lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Associates with EBI3 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. Cytokine with pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR which appears to be required but not sufficient for IL-27-mediated signal transduction. IL-27 potentiate the early phase of TH1 response and suppress TH2 and TH17 differentiation. It induces the differentiation of TH1 cells via two distinct pathways, p38 MAPK/TBX21- and ICAM1/ITGAL/ERK-dependent pathways. It also induces STAT1, STAT3, STAT4 and STAT5 phosphorylation and activates TBX21/T-Bet via STAT1 with resulting IL12RB2 up-regulation, an event crucial to TH1 cell commitment. It suppresses the expression of GATA3, the inhibitor TH1 cells development. In CD8 T-cells, it activates STATs as well as GZMB. IL-27 reveals to be a potent inhibitor of TH17 cell development and of IL-17 production. Indeed IL27 alone is also able to inhibit the production of IL17 by CD4 and CD8 T-cells. While IL-27 suppressed the development of pro-inflammatory Th17 cells via STAT1, it inhibits the development of anti-inflammatory inducible regulatory T-cells, iTreg, independently of STAT1. IL-27 also has an effect on cytokine production, it suppresses pro-inflammatory cytokine production such as IL2, IL4, IL5 and IL6 and activates suppressors of cytokine signaling such as SOCS1 and SOCS3. Apart from suppression of cytokine production, IL-27 also antagonizes the effects of some cytokines such as IL6 through direct effects on T-cells. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines such as IP-10/CXCL10 and MIG/CXCL9. In vein endothelial cells, it induces IRF1/interferon regulatory factor 1 and increase the expression of MHC class II transactivator/CIITA with resulting up-regulation of major histocompatibility complex class II (By similarity).
Subcellular Localization:
Secreted. Note=Does not seem to be secreted without coexpression of EBI3.
Sequence:
MGQMADDLGWRLSLLLLSLLLARAGVWGFPRPPGRPPLSLQELQREFKVSLHLARKLLSEVRVQARHFAESHLPGVNLDLLPLGEQLPNVSLNFQAWRGLSDPERLCFLSMTLRPFHTLLGGLGSQGFWTSSERMQLWAIRLDLRDLQQHLRFQVLAAGFNLPGQEEEENEAGRELLPGAPGGPSKPAAQVSWPRLLYTYQLLHSLELVLSRAMRDFLLLSRAGNPAPALGFPTPSSPP
The following text describes a protein:
Function:
Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Forms a heterotetrameric complex with the closed conformation form of MAD2L1 (C-MAD2) at unattached kinetochores during prometaphase, recruits an open conformation of MAD2L1 (O-MAD2) and promotes the conversion of O-MAD2 to C-MAD2, which ensures mitotic checkpoint signaling.
Subcellular Localization:
Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Nucleus envelope.
Sequence:
MNVTPEDNTEVVRMMGDFNSYLAEGRRQHSNSSLLFDMGDTTAGKGDLTMKLETSRDESTVQWDRPETAKRNRVRRLEQQHALEKQGELLWTRSKVAKLETAISQLETEKKREKIEFEKGQETFRMQYERDLEQVNDLRHKLEFLEREEKQAKEELAEERKKLTTIKTQSEKRIMGLQREKLHIQAELEELREGSRSQISSLRNQVKRLEAELEMSDSELAEAQQQVQHHRGQAQARLEQVQQLQEDRIRAVTAEHKVKELELQLSQVQESAAMAKLMKTRLARYEQLEKENKKLLEQNKFYRETSENNQLLKEKLLSLETKYGRAEHSNLQLIKEVEDLRARLKQWEGIDPSGGQTPRSPAEIAKWIAELQRKEALLTEKTGQLTSSARESEAGQKAAASRLREVESQLFASTEKTNQQADLIKKLQRRLLLVTKDRDSIRNILESYESEVTRASSDDGLLQRLQDSEESAQRYQRHMTSLEEDLQRLNAQASEERIKAHRLESELSQLKTQTPSPAPNPISSQEVTTLRKKVEDLEEDRQKLLEEKEILEARVEQRHLQGDFDPTKTKVVHFGLNPTALRRQHRQEELEKLREECEKLRQRLRAAEEGVAADVTASILQTPSSKEMEDLKKQLTTAETKNTRLKEVFQQKIHEFRQACYMLLGYKVDVVKDNNYKLMSMYAERQEDCLMFQMVPGGELQLLETEFSNSQAVMMLVDLHLKTQHSIPAFLSALTLDLFSQQTIA
The following text describes a protein:
Function:
Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Sequence:
MESITFGVLTISDTCWQEPEKDTSGPILRQLIGETFANTQVIGNIVPDEKDIIQQELRKWIDREELRVILTTGGTGFAPRDVTPEATRQLLEKECPQLSMYITLESIKQTQYAALSRGLCGIAGNTLILNLPGSEKAVKECFQTISALLPHAVHLIGDDVSLVRKTHAEVQGSAQKSHICPHKTGTGTDSDRNSPYPMLPVQEVLSIIFNTVQKTANLNKILLEMNAPVNIPPFRASIKDGYAMKSTGFSGTKRVLGCIAAGDSPNSLPLAEDECYKINTGAPLPLEADCVVQVEDTKLLQLDKNGQESLVDILVEPQAGLDVRPVGYDLSTNDRIFPALDPSPVVVKSLLASVGNRLILSKPKVAIVSTGSELCSPRNQLTPGKIFDSNTTMLTELLVYFGFNCMHTCVLSDSFQRTKESLLELFEVVDFVICSGGVSMGDKDFVKSVLEDLQFRIHCGRVNIKPGKPMTFASRKDKYFFGLPGNPVSAFVTFHLFALPAIRFAAGWDRCKCSLSVLNVKLLNDFSLDSRPEFVRASVISKSGELYASVNGNQISSRLQSIVGADVLINLPARTSDRPLAKAGEIFPASVLRFDFISKYE
The following text describes a protein:
Function:
Bidirectional monofunctional enoyl-CoA hydratase 2 involved in the degradation of even cis-unsaturated fatty acids. Devoid of 3-hydroxyacyl-CoA dehydrogenase activity.
Subcellular Localization:
Peroxisome.
Sequence:
MATSDSEFNSDLLLAHKLPETRYTYNERDVAIYALGIGACGQDAVDSDELKFVYHRNGQDLIQVLPTFASLFTLGSLTEGLDLPGFKYDPSLLLHGQQYIEIYRPLPSKASLINKVSLAGLQDKGKAAILELETRSYEEGSGELLCMNRTTVFLRGAGGFSNSSQPFSYKNYPSNQGLAVKIPQRQPLTVCEERTQPSQALLYRLSGDYNPLHSDPEFAKLAGFPRPILHGLCTLGFAIKAIIKCVCKGDPTAVKTISGRFLTTVFPGETLITEMWLEGLRVIYQTKVKERNKTVLAGYVDIRGLSSSL
The following text describes a protein:
Function:
Catalyzes the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues. Also involved in bacteriophage N4 adsorption.
Subcellular Localization:
Cytoplasm.
Sequence:
MKVLTVFGTRPEAIKMAPLVHALAKDPFFEAKVCVTAQHREMLDQVLKLFSIVPDYDLNIMQPGQGLTEITCRILEGLKPILAEFKPDVVLVHGDTTTTLATSLAAFYQRIPVGHVEAGLRTGDLYSPWPEEANRTLTGHLAMYHFSPTETSRQNLLRENVADSRIFITGNTVIDALLWVRDQVMSSDKLRSELAANYPFIDPDKKMILVTGHRRESFGRGFEEICHALADIATTHQDIQIVYPVHLNPNVREPVNRILGHVKNVILIDPQEYLPFVWLMNHAWLILTDSGGIQEEAPSLGKPVLVMRDTTERPEAVTAGTVRLVGTDKQRIVEEVTRLLKDENEYQAMSRAHNPYGDGQACSRILEALKNNRISL
The following text describes a protein:
Function:
Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).
Subcellular Localization:
Golgi apparatus, trans-Golgi network membrane; Lipid-anchor. Membrane raft. Endosome. Endosome membrane. Cytoplasmic vesicle. Cell projection, dendrite. Presynaptic cell membrane. Synapse, synaptosome. Mitochondrion. Membrane; Lipid-anchor. Cell membrane. Perikaryon. Cell projection, neuron projection. Note=Found in subdomains of the plasma membrane termed non-caveolar membrane rafts. Transported from neuronal cell body to neuron projections and neurite tips in a BLOC-1- and AP-3-complexes-dependent manner.
Sequence:
MDETSPLVSPERAQPPEYTFPSGSGAHFPQVPGGAVRVAAAAGSGPSPPCSPGHDRERQPLLDRARGAAAQGQTHTVAVQAQALAAQAAVAAHAVQTHRERNDFPEDPEFEVVVRQAEVAIECSIYPERIYQGSSGSYFVKDSQGRIVAVFKPKNEEPYGHLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDCPMDNSSCRDTDWVMVREPVIKVAAIDNGLAFPLKHPDSWRAYPFYWAWLPQAKVPFSQEIKDLILPKISDPNFIKDLEEDLYELFKRDPGFDRGQFHKQIAVMRGQILNLTQALKDNKSPLHLVQMPPVIVETARSHQRSASESYTQSFQSRKPFFSWW
The following text describes a protein:
Function:
Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Binds to and inhibits the endogenous nicotinic acetylcholine receptors (nAChR) in human rhabdomyosarcoma TE 671 cell line with an IC(50) of 48.2 mM. This neurotoxin is lethal to mice by intraperitoneal injection and to zebrafish by injection at the back of the dorsolateral region.
Subcellular Localization:
Secreted.
Sequence:
MICYNQQSTEPPTTKTCSEGQCYKKTWSDHRGTIIERGCACPNVKPGVKISCCSSDKCR
The following text describes a protein:
Function:
Required for correct biomineralization of the magnetosome; probably converts and then transports some form of iron. It is partially functionally redundant with MamH. May function with MamX, MamY amd Mms6 in biomineralization (Probable). Despite its strong similarity to MsrQ (AC V6EX82) this protein does not genetically interact with bona fide MsrP (AC V6F0A4), which is encoded elsewhere in the genome.
Miscellaneous:
MISCELLANEOUS: This bacteria makes up to 60 cubo-octahedral magnetosomes of about 45 nm in diameter which contain membrane-bound crystals of magnetite (Fe(3)O(4)).
Subcellular Localization:
Magnetosome membrane; Multi-pass membrane protein.
Domain:
Deletion of the C-terminal 'ferric reductase' domain (residues 444-645) phenocopies the deletion mutant; makes a magnetosome with normal crystals sandwiched between flake-like crystals.
Sequence:
MLEAWMPKSGKPSTGTTPADFAPTQWNIIYLLMTVGSLVAALSISIQPLLLDKIFGIAFEKEGAVNADIQVVAEIVSIVCVGWFGLLSDRIGRVRIIATGFLIAVAGAAMSLLSLQIGLAFGAAGLVLFYLTRVLLTVGADTVQLQLSTLVGDVSSRANRPRLMGNLVFMMVFGGTMLSAIIMQMADYKGGVFIIMCLPLLIGIAGFQMTRESLRDVAQPQQAPTGDEHPLRQVWSVITSDPRLQLAFAAAFYTRADVIILSLFFSLWCISVSDLVGVTRTYATAHAAVMIGLLGLAVLAAIPLWRSFIERHSRISAIGASLSLAAVGYIWLGMFANPFNWLVALPLLMVGIGHAGCFVTLQVLTVDVSPKPILGAMVGAGYLVGGLGTVMLVQSGGYYFDALGPRAPFILMGTGKMLVTLYAAWLLANGIDETCDHHLKSTRKVDWKPLVFLTAALPFVWLIGRSVIEGYFSNGSLGEAPVGFVNRYLGDWAFTFLIISLSMRPVQEITGIKSLAKYRRMIGLFAFFYAVLHVLAYVTLEWALNLGDMASDIYKRPFILLGLAAFLLLIPLAFTSTNSQIKKIGGKRWKRLHRATYVINALVALHFILAANHENGEPYVYAAAVIVLLWYRFYQWRGGNVLRALRIG
The following text describes a protein:
Function:
Has antibacterial activity.
Subcellular Localization:
Secreted.
Sequence:
MDLPYLETQAPSMSMPFFFTDHSAMRLHVLFFMLLFLTLLSPVRSGLASGENHCLNLSGVCRRDICKMTEDQIGACKRRWVCCRAWWILIPIPTPLIYSDYQEPLKPKLK
The following text describes a protein:
Function:
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSLDAVVHGARELVVGPAAGGDTLETHADGAVAVVDGAVAAVGDTADVLAAYPAENATTAIDATGKTVLPGFVDPHTHALFAGDRSDEFAAKLRGKPYQEILAEGGGILRTVDAVRAASDAALVANLTAQLDVMLAHGTTTAEVKTGYGLDTETECRMLDAIAAAAAEHPVDVVTTFLGAHAVPDDTDADAYVDAVIDDQLPAAANGPARFCDVFCEADVFTVEQSRRILDAGREHGLAPKLHAEEFTRLGGAQLAADLGATSADHLLHATPEDAAALADAGVTPVLLPATAFVLDEAYADPQQFLAAADNRTGAPVALGTDLNPNCYTHSMGFVVSLACNGMRMAPADAVLAATAWAASALDRGRDGTGTLREGTDGDVLVVDAPSHVHLPYNPGVNNVEAVLTDGTVAVGGGGA
The following text describes a protein:
Function:
One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Localization:
Cell junction, gap junction. Cell membrane; Multi-pass membrane protein.
Sequence:
MCGSFLRQLLAEDSRHSTAVGHLLLPVLLGFRLVLLAASGTGIYGDEQSEFVCHTQQAGCKAACYDAFHPFSPLRFWAFQVILVAVPSTLYMGLILYHVIWRWEESGKVKEETLIHQGEKSRDASGAGSPRLLWAYVAQLGVRLVLEGAALGLQYHLYGFKIPSSFACRREPCLGSITCYLSRPFEKTIFLKTMFGVSGLCLLFTLVELVLLGLGKWWRTWKHKSPSNYSSTSESTKKHKDPTDNFPAVEAKEQFQEAEL
The following text describes a protein:
Function:
Involved in auxin transport. Regulator of the auxin signaling pathway.
Subcellular Localization:
Cell membrane.
Sequence:
MDPWDTYNIPLDHQHRLRNRRDHRHPSFSSTLLDQIYRSIDDSSTNSSSMRKTKHQNREDTRVSANRRDDFNRSKNLKTIEPVFFKHSSSSSSDSSGFSSSESDYFYRRSKSSPAISHPKPIRTTVERFERSPQNHRPNSSNKQEHGSFLKTKSKALKIYSDLKKVKQPISPGGRLATFLNSIFTGAGNTKKLNKINTTVTSTTAAAAAASSTTTCSSASSFSRSCLSKTPSSSEKSKRSVRFCPVNVIFDEDSSKYNNKNNKVYGNNEREYESIRHTLENRVMEENRRVIEAAKELLRSYQKKNKEVIEVSVEDDEEDDDDDALSCTSSDLFELDNLSAIGIDRYREELPVYETTRLNTNRIISR
The following text describes a protein:
Function:
Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides. May play a role in cell-cell adhesion processes in the retina, via homomeric interaction between octamers present on the surface of two neighboring cells. Required for normal structure and function of the retina.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Extracellular side. Secreted.
Sequence:
MSRKIEGFLLLLLFGYEATLGLSSTEDEGEDPWYQKACKCDCQGGPNALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKFQDSSQWLQIDLKEIKVISGILTQGRCDIDEWMTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRTSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECVSKCA
The following text describes a protein:
Function:
Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins including adhesion proteins, growth factor precursors and cytokines important for inflammation and immunity (By similarity). Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2 (By similarity). Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R. Mediates the proteolytic cleavage and shedding of FCGR3A upon NK cell stimulation, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (By similarity).
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Domain:
Must be membrane anchored to cleave the different substrates. The cytoplasmic domain is not required for the this activity. Only the catalytic domain is essential to shed TNF and p75 TNFR (By similarity); The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Sequence:
MRQRLLFLTTLVPFVLAPRPPEEPGSGSHLRLEKLDSLLSDYDILSLSNIQQHSIRKRDLQSATHLETLLTFSALKRHFKLYLTSSTERFSQNLRVVVVDGKEESEYSVKWQDFFSGHVVGEPDSRVLAHIGDDDVTVRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKDFSRLQSPKVCGYLNADSEELLPKGLIDREPSEEFVRRVKRRAEPNPLKNTCKLLVVADHRFYKYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGVQIEQIRILKSPQEVKPGERHFNMAKSFPNEEKDAWDVKMLLEQFSLDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYNPGVKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGNSRVDEGEECDPGIMYLNNDTCCNSDCTLKPGVQCSDRNSPCCKNCQFETAQKKCQEAINATCKGVSYCTGNSSECPPPGDAEDDTVCLDLGKCKAGKCIPFCKREQELESCACADTDNSCKVCCRNLSGPCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWDFIDQLSINTFGKFLADNIVGSVLVFSLIFWIPFSILVHCVDKKLDKQYESLSLFHHSNIEMLSSMDSASVRIIKPFPAPQTPGRLQALQPAAMMPPVSAAPKLDHQRMDTIQEDPSTDSHVDDDGFEKDPFPNSSAAAKSFEDLTDHPVTRSEKAASFKLQRQSRVDSKETEC
The following text describes a protein:
Function:
Trans-acting transcriptional regulator of RuBisCO genes (rbcL and rbcS) expression.
Sequence:
MSIDLKQLKYFLAVAEEKSFSRAAERLHISQPPLSQQIMKLESELGVKLFARTTRTFELTVAGKALMSEAADLLARMRMTIDTIRQIDRGEVGRLRVGIVGSAMWGPIPSLLEEFQTKFPRVTWTLHEMGPTLQYEALRAKQVDVGFWREPRIDDDVLKNDNLRQELCFREDVCVAINEHHPLAKQEAIELMDIAEEPMLTLALDKSSFPRYLMQCCVQAGFQPTIAQEATEPQTLLAMVGAGLGVALMPETTSRIGWPGVVFVPIRSNPPSANLYITYTTQDDAPVVRAFLNILNPAVAG
The following text describes a protein:
Function:
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation-induced autophagy. Involved in correct atg9 trafficking to the preautophagosomal structure. Might also be involved in premeiotic DNA replication (By similarity). Required for the recruitment of the atg5-atg12/atg16 complex to the preautophagosomal structure.
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein.
Domain:
The N-terminus might form a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane; The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway, for the recruitment of atg8 and atg16 to the PAS in nutrient-rich medium, and for its recruitment to and dissociation from the PAS under starvation conditions.
Sequence:
MHFFVRKYRGKAALLSIGTFDGYKIYNCDPFGKCFHKIQGATSIVEMLFSTSLVALVEKDDGNNRKLKLINTKKSTTICELTFPTPLLAVKLNRKRLLAVLEEQIYVYDISNMLLLHTIETTSNVFAVCALSPNSENCYLAYPDSRDHEPRTEGESSSPNVSNSAVSGQVILWDVINCKQITKIEAHKDSLACLAFNSDGTMLATASDNGRIIRVFAIPSGQRLYQFRRGSLPAQIYSIAFHPDSSLLTVTSSTQTVHIFRLKEVYSNLERQGLLPSSPPPKESLLRRSSRSLIGTVGGYLPQSVSGMLDPERDFAYAHIPGDKVTSIAAFGPDNTIVNVATYDGNLYSFRVNLRTGGECAMVNHFCVGLTAA
The following text describes a protein:
Function:
Potassium transporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MDDVEEGVGRPAVQLQYTTKRAASSPWGLRKATLLLAYQSFGVVYGDLCISPVYVYKNTFSGKLRLHEEDEEILGVLSLVFWSLTLIPLLKYIILVLGADDDGEGGTFALYSLMCRRSRMGLLMNSINDGCLSVYSQEEEPREEELKSSLAIKSFIERHYSLRVLLLLFVLMGTSMVIGDGVFTPTMSVLSAVSGLRIKFPELHESKKLFIIHIAHNDLLLLGADASQYFPDYTVLLACFILVVLFALQHYGTHRVGFLFAPILLAWLGCIGGIGIYNIFRWNPSVVRALSPYYIYNFFRKAGKDGWSSLGGIVLCITGAEAMFADLGHFSKLSLRLGFTIVVYPCLVLAYMGEAAYLSKHREDLQSSFYKALPDRVFWPVLIIATLATVVGSQAIISATFSIISQSRALGCFPRIKIVHTSSHVHGQIYIPEVNWALMFLCLAVTVGFRDTEMIGNAYGLAVILVMFATTCLMFLVITVVWSRSVALAALFTAGFGSVELTYLSACLAKVPHGGWLPLLLSLGTLLAMSTWHYGTKRKREHEAQSKVRLDRFLGLSAGMGLVRVPGVGFVYAASAAAGGVPPVFAHFVTNFPAFHRVLVFVSLQTLAVPRVPPGERFLVGRVGAPAHRMFRCVVRYGYKEGRRDHFNFENQLLMKVVEFLQLQDAAAAAKAGGCVSGSGELSVIPAHVDAGSAPPSCSEIDAGRRVRFEEPSGAAAGSEEEVKTLLEELESGVSYMIGHTCVQAHESSPAVKKFAINVVYGFLRRNSRRPAVELGIPNTSLIEVGMTYKI
The following text describes a protein:
Function:
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring (By similarity). This cyanobacterium does not encode bioA (which catalyzes the formation of the precursor for this reaction in the cannonical pathway), instead it encodes bioU, which replaces bioA and also performs the first half of the cannonical BioD reaction. Thus in this bacteria BioD has a different substrate. In Synechocystis replacement of bioU by bioA from E.coli leads to biotin synthesis, showing BioD can use the 'cannonical' 7,8-diammoniononanoate as a substrate.
Subcellular Localization:
Cytoplasm.
Sequence:
MSNFSRAVDQKTLLVAGCDTGVGKTVTTSALAAYWWKCGKDQSFGLMKLMQTGLGDDELYQQLFGHLTRWDVVTPLKFATPLAPPLAADQEGKTIDLGVVWQTLQTMQQNHDHVLVEALGSLGSPVTHELTVADIAALWRLETILVVPVQLGAMGQAIAQVALARQTKVKLKGLVLSCASPEAEGKVEDWATPAMLESFTHLPVLGIVPYLTESERENLSRLAEITARFGLEKLAYF
The following text describes a protein:
Function:
Promotes the exchange of Ras-bound GDP by GTP.
Domain:
The DH (DBL-homology) domain mediates interaction with RASGRF2.
Sequence:
MQKAIRLNDGHVVSLGLLAQRDGTRKGYLSKRSSDNPKWQTKWFALLQNLLFYFESDSSSRPSGLYLLEGSICKRMPSPKRGTSSKESDKQHHYFTVNFSNDSQKSLELRTDDSKDCDEWVAAIARASYKILATEHEALMQKYLHLLQVVETEKTVAKQLRQQLEDGEVEIERLKAEIANLIKDNERIQSNQLVAPEDEDSDIKKIKKVQSFLRGWLCRRKWKNIIQDYIRSPHADSMRKRNQVVFSMLEAEAEYVQQLHILVNNFLRPLRMAASSKKPPITHDDVSSIFLNSETIMFLHQIFYQGLKARIASWPTLVLADLFDILLPMLNIYQEFVRNHQYSLQILAHCKQNRDFDKLLKQYEAKPDCEERTLETFLTYPMFQIPRYILTLHELLAHTPHEHVERNSLDYAKSKLEELSRVMHDEVSETENIRKNLAIERMITEGCEILLDTSQTFVRQGSLIQVPMSEKGKINKGRLGSLSLKKEGERQCFLFSKHLIICTRGSGSKLHLTKNGVISLIDCTLLDDPENMDDDGKGQEVDHLDFKIWVEPKDSPPFTVILVASSRQEKAAWTSDIIQCVDNIRCNGLMMNAFEENSKVTVPQMIKSDASLYCDDVDIRFSKTMNSCKVLQIRYASVERLLERLTDLRFLSIDFLNTFLHSYRVFTDAVVVLDKLISIYKKPITAIPARSLELLFSSSHNTKLLYGDAPKSPRASRKFSSPPPLAIGTSSPVRRRKLSLNIPIITGGKALELASLGCPSDGYTNIHSPISPFGKTTLDTSKLCVASSLTRTPEEIDMTTLEESSGFRKPTSDILKEESDDDQSDVDDTEVSPPTPKSFRNRITQEFPLFNYNSGIMMTCRDLMDSNRSPLSATSAFAIATAGANESPANKEIYRRMSLANTGYSSDQRNIDKEFVIRRAATNRVLNVLRHWVTKHSQDFETDDLLKYKVICFLEEVMHDPDLLPQERKAAANIMRTLTQEEITENHSMLDELLLMTEGVKTEPFENHSAMEIAEQLTLLDHLVFKSIPYEEFFGQGWMKADKNERTPYIMKTTRHFNHISNLIASEILRNEEVSARASTIEKWVAVADICRCLHNYNAVLEITSSINRSAIFRLKKTWLKVSKQTKSLFDKLQKLVSSDGRFKNLRETLRNCDPPCVPYLGMYLTDLAFLEEGTPNYTEDGLVNFSKMRMISHIIREIRQFQQTTYKIEPQPKVTQYLVDETFVLDDESLYEASLRIEPKLPT
The following text describes a protein:
Function:
Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum. Membrane; Multi-pass membrane protein.
Sequence:
MTDLTIIVPTYNEAENIEQLIIQLEDTLKDINFDILVMDDNSPDKTGEKVQRLKSEGHKCDVVIRTENRGLSPAVIEGFGIAKGNVVLVMDADLQHPVSVVPKLYEAIKNGAEVAVGSRHCPGGGIENWAFHRRVISWGAALLARPFTSVSDPMSGFFAVKSSILKRSKLEAKGYKILLEVLVKTGAKNVVEVPIIFTTRVHGESKLTGGVMTNYLLHLFSLFCYPGTCPLLKFIVVGGLGTIIDILIFTLLVSIGLPGGFAQTLSFIAALCNNFFLNSLWTFPQNVDVNEKKKQFIKFGVVSCVAFIIRSLLFKLGRMYVPDEFPYIQMLLFVVIGTVTIINFIGSKLIVFA
The following text describes a protein:
Function:
Probable methyltransferase.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSDIVYANVSHYNKIEASKYDNPSTLAISKVISSKILQFEDNSETSLRHDLPKYDQDRLLLTSDDDLTNVNNFWKKSGMSILDFACGTGLISQHLFPYCKQIVGIDVSQDMVDVYNEKFRKMNIPKERACAYVLSLDDLDGNGDEPFSTEFDAVVCSMAYHHIKDLQEVTNKLSKLLKPNGRLFVADLIKGGDTFHGNLHPDEIAKLGVAHHGGFTPQSILNLFKNASLSNAEVIGKAQANVWVDEAKYQRSTQSKDAKTLDLANGEKLYEVKLQLMVISGIKT
The following text describes a protein:
Function:
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MKLYFIALQFLTVVPLPFRLRWDERALGRSMAFFPLAGLTLGTLLAGADMLFAALVPRPVSDLLLVALLAGVTGALHLDGLADVCDGLAARGGRERFLAVMKDPRVGAVGVVGLVLGLALKYQALLAVPDDLKRQALLLFPAVARYAQVQMTVGANRARQDGLGAAFIAGTGMFQLVTAGTITAVAAWLLLGPAGMAVLAASVLFTGGFRWWFHRHLGGVTGDVIGCASELNEILCLLVILALHRG