lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate.
Subcellular Localization:
Nucleus.
Sequence:
MALTNRDRERGSGPLPNRWLYCPRKSDTIIAERFLAFKTPLSNNFHDKMPIECTFQPEMLFEYCKTLKVKLGLWVDLTNTKRFYDRSAVEELGAKYIKLQCRGHGETPSPEQTHSFIEIVDNFINERPFDVIAVHCTHGFNRTGFLIVCYLVERLDCSVSAALAIFASARPPGIYKQDYINELYKRYEDTNAAPAAPEQPNWCLDYDDGNGDGFVQDNSSSTSQQAGEQDDDAEEVEGEDAGGDCDASTSDGQPRKKRRREMIIKNATFMAGVPGVRQVSDQPRLGDLQRKVQDWCDWKKNGFPGAQPVSMDRENIKRLSEIPYRVSWKADGTRYMMLIDGRDEVYFFDRNHSCFQVENVTFVESRNLNEHLDGTLVDGEMVLDKIGETVTPRYLIYDIVRLSNRDVRDEPFYPNRLDYIKTEVIGPRILGMKHGIINQRLQAFSVRGKDFWDIWMSARLLGEKFSRTLAHEPDGLIFQPSKQPYTAGTCSDVFKWKPHELNSVDFRLKIITERGEGLLTKKVGFLYVGGHDAPYGRMQRLTKETRELDNRIVECTMNQFGNWDFMRERTDKKNPNSYNTARSVVDSIKHPVTKEYLLNFIASSGYRNDHVMMPPPINSHNQNHNHNHFYPHGHGQHQRRPCVNPTLGN
The following text describes a protein:
Function:
Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding.
Sequence:
MMQQLRRSQPSPCHLRGSRFTGAGLPARPMLALGAAAARRSRPETVQLSACHAAAASAQPRPRAVADSALGASSTSVQVRGKLLLQNFFADDGSDSQRQLRLSIQLVSATVAGPDGRGVKAEASVLDAVVGSGDTELDVDLTWDEALGAPGAVVVKNHSDFPVYLRLLSMPTRVLGADDKAATTAAVHFACNGWVYPVDKHPYRLFFTNDACVKEETPSSLLKYREDELAVLRGDGETADRPFQPWDRVYDYALYNDLGNPDLRRDLARPVLGGSREYPYPRRTKTGRPAAKTGPCPYPQSESRAPLDEEIYVPCDERVGFGSVPAPTLPPLGGHFSSLADVYRLFGLDDVGRLPEAKGVINSGAPFPVVPQVISVNPTHWRKDEEFARQMIAGANPVCIKRVTKFPLTSELDRGVFGDQDSKITEDHVEKNMGGMTLQQAVEEGRLYVVDHHDWVMPYLKRINELPGEEEKAEVSQRKVYAARTLLFLNREDSTLKPLAIELSSPHPEKEQLGAVSTVYTPPDSRDDDDDGITAGRFSVWELAKAHAAANDTVENNFVTHWLNTHASMEPIVIAANRQLSVLHPIHRLLKPHFRKTLHINAVARQIVVGSGDQRKDGSVFRGIHEVTYFPSRYNMEMSSMAYRAWNFTGLALPNDLINRGVAKGDAKKPETLELVIKDDYPYAADGLEMWAAIKDWVADYCAIYYGDDGAVARDSELQGWWSEVRNVGHGDLSDAPWWPAMDCLADLVETCTTIVWLGSAYHAAISFGQYDYQGFIPNGPSLTTRPVPDPEVTVTVAESDFLESVTPVAEALGFMSISSGPLGLVGTEVYLGQRPDTEQWTSERSAAEALAVFRARLEEVAGNIERRNADPALKNRTGPVEVPYTLLKPTAQPGPVLRGIPNSITV
The following text describes a protein:
Function:
ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Subcellular Localization:
Mitochondrion matrix.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MPPPPKRKWPNRPRGGGGANGSASGTPTTPRSTVAQQPKRPKVEDAAPAAEGVDVKQMYSTSAGNASAKPFSELSSVLDKSLLDGLDKMGFEFMSPVQQKVLTELPSLSSDCVVQAKTGTGKTVAFLLPAIQNLLAGNMPPRGKVAILVVCPTRELALQIAKECNGVTACLPRKMECHTAFGGTSRASNLKAFLNGNPTILVATPGRLDDILGEEHVRERFTHLKTVVLDEADQMLDAGFAPAVKKILRRIPPKSDGWQGMCFSATLPKEVLDIAKIVLFPGFTHLTTVDPNEVPTHERVPQYFLSVPNVGQTFAALSALIQEEHKQDPTDFKAIVFGTTANGVGLLYDLYKHALPQFRVFELHSRMSQPMRTRTTAQFKEATSGILFASDVVGRGMDFPNVGLVVQLGLPSSTEQYVHRVGRTARAGKDGRAVLVLFEKEAFFPRINRTLPIKPYPVDIAAKVPEQEAAITRAFANVEEEAKAKAYQAFLGYNKTFLKKLQLSTTELVRVANEYSRAMGCPEPPLIEKSTIGKMGLKGVPGLNIGSRRH
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MRKNQTTIKTRPARAISQAKDPRESQFPIIEQKQAKPSSVIRSSKKSLDFNRLIKNPRLNDSRLEEALEADLSFKKMELKDNRLQKGSPQKPNLQLISETSQAENEQRASTPPRKNRKEGQDFNARSESFATLEPMHHAEETLAENLRIFIKIYEIMNYLLNSMKKNTTLELINQINQYMELTEDTGFQYLEELLQEHAKQVRQIFLILRVGIVVLVNCFFDLHFYLSSMSNIKNILLYNIQNLSHLSDILLEKLKEKTRISSIFIVVFLIVIQHQQENHCHQKARLLDLHQVEHRIITKSLQIPYKKVRRDLYQFLIIFLRSLQNYTIKESLRNLQEFISFYFTIQQSYQGLLGIPLICVAPQPYLPYTNPKTYTLVLDMDETLIHFTDQTGHFLIRPFTHQFLQEMSQFYELVVFTAGLPDYANWVLDQVDKNKNISYRLFRQHALQYSNQFIKDLSRLGRDLSKCIIVDNVPDNFQNQPENGIFIKTWYSDQNDTALAELGPILKSIVMKKAEDVRLALKEVRKMLTQSIQLPPLQG
The following text describes a protein:
Function:
Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
Sequence:
MTSSEKVTYVPAGEIDKVFAHTTNLASSGLNTKILACSDEFFAAASNLLTPTPPINRPGVFVHTGAWYDGWETRRHNPEPYDWVVIKLGVASGAIQGVEVDTGFFHGNYGEKAELQGTYAPVDSGVTDEQIADPSFNGWTTILPPQPCGPSQRRAWKLNDYDPSNPKPYTHVRLLMYPDGGFARLRLYGHAIPPPAPEHINSAEAPIEELSSALLGGLALSASNQHYTPISNLILPGRGKDMGDGWETARSRIPGYTDWAIFQLGLPGSVAKIVVDTKDFRGNFPRAVRVHGLLEGSVAAGEVPAHDHPDWIPLLSGDKFCKADTEHVYEGAELAAGGEDTRTFTHMKLTLIPDGGVKRFRIFGQKGDDAAIENGSDSGGRILSPGAMGITKYCIEERRRKNASKSGSQTVLIIARVAGKFQPITQIS
The following text describes a protein:
Function:
Rho subunit of the pentameric ligand-gated chloride channels responsible for mediating the effects of gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the brain. Rho-containing GABA-gated chloride channels are a subclass of GABA(A) receptors (GABAARs) entirely composed of rho subunits, where GABA molecules bind at the rho intersubunit interfaces (By similarity). When activated by GABA, rho-GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient.
Subcellular Localization:
Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Domain:
GABAARs subunits share a common topological structure: a peptide sequence made up of a long extracellular N-terminal, four transmembrane domains, intracellular or cytoplasmic domain located between the third and the fourth transmembrane domains.
Sequence:
MVLAFWLAFFTYTWITLMLDASAVKEPHQQCLSSPKQTRIRETRMRKDDLTKVWPLKREQLLHIEDHDFSTRPGFGGSPVPVGIDVQVESIDSISEVNMDFTMTFYLRHYWKDERLSFPSTTNKSMTFDRRLIQKIWVPDIFFVHSKRSFIHDTTVENIMLRVHPDGNVLFSLRITVSAMCFMDFSRFPLDTQNCSLELESYAYNEEDLMLYWKHGNKSLNTEEHISLSQFFIEEFSASSGLAFYSSTGWYYRLFINFVLRRHIFFFVLQTYFPAMLMVMLSWVSFWIDRRAVPARVSLGITTVLTMSTIVTGVSASMPQVSYVKAVDVYMWVSSLFVFLSVIEYAAVNYLTTVEEWKQLNRRGKISGMYNIDAVQAMAFDGCYHDGETDVDQTSFFLHSEEDSMRTKFTGSPCADSSQIKRKSLGGNVGRIILENNHVIDTYSRIVFPVVYIIFNLFYWGIYV
The following text describes a protein:
Function:
Induces translational repression through 28S ribosomal RNA cleavage in response to ER stress. Pro-apoptotic. Appears to play no role in the unfolded-protein response, unlike closely related proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MASAVRGSRPWPRLGLQLQFAALLLGTLSPQVHTLRPENLLLVSTLDGSLHALSKQTGDLKWTLRDDPVIEGPMYVTEMAFLSDPADGSLYILGTQKQQGLMKLPFTIPELVHASPCRSSDGVFYTGRKQDAWFVVDPESGETQMTLTTEGPSTPRLYIGRTQYTVTMHDPRAPALRWNTTYRRYSAPPMDGSPGKYMSHLASCGMGLLLTVDPGSGTVLWTQDLGVPVMGVYTWHQDGLRQLPHLTLARDTLHFLALRWGHIRLPASGPRDTATLFSTLDTQLLMTLYVGKDETGFYVSKALVHTGVALVPRGLTLAPADGPTTDEVTLQVSGEREGSPSTAVRYPSGSVALPSQWLLIGHHELPPVLHTTMLRVHPTLGSGTAETRPPENTQAPAFFLELLSLSREKLWDSELHPEEKTPDSYLGLGPQDLLAASLTAVLLGGWILFVMRQQQPQVVEKQQETPLAPADFAHISQDAQSLHSGASRRSQKRLQSPSKQAQPLDDPEAEQLTVVGKISFNPKDVLGRGAGGTFVFRGQFEGRAVAVKRLLRECFGLVRREVQLLQESDRHPNVLRYFCTERGPQFHYIALELCRASLQEYVENPDLDRGGLEPEVVLQQLMSGLAHLHSLHIVHRDLKPGNILITGPDSQGLGRVVLSDFGLCKKLPAGRCSFSLHSGIPGTEGWMAPELLQLLPPDSPTSAVDIFSAGCVFYYVLSGGSHPFGDSLYRQANILTGAPCLAHLEEEVHDKVVARDLVGAMLSPLPQPRPSAPQVLAHPFFWSRAKQLQFFQDVSDWLEKESEQEPLVRALEAGGCAVVRDNWHEHISMPLQTDLRKFRSYKGTSVRDLLRAVRNKKHHYRELPVEVRQALGQVPDGFVQYFTNRFPRLLLHTHRAMRSCASESLFLPYYPPDSEARRPCPGATGR
The following text describes a protein:
Function:
Plays a crucial role in virion assembly and budding.
Subcellular Localization:
Virion. Host cytoplasm. Host cell membrane; Peripheral membrane protein. Note=During viral budding, associates with the inner side of the plasma membrane of infected cells. Found in nuclear punctate structures that have been proposed to be the sites of viral replication and transcription, also termed viral speckles of transcripts (vSPOTs) (By similarity).
Sequence:
MNSKHSYVELKDKVIVPGWPTLMLEIDFVGGTSRNQFLNIPFLSVKEPLQLPREKKLTDYFTIDVEPAGHSLVNIYFQIDDFLLLTLNSLSVYKDPIRKYMFLRLNKEQSKHAINAAFNVFSYRLRNIGVGPLGPDIRSSGP
The following text describes a protein:
Function:
Promotes guanine-nucleotide exchange on ARF1 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays a role in the epithelial polarization (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein. Cell junction, adherens junction. Cell junction, tight junction. Note=Translocates from the cytosol to membranes enriched in phosphatidylinositol 3,4,5-trisphosphate.
Domain:
Binds via its PH domain to the inositol head group of phosphatidylinositol 3,4,5-trisphosphate; Autoinhibited by its C-terminal basic region.
Sequence:
MDEDGGGEGGGVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEESKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDEFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFIAMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK
The following text describes a protein:
Function:
Lipolytic acyl hydrolase (LAH).
Domain:
The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence:
MASQSTQTSKKVTILSIDGGGIRGIIPAVILHELEKHLQKLDGPNARIADYFDIIAGTSTGSILTAMVTAPEKKRLNSNEPNERPRPRFDASSYVPFYEDKGKVIFGSPIFHVHDYPKKVKEAVWYVLSRFTSPINWFEAGMAILTRHGPSALRSAIKKELGDVKLRETVTKVVIPTFRIKKTKPVIFTSDMTIDLKNKPYEDFDLADVVLASSAAPTFFPPHNIHFKGKDEGFFDGGVSANNPTLAALCEATRTYGNERNYGNYLVLSLGTGRAGTIRPQAGQGLAEWFFKEIVGKFKFQFILNTVDDAVEFYLSRIFHSNGPNTNYLRIQANLSLRPPFSFNSCLAPEYDEVKGEAEQMDNASWSNTLTLKNIGMRLLDKNVMIVNPDTGEIDKLEYKYKDALAKFAKELVVEKKKQRPGN
The following text describes a protein:
Function:
Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
Subcellular Localization:
Cytoplasm.
Sequence:
MESSSPGMRWDADDVTPLFSCPSSDEETMKRGTALNGSTLVSSLLPSLPLFLSSSSSMRSSDLHFSSRLLISTDANLVFSVHAAVDGAQENSLALTAKIGTTSRGIGPTYSSKCFRNGVRVADLIGDTYAFEDRYRRLVSYYRNQFPNIQVDEDVELAKFKELRAKLESLQLVGDTVGYLHKAISEGKKLLVEGANGALLDIDFVVKAYQTRVGTGPFPTELFDDDGAKLQSIGQEVGVTTGRKRRCGWLDLFLLRRSAQINGYTHIALTKLDILDSFPELKVGGSRGCTR
The following text describes a protein:
Function:
Catalyzes pseudouridylation at position 35 in U2 snRNA stem-loop II region which induces particular conformation of the mRNA-U2 snRNA duplex and places the nucleophile in an accessible position for the first step of splicing. Also catalyzes pseudouridylation at position 56 in U2 snRNA. Also catalyzes pseudouridylation at position 50 in 5S rRNA, position 13 in cytoplasmic tRNAs, and position 35 in pre-tRNA(Tyr). Pseudouridine residues in tRNAs may stabilize the local RNA conformation, favor interactions with protein partners and play an important role in the stabilization of the codon-anticodon interaction with mRNA. Also catalyzes pseudouridylation of mRNAs in response to heat shock: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAR-3'.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MSQENHVDVPRKRIRIDQSESSRNLERNGLEDEANAPSDLSGQKFYMTESDVGIDAFLNPNLPSIDGIIKARFTDFAVFEVDTDGNIVHLTDMEAHDPILSKATGDKETEDAKDSSNQDISNDQKAPSFKEQEPATLPILPNDLQSIIPKGIGNEFIQSLHKLSVGEITDPISLILPENTPPMDKGQRTILHQFIRNNFSGLESSTKGNGTFTVSKTTRKNQPRSRRDPRLSWKALGGEYCHFHLYKENRDSMDCLGKIARLLKVPTRTLSIAGTKDRRGVTCQRVAIHHVRASRLAQLNSGSLKNSTYGFLLGNYSYKNSNLRLGDLKGNEFHIVVRNVITPKEKVVEALNSLKEHGFINYFGLQRFGTSSVGTHTIGVRLLQSDWKGAVDLILSPRPEHTGSVKEAIDLWHSTHDAEASLRILPRRMIAESSILETWSRSGNQTDYLGAFQRIPRHLRSIYPHAYQSYVWNRVASWRIKNLGDRPVVGDLVYSTESNGLSQKSPIVDPEAPDLLEDLPVSSKLSARPIEEDEVNNFSIYDIVLPLPGRNVIYPKNETFDIYKSVMNEASLDPLNMSRKDRELSLPGDYRKLLVRPENMEFNFIKYDNMEQQLILTDKDRLENRSISVSSEVGKHTAVTLKFVLPSSAYATMALREALRTATASGDQRMLMPAVLKDSI
The following text describes a protein:
Function:
Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes.
Subcellular Localization:
Cell membrane, sarcolemma, T-tubule. Endoplasmic reticulum membrane; Single-pass type III membrane protein. Preautophagosomal structure membrane; Single-pass type III membrane protein.
Sequence:
MVQAAKPQSPVGGKQGAMTEVSSNVWVALVLGVFSAIFAWIWFRGTNEQERSEPQKESEQVGVGESAPRQEPSASQQEDGGVAQGKMSARIPVGAQVQPVVSAHVPRHVLEQESQRVPDHDAAQNKKPKSKVILEPIVKAKESLNPCQTETPQVLCKTENGALSIQKEFDLGKKDYPEPSVAEDELIVPQECVYSMPGMPCEDQVVECKLSPNVKTTGAITECQEQEDAFLPHSSGGGNYEAILLPQSRTEAEHMDLPVPNLIGEKCEPVHSPEKIELVRATISDAKLPDTDNTKLKRVAAVQPMSHNIKVDFKVHYITHSDTQWVAVIGNHENLGGWETLVPLKSGKDGFWSHSVILPADTSVEWKFVMVENGKIKRWEECCNRSLTTGHDDVEAHELWGYL
The following text describes a protein:
Function:
Acts as a membrane anchor for Skb1 in forming plasma membrane microdomains. Promotes mitotic entry by sequestering mitotic inhibitor Skb1 from its regulatory targets Cdr1 and Wee1.
Subcellular Localization:
Cell membrane.
Sequence:
MSSIIQNPIESSYFVEDLSAVGNSQLHSGRSLTYGDRKANIDTRSGGGRRFWSNLNDSGNSFGAVPASSMNLSYGPTKSATISSKDGAMSRSSRYYVSSELKATLPSLDGRRLSKRNAANHASHHRMPDESASYRTRGEYESSSPRVPQKSLRRYYSTRTAQRLDVRRPASRSSRYSKTSDLPPSDPGRFVDDSDLTPHTDFTNRFVDSDFDPDSGVGRSSSPDQMMSRNNNLNINARMTSTSSKPYAKENQQLISSMAPVEQKNSFSTAREQYVAPALSFAEPVETQHNHMPKTTPLRGTSTVMNGSPIGPYSSSSNATGMYGVSKGHSSSTRRPFFSDVGSSQPAEEFVGSSSSHGRQQDSYIADDSDSERSYRRVRDQYLSKPRLSDKNRYSTFSEFPGQGTPSASQSNLRRSNTVRPTSFYYEKLHIKNDNPSFQALPYETTTQERKPVVKPDSIKTVKPEKKKSKGFFKKLMHKISHIFD
The following text describes a protein:
Function:
Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity).
Miscellaneous:
MISCELLANEOUS: Several bitter taste receptors are expressed in a single taste receptor cell.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MVPTQVTIFSIIMYVLESLVIIVQSCTTVAVLFREWMHFQRLSPVETILISLGISHFCLQWTSMLYNFGTYSRPVLLFWKVSVVWEFMNILTFWLTSWLAVLYCVKVSSFTHPIFLWLRMKILKLVLWLILGALIASCLSIIPSVVKYHIQMELVTLDNLPKNNSLILRLQQFEWYFSNPLKMIGFGIPFFVFLASIILLTVSLVQHWVQMKHYSSSNSSLKAQFTVLKSLATFFTFFTSYFLTIVISFIGTVFDKKSWFWVCEAVIYGLVCIHFTSLMMSNPALKKALKLQFWSPEPS
The following text describes a protein:
Function:
Choline transporter.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MGARAGPPDGSEESKKEWGKYEYPGDVKHMKCHNCFCAIVFLILFGCMIALLVIGVLRAKVWTLTKSWDTHGFYCGFDNSQLNIKGAPEGLVKPNLVDYPYLFFDALNVTRQICVSKCPTNGDLQAIIKHNVTKSENVTYLDNTTYNTNYYPDANETYEYKTTVVFNRCIPEVNLEEDLINGTQFIDGLKQALDAIPALSSALNSVFNLKWQILACSAASLIVGLVWIMLLRCITGCIVYFVVMLVPIALIGFGVWLFMKGSLMGTISEVVKTKKLTGSQITAVIVWVIAFMVILIIIFLWSKLKSTVAIIKVAAKALGHNFMVIFVPIITMIFAFLLWAALLVSSVTLYTSADFKYWVDDDGLDKGIGQIKFDLNKVLQYMLIYNFVYLVFISVHMYFVNYYASSVTLVKWYFTGQEGKTCCGCTCFYGFWLAWTKGLGTITISSLIMTPLYLFIIFMEYLDKKSKQEGAPIIVQFLIKCLKCCLWCFTKIVQYLNKVLFTIQQIFNTNWGPSAKLVIDVVVSDTLLTIMLNGISFFILFLSKVVVSIITTLGFMIWVYYVKKDSIAGSILAAAAVFFLSYIVSSFLLSAFDNIIDIVFVCYQSEKSIPGYEAGDASKMVNQTITDMKGAHENANTSSKVSAEKLEDENEMKE
The following text describes a protein:
Function:
Involved in the uptake of nicotinic acid.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSNKFTMESPKHLVDDVLFISPTNDGSEEKPTEVTFQEDEGHDASLHNRSHDKKSELATEREIMATTTDDDGIPSPSHPMEKRVLRKMDIYLIPLMGMLYFLSNLDKSNIGNAEVAGLSKDIHLVGTQYNTCVTVFFATYVLFDPIGTNLLKIMGPPLMMSICLTCFGAISLGTAWVKNYAQLIVVRLLLGAFEGMIYPAINMYLSVCYRREQYALRFAFVFSAACLSSSFGGLIAYGCSKISGSLKDWQYIYIVEGCISLGFVPFYAFGLSKNLEDSWFFNKEEKEYISERYKTMNTFDPDEKFEWFQVWQAVKDVKTWASAVALFGIDLTTFGLTVFLPIIITSMGFTNVRAQLMTVPIYFLTAIVFFICAVWSDRIKLRSPFILGACLTTSIGIAIVLGSQVHGVRYFGVYILCMGIYVNAACNCLWLSGNTGNYFKRATALGINLFFGSGSGLVSGQIFVAKDKPRYIKGLSISLAFQVFSIFMTVVQIFLYKRENDKKKAIIDRCNELGEPIPYDERLSDKNPEFKYMY
The following text describes a protein:
Function:
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Has an acyl-CoA thioesterase activity towards the long chain fatty acyl-CoA thioester palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA). Displays a substrate preference for fatty acyl-CoAs with chain-lengths C12-C18.
Subcellular Localization:
Endoplasmic reticulum membrane; Lipid-anchor. Cell membrane; Lipid-anchor.
Sequence:
MSALEWYAHKSLGDGIFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLRDRAARDNAACRPLLAVATHVHFDHSGGLYQFDRVAVHHAEAEALARGDNFETVTWLSDSEVVRAPSPGWRARQFRVQAVQPTLVLQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDRGLVEKVLPGHFNTFGAERLFRLASNYISKAGICHKVSTFAMRSLASLALRVTNSRTSP
The following text describes a protein:
Function:
Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the second glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(1)Man(9)GlcNAc(2)-PP-Dol to produce Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MDHREKSDRRLLLWFFAVATAVKLLLIPSSRSTDFEVHRNWLAITNSLPLTKWYFDETSQWTLDYPPFFAYFERFLSIFARLVDPRIVDLQSGLDYNAESVIYFQRISVIVSDLCLLYGVYRLTRKLEPLKRNLICALVIWSPGLLIVDHIHFQYNGFLLGWLLLSISFLQEGRDLLGGFLFAVLLCFKHLFAVTAPVYFVYLLRHYCWSGLVTGFRRLVTIGAVVVAVFAAAYGPFIYHGQIQQVISRMFPFGRGLCHAYWAPNFWVFYIILDKGLAVLLRKLGYEIQIPSASFTGGLVGDSSPFAVLPQITPLTTFAMVLLAISPCLIKAWKKPHSGLVARWVAYAYTCGFLFGWHVHEKASLHFTIPLAIVAVQSLEDAKHYFLVSIVSCYSLYPLLYEPQEYPIKVLLLLLHSVVMWLGFAAQYTDYKAQKKETSEIKSKFRIGCFEKSYLMGLIIVEIVSQFLHPYFLGDKLPFLPLMLISTYCTVGIMYSWIWQLRKILT
The following text describes a protein:
Function:
Catalyzes the hydrolysis of the 5-position phosphate of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol-3,4,5-bisphosphate (PtdIns(3,4,5)P3), with the greatest catalytic activity towards PtdIns(4,5)P2. Able also to hydrolyze the 5-phosphate of inositol 1,4,5-trisphosphate and of inositol 1,3,4,5-tetrakisphosphate. Regulates traffic in the endosomal pathway by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with endosomes. Involved in primary cilia assembly. Acts as a regulator of phagocytosis, hydrolyzing PtdIns(4,5)P2 to promote phagosome closure, through attenuation of PI3K signaling.
Subcellular Localization:
Cell projection, cilium, photoreceptor outer segment. Cytoplasmic vesicle, phagosome membrane. Early endosome membrane. Golgi apparatus, trans-Golgi network. Membrane, clathrin-coated pit.
Sequence:
MSNNARKMCVCFERRGLGTVFFFVSFSLAVIQGLEVTGGRRVPCELSLARLGGEYNLIIRSREKEVPVQDNIPINSRFKCLQEAEETLLIDIATNTGCKIRVQGDWTAERLFEIPDEEQCLAFLDEVLRIQKAPSKASFPDPVDNASWQQVKGLSRPTGPISAGFEDNFSAMSLEKRRNLQNQQMSAHRDPPPPPLPPNRPVLREKESMSKEQPKVSGTMRMLFTPSTNTQSGQREGLIKHAIAKREKEYVNIQNFSFQELDLSTEAFFYFDSTKEQEWLTAVEKALHSKAKYKKVQLVRLVGMMLLVFARKEHYSYIRDIMAETVGTGIMGKMGNKGGVAVRFVFHNTSFCIVNSHLAAHVEDFERRNQDYKDICARMSFLPPDQGLPQLTIMKHDVVIWLGDLNYRLCLPDANNVKTMISKNELQKLLTYDQLNIQRTQKTAFADFTEGEINFIPTYKFDSKTDRWDSSGKCRVPAWCDRILWRGTDVNQLQYRSHMDLKTSDHKPVSSLFLIGVKVVDDRRYRKVFEDIVRMMDRMENDFLPSLELSRREFTFENVKFRQLQKEKFQITNNGQVTCHFSFIPKLNDSQYCKPWLRAEPCEGYLEPNETVDISLDVYVSKDSVTLLNSGEDKIEDILVLHLDRGKDYFLTISGSYLPSCFGTSLETLCRMRRPIREVPITKLIDLEEDNFLEKEKSLLDMVPQDSEDSSSERPLQIPKEIWILVDHLFKNACHQEDLFQTPGMQDELQDIIECLDTSIPETIPGSNHSVAEALLIFLEALPEPVICYELYQRCLECSQDSRLCRQVICQLPRSHRNVFRYVMAFLRELLKYSESNNVSANMIGKHWPEPAMSPLSPCHSAGFSHRNACFPAATLFASLLLRPPPTVVLKQTPQDRQLAISFLLGFLLGAEDY
The following text describes a protein:
Function:
Beta-mannosyltransferase involved in cell wall biosynthesis. Required for beta-1,2-mannose transfer on phospholipomannan.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
MVQKQYRFAPKSIFTFVFLCFVAIVVIISTSSLVQVEESLDPIEVSDEIKKHDRKVVIFPSNFQSANNKLADFLTEAFGQRLNKGDIVYKNRDTYELPQTVYTWNTIDLFQSIGEKDNLKCEKIPLNFEISKIYNKNADLYKILRDFKNENSFYYKEVSVFFPDLGKQLRERTIEKHWFQLIGSSVWLEQYGVHLMISRVIYTKTGNKVQPVISLSYVQAFDRNWTELKNVTLVVPDSGKAKFKTVSYPSFIPIPVYHNVNQQRGKFYGVEDPRIMLVKNKEGYEEPLIVYNSFNRSPPNANYLEEIKNLVKLDTYRSIFMAWIWRTQLGKSNVGSSLPDLATTDDHKYVKVKELSLPNKKRPKTEKNWTPFVIYEDQKKQGYDSHLYFIYSFQDLSILKCSLWDAGNCIWEYRMNNKKTKISELRGGTELMNVNQLLDKYNFAGLETVKDQFKGKEVWISFARAALSKCGCGSKMYRPNFTVLVKQGGRFQLSFVSSYMDFGVPILPWAKGKGLCNGKNLLIPNGISNWVLAKDEGGGFQDYMTLSLSRSDSTVDIIHMKGILKSILSEYLLQTNRDVLNNNAIHCALLESESYCKSYAENYRAHLKRWQN
The following text describes a protein:
Function:
Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.
Sequence:
MAAAAASSFSYFPSPLPPAWSESLYCLSPEHVQERLQDDAVETVTSVEQAKVEDKIQEVFNTYKINHHVPRLILHREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPESVASDVCQFLERCQSPTGGFGGGPGQHPHLAPTYAAVNALCIIGTEEAFDVINREKLLEYLYSLKQPDGSFIMHIGGEVDVRSAYCAASVASLTNIITPKLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKEKSLNLKCLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSRWMFHQQALQEYILLCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGEILCDVVLGVPENRLQPTHPVYNIAPDKVVQAVMYFLQKPIPCVEEEVAASSAATD
The following text describes a protein:
Function:
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Sequence:
MLRLGSHVSMSGKKMLLGASEEAASYGSNTFMIYTGAPQNTRRKPIEELNIEAGLEHMKAHDMADIVVHAPYIINIGNSVKPETFELGVNFLQSEIERTRALGAKQIVLHPGAHVGEGADKGIKQIIQGLNEALIHDQDVQIALETMAGKGSECGRTFEELAQIIDGVTHNELLSVTFDTCHTHDAGYDIVNDFDGVLNQFDKIVGIDRLKVLHINDSKNERGAHKDRHANIGFGHIGFDALHYIVHHPQLADVPKILETPYVGGDKASKKAPYKWEIAMLKNGEFDPDLLNKIQNS
The following text describes a protein:
Function:
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Sequence:
MERILSSRLALDPQEFVEGGAGAEETGEGLEEDAEDVQDAYSEGAGECYPAETEVKLEYPTVPIPIPVKVTVGTSARPPNSSQPASNLSARAPKRPRKRRSNFPMEKMMEQFLEQSAQAEENFYRLEEQRLQAEDRRRETEHARELHMLQMLGQMFSSMSSSRAVSSTVGSAASPSKPPPPVRPPVISSASHSHVRRPSAQTDCFSQQSQSLSAETQALAFERYFTLGSSAHRGMDEDIFSLVKTIIPPLTSKKHKGQDGRIGIIGGCQDYTGAPYFAAISALKVGADLSHVFCTKDAATVIKSYSPELIVHPVLDSLNAVEEIEKWLPRLHAVVVGPGLGREDVLLKTAKEVIEKSKARDIPVVIDADGLWLVTQQPSVIQGYQKGILTPNFMEFTRLYEALHHEPMNAGDRQRSVLQLSAAMGNVTVVLKGDQDLISDGSKVYSCSIEGSGRRCGGQGDLLSGSLGVLAHWAHSAPEIKARSLNPSVVAAFGACSLTRWCNNQAFQRHGRSTTTTDMIQEIGPAFRKLFES
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MESGAGEWASKPAQSAASSDNGSNDAGDFECNICLELAQDPVLTLCGHLYCWPCLYRWLTHHSHCHECPVCKALIQEEKLVPLYGRGKTQTDPRSKSYPGIDIPNRPSGQRPETAPPPDANQFANYGFGFMGGFMPMAYARFGNFTLSTAFGGLIPALFNVQFHGFQDATVYGTTSDSCAWTAG