, cough, itch, and inner ear function. Has a relatively high Ca(2+) selectivity, with a preference for divalent over monovalent cations (Ca(2+) > Ba(2+) > Mg(2+) > NH4(+) > Li(+) > K(+)), the influx of cation into the cytoplasm leads to membrane depolarization. Has a central role in the pain response to endogenous inflammatory mediators, such as bradykinin and to a diverse array of irritants. Activated by a large variety of structurally unrelated electrophilic and non-electrophilic chemical compounds, such as allylthiocyanate (AITC) from mustard oil or wasabi, cinnamaldehyde, diallyl disulfide (DADS) from garlic, and acrolein, an environmental irritant. Electrophilic ligands activate TRPA1 by interacting with critical N-terminal Cys residues in a covalent manner. Non-electrophile agonists bind at distinct sites in the transmembrane domain to promote channel activation. Also acts as an ionotropic cannabinoid receptor by being activated by delta(9)-tetrahydrocannabinol (THC), the psychoactive component of marijuana. May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
C-terminal helices from the four subunits associate to form atypical coiled coil structure; this region is probably involved in binding the inositol polyphosphates that are required for optimal channel activity (in vitro); The ANK repeat domain consists of a convex stem structure formed by five ANK repeats and 11 additional ANK repeats that form a crescent-shaped structure that surrounds the protein core.
Sequence:
MKRSLRKMWRPGEKKEPQGVVYEDVPDDTEDFKESLKVVFEGSAYGLQNFNKQKKLKRCDDMDTFFLHYAAAEGQIELMEKITRDSSLEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEHGYSRQLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSYSGSVDIVNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGHAKAVALLLSHNADIVLNKQQASFLHLALHNKRKEVVLTIIRSKRWDECLKIFSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHSTEDKSCRDYYIEYNFKYLQCPLEFTKKTPTQDVIYEPLTALNAMVQNNRIELLNHPVCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIKPGMAFNSTGIINETSDHSEILDTTNSYLIKTCMILVFLSSIFGYCKEAGQIFQQKRNYFMDISNVLEWIIYTTGIIFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQRFENCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNLQDPFSSPLLSIIQTFSMMLGDINYRESFLEPYLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLAVGDIAEVQKHASLKRIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYPNKPRSGGMLFHIFCFLFCTGEIRQEIPNADKSLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISETEDDDSHCSFQDRFKKEQMEQRNSRWNTVLRAVKAKTHHLEP
The following text describes a protein:
Function:
Potential glycopeptide transferase involved in O-linked oligosaccharide biosynthesis (By similarity). In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Domain:
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
Sequence:
MRRHVVLSIFVFAGIVFAAEEAEKLPKCEHVDPYENLEGWLDLKPLTERKCNHTLKENLTEAESKKSEWGIKSFAFDALSSEKLGPNRNVGKQAHKLCEEEKYDASYSTSVVVIHHNEALSTILRMINGIIEFTPKSLLKEIVLYEDASEEDHVLTKHLEKFAKIKGLEDKLIIKRSEYRQGLIRAKVHASRLATGEVIVFMDSHCEVAERWLEPLLQPIKEDPKSIVLPVVDLINPVSFDYSPSMVAKSGFDWGFTFKWIYLPWEYFETPENNVKPFNSPAMPGGLLAMRKEYFVELGEYDMGMEIWGSENIELSLKAWLCGGRVVVAPCSRVGHVFRMRRPYTSKPGMDTALYNAVRVAKTWLGEYESKFFAVKPRGAKMVFGDLTEPMQVKDRLKCKDMKWFIENVYPELEPKVHDEL
The following text describes a protein:
Function:
Part of an energy-coupled inorganic carbon pump.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Endomembrane system; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MRKLAMSDWLNFLPMLLPTALVAAVLVPDSLTRRHVVSWRRWINIAVASQVAVLLVVFAIRWWGVASGATDGLLASGELSSGELGVASPVLLDGLSGLMLLLVTFIGWVTCQYSIEYLDGSPNQGRYYRFSAVTIGAVSWMVVSGHLVVFAVAWIAMNLALHQLLVLHPEQPGAKRAAWTKFAINRVGDVALLAGFGLLFVHFDSPYLQDIFASVGNMVIDSQSVPTTLLAACAFLMIAAVIQSVQFPFHTWLPETLNSPTPVSALMHAGIVNAGGYLVIRFSPIFELVPTNLHVLAIIGLFTTVMAAAVMMTQTSVKKSLAYSTIAQMGFMMLQCGLGAYTAATVHIVAHSLYKANSFLRSGSVVSDAKAITGASDLKQPLTWYETTFAITAACVLFAIVSIQLNVSPNEKAGGLILGGILCLALSHWIGEAIRSGSRWLVVQCTAISGLICLLYVGCYLATDALTAGSLPSLPTPTNNLVVTSTIAAGFAGLLVLQSRIRSASETPWLQTLQIHASNGFYIDHCIRRVFRAFASA
The following text describes a protein:
Function:
As part of the CRL3 E3 ubiquitin ligase complex; polyubiquitylates monoubiquitylated RNA polymerase II subunit rpb1 to trigger its proteolysis; plays a role in global genomic repair.
Sequence:
MYSLKDLCIQVAQKHVHDIDDIGDCPFELVKPILEKARPEHLIDLEEKSPHLKVDTQPLWKDHVLRDFGLELQKRTILNNIDDWRGLYGKLKKKRNAHYNVASAKLRSAYTKLEQSKQNKRIVPLEREPRAARPPKRPRPMSNYCPKSSLMARAKSDFLKKASATRHIVSATSSSRSFPQLHPLGRSSSNATNTSTKRPLTSNTYPSIPLPPKSFTSQNFKSFNAVKTQPSSSSSPSISRPTSFPMSFFPNPSRFSSQVPKRI
The following text describes a protein:
Function:
Probable transcriptional regulator, which participates in the transcriptional repression of the presenilin protein hop-1.
Subcellular Localization:
Nucleus.
Sequence:
MPPRKRKLEELKNEQGEQGSYKCHLCGQCFYRGCGLASHLRRHAPVTFDCEHCAYTCKHKYAYDRHLLQSHPELVESGPLVRMFKNEDEDAPMPILEREADVSDDAVKYEALSSFSEPEPISYKCPLCISTFGSHARAVYHILSHRVKLYQAPKSLKFFSRKTMQALGGFRLESQLMIKWRLQYDNRSVDEKRTRLWRYMEENFGHEHLKQPKLESDNPSTSSSFESQTNLNDSSIIKKKLVMKCGTVFGQRLIHDNTQYYLCRNCPYVSWNVSSLWRHFRHHIQKSKQSWTCIACSYSSSSRVKIDLHVKMHKEMPEIDLEFATWLRYERRINKNDLNKPTNKKKKPDGGNGSNHSDMRSLHAFLSLKNSKNNVVKHDIDAPTLHPLSPAPKLVAMTQFDFGEIVTYKSVNPLHQINKNNSNPTVLPNKRNSIKTSKSDTQIALSVKQSSSMKMVKVSPGKVYQLPKTSKFYRPESPDSLASNNSAHGDEIESTSSDQFQQSVKVPKYEDFLNMKPVMPYFQKQRHPLEAIAMYEKAKREYEKNHCFPNLPIFEFNIEYKNLHPLAKAQYGKNNMKEYFLNEMEVEKSRECTDCPFKHNDLQQFRLHRDKHFYGGSHTCPECNYSSNNHNQVVEHTFVDHYLSDVRLVEGLPSSDSEDDNIPVPPDTPQRKKKAPKRGKRRGW
The following text describes a protein:
Function:
Determines thylakoid architecture by inducing membrane curvature.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Sequence:
MASISATLPSPLLLTQRKSNLTSIQKLPFSLTRGTNDLSPLSLTRNPSSISLMVKASGESSDSSTDLDVVSTIQNVWDKSEDRLGLIGLGFAGIVALWASLNLITAIDKLPVISSGFELVGILFSTWFTYRYLLFKPDRQELSKIVKKSVADILGQ
The following text describes a protein:
Function:
Ammonium transporter that mediates the excretion of ammonium from the prestalk cells from the slug. Controls ammonium homeostasis during growth and development. Ammonium has been shown to function as a morphogen at multiple steps during the development.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Contractile vacuole membrane; Multi-pass membrane protein. Cytoplasmic vesicle, phagosome membrane; Multi-pass membrane protein.
Sequence:
MEYLELNGTKEGLSAAVDDMWVLNATYLVFYMQAGFCMLEAGVVRAKNAKSIIMKSIIDTAIGSLLFWALGFGLAFGNADKASNPVIGTSHFFLINYQNLSFFAFQWAFCATSITIVSGSLAERVHVTSCLVYTIVMSAFIYPLSAHWVWSYNGWLRMIGFNGIIDFSGSIVVHIVGGCIGLVGTYLVGPRIGRFDSESGKPKPLPGHSITIYTLGAFIIWYGFYGFNTGSTLGISGGGIAIASRSAVTMTIIACASCATTLLAIKIKSGKYDVVKSVNSLLGGLVSSAAVCSLIDPWAAFIIGCVTSFVYLGCSHLLIKLRIDDPLDSSAIHLGCGIWGALSVGLFSTQENLSLVLKKSTNVYGLFFGGGFEQLGIQLLGIIIVMAWCFFCASILFTILKKFHLLRIEPTKELMGIDIDSAGGPAYQWDN
The following text describes a protein:
Function:
Binds, sorts and targets the polycystin complex (lov-1 and pkd-2) for lysosomal degradation, acting on early endosomes located at the ciliary base. Functions in the germline together with the ephrin receptor (vab-1) signaling pathway to negatively regulate MAPK activation. May have a role as a positive regulator of meiotic maturation in oocytes, acting independently of vab-1.
Subcellular Localization:
Cell projection, cilium. Endosome. Note=Located to early endosomes at the ciliary base but not cilium proper of male-specific sensory neurons.
Sequence:
MKKQKSFPMSAYEDLLGKITAPTITVENWEGILAFCDMINNDFEGSKTGIKSLRKRLNNRDPHVVLLAISVLDSCWANCEERFRKEVSSAQFINELKALCTSSQRQVAEKMRLTVQKWVDTECKTEQSLSLIVTLHKNLVADGYSFVVDDPKSKTKAIDAKFANDPNYVGSAQEEEAIAKAIAASLADAEKQEKAKKSTSTMYPSAKASSPAVQTNSNIPEKNVRALYDFEAAESNELSFVAGDIITITDESNPHWWTGRIGTQQGLFPSSFVTNQLDDLKSKETDSSQKAPEVVASINEAILVRCLQVLHECDPTGERQDPEDLAQLEAASYAQGNLIDAHLASIDRQSNSLAQIDVAIRDVLALYDDAIQKGGFQHQSQGMYQQPMQQYNYQQPPNRAYYPPTGPVQQQQPQQYPPQHYPAPGAQPQYACPPNSVPQPQQQQQQWPAPSSQPQQY