ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9EQD2 | MGKRWDSNSSGSWDHIWSGNDTQHPWYSDINITYMNYYLHQPHVTAVFISSYFLIFFLCMVGNTVVCFVVIRNRYMHTVTNFFIFNLAISDLLVGIFCMPITLLDNIIAGWPFGSSMCKISGLVQGISVAASVFTLVAIAVDRFRCVVYPFKPKLTVKTAFVMIVIIWGLAITIMTPSAIMLHVQEEKYYRVRLSSHNKTSTVYWCREDWPNQEMRRIYTTVLFATIYLAPLSLIVIMYARIGASLFKTSAHSTGKQRLEQWHVSKKKQKVIKMLLTVALLFILSWLPLWTLMMLSDYADLSPNKLRVINIYVYPFAHWLAFCNSSVNPIIYGFFNENFRSGFQDAFQFCQKKVKPQEAYGLRAKRNLDINTSGLLVHEPASQNPSGENLGCRKSADNPTQESLMEETGEATNSTET | Function: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47711
Sequence Length: 417
Subcellular Location: Cell membrane
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Q9VNM1 | MIISMNQTEPAQLADGEHLSGYASSSNSVRYLDDRHPLDYLDLGTVHALNTTAINTSDLNETGSRPLDPVLIDRFLSNRAVDSPWYHMLISMYGVLIVFGALGNTLVVIAVIRKPIMRTARNLFILNLAISDLLLCLVTMPLTLMEILSKYWPYGSCSILCKTIAMLQALCIFVSTISITAIAFDRYQVIVYPTRDSLQFVGAVTILAGIWALALLLASPLFVYKELINTDTPALLQQIGLQDTIPYCIEDWPSRNGRFYYSIFSLCVQYLVPILIVSVAYFGIYNKLKSRITVVAVQASSAQRKVERGRRMKRTNCLLISIAIIFGVSWLPLNFFNLYADMERSPVTQSMLVRYAICHMIGMSSACSNPLLYGWLNDNFRKEFQELLCRCSDTNVALNGHTTGCNVQAAARRRRKLGAELSKGELKLLGPGGAQSGTAGGEGGLAATDFMTGHHEGGLRSAITESVALTDHNPVPSEVTKLMPR | Function: Receptor for NPF. Integral part of the sensory system that mediates food signaling, providing the neural basis for the regulation of food response; coordinates larval foraging and social behavior changes during development. Required in dopaminergic (DA) neurons that innervate the mushroom body for satiety to suppress appetitive memory performance; a key factor in the internal state of hunger in the brain. NPF neurons coordinately modulate diverse sensory and motor neurons important for feeding, flight, and locomotion. NPF/NPFR pathway exerts its suppressive effect on larval aversion to diverse stressful stimuli (chemical stress and noxious heat) through attenuation of TRP channel-induced neuronal excitation. NPF neural signaling system plays a physiological role in acute modulation of alcohol sensitivity in adults, rather than a general response to intoxication by sedative agents. Activation and inhibition of the NPF system reduces and enhances ethanol preference, respectively. Sexual experience, the NPF system activity and ethanol consumption are all linked; sexual deprivation is a major contributor to enhanced ethanol preference.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53537
Sequence Length: 485
Subcellular Location: Membrane
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Q18179 | MGSVNESCDNYVEIFNKINYFFRDDQVINGTEYSPKEFGYFITFAYMLIILFGAIGNFLTIIVVILNPAMRTTRNFFILNLALSDFFVCIVTAPTTLYTVLYMFWPFSRTLCKIAGSLQGFNIFLSTFSIASIAVDRYVLIIFPTKRERQQNLSFCFFIMIWVISLILAVPLLQASDLTPVFVEPSCDLALYICHEQNEIWEKMIISKGTYTLAVLITQYAFPLFSLVFAYSRIAHRMKLRFANRNQNVTTNTNTSQRRRSVVERQRRTHLLLVCVVAVFAVAWLPLNVFHIFNTFELVNSFSVTTFSICHCLAMCSACLNPLIYAFFNHNFRIEFMHLFDRVGLRSLRVVIFGEQESLKKSMRTEFRSRGGCKTVTTAEPATFQRMNESMILSAMEQDEQL | Function: Could be a receptor for neuropeptide Y and peptide YY.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46439
Sequence Length: 402
Subcellular Location: Cell membrane
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Q09638 | MSVAVGIPYVCFFIILSVVGIIGNVIVIYAIAGDRNMRKSVMNILLLNLAVADLANLIFTIPEWIPPVFFGSTDWLFPSFLCPVCRYLECVFLFASISTQMIVCIERYIAIVLPMQARQLCSRRNVLITVLVDWIFVACFASPYAVWHSVKTKDRNTNSLRFKLFQLSATCSNTVGKSTWWQGYKLTEFLAFYFVPCFIITVVYTKVAKCLWCKDPTLQCETRSCLDNKSSSRSSDALRTRRNVVKMLIACVAVYFVCYSPIQVIFLSKAVLNVTIHPPYDFILLMNALAMTCSASNPLLYTLFSQKFRRRLRDVLYCPSDVENETKTYYSINNTSIVGPRASFN | Function: Probable receptor for neuropeptide ligand nlp-8 that plays a role in octopamine signaling and specifically, the octopamine inhibition of aversion responses in olfactory sensory neurons.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39233
Sequence Length: 345
Subcellular Location: Cell membrane
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Q09502 | MSSFYNEAKFLISDGEQMRIDTYAVGRKTMQQSDAFKGTFYENFTLVYALPLSNHDNSSLMLIAGFYALLFMFGTCGNAAILAVVHHVKGQDPRSRHNTTLTYICILSIVDFLSMLPIPMTIIDQILGFWMFDTFACKLFRLLEHIGKIFSTFILVAFSIDRYCAVCHPLQVRVRNQRTVFVFLGIMFFVTCVMLSPILLYAHSKELVMHEKVDLDQEVITRMHLYKCVDDLGRELFVVFTLYSFVLAYLMPLLFMIYFYYEMLIRLFKQANVIKQTLVGRRSGGEEKKLTIPVGHIAIYTLAICSFHFICWTPYWISILYSLYEELYQDTKSTASPPTYAFIYFMYGVHALPYINSASNFILYGLLNRQLHNAPERKYTRNGVGGRQMSHALTTNTRPEYSELIAIPSSSCRPDSRVSAMIHNNNNNTESLPLAQNISNMTNKDSATIVPMPMSANVDGNEIYNWITPDTESVIL | Function: Probable receptor for neuropeptide ligand nlp-9 that plays a role in octopamine signaling and specifically, the octapamine inhibition of aversion responses in olfactory sensory neurons . In AWB olfactory sensory neurons, required for the detection of preferred food sources .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54548
Sequence Length: 476
Subcellular Location: Cell membrane
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P93002 | MDTTIDGFADSYEISSTSFVATDNTDSSIVYLAAEQVLTGPDVSALQLLSNSFESVFDSPDDFYSDAKLVLSDGREVSFHRCVLSARSSFFKSALAAAKKEKDSNNTAAVKLELKEIAKDYEVGFDSVVTVLAYVYSSRVRPPPKGVSECADENCCHVACRPAVDFMLEVLYLAFIFKIPELITLYQRHLLDVVDKVVIEDTLVILKLANICGKACMKLLDRCKEIIVKSNVDMVSLEKSLPEELVKEIIDRRKELGLEVPKVKKHVSNVHKALDSDDIELVKLLLKEDHTNLDDACALHFAVAYCNVKTATDLLKLDLADVNHRNPRGYTVLHVAAMRKEPQLILSLLEKGASASEATLEGRTALMIAKQATMAVECNNIPEQCKHSLKGRLCVEILEQEDKREQIPRDVPPSFAVAADELKMTLLDLENRVALAQRLFPTEAQAAMEIAEMKGTCEFIVTSLEPDRLTGTKRTSPGVKIAPFRILEEHQSRLKALSKTVELGKRFFPRCSAVLDQIMNCEDLTQLACGEDDTAEKRLQKKQRYMEIQETLKKAFSEDNLELGNSSLTDSTSSTSKSTGGKRSNRKLSHRRR | Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Key positive regulator of the SA-dependent signaling pathway that negatively regulates JA-dependent signaling pathway. Mediates the binding of TGA factors to the as-1 motif found in the pathogenesis-related PR-1 gene, leading to the transcriptional regulation of the gene defense. Controls the onset of systemic acquired resistance (SAR). Upon SAR induction, a biphasic change in cellular reduction potential occurs, resulting in reduction of the cytoplasmic oligomeric form to a monomeric form that accumulates in the nucleus and activates gene expression. Phosphorylated form is target of proteasome degradation.
PTM: Phosphorylated at Ser-11 and Ser-15 in the nucleus; facilitates its recruitment to a cullin3-based ubiquitin ligase leading to polyubiquitination and subsequent CUL3/CSN-mediated degradation.
Sequence Mass (Da): 66032
Sequence Length: 593
Domain: The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q18534 | MEVENFTDCQVYWKVYPDPSQSIYAIVPFLTVYLFLFFLGLFGNVTLIYVTCSHKALLSVQNIFILNLAASDCMMCILSLPITPITNVYKNWYFGNLLCHLIPCIQGISIFVCTFSLGAIALDRYILVVRPHSTPLSQRGAFLTTVLLWILSFVVTLPYAFNMQMIEYTEERICGYFCTEKWESAKSRRAYTMIVMLAQFVVPFAVMAFCYANIVSVLSKRAQTKIRKMVERTSALESSCAFPSHGLEQYENELNEFLDKQEKEKQRVVLQNRRTTSILVTMVVWFGITWLPHNVISLIIEYDDTQSFFRLYGRDDYDISYLLNLFTHSIAMSNNVLNPVLYAWLNPSFRQLVIKTYFGDRRKSDRIINQTSVYKTKIVHDTKHLNGRAKIGGGGSHEALKERELNSCSENLSYHVNGHTRTPTPEVQLNEVSSPEISKLVAEPEELIEFSVNDTLV | Function: G-protein coupled receptor for FARP(FMRFamide related peptide) neuropeptides . Activated by FARP neuropeptides flp-18 and flp-21 . Plays a role in modulating social and feeding behavior . Required to modulate locomotion quiescence during the sleep-like state called lethargus, which occurs during molting between larval and adult stages, in part by regulating touch sensitivity .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52464
Sequence Length: 457
Subcellular Location: Membrane
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P22211 | MSSLTRLLQEKRKNETSNSSPRTSADTLTTTPESQSLDLHSRNKSSSHIGSVSNSSSSDRNRANVPVPGSVTTVTQIYSEEDSSSTAGSSLDDRNQFSSSFLNANFAHTASFYGTSAQSRDRFGSLINDQGTAGLSSHGGSFAAQNRITSRLSTTSHTSGRAIPSLSSSIPYSVPNSNKDNNSSNSNSSSLSSSWLETYAGGMPNNISAIDSNVISSPKVDSVEPRFVISKQKLQKASMDSNNANATQSRSISRSGSFSSQLGNFFFSKNSKESSNSNSAGMSFSANSNGPSPNIKNPNVTNGSTPIPKPIRARQSSIYSASRQPTGSYTDNFYGSPSSVHDHLPPSQSVPRSQHSSIGDLKRFFKKSSNSNLSSNSNNVIPNGSPLSSGIAVPSHSHSSSHFAAGNNSYSTSYNGNGDTIYSHSHGGSGIPFSKRYIKTGADLGAGAGGSVKLAQRISDNKIFAVKEFRTKFENESKRDYVKKITSEYCIGTTLNHPNIIETIEIVYENDRILQVMEYCEYDLFAIVMSNKMSYEEICCCFKQILTGVQYLHSIGLAHRDLKLDNCVINEKGIVKLIDFGAAVVFSYPFSKNLVEASGIVGSDPYLAPEVCIFAKYDPRPVDIWSSAIIFACMILKKFPWKIPKLRDNSFKLFCSGRDCDSLSSLVTRTPDPPSYDESHSTEKKKPESSSNNVSDPNNVNIGPQRLLHSLPEETQHIVGRMIDLAPACRGNIEEIMEDPWIRSIDMCHLVEDGLSFKVVRGEDHHHTQVDQSEAHIAGLEKKKKKQNNQ | Function: Nutrient-regulated protein kinase that promotes the activity of at least 6 distinct transport systems for nitrogenous nutrients under conditions of nitrogen catabolite derepression. Under poor nitrogen growth conditions, required for post-Golgi sorting of the general amino acid permease GAP1 and the three known ammonia permeases, MEP1/2/3, to the plasma membrane. Contributes also to the stability and the retention of GAP1 at the plasma membrane. Inversely, promotes the degradation of tryptophan permease TAT2 under the same conditions. Activity is regulated by the TOR signaling pathway via phosphatase SIT4. Although thought to be involved in regulation of GLN3-dependent transcription by nitrogen catabolite repression, this seems to be an indirect effect from the reduced uptake of the nitrogen-repressing compound.
PTM: Hyperphosphorylated in nitrogen-rich growth medium. Nitrogen limitation (or rapamycin treatment) leads to substantial, though not complete dephosphorylation. Autophosphorylation plays only a minor role and seems not to be regulated by the quality of the nitrogen source.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 85990
Sequence Length: 790
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q59E83 | MDEGGGIGSSLLSRITTTASEIMMRNEPTTTENPAVQEMNHIYHLTPSMKMLCILFYSILCVCCVYGNVLVILVIVYFKRLRTATNILILNLAVADLLISVFCIPFSYWQVLIYDDQRWLFGSMMCSLLAFLQAMAVFLSAWTLVVISFDRWMAIMFLLTPNIRITRRRALYLVAATWIFSILMALPLLFTTRFFEDQDGLPNCGENWTYFGDSGEQVRKVYSSMVLILQYVVPQAVLIITYTHIGIKMWNSRVPGMQNGATKKMIVDRHESVKKLVPMVILISALFALCWLPLLILINVIPEFYPDINSWGYILYLWWFAHGLAMSHSMVNPIIYFIRNARFREGFCFFSSKLLPCISFKELRLLTDNTSRSFRNRSRFSGVINPTSSDEKPATSLTRYSRSGVLDRQTCRSARFFEARPLVVVRNNSANSLA | Function: Receptor for the LURY-1-1 and LURY-1-2 peptides which control food-related processes including feeding, lifespan, egg-laying and roaming behavior . Receptor for flp-7 which stimulates serotonin-induced fat loss . Serotonin induces secretion of flp-7 from neurons and binding to npr-22 which leads to induction of the atgp-1 lipase and subsequent fat loss . Acts in vitro as a receptor for the flp-7 FMRFamide-like neuropeptides TPMQRSSMVRF-amide, SPMQRSSMVRF-amide, SPMERSAMVRF-amide and SPMDRSKMVRF-amide . Also acts in vitro as a receptor for a number of other FMRFamide-like neuropeptides including the flp-1 neuropeptide PNFMRY-amide, the flp-9 neuropeptide KPSFVRF-amide, the flp-11 neuropeptides AMRNALVRF-amide, ASGGMRNALVRF-amide and NGAPQPFVRF-amide, the flp-13 neuropeptides AADGAPLIRF-amide, ASPSAPLIRF-amide, SPSAVPLIRF-amide, SAAAPLIRF-amide and ASSAPLIRF-amide, and the flp-22 neuropeptide SPSAKWMRF-amide . The SPMERSAMVRF-amide neuropeptide from flp-7 acts as the strongest in vitro activator of npr-22 .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49751
Sequence Length: 434
Subcellular Location: Cell membrane
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Q03613 | MDFTENEEEYEHWTHIERRVPFQGYRTYVASTYISFNVVGFVINAWVLYVVAPLLFAPAIKVPKSILFYIFALCVGDLMTMIAMLLLVIELVFGTWQFSSMVCTSYLIFDSMNKFMAPMIVFLISRTCYSTVCLDKTRGEKAATLKYAIIQFCIAFAFVMILLWPVFAYSQVFTFYMNPNSTAQEVTVMRKCGFFPPPQIEFWFNLIACITSYAVPLFGIIYWYVSVPFFLKRRALTTLVASSSMDAALRKVITTVLLLTVIYVLCWTPYWVSMFANRIWIMEKKSIIIISYFIHLLPYISCVAYPLIFTLLNRGIRSAHAKIVADQRRRFRSLTDEASSQIRTAIRTIPGTKMKKNEFLTRTEEISSDKIASEAVSEFREGLPSQTSFPDETLL | Function: Not known. Putative receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45549
Sequence Length: 395
Subcellular Location: Cell membrane
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P39923 | MLSYFQGFVPIHTIFYSVFHPTEGSKIKYEFPPNNLKNHGINFNTFKNYIIPKPILCHKLITFKYGTYRIVCYPVTINSPIYARNFFSFNFVFVFPYDCETSPYEPAITRLGKMFKVLEEQNQLLSKSERDPVFFDLKVLENSTTTPSTAGPSSTPNPSSNTTPTHPTSEKDTKDMRSSRYSDLIKDLGLPQSAFSIQDLLMRIFQDLNNYSECLIPIDEGNAVDIKIFPLLRPPTTCVSLEDVPLSSVNLKKIIDVNWDPTMMSIVPYIDGLNSIAKISKLSNSDPGLVIECIRHLIYYKCVTLSDIFQFSNIYAPSSLIRNFLTDPLMASDCQSYVTFPEVSKISNLPLNKSLGSGDQDSPSFSVRRKSKSSSIPSNPDSRTTSFSSTSRVSQNSSLNSSFSSIYKDWRQSQTSCSSSNIHVINNRNRFLPTRSCLFDLYRSLSQGQTLKTWYESKYMILKENNIDIRRFITFGLEKRIIYRCYSFPVMINAGSREPKEMTPIITKDLVNNDKLLEKRNHNHLLSATGSRNTAQSGNLKPERPSKVSFEMQRVSSLATGKSTMPKLSDEEEGILEESIRNAETFDKICVLLSKPKLEVESYLNELGEFKVINS | Function: Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis . Mediates inactivation of the TORC1 complex in response to amino acid starvation . Post-transcriptional regulator of nitrogen permeases . May be involved in putative NPR1-dependent phosphorylation of nitrogen permeases or in the processing and targeting of nitrogen permeases at the level of the endoplasmic reticulum .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69859
Sequence Length: 615
Subcellular Location: Vacuole membrane
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O10440 | MSILISPSDNTGWGLGTGKMYGGARKRSAEHPVHVRSYWRAAWGSRNRRRVATVAAEDAEAPQLEDVAQAPATVPIVRRHRRRVGGSARTRGLRKSARVRAAARAIVRAVNGAAAAAAPTVPASANFAAMVGAIANARAAYRHRRSRAGINPVPASRSTTRVRLPRTVRFHPSMGAFHRRWWRIHTRGRRKASVRRRRT | Function: Plays a role in the inhibition of host immune response within the nucleus. Interacts with cellular nucleosomes and immobilizes the host immune danger signal HMGB1 on chromatin. In turn, prevents HMGB1 release out of the cell and thus decreases inflammation. Also plays a role in the wrapping and condensation of the viral DNA. May also promote viral genome import into the nucleus.
PTM: Cleaved near the N-terminus by the viral protease during virion maturation to form the mature protein.
Sequence Mass (Da): 21927
Sequence Length: 199
Subcellular Location: Virion
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Q8JN70 | MPILISPSDNTGWGLGKLRIRATGLTFTDSTPVSVRHYFRDSGGQRNGRATRAHLRRNLKKYRRKHDRRTHTRRVQPDVILIKAGRRTARSARRRSARKSRSEKTGPRIRYTRRI | Function: Plays a role in the inhibition of host immune response within the nucleus. Interacts with cellular nucleosomes and immobilizes the host immune danger signal HMGB1 on chromatin. In turn, prevents HMGB1 release out of the cell and thus decreases inflammation. Also plays a role in the wrapping and condensation of the viral DNA. May also promote viral genome import into the nucleus.
PTM: Cleaved near the N-terminus by the viral protease during virion maturation to form the mature protein.
Sequence Mass (Da): 13459
Sequence Length: 115
Subcellular Location: Virion
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O76745 | MKLLLSAGAALAFVLGLCAAGSPPAQLSVHTVSWNSGHERAPTNLEELLGLNSGETPDVIAVAVQGFGFQTDKPQQGPACVKNFQSLLTSKGYTKLKNTITETMGLTVYCLEKHLDQNTLKNETIIVTVDDQKKSGGIVTSFTIYNKRFSFTTSRMSDEDVTSTNTKYAYDTRLDYSKKDDPSDFLFWIGDLNVRVETNATHAKSLVDQNNIDGLMAFDQLKKAKEQKLFDGWTEPQVTFKPTYKFKPNTDEYDLSATPSWTDRALYKSGTGKTIQPLSYNSLTNYKQTEHRPVLAKFRVTL | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Heme-based protein that delivers nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation (Probable). In place of heme, the heme-binding cysteine can also reversibly bind NO when it is present in high concentrations .
PTM: The N-terminus is blocked.
Sequence Mass (Da): 33624
Sequence Length: 302
Subcellular Location: Secreted
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P29922 | MMTFAFYLFAISACVAGFMVVIGRNPVHSVLWLILAFLSAAGLFVLQGAEFVAMLLVVVYVGAVAVLFLFVVMMLDVDFAELKGELARYLPLALVIGVVLLAQLGIAFSGWTPSDQAESLRAAPVDAAVENTLGLGLVLYDRYVLMFQLAGLVLLVAMIGAIVLTMRHRKDVKRQNVLEQMWRDPAKTMELKDVKPGQGL | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21819
Sequence Length: 200
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q56225 | MSLLEGLALFLLLLSGVLVVTLRNAIHAALALILNFLVLAGVYVALDARFLGFIQVIVYAGAIVVLFLFVIMLLFAAQGEIGFDPLVRSRPLAALLALGVAGILAAGLWGLDLAFTQDLKGGLPQALGPLLYGDWLFVLLAVGFLLMAATVVAVALVEPGKASRAKEAEKREEVAR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18551
Sequence Length: 176
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q56226 | MSYLLTSALLFALGVYGVLTRRTAILVFLSIELMLNAANLSLVGFARAYGLDGQVAALMVIAVAAAEVAVGLGLIVAIFRHRESTAVDDLSELRG | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9996
Sequence Length: 95
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q56227 | MALLGTILLPLLGFALLGLFGKRMREPLPGVLASGLVLASFLLGAGLLLSGGARFQAEWLPGIPFSLLLDNLSGFMLLIVTGVGFLIHVYAIGYMGGDPGYSRFFAYFNLFIAMMLTLVLADSYPVMFIGWEGVGLASFLLIGFWYKNPQYADSARKAFIVNRIGDLGFMLGMAILWALYGTLSISELKEAMEGPLKNPDLLALAGLLLFLGAVGKSAQIPLMVWLPDAMAGPTPVSALIHAATMVTAGVYLIARSSFLYSVLPDVSYAIAVVGLLTAAYGALSAFGQTDIKKIVAYSTISQLGYMFLAAGVGAYWVALFHVFTHAFFKALLFLASGSVIHALGGEQDVRKMGGLWKHLPQTRWHALIGALALGGLPLLSGFWSKDAILAATLTYPFGGVGFYVGALLVAVLTAMYAMRWFVLVFLGEERGHHHPHEAPPVMLWPNHLLALGSVLAGYLALPHPLPNVLEPFLKPALAEVEAHHLSLGAEWGLIALSAAVALLGLWAGFVFFQRKVFPAWYLAFEAASREAFYVDRAYNALIVNPLKALAEALFYGDRGLLSGYFGLGGAARSLGQGLARLQTGYLRVYALLFVLGALLLLGVMRW | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65141
Sequence Length: 606
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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P29925 | MTNLLSIITFLPIVAAIIMALFLRGQDEAAARNAKWLALLTTTATFVISLFVLFRFDPANTGFQFVEDHAWIMGVCYKMGVDGISVLFVLLTTFMMPLTILSTWQVQDKVKEYMIAFLVLEGLMIGVFTALDLVLFYLFFEAGLIPMFLIIGIWGGKDRIYASFKFFLYTFLGSVLMLVAMIAMYRMAGTTDIPTLLTFDFPSENFRLLGMTVVGGMQMLLFLAFFASFAVKMPMWPVHTWLPDAHVQAPTAGSVLLAAVLLKMGGYGFLRFSLPMFPVASGVAQPYVFWLSAIAIVYTSLVALAQSDMKKVIAYSSVAHMGYVTMGVFAANQIGVDGAIFQMLSHGFISGALFLCVGVIYDRMHTREIDAYGGLVNRMPAYAAVFMFFTMANVGLPGTSGFVGEFLTLMGVFRVDTWVALVATSGVILSAAYALWLYRRVTLGQLIKESLKSITDMTPRERWVFIPLIAMTLILGVYPRLVTDVTGPAVAALVQDYNQSQPAAPVATAQASH | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56417
Sequence Length: 513
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q56228 | MVVLAVLLPVVFGALLLLGLPRALGVLGAGLSFLLNLYLFLTHPGGVAHAFQAPLLPGAGVYWAFGLDGLSALFFLTIALTVFLGALVARVEGRFLGLALLMEGLLLGLFAARDLLVFYVFFEAALIPALLMLYLYGGEGRTRALYTFVLFTLVGSLPMLAAVLGARLLSGSPTFLLEDLLAHPLQEEAAFWVFLGFALAFAIKTPLFPLHAWLPPFHQENHPSGLADALGTLYKVGVFAFFRFAIPLAPEGFAQAQGLLLFLAALSALYGAWVAFAAKDFKTLLAYAGLSHMGVAALGVFSGTPEGAMGGLYLLAASGVYTGGLFLLAGRLYERTGTLEIGRYRGLAQSAPGLAALALILFLAMVGLPGLSGFPGEFLTLLGAYKASPWLAALAFLSVIASAAYALTAFQKTFWEEGGSGVKDLAGAEWGFALLSVLALLLMGVFPGYFARGLHPLAEAFAKLLGGGA | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49219
Sequence Length: 469
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q56229 | MTLAILAVFSVALTLLGFVLPPQGVKRATLLGLALALASLLLTWGKPFAFGPYAVDGVSQVFTLLALLGALWTVGLVRSGRFEFYLLVLYAALGMHLLASTRHLLLMLVALEALSLPLYALATWRRGQGLEAALKYFLLGALAAAFFLYGAALFYGATGSLVLGAPGEGPLYALALGLLLVGLGFKAALAPFHFWTPDVYQGSPTPVVLFMATSVKAAAFAALLRVAAPPEALALLVALSVVVGNLAALAQKEAKRLLAYSSIAHAGYMALALYTGNAQALGFYLLTYVLATGLAFAVLSQISPDRVPLEALRGLYRKDPLLGLAFLVAMLSLLGLPPLAGFWGKYLAFAEAARAGAWGVLVLALVTSAVSAYYYLGLGLAVFARPEETPFRPGPPWARAAVVAAGVLLLALGLLPGLVLPALAAGG | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44436
Sequence Length: 427
Subcellular Location: Cell inner membrane
EC: 7.1.1.-
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Q5SKZ7 | MSASSERELYEAWVELLSWMREYAQAKGVRFEKEADFPDFIYRMERPYDLPTTIMTASLSDGLGEPFLLADVSPRHAKLKRIGLRLPRAHIHLHAHYEPGKGLVTGKIPLTKERFFALADRAREALAFA | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. The Nqo15 subunit has probably a role in complex stabilization, and may be also involved in the storage of iron for iron-sulfur cluster regeneration in the complex.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14788
Sequence Length: 129
Domain: Has a similar fold to the mitochondrial iron chaperone frataxin.
Subcellular Location: Cell membrane
EC: 7.1.1.-
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P15559 | MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVFIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKKEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK | Function: Flavin-containing quinone reductase that catalyzes two-electron reduction of quinones to hydroquinones using either NADH or NADPH as electron donors. In a ping-pong kinetic mechanism, the electrons are sequentially transferred from NAD(P)H to flavin cofactor and then from reduced flavin to the quinone, bypassing the formation of semiquinone and reactive oxygen species (By similarity). Regulates cellular redox state primarily through quinone detoxification. Reduces components of plasma membrane redox system such as coenzyme Q and vitamin quinones, producing antioxidant hydroquinone forms. In the process may function as superoxide scavenger to prevent hydroquinone oxidation and facilitate excretion . Alternatively, can activate quinones and their derivatives by generating redox reactive hydroquinones with DNA cross-linking antitumor potential . Acts as a gatekeeper of the core 20S proteasome known to degrade proteins with unstructured regions. Upon oxidative stress, interacts with tumor suppressors TP53 and TP73 in a NADH-dependent way and inhibits their ubiquitin-independent degradation by the 20S proteasome .
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 30868
Sequence Length: 274
Subcellular Location: Cytoplasm
EC: 1.6.5.2
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Q941Z0 | MEAAAARPVIRVAAICGSLRKASYNGGLLRAAAGVCEESIPGLRVDHVDISGLPLLNTDLETADGGFPPAVEAFRDKVRQADCFLFGSPEYNYSIATPLKNALDWASRGQNCWADKPAAIVSAGGGFGGGRSQYHLRQVGVFLDLHFINKPELAVKAFEQPPKFDSDGNLIDAQIRERIKQVLLSLQAFTLRLQKKD | Function: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 21324
Sequence Length: 197
EC: 1.6.5.2
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Q941Y8 | MEGSTSPKALRVAAISGSLRRGSANTGLIRAAKEICEESIPGMVIDHVDIPDLPLLNTDMEVDDGFPPAVEAFRASVRAADCFLFASPEYNYSISGPLKNALDWGSRPPNCWADRAAAIVSASGGSGGSRSMYHIRQVGVFLDIHFINKPEVFIKAHQPPKKFDSDGNLIDPEIKEELKDMLLSLQAFALRLQGKPANSKHAA | Function: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 21916
Sequence Length: 203
EC: 1.6.5.2
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Q8EHV6 | MSDAKELKQVLTGPIVNNNPIALQVLGVCSALAVTSKLETALVMALALTAVTAFSNLFISMIRNHIPSSVRIIVQMTIIASLVIVVDQLLQAYAYQISKQLSVFVGLIITNCIVMGRAEAYAMKTPPMMSFMDGIGNGLGYGAILLAVGFVRELFGNGSLFGVQILHKISDGGWYQPNGLLLLPPSAFFLIGMLIWIIRTYKPEQVEAKG | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22645
Sequence Length: 210
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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Q9LK88 | MEAVTAIKPLIRVAALSGSLRKTSFHTGLLRAAIDLTKESVPGLQIEYIDISPLPLINTDLEVNGTYPPVVEAFRQKILEADSILFASPEYNFSVSAPLKNALDWASRPPNVWADKPAAIISTGGGFGGGRSQYHLRQIGVFLDLHFINKPEFTLNAFQPPQKFDAEGNLVDEVTKERLKQVLLSLQAFTLRLQGK | Function: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 21556
Sequence Length: 196
Subcellular Location: Cell membrane
EC: 1.6.5.2
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P51843 | MAGENHQWQGSILYNMLMSAKQTRAAPEAPETRLVDQCWGCSCGDEPGVGREGLLGGRNVALLYRCCFCGKDHPRQGSILYSMLTSAKQTYAAPKAPEATLGPCWGCSCGSDPGVGRAGLPGGRPVALLYRCCFCGEDHPRQGSILYSLLTSSKQTHVAPAAPEARPGGAWWDRSYFAQRPGGKEALPGGRATALLYRCCFCGEDHPQQGSTLYCVPTSTNQAQAAPEERPRAPWWDTSSGALRPVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRNCWASLLMLELAQDRLQFETVEVSEPSMLQKILTTRRRETGGNEPLPVPTLQHHLAPPAEARKVPSASQVQAIKCFLSKCWSLNISTKEYAYLKGTVLFNPDVPGLQCVKYIQGLQWGTQQILSEHTRMTHQGPHDRFIELNSTLFLLRFINANVIAELFFRPIIGTVSMDDMMLEMLCTKI | Function: Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency (By similarity).
Sequence Mass (Da): 51718
Sequence Length: 470
Domain: Homodimerization involved an interaction between amino and carboxy termini involving LXXLL motifs and steroid binding domain (AF-2 motif). Heterodimerizes with NR5A1 and NROB2 through its N-terminal LXXLL motifs.
Subcellular Location: Nucleus
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P79386 | MAGEDHQWQGSILYNMLMSAKQTHATREAPEARLRGSCWGCSCGSEPPVGREGQPGGPAVALLYRCCFCGEDHPRQGSILYNMLTSAKQTQETPEAPEARLGGACWGCSCGSEPRVGREELPGGRATVLLYRCCFCGEEHPRQGSILYSLLTSAKQTHVALEAPEARPGGAWWDRSYCAQRLGAREELPGGRPVTLPYRCCFCGEDHPRQSGILCNMPMSAKQTHVAPEAQPGAPWWDPSCAAQRVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRSCWAPLLMLELAQDRLNFETVETLEPSLLQMILTTRRQETEGDEPPSPQPPVQPHLVLPSEAEHLPSVAEVQAIKGFLAKCWSLDISTKEYAYLKGTVLFNPDLPGLQCVKYIQGLQWGTQQILSEHIRMTHRGYQARFAELNSALFLLRFINANVLAELFFRPIIGTVSMDDMMLEMLCAKL | Function: Orphan nuclear receptor. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis. Acts as a coregulatory protein that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency (By similarity).
Sequence Mass (Da): 52128
Sequence Length: 471
Domain: Homodimerization involved an interaction between amino and carboxy termini involving LXXLL motifs and steroid binding domain (AF-2 motif). Heterodimerizes with NR5A1 and NROB2 through its N-terminal LXXLL motifs (By similarity).
Subcellular Location: Nucleus
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Q15466 | MSTSQPGACPCQGAASRPAILYALLSSSLKAVPRPRSRCLCRQHRPVQLCAPHRTCREALDVLAKTVAFLRNLPSFWQLPPQDQRRLLQGCWGPLFLLGLAQDAVTFEVAEAPVPSILKKILLEEPSSSGGSGQLPDRPQPSLAAVQWLQCCLESFWSLELSPKEYACLKGTILFNPDVPGLQAASHIGHLQQEAHWVLCEVLEPWCPAAQGRLTRVLLTASTLKSIPTSLLGDLFFRPIIGDVDIAGLLGDMLLLR | Function: Transcriptional regulator that acts as a negative regulator of receptor-dependent signaling pathways (By similarity). Specifically inhibits transactivation of the nuclear receptor with which it interacts (By similarity). Inhibits transcriptional activity of NEUROD1 on E-box-containing promoter by interfering with the coactivation function of the p300/CBP-mediated transcription complex for NEUROD1 . Essential component of the liver circadian clock which via its interaction with NR1D1 and RORG regulates NPAS2-mediated hepatic lipid metabolism (By similarity). Regulates the circadian expression of cytochrome P450 (CYP) enzymes (By similarity). Represses: NR5A2 and HNF4A to down-regulate CYP2C38, NFLI3 to up-regulate CYP2A5, BHLHE41/HNF1A axis to up-regulate CYP1A2, CYP2E1 and CYP3A11, and NR1D1 to up-regulate CYP2B10, CYP4A10 and CYP4A14 (By similarity).
PTM: Arginine methylation by PRMT5 enhances repression activity of metabolic genes in liver in response to bile acid signaling, by increasing interaction with cofactors.
Sequence Mass (Da): 28058
Sequence Length: 257
Subcellular Location: Nucleus
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Q90ZN1 | MPGSLKEETALLLEDYFQHRAGGAALPPSATAAELRRAAAELERRERPFFRSCAPLARAEPREAAALLRKVAAQLEAEGGLNWGRLLALVVFTGTLAAALAESGCEEGPSRLAAALAAYLAEEQGEWLEEHGGWDGFCRFFGRHGSQPADQNSTLSNAIMAAAGFGIAGLAFLLVVR | Function: Shows anti-apoptotic properties. Counteract the pro-apoptotic activity of BAX.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18778
Sequence Length: 177
Subcellular Location: Cell membrane
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A1XQX1 | MLRLWPGGAPGGLASILLRISLRLALWLPPLTLGSALAEGPGELYVPQHMPHHLVPAARSHAPLRAGHAGTTYIFGRDGGLIVYTWPPNDRPSTRADRLAVGFSTQQKDAVLVRVDSSSGLGDYLQLQIERGNIKVVFNVGTDDINIEETSKFVNDGKYHIVRFTRSGGNATLQVDDLPVIERYPSGNIDNERLAIARQRIPYRLGRVVDDWLLDKGRQLTIFNSQTTIKIGGWEKGSRPFQGQLSGLYYNGLKVLNMAAEGDPNVRVEGSARLVGDMPSSSITPQSSVSAAGNRSETSPSITDITTTTASNRQGKQTTTPQDDLLVASAECPSDDEDIDPCDPSSGGLAHPPLPEAKGYPSPEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYHVDESRNYISNSATQPNGAAVKEKPIGVPKNKKDKKNKDKEYYV | Function: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May play a role in formation or maintenance of synaptic junctions.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48706
Sequence Length: 449
Subcellular Location: Membrane
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A1XQX3 | MFGGWRLVVWQIFSEIITRRLGFWICLYFAALSVGMISGSEPLVRTRHIQNTHTVPINRSPGSLRAWQAGSTYVFGRQGGVITYSWPPHDRPSTRVDRLALGFSTLMEDATLVRVDSSAGLGDYLKLHIVKGNVVAVFNVGTYDINIEEKAKLVNDGNYHIVRFTRSGGNATLQVDDLPVIERFPPGHIDSHRLGTGRLPYRRLVEESLPKNGRQLTIFNSQMTIRIGGWQKQQVSGFQGQMSGFYYNGLKVFSMAADGDPNVRMEGSVRLVGELQSSSTPHGGATVYQSSVTEISSTTSNTITITYSTPADEQQTTDELLVASAECPSDDEDIDPCEPSSGTLCCFVPPAGPTGPAISSFPGPAEVFRESNGTTGMVVGIVAGAALCILILLYAMYKYRNRDEGSYHVDESRNYICNSNGAALKEKNTADDDSGSKSKKNKNKEYYV | Function: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May play a role in formation or maintenance of synaptic junctions.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 49054
Sequence Length: 448
Subcellular Location: Membrane
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Q08E02 | MTTLDSNNNTGGVITYIGSSGSSPNRTSPESLYSDSSNGSFQSLTQGCPTYFPPSPTGSLTQDPARSFGSIPPSLGDDGSPSSSSSSSSSSSSSFYNGSPPGGLQVALEDSNRVSPSKSTSNITKLNGMVLLCKVCGDVASGFHYGVHACEGCKGFFRRSIQQNIQYKRCLKNENCSIVRINRNRCQQCRFKKCLSVGMSRDAVRFGRIPKREKQRMLAEMQSAMNLANNQLSSQCPLETPPTQHPTPGPMGPSPPPAPAPSPLVGFSQFPQQLTPPRSPSPEPTVEDVISQVARAHREIFTYAHDKLGTSPGNFNANHASGNRPATTPHRWESQGCPPANDNIMAAQRHNEALNSLRQASSSYPPPWPPGAAHHSCHQPNSNGHRLCPTHVYPAPEGEAPVNSPRQGNSKNILLACPMNMYPHGRSGRTVQEIWEDFSMSFTPAVREVVEFAKHIPGFRDLSQHDQVTLLKAGTFEVLMVRFASLFNVKDQTVMFLSRTTYSLQELGAMGMGDLLNAMFDFSEKLNSLALTEEELGLFTAVVLVSADRSGMENSASVEQLQETLLRALRALVLKNRPSETSRFTKLLLKLPDLRTLNNMHSEKLLSFRVDAQ | Function: Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core clock components BMAL1, CLOCK and CRY1. Also regulates genes involved in metabolic functions, including lipid and bile acid metabolism, adipogenesis, gluconeogenesis and the macrophage inflammatory response. Acts as a receptor for heme which stimulates its interaction with the NCOR1/HDAC3 corepressor complex, enhancing transcriptional repression. Recognizes two classes of DNA response elements within the promoter of its target genes and can bind to DNA as either monomers or homodimers, depending on the nature of the response element. Binds as a monomer to a response element composed of the consensus half-site motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence (RevRE), or as a homodimer to a direct repeat of the core motif spaced by two nucleotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and regulates the levels of its ligand heme by repressing the expression of PPARGC1A, a potent inducer of heme synthesis. Regulates lipid metabolism by repressing the expression of APOC3 and by influencing the activity of sterol response element binding proteins (SREBPs); represses INSIG2 which interferes with the proteolytic activation of SREBPs which in turn govern the rhythmic expression of enzymes with key functions in sterol and fatty acid synthesis. Regulates gluconeogenesis via repression of G6PC1 and PEPCK and adipocyte differentiation via repression of PPARG. Regulates glucagon release in pancreatic alpha-cells via the AMPK-NAMPT-SIRT1 pathway and the proliferation, glucose-induced insulin secretion and expression of key lipogenic genes in pancreatic-beta cells. Positively regulates bile acid synthesis by increasing hepatic expression of CYP7A1 via repression of NR0B2 and NFIL3 which are negative regulators of CYP7A1. Modulates skeletal muscle oxidative capacity by regulating mitochondrial biogenesis and autophagy; controls mitochondrial biogenesis and respiration by interfering with the STK11-PRKAA1/2-SIRT1-PPARGC1A signaling pathway. Represses the expression of SERPINE1/PAI1, an important modulator of cardiovascular disease and the expression of inflammatory cytokines and chemokines in macrophages. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). Plays a role in the circadian regulation of body temperature and negatively regulates thermogenic transcriptional programs in brown adipose tissue (BAT); imposes a circadian oscillation in BAT activity, increasing body temperature when awake and depressing thermogenesis during sleep. In concert with NR2E3, regulates transcriptional networks critical for photoreceptor development and function. In addition to its activity as a repressor, can also act as a transcriptional activator. In the ovarian granulosa cells acts as a transcriptional activator of STAR which plays a role in steroid biosynthesis. In collaboration with SP1, activates GJA1 transcription in a heme-independent manner (By similarity). Represses the transcription of CYP2B10, CYP4A10 and CYP4A14 (By similarity). Represses the transcription of CES2 (By similarity). Represses and regulates the circadian expression of TSHB in a NCOR1-dependent manner (By similarity). Negatively regulates the protein stability of NR3C1 and influences the time-dependent subcellular distribution of NR3C1, thereby affecting its transcriptional regulatory activity (By similarity). Plays a critical role in the circadian control of neutrophilic inflammation in the lung; under resting, non-stress conditions, acts as a rhythmic repressor to limit inflammatory activity whereas in the presence of inflammatory triggers undergoes ubiquitin-mediated degradation thereby relieving inhibition of the inflammatory response (By similarity). Plays a key role in the circadian regulation of microglial activation and neuroinflammation; suppresses microglial activation through the NF-kappaB pathway in the central nervous system (By similarity). Plays a role in the regulation of the diurnal rhythms of lipid and protein metabolism in the skeletal muscle via transcriptional repression of genes controlling lipid and amino acid metabolism in the muscle (By similarity).
PTM: Ubiquitinated, leading to its proteasomal degradation (By similarity). Ubiquitinated by the SCF(FBXW7) complex when phosphorylated by CDK1 leading to its proteasomal degradation (By similarity). Ubiquitinated by SIAH2; leading to its proteasomal degradation (By similarity). Rapidly ubiquitinated in response to inflammatory triggers and sumoylation is a prerequisite to its ubiquitination (By similarity).
Sequence Mass (Da): 66785
Sequence Length: 613
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Subcellular Location: Nucleus
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Q8WWG1 | MPTDHEEPCGPSHKSFCLNGGLCYVIPTIPSPFCRCVENYTGARCEEVFLPGSSIQTKSNLFEAFVALAVLVTLIIGAFYFLCRKGHFQRASSVQYDINLVETSSTSAHHSHEQH | Function: Low affinity ligand for the ERBB4 tyrosine kinase receptor. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. Does not bind to the ERBB1, ERBB2 and ERBB3 receptors (By similarity).
PTM: Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 12722
Sequence Length: 115
Domain: The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization (By similarity).
Subcellular Location: Cell membrane
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Q9WTX4 | MPTDHEQPCGPRHRSFCLNGGICYVIPTIPSPFCRCIENYTGARCEEVFLPSSSIPSESNLSAAFVVLAVLLTLTIAALCFLCRKGHLQRASSVQCEISLVETNNTRTRHSHREH | Function: Low affinity ligand for the ERBB4 tyrosine kinase receptor. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. Does not bind to the ERBB1, ERBB2 and ERBB3 receptors.
PTM: Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 12744
Sequence Length: 115
Domain: The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization (By similarity).
Subcellular Location: Cell membrane
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Q07428 | MSGQMFKVEIVTRPANFEKLKQELGKIGVTSLTFSNVHGCGLQKAHTELYRGVKIESNVYERLKIEIVVSKVPVDQVTETAKRVLKTGSPGDGKIFVYEISNTINIRTGEEGPEAL | Function: Required for full induction of the nrgAB operon under conditions of ammonium limitation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12822
Sequence Length: 116
Subcellular Location: Cell membrane
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P0DV45 | MLNKSAALVPVVLAFLFLFLCFQCLYADIRCLTGKDGAVHLEMEAKPLTIEPRPGVFFDAWGYCLKGDVPTVPGPVIKVREGTKVKILFRNKLTVPASIHPHGVKYTTANVGVNIAGNPASIVAPGDSRIFEWDTAGTPGTWFYHSYVFERGGEEGLSRGLWGALIVEPVGGDPNPPDKEFVVFMHAFNVNGQEYYAFNNKSGDIELMRGDSSAFPGETWKAKMGDKVRFHLINITEEAHTFHTHGHRWLDKSCDKLIDTIGLNPFDSYVLDFVAGEGVGKGNWAFHCQSQEHMMNGMFGIFMVEEGKRVNAVIASCDEGRKTLSAPGQDRQPPTLEGFSGAYMYPEITEKNMYESFAGLEKGDGIWGDYYSPIPLYTYFNPSRHYVPPESDAYTNLLVKYRPDQCVECHEETTPGIVAEWKMSNHANPKKNPHVSAETQEIEALIGKELNNWRPGTKDGVYCSYCHGSDHEKLFMPTVDNSCGACHPKQAAEFIKGRDHGRPNHPQSWEGNVSTPWYAEYYRRGEGYSMVGCDQCHQNMSSCDDCHSRHRFSAAEARRPEACSICHMGPDHPDWESYSRSKWGVIYETTKERWNWDKNLAEVIPGEDYLAPTCQYCHMYVGNNKWEMNVETKGIWRMGVIPPKEVEFKSGLKDFPYGIKIPPMDKKLEIYSAESQEKRRKWVELCSKCHSSRFAGMWLDSLDQYMFESWRRIDEAQLIIEKLFSENAIEPPPEKRPPFPLSDLIIKVLGAEKLGAEMYRLFKQTNGHLPVIGPILGAYSIFTQNEGNPGGIEREYAEMWFWSHLQGYKGAAHAQPDISWWWGTAQGVGNLTRIRDEAEKLRRLKSGSSSGF | Cofactor: Binds 8 heme groups per subunit.
Function: A nitrite reductase-hydroxylamine oxidoreductase protein that probably functions in the type 1 encapsulin nanocompartment. Probably involved in reductive catalysis. Targeted to the encapsulin nanocompartment by association with the diheme domain of the encapsulin shell protein (AC Q1Q6L7) (Probable). Catalyzes the reduction of nitrite to nitric oxide (NO) (By similarity). Catalyzes the oxidation of hydroxylamine to nitrite (By similarity).
Catalytic Activity: 4 Fe(III)-[cytochrome c] + H2O + hydroxylamine = 4 Fe(II)-[cytochrome c] + 5 H(+) + nitrite
Sequence Mass (Da): 96352
Sequence Length: 852
Subcellular Location: Encapsulin nanocompartment
EC: 1.7.2.1
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Q923B3 | MASTLPTTWPHESVKFEDVSLTFTEEEWAQLDFQQKCLYREIMMENYSNMISVEHHFSKPNVISQLEKAEDCWPMQREIPQDTLPECSWPSPDPGMNSFPSKSPLMKIEVVEVLTLNKDVAGPRNALIQSLYPEDLNPGNLKPAQQPSKRLTDTEASRQKFRHFQYEESAGPQKAMSQLRKLCHQWLQPNTRSKKQILELLVLEQFLNALPEKFRVWVESQHPEDCKAVVALLENMTSVSKDDASLACSSEATDQLKEKRKGVATLPVTFAAEVPAEEPVTFQDVAVDFNEEEWRLLGPTQKTEYHDVMLETLGNLVSVGWEPTLGNRELTPDSPIPVVKPIHDPNTNDLSRNGTQSTVFESILEDGVKEMHSIESNQVGNLQEKGHPQKKFSESSKSQDQTSRHKSQGSLNEVLPRKYVKVKQKGTGKRKGRTNTISMTRGLRIRKQQKDSVEWQGRSGSTPVTHGSSIKKQQQGSEQGKPGTSRDPITLTVPAKVYQKATGSEESIFMDSSDAMVPDVPPKIHQKGPEWHKVGESNNSMLQGSSVQNHQMESGAGRASDNSLLTHALPVKSHQKGYKEGNVQGNRNSWKHIKPHQKGSKGERVEELSTSEKHVPYVKNHLKTSERGKDREINASIKCDPYIKTYYRGSDVGRLRRANNCRKAFSLHAQQISFIKIHKGSQVCRCSECGKLFRNARYFSVHKKIHTGERPYMCMACGKAFVQSSSLTQHLRIHSGERPFECSECGRTFNDRSAISQHLRTHTGAKPYHCERCGKAFRQSSHLTRHERTHTGERPYVCIKCGKAFTQSSHLIGHQKTHGIKFKKQPKL | Function: Transcription regulator involved in NGFR/p75(NTR)-mediated apoptosis. Essential component of the NGFR/p75(NTR) apoptotic pathway: upon ligand-binding and subsequent cleavage of NGFR/p75(NTR), binds to the intracellular domain (ICD) cleavage product of NGFR/p75(NTR), translocates to the nucleus and induces apoptosis, possibly by regulating expression of key regulators of apoptosis. Induces NGFR/p75(NTR)-mediated apoptosis in retina and sympathetic neurons. May also regulate expression of neuronal cholesterol biosynthesis genes. Probably acts as a transcription repressor: specifically binds to the 3'-end of zinc-finger coding genes and recruiting chromatin-modifying proteins such as SETDB1 and TRIM28/KAP1, leading to transcription repression.
PTM: Ubiquitinated by TRAF6 at Lys-15 through 'Lys-63'-linked polyubiquitination. 'Lys-63'-linked polyubiquitination occurs in response to NGFR/p75(NTR) cleavage by gamma-secretase and promotes binding with the ICD cleavage product of NGFR/p75(NTR), followed by translocation into the nucleus and subsequent apoptosis.
Sequence Mass (Da): 93650
Sequence Length: 828
Subcellular Location: Cytoplasm
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P62511 | MTSQLAGFKGTRGTLLVGIGGCSSSGKSTIAKLAVQVLEDAVLVHQDDFYRHDDEVPFDEEYQIGNWDVPEALDMAQFERELDHIRATGRPAAKLVHNGNIDDVGKFGISEEYLEELRRRYRGRISQPVVLVDGFMLYHDDKVAARFDCRLLVRAPYATMKARRASRGGYKTLDSFWQDPPFYFDKFVYKSYAATHARLFRNCDVEDRLVAPDVQEIYNGDEAQITCVLEQVLDAIAAAQC | Function: Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN).
Catalytic Activity: ATP + beta-nicotinamide D-riboside = ADP + beta-nicotinamide D-ribonucleotide + H(+)
Sequence Mass (Da): 27239
Sequence Length: 241
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis.
EC: 2.7.1.22
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Q63376 | MPPGGSGQGGCPRRPPALAGPLPPPPPPPPLPLLLGLLLLLGAAEGARVSSSLSTTHHVHHFHSKHGTVPIAINRMPFLTRSGHAGTTYIFGKGGALITYTWPPNDRPSTRMDRLAVGFSTHQRSAVLVRVDSASGLGDYLQLHIDQGTVGVIFNVGTDDITIDEPNAIVSDGKYHVVRFTRSGGNATLQVDSWPVNERYPAGNFDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQAAIKIGGRDQGRPFQGQVSGLYYNGLKVLALAAESDPNVRTEGHLRLVGEGPSVLLSAETTATTLLADMATTIMETTTTMATTTTRRGRSPTMRDSTTQNTDDLLVASAECPSDDEDLEECEPSTGGELILPIITEDSLDPPPVATRSPFVPPPPTFYPFLTGVGATQDTLPPPAARRPSSGGPCQAERDDSDCEEPVEASGFASGEVFDSSLPPTDDEDFYTTFPLVTDRTTLLSPRKPAPRPNLRTDGATGAPGVLLAPSAPAPNLPAGKMNHRDPLQPLLENPPLGPGVPTAFEPRRPPPLRPGVTSVPGFPRLPTANPTGPGERGPPGAVEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDQSRNYISNSAQSNGAVVKEKAPAAPKTPSKAKKNKDKEYYV | Function: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion.
PTM: O-glycosylated; contains heparan sulfate. Heparan sulfate attachment is required for synapse development by mediating interactions with neuroligins.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70547
Sequence Length: 662
Subcellular Location: Presynaptic cell membrane
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Q0JIL1 | MGREPEMEEARENGGVGGSVLPLASLISPTGNEVQISELEGKIIGLYFAANWYPKCEAFTPALTAAYHQLKEHGAGFEVIFVSCDENRPSFERFHRAMPWPAVPFGDIGCKKRLSERFQVEGIPRLVVLAPNGEVVQPDAVELVHRYGDRAFPFTSARVAELEADEQRKFASQTLEKIFSVSGKDYVNGSQEQVPISSLVGKTVGLYFSAHRCAPCIKFTAKLAAIYSNLKGKAEDFEIIYIPMDKEEDGYLRSCSDMPWLALPYDDGASSGALARYFDVREIPTLVVVGPDGKTVTREGRNLVNLYFDMAFPFTDEQIRLLQEMEDEDAKGYPPSLRHTGHRHELSIVSDKSGGGPYICCECDEQGLGWAYQCIACGYEIHLRCGRDMEGRAE | Function: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions.
Catalytic Activity: [protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH
Sequence Mass (Da): 43776
Sequence Length: 394
EC: 1.8.1.8
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Q28143 | MHLRIHARRNPPRRPAWTLGIWSLFWGCIVSSVWSSSNVASSSSSPGSHSQHEHHFHGSKHHSVPISIYRSPVSLRGGHAGATYIFGKSGGLILYTWPANDRPSTRSDRLAVGFSTTVKDGILVRIDSAPGLGDFLQLHIEQGKIGVVFNIGTVDISIKEERTPVNDGKYHVVRFTRNGGNATLQVDNWPVNEHYPTGNTDNERFQMVKQKIPFKYNRPVEEWLQEKGRQLTIFNTQAQIAIGGKDKGRLFQGQLSGLYYDGLKVLNMAAENNPNIKINGSVRLVGEVPSILGTTQTTSMPPEMSTTVMETTTTMATTTTRKNRSTASIQPTSDDLVSSAECSSDDEDFVECEPSTANPTEPGVRRVPGASEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDETRNYISNSAQSNGTLLKEKPPSSKGGHKKQKNKDKEYYV | Function: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling (By similarity).
PTM: Proccessed by alpha-secretase leading to the formation of an extracellular soluble protein as well as a C-terminal membrane-embedded fragment (CTF). Proteolysis of these CTFs by gamma-secretase releases intracellular domains (ICDs) and extracellular peptides (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 50244
Sequence Length: 456
Subcellular Location: Presynaptic cell membrane
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Q9HDB5 | MHLRIHARRSPPRRPAWTLGIWFLFWGCIVSSVWSSSNVASSSSTSSSPGSHSQHEHHFHGSKHHSVPISIYRSPVSLRGGHAGATYIFGKSGGLILYTWPANDRPSTRSDRLAVGFSTTVKDGILVRIDSAPGLGDFLQLHIEQGKIGVVFNIGTVDISIKEERTPVNDGKYHVVRFTRNGGNATLQVDNWPVNEHYPTGRQLTIFNTQAQIAIGGKDKGRLFQGQLSGLYYDGLKVLNMAAENNPNIKINGSVRLVGEVPSILGTTQTTSMPPEMSTTVMETTTTMATTTTRKNRSTASIQPTSDDLVSSAECSSDDEDFVECEPSTGGELVIPLLVEDPLATPPIATRAPSITLPPTFRPLLTIIETTKDSLSMTSEAGLPCLSDQGSDGCDDDGLVISGYGSGETFDSNLPPTDDEDFYTTFSLVTDKSLSTSIFEGGYKAHAPKWESKDFRPNKVSETSRTTTTSLSPELIRFTASSSSGMVPKLPAGKMNNRDLKPQPDIVLLPLPTAYELDSTKLKSPLITSPMFRNVPTANPTEPGIRRVPGASEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDETRNYISNSAQSNGTLMKEKQQSSKSGHKKQKNKDREYYV | Function: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling (By similarity).
PTM: Proccessed by alpha-secretase leading to the formation of an extracellular soluble protein as well as a C-terminal membrane-embedded fragment (CTF). Proteolysis of these CTFs by gamma-secretase releases intracellular domains (ICDs) and extracellular peptides.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 69305
Sequence Length: 637
Subcellular Location: Presynaptic cell membrane
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Q8C985 | MHLRIHPRRSPPRRPAWTLGIWSLFWGCIVSSVWSSSNVASSSSSSPGSHSQQEHHFHGSKHHSVPISIYRSPVSLRGGHAGATYIFGKSGGLILYTWPANDRPSTRSDRLAVGFSTTVKDGILVRIDSAPGLGDFLQLHIEQGKIGVVFNIGTVDISIKEERTPVNDGKYHVVRFTRNGGNATLQVDNWPVNEHYPTGNTDNERLQMVKQKIPFKYNRPVEEWLQEKGRQLTIFNTQAQIAIGGKDKGRLFQGQLSGLYYDGLKVLNMAAENNPNIKINGSVRLVGEVPSVSGTTQTTSMPPEMSTTVMETTTTMATTTTRKNRSTASIQPTSDDLVSSAECSSDDEDFVECEPSTGRSDKSLSTSIFEGGYKAHAPKWESKDFRPNKVSETSRTTTTSLSPELIRFTASSSSGMVPKLPAGKMNNRDLKPQPDIVLLPLPTAYELDSTKLKSPLITSPMFRNVPTANPTEPGIRRVPGASEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDETRNYISNSAQSNGTLMKEKQASSKSGHKKQKNKDKEYYV | Function: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling (By similarity).
PTM: Proccessed by alpha-secretase leading to the formation of an extracellular soluble protein as well as a C-terminal membrane-embedded fragment (CTF). Proteolysis of these CTFs by gamma-secretase releases intracellular domains (ICDs) and extracellular peptides (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 62376
Sequence Length: 567
Subcellular Location: Presynaptic cell membrane
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Q8VZQ0 | MAVSADYQVKFPESGDLYSILAAEGIEFLLSHSGEVPLEYIHGKTICLFFSAIWCRPCKDFTPELIKLYENLQNRGEELEIIFVSFDHDMTSFYEHFWCMPWLAVPFNLSLLNKLRDKYGISRIPSLVPLYSDEISVAEDVIGLIEDYGSEAFPFTKKRKEELKAIDDSKRLGGQLEKLLTHESRNYVVARNGSKVLVSKLVGKTIGLYFGAHWCPPFRSFTSQLVDVYNELATTDKGSFEVILISTDRDSREFNINMTNMPWLAIPYEDRTRQDLCRIFNVKLIPALVIIGPEEKTVTTNAREMVSLYGSRSFPFTESRIVELKACLKKEGDSLPRKVKDNKHEHELKLDMAKAYVCDFCKKQGRFWAFSCNACDYDLHPTCVEEEEALLV | Function: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions.
Catalytic Activity: [protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH
Sequence Mass (Da): 44963
Sequence Length: 392
EC: 1.8.1.8
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Q7XPE8 | MGETAEGVEAGEKYVSIPQLAGVGTLLSNGGKEIPLSSIEGKRICLFFSAHWCRPCRNFTPKLLQIYRKLRNTCKNMEIIFISLDRDEISFLDYFKGMPWLALPFDTGLRQKLCVQFDIEHIPALIPLSTTLSHGFRVEEDAVKLVEEYGVDAYPFGAKRRSELEGMDDARRQGGNLLQLLGCKEREYVISADGIKTPISDLNGKTIGLYFGAHWCPPCRAFTKQLREAYDELKALRPGNFQVIFISMDRNEEEFQASLSAMPWFAIPYSDTTVQELSRIFTIKGIPTLLILGPDGKVFKTDGRRIISKYGAMAFPFTESRAYELEEVLKKERDSLPHRVRDHRHEHELELDMAKAYLSTQLFHQTPSVQPCRLNLKTLREEYHLIFTNSNRKTSRPQSSYTRQQRDLNNLYSDPKHLPQLHKHFDQSNVATAENSLRFLNGEPENSDISSIHVAFADLAGKIRGEDDKRD | Function: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions.
Catalytic Activity: [protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH
Sequence Mass (Da): 53797
Sequence Length: 471
EC: 1.8.1.8
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A0A1C9II22 | MSLEKRWSLEGTTALVTGGTKGIGHAIVEELVGFGARVYTCSRNEAELRKCLQEWENLKYDVTGSVCDVSSRTEREKLAEEVSSVFNGKLNILINNAGGYVNKPIDGFTAEDFSFLVAVNLESAFHLCQLAHPMLKASGTGSIVHISSCCAQIAIPGHSIYSSTKGAINQLTRNLACEWAKDNIRTNSIAPGAIRTPGTESFVIDKDALDREVSRVPFGRIGEPEEVASLAAFLCMPSASYITGQVICVDGGRTING | Function: In the Amaryllidaceae alkaloids biosynthesic pathway, catalyzes the conversion of noroxomaritidine to oxomaritidine, a precursor of haemanthamine- and crinamine-type alkaloids, promising anticancer agents . Can also, to some extent, catalyze the condensation of 3,4-dihydroxybenzaldehyde (3,4-DHBA) and tyramine to produce norbelladine, and of isovanillin and tyramine to produce 4'-O-methylnorbelladine .
Catalytic Activity: (10bR,4aS)-noroxomaritidine + H(+) + NADPH = (10bR,4aS)-oxomaritidine + NADP(+)
Sequence Mass (Da): 27605
Sequence Length: 257
Pathway: Alkaloid biosynthesis.
EC: 1.1.1.-
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P03134 | MAGNAYSDEVLGATNWLKEKSNQEVFSFVFKNENVQLNGKDIGWNSYKKELQEDELKSLQRGAETTWDQSEDMEWETTVDEMTKKQVFIFDSLVKKCLFEVLNTKNIFPGDVNWFVQHEWGKDQGWHCHVLIGGKDFSQAQGKWWRRQLNVYWSRWLVTACNVQLTPAERIKLREIAEDNEWVTLLTYKHKQTKKDYTKCVLFGNMIAYYFLTKKKISTSPPRDGGYFLSSDSGWKTNFLKEGERHLVSKLYTDDMRPETVETTVTTAQETKRGRIQTKKEVSIKTTLKELVHKRVTSPEDWMMMQPDSYIEMMAQPGGENLLKNTLEICTLTLARTKTAFDLILEKAETSKLTNFSLPDTRTCRIFAFHGWNYVKVCHAICCVLNRQGGKRNTVLFHGPASTGKSIIAQAIAQAVGNVGCYNAANVNFPFNDCTNKNLIWVEEAGNFGQQVNQFKAICSGQTIRIDQKGKGSKQIEPTPVIMTTNENITVVRIGCEERPEHTQPIRDRMLNIHLTHTLPGDFGLVDKNEWPMICAWLVKNGYQSTMASYCAKWGKVPDWSENWAEPKVPTPINLLGSARSPFTTPKSTPLSQNYALTPLASDLEDLALEPWSTPNTPVAGTAETQNTGEAGSKACQDGQLSPTWSEIEEDLRACFGAEPLKKDFSEPLNLD | Cofactor: The endonuclease active site can probably bind other divalent cations.
Function: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication . Also plays a role in viral packaging and transactivation of several promoters . Binds site-specifically to 2-3 approximate tandem copies of the tetranucleotide 5'TGGT3' within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR) . Cooperatively binds Ori with host PIF and probably other host factors, which activate the nickase function of NS1 . Becomes covalently attached to the 5' end of the nick and provides a 3'OH for priming DNA synthesis . The helicase activity unwinds DNA in a 3'-5' direction on the longer strand . Participates in the transcriptional regulation of several promoters including the viral p38 promoter that regulates the expression of VP1 and VP2 transcripts . Inhibits the host cell cycle during the G1/S transition, the S-phase, and the G2/M transition . These arrests may provide essential cellular factors for viral DNA replication. Promotes apoptosis in host cell .
PTM: Phosphorylated.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 76249
Sequence Length: 672
Domain: In the N-terminus, the endonuclease region is involved in binding to the origin of replication (By similarity). In the middle, there are the ATPase and helicase activities (By similarity). The C-terminus probably contains a transactivation domain .
Subcellular Location: Host nucleus
EC: 3.1.21.-
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P07296 | MATGGLAKWVGAVQAFGHPSWSYVIKLRHGHVTMIERGFYELCGGENWNMLHELPGDNGLLEMWESRESMLESWSPGDGHSWAMAWAGWRAARETMQRRQYVNEPTFSCWSQSELGENGWHVHIIIGGPGLTRQNAAISRSILCTSFFKHLLITIRQRTHAPYTVLSRDELNAWNWLQKIAQRVMRGDMDDIVDILKCRKANGTLVAQAINGTEFITRYMLPKNRKVANTVLTRHTTPEQSYDSTWGKTYGFAVCNGETVSEFTRKDLWKVLYNIYTAHPAENMLNSNPSVWGDLPRVSANRIDADDAEARSRPIKLSRKQKIMAEVIQRATDGLLLTYNDLVVHLSDLMLMLEGMPGGSKTAEQLLTMIHIKLCAKYNAYEFMLMKTPATQNMNPGAPHYDCQGNLVFKLLNLQGYNPWQVGHWLVMMLSKKTGKRNSTLFYGPASTGKTNLAKAICHAVGLYGCVNHNNKQFPFNDAPNKMILWWEECIMTTDYVEAAKCVLGGTHVRVDVKHKDSRELPQIPVLLSSNHDVYTVVGGNATFGVHAAPLKERITQMNFMKQLPNTFGEITPGMISNWLSHCAHIHQEHLSLEGFAIKWDVQSVGNSFPLQTLCPGHSQNWTFSENGVCWHCGGFIQPTPESDTDSDGDPDPDGAVAGDSDTSANSESTVSFSSNDSGLGSVTSSAPSVPDRAEEIEEIPSECLEWMREEVDRLSAHDINSLAHQATGFILDPIPEEPEERERDLAREDAEPEASTSHTPATKRARVEEGEPWDGTQPITEGDWIDFESRQKRRRLEREEKGGEDEDMEVQESDPSAWGEKLGIVEKPGEEPIVLYCFETLPESDEEGDSDKENKTHTV | Cofactor: The endonuclease active site can probably bind other divalent cations.
Function: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication. Also plays a role in viral packaging and transactivation of several promoters. Binds site-specifically to 2-3 approximate tandem copies within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR). Becomes covalently attached to the 5' end of the nick and provides a 3'OH for priming DNA synthesis. The helicase activity unwinds DNA in a 3'-5' direction on the longer strand. Participates in the transcriptional regulation of several promoters.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 96466
Sequence Length: 860
Domain: In the N-terminus, the endonuclease region is involved in binding to the origin of replication. In the middle, there are the ATPase and helicase activities. The C-terminus probably contains a transactivation domain.
Subcellular Location: Host nucleus
EC: 3.1.21.-
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Q9PZT1 | MELFRGVLQVSSNVLDCANDNWWCSLLDLDTSDWEPLTHTNRLMAIYLSSVASKLDFTGGPLAGCLYFFQVECNKFEEGYHIHVVIGGPGLNPRNLTVCVEGLFNNVLYHLVTENVKLKFLPGMTTKGKYFRDGEQFIENYLMKKIPLNVVWCVTNIDGYIDTCISATFRRGACHAKKPRITTAINDTSSDAGESSGTGAEVVPINGKGTKASIKFQTMVNWLCENRVFTEDKWKLVDFNQYTLLSSSHSGSFQIQSALKLAIYKATNLVPTSTFLLHTDFEQVMCIKDNKIVKLLLCQNYDPLLVGQHVLKWIDKKCGKKNTLWFYGPPSTGKTNLAMAIAKSVPVYGMVNWNNENFPFNDVAGKSLVVWDEGIIKSTIVEAAKAILGGQPTRVDQKMRGSVAVPGVPVVITSNGDITFVVSGNTTTTVHAKALKERMVKLNFTVRCSPDMGLLTEADVQQWLTWCNAQSWDHYENWAINYTFDFPGINADALHPDLQTTPIVTDTSISSSGGESSEELSESSFFNLITPGAWNTETPRSSTPIPGTSSGESFVGSSVSSEVVAASWEEAFYTPLADQFRELLVGVDYVWDGVRGLPVCCVQHINNSGGGLGLCPHCINVGAWYNGWKFREFTPDLVRCSCHVGASNPFSVLTCKKCAYLSGLQSFVDYE | Cofactor: The endonuclease active site can probably bind other divalent cations.
Function: Multifunctional protein essential for viral DNA replication, which cooperatively interacts with the viral DNA origin of replication and transactivates several promoters including the viral p6 promoter . Binds the origin of replication and performs an endonucleolytic nick within a conserved sequence in the viral genome, thereby initiating the rolling circle replication (RCR) . Participates in the transcriptional regulation the viral p6 promoter that regulates all viral transcripts and the cellular CDN1A or IL6 promoters . Transactivates several host promoters some of which induce the S cell cycle phase for the production of host replicative proteins . Up-regulates the expression of host E2F4 and E2F5 and interacts with both these factors thereby inhibiting the host cell cycle G2/M transition . This arrest promotes apoptosis for viral release .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 74065
Sequence Length: 671
Domain: In the N-terminus, the endonuclease region is involved in binding to the origin of replication on the viral DNA as well as to the overlapping viral promoter p6. In the middle, there are the ATPase and helicase activities. The C-terminus probably contains a transactivation domain.
Subcellular Location: Host nucleus
EC: 3.1.21.-
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D4AWH0 | MKSRVYVRFDRGFHVICPYQAKLAGSRKNDGAGYISPLALKSPIGLQHDLEDGCRIRSAFGKCIVNSRFLALIDVRKSGFKERGSKEPHGNSFVYWVTYSFLQFFETTMDELPSGRGMGGRLPFNQSFWEEFLSGREGQLPTLPDISHVSKSVIRILGGNPGSMHLQGTNTYLVGTGRSRILIDTAQGLPVWIDCISSFLHTQKIELSYVLLTHWHGDHTGGVPDLIAQNSSLADKIYKNHPDSGQNPITHGQIFSVDGATVRAIFTPGHSVDHMCFLLEEENALFTGDNVLGHGFSVAQDLGRYMDSLRDMASLGCRIGYPAHGAVIENLPGKLEEYIQHREGRERMMLSALTRQRVRGEGLREEGVKCGLTLNEIVMAIYGKLPPEVIEKALAPSLLQVLWKLTEDRMVGFKPGDPLKRQWFALEQRKRNKARGYPS | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of neosartoricin B, a prenylated anthracenone that probably exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent . The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (By similarity). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (By similarity). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (By similarity). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (By similarity). Neosartoricin B can be converted into two additional compounds neosartoricins C and D (By similarity). Neosartoricin C is a spirocyclic compound that is cyclized through the attack of C3 hydroxyl on C14, followed by dehydration (By similarity). On the other hand, neosartoricin D is a further cyclized compound in which attack of C2 on C14 in neosartoricin C results in the formation of the acetal-containing dioxabicyclo-octanone ring (By similarity). Both of these compounds are novel and possibly represent related metabolites of the gene cluster (By similarity).
Sequence Mass (Da): 49014
Sequence Length: 439
Pathway: Secondary metabolite biosynthesis.
EC: 3.1.-.-
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D4AWH1 | MGKQQETILIIGAGIAGLTTSRLLTNNGIPNVVFEASTPDRSQGFAISLQEFGYSALLAALGDLPFSSLIRGVAPDRQIGGSGWIDQALRDNRTGEVLVAPDLTTAKQTIVRANRNALRHWIADCGEDELDVRYGHKLQRIEGRLGDVTAVFENNARYKGSLIIAADGVNSTVRSQILPNVVPETIPLIHYHGEFQLPHSAFDELIRPHSRQSNILVGVGDRFNTPLSICNITKSQVHLDWSYSRTVKGENDILYRPNVPSEEAKQIPPALLEELDTLCLAEPWKSFLNSESVKTHRVFHWTTRCVYITQDDARHAGEQGVVFVGDSWHAMPIFGGEGGNHALLDGVELADAIITSTSNSGKGSWDNVVKNYYGGAWKRSQDAVRRSTQRFFLLHRPATEWKEISEKKKQIA | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of neosartoricin B, a prenylated anthracenone that probably exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent . The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (By similarity). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (By similarity). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (By similarity). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (By similarity). Neosartoricin B can be converted into two additional compounds neosartoricins C and D (By similarity). Neosartoricin C is a spirocyclic compound that is cyclized through the attack of C3 hydroxyl on C14, followed by dehydration (By similarity). On the other hand, neosartoricin D is a further cyclized compound in which attack of C2 on C14 in neosartoricin C results in the formation of the acetal-containing dioxabicyclo-octanone ring (By similarity). Both of these compounds are novel and possibly represent related metabolites of the gene cluster (By similarity).
Sequence Mass (Da): 45585
Sequence Length: 412
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q86197 | MTQSVSLSDFIVKTEDGYMPSDRECIALDRYLSKEQKELRETFKDGKNDRAALRIKMFLCPSPSRRFTQHGVVPMREIKTNTDMPSTLWTLVTDWLLNLLQDEENQEMFEDFISSKFPDVLASADKLARFAQRLEDRKDVLRKNFGKAMNAFGACFWAIKPTFATEGKCNVVRASDDSIILEFQPVPEYFRCGKSKATFYKLYPLSDEQPVNGMLALKAVAGNQFFMYHGHGHIRTVPYHELLTLSNHSLVKIKKRSKTFLNHHSQLNVVVNFSICSME | Function: Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments.
Sequence Mass (Da): 32110
Sequence Length: 279
Subcellular Location: Host cytoplasm
EC: 3.6.4.-
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Q9PY93 | MAELACFVSFSLTEDKVVWYPINKKAVQTMLCAKVEKDQRSNYYDTILYGVAPPPEFRNRFKTNERYGLDYESDQYTELVNLLADTLNMVSMPTEKFQFDIVKTVVQVRHLENLLCRIKDVNDILNANVKLRVKAVMIACNLVNETETTPLTESNDIVYQDSYFTITKLDYSNHKLLPLMADEYKITINTKTDIPDRNQTAFAAYIRYNFNKFAAISHGKRHWRLVLHSQLMSHAERLDRKIKSDKKHGRQFSYDDGDMAFVHPGWKTCIGQLCGGTTFEVAKTSLYSIKPSKTVRTATNKIESDLISMVGN | Function: Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments.
Sequence Mass (Da): 35915
Sequence Length: 312
Subcellular Location: Host cytoplasm
EC: 3.6.4.-
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Q45UF4 | MVSIKVSLADFIVKTEEGWIPSDNCPALDRFKTKTEKELLDSIKKEGADRASIRKQLFLTSISNKRLTQLGGVPVRDIRTSTTIPSSTRNLITDWLLNIFNDEESGEEVESAIASKYPDIFCSADKISRVAQRLENRRDRVHEDGFRILSATMLAIDSDIATEGKCEIVRATEDAIIAKFEPVSEHLCIGNPRGVFYKAFPIKKEQPMVYGVKALLGISNRDFIMNHGHGHLRTVPYSEINNAVRSFAKKNEAEIKRIRSDSLSPNAGEKFINMCDMLLQKEKIETVIAKIMKSDKN | Function: Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments.
Sequence Mass (Da): 33433
Sequence Length: 297
Subcellular Location: Host cytoplasm
EC: 3.6.4.-
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Q8V790 | MENATTINETLVEEVYNMTMSYFEHNVIIMKYFPFLASILTIAFTAWKMGKSTFKVTKTVAGSGFKVVRVIVITIFNCIMRLFGSKTEIVSDDRLDALASKILAQINNQVKVIEQLTKRELEQVKLLADIYEMLKFKKDEVDMSFETNKKEYEKWVKDPYQPTRAVSLD | Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly.
PTM: The N-glycosyl content is primarily Man(9)GlcNAc, with a small amount of Man(8)GlcNAc.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 19572
Sequence Length: 169
Domain: Binds 1 calcium ion per tetramer.
Subcellular Location: Host rough endoplasmic reticulum membrane
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P04513 | MEKLTDLNYTLSVITLMNSTLHTILEDPGMAYFPYIVSVLTVLFTLHKASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMDRVVKEMRRQLEMIDKLTTREIEQVELLKRIHDKLMIRTVDEIDMTKEINQKNVRTLEEWENGRNPYEPKEVTAAM | Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly.
PTM: Mannosylated.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 20492
Sequence Length: 175
Domain: A disordered 28 aa C-terminal domain is presented to the cytoplasm by each subunit of the tetrameric receptor.
Subcellular Location: Host rough endoplasmic reticulum membrane
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Q5QGZ2 | MAESSDMQELFVQATYEEILKLASSVNHEQIRETISSSSPQKILTGTMLTLGALLTTLIVKKKGTKFLTTKVQSNVAYLAEMVVWKANQTVKTICDEVLHQRKVIEKLQCLDKMCSEIEKLRYDMEHFQGMDVTKELIQMCEQKMIDIDSKVKEVERSCDRRIRDYDWKIATLTAHPTQQLPAHIDIINQHIEDDAETQIIQQHMNKQARVKLNSRNRL | Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 25347
Sequence Length: 219
Subcellular Location: Host rough endoplasmic reticulum membrane
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Q9CZ57 | MAAPVLRCVRKLLKLVDFTPVPRRYRYKKKWATTEPQFTASRLALQNFDMTYSVQFGDLWPSIRVSLLSEQKYGALVNNFAAWDSVSAKLEQLSAKDFVSEAISHQKLEPESGLSPTPSLDCSPNLRCFTFSRGDVSRFPPARLGSLGLMDYYLMDAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQTGCCRNLAANDLSTSRTGRLQKVLHSYVPQDIREGNQVRVTSWDGRKWGELEGDTYDRVLVDVPCTTDRHSLHEEENNIFQRSRKKERQMLPMLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAIELLANQYNIKVQVEDLSHFRKLFMDTFCFFPSCQVGELVIPNLMVNFGPMYFCKLHRLP | Function: Involved in mitochondrial ribosome assembly. 5-methylcytosine rRNA methyltransferase that probably is involved in mitochondrial ribosome small subunit (SSU) maturation by methylation of mitochondrial 12S rRNA at position 911; the function is independent of MTERFD2/MTERF4 and assembled mitochondrial ribosome large subunit (LSU). Targeted to LSU by MTERFD2/MTERF4 and probably is involved in a final step in ribosome biogenesis to ensure that SSU and LSU are assembled. In vitro can methylate 16S rRNA of the LSU; the methylation is enhanced by MTERFD/MTERF4.
Catalytic Activity: a cytidine in rRNA + S-adenosyl-L-methionine = a 5-methylcytidine in rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42853
Sequence Length: 381
Subcellular Location: Mitochondrion
EC: 2.1.1.-
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Q8GYE8 | MVARRNKPKAPLVKHRFSGGDSHKPKPPPATKQPFSGVESHKPKTSPATKQKFSGVESHKPKTPPGKQRFSGAESRKPKTPPATKQKFSSLERSALYARREAANILRTVLRGDAERRAVASIKSLVLSPSVRNKRGTFALVCETLKYLTVIKDVLDIANVLNSKWKRQEPLVFIVCYDILFGKDTPSIGDAEKFLMRHKEALLSGLATLLVRKKVDSVDQLLGSKLTGHLKPRYVRVNTLKMDVDSAVQELEKHYTVQKDETVPDLLVLPPGSDLHAHRLVANGRIFLQGKASSMVAAALQPQAGWEVLDACSAPGNKTIHLAALMEGQGKIIACELNEERVKRLEHTIKLSGASNIEVCHGDFLGLNPKDPSFAKIRAILLDPSCSGSGTITDRLDHLLPSHSEDNNMNYDSMRLHKLAVFQKKALAHALSFPKVERVVYSTCSIYQIENEDVVSSVLPLASSLGFKLATPFPQWQRRGLPVFAGSEHLLRMDPVEDKEGFFIALFVRANKLDNPKSSELPDRVCRRRPKERTMQLHPYLCPKMFRAWSGTLHRLKTRFLLSRNGC | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 2268 (m5C2268) in 25S rRNA.
Catalytic Activity: a cytidine in 25S rRNA + S-adenosyl-L-methionine = a 5-methylcytidine in 25S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 63174
Sequence Length: 567
EC: 2.1.1.-
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Q9NAA7 | MATDALYNEVAEIIRCVLAKEKSVRNAVYGSSYKNKKALLRLSCESLKFRPVFDEILQDKELKSMKRDANIGGSVELLYVLMYETLVGSGLTRCSQELKSVISRRIQRIKEVEHAMQDEGRGIKAMKEADDGMKKIQIPRYARINTLKWTADEAMKTLETEKWKILGTLKPENFAEMVTKMKDDEVYVDPHVENLIIFAPNIQNFYEYWMVEQRYLILQDKASCLPAFLLNPRPGSQVFDTCAAPGMKTSHAAAIMENQGKVWAMDRAADRVATMKQLLDASKVAIASSFCGDFLKTDVTDKKFSKVKFAIVDPPCSGSGIVKRMDEITGGNAEKERLEKLKNLQAMILKHALKLPGLKRAVYSTCSVHEEENEQVVDEVLLDTYVRQNYVLKKNVLPEWTYRGLKTYEVGEHCLRANPKVTLTNGFFVAVFERVKSSE | Function: S-adenosyl-L-methionine-dependent methyltransferase which methylates the carbon-5 position of cytosine 2381 to 5-methylcytosine (m5C2381) in 26S rRNA . Plays a role in the production of mature 5S, 5.8S, 18S and 26S rRNAs and promotes the processing of the internally transcribed spacer 2 (ITS2), which separates the 5.8S and 26S rRNAs on large pre-rRNA precursors . May play a role in the translation of leucine and proline codons (Probable). May play a role in maintaining ribosomal frameshifting in response to osmotic stress . Not required for global translation .
Catalytic Activity: a cytidine in 26S rRNA + S-adenosyl-L-methionine = a 5-methylcytidine in 26S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49839
Sequence Length: 439
EC: 2.1.1.-
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Q9VDZ4 | MSKKPHSIKVPTQYRATAKILKAALEQQKCIKTLIFAEKHARTRSLHTVLKKFSENRVALEKAIEETGLLRDNPSFDPSLAKILVTELLFGRKELNGESKPVQTVRSYKDRLLNSIRDFGVQRKEPNPRYVRINTNLYSLAEALDYLHKSDWRRKELPADASYADFLTAIKSLAENEFMTDLHVEGVLIFPAKWSNYWVRHPLVHSKRFILQNKATCLAAELLAPPSGATVLDMCAAPGMKTVHICNVMQNKGCIYSVEQDHVRYNTLCEITKDAGCDIVKPILGDALNLTPERFPDVEYILVDPSCSGSGMQNRMTVCDEPKEDKRLQKLQGLQIKILSHAMGAFPNVKRIAYCTCSLWKEENEQVVQRCLQLNPSFKLLSCKKALRNKWHNVGDKDYPNIGKNVLYCQPDSDLTDGIFLALFEKRREGEKD | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of a cytosine in 28S rRNA.
Catalytic Activity: a cytidine in 28S rRNA + S-adenosyl-L-methionine = a 5-methylcytidine in 28S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49280
Sequence Length: 433
EC: 2.1.1.-
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Q96P11 | MGLYAAAAGVLAGVESRQGSIKGLVYSSNFQNVKQLYALVCETQRYSAVLDAVIASAGLLRAEKKLRPHLAKVLVYELLLGKGFRGGGGRWKALLGRHQARLKAELARLKVHRGVSRNEDLLEVGSRPGPASQLPRFVRVNTLKTCSDDVVDYFKRQGFSYQGRASSLDDLRALKGKHFLLDPLMPELLVFPAQTDLHEHPLYRAGHLILQDRASCLPAMLLDPPPGSHVIDACAAPGNKTSHLAALLKNQGKIFAFDLDAKRLASMATLLARAGVSCCELAEEDFLAVSPSDPRYHEVHYILLDPSCSGSGMPSRQLEEPGAGTPSPVRLHALAGFQQRALCHALTFPSLQRLVYSTCSLCQEENEDVVRDALQQNPGAFRLAPALPAWPHRGLSTFPGAEHCLRASPETTLSSGFFVAVIERVEVPR | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 3782 (m5C3782) in 28S rRNA . m5C3782 promotes protein translation without affecting ribosome biogenesis and fidelity . Required for corpus callosum and cerebral cortex development (By similarity).
Catalytic Activity: cytidine(3782) in 28S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(3782) in 28S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 46692
Sequence Length: 429
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q8K4F6 | MGLYAAAAAVLAGVESRQGSLKGLVYSSNFQNLKQLYALVCETQRYSAVLDAVIASAGLLRAEKKLRPHLAKVLVYELLLGKGFRGGGGRWKALLGRHQARLKAELARLKVHRGVSRNEDLLQESSRPGQAYQVPRFVRVNTLKTRPEDAIDYFKRQGFSYQGRASSLEDLRALKGQHFLLDPLLPELLVFPAQTDLHEHPLYRAGHLILQDKASCLPAMLLSPPPGSHVIDACAAPGNKTSYIAALLKNQGKIFAFDQDAKRLAAMATLVARAGVSCCELAEKDFLTVSPSDQRYSQVQYILLDPSCSGSGMLSRQLEEHGEGTPSKERLQALAGFQQRALCHALRFPSLQRLVYSTCSLCQEENEDVVQEALQHNSGTFRLAPVLPTWPHRGLSTFPGSEHCLRASPETTLTGGFFIAVFERAEVVPTPAPQTDAMDPEPLSQVPKRKRRRKAAVGASMQPST | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 3438 (m5C3438) in 28S rRNA . m5C3782 promotes protein translation without affecting ribosome biogenesis and fidelity (By similarity). Required for corpus callosum and cerebral cortex development .
Catalytic Activity: a cytidine in 28S rRNA + S-adenosyl-L-methionine = a 5-methylcytidine in 28S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51030
Sequence Length: 465
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q8TEA1 | MSIFPKISLRPEVENYLKEGFMNKEIVTALGKQEAERKFETLLKHLSHPPSFTTVRVNTHLASVQHVKNLLLDELQKQFNGLSVPILQHPDLQDVLLIPVIGPRKNIKKQQCEAIVGAQCGNAVLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKCKKGAKEFDGTKVFLGNGISELSRKEIFSGLPELKGMGIRMTEPVYLSPSFDSVLPRYLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAVKLDMVEDTEGEPPFLPESFDRILLDAPCSGMGQRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGLSCEQLKQLQRFDPSAVPLPDTDMDSLREARREDMLRLANKDSIGFFIAKFVKCKST | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C5 position of cytosine 72 in tRNA(Thr)(TGT) and tRNA(Cys)(GCA) . In vitro also methylates tRNA(Thr)(AGT) . Methylation requires, in the acceptor stem region, the presence of the 3'-CCA terminus, the target site C72, the discriminator base U73, and the second and third base pairs (2:71 and 3:70) in the tRNA substrates .
Catalytic Activity: cytidine(72) in tRNA(Thr) + S-adenosyl-L-methionine = 5-methylcytidine(72) in tRNA(Thr) + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51770
Sequence Length: 469
Domain: The PUA domain plays a role in tRNA recognition through precisely recognizing the CCA end and the D-stem region of tRNA.
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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O57712 | MAMNYLEAFPKELREYYKNLFGKEEANKIMKKLREPVEHYYIRVNTLKISREKLIGELKKEGLKPLRSPYLPEGLYFVREGPNFSDDFEPKLPVVVANKYAAESVYQGAMLYAPGVLKADKNIKEGDEVQIRDPKGLLVGIGIARMDYKEMTEATRGLAVEVTLPKFKLPSLSELKAFEKGYFYPQGLPSMVTARVLEPKEDDVIIDMAAAPGGKTTHIAQLLENKGEIIAIDKSKNRLRKMEENIKRLGVKNVKLVQMDARKLPDLGIKADKILLDAPCTALGVRPKLWEERTLKHIEATARYQRAFIWAAIKSLRRGGVLVYSTCTLSYEENEGNVKFMIRKGMKLEEQSIFIGSPGIGMNKVQRFYPHKHLTQGFFIAKLRKVKDI | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C5 position of cytosine 72 in several tRNAs. This modification appears to slightly promote the thermal stability of P.horikoshii tRNAs, but does not affect their amino acid accepting activity. Four elements in the acceptor stems of tRNAs are essential for substrate recognition by this enzyme: the target site C72, the 3'-CCA terminus, U73 or G73, and the second base pair C2:G71.
Catalytic Activity: cytidine(72) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(72) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 44284
Sequence Length: 389
EC: 2.1.1.-
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Q9W0C1 | MADAAPAGDAPPNAGAPAGEGGDGEIVGGPHNPQQIAAQKRLQQTQAQVDEVVDIMRTNVEKVLERDSKLSELDDRADALQQGASQFEQQAGKLKRKFWLQNLKMMIIMGVIGLVVVGIIANKLGLIGGEQPPQYQYPPQYMQPPPPPPQQPAGGQSSLVDAAGAGDGAGAGGSAGAGDHGGV | Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane . Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters . Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles . Also involved in a neuron-specific sort-and-degrade mechanism that promotes endolysosomal degradation and is required for neuronal maintenance .
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 18776
Sequence Length: 183
Subcellular Location: Cytoplasmic vesicle
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Q8R4G0 | MYLSRFLSIHALWVTVSSVMQPYLFVWGHYDVCKSLIYTEEGKVWDYTACQPESTDMTKYLKVKLDPPDITCGDPPESFCAMGNPYMCNNECDASTPELAHPPELMFDFEGRHPSTFWQSATWKEYPKPLQVNITLSWSKTIELTDNIVITFESGRPDQMILEKSLDYGRTWQPYQYYATDCLHAFHMDPKSVKDLSQHTVLEIICTEEYSTGYSTNSKIIHFEIKDRFAFFAGPRLRNMASLYGQLDTTKKLRDFFTVTDLRIRLLRPAVGEIFVDELHLARYFYAISDIKVRGRCKCNLHATSCLYDNSKLTCECEHNTTGPDCGKCKKNYQGRPWSPGSYLPIPKGTANTCIPSISSIGNCECFGHSNRCSYIDLLNTVICVSCKHNTRGQHCELCRLGYFRNASAQLDDENVCIECYCNPLGSIHDRCNGSGFCECKTGTTGPKCDECLPGNSWYYGCQPNVCDNELLHCQNGGTCQNNVRCACPDAYTGILCEKLRCEEAGSCGSESGQGAPPRGSPALLLLTMLLGTAGPLVF | Function: Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 60566
Sequence Length: 539
Domain: The laminin N-terminal domain mediates 1:1 binding to NGL ligand with sub-micromolar affinity. Three NGL-binding loops mediate discrimination for LRRC4C/NGL1 among other NGLs by binding specifically to its LRR repeats. This specificity drives the sorting of a mixed population of molecules into discrete cell surface subdomains (By similarity).
Subcellular Location: Cell membrane
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Q96CW9 | MLHLLALFLHCLPLASGDYDICKSWVTTDEGPTWEFYACQPKVMRLKDYVKVKVEPSGITCGDPPERFCSHENPYLCSNECDASNPDLAHPPRLMFDKEEEGLATYWQSITWSRYPSPLEANITLSWNKTVELTDDVVMTFEYGRPTVMVLEKSLDNGRTWQPYQFYAEDCMEAFGMSARRARDMSSSSAHRVLCTEEYSRWAGSKKEKHVRFEVRDRFAIFAGPDLRNMDNLYTRLESAKGLKEFFTLTDLRMRLLRPALGGTYVQRENLYKYFYAISNIEVIGRCKCNLHANLCSMREGSLQCECEHNTTGPDCGKCKKNFRTRSWRAGSYLPLPHGSPNACATAGSFGNCECYGHSNRCSYIDFLNVVTCVSCKHNTRGQHCQHCRLGYYRNGSAELDDENVCIECNCNQIGSVHDRCNETGFCECREGAAGPKCDDCLPTHYWRQGCYPNVCDDDQLLCQNGGTCLQNQRCACPRGYTGVRCEQPRCDPADDDGGLDCDRAPGAAPRPATLLGCLLLLGLAARLGR | Function: Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 59799
Sequence Length: 530
Domain: The laminin N-terminal domain mediates 1:1 binding to NGL ligand with sub-micromolar affinity. Three NGL-binding loops mediate discrimination for LRRC4C/NGL1 among other NGLs by binding specifically to its LRR repeats. This specificity drives the sorting of a mixed population of molecules into discrete cell surface subdomains.
Subcellular Location: Cell membrane
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Q8R4F1 | MLRLLALFLHCLPLVSGDYDICKSWVTTDEGPTWEFYACQPKVMRLKDYVKVKVEPSGITCGDPPERFCSHENPYLCSNECDASNPDLAHPPRLMFDREDEGLATYWQSVTWSRYPSPLEANITLSWNKSVELTDDVVVTFEYGRPTVMVLEKSLDNGRTWQPYQFYAEDCMEAFGMSARRARDMSPSSAHRVLCTEEYSRWAGSKKEKHVRFEVRDRFAIFAGPDLRNMDNLYTRMESAKGLKEFFTFTDLRMRLLRPALGGTYVQRENLYKYFYAISNIEVIGRCKCNLHANLCTVREGSLQCECEHNTTGPDCGRCKKNFRTRAWRAGSYLPLPHGSPNACAAAGSAFGSQTKPPTMAPLGDSSFWPQVSSSAEAVAISVAVPSQAKDSTLFELKPRSPQVIPIEEFQDCECYGHSNRCSYIDFLNVVTCVSCKHNTRGQHCQHCRLGYYRNGSAELDDENVCIECNCNQIGSVHDRCNETGFCECREGAVGPKCDDCLPTHYWRQGCYPNVCDDDQLLCQNGGTCQQNQRCACPPGYTGIRCEQPRCDLADDAGPDCDRAPGIVPRPDTLLGCLLLLGLAARLAC | Function: Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 66166
Sequence Length: 589
Domain: The laminin N-terminal domain mediates 1:1 binding to NGL ligand with sub-micromolar affinity. Three NGL-binding loops mediate discrimination for LRRC4/NGL2 among other NGLs by binding specifically to its LRR repeats. This specificity drives the sorting of a mixed population of molecules into discrete cell surface subdomains (By similarity).
Subcellular Location: Cell membrane
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A0A455LN84 | MAKIALILGSVRSPRVGNDVTGWVHDVLKSRPSDDLQIEPLVIADFNLPVYDEPVMPAMVPAMKQFTKEHSKRWSAAIASYQGYIFVIPEYNGGIAGGTKNAVDYLYNEWPGKPVAIISYGTQGGNRANAQLSESLELVMKMKVAPTKVLLPFAAGTDVFSAINDGVLGEESQKAWAEAGKKEDILKALDEVKELLKQPKE | Function: NAD(P)H-dependent FMN reductase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids nectripenoids A and B, as well as cochliquninone D and isocochliquninone E . The pathway probably begins with the HR-PKS ntnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS ntnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of nectripenoids (Probable). The FAD-dependent monooxygenase ntnJ then performs an oxidative decarboxylation at C11 of the ntnH/ntnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation (Probable). The membrane-bound polyprenyl transferase ntnF then introduces a farnesyl group before the FAD-dependent monooxygenase ntnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by ntnA (Probable). The terpene cyclase/mutase ntnI then initiates the sequential tricyclic ring formation through protonation of the terminal epoxide and catalyzes the regioselective and stereoselective 6/6/6-tricyclic ring formation (Probable). The cytochrome P450 monooxygenase ntnM may then hydroxylate C1' (Probable).
Catalytic Activity: FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH
Sequence Mass (Da): 21931
Sequence Length: 201
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.5.1.39
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Q1QDI9 | MDIILASGSPRRRELLSRVQLEFTVISVDIDETPYQDESPEDYIVRMVAAKAEAATVQLNRQLKNNDAHIYQSLLSKPIILLTSDTIGVLPDGKTVLVKPNNREDAYRMWQQMSDSTHEVWTAVQATQLSLQPKRSDEFNNEQVWQIINQQQIIERTEVTFVALTLEMMSDYWDSGEPADKAGGYGIQGLGAAWVSRINGSYTNVVGLPLAQTLALIKEMNDTDTL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 25387
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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P58634 | MEPTAAPHPHLYLASQSPRRQELLRQIGVRFELLLADGDEDAEALEAVLLGETPDDYVQRVCALKAQAAARRRAARGLPARPILTSDTTVCLGGEILGKPADAADAHRMLRGMSGREHRVLTAVTVVTADGTPMHALSVSQVRFAVLTDVDIARYIASGEPFGKAGAYGIQGRAAAFVAHISGSYSGIMGLPLFETAALLAQAAITL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21866
Sequence Length: 207
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q7UWY8 | MNDLPRAELPGSGSPNPESLILASGSPRRAQLLSAAGYEFSVQPASDSAECGICSRETAPEMVARLAYRKAADVVARIDDGLVLAADTVASCVGNILGKPHNRDHAEEMLRLLSGRNHDVFTGVCLWSRRDEKFVVDVVRTRLQMSDLTDQQLTEHLDSLRWDGKAGAFGYQDGNDWLKVIGNDSESNVVGLPMERLAELLENFEQNAEKITTPTIDSIESSDSSCS | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 24707
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q2RQN0 | MTHGDNRDGPGRETRSSGPLVLASASPRRVDLLAQIGLVPDAIDPADLDETPAADELPRPYAERVARAKALAVAPRHPGAWVLAGDTVVARGRRILPKAEDAKTAKTCLEMLSGARHRVIGAIALVTPEGRLIERSVVSQVAFKRLSAAEIAEYLAGDEWRGKAGGYAIQGRAAAFVRWLEGSHSNVVGLPLFETNALLAGTGYRPGRDG | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22256
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q1AVT5 | MGLVLASESARRVELLRRAGYGFEARRSGFPEVVLDDPRETAVANARGKAEAVASTLPGEEVVLAADTVVYLPGEPGGILGQARDAGDVRRMLGLLEGRTHEVHSGVAVAGGGRVAVRHAVTEVRMRRLEPGEAEWYAACGEGVGKAGGYALQGRAAVFVEWIFGDYTNVVGLPLPLTIRMLRRFGVRPG | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20191
Sequence Length: 190
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q9PI04 | MLILASSSISRANLLKTAKIDFRQVSFDYDENLNKNISPFLYVQKIVLEKERQFLSTLGKDFQNQNLLFADSIVCIDEKILTKAKDKKEAYEMLALQNGKYASILSAFLLVKPEKRVFSLSKTTLYFKNFDENALRDYVENDLYKGKAGCIMCEGFHQNFITQQVGNLSTALGLDIQTLKAYL | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 20905
Sequence Length: 183
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q9AC58 | MSLTPVTLASQSSARQMILKNAGVAFEAVSPGVDEDAAKAGLLAEDVTPRDIADALAEMKAVKVSTKRPGLVIGADQTLDLKGRLIDKAGSLDEARARLLELRGTTHKLHSAVVVARDGRPIWRIVESAKLSVRPFSDAWLDRYIERRGEALLWSVGCYELESEGVQLFDKIEGDYFTILGLPLVGLLDFLRLHGALTV | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21621
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q3IYH0 | MRLLLASASETRLALLRAAGLELDALPARIDEEGVRAALEAEGASPLDVADTLAEMKAQKLAERHREALVLGCDQVLAFRREVWGKAPSPEALRAQLLRLRGETHKLISALVLYEEGRPVWRHAGEVRLTMRECSDGWIDGYIARNWETVRHSVGGYHLEGEGVRLFSAVEGDYFTVLGLPLLPLLNYLGQRGFIPT | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21836
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q9Z9F9 | MSLPLVLGSSSPRRKFILEKFRVPFTVIPSNFDESKVSYSGDPIAYTQELAAQKAYAVSELHSPCDCIILTGDTIVSYDGRIFTKPQDKADAIQMLKTLRNQTHDVVTSIAVLHKGKLLTGSETSQISLTMIPDHRIESYIDTVGTLNNCGAYDVCHGGLILKKVHGCVYNVQGLPIQTLKYLLEELNIDLWDYSI | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21750
Sequence Length: 196
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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C3PEA3 | MRLVLASQSPSRLSILRGAGVEPVIAPAHVDERAIEERLAGAEPAEIVCALAAAKAEAIAPDYPEDVVVGGDSMLLLDGSLQGKPHTPEATVERWHAQAGRAAELITGHCVLYGEERFVEASRTTVHFAQASDADIEAYARTGEPLECAGAFTLEALGGWFIDRIEGDPSSVIGLSLPVLRRALYSFGLNVSEFWAQH | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21130
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q8NSH0 | MQIVLASQSPSRRRILNSAGVEPLIHPADVDEDALLHSLNGSAPEEIVRQLALAKAQVVAPSYPGDVVIGGDSMLLIDATLQGKPHTREATIERWKQQRGNKATLITGHAIIFGDEVIVESSSTNIHFAEASDVDIERYADSGEPLECAGAFTLEALGGWFIDSIEGDPSSVIGLSLPVVRRALYRLGFNASDFWNM | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21248
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q6A725 | MTTCFVLASKSPARLRMLRSAGIEPVVIASGADESHLRGEDAVAMTARLSRLKAHSVIESGALEEYPADRMIVVACDSVLNLDGRILGKPHTAERARQWWRRMRGHQGVLVSGHHVAVIVNGQLREQTRIGQTVVTFADLTDAEIDAYVDSGEPAAVAGAFTIDGLGGAFITRINGDPHNVTGISLPLLRQMLMDLDVEWSSLWNGPKGGHLS | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 22969
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
B1I4S1 | MFRIVLASASPRRRELLQSLGLEFEVLPAGVNEDFAGRDPADMAESLAERKARAVAGRVGDGLILGADIVVFQRGRFLGKPEGPEEAAAMLTALQGDTHEVLTGVSLIRMPDGHAVVDHERTRVHFRAMTAQEIDWYVATGEPLDKAGAYAIQGLGGLFVRGIKGCWFNVVGLPLPLLSGLFRRQGVDLLNLVGTNWSSSGRR | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21946
Sequence Length: 203
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q55G28 | MILDILVKLNKLKIILASTSPRRIEYLGKLGVKFEIVESKFKEDLDKSQFQSVYDYCLENAKLKAIHAGIQLKEQNQQPNIIIGSDSIVVYDNKIFEKPKSLEEAKSMLTLLSGKIHTVCTAVHIEFFNENTNSKGSSSFYTLTNVEFDQLSPELINYYVDNFKPLDKAGSYGIQQTPAASFIKSINGDFYNVTGLPIHDLSINLRKIYVDNFLEK | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 24511
Sequence Length: 216
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
P19905 | MSKGYVWVVDDDSSIRWVMEKTSPLPT | Function: Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes.
PTM: Phosphorylated and dephosphorylated by NtrB.
Sequence Mass (Da): 3128
Sequence Length: 27
Subcellular Location: Cytoplasm
|
Q9P121 | MGVCGYLFLPWKCLVVVSLRLLFLVPTGVPVRSGDATFPKAMDNVTVRQGESATLRCTIDNRVTRVAWLNRSTILYAGNDKWCLDPRVVLLSNTQTQYSIEIQNVDVYDEGPYTCSVQTDNHPKTSRVHLIVQVSPKIVEISSDISINEGNNISLTCIATGRPEPTVTWRHISPKAVGFVSEDEYLEIQGITREQSGDYECSASNDVAAPVVRRVKVTVNYPPYISEAKGTGVPVGQKGTLQCEASAVPSAEFQWYKDDKRLIEGKKGVKVENRPFLSKLIFFNVSEHDYGNYTCVASNKLGHTNASIMLFGPGAVSEVSNGTSRRAGCVWLLPLLVLHLLLKF | Function: Neural cell adhesion molecule.
Location Topology: Lipid-anchor
Sequence Mass (Da): 37971
Sequence Length: 344
Subcellular Location: Cell membrane
|
Q62718 | MGVCGYLFLPWKCLVVVSLRLLFLVPTGVPVRSGDATFPKAMDNVTVRQGESATLRCTIDNRVTRVAWLNRSTILYAGNDKWCLDPRVVLLSNTQTQYSIEIQNVDVYDEGPYTCSVQTDNHPKTSRVHLIVQVSPKIVEISSDISINEGNNISLTCIATGRPEPTVTWRHISPKAVGFVSEDEYLEIQGITREQSGEYECSASNDVAAPVVRRVNVTVNYPPYISEAKGTGVPVGQKGTLQCEASAVPSAEFQWFKDDKRLVEGKKGVKVENRPFLSRLTFFNVSEHDYGNYTCVASNKLGHTNASIMLFGPGAVSEVNNGTSRRAGCIWLLPLLVLHLLLKF | Function: Neural cell adhesion molecule.
Location Topology: Lipid-anchor
Sequence Mass (Da): 37998
Sequence Length: 344
Subcellular Location: Cell membrane
|
Q91009 | WGCLRLPLPLCHALAAHCRCPASHTLRCREPLTVSSLSALLLGAHRPTDVIIENQALLTSLTRDDTRMLWDLRHLTISNSGLQYISDDAFQDNHRLSHVNLSFNALTSLSWKTFQHLPLQELTLEGNPFNCSCGIRWLQLWQNGSRAELGNQSLLCWEGSMLVALDSHPLHDCEPPTARIEHPDVVLRQGDSVNLTCHIWGEPSATGEWVLPHVGSEPSVTKLSEWELVLEINNISSSLNHKDLTCRAENSVGLAEDSVMLNVTFPPVILLLSEAIPQHFWCIPFSVDSNPTPRILWLFNGSMLPEGPYIHTRIVEYEPNSTVLHGCLQLNRPTHVNNGNYTLVVQNPLGRAARSIQGRFMDNPFSFSPEEPIPVSISPLGTRNSSLEGPVETADEHTFGVSVAVALAVFASLFLSVMLIALNKCGHRSKFGINRSAVLAPEDGLAMSLHFMTLGSSPVSSTESKLDGLKSNFIENPQYFCNACVHHVQRRDIVLKWELGEGAFGKVFLAECSHLLPEQEKTLVAVKALKEVTENARLDFQREAELLTVLQHEHIVKFYGVCTEGDPLIMVFEYMKHGDLNRFLRSHGPDAKILDQGQGQPCGQLTLSHMLQIATQIASGMVYLASLHFVHRDLATRNCLVGHDLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQGRELERPRTCPSEVYDIMQSCWQREPQQRSIQDIHSRLQALVKTPPIYLDILG | Function: Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand, it can also bind and be activated by NTF3/neurotrophin-3. Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors that regulate distinct overlapping signaling cascades driving cell survival and differentiation. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors.
PTM: Ligand-mediated auto-phosphorylation.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 87339
Sequence Length: 778
Subcellular Location: Cell membrane
EC: 2.7.10.1
|
P04629 | MLRGGRRGQLGWHSWAAGPGSLLAWLILASAGAAPCPDACCPHGSSGLRCTRDGALDSLHHLPGAENLTELYIENQQHLQHLELRDLRGLGELRNLTIVKSGLRFVAPDAFHFTPRLSRLNLSFNALESLSWKTVQGLSLQELVLSGNPLHCSCALRWLQRWEEEGLGGVPEQKLQCHGQGPLAHMPNASCGVPTLKVQVPNASVDVGDDVLLRCQVEGRGLEQAGWILTELEQSATVMKSGGLPSLGLTLANVTSDLNRKNVTCWAENDVGRAEVSVQVNVSFPASVQLHTAVEMHHWCIPFSVDGQPAPSLRWLFNGSVLNETSFIFTEFLEPAANETVRHGCLRLNQPTHVNNGNYTLLAANPFGQASASIMAAFMDNPFEFNPEDPIPVSFSPVDTNSTSGDPVEKKDETPFGVSVAVGLAVFACLFLSTLLLVLNKCGRRNKFGINRPAVLAPEDGLAMSLHFMTLGGSSLSPTEGKGSGLQGHIIENPQYFSDACVHHIKRRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKEASESARQDFQREAELLTMLQHQHIVRFFGVCTEGRPLLMVFEYMRHGDLNRFLRSHGPDAKLLAGGEDVAPGPLGLGQLLAVASQVAAGMVYLAGLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWYQLSNTEAIDCITQGRELERPRACPPEVYAIMRGCWQREPQQRHSIKDVHARLQALAQAPPVYLDVLG | Function: Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand . Can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival (By similarity). Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation . Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors.
PTM: Ligand-mediated autophosphorylation . Interaction with SQSTM1 is phosphotyrosine-dependent. Autophosphorylation at Tyr-496 mediates interaction and phosphorylation of SHC1 .
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 87497
Sequence Length: 796
Domain: The transmembrane domain mediates interaction with KIDINS220.
Subcellular Location: Cell membrane
EC: 2.7.10.1
|
Q63604 | MSPWPRWHGPAMARLWGLCLLVLGFWRASLACPMSCKCSTTRIWCTEPSPGIVAFPRLEPNSIDPENITEILIANQKRLEIINEDDVEAYVGLKNLTIVDSGLKFVAYKAFLKNGNLRHINFTRNKLTSLSRRHFRHLDLSDLILTGNPFTCSCDIMWLKTLQETKSSPDTQDLYCLNESSKNTPLANLQIPNCGLPSARLAAPNLTVEEGKSVTISCSVGGDPLPTLYWDVGNLVSKHMNETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVRGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLMAKNEYGKDERQISAHFMGRPGVDYETNPNYPEVLYEDWTTPTDIGDTTNKSNEIPSTDVADQTNREHLSVYAVVVIASVVGFCLLVMLLLLKLARHSKFGMKGPASVISNDDDSASPLHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHTRKNIKNIHTLLQNLAKASPVYLDILG | Function: Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin-dependent calcium signaling in glial cells.
PTM: Phosphorylated. Undergoes ligand-mediated autophosphorylation that is required for interaction with SHC1 and PLCG1 and other downstream effectors. Some isoforms are not phosphorylated.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 92186
Sequence Length: 821
Subcellular Location: Cell membrane
EC: 2.7.10.1
|
Q91044 | MDVSLCPTKCTFWRVFLLWSIWGDYLLSVLACPANCLCSKTDINCKKPDDGNLFPLLEGQDSGSSNGNTSINITDISRNITSIHIENWKNLQTLNAVDMELYTGLQRLTIRNSGLRNIQPRAFAKNPHLRYIDLSGNRLTTLSWQLFQTLRLFDLRLERNPFNCSCDIRWIQLWQEKGEANLQSQQLHCMNLDTAVILLRNMNITQCDLPEISVSHVNLTVREGENAVITCNGSGSPLPDVDWTVADLHSINTHQTNLNWTNVHAINLTLVNVTSEDNGFLLTCIAENVVGMSNASVLLTVYYPPRILTLEEPVLHLEHCIAFAVHGNPAPTLHWLHNGQVLRETEIIHMEFYQQGEVSEGCLLFNKPTHYNNGNYTIVATNQLGSANQTIKGHFLEKPFPESTDNFVSIGDYEVSPTPPITVTHKPEEDTFGVSIAVGLAAFACVLLVVLFIMINKYGRRSKFGMKGPVAVISGEEDSASPLHHINHGITTPSSLDAGPDTVVIGMTRIPVIENPQYFRQGHNCHKPDTYVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTNDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHALGKATPIYLDILG | Function: Receptor tyrosine kinase involved in nervous system and probably heart development. Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation (By similarity). The KT and KD isoforms fail to stimulate transformation, process outgrowth or survival. Isoform KI25 exhibits tyrosine phosphorylation in the absence of ligand and is unable to mediate survival of neuronal cells .
PTM: Ligand-mediated auto-phosphorylation.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 93181
Sequence Length: 827
Subcellular Location: Membrane
EC: 2.7.10.1
|
Q16288 | MDVSLCPAKCSFWRIFLLGSVWLDYVGSVLACPANCVCSKTEINCRRPDDGNLFPLLEGQDSGNSNGNASINITDISRNITSIHIENWRSLHTLNAVDMELYTGLQKLTIKNSGLRSIQPRAFAKNPHLRYINLSSNRLTTLSWQLFQTLSLRELQLEQNFFNCSCDIRWMQLWQEQGEAKLNSQNLYCINADGSQLPLFRMNISQCDLPEISVSHVNLTVREGDNAVITCNGSGSPLPDVDWIVTGLQSINTHQTNLNWTNVHAINLTLVNVTSEDNGFTLTCIAENVVGMSNASVALTVYYPPRVVSLEEPELRLEHCIEFVVRGNPPPTLHWLHNGQPLRESKIIHVEYYQEGEISEGCLLFNKPTHYNNGNYTLIAKNPLGTANQTINGHFLKEPFPESTDNFILFDEVSPTPPITVTHKPEEDTFGVSIAVGLAAFACVLLVVLFVMINKYGRRSKFGMKGPVAVISGEEDSASPLHHINHGITTPSSLDAGPDTVVIGMTRIPVIENPQYFRQGHNCHKPDTYVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGMSRDVYSTDYYRLFNPSGNDFCIWCEVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHALGKATPIYLDILG | Function: Receptor tyrosine kinase involved in nervous system and probably heart development. Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation.
PTM: Ligand-mediated auto-phosphorylation.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 94428
Sequence Length: 839
Subcellular Location: Membrane
EC: 2.7.10.1
|
P48902 | MTLQSVLLGAMIILGPILSMTSSNWIIIWIGLEISLLGFVSYYMLMKKIMSGEGIMMYFLIQSVSSTVMLLNGLYIFVNHASSYIYLFIFITMLMLKIGMFPLHFWIIPVYSKLSYLNIGIVGLLLKIVPMWILMHMGCITSEMLNLITMLSVTSMLFGALIGMNLSKMRMVLGASTITHNGWLGMSCISGSLFKYFITYGFSLVILLVFLYLGDKMSISLSLLSLSGLPPFMLFIGKINVLLMMMETNLWFIVLVFAILSAVISLVYYLKFSVMFFMNMKNNYLKHYKMAMFLLVNVTFGMLLFLT | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34865
Sequence Length: 307
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
Q33636 | CKLMAFSSINHLGWMLLAMMNNELLWMTYFLLYSLLSISIIMMFNNFKLFYFNQIFNISMMNPIIKFLIFLNLLSLGGLPPFLGFLPKWLVIQNLTSMNQLFILTISVCLTLITLYFYLRLSYSIFMLNYQKNTWMLKNIYSMKMSSMSLILNFISIGGLLMILMFYMIL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20106
Sequence Length: 170
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
P34848 | MKKISNNIFLIMLIFGTLVTISSNSWLGAWMGLEINLLSFIPLMNDNKKNLLTSESSLKYFLTQAFASSILLFAIIMLMFLYNNNLSLYNSFNEILILSTLLLKSGAAPFHFWFPEVMEGLSWVNGLILMTWQKIAPLMLISYNFIYNFFMISIILSMLIGSLGGLNQTSIRKLMAFSSINHLGWMLLAMMNNEMLWMTYFLMYSLLSFSIVLMFNNFKLFYFNQIFNLSMMNPIIKLLIFLNLLSLGGLPPFLGFLPKWLVIQNLTAMNQLFILTISVCLTLITLYFYLRLSYSIFMLNYQKNSWMLKNNFNNKMSSISLIFNFISIGGLVMISMIYIIM | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39469
Sequence Length: 341
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
P34849 | MFFMNFKYHWFIYFLITIFVLMMNSNNIFIQWMLMEFGTIISISLINIKSTNKTPSLIYYSVSVISSIFLFFMIIVYLSSISFTKTDTFNFMVQMMFFLKIGTFPFHFWMIYSYEMMNWKQIFLMSTLIKFIPIYMMVSMTKINSWTLYFLITNSLYISFYANKFYTLKKLLACSTIFNSFYFIFILELNKNMFIAMIILYSFNYFLLISFLNKFNIQNFNFMFYNKYQMYTFLTLMFNYSMYPIFLSFVIKWNLIFMMVSVKAYNWILFLLMISSMLMIWNYIIILKRVFLKMNFYKNNFIDDKDNKYMYHSYFALTLLSFNISFFITLNFL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40879
Sequence Length: 333
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
O05000 | MKAEFVRILPHMFNLFLAVFPEIFIINATFILLIHGVVFSTSKKYDYPPLASNVGWLGLLSVLITLLLLAAGAPLLTIAHLFWNNLFRRDNFTYFCQIFLLLSTAGTISMCFDFFDQERFDAFEFIVLILLSTCGMLFMISAYDLIAMYLAIELQSLCFYVIAASKRKSEFSTEAGLKYLILGAFSSGILLFPCSMIYGSTGATHFDQLAKILTGYEITGARSSGIFMGILFIAVGFLFKITAVPFHMWAPDIYEGSPTPVTAFLSIAPKISIFANILRVFIYGSYGATLQQIFFFCSIASMILGALAAMAQTKVKRLLAYSSIGHVGYICIGFSCGTIEGIQSLLIGIFIYALMTMDAFAIVLALRQTRVKYIADLGALAKTNPILAITFSITMFSYAGIPPLAGFCSKFYLFFAALGCGAYFLALVGVVTSVIGCFYYIRLVKRMFFDTPRTWILYEPMDRNKSLLLAMTSFFITLFLLYPSPLFSVTHQMALSLYL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55490
Sequence Length: 499
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
P19042 | MIEESKENSLKYFLIQSVASVIFLASILNQSFSFLIPFALLIKIGAAPFHMWLVSISKSMSWKVLSLLMTFQKIGPLLGLAMLSSVSHLSWLMVNMSSFLLMLVYYVTYLAILYFAVILLQQTPMYSLAQMNSNAS | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15331
Sequence Length: 136
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
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