lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain. Inhibits nicotine-induced Ca(2+) influx through nAChRs (By similarity). In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner (By similarity). Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity).
Subcellular Localization:
Secreted. Cytoplasm. Cell membrane; Lipid-anchor, GPI-anchor. Synapse, synaptosome. Membrane raft. Cell projection, dendrite. Perikaryon. Note=Colocalizes with alpha-3:beta-4- and alpha-7- nicotinic acetylcholine receptors (nAChRs) in the primary cortex and hippocampus.
Domain:
The UPAR/Ly6 domain is sufficient for inhibiting alpha-3:beta-4 and alpha-7-dependent nAChR currents.
Sequence:
MEPSPALAWLLLLSLVADCLKAAQSRDFTVKDIIYLHPSTTPYPGGFKCFTCEKAADNYECNRWAPDIYCPRDTRYCYTQHTMEVTGNSISVTKRCVPLEECLSTGCRDSEHEGYKICTSCCEGNICNLPLPRNETDATFATTSPINQTNGHPHCVSVIVSCLWVWLGLTL
The following text describes a protein:
Function:
Cyclic nucleotide-regulated potassium channel activated by cAMP.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSVLPFLRIYAPLNAVLAAPGLLAVAALTIPDMSGRSRLALAALLAVIWGAYLLQLAATLLKRRAGVVRDRTPKIAIDVLAVLVPLAAFLLDGSPDWSLYCAVWLLKPLRDSTFFPVLGRVLANEARNLIGVTTLFGVVLFAVALAAYVIERDIQPEKFGSIPQAMWWAVVTLSTTGYGDTIPQSFAGRVLAGAVMMSGIGIFGLWAGILATGFYQEVRRGDFVRNWQLVAAVPLFQKLGPAVLVEIVRALRARTVPAGAVICRIGEPGDRMFFVVEGSVSVATPNPVELGPGAFFGEMALISGEPRSATVSAATTVSLLSLHSADFQMLCSSSPEIAEIFRKTALERRGAAASA
The following text describes a protein:
Function:
Photoreceptor required for image-forming vision at low light intensity. Can use both retinal and 3-dehydroretinal as visual pigment. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Signaling via GNAQ probably mediates the activation of phospholipase C.
Subcellular Localization:
Cell projection, rhabdomere membrane; Multi-pass membrane protein.
Sequence:
LHMIHLHWYQYPPMNPMMYPLLLIFMFITGIPCLAGNFVTIWVFMTTKSLRSPANLLVVNLAMSDFLMMFTMFPPMMITCYYHTWTLGPTFCQVYAFLGNLFGCTSIWTMVFITFDRYNVIVKGVAGEPLSNKKAALWILSAWVLSFSWCSAPFFGWNRYVPEGNLTGCGTDYLSEDALSRSYLYVYSVWVYFLPLLITIYCYVFIIKAVAAHEKGMRDQAKKMGIKSLRNEEAQKTSAECRLAKIAMTTVALWFIAWTPYLLINWVGMFARSYLSPVYTIWGYVFAKANAVYNPIVYAIS
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Sequence:
MTSPASIAEPRDGAPKLDPAAVPALSIDGVSHAYGPRRALMDVSFNVQPASFTALLGLNGAGKSTLFSLITRLFGIQSGRVGIFGHDVSKSPGEALRLLGVVFQPRTLDLDLSLTQNLLYHAALHGISHREAAARSAELLGRIGLSERAGSKVRDLSGGQMRRLEIARALLHRPRLLLLDEPTVGLDVKARADIISHVRQLVTEQGIGVLWATHLFDEIMAGDDLVVLHQGKVLAQGPMSRVVTEAGAQDVNTAFMRLTGAQVVPGGGV
The following text describes a protein:
Function:
Polysaccharide-binding protein present at the surface of the cell. Probably mediates xyloglucan-binding before xyloglucan transport in the periplasm for degradation.
Miscellaneous:
MISCELLANEOUS: Gut bacteria supply the human body with energy from dietary polysaccharides through glycosidases that are absent in the human genome. Xyloglucans are a ubiquitous family of highly branched plant cell wall polysaccharides present in the vegetables we consume. Enzymes involved in xyloglucan degradation mediate the conversion of otherwise indigestible plant polysaccharides to short-chain fatty acids.
Subcellular Localization:
Cell outer membrane; Lipid-anchor. Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus.
Sequence:
MKSIYKYLDTRLFLIGLLVLPFLAVVSCQNDDDDAIPVIHYIRVTDPAKADSTFTDVNPGTMIVVVGEHLGGTQKVYINDQEVSFNRNYVTSTSIILTVPNELELTGQNPELKGEIRIETEHGVAAYNMHVLSPAPYITRISATYPIKPGDQMTVIGGNFYEVQAVYLSTEQPAKDGTRPVDVQEITNYEVNNKYSQITLTAPANLLEEGYLVVECYTSSAVTEFKKNGPKPVVTAVSSTMPVVGSTVTITGQNFIEVSRVNINGEFDIPVGDITTSNTFDEISFVLPQAPTQSGHISVTAIGGTVESAEIFYPLENVILNYDGIGSHVWGDCSFVVADGSSAPYVSNGTCLGITGTVSASNYWWKQSYSNAQWVNTSIIPGNIPIDDLKLQFECFVKEVFTGPVFQIAMCENFDAALNGYVPVSSFTGKTETGKWMQCSVSLSSVVADATYQDFLNRNSTHIGVYATNPGSSQATIEVYFDNFRIVRK
The following text describes a protein:
Function:
Acts as a chaperone, as it has a significant ability to suppress the thermal denaturation of alcohol dehydrogenase. Cells overexpressing this gene grow more slowly than wild-type cells, and are less susceptible to autolysis following saturation of the culture in vitro, suggesting this protein may slow down the growth rate of M.tuberculosis in culture and by extension during macrophage infection.
Subcellular Localization:
Cytoplasm. Secreted, cell wall. Note=Probably the external side of the cell wall; the protein is very abundant in older organisms and surface coating could be the result of autolysis of older organisms.
Sequence:
MATTLPVQRHPRSLFPEFSELFAAFPSFAGLRPTFDTRLMRLEDEMKEGRYEVRAELPGVDPDKDVDIMVRDGQLTIKAERTEQKDFDGRSEFAYGSFVRTVSLPVGADEDDIKATYDKGILTVSVAVSEGKPTEKHIQIRSTN
The following text describes a protein:
Function:
Lipoamide dehydrogenase is a component of the plastidial pyruvate dehydrogenase complex (PDC).
Subcellular Localization:
Plastid, chloroplast stroma.
Sequence:
MQASISLSSSSPSSLAFARSDRAVEFFSTNASKPSSFRFCGLRGEALGFSTLKRSGCNQVALSQRRLFKKLSASLKDNGVPSKGFDYDLVIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQSEHHLNALGLQVSSAGYDRQGVADHANNLATKIRNNLTNSLKALGVDILTGVGTILGPQKVKYGKAGFSDNVITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLEFIPDWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEIGKSAQRVLINPRKIDYHTGVFASKIIPARDGKPVTIELIDAKTKEPRDTLEVDAALIATGRAPFTKGLGLDNINVETQRGFVPVDECMRVIDKNGKLVPHVYCIGDANGKMMLAHAASAQGISVVEQVSGKDHVLNHLSIPAACFTHPEISFVGLTEPQARERAEKEGYEISITKTSFKANTKALAENEGEGLAKLIYRPDTGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKFAVHAHPTLSEVLDELFKSAKVNSGVSNPVKEPVAI
The following text describes a protein:
Function:
Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Specific for lipid substrates, inactive towards water soluble inositol phosphates. Specific for lipid substrates, inactive towards water soluble inositol phosphates (By similarity). Plays an essential role in the primary cilium by controlling ciliary growth and phosphoinositide 3-kinase (PI3K) signaling and stability.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Nucleus. Note=Peripheral membrane protein associated with Golgi stacks.
Sequence:
MPSKSACLRHTEAPGQLEGRMLQGQPPNTEKKLIPTPGFLPASDSQGSETNPMPPFSIPAKTSNQNPQTKANLITPQPPIRPKLERTLSLDDKGWRRRRFRGSQEDLTVQNGASPCRGSLQDSVAQSPAYSRPLPCLSTSLQEIPKSRRATGSEGGSPSLWSDCLSGMISTSLDLLHRDAASGGPPSRLASLHASHTPPAMDLSIASSSLRTANKVDPEHTDYKLRMQTRLVRAHSNLGPSRPRSPLAGDDHSIHSARSFSLLAPIRTKDIRSRSYLEGSLLASGALLGAEELARYFPDRNMALFVATWNMQGQKELPASLDEFLLPTEADYTQDLYVIGIQEGCSDRREWETRLQETLGPQYVLLSSAAHGVLYMSLFIRRDLIWFCSEVEYSTVTTRIVSQIKTKGALGVSFTFFGTSFLFITSHFTSGDGKVAERLLDYSRTIQALALPRNVPDTNPYRSSAGDVTTRFDEVFWFGDFNFRLSGGRVAVEAFLKQKPEVDVLALLQHDQLTREMKKGSIFRGFEEAEIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYKSRHKGDICPMKYSSCPGIKTSDHRPVYGLFQVKVRPGRDNIPLAAGKFDRELYLIGIKRRISKEIQRQEALKSQSSSAVCTVS
The following text describes a protein:
Function:
Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Up-regulates STATc tyrosine phosphorylation via an inhibitory effect on ptpC accumulation. Recognizes activated receptor tyrosine kinases, RTKs and terminates signaling.
Subcellular Localization:
Cytoplasm. Nucleus. Note=A very small proportion appears to be nuclear but this may reflect cytoplasmic contamination of the nuclei.
Domain:
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme; The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.
Sequence:
MNRATITSNKSNAPSFLSIPLLAHNNNINNNNNNINNNNNNNNINSNNNGTTTTTTTTTITTISYKNNISELITIIDKIIKDLNNFKSKTVLNDQEFSELNNTIQFTKTSLVNYIHYENENKINFNLSDSKIICSEIKIIEYGIESFIFSICKLYQDLIQFQQLLLKLSSPPTTITFNTTINSTNSFTSNLIINNLLKVDSILKQSIDQLLALFPPSSSSLNNENNNNNNNNYNPYELLSNEAKVLWNQFGGNKITFVPWSIFFKGFQKFFNKEILAYESSLRYTLDFTRDGYVTPFKLSVFIKWFGALPVSLGIFQDVINSKIFSGFISGIEATQLLSRQQVGYYLLRCSKTIVGAFAITFVDSTNHIRHCLLYPVTSSINGGLTLQKPPDIFKSILSFILSFSSKLKYPIGPLDNDLLPPLSIINNNPILILPDENNNNQNNNQNNNNNNINTFSTSPSSFFTIDSSNSSDTNKSPTKSRKSSFKNDKDKKEKEKEKGKDKEKEKERVSDENFDNLPTFLNSEDENDNNNNNNNNNNNNNNNNNNNNNNNNNNSSNNNNCNIKETHQTTSNGSSGNNNNNNNNNNNNNNNNNNNNSSSTTKRNNNNNGSDESKDLCTVCMDNEINTVFLECGHLSCCSLCSVKLKKCPICRSRITRVINIFKS
The following text describes a protein:
Function:
Cyclin-dependent kinase that phosphorylates the transcription factor ETS2 (in vitro) and positively controls its proteasomal degradation (in cells). Involved in the regulation of actin cytoskeleton organization through the phosphorylation of actin dynamics regulators such as PKN2. Is a negative regulator of ciliogenesis through phosphorylation of PKN2 and promotion of RhoA signaling.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium basal body.
Sequence:
MTGFCWRKSGLLGDMEEDRLGRCRSVKEFEKLNRIGEGTYGIVYRARDTKSNEIVALKKVRMDKEKDGIPISSLREITLLLKLRHPNIVELKEVVVGNHLESIFLVMGYCEQDLASLLENMQTPFSEAQVKCICFQLLTGLQYLHESFIVHRDLKVSNLLMTDKGCVKIADFGLARAFSTPAKQMTPKVVTLWYRAPELLLGSTTQTTAIDMWAVGCILAELLAHKPLLPGSSEIQQIDLIIQLLGTPNENIWPGFSKLPLVGQYTVRKQPYNNLKHKFPWLSEAGLRLLNFLFMYDPKKRATAEDSLASSYFKEKPLPCEPQLMPTFPHHRNKRASGTGAESQCKRSKP
The following text describes a protein:
Function:
Overexpression affects chitinase expression, cell separation and budding pattern, and increases trehalose accumulation and heat resistance by inhibiting protein kinase CBK1. Overexpression also suppresses temperature-induced hyperosmosensitivity and sensitivity to cell wall degrading enzymes. Overexpression of both LRE1 and PBN1 confers resistance to laminarinase.
Sequence:
MPNTHTQHVQISEPNPVNTLSTPSKRGHRHRRSLAISGDFDFLKQPAAIVNLPPPQAAENCPSTAPTAVSSTLSPIRYNRFPCKTNEDAGTLDLPEPRFYPLSPKNNLQTPSPRFFISEEPSFSSPVKGVPDAIINLDDALKTRPRSFKSHRRSESAPPDLEVMVDKGNCAAGSNSMIKEEEDSLIEPESKNEYYEQKLPTALLSPLRPSLCVSEQAIDVDDSALNGSPTHHNHGMQNANARNSNTFNSLKIKGQKQRYYHYTKQLPLTVGCDSQSPKEQRSAASMTINQAMTPSSLAYTPSKLASTPATPVSFYDSNADINLESDNFPLKDNPRYAKDGYPKKCGNSQLNRVLDSDKRQDFSGESRRRRSGSPISHMQHRNLIDNMKGRRNSNTINSIFNYKSQHYEMPYDDMMKNENINAQSMPFSVNGVNNENSIGGVITRADDAPLQHSVVKSCTPDGKEEMNRLKSNDSNEYSKSEGQIRTNSQLSKDILMGEPGDMVDLSSFVNAQRKASNETGDLVFSLSQDDDALKTFHASNSAATSNESWCISDDALGKQAQDSEVRRKRKSKLGLFRHIFSRK
The following text describes a protein:
Function:
Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Subcellular Localization:
Nucleus.
Sequence:
MFNLKCTPTAKHAVKVAPKTPTSARRKSSATSSQLPVQKETPYRLRRKIKQNLSKMKEEERGSSSSESDSEKSSSDDEKRNSADMDPYDESGKGYFSLSGKGNTSNHTLSKLGRPVMAPDEINRILEVACDPHATHRKALLRQHRTRFSLWWALLREGFNLLLHGPGSKIKLLQSFKDDMLSESFCVTVNGFNPGLTLQEILTTIIRQVIGQDSSPAPGLAGQVDHIVEHFSKEDADELYLLINNIDGPNLRQSKAQAVLSRLSAVAHIHIVASVDHVNASLLWDQETSRAYRFVWINATTFEPYVLESSLEPLKSCAASTLGSLQHVFCSLTPNARKIFLLIARHQLDSASSPGYSGLSFQDCYHRCREEFLVNSDLTLRAQLREFLDHLLLKIKKGHDGTENLLIPLQNEALRLFVEQKEEDDR
The following text describes a protein:
Function:
Component of the DNA damage/stress response pathway that functions downstream of p53/TP53 and can either promote cell survival or apoptosis. Associated with CRADD and the CASP2 caspase, it forms the PIDDosome a complex that activates CASP2 and triggers apoptosis. Associated with IKBKG and RIPK1, it enhances sumoylation and ubiquitination of IKBKG which is important for activation of the transcription factor NF-kappa-B.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAAEAEGLEPQAAATEDAAGDATEAADAELRLLVGNRLSLDLYPGGCHRLLHLCAQRPPQLGEVEFLQLSGHEDPQLLEATLTQVPRNLQRLRSLVLRGGQHWDVLGACLRGSLTTLPAGLSGLARLAHLDLSFNSLETLPACIPQMRGLSTLLLSYNHLSELPEALGALPSLTFLSVTHNRLQTLPIALGALSTLQRLDLSGNLLDTLPPEIGGLSSLTELNLASNRLQGLPTSLVGLRSLRLLVLHSNLLTSVPTGLVHLPLLTRLDLRDNQLRDVPPELLDAPFVRLQGNPLGEALPAPQSPPEAPVILEMPRLFLNSDVDSFPVTPQGCSVTLACGVRLQFPAGATASPVNIQYRLWLPEPRLVPLGPHDSLLSGVLELQPHGVAFRQKVSLWLLFVPPRIRRCREVVVRTLSGDSWGDLDTHVEEEAPKRLWAHCQVPHFSWFLVVSRPVSNTCLVPPEGTLLCCSGYPGVKVTFPPGATEEPRSVCMQVVRMASRELRALLGEPEAAASPLLCLSQSGGPPSFLQPVTVQLPLPPGVTGLSLDRSCLHLLYRTPLEAAWDDITAQVALELTHLYARFQVTHFSWYWLWYTTKTCVQDLARKAWERLRLHRVNLIALQRRRDPEQVLLQCLPRDKVDATLRRLLDRYRGPEPSDTVEMFEGEKFFAAFEKGIDVDAERPDCVEGRVCFVFYSHLKNVKEVYVTTTLDRQVQAVRGQVSFYRGAVPEEVPEEAKAARQKKGMDTVWMATLPIKLPVWPGVVAAVYEGGRGGTEAWGWSGAEGRAHCTPSFSQRLRGSEGLGQGRGPGLSLAPLNLGDAETGFLTQSNLLTVAGRLGPDWPAVALHLGLPYRELQRIRHEFRDDLDGQIRHMLFSWAERQAGQPGAVGLLLRALEQSDRLDVAEEVRAILELGRQKYKDSIQRTSLAPRGLDPADPAAPQSVESAQA
The following text describes a protein:
Function:
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence:
MKTFALILAGGQASRMGGEDKGLALLGGKALIDHVIDRVRPQVSHIAISTNRNLEEYARRSPHIFPDARQWQHFGPLSALCTAANDLQLAAADWLLVVPCDMPYLPDDLVARFETVSKRTPLCNAYYVETPITMHYNIMYIRPQILQSAIPYLFSGMKTLRSWLQQQRARPVRFEFDGHFADLNTQIDLQEG
The following text describes a protein:
Function:
Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.
Subcellular Localization:
Cytoplasm.
Sequence:
MKNVIIGTAGHIDHGKTTLIKALTGRETDTLREEKDRGISINLGFTFFDLPSGKRAGIVDVPGHEKFVKNMLAGVSGIDVVLMVIASDEGIMPQTKEHLEILQLLNVNKGIIVLTKTDMVEPEWLDMVKEDLREELKDTFLENADIYPVSSKTKEGIDELIKAIDNMTEHIETKDIQGHFRLPVDRVFSIMGFGTVVTGTVISGSIKEGQTVQIYPSKVVTKVRGIQVHDEPTKIAEAGQRCAINLSNIKKTDVDRGDIVSIENLMEPSMMIDCKLYYLKSASKPLENRQRVRLYHGTSEIICRVVILDKEYLNPGEEGYVQLRLEKPITCQRNDRYVMRSYSPMVTIAGGSIIDPLPKKAKRFNEKYIEELKLKESGDTSNIIEKIIEKLSSKFPNEDEILKALGKNEENISDEIEELIKLQKIVSFSNGDKKVYTHINYIDKKVKEMTSILKEFHQKNPLKWGVSKEELRIRALGKDIKQKTYDKLLELLESKELIKIHGKYISEHDFNVEFNKEQKAIYDRIIVNYKKEKYSPPKYEELISREQNEIEFKRVYEAVLEEGTLFKVNEDCILLTSDYNEAKEKVKKYIEDNGKITVAEFRDMMDTSRKYSLAILEHFDGIKFTKRNGDERVLY
The following text describes a protein:
Function:
Putative mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Domain:
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of Timm8ab from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).
Sequence:
MESAWSSRGTSLGSSDPQLQRFMEAEVQKQRVQLLIHHMTELCWEKCMDKPGPRLDGRAELCLVNCVERFIDTSQFILNRLEQTQKARPLFSERLSD
The following text describes a protein:
Function:
Probable GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Regulates the localization and assembly of presynaptic components during presynaptic development and is required for specifying the identity of axons during initial polarity acquisition. In these roles it is thought to act cell autonomously downstream of syg-1 and syg-2 and upstream of syd-2, possibly as a positive regulator of the latter. Required for the control of movement, egg-laying and the correct localization of elks-1 (By similarity).
Subcellular Localization:
Synapse. Note=Presynaptic terminals.
Sequence:
MLPLQGFNMTYPRKGVMPYPSTFLYREEPSVSTTECCCCWLCRLLCCCSTVDSQTALRDRMNASQPPPGGGGRLPDEVYRKIKAVDQGQSTLTQSGIQGLSARTLDENQRGDLVFQLVEIIKKPGQSLGLYLREGNGKDRSDGVFVSRFGDNSELAKSFLMSIDDVVLILSIPRRLLLRIRFSKSMRHEVITSRSSERPVVVFHKYDDRRDSETNAPILSQPTSTANTWLGKKSRQQMEEMRNATTTSTMRAAHASTSSPRNHFAPRLVNGHSQPIGVPSASSASTSDHHYQRFASEPSDSVSRTARVPPPRLASATVRRTESFNSAPGVSSSAPMYTLPRSSTAVPPPDIIGSIPHSARDPLMRSDLPYDPLTGRLSSSVPTDPLLSRSLCSPILPRTLRQPNDSNKSNSLPRRRIMTGGRNVKWRNDVVSTSDLCGEESDGAISAPEYSSPPFSRLTQQQQFRLSNGSPGRTVNDIFSAAEYRNWAGPYDPRGMYGPYPPGQRTTRWSHTYGEQRAPRTSSLPGRTVLAQSLVGSPVLPRHPPPIVQDRPSAVFDRYHVSPLMNRRAPLRAAGPGINVDRLSVSSLTGILYVHILEGRGLKIPEKQKGLTEEMYCVLEVDEQHRARTGVSTIEQKFKWRETFHIDVVNATVSNFFVYSWHPQFRHKLCHKGSLKLLEAFVVDQLNDDRVFALNLEPRGQLIVRIGFHDLQAVFRRTVNPRLNGVFGVPLGRLVQRERRDTPIVLTRLIQEIEKRGVDLSGLYVLCGSVEKKKMLRAQLESNPLGTDLNAENIPDTNVIACLIKDFLRELPEPLISPQIHGMLLEAATVALPNDVQANRTLVLKIIDCLQLSAKNCLLLVLDHLSTILCSSPHNGLTPTRLSLIFAPLLFFCLDAISPYTTSPTSKMAAVRSLDMNQASSSLQMILSIWPSRVNSESGSDSPATSGQKGGGGVSYVSESQC
The following text describes a protein:
Function:
May be involved in synaptic functions in the CNS.
Subcellular Localization:
Endoplasmic reticulum. Golgi apparatus, cis-Golgi network. Secreted. Synapse. Note=In the absence of CBLN1, remains in the endoplasmic reticulum/cis-Golgi apparatus. Partial secretion depends on an association with CBLN1 and maybe CBLN4, but not on CBLN2 (By similarity).
Sequence:
MLGAKPHWLPGPLHSPGLPLVLVLLALGAGWAQEGSEPVLLEGECLVVCEPGRAAAGGPGGAALGEAPPGRVAFAAVRSHHHEPAGETGNGTSGAIYFDQVLVNEGGGFDRASGSFVAPVRGVYSFRFHVVKVYNRQTVQVSLMLNTWPVISAFANDPDVTREAATSSVLLPLDPGDRVSLRLRRGNLLGGWKYSSFSGFLIFPL
The following text describes a protein:
Function:
4-hydroxytryptamine kinase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product. The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD. PsiD does not decarboxylate phenylalanine, tyrosine, or 5-hydroxy- L -tryptophan (5-HTP). 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well. The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine. The kinase psiK catalyzes the 4-O-phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin. The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin. 4-hydroxy-6-methyl-l-tryptophancan also be converted the decarboxylase PsiD, kinase PsiK, and methyltransferase PsiM into respectively 6-methyl-norbaeocystin, 6-methylbaeocystin, and 6-methylpsilocybin (By similarity). PsiK kinase can also turn psilocin into psilocybin. This activity may represent a protective mechanism to rephosphorylate the unstable psilocin to the stable psilocybin in case of intracellular ester cleavage. Moreover, psiK is able to O-phosphorylate the quaternary amine 4-hydroxy-N,N,N-trimethyltryptamine (4-OH-TMT) to yield aeruginascin, another bioactive compound found in Psilocybe species.
Sequence:
MTFDLKTEEGLLSYLTKHLSLDVAPNGVKRLSGGFVNVTWRVGLNAPYHGHTSIILKHAQPHLSSDIDFKIGVERSAYEYQALKIVSANSSLLGSSDIRVSVPEGLHYDVVNNALIMQDVGTMKTLLDYVTAKPPISAEIASLVGSQIGAFIARLHNLGRENKDKDDFKFFSGNIVGRTTADQLYQTIIPNAAKYGIDDPILPIVVKELVEEVMNSEETLIMADLWSGNILLQFDENSTELTRIWLVDWELCKYGPPSLDMGYFLGDCFLVARFQDQLVGTSMRQAYLKSYARNVKEPINYAKATAGIGAHLVMWTDFMKWGNDEEREEFVKKGVEAFHEANEDNRNGEITSILVKEASRT
The following text describes a protein:
Function:
Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MPKTLRQKLLLALIALLLIVAGYYWNVGLELFNEQPTRPGQDNTIDYYAENAHSLQYQEDGSLDYEMTAVKLEHQKATDITFVTTPDLLLFRGNVQPWHIQSARAEVGPKGKEVELIDDVRVARTDAKGQPSILTTTRLTVFPDKNYAQTEQAVKIDAANGVTTAVGMKAYLKDSRMHLLSNVRGQHEVR
The following text describes a protein:
Function:
Necessary for efficient adipogenesis. Does not show ion channel activity.
Subcellular Localization:
Nucleus inner membrane; Multi-pass membrane protein.
Sequence:
MSGQLERCEREWHELEGEFQELQETHRIYKQKLEELTAFQTLCSSSINKQKTRLKDLKHTLQRYKRHASQEEAELVQQLGANIKERQNVFFDMEAYLPKKNGLLTWWPSQIFPSRLYLNLVLGNVNVTLLSKQAKFAYKDEYEKFKLYLTIILLLGAVACRFVLHYRVTDEIFNFLLVWYYCTLTIRESILISNGSRIKGWWVSHHYVSTFLSGVMLTWPNGLIYQKFRNQFLAFSIFQSCVQFLQYYYQRGCLYRLRALGERNHLDLTVEGFQSWMWRGLTFLLPFLFCGHFWQLYNAVTLFELSSHEECKEWQVYGPVWCGWCVCIGMGGGPGEGWGHFGKNSVSSTTLYPFLCCPVCC
The following text describes a protein:
Function:
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Sequence:
MNIADGRQAFSAPAKLNLDLRITGRREDGYHNIESIFCLIDLQDTVYLKPRDDGKIILHNPVDGMPQEVDLSYRAASLLQKYARNPAGVEIWLDKKIPTGAGLGGGSSDAATVLLVLNRWWQCGLTQRQLIDSGAALGADVPFFIFGKNAFARGIGDRLDEMDIPKQWYVIVKPPVHVSTAKIFTHESLTRNSASSIMPTFQNLQPFRNDMQAVVFKEYPEVWKAYSELSRYGFALMTGSGACVFTACQDRNSAYNIYRQVSDLYEAYLAEGLSKHPLLSV
The following text describes a protein:
Function:
Induces caspases and apoptosis. Counters the protective effect of BCL2; [BH3-interacting domain death agonist p15]: Induces caspase activation and apoptosis (By similarity). Allows the release of cytochrome c.
Subcellular Localization:
Cytoplasm. Mitochondrion membrane. Mitochondrion outer membrane. Note=When uncleaved, it is predominantly cytoplasmic; [BH3-interacting domain death agonist p15]: Mitochondrion membrane. Note=Translocates to mitochondria as an integral membrane protein; [BH3-interacting domain death agonist p13]: Mitochondrion membrane. Note=Associated with the mitochondrial membrane.
Domain:
Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. Apoptotic members of the Bcl-2 family.
Sequence:
MDSEVSNGSGLGAEHITDLLVFGFLQSSGCTRQELEVLGRELPVQAYWEADLEDELQTDGSQASRSFNQGRIEPDSESQEEIIHNIARHLAQIGDEMDHNIQPTLVRQLAAQFMNGSLSEEDKRNCLAKALDEVKTAFPRDMENDKAMLIMTMLLAKKVASHAPSLLRDVFHTTVNFINQNLFSYVRNLVRNEMD
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1).
Subcellular Localization:
Nucleus.
Sequence:
MPSSTASGSAVVYNLADWIPAHERPDSALAVEDFVSLEDLRFKSVFDDGLYDNQDLVPAGLLQAYFETQHRLDRIYDEGSGWAYVRARNSLYPECDGGSRKNQLNRASDKLIQLDDAVPFVGSSPSISTGTQPEGPDLLFADLCSAPGGWSYTILERFPRARGVAMSLSADGGKVGLTWDPRLEPFISSRRLKTTLGVDGTGSVYNPDNVTLLTQLHAAVRELHGPYALFLADGGFLIEGPGGRRHVEHLQESIVAKLLYSEVVAGLRLLKHSGNMVVKMFGSCTVLTSHLLYLLLVCFQDLHTVKPGRSRIVNEEKYIVARGYKGLPRDVLDHLVAVLRDWNERDSDGGPWSLTRLLKPNDSPGYKRYLQMLKELNTTLISVSNKALAGVIDQAEDILKSGGARSRSAPRRKLKM