entry
stringlengths 6
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stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
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stringlengths 7
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A6NNZ2
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TBB8B_HUMAN
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Tubulin beta 8B
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MREIVLTQTGQCGNQIGAKFWEVISDEHAIDSAGTYHGDSHLQLERINVHHHEASGGRYVPRAVLVDLEPGTMDSVHSGPFGQVFRPDNFISGQCGAGNNWAKGRYTEGAELTESVMDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIINTFSILPSPKVSDTVVEPYNATLSVHQLIENADETFCIDNEALYDICSRTLKLPTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVAELTQQMFDAKNMMAACDPRHGCYLTVAAIFRGRMPMREVDEQMFNIQDKNSSYFADWFPDNVKTAVCDIPPRGLKMSATFIGNNAAIQELFTCVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDEEYAEEEVA
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Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
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A6P320
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MARHB_RAT
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E3 ubiquitin-protein ligase MARCHF11 (EC 2.3.2.27) (Membrane-associated RING finger protein 11) (Membrane-associated RING-CH protein XI) (MARCH-XI) (RING-type E3 ubiquitin transferase MARCHF11)
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MSDEGSKRGSRADSLEAEPPLPPPPPPPPPGESSLVPTSPRYRPPLPAPLERIVGSGEPPVELAPRRKGEPLPPLPPSRLPGDQEVSAAGDSCEGPRRLPEVKLPEAAAGKGSPAEPEAGACREGERRGTGDQPETRSVYSSRSSSSGGSGDQRSGHQHQHHQPICKICFQGAEQGELLNPCRCDGSVRYTHQLCLLKWISERGSWTCELCCYRYHVTAIKMKQPCQWQSISITLVEKVQMIAVILGSLFLIASVTWLLWSAFSPYAVWQRKDILFQICYGMYGFMDLVCIGLIVHEGAAVYRVFKRWRAVNLHWDVLNYDKATDIEESSRGESSTSRTLWLPLSALRNRNLVHPTQLTSPRFQCGYVLLHLFNRMRAHEDVSEDNGSGEVVMRVTSV
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E3 ubiquitin-protein ligase that mediates polyubiquitination of CD4. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May play a role in ubuquitin-dependent protein sorting in developmenting spermatids.
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A6P6V9
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CBDAS_CANSA
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Cannabidiolic acid synthase (CBDA synthase) (EC 1.21.3.8)
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MKCSTFSFWFVCKIIFFFFSFNIQTSIANPRENFLKCFSQYIPNNATNLKLVYTQNNPLYMSVLNSTIHNLRFTSDTTPKPLVIVTPSHVSHIQGTILCSKKVGLQIRTRSGGHDSEGMSYISQVPFVIVDLRNMRSIKIDVHSQTAWVEAGATLGEVYYWVNEKNENLSLAAGYCPTVCAGGHFGGGGYGPLMRNYGLAADNIIDAHLVNVHGKVLDRKSMGEDLFWALRGGGAESFGIIVAWKIRLVAVPKSTMFSVKKIMEIHELVKLVNKWQNIAYKYDKDLLLMTHFITRNITDNQGKNKTAIHTYFSSVFLGGVDSLVDLMNKSFPELGIKKTDCRQLSWIDTIIFYSGVVNYDTDNFNKEILLDRSAGQNGAFKIKLDYVKKPIPESVFVQILEKLYEEDIGAGMYALYPYGGIMDEISESAIPFPHRAGILYELWYICSWEKQEDNEKHLNWIRNIYNFMTPYVSKNPRLAYLNYRDLDIGINDPKNPNNYTQARIWGEKYFGKNFDRLVKVKTLVDPNNFFRNEQSIPPLPRHRH
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Oxidoreductase involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity. Catalyzes the stereoselective oxidative cyclization of the monoterpene moiety in cannabigerolic acid (CBGA), producing cannabidiolate (CBDA), the major cannabioid in fiber-type Cannabis plants. Can also use cannabinerolic acid as substrate, but not cannabigerol or cannabinerol.
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A6P7H6
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FGF13_XENLA
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Fibroblast growth factor 13 (FGF-13) (xFGF13)
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MAAAIASSLIRQKRQAREREKSNACKCVSSPSKSKGNCEKNKLNVFSRVKLFGSKKRRRRRPEPQLKGIVTKLYSRQGYHLQLQPDGTIDGAKEEESSATVFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSEHFTPECKFKESVFENYYVTYSSMIYRQQHSGRSWFLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVLNGGKSMSQNDST
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Microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules (By similarity). Through its action on microtubules, may participate in the refinement of axons by negatively regulating axonal and leading processes branching (By similarity). Plays a crucial role in neuron polarization and migration (By similarity). Regulates voltage-gated sodium channel transport and function (By similarity). Required for proper head development, it is involved in neural differentiation through regulation of the mek5-erk5 pathway.
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A6PVC2
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TTLL8_HUMAN
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Protein monoglycylase TTLL8 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 8)
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MEPERKGLSLASSSDGDGREENKLKQGISQDLASSSRLDRYKIARQLTEKAIKEKKIFSIYGHYPVVRAALRRKGWVEKKFHFLPKVIPDVEDEGARVNDDTCAKVKENQEMALEKTDNIHDVMSRLVKNEMPYLLWTIKRDIIDYHSLTYDQMLNHYAKTASFTTKIGLCVNMRSLPWYVPANPDSFFPRCYSLCTESEQQEFLEDFRRTMASSILKWVVSHQSCSRSSRSKPRDQREEAGSSDLSSRQDAENAEAKLRGLPGQLVDIACKVCQAYLGQLEHEDIDTSADAVEDLTEAEWEDLTQQYYSLVHGDAFISNSRNYFSQCQALLNRITSVNPQTDIDGLRNIWIIKPAAKSRGRDIVCMDRVEEILELAAADHPLSRDNKWVVQKYIETPLLICDTKFDIRQWFLVTDWNPLTIWFYKESYLRFSTQRFSLDKLDSAIHLCNNAVQKYLKNDVGRSPLLPAHNMWTSTRFQEYLQRQGRGAVWGSVIYPSMKKAIAHAMKVAQDHVEPRKNSFELYGADFVLGRDFRPWLIEINSSPTMHPSTPVTAQLCAQVQEDTIKVAVDRSCDIGNFELLWRQPVVEPPPFSGSDLCVAGVSVRRARRQVLPVCNLKASASLLDAQPLKARGPSAMPDPAQGPPSPALQRDLGLKEEKGLPLALLAPLRGAAESGGAAQPTRTKAAGKVELPACPCRHVDSQAPNTGVPVAQPAKSWDPNQLNAHPLEPVLRGLKTAEGALRPPPGGKGEGTVCSRLPHHGHHVAACQTTGTTWDGGPGVCFLRQLLASELPMGPGLPRDPRAPPCLVCRGLLPPAGPCKRCRSFCAAVLQGASFVRLGGRSCSPRTP
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Monoglycylase which modifies both tubulin and non-tubulin proteins, adding a single glycine to the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of target proteins. Not involved in elongation step of the polyglycylation reaction. Preferentially monoglycylates alpha-tubulin over beta-tubulin. Together with TTLL3, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance. Together with TTLL3, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility. Monoglycylates non-tubulin proteins such as ANP32A, ANP32B, SET, NCL and NAP1.
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A6Q0K5
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CP12_CHLRE
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Calvin cycle protein CP12, chloroplastic (CP12 domain-containing protein) (Chloroplast protein 12)
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MMLTKSVVISRPAVRPVSTRRAVVVRASGQPAVDLNKKVQDAVKEAEDACAKGTSADCAVAWDTVEELSAAVSHKKDAVKADVTLTDPLEAFCKDAPDADECRVYED
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Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues.
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A6QEK3
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HCHA_STAAE
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGINREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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A6QEP0
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CHDC_STAAE
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Coproheme decarboxylase (EC 1.3.98.5) (Coproheme III oxidative decarboxylase) (Hydrogen peroxide-dependent heme synthase)
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MSQAAETLDGWYSLHLFYAVDWASLRIVPKDERDALVTEFQSFLENTATVRSSKSGDQAIYNITGQKADLLLWFLRPEMKSLNHIENEFNKLRIADFLIPTYSYVSVIELSNYLAGKSDEDPYENPHIKARLYPELPHSDYICFYPMNKRRNETYNWYMLTMEERQKLMYDHGMIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFFVGHIINTNEFDQFFAIS
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Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway. The reaction occurs in a stepwise manner with a three-propionate harderoheme intermediate. The first decarboxylation step is fast and yields the three-propionate harderoheme isomer III intermediate, while the slower second decarboxylation appears to control the overall rate. H(2)O(2) is the assumed biological oxidant, but either H(2)O(2) or peracetic acid yields the same intermediates and products. Has weak peroxidase and catalase activities in vitro.
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A6QG31
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ISDA_STAAE
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Iron-regulated surface determinant protein A (Fur-regulated protein A) (Staphylococcal transferrin-binding protein A)
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MTKHYLNSKYQSEQRSSAMKKITMGTASIILGSLVYIGADSQQVNAATEATNATNNQSTQVSQATSQPINFQVQKDGSSEKSHMDDYMQHPGKVIKQNNKYYFQTVLNNASFWKEYKFYNANNQELATTVVNDNKKADTRTINVAVEPGYKSLTTKVHIVVPQINYNHRYTTHLEFEKAIPTLADAAKPNNVKPVQPKPAQPKTPTEQTKPVQPKVEKVKPTVTTTSKVEDNHSTKVVSTDTTKDQTKTQTAHTVKTAQTAQEQNKVQTPVKDVATAKSESNNQAVSDNKSQQTNKVTKHNETPKQASKAKELPKTGLTSVDNFISTVAFATLALLGSLSLLLFKRKESK
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Cell wall-anchored surface receptor that participates in the extraction of heme from oxidized methemoglobin/metHb to enable growth on hemoglobin as a sole iron source. Receives heme from IsdB and transfers it to IsdC (By similarity). Plays also a role in the inhibition of host immune response. Protects S.aureus against the bactericidal protease activity of apolactoferrin. Decreases bacterial cellular hydrophobicity, which renders S.aureus resistant to bactericidal human skin fatty acids as well as to beta-defensins and cathelicidin. Also binds fibronectin and chains B-beta and gamma of fibrinogen, promoting clumping of S.aureus with fibrinogen. Involved in adherence of S.aureus to human desquamated nasal epithelial cells and is required for nasal colonization.
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A6QGC0
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PRKC_STAAE
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Serine/threonine-protein kinase PrkC (Ser/Thr-protein kinase PrkC) (EC 2.7.11.1)
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MIGKIINERYKIVDKLGGGGMSTVYLAEDTILNIKVAIKAIFIPPREKEETLKRFEREVHNSSQLSHQNIVSMIDVDEEDDCYYLVMEYIEGPTLSEYIESHGPLSVDTAINFTNQILDGIKHAHDMRIVHRDIKPQNILIDSNKTLKIFDFGIAKALSETSLTQTNHVLGTVQYFSPEQAKGEATDECTDIYSIGIVLYEMLVGEPPFNGETAVSIAIKHIQDSVPNVTTDVRKDIPQSLSNVILRATEKDKANRYKTIQEMKDDLSSVLHENRANEDVYELDKMKTIAVPLKKEDLAKHISEHKSNQPKRETTQVPIVNGPAHHQQFQKPEGTVYEPKPKKKSTRKIVLLSLIFSLLMIALVSFVAMAMFGNKYEETPDVIGKSVKEAEQIFNKNNLKLGKISRSYSDKYPENEIIKTTPNTGERVERGDSVDVVISKGPEKVKMPNVIGLPKEEALQKLKSLGLKDVTIEKVYNNQAPKGYIANQSVTANTEIAIHDSNIKLYESLGIKQVYVEDFEHKSFSKAKKALEEKGFKVESKEEYSDDIDEGDVISQSPKGKSVDEGSTISFVVSKGKKSDSSDVKTTTESVDVPYTGKNDKSQKVKVYIKDKDNDGSTEKGSFDITSDQRIDIPLRIEKGKTASYIVKVDGKTVAEKEVSYDDV
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Probable protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing either m-Dpm (meso-diaminopimelate) or L-lys, which act as spore germinants. Probably autophosphorylates and phosphorylates FusA (EF-G, elongation factor G) the latter modification is likely necessary for germination in response to peptidoglycan.
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A6QIG7
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CHIPS_STAAE
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Chemotaxis inhibitory protein (CHIPS)
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MKKKLATTVLALSFLTAGISTHHHSAKAFTFEPFPTNEEIESNKKMLEKEKAYKESFKNSGLPTTLGKLDERLRNYLKKGTKNSAQFEKMVILTENKGYYTVYLNTPLAEDRKNVELLGKMYKTYFFKKGESKSSYVINGPGKTNEYAY
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Involved in countering the first line of host defense mechanisms. Specifically inhibits the response of human neutrophils and monocytes to complement anaphylatoxin C5a and formylated peptides, like N-formyl-methionyl-leucyl-phenylalanine (fMLP). Acts by binding directly to the C5a receptor (C5aR) and formylated peptide receptor (FPR), thereby blocking the C5a- and fMLP-induced calcium responses. Prevents phagocytosis of the bacterium.
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A6QLE5
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NLRP3_BOVIN
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NACHT, LRR and PYD domains-containing protein 3 (EC 3.6.4.-)
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MRMVSVRCKLARYLEDLEDIDFKKFKMHLEDYPSQKGCTSIPRGQTEKADHVDLATLMIDFNGEEKAWAMAKWIFAAINRRDLYEKAKREEPEWENANISVLSQEESLEEEWMGLLGYLSRISICRKKKDYCKKYRKYVRSKFQCIKDRNARLGESVNLNKRFTRLRLIKEHRSQQEREHELLAIGRTWAKIQDSPVSSVNLELLFDPEDQHSEPVHTVVFQGAAGIGKTILARKIMLDWASEKLYQDRFDYLFYIHCREVSLGTQRSLGDLIASCCPGPNPPIGKIVSKPSRILFLMDGFDELQGAFDEHTEALCTNWRKVERGDILLSSLIRKRLLPEASLLITTRPVALEKLQHLLGQARHVEILGFSEARRKEYFLKYFSDEQQAREAFRLIQENEILFTMCFIPLVCWIVCTGLKQQMDSGKSLARTSKTTTAVYIFFLSSLLQSQGGSQENHNSATLWGLCSLAADGIWNQKILFQECDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSFIHMTFQEFFAAMYYLLEEDNHGEMRNTPQACSKLPNRDVKVLLENYGKFEKGYLIFVVRFLFGLINQERTSYLEKKLSCKISQKIRLELLKWIEAKANAKTLQIEPSQLELFYCLYEMQEEDFVQRAMSHFPKIEIKLSTRMDHVVSSFCIENCRHVESLSLRLLHNSPKEEEEEEEVRHSHMDRSVLSDFEVAYSQGLVNYLTSSICRGIFSVLSNNWNLTELNLSGNTLGDPGMNVLCETLQQPGCNIRRLWLGQCCLSHQCCFNISSVLSNNQKLVELDLSHNALGDFGIRLLCVGLRHLFCNLKKLWLVSCCLTSASCEDLASVLSTNHSLTRLYLGENALGDSGVGILCEKVKNPHCNLQKLGLVNSGLTSGCCPALSSVLSTNQNLTHLYLQGNALGDMGVKLLCEGLLHRNCKLQVLELDNCSLTSHCCWDLSTLLTSNQSLRKLCLGNNDLGDLGVMLLCEVLKQQGCLLKSLRLCEMYFNYDTKRALETLQEEKPELTIVFEPSR
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Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis. In response to pathogens and other damage-associated signals that affect the integrity of membranes, initiates the formation of the inflammasome polymeric complex composed of NLRP3, CASP1 and PYCARD/ASC. Recruitment of pro-caspase-1 (proCASP1) to the NLRP3 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis. Activation of NLRP3 inflammasome is also required for HMGB1 secretion stimulating inflammatory responses (By similarity). Under resting conditions, ADP-bound NLRP3 is autoinhibited (By similarity). NLRP3 activation stimuli include extracellular ATP, nigericin, reactive oxygen species, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc. Almost all stimuli trigger intracellular K(+) efflux (By similarity). These stimuli lead to membrane perturbation and activation of NLRP3 (By similarity). Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes and formation of an active inflammasome complex. Associates with dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). Shows ATPase activity (By similarity). Independently of inflammasome activation, regulates the differentiation of T helper 2 (Th2) cells and has a role in Th2 cell-dependent asthma and tumor growth. During Th2 differentiation, required for optimal IRF4 binding to IL4 promoter and for IRF4-dependent IL4 transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-3'. May also participate in the transcription of IL5, IL13, GATA3, CCR3, CCR4 and MAF.
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A6QLI1
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VGLU2_BOVIN
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Vesicular glutamate transporter 2 (VGluT2) (Solute carrier family 17 member 6)
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MESVKQRILTPGKEGLKNFAGKSLGQIYRVLEKKQDAGETIELTEDGKPLEVPEKKAPLCDCTCFGLPRRYIIAIMSGLGFCISFGIRCNLGVAIVDMVNNSTIHRGGKVIKEKAKFNWDPETVGMIHGSFFWGYIITQIPGGYIASRLAANRVFGAAILLTSTLNMLIPSAARVHYGCVIFVRILQGLVEGVTYPACHGIWSKWAPPLERSRLATTSFCGSYAGAVIAMPLAGILVQYTGWSSVFYVYGSFGMIWYMFWLLVSYESPAKHPTITDEERRYIEESIGESANLLGAMEKFKTPWRKFFTSMPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFEISKVGMLSAVPHLVMTIIVPIGGQIADFLRSKQILSTTTVRKIMNCGGFGMEATLLLVVGYSHTRGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPIIVGAMTKNKSREEWQYVFLIAALVHYGGVIFYAIFASGEKQPWADPEETSEEKCGFIHEDELDEETGDITQNYINYGTTKSYGATTQANGGWPNGWEKKEEFVQEEVQNSYNYKDRDDYS
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Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as a uniporter which transports preferentially L-glutamate but also, phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane therefore affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, functions as a vesicular K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular L-glutamate uptake. The vesicular H(+)/H(+) antiport activity is electroneutral. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Also involved in the regulation of retinal hyaloid vessel regression during postnatal development (By similarity). May also play a role in the endocrine L-glutamatergic system of other tissues such as pineal gland and pancreas (By similarity).
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A6QLJ0
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ERCC2_BOVIN
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General transcription and DNA repair factor IIH helicase subunit XPD (TFIIH subunit XPD) (EC 3.6.4.12) (CXPD) (DNA excision repair protein ERCC-2) (DNA repair protein complementing XP-D cells) (Xeroderma pigmentosum group D-complementing protein)
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MKLNVDGLLVYFPYDYIYPEQFSYMLELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLSFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQRDSSLPHCRFYEEFDVHGRQVPLPTGIYNLDDLKAVGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQANLETLQKTVLRIKETDEQRLREEYRRLVEGLREASAARETDAHLANPVLPDEVLKEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLYTLEISDLTDFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARADKRGKLPRWIQEHLTDANLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLESEETLRRIEQIAQQL
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ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers.
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A6QLK2
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SOSB1_BOVIN
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SOSS complex subunit B1 (Nucleic acid-binding protein 2) (Oligonucleotide/oligosaccharide-binding fold-containing protein 2B) (Sensor of single-strand DNA complex subunit B1) (Sensor of ssDNA subunit B1) (SOSS-B1) (Single-stranded DNA-binding protein 1)
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MTTETFVKDIKPGLKNLNLIFIVLETGRVTKTKDGHEVRTCKVADKTGSINISVWDDVGNLIQPGDIIRLTKGYASVFKGCLTLYTGRGGDLQKIGEFCMVYSEVPNFSEPNPEYSAQQAPNKTVQNDSGPAAPQPPTGPPATSPASESQNGNGLSAPPGSGGGPHPPHTPSHPPSTRITRSQPNHTAAGPPGPSNNPVSNGKETRRSSKR
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Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways (By similarity).
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A6QLP2
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SAHH3_BOVIN
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Adenosylhomocysteinase 3 (AdoHcyase 3) (EC 3.13.2.1) (IP(3)Rs binding protein released with IP(3) 2) (IRBIT2) (Long-IRBIT)
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MSVQVVSAAAAAKVPEVELKDLSPSEAEPQLGLSTAAVSAMAPPAGGGDPEAPAPAAERPPAPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVKKQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNSKGNSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIILLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY
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May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate (By similarity).
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A6QLT2
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MTMR2_BOVIN
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Myotubularin-related protein 2 (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64)
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MEKSSSCESLGSQPAVARPPSVDSLSSASTSHSENSVHTKSASVVSSDSISTSAENFSPDLRVLRESNKLAEMEEPPLLPGENIKDMAKDVTYICPFTGAVRGTLTVTNYRLYFKSMERDPPFVLDASLGVISRVEKIGGASSRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNNLSLFAFEYKEVFPENGWKLYDSLSEYRRQGIPNESWRITKVNERYELCDTYPALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATITRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPNIEETHWLSNLESTHWLEHIKLILAGALRIADRVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPRRTVSLWSYINSQLEDFTNPLYGSYSNHVLYPVASMRHLELWVGYYVRWNPRMKPQEPIHNRYKELLAKRAELQKKVEELQREISNRSTSSSERAGSPAQCVTPVQTVV
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Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate (By similarity). Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Stabilizes SBF2/MTMR13 at the membranes. Specifically in peripheral nerves, stabilizes SBF2/MTMR13 protein (By similarity).
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A6QLT4
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MTM1_BOVIN
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Myotubularin (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64)
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MASAPTSKYNSHSLENESIKRTSRDGVNRDVGETLPRLPGEIRITDKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSALILDVPLGVISRIEKMGGATSRGENSYGLDITCKDLRNLRFALKQEGHSRRDMFEILTRYAFPLAHSLPIFAFLNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRITFINKCYKLCDTYPALLVVPYRASDEDLRRVATFRSRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKEDERYLDVIRETNRQVNKLTIYDARPNVNAVANKATGGGYESDDVYHNAELFFLDIHNIHVMRESLKKVKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADRVSSGKSSVVVHCSDGWDRTAQLTSLAMLMLDSFYRSIEGFEILVQKEWISFGHKFASRIGHGDKNHADADRSPIFLQFIDCVWQMSKQFPTAFEFNERFLITILDHLYSCRFGTFLYNCESAREKQKVTERTVSLWSLINSNKDKFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRIKQQQPNPVEQRYMELLALRDEYIKRLDELQLANSAKLSDPSASPSSPSQMMPHVQTHF
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Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis. In skeletal muscles, stabilizes MTMR12 protein levels.
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A6QLW8
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S22A7_BOVIN
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Solute carrier family 22 member 7 (Organic anion transporter 2)
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MGFEELLDKVGGFGPFQLRNVALLALPRVLLPMHFLLPIFLAAVPAHRCALPGVPDNFSNEDAWLEAHLPREPDGRLSACLRFTHPQALPNSTLWGEGQNSGEQPEGEPSTVPCPQGWEYNHSEFSSTIATEWDLVCEQKGLNKAISTFFFAGVLVGAEVYGYLSDRFGRRRLLLVAYVSSLALGLASAASVSYIMFAITRTLTGMALAGFTIIVMPLELEWLDVRHRTVAGVLSSTFWTGGVMLLALIGYLIRDWRWLLLTVTLPCVPGILTLWWVPESARWLLTQGRVEEAHRYLLRCARLNGPPVGEDSLSREALNKVAAAERMVRRPSYLDLFRTPRLRYISLCCMVVWFGVNFSYYGVSLDLSGLGLNVYLTQLVFGAVELPSKLLVYLSVRHAGRRLTMAGTLLGAALAVGLRILVSPEMKSWSTALAVMGKAFSEAAFTTAYLFTSELYPTVLRQTGMGLTALVGRLGGSLAPLAALLDGVWLSLPKLAYGGIALLAACTALLLPETKQAQLPETIQDVERKSAPSSLQEEEMPMKQVQD
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Functions as a Na(+)-independent bidirectional multispecific transporter. Contributes to the renal and hepatic elimination of endogenous organic compounds from the systemic circulation into the urine and bile, respectively. Capable of transporting a wide range of purine and pyrimidine nucleobases, nucleosides and nucleotides, with cGMP, 2'deoxyguanosine and GMP being the preferred substrates. Functions as a pH- and chloride-independent cGMP bidirectional facilitative transporter that can regulate both intracellular and extracellular levels of cGMP and may be involved in cGMP signaling pathways. Mediates orotate/glutamate bidirectional exchange and most likely display a physiological role in hepatic release of glutamate into the blood. Involved in renal secretion and possible reabsorption of creatinine. Able to uptake prostaglandin E2 (PGE2) and may contribute to PGE2 renal excretion. Also transports alpha-ketoglutarate and urate. Apart from the orotate/glutamate exchange, the counterions for the uptake of other SLC22A7/OAT2 substrates remain to be identified.
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A6QNM7
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UBP33_BOVIN
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Ubiquitin carboxyl-terminal hydrolase 33 (EC 3.4.19.12) (Deubiquitinating enzyme 33) (Ubiquitin thioesterase 33) (Ubiquitin-specific-processing protease 33)
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MSSFRSHCPHLDSVGEITKEDLIQKSHGSCQDCKVRGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEVFLDRKLGTQPSLPHVKPLHQIQENGVQDFKIPSNTTLKTPLVAVFDDLDIEVEEEDELKARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPTTLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQVMEVEEDPQTIMTEETMEEDKSQSDVDFQSCESCSSSDKAENENGSRSFSEDNNETTMLIQDDENNSEMSKDWQKEKMCNKINKVHSEGELDKDRDSVSETADLNNQETVKVQIHSRASEYITDVHLNDLSTPQILPSNEGVNPRLSASPPKSGNLWPGLPPTHKKVQSALSPKRKKQHKKYRSVISDIFDGTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSIVKAGSCGEAYAPQGWIAFFMEYVKRFVVSCVPSWFWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPVQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQKERRRISNLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGGVPPRKAGYIEDLVLMLPQNIWDNLYSRYGGGPAVNHLYICHTCQIEAEKIEKRRKTELEIFIRLNRAFQEEDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCGNVILRQGADSGQISEETWNFLQSIYGGGPEVILRPPVVHVDPDAVQAEEKIEVETRSL
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Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
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A6QP16
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ZRAN1_BOVIN
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Ubiquitin thioesterase ZRANB1 (EC 3.4.19.12) (Zinc finger Ran-binding domain-containing protein 1)
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MSERGIKWACEYCTYENWPSAIKCTMCRAQRPSGTIITEDPFKSGSSDVGRDWDPSSTEGGSSPLICPDSSARPRVKSSYSMENANKWSCHMCTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSGSRPVAFSVDPCEEYNDRNKLNTRTQHWTCSICTYENWAKAKKCVVCDHPRPNNIEAIEFAETEEASSIINEQDRARWRGSCSSGNSQRRSPPTMKRDSEVKMDFQRIELAGAVGSKEELEVDFKKLKQIKNRMKKTDWLFLNACVGVVEGDLAAIEAYKSSGGDIARQLTADEVRLLNRPSAFDVGYTLVHLAIRFQRQDMLAILLTEVSQQAAKCIPAMVCPELTEQIRREIAASLHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINWSLELATRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLHDCSHWFYTRWKDWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYGNRGAGANLNTDDDVTITFLPLVDSERKLLHVHFLSAQELGNEEQQEKLLREWLDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDRYRQIRPCTSLSDGEEDEDDEDE
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Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (By similarity). Positive regulator of the Wnt signaling pathway that deubiquitinates APC protein, a negative regulator of Wnt-mediated transcription (By similarity). Acts as a regulator of autophagy by mediating deubiquitination of PIK3C3/VPS34, thereby promoting autophagosome maturation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the stress fiber dynamics and cell migration (By similarity).
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A6QP84
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SOAT_BOVIN
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Sodium-dependent organic anion transporter (Soat) (Solute carrier family 10 member 6) (SLC10A6)
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MRANCSSGLACPANSSEEELPEGLKAFGNLDLVFTVVSALMIGLLMFSLGCSVEVQKLWGHIRRPWGIAVGMLCQFGLMPLIAYLLIISFSLKPLQAIAVLIMGCCPGGTVSNIFTFWVDGDMDLSISMTTCSTMAALGMMPLCLYLYTLSWNLEQNLTIPYQNIGITLVCLIIPVAFGIYVNYRWPKQSKIILKIGAIAGGLLFLVVTGAGMVLMKEFWSSDIILLMISFIFPLIGHATGFLLALLTHQSWQRCRTISLETGTQNVQMCFTMLQLSFTAEQLVQIFGFVLAYGLFQMLNGFFMVAAYKMYKRRLKNKHGNEKPSCQEARHRKKSTSPKETTAFLEVNEEATLSPGPSGPVDPHGAPTPTGDIARAK
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Transports sulfoconjugated steroid hormones from the extracellular compartment into the cytosol in a sodium-dependent manner without hydrolysis. Steroid sulfate hormones are commonly considered to be biologically inactive metabolites, that may be activated by steroid sulfatases into free steroids (By similarity). May play an important role by delivering sulfoconjugated steroids to specific target cells in reproductive organs (By similarity). May play a role transporting the estriol precursor 16alpha-hydroxydehydroepiandrosterone 3-sulfate (16a-OH-DHEAS) at the fetal blood vessel endothelium (By similarity). Can also transport other sulfoconjugated molecules such as taurolithocholic acid-3-sulfate and sulfoconjugated pyrenes (By similarity).
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A6QPB3
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COHA1_BOVIN
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Collagen alpha-1(XVII) chain (180 kDa bullous pemphigoid antigen 2) (Bullous pemphigoid antigen 2) [Cleaved into: 120 kDa linear IgA disease antigen homolog]
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MDITQKNKRDGTEVTERIITETVTTRLTSLPPKGGTSNGYAKTGSLGGGSRLEKQSLTHGSSGYINSSGSLRGNASTSSYRRAHSPASTLPNSPGSTFERKTHVTRHGTYEGSSSGNSSPEYPRKEFASSSTRGRSQTRESEIRVRLQSASPSTRWTELDDVKRLLKGSRSASVSPTRNSSNTLPIPKKGTVETKVVTASSQSVSGTYDTTILDANLPSHVWSSTLPAGSSMGTYHNNITTQSSSLLNTNAYSAGSVFGVPNNMASCSATLQPGISTSSSVFGMQNNLAPSSSTLSHGMAATSTAYGVKKNMPQSPTAVSTGVSTSAASTTNVQNDDLLHKDCKFLILEKDNTPAKKEMELLIMTKDSGKVFTASPASVAATSFSEDTLKKEKQAAYTDTYLVSEANGDVKTVTAKGNGASADIHGYDHRRGGGGGGGSGGALGSGAAGGGGKGSWGAAPTWCPCGSWCSWWKWLLGLLLTWLLLLGLLFGLIALAEEVRKLKARVEELEKMRGRLSYNEKMERSSQDSVQGVAPRLGEGLGKSELDDYNLEDVWQFMKVRLMTEQENGNLRGSPGPKGDMGVQGPKGDRGFPGTPGIPGPLGHQGPEGPKGQKGNVGEPGMEGPMGQRGREGPMGPRGEPGPPGFGEKGDRGDAGKPGIPGPPGVPGSVGPKGSIGPQGLRGEVGLPGIKGDKGPMGPPGPKGDQGEKGPRGLTGEPGLKGLPGAVGEPGAKGAMGPAGPDGHQGPRGEQGLPGMPGTRGLPGPSGDPGKPGLTGPQGPQGIPGTPGRPGVKGEPGAPGKIMTSEGSSTITVPGPPGPPGAMGPPGPPGAPGPVGPAGLPGQQGPRGEPGLAGESFMGSSSSFSEVLSTQGIDLRGPPGPPGPPGPPGEGLPGPPGPPGSLLTSSETFFSGPPGPPGPPGPKGDQGPPGPRGHQGERGFPGLSGSGSSSLGLNLQGPPGPPGPQGPKGDKGDPGVPGAPGIPGGPSRGGSSSSTTFMQGPPGPPGPPGPPGSLSSSGLEIQQYISDYMQSDSIRPYLSGVQGPPGPPGPPGPVTTITGETFNYSELASLVVSYLQTSGYNIGTSSTSISSEDILAALRRDDVRQYLQQYLMPQGAGGDWFLQSLDYAELSNRILSYMSSTGVSIGLPGPPGPPGLPGTSYEELLSLLQGSEFRGIVGPPGPPGPPGLPGSSWSSISTEDLSSYLQTAGLSSIPGPPGPPGPPGPRGPPGISGALATYAAENSDSFRSELISYLTSPDVRSFIVGPPGPPGPQGPPGDTRLVSTDSSYSRSGSSSSFSRDTSYSSSMGIGGASGGSLGEAGAFGMDMGRGYGAAAESGMYGGNGRFGTSFAGGLDYNELAVRVSESLQRQGLLQGMAYTVQGPPGRPGPQGPPGISKIFSAYSNVTEDLMDFFRTYGAIPGPPGQKGEMGIPGPKGERGPAGPPGPRGHKGEKGDKGDQFYIGRRRRSIAVKP
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May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane. The 120 kDa linear IgA disease antigen homolog is an anchoring filament component involved in dermal-epidermal cohesion.
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A6QQJ8
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ZC12A_BOVIN
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Ribonuclease ZC3H12A (EC 3.1.-.-) (Zinc finger CCCH domain-containing protein 12A)
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MSLWELEDRRSCQGTPRPAQEPTAEEATTAELQMKVDFFRKLGYSSAEIHSVLQKLGIQADTNTVLGELVKHGSAAERERQASPDPCPQLPLVPRGGGTPKAPTVETYPPEEDKEGSDLRPIVIDGSNVAMSHGNKDVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRDLEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAFESDGIVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLTSEHKKQPCPYGRKCTYGIKCRFLHPERPSRPQRSVADELRANALLPPSRAASKDKNSRRPSPSSQPGSLPTEHEQCSPDRKKLGAQASPGTPREGLMQTFAPTGRSLPPSGSSGGSFGPSEWFPQTLDSLPYASQDCLDSGIGSLESQMSELWGVRGGGPGEPGPPRGPYAGYCTYGAELPATPAFSAFSRALGAGHFSVPADYAPPPAAFPPREYWSEPYQLPPPTQRLQEPQAPGPGADRGPWGGAGRLAKERASVYTKLCGVFPPHLVEAVMSRFPQLLDPQQLAAEILSYKSQHLSE
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Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay. Modulates the inflammatory response by promoting the degradation of a set of translationally active cytokine-induced inflammation-related mRNAs, such as IL6 and IL12B, during the early phase of inflammation. Prevents aberrant T-cell-mediated immune reaction by degradation of multiple mRNAs controlling T-cell activation, such as those encoding cytokines (IL6 and IL2), cell surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription factor (REL). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (By similarity). Together with RC3H1, destabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR (By similarity). Self regulates by destabilizing its own mRNA. Cleaves mRNA harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-dependent manner (By similarity). Plays a role in the inhibition of microRNAs (miRNAs) biogenesis (By similarity). Cleaves the terminal loop of a set of precursor miRNAs (pre-miRNAs) important for the regulation of the inflammatory response leading to their degradation, and thus preventing the biosynthesis of mature miRNAs (By similarity). Also plays a role in promoting angiogenesis in response to inflammatory cytokines by inhibiting the production of antiangiogenic microRNAs via its anti-dicer RNase activity (By similarity). Affects the overall ubiquitination of cellular proteins. Positively regulates deubiquitinase activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains on TNF receptor-associated factors (TRAFs), preventing JNK and NF-kappa-B signaling pathway activation, and hence negatively regulating macrophage-mediated inflammatory response and immune homeostasis (By similarity). Induces also deubiquitination of the transcription factor HIF1A, probably leading to its stabilization and nuclear import, thereby positively regulating the expression of proangiogenic HIF1A-targeted genes. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (By similarity). Prevents stress granules (SGs) formation and promotes macrophage apoptosis under stress conditions, including arsenite-induced oxidative stress, heat shock, and energy deprivation. Plays a role in the regulation of macrophage polarization promotes IL4-induced polarization of macrophages M1 into anti-inflammatory M2 state. May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis (By similarity). Functions as a positive regulator of glial differentiation of neuroprogenitor cells through an amyloid precursor protein (APP)-dependent signaling pathway (By similarity). Attenuates septic myocardial contractile dysfunction in response to lipopolysaccharide (LPS) by reducing I-kappa-B-kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial pro-inflammatory cytokine production (By similarity).
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A6QQL0
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S15A4_BOVIN
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Solute carrier family 15 member 4 (Peptide/histidine transporter 1)
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MEGAGDERAPLLGARRTAFAGRRAACAAVLLTELLERAAFYGVTANLVLFLNGTAFGWEGAEASQALLLFMGLTYLVSPFGGWLADARLGRARAILLSLALYLLGMLAFPLLAAPATRSALCGAPGPTNVRNCSAPPCTDTPTRYCAPAVLSALALVGLGVGAVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAIVSLGGIAYIQQNVSFVTGYAIPAVCIGVAFVVFLCGQTFFITKPPDGSAFTDMFRILVYSCRPQKRIREHSPSGEGIGVFQQSSKHSLFDSCKMSRGGPFPEDKVEDVKALVKIVPVFLALIPYWTVYFQMQTTYVLQSLHLKIPEISSITTNPHTFPAAWLTMFDAVLILLLIPLKDKLVDPILKRNGLLPSSLKRIAVGMFFVMCSAFAAGILESKRLDLVKEKTINQTIGNVVYYAADLPIWWQVPQYVLIGVSEIFASIAGLEFAYSAAPKSMQSAIMGLFFFFSGVGSFVGSGLLALVSLKAIGWMSSHTDFGNINGCYLNYYFFLLAAIQGATLLLFLIVSVKYDRQRSRANGTPASRRT
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Proton-coupled amino-acid transporter that mediates the transmembrane transport of L-histidine and some di- and tripeptides from inside the lysosome to the cytosol, and plays a key role in innate immune response. Able to transport a variety of di- and tripeptides, including carnosine and some peptidoglycans (By similarity). Transporter activity is pH-dependent and maximized in the acidic lysosomal environment (By similarity). Involved in the detection of microbial pathogens by toll-like receptors (TLRs) and NOD-like receptors (NLRs), probably by mediating transport of bacterial peptidoglycans across the endolysosomal membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand, and L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate (tri-DAP), the NOD1 ligand. Required for TLR7, TLR8 and TLR9-mediated type I interferon (IFN-I) productions in plasmacytoid dendritic cells (pDCs). Independently of its transporter activity, also promotes the recruitment of innate immune adapter TASL to endolysosome downstream of TLR7, TLR8 and TLR9: TASL recruitment leads to the specific recruitment and activation of IRF5 (By similarity). Required for isotype class switch recombination to IgG2c isotype in response to TLR9 stimulation. Required for mast cell secretory-granule homeostasis by limiting mast cell functions and inflammatory responses (By similarity).
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A6QR55
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UBP4_BOVIN
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Ubiquitin carboxyl-terminal hydrolase 4 (EC 3.4.19.12) (Deubiquitinating enzyme 4) (Ubiquitin thioesterase 4) (Ubiquitin-specific-processing protease 4)
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MAEGGGYRERPDAETQKSELGALMRTTLQRGAQWYLIDSRWFKQWKKYVGFDSWDMYNVGEHNLYPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPAEAWNKLLNWYGCVEGQQPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQNEDGTWPRQTQQSKSSTAPSRNFTTSPKSSASPYSSVSASPIANGDSTNTSGMHSSGVSRGGSGFSASYNCQESPLTHVQPGLCGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFLLDGLHEDLNRVKKKPYLELKDANGRPDAVVAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRVMEIFLVPADPRCRPTQYRVVVPLMGAVSDLCEALSKLSGIAAENMVVTDVYNHRFHKIFQMDEGLNHIMPRDDIFVYEVCSTSPDGSECVTLPVYFRERKSRPSSTSTGAVLYGQPLLVSVPKHKLTLESLYQAVCERISRYIKQPLPDESGSSPLELGACNGSRSGCAGEDEEEMEHQEEGREQLSETEGSGDDEPGSDHGEATQKKNKGRPCPRRLFTFSLVNSYGTADINSLATDGKLLKLNSRSTLAIDWDSETRSCYYNEQESETYEKHVSMLQPQKKKKTAVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVRGLNMSEFVCDPSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLACEDQIVTKAAYVLFYQRRDDEFHKTPSLSFPGSSDGGARPSSSQQGTGDDETYSMDTN
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Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins. Deubiquitinates PDPK1. Deubiquitinates TRIM21. Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface. Deubiquitinates HAS2. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER.
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A6R8Q8
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ARO1_AJECN
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MGVPTKISILGRESIVADFGIWRNYVAKDLLSSCSSSTYVLISDTNLTPLYLEGFQKSFEDAATNVSPKPRLLTYEIPPGESSKSRETKADIEDWMLARQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALERDAETILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECISIGMVKEAELARHLGILNNVSVSRISKCLANYGLPTSLKDQRIKKLTAGKHCSVEQLIAYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKGLDVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWEDEGEVLVVSGKGGRMEASSSELYVGNAGTASRFLTTVATLARKSSVDSSVLTGNARMKQRPIGDLVDALAANGASIEYLENLGCLPLKIAASGGFAGGEINLAAKVSSQYVSSLLMCAPYAKTPVTLRLVGGKPISQPYIDMTTAMMRSFGVEVKKSETEEHTYHIPLGFYTNPVEYIVESDASSATYPLAAAAITGTSCTVPNIGSKSLQGDARFAVDVLRPMGCAVDQNDFSTRVTGPPGGILSPLPNINMEPMTDAFLTASVLAAVARGKGSNRTTRIFGIANQRVKECNRIKAMKDELAKFGVVCREHDDGLEIDGIDRATLHHPSDGVYCYDDHRVAMSFSVLSLVAHEPTLILEKECVGKTWPGWWDCLSQTFKVKLDGKEVGKRTETNPIVHVNKSAASIFIIGMRGAGKTTSGFWVSKALQRPFIDLDDELERTEAYVEDMMSVWLRRKPWYEECSNVQYYSRLTGLDGMTQVSGGFNRFLKVITGEVDSLAKMRRKQNTFFVSLTLPDLGLAAHILKEVTLGSDAVELRVDLLKDPQSDNEIPSVDYVAEQISVLRSRTSVPLVFTIRTKGQGGRFPDDAYDAALQLYRLAVRMGSEFVDLEISFPEQLLRTVTEMKGFSTIIASHHDPKGQLSWVNGSWIQFYNKALQYGDVIKLVGVARSIDDNISLKKFKTWAEEKHNIPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKAKKFAVIGNPVSASRSPAMHNTLFRQMGLPHTYGTLETDNPEVAKEFIRSPGFGGASVTIPLKLSIMPLLDEIAPEAMSIGAVNTIVCAPPAPDSKSQTPRLIGHNTDWQGMVRCLSDAGAYAAATPTTASAGLVIGGGGTARAAIFALQNMGYSPIYVLGRSPDKLSSMTSTFHTDHDIRILEDVKALESLPTVAIGTIPGDKPIEPHMREILCKLFDLCEKANSDTEQARGVSTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTNITPVYEYARCWKVYDVKLINCERGNAISLLVLEAFTHAFYEHPVLNHSS
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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A6T7D6
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PYRC_KLEP7
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Dihydroorotase (DHOase) (EC 3.5.2.3)
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MTAQSQVLKIRRPDDWHIHLRDDDMLKTVVPYTSEFYGRAIVMPNLVPPVTTVAAAIAYRQRIMDAVPAGHDFTPLMTCYLTDSLDPAELERGFNEGVFTAAKLYPANATTNSSHGVTSTDAIMPVLERMEKLGMPLLVHGEVTHAEIDIFDREARFIETVMEPLRQRLPGLKVVFEHITTKDAAEYVRDGNELLAATITPQHLMFNRNHMLVGGIRPHLYCLPVLKRNIHQQALRELVASGFSRAFLGTDSAPHARHRKEASCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSLNGPRFYGLPVNESYVELVREETTVVDSIALPNDTLVPFLAGETVRWTVKK
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Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:20676924}.
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A6T923
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HPXO_KLEP7
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FAD-dependent urate hydroxylase (EC 1.14.13.113) (FAD-dependent urate oxidase)
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MKAIVIGAGIGGLSAAVALKQSGIDCDVYEAVKEIKPVGAAISVWPNGVKCMAHLGMGDIMETFGGPLRRMAYRDFRSGENMTQFSLAPLIERTGSRPCPVSRAELQREMLDYWGRDSVQFGKRVTRCEEDADGVTVWFTDGSSASGDLLIAADGSHSALRPWVLGFTPQRRYAGYVNWNGLVEIDEALAPGDQWTTFVGEGKRVSLMPVSAGRFYFFFDVPLPAGLAEDRDTLRADLSRYFAGWAPPVQKLIAALDPQTTNRIEIHDIEPFSRLVRGRVALLGDAGHSTTPDIGQGGCAAMEDAVVLGAVFRQTRDIAAALREYEAQRCDRVRDLVLKARKRCDITHGKDMQLTEAWYQELREETGERIINGMCDTILSGPLG
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Catalyzes the hydroxylation of urate to 5-hydroxyisourate (HIU).
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A6TGM4
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FADB_KLEP7
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGHALDVLEKQSDLKGLLLRSEKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTISAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIAAGKDVGADQALKIGLVDGVVAAEKLRDGALAILRQAMNGDLDWKAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARLGREEALVLENKSFVPLAHTNEARALVGIFLNDQYVKAKAKKLTKDVETPKHAAVLGAGIMGGGIAYQSAWKGVPVVMKDISDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIQPTLEYSGFDRVDVVVEAVVENPKVKKAVLAETESKVRPDTVLASNTSTIPISELASVLQRPENFCGMHFFNPVHRMPLVEVIRGEKTSDNTIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKDDSKGKPKKEEDAAVDSLLADVSQPKRDFSDEEIIARMMIPMVNEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTIGSAKYLDMAQQYQHLGPLYEVPAGLRDKARHNEAYYPQVEPARPVGALKTA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A6TZ28
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HCHA_STAA2
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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A6X8Z5
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RHG31_MOUSE
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Rho GTPase-activating protein 31 (Cdc42 GTPase-activating protein)
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MKNKGAKQKLKRKGAASAFGCDLTEYLESSGQDVPYVLKSCAEFIETHGIVDGIYRLSGITSNIQRLRQEFGSDQCPDLTREVYLQDIHCVGSLCKLYFRELPNPLLTYELYEKFTEAVSHRPEEGQLARIQNVILELPPPHYRTLEYLIRHLAHIASFSSKTNMHARNLALVWAPNLLRSKKIEATICNGDAAFLAVRVQQVVIEFILNHADQIFNGGAPGALQQDESRTITKSLTLPALSLPMKLVSLEEAQARSLATNHPARKERRENSLPEIVPPPFHTVLELPDNKRKLSSKSKKWKSIFNLGRSGSDSKSKLSRNGSVFVRGQRLSVEKATIRPAKSMDSLCSVPVEGKENKGNFSRTVTTGGFFIPATKMHASSTGSSCDLSKEGEWGQEGMPAGAEGGCEVGGQIRPLPEQLKVFRPIGDPESEQSAPKLLGMFYTSSDSPGKSVFTSSLFQMEPSPRHQRKALNISEPFAVSVPLRVSAVISTNSTPCRTPPKELQSLSSLEEFSFQGSESGGWPEEEKPLGAESFPGSVTKKAATEDTKPEPEVPGRAECSQSPPLDPGTQVEKKTLHVSLGSQVSKEAEKRPKAEKVMEESQGASQPKPSTPQESLGAGTEPLILHEMDEEDLAQALIWPEIQQELKIIESEEEFSSLPPAAQKTSPIPESSPAPFPFPEAPGSLPSSSAPREVWTRDAANQSIQEAAILTDREKLEPVCSLLESESQQELSPDPASLAPLEMLLFEKVSSPARIEIGGPRNLSPPLTPAPPPPTPLEEEPEVLLSKEGPDREDAARDSRTDVYTEQPTPKESPGIPTPCQREEAIASPNEKQNARHAVPENKGPGLPSPTKEVDIIPQEEGGAPHSAQEPSDCDEDDTVTDPAQHGLEMVEPWEEPQWVTSPLHSPTLKEVQESQTQGSQGHRLERRLCHRPSLRQSHSLDSKTTGNSHWTLEAPFSSSCANLETERNYEPLQPPAARTKIAGLEEKALKAFREFSGLKGLEVLPSQKGPSGIQPKPVETNFMGLAEGKEQEPQLELSNRQMKHSDVPGPDSSKESSPRAQDSTLPGEHPLQLQLKNTECGPSKGKHRPSSLNLDSATPIADLFRLENGAPFSSPGIELSELGDTKVTWMSSSHCKAAPWNSQDTQDLDIVAHTLTGRRNSAPVSVSAVRTSFMVKMCQAKAVPVIPPKIQYTQIPQPLPSQSTGEGGAQPLERSQEEPGSTPEIPQKSTKDDSPSSLGSPEEEQPKQETGASASRRQASITSCMYEGSSCSPEPSASTLASTQDAVVQCRKRTSETEPSGDNLLSSKLERASGGPKAFHRSRPGRPQSLILFPIMDHLPSSPTVIDSKVLLSPIRSPTQTVSPGLLCGELAENTWITPEGVTLRNKMTIPKNGQRLETSTSCFYQPQRRSVILDGRSGRQIE
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Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration.
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A6X935
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ITIH4_MOUSE
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Inter alpha-trypsin inhibitor, heavy chain 4 (ITI heavy chain H4) (ITI-HC4) (Inter-alpha-inhibitor heavy chain 4)
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MKSPAPAHMWNLVLFLPSLLAVLPTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADAVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYSAAVGRGESAGIVKTTGRQTEKFEVSVNVAPGSKITFELIYQELLQRRLGMYELLLKVRPQQLVKHLQMDIYIFEPQGISILETESTFMTPELANALTTSQNKTKAHIRFKPTLSQQQKSQSEQDTVLNGDFIVRYDVNRSDSGGSIQIEEGYFVHHFAPENLPTMSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNYASRIRAHGGTNINNAVLLAVELLDRSNQAELLPSKSVSLIILLTDGDPTVGETNPTIIQNNVREAINGQYSLFCLGFGFDVNYPFLEKMALDNGGLARRIYEDSDSALQLQDFYHEVANPLLSSVAFEYPSDAVEEVTRYKFQHHFKGSEMVVAGKLQDQGPDVLLAKVSGQMHMQNITFQTEASVAQQEKEFKSPKYIFHNFMERLWALLTIQQQLEQRISASGAELEALEAQVLNLSLKYNFVTPLTHMVVTKPEGQEQFQVAEKPVEVGDGMQRLPLAAQAHPFRPPVRGSKLMTVLKGSRSQIPRLGDAVRASRQYIPPGFPGPPGPPGFPAPPGPPGFPAPPGPPLASGSDFSLQPSYERMLSLPSVAAQYPADPHLVVTEKSKESTIPEESPNPDHPQVPTITLPLPGSSVDQLCVDILHSEKPMKLFVDPSQGLEVTGKYENTGFSWLEVTIQKPHLQVHATPERLVVTRGRKNTEYKWKKTLFSVLPGLKMTMNMMGLLQLSGPDKVTIGLLSLDDPQRGLMLLLNDTQHFSNNVKGELGQFYRDIVWEPPVEPDNTKRTVKVQGVDYLATRELKLSYQEGFPGAEISCWTVEI
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Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration.
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A6XH05
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CINS1_SALFT
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Cineole synthase 1, chloroplastic (Sf-CinS1) (EC 4.2.3.108) (Alpha-pinene synthase) (EC 4.2.3.-) (Alpha-terpineol synthase) (EC 4.2.3.111) (Beta-pinene synthase) (EC 4.2.3.-) (Myrcene synthase) (EC 4.2.3.15) (Sabinene synthase) (EC 4.2.3.-)
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MSSLIMQVVIPKPAKFFHNNLFSLSSKRHRFSTTTTTRGGRWARCSLQTGNEIQTERRTGGYQPTLWDFSTIQSFDSEYKEEKHLMRAAGMIDQVKMMLQEEVDSIRRLELIDDLRRLGISCHFEREIVEILNSKYYTNNEIDERDLYSTALRFRLLRQYDFSVSQEVFDCFKNAKGTDFKPSLVDDTRGLLQLYEASFLSAQGEETLRLARDFATKFLQKRVLVDKDINLLSSIERALELPTHWRVQMPNARSFIDAYKRRPDMNPTVLELAKLDFNMVQAQFQQELKEASRWWNSTGLVHELPFVRDRIVECYYWTTGVVERRQHGYERIMLTKINALVTTIDDVFDIYGTLEELQLFTTAIQRWDIESMKQLPPYMQICYLALFNFVNEMAYDTLRDKGFDSTPYLRKVWVGLIESYLIEAKWYYKGHKPSLEEYMKNSWISIGGIPILSHLFFRLTDSIEEEAAESMHKYHDIVRASCTILRLADDMGTSLDEVERGDVPKSVQCYMNEKNASEEEAREHVRSLIDQTWKMMNKEMMTSSFSKYFVEVSANLARMAQWIYQHESDGFGMQHSLVNKMLRDLLFHRYE
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Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products, components of the chemical defense arsenal. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into 1,8-cineole, and, as minor products, alpha-terpineol, beta-pinene, alpha-pinene, sabinene and myrcene.
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A6XH06
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SABS1_SALPM
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Sabinene synthase 1, chloroplastic (Sp-SabS1) (EC 4.2.3.-) (Myrcene synthase) (EC 4.2.3.15)
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MPLNSLHNLERKPSKAWSTSCTAPAARLQASFSLQQEEPRQIRRSGDYQPSLWDFNYIQSLNTPYKEQRYVNRQAELIMQVRMLLKVKMEAIQQLELIDDLQYLGLSYFFPDEIKQILSSIHNEHRYFHNNDLYLTALGFRILRQHGFNVSEDVFDCFKTEKCSDFNANLAQDTKGMLQLYEASFLLREGEDTLELARRFSTRSLREKLDEDGDEIDEDLSSWIRHSLDLPLHWRIQGLEARWFLDAYARRPDMNPLIFKLAKLNFNIVQATYQEELKDVSRWWNSSCLAEKLPFVRDRIVECFFWAIGAFEPHQYSYQRKMAAIIITFVTIIDDVYDVYGTLEELELFTDMIRRWDNISISQLPYYMQVCYLALYNFVSERAYDILKDQHFNSIPYLQRSWVSLVEGYLKEAYWYYNGYKPSLEEYLNNAKISISAPTIISQLYFTLANSTDETVIESLYEYHNILYLSGTILRLADDLGTSQHELERGDVPKAIQCYMKDTNASEREAVEHVKFLIRETWKEMNTVTTASDCPFTDDLVAVATNLARAAQFIYLDGDGHGVQHSEIHQQMGGLLFQPYV
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Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products, components of the chemical defense arsenal. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into sabinene, and, as minor products, myrcene.
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A6XIP3
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GP_HAZVJ
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Envelopment polyprotein (M polyprotein) [Cleaved into: GP38; Glycoprotein N (Gn) (Glycoprotein G2); Non-Structural protein M (NSm); Glycoprotein C (Gc) (Glycoprotein G1)]
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MEGSYWWLSLLALLAWGANGESTSPAETSPAPTTPNPPVVNPSLRRKIVNQRILSAMGMDSDPSNEALNGVCQSIHSNGCNANELKLRLADFFIDTNSSQCYDEILVKKPCSSLTPAHNSHWVPRGLDKSEVDKIFDTKLKLFFSQSRKVTCLSASALNPSQFVKHFQVKIQETSGPAKQSLRSLHCVNLVWSHSHKGEKEVVHVLQSAVPVKLKNCLAMLNFRQCYYNQQSEGPVVVPSYQHNGEKWVTGAYTMTVEVDKHADGPCEISTTCITEGSEIKPGVHSLRGFKTTLVIHGKRNTGRRLLSSSNARQECSSGTFLGEGGSAQVVGPKNDGPGDHITFCNGSVVTKIRLGQEHGCYTVRRIKTYRNCRPEEGSSACEVDDELKPCGAQKCMNVHLSVKGLVKTSRGSNVQVHSCDKDCLIQIPEGFGDIQIDCPGGTQHYLESNVLDVDCPMYNRLGGLMLYFCRMSHRPRTCLALFIWLGAGYGITCIAGYMVYYAILALSMLTRCLKRKYMVKGDFCLKCEQKCVTSLDQTLHDESCSYNICPYCGNRLPEEGLRRHVPSCPKRKQRLEEIDLYLDYLLVPCPLHFALSTAVKLGTLLKRLSWVTVFLCLFLTAIAPVQGQVTTSPVLPSNQSTECTLLPPPVFLIFSAVLMSKTLKRMGPVNKVGAAGHSARRTNSPKNLYKSKQIANTKSGPREPRRRVVVKALLILTASSALQSIHLAQAFDSGSLPEGAWEEEMQLVQGCNQECSLEEDECSCPDGQSMTRKLLFFKGLNSAASKMASSHRLLTSVSIDTPWGAIKVESTYKPRLASSNIQLAWNSIEEQGDKVILSGKSTSIIKLEEKTGMQWSLGSESAAEEKRLLVSILDYTQVYSSTFQYITGDRTVSEWPKATCTGDCPDRCGCSTSSCLYKSWPHSRNWRCNPTWCWGVGTGCTCCGVDILRPFNKYFVTKWTTEYVRTDVLVCVELTDQERHCDVVEAGSQFVIGPVRVVVSDPQNVQTKLPSEILTIQKLEGNQVVDIMHATSIVSAKNACKLQSCTHGSPGDMQILHTDNLIQHSHDGGLNLADLNPLVNSTWMSWEGCDLDYYCTTGSWPSCTYTGINSENTESFDNLLNTESNLCERFHFHSKRISASGSTLQMDLKGRPNSGGGELSVLVDVKGLELHSKKISLKGLSFKTLSCSGCYACSSGLSCTVEVRIERPDEFTVHLRSVSPDIAVAEGSIIARRMTGGPLSRLRAFAVRKVKKICFEIVEKSYCKDCKNEDTTKCIEVELQPPKDILLEHKGTIIKRQNETCVSGLQCWTESASSFVSGVGSFFRNYLGSITLGIVLTLLPVAVVLLFFCYGDKLFKLCSCFRCCRGLSRGKVRKELDEDELRNKLKKFSKEGELFGKEKKDARTIALLLSGKGKNYKELV
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[Glycoprotein N]: Glycoprotein N and glycoprotein C interact with each other and are present at the surface of the virion. Glycoprotein N probably locks the Gn-Gc complex in a prefusion state. Glycoprotein N and glycoprotein C are able to attach the virion to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis.
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A6XKM2
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CXA1_URSAM
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Gap junction alpha-1 protein (Connexin-43) (Cx43)
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MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGKSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNSKKLATGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI
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Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract. May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles (By similarity).
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A6XMY0
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ARA1_HYAAR
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Arasin 1 (Ara-1) (Proline-rich antimicrobial peptide) (PR-AMP) (Pro-rich AMP)
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MERRTLLVVLLVCSCVVAAAAEASPSRWPSPGRPRPFPGRPKPIFRPRPCNCYAPPCPCDRWRH
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Antimicrobial peptide that has a large activity spectrum with activity against Gram-positive, Gram-negative bacteria, as well as against fungi. Shows activity at micromolar concentrations. Displays minimal inhibitory concentration (MIC) values lower than minimal bactericidal concentrations (MBC). Synthetic peptides with similar activities than the full length peptide (composed of the first 23 or 25 amino acids (Arasin 1(26-48) or Arasin 1(26-50))) may have a dual mode of action depending on the peptide concentrations. At MIC concentrations, the peptide penetrates into the cytoplasm of target cells (tested on the Gram-negative E.Coli). The two inner membrane proteins YgdD and SbmA may be required for this uptake. At concentrations higher than MIC, arasin may act by disrupting membranes. Full-length and N-terminal peptides do not show hemolytic activity.
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A6XNC6
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UGFGT_MEDTR
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Flavonoid 3-O-glucosyltransferase (EC 2.4.1.-) (UDP glucose:flavonoid 3-O-glucosyltransferase) (UDP-glycosyltransferase 78G1)
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MSTFKNEMNGNNLLHVAVLAFPFGTHAAPLLSLVKKIATEAPKVTFSFFCTTTTNDTLFSRSNEFLPNIKYYNVHDGLPKGYVSSGNPREPIFLFIKAMQENFKHVIDEAVAETGKNITCLVTDAFFWFGADLAEEMHAKWVPLWTAGPHSLLTHVYTDLIREKTGSKEVHDVKSIDVLPGFPELKASDLPEGVIKDIDVPFATMLHKMGLELPRANAVAINSFATIHPLIENELNSKFKLLLNVGPFNLTTPQRKVSDEHGCLEWLDQHENSSVVYISFGSVVTPPPHELTALAESLEECGFPFIWSFRGDPKEKLPKGFLERTKTKGKIVAWAPQVEILKHSSVGVFLTHSGWNSVLECIVGGVPMISRPFFGDQGLNTILTESVLEIGVGVDNGVLTKESIKKALELTMSSEKGGIMRQKIVKLKESAFKAVEQNGTSAMDFTTLIQIVTS
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Catalyzes the glycosylation of flavonoids at the 3-O-position. Glycosylates the 7-O-position if the 3-O-position is not available. Also able to perform 3-O-glycosylation of anthocyanidins.
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A6Y9S5
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LGA1_HYPJE
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L-threo-3-deoxy-hexylosonate aldolase (EC 4.1.2.54) (L-threo-3-deoxy-hexulosonate aldolase)
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MAPPSLPCGIYAPTMTFFHPESEDIDIPTIKHHAQRLAKAGLAGLVVMGSNGEAVHCTRDEKIAVLSATREALDAAGFQSVPVLFGATEGSVRGTIELCKLAAAAGAAAALVLPPSYYRAQTDEASIEAYFVAVADASPIPLVLYNYPGAVSGIDMDSDLLIRLAQHKNIVGTKFTCGNTGKLTRVALATDAKTPFRDGSGYMAFGGMCDFTLQTLVSGGSGIIAGGANVMPKLCVKVWDSYSQGNRDEAEKLQKVLSRGDWPLTKAAIAGTKSAIQTYYGYGGYPRRPLKRLEQARVSAIEEGIREAMEIEKTL
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Mediates the conversion of 2-dehydro-3-deoxy-L-galactonate to pyruvate and L-glyceraldehyde in D-galacturonate catabolic process.
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A6YFB5
|
HTRA1_XENLA
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Serine protease HTRA1 (EC 3.4.21.-) (High-temperature requirement A serine peptidase 1) (Serine protease 11)
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MTMLWLAVLLTCGAPAALLPTSGVGCPARCDPSSCSPAPTNCQSGETALRCGCCSVCAAAENERCGEGPEDPLCASGLRCVRNGGVTRCQCPSNQPVCGSDGKTYSSLCRLQAESKAVQGRGVAAIIPIQRGDCQQGQKDPDSPRYKYNFIADVVEKIAPAVVHIELFRILPFFKREVPAASGSGFIVSEDGLILTNAHVVTNKHRLKVERSDGSTYDAQIIDVDEKADIALIKIKAKGKLPVLLLGRSEELRPGEFVVAIGSPFSLQNTVTTGIVSTAQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVVGINTLKVTAGISFAIPSDKIRKFMAESHNRQSTGQGTKKKKYLGIRMMSLSQGKLKELKEQVKDFPENTSGAYIVEVLPDTPAEEAGLKEGDIIISISGKTVTSSSEVSEAIKKEGTLQMVIRRGNEDIPISVTPKEIEF
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Serine protease with a variety of targets, including extracellular matrix proteins and proteoglycans such as biglycan, syndecan-4 and glypican-4. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Consequently, facilitates inductive processes in the developing embryo, such as posteriorization, mesoderm induction and neuronal differentiation. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. Consequently, may regulate many physiological processes. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets.
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A6YP92
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ARX_RAT
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Homeobox protein ARX (Aristaless-related homeobox)
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MSNQYQEEGCSERPECKSKSPTLLSSYCIDSILGRRSPCKMRLLGAAQSLPAPLASRTDQEKAMQGSPKGSSAPFEAELHLPPKLRRLYGPGGGRLLQGAAAAAAAAAAAAAAAATATGTAGPRGEVPPPPPPAARPGERQDSAGAVAAAAAAAWDTLKISQAPQVSISRSKSYRENGAPFVPPPPALDELGGPGGVAHPEERLSAASGPGSAPAAGGGTGTEEDEEELLEDEEDEDEEEELLEDDEEELLEDDARALLKEPRRCSVATTGTVAAAAAAAAAAAAVATEGGELSPKEELLLHPEDAEGKDGEDSVCLSAGSDSEEGLLKRKQRRYRTTFTSYQLEELERAFQKTHYPDVFTREELAMRLDLTEARVQVWFQNRRAKWRKREKAGAQTHPPGLPFPGPLSATHPLSPYLDASPFPPHHPALDSAWTAAAAAAAAAFPSLPPPPGSASLPPSGAPLGLSTFLGAAVFRHPAFISPAFGRLFSTMAPLTSASTAAALLRQPTPAVEGAVASGALADPATAAADRRASSIAALRLKAKEHAAQLTQLNILPGTSTGKEVC
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Transcription factor. Binds to specific sequence motif 5'-TAATTA-3' in regulatory elements of target genes, such as histone demethylase KDM5C. Positively modulates transcription of KDM5C. Activates expression of KDM5C synergistically with histone lysine demethylase PHF8 and perhaps in competition with transcription regulator ZNF711 synergy may be related to enrichment of histone H3K4me3 in regulatory elements. Required for normal brain development (By similarity). Plays a role in neuronal proliferation, interneuronal migration and differentiation in the embryonic forebrain. May also be involved in axonal guidance in the floor plate (By similarity).
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A6YSL1
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RNC1_MAIZE
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Ribonuclease III domain-containing protein RNC1, chloroplastic (Chloroplast ribonuclease III domain protein)
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MGPPAMAFQALTLTPLPFSLHSSSRRVRVLAVAADQTPPPAPPSEPANSPSRLLRELAQRKKAVSPKKKHPPRRFILKPPLDDERLTRRFLSSPQLSLKALPLLSSCLPSAPLSTADRTWMDEYLLEAKQALGYPLAPSETLGEGDDCPARHFDVLFYLAFQHLDPSSERTRMRHVRNGHSRLWFLGQYVLELAFCEFFLQRYPRESPGPMRERVFALIGKKVLPRWLKAASLHNLVFPYDDLDKMIRKDREPPSKAVFWAIFGAIYLCFGMPEVYRVLFEAFGMDPDDESCQPKLRRQLEDVDYVSVEFEKRQLTWQDVAAYRPPPDALFAHPRLFRACVPPGMHRFRGNIWDFDSRPKVMTTLGYPLPMNDRIPEITEARNIELGLGLQLCFLHPSKHKFEHPRFCYERLEYVGQKIQDLVMAERLLMKHLDAPGRWLAEKHRRTLMNKYCGRYLRDKHLQHYIIYGETVQDRFEHNRRLRNPSTTSVQQALHGLAYCVYGKPDVRRLMFEVFDFEQVQPKAV
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Binds specific group II introns in chloroplasts and facilitates their splicing. Acts on both subgroup IIA and subgroup IIB introns. The substrates of the subgroup II also require the CRM domain proteins CAF1 or CAF2. Binds both single-stranded and double-stranded RNA non-specifically, but lacks endonuclease activity. Required for plastid ribosome biogenesis.
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A6ZM04
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PIF1_YEAS7
|
ATP-dependent DNA helicase PIF1 (EC 3.6.4.12) (DNA repair and recombination helicase PIF1) (Petite integration frequency protein 1) (Telomere stability protein 1)
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MPKWIRSTLNHIIPRRPFICSFNSFLLLKNVSHAKLSFSMSSRGFRSNNFIQAQLKHPSILSKEDLDLLSDSDDWEEPDCIQLETEKQEKKIITDIHKEDPVDKKPMRDKNVMNFINKDSPLSWNDMFKPSIIQPPQLISENSFDQSSQKKSRSTGFKNPLRPALKKESSFDELQNSSISQERSLEMINENEKKKMQFGEKIAVLTQRPSFTELQNDQDDSNLNPHNGVKVKIPICLSKEQESIIKLAENGHNIFYTGSAGTGKSILLREMIKVLKGIYGRENVAVTASTGLAACNIGGITIHSFAGIGLGKGDADKLYKKVRRSRKHLRRWENIGALVVDEISMLDAELLDKLDFIARKIRKNHQPFGGIQLIFCGDFFQLPPVSKDPNRPTKFAFESKAWKEGVKMTIMLQKVFRQRGDVKFIDMLNRMRLGNIDDETEREFKKLSRPLPDDEIIPAELYSTRMEVERANNSRLSKLPGQVHIFNAIDGGALEDEELKERLLQNFLAPKELHLKVGAQVMMVKNLDATLVNGSLGKVIEFMDPETYFCYEALTNDPSMPPEKLETWAENPSKLKAAMEREQSDGEESAVASRKSSVKEGFAKSDIGEPVSPLDSSVFDFMKRVKTDDEVVLENIKRKEQLMQTIHQNSAGKRRLPLVRFKASDMSTRMVLVEPEDWAIEDENEKPLVSRVQLPLMLAWSLSIHKSQGQTLPKVKVDLRRVFEKGQAYVALSRAVSREGLQVLNFDRTRIKAHQKVIDFYLTLSSAESAYKQLEADEQVKKRKLDYAPGPKYKAKSKSKSNSPAPISATTQSNSGIAAMLQRHSRKRFQLKKESNSNQVHSLVSDEPRGQDTEDHILE
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DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule of ATP. Processes at an unwinding rate of about 75 bp/s. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Involved in the maintenance of ribosomal (rDNA). Required for efficient fork arrest at the replication fork barrier within rDNA. Involved in the maintenance of mitochondrial (mtDNA). Required to maintain mtDNA under conditions that introduce dsDNA breaks in mtDNA, either preventing or repairing dsDNA breaks. May inhibit replication progression to allow time for repair. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. May have a role in conjunction with DNA2 helicase/nuclease in 5'-flap extension during Okazaki fragment processing (By similarity). {ECO:0000255|HAMAP-Rule:MF_03176}.
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A6ZXH8
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ATG9_YEAS7
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Autophagy-related protein 9 (Cytoplasm to vacuole targeting protein 7)
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MERDEYQLPNSHGKNTFLSRIFGLQSDEVNPSLNSQEMSNFPLPDIERGSSLLHSTNDSREDVDENDLRVPESDQGTSTEEEDEVDEEQVQAYAPQISDGLNGDHQLNSVTSKENVLETEKSNLERLVEGSTDDSVPKVGQLSSEEEEDNEFINNDGFDDDTPLFQKSKIHEFSSKKSNTIEDGKRPLFFRHIYQNNRPQRDTQKLFTSSNAIHHDKDKSANNGPRNINGNQKHGTKYFGSATQPRFTGSPLNNTNRFTKLFPLRKPNLLSNISVLNNTPEDRINTLSVKERALWKWANVENLDIFLQDVYNYYLGNGFYCIILEKILNICTLLFVVFVSTYMGHCVDYSKLPTSHRVSDIIIDKCYSNSITGFTKFFLWMFYFFVILKIVQLYFDVQKLSELQNFYKYLLNISDDELQTLPWQNVIQQLMYLKDQNAMTANVVEVKAKNRIDAHDVANRIMRRENYLIALYNSDILNLSLPIPLFRTNVLTKTLEWNINLCVMGFVFNESGFIKQSILKPSQREFTREELQKRFMLAGFLNIILAPFLVTYFVLLYFFRYFNEYKTSPGSIGARQYTPIAEWKFREYNELYHIFKKRISLSTTLANKYVDQFPKEKTNLFLKFVSFICGSFVAILAFLTVFDPENFLNFEITSDRSVIFYITILGAIWSVSRNTITQEYHVFDPEETLKELYEYTHYLPKEWEGRYHKEEIKLEFCKLYNLRIVILLRELTSLMITPFVLWFSLPSSAGRIVDFFRENSEYVDGLGYVCKYAMFNMKNIDGEDTHSMDEDSLTKKIAVNGSHTLNSKRRSKFTAEDHSDKDLANNKMLQSYVYFMDDYSNSENLTGKYQLPAKKGYPNNEGDSFLNNKYSWRKQFQPGQKPELFRIGKHALGPGHNISPAIYSTRNPGKNWDNNNNGDDIKNGTNNATAKNDDNNGNNDHEYVLTESFLDSGAFPNHDVIDHNKMLNSNYNGNGILNKGGVLGLVKEYYKKSDVGR
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Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking. Recruits vesicle-tethering proteins TRS85 and YPT1 to the autophagosome formation site. Recruits also ATG23 and ATG8 to the PAS.
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A6ZY89
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ARO1_YEAS7
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALILAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTPSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVATPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREGWYKECSNFSFFAPHCSAETEFQALRRSFSKYIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTKKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKIIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFVPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKAPFKAIFDAVTKE
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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A7BFV8
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SPT_BACTC
|
Serine palmitoyltransferase (SPT) (EC 2.3.1.50)
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MKHNLQDNLQGEQMANTNSNGGKKPFSDAKIIERANLLRDNDLYFFFRAIEETEASTVTVKGKKQIMIGSNNYLGLTHHPAVKEAAIKAVEKYGTGCTGSRFLNGNLNIHEELDEKLAAYLGHEKAIVFSTGMQANLGALSAICGPKDLMLFDSENHASIIDASRLSLGTTFKYKHNDMASLEELLESNMSRFNRVIIVADGVFSMTGDILRLPEVVKLAKKYGAYVYVDDAHGLGVMGPQGRGTMAHFDVTKDVDFNMGTFSKSFASIGGVISGSKDAIDYVRHSARSFMFSASMPPAAVATVSACIDVVQNDETILNNLWSNVEFMRNGFKELGFFTYGSQTPIIPLFIGDDMKALKMTKWLESKGVFCTPVLPPAVPKGETLIRTSYMASHNREDLSTVLEVFAEAKKIFDIPNHLH
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Catalyzes the condensation of L-serine with palmitoyl-CoA (hexadecanoyl-CoA) to produce 3-oxosphinganine.
|
A7BHQ9
|
TYRO_PHONA
|
Tyrosinase (EC 1.14.18.1)
|
MSRVVITGVSGTIANRLEINDFVKNDKFFSLYIQALQVMSSVPPQENVRSFFQIGGIHGLPYTPWDGITGDQPFDPNTQWGGYCTHGSVLFPTWHRPYVLLYEQILHKHVQDIAATYTTSDKAAWVQAAANLRQPYWDWAANAVPPDQVIVSKKVTITGSNGHKVEVDNPLYHYKFHPIDSSFPRPYSEWPTTLRQPNSSRPNATDNVAKLRNVLRASQENITSNTYSMLTRVHTWKAFSNHTVGDGGSTSNSLEAIHDGIHVDVGGGGHMGDPAVAAFDPIFFLHHCNVDRLLSLWAAINPGVWVSPGDSEDGTFILPPEAPVDVSTPLTPFSNTETTFWASGGITDTTKLGYTYPEFNGLDLGNAQAVKAAIGNIVNRLYGASVFSGFAAATSAIGAGSVASLAADVPLEKAPAPAPEAAAQPPVPAPAHVEPAVRAVSVHAAAAQPHAEPPVHVSAGGHPSPHGFYDWTARIEFKKYEFGSSFSVLLFLGPVPEDPEQWLVSPNFVGAHHAFVNSAAGHCANCRSQGNVVVEGFVHLTKYISEHAGLRSLNPEVVEPYLTNELHWRVLKADGSVGQLESLEVSVYGTPMNLPVGAMFPVPGNRRHFHGITHGRVGGSRHAIV
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This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.
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A7DTF0
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MRG1_CAEEL
|
Mortality factor related protein 1
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MSSKKNFEVGENVACIYKGKPYDAKITDIKTNSDGKELYCVHFKGWNNRYDEKIPVGEEKDRIFKGTASEYAEKHNAELPTTALKPKKKSLAAEAPRDDRDDTPGTSKGKKAKSVTIAPVMTADDMKVELPKPLRKILIDDYDLVCRYFINIVPHEYSVDQIIEDYIKTIPVSNEQMRTVDDLLIEYEEADIKITNLALICTARGLVDYFNVTLGSSYQLLYKFERPQYNDLVKKRAMEKGIDITNPTALQDSGFRPSQEYGIVHFLRMLAKLPDYLKLTQWNDHVINRIMIGVHDLIVFLNKNHGKYYRGSSDYQGASNDYYRRSLAADDGVGANQ
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Protein involved in the remodeling of chromatin thereby regulating various processes including transcription, chromosome synapsis and genome integrity. Mainly binds genomic loci carrying trimethylated histone H3 'Lys-36' (H3K36me3) or 'Lys-4' (H3K4me3), and acetylated histone H3 'Lys-9' (H3K9ac), 'Lys-27' (H3K27ac). During meiosis, required for the presynaptic pairing of homologous chromosomal regions outside of the pairing center and for the progression of chromosome synapsis. Essential maternal factor required in postembryonic germline development and in maintaining germ cell identity. Plays an important role in maintaining genomic integrity in primordial germ cells (PGCs) during meiosis by regulating DNA double-strand break (DSB) repair and synapsis. Also, required for chromatin-based transcriptional silencing in PGCs and for silencing of X-linked genes in the maternal germ line. By retaining histone acetyltransferase, cbp-1, in euchromatin, promotes the anchoring of heterochromatin at the inner nuclear membrane in intestinal and hypodermal cells.
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A7DY56
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TRN1_COCOF
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Tropinone reductase (EC 1.1.1.206) (EC 1.1.1.236)
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MANLRESSRDKSRWSLEGMTALVTGGSKGIGEAVVEELAMLGARVHTCARDETQLQESLREWQAKGFQVTTSVCDVSSRDQREKLMETVSSLFQGKLNILVNNAGTCITKPTIDYTSEDFSFLMSTNLESSFHLSQLAHPLLKSSGLGSIVLISSVASVVHVNVGSIYGATKGAMNQLARNLACEWASDSIKVNSVCPGFISTPLASNYFRNEEFKKEVENIIPTGRVGEANEVSSLVAYLCLPAASYVTGQTICVDGGFSVNGFTFKSLPLR
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Oxidoreductase having both tropinone reductase I and II activities. Involved in the tropane alkaloids calystegines and cochlearine biosynthesis. Can use tropinone and nortropinone as substrates and produces both tropine and pseudotropine. Able to oxidize pseudotropine in the reverse reaction.
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A7E2V4
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ZSWM8_HUMAN
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Zinc finger SWIM domain-containing protein 8
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MELMFAEWEDGERFSFEDSDRFEEDSLCSFISEAESLCQNWRGWRKQSAGPNSPTGGGGGGGSGGTRMRDGLVIPLVELSAKQVAFHIPFEVVEKVYPPVPEQLQLRIAFWSFPENEEDIRLYSCLANGSADEFQRGDQLFRMRAVKDPLQIGFHLSATVVPPQMVPPKGAYNVAVMFDRCRVTSCSCTCGAGAKWCTHVVALCLFRIHNASAVCLRAPVSESLSRLQRDQLQKFAQYLISELPQQILPTAQRLLDELLSSQSTAINTVCGAPDPTAGPSASDQSTWYLDESTLTDNIKKTLHKFCGPSPVVFSDVNSMYLSSTEPPAAAEWACLLRPLRGREPEGVWNLLSIVREMFKRRDSNAAPLLEILTDQCLTYEQITGWWYSVRTSASHSSASGHTGRSNGQSEVAAHACASMCDEMVTLWRLAVLDPALSPQRRRELCTQLRQWQLKVIENVKRGQHKKTLERLFPGFRPAVEACYFNWEEAYPLPGVTYSGTDRKLALCWARALPSRPGASRSGGLEESRDRPRPLPTEPAVRPKEPGTKRKGLGEGVPSSQRGPRRLSAEGGDKALHKMGPGGGKAKALGGAGSGSKGSAGGGSKRRLSSEDSSLEPDLAEMSLDDSSLALGAEASTFGGFPESPPPCPLHGGSRGPSTFLPEPPDTYEEDGGVYFSEGPEPPTASVGPPGLLPGDVCTQDDLPSTDESGNGLPKTKEAAPAVGEEDDDYQAYYLNAQDGAGGEEEKAEGGAGEEHDLFAGLKPLEQESRMEVLFACAEALHAHGYSSEASRLTVELAQDLLANPPDLKVEPPPAKGKKNKVSTSRQTWVATNTLSKAAFLLTVLSERPEHHNLAFRVGMFALELQRPPASTKALEVKLAYQESEVAALLKKIPLGPSEMSTMRCRAEELREGTLCDYRPVLPLMLASFIFDVLCAPGSRPPSRNWNSETPGDEELGFEAAVAALGMKTTVSEAEHPLLCEGTRREKGDLALALMITYKDDQAKLKKILDKLLDRESQTHKPQTLSSFYSSSRPTTASQRSPSKHGGPSAPGALQPLTSGSAGPAQPGSVAGAGPGPTEGFTEKNVPESSPHSPCEGLPSEAALTPRPEGKVPSRLALGSRGGYNGRGWGSPGRPKKKHTGMASIDSSAPETTSDSSPTLSRRPLRGGWAPTSWGRGQDSDSISSSSSDSLGSSSSSGSRRASASGGARAKTVEVGRYKGRRPESHAPHVPNQPSEAAAHFYFELAKTVLIKAGGNSSTSIFTHPSSSGGHQGPHRNLHLCAFEIGLYALGLHNFVSPNWLSRTYSSHVSWITGQAMEIGSAALTILVECWDGHLTPPEVASLADRASRARDSNMVRAAAELALSCLPHAHALNPNEIQRALVQCKEQDNLMLEKACMAVEEAAKGGGVYPEVLFEVAHQWFWLYEQTAGGSSTAREGATSCSASGIRAGGEAGRGMPEGRGGPGTEPVTVAAAAVTAAATVVPVISVGSSLYPGPGLGHGHSPGLHPYTALQPHLPCSPQYLTHPAHPAHPMPHMPRPAVFPVPSSAYPQGVHPAFLGAQYPYSVTPPSLAATAVSFPVPSMAPITVHPYHTEPGLPLPTSVACELWGQGTVSSVHPASTFPAIQGASLPALTTQPSPLVSGGFPPPEEETHSQPVNPHSLHHLHAAYRVGMLALEMLGRRAHNDHPNNFSRSPPYTDDVKWLLGLAAKLGVNYVHQFCVGAAKGVLSPFVLQEIVMETLQRLSPAHAHNHLRAPAFHQLVQRCQQAYMQYIHHRLIHLTPADYDDFVNAIRSARSAFCLTPMGMMQFNDILQNLKRSKQTKELWQRVSLEMATFSP
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Substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex that promotes target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs). The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquitination and subsequent degradation of AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs for degradation. Specifically recognizes and binds AGO proteins when they are engaged with a TDMD target. May also act as a regulator of axon guidance: specifically recognizes misfolded ROBO3 and promotes its ubiquitination and subsequent degradation.
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A7E2Y1
|
MYH7B_HUMAN
|
Myosin-7B (Antigen MLAA-21) (Myosin cardiac muscle beta chain) (Myosin heavy chain 7B, cardiac muscle beta isoform) (Slow A MYH14)
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MSGNKRGSRASCPHRGAECLLPWAALNLQGFQLLLLHPSATAMMDVSELGESARYLRQGYQEMTKVHTIPWDGKKRVWVPDEQDAYVEAEVKSEATGGRVTVETKDQKVLMVREAELQPMNPPRFDLLEDMAMMTHLNEASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFKAGLLGVLEELRDQRLAKVLTLLQARSRGRLMRLEYQRLLGGRDALFTIQWNIRAFNAVKNWSWMKLFFKMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPKHKE
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Involved in muscle contraction.
|
A7E320
|
UHRF1_BOVIN
|
E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)
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MWIQVRTMDGKVAHTVDSLSRLTKVEELRKKIQELFHVEPGLQRLFYRGKQMEDGHTLFDYDVRLNDTIQLLVRQSLVLPVPVPSSSGGSKERDSELSDTDSGCGLAQSESDKSSNSGEAANEPEGKADEDECDETELGLYKVGEYVDARDTNMGAWFEAKVIRVTRKAPAHDQPSSSSSKPEDDIIYHVTYDDYPENGVVQMTSQNVRARARHTIKWEDLQVGQVVMVNYNPDLPKDRGFWYDAEILRKRETRTARELHANVRIGGDSLNDCRIVFVDEVFKIERPGEGNPMVENPMRRKSGPSCKHCKDDERKLCRMCACHVCGGKQDPDKQLMCDECDMAFHIYCLRPPLSSVPPEEEWYCPDCRIDSSEVVQAGEKLKESKKKAKMASATSSSQRDWGKGMACVGRTKECTIVPSNHFGPIPGIPVGTMWRFRVQVSESGVHRPHVAGIHGRSNHGAYSLVLAGGYEDDVDHGNSFTYTGSGGRDLSGNKRTAEQSCDQKLTNTNRALALNCFAPINDLKGAEAKDWRSGKPVRVVRNVKGRKHSKYAPIEGNRYDGIYKVVRYWPEKGKSGFLVWRFLLRRDDVEPGPWTKEGKDRIKKLGLTMQYPEGYLEALARKEKENSKQAALDKEEEDGEEGFTSPRKGKRKSKSAGGDGSSRGTPKKTKVEPYSLTTQQSSLIKEDKSNMKLWTEILKSLKDGPKFLSKVEETFQCICCQELVFRPITTVCQHNVCKDCLDRSFKAQVFSCPACRYDLGRSYAMTVNQPLQAVLSQLFPGYGSGR
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Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. Plays a role in DNA repair by cooperating with UHRF1 to ensure recruitment of FANCD2 to interstrand cross-links (ICLs) leading to FANCD2 activation (By similarity).
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A7E3N2
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NCF2_RAT
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Neutrophil cytosol factor 2 (NCF-2) (Neutrophil NADPH oxidase factor 2)
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MSLAEAIRLWNEGVQAADKKDWKGALEAFSEVQDPHSRICFNIGCMYTILDNLQEAEQAFTKSINRDKHLAVAYFQRGMLYYSMEKYRPASVGRKAALLFLGSYNLVARIIVGYPLSPGKVLYNIALMHAKKEEWKKAEEQLALATNMKSEPRHSKIDKAMESIWKRCPTSHLPLDPPQVTMALWFEEGGVGKRSVVASVVHQDNFSGFAPLQPQSAEPPPRPKTPEIFRALEGEAHRVLFGFVPETPEELQVMPGNIVFVLKKGSDNWATVMFNGQKGLVPCNYLEPVELRIHPQSQPQEDTSLESDIPPPPNSSPPERLQLSPGWCQQLGPLRCPPFLLHQEVKRSVPMPYMLKVHYKYTVVMETQLGLPYSQLRNMVSKKLELLPEHTKLSYQRRDSPELLLLSEESMKDAWAQVKNYCLTLWCEHTVGDQGFVDEPKEKENSDADNRTTEPQPKEGTQVVAIFSYDATQPEDLEFVEGDVILVLSHVNEEWLEGECKGKIGIFPKAFVEGCAAKNLEGTPREV
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NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).
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A7E3S4
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RAF1_BOVIN
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RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
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MEHIQGAWKTISNGFGFKDTVFDGTSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTVGDGGVPALPSLTMRRMRESVSRIPPGSQHRYSTPHAFTFSASSPSSEGSLSQRQRSTSTPNVHMVSATLPVDSRMIEDAIRSHSESGSPSALSSSPNNLSPTGWSQPKTPAPAQRERAPGSSTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSILWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF
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Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation (By similarity).
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A7EK16
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MYO1_SCLS1
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Myosin-1 (Class I unconventional myosin) (Type I myosin)
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MGISRRPKADKNASAADSAPGGKPNIQKAQFDTTKKKEVGVSDLTLISKVSNEAINENLKKRFDNREIYTYIGHVLVSVNPFRDLGIYTDAVLESYKGKNRLEMPPHVFAVAESAYYNMNAYKDNQCVIISGESGAGKTEAAKRIMQYIANVSGGSNSSIQETKEMVLATNPLLESFGNAKTLRNNNSSRFGKYLQLQFNAQGEPVGADITNYLLEKTRVVTQIKDERNFHIFYQFTKGASQAYRESYGIQQPSQYLYTSKAGCFDVDGIDDLAEYQDTLQAMKVIGLSQAEQDEIFRMLAAILWTGNIQFREGDDGYATVVDQSVVDFLAYLLDVDAAHVIQAITIRILTPRNGEVIESPANVPQAMATRDALAKAIYNNLFDWIVERVNKSLTARAETSNSIGILDIYGFEIFEQNSFEQLCINYVNEKLQQIFIQLTLKTEQEEYAREQIKWTPIKYFDNKIVCDLIEAIRPPGVFSAMKDATKTAHADPAACDRTFMQAISGMSNPHLTPRQGNFIIKHYAGDVSYTVEGITDKNKDQLLKGLLNLFGQSRNHFIHELFPHQVDQDNRKQPPSAGDKIKASANDLVTTLMKATPSYIRTIKPNENKSPTEYNEKNVLHQVKYLGLQENVRIRRAGFAYRQTFDKFVERFYLLSPKTSYAGDYIWTGDSKTGAMQILKDTNIPVEEYQMGVTKAFIKAPETLFALEHMRDRYWHNMAARIQRVWRAFLQIRIEAATRIQRMFRKKREGKEFLELREKGHQILQGRKERRRYSLLGSRRFMGDYLGIAATTGPGSKIRGSINLPASEVTLFSCRGEILETKFGRSSKLSPRIFIMTRTKFYIVSQLLVNKQVQIAVEKAIPLGAIKFVSISTCRDDWFSLGVGSPQEADPLLTCVFKTELFTHMQAAMPGGGFNLKIGDSIEYAKKPNKMQLIKVVKDSQQAQDHYKSATIHTQAGEPPNSRSKPLPKGKPVAAKPFTSGRLIKPGGPGGRPSRLTNGNRPTPKPVPTPAPAAARPVPAVNPVAASIPVHTRNTSVQSTQSTRAVPPPPPPAPPAPPPAPVSKEPQYRVLYEFAGQSANEFSLKQGEIVTVLQKETNGWWLTKNVRGQGWAPTAYLEEVTPPPPPPVATRPAPPPAPGPPKMNGTNGAAIRSKPTPPAPPAKRPAAGRKPAPPPAPRDSGMSISSNGSGNNSGRSTPTPSLAGGLAEALRARQSAMQGNAKREDEDDW
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Type-I myosin implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions as actin nucleation-promoting factor (NPF) for the Arp2/3 complex (By similarity).
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A7F0W2
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ATG1_SCLS1
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Serine/threonine-protein kinase ATG1 (EC 2.7.11.1) (Autophagy-related protein 1)
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MASKTPSSSSSRRPRNVGVGSFTINEEIGKGSFATVYRGTHVPSGSLVAIKSVNLGRLNKKLKDNLYVEIEILKSLHHPHIVALMDCRESTSHIHLMMEYCELGDLSYFIKKRDKLADNPSLFDMIRKYPMPVDGGLNQVVVRHFFKQLSSAMEFLRDRDFVHRDVKPQNLLLIPSPDWMAKSKNGPEAMKASKESIVPMVGINSLPMLKLADFGFARSLPSTSLAETLCGSPLYMAPEILRYEKYDARADLWSIGTVLYEMMTGKPPFRAANHVELLRKIEQNEDEIRFPSKTVFSRDLKDIARRFLKKRPEDRITFPEYFAHPVVTGPIPGLVGEDLPKEIITPSRSPEASVARHPSLRERQRENPTPKPVETTYESLIARDIGEQAPRSPHIEANQPVEIPGHKSGRPGSRDRPSAISAATAPNVDTLPRQRDRTERHYAPIGRPVSRKPSYDEQANLPVQEEIRSSDSITEAEQDVRDAREYVLVEKKAVEVNAFADEMAASPRLAHANHIPKQPTRRHTSMGAPNSTSGAVAVPPSRAVQKAQGNTRPDTSSARNSYGSYGKTGSSPSTASAIAKALQGASVRVFGVSWSPTLIGKGPSPQQLYNPYPAYPTPNTGFIGDARPIDEDQRVVNVIEDSATRSDVVYGFAEVKYRQLIPLAPSMNHGLGGPNNEKVGDAMDEDDGLTVEAIVNLSEEALVLYVKSLSLLSKSMDIAGAWWLRKNRGGVISGGHTPGSDSSSAVQAGNRINGAVQWVRTRFNEVLEKAELVRLKLVEAQKRLPEDHPGHPSNHATASKIVGGSSTTDGVVLSSGITAEKLMYDRALEMSRTAAINELANEDLPGCEISYTTAIRMLEAVLENDEELIPRKRSPSLREDKEKCDGGEVNGINFGDRKDVLKVLQMIRTRLHVLKKKMAVIARHQSMPPPSSPRHSHSGGTTPTIANTPPH
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Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8.
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A7F7H0
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ARO1_SCLS1
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MGSTTFENPTRIEILGKEDIIVDFDIWRNFVAEDLLSDLPSSTYVLITDTNLSPLYVPAFQQSFEALAAKSSSTPRLLTYEIPPGENSKSRETKAEIEDWMLSHQCTRDSVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLVGAFWQPQRIYIDLRFLETLPVREFINGMAEVVKTAAIWDEAEFSALEDNANLIMTTIRAKNTDCSTRLGPIRDILKRIVLGSAKTKADVVSADEREGGLRNILNFGHSIGHAFEAILTPQVLHGEAVAIGMVKEAELARHLGVLKPGAVARLVKCIASYGLPTSLADKRIQKLTAGKLCPVDVLLEKMGVDKKNDGRKKKIVLLSAIGKTYEPKASVVEDRSIRVVLSDSVEVRPSVPETLNVEVTPPGSKSISNRALVLAALGTGPCRIKNLLHSDDVEFMLTSIGKLGGATYAWEDAGEVLCVQGKGGDLHASPTELYIGNAGTASRFLTTVVSLCKPSASTKSTILTGNARMKVRPIGPLVDSLRANGVDIEYLEKEHSLPLNVAASGGFTGGDINLAATVSSQYVSSLLMCAPYAKNPVTLRLVGGKPISQLYIDMTTAMMAAFGIHVVRSQTEEHTYHIPQGVYKNPEEYVVESDASSATYPLAVAAISGTTCTIPNIGCKSIQGDARFAIDVLKPMGCKVVQTDYSTTVTGPPIGSLQAIEEVDMEPMTDAFLTASVLGAVAKGTTKIRGIANQRVKECNRIKAMKDELAKFGVTCRELEDGIEVDGVPIKDLKHPAEGIHCYDDHRVAMSFSVLSVAASQPVLIEERECVGKTWPGWWDILSKSFQVELAGKEVKATHSKKIGIPALPDKSIFIIGMRGAGKTTAGAWAAKILGRPYKDLDVELERISGMSIPDMVRSKGWDFFRAAELDLLKHCLTDQPEKHVFACGGGVVEMPEARELLINFHKSGGIVLLVHRDTEQVMDYLRIDKTRPAYVEDMMGVYSRRKPWFNECSNFQYHSKGSGASALSVAEQDFARFLHHISGKSLHFDEMRNKPQSFFVSLTMPDISGAAYILPSVAVGSDAVEVRVDLLEDPSSTNGIPGTDFLSVQIAHLRSVVHLPVIFTVRTVSQGGRFPDAAHEEALKLYKLAVKMGIEYIDLEIAFPDELLQEVTEAKGFSRIIASHHDPQGTLSWKNGGWFQHYNRALQYGDIIKLVGSAKSIEDNFALAKFKKTMAAAHDTPLIAINMGVTGKLSRVLNGFMTPVSHPSLPFKAAPGQLSAAEIRSTLSTLGEIEPKSFYLFGTPISQSRSPALHNTLFKQTGLPHRYSRLETDRVADVQDVIRAPDFGGASVTIPLKLDIIPLLDSVTDAVKVIGAVNTIIPTPDNPPRLVGENTDWLGMTHSLMSASHTPSPVDSPSPALVIGAGGTARAAIYALHSLGHSPIYMVARTPSKLDTLINSFPSSFNIIPLPSTTSATELTTPPAVAISTIPADRPIESNMRETLAVLLRHEKKDEGKQRTLLEMAYKPSQTPLMRMAEDAGWVAIPGLEVLSAQGWYQFQKWTSIQPLYVDARAAVMGDSTA
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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A7GBG3
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BXF_CLOBL
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Botulinum neurotoxin type F (BoNT/F) (Bontoxilysin-F) [Cleaved into: Botulinum neurotoxin F light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin F heavy chain (HC)]
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MPVVINSFNYNDPVNDDTILYMQIPYEEKSKKYYKAFEIMRNVWIIPERNTIGTDPSDFDPPASLENGSSAYYDPNYLTTDAEKDRYLKTTIKLFKRINSNPAGEVLLQEISYAKPYLGNEHTPINEFHPVTRTTSVNIKSSTNVKSSIILNLLVLGAGPDIFENSSYPVRKLMDSGGVYDPSNDGFGSINIVTFSPEYEYTFNDISGGYNSSTESFIADPAISLAHELIHALHGLYGARGVTYKETIKVKQAPLMIAEKPIRLEEFLTFGGQDLNIITSAMKEKIYNNLLANYEKIATRLSRVNSAPPEYDINEYKDYFQWKYGLDKNADGSYTVNENKFNEIYKKLYSFTEIDLANKFKVKCRNTYFIKYGFLKVPNLLDDDIYTVSEGFNIGNLAVNNRGQNIKLNPKIIDSIPDKGLVEKIVKFCKSVIPRKGTKAPPRLCIRVNNRELFFVASESSYNENDINTPKEIDDTTNLNNNYRNNLDEVILDYNSETIPQISNQTLNTLVQDDSYVPRYDSNGTSEIEEHNVVDLNVFFYLHAQKVPEGETNISLTSSIDTALSEESQVYTFFSSEFINTINKPVHAALFISWINQVIRDFTTEATQKSTFDKIADISLVVPYVGLALNIGNEVQKENFKEAFELLGAGILLEFVPELLIPTILVFTIKSFIGSSENKNKIIKAINNSLMERETKWKEIYSWIVSNWLTRINTQFNKRKEQMYQALQNQVDAIKTVIEYKYNNYTSDERNRLESEYNINNIREELNKKVSLAMENIERFITESSIFYLMKLINEAKVSKLREYDEGVKEYLLDYISEHRSILGNSVQELNDLVTSTLNNSIPFELSSYTNDKILILYFNKLYKKIKDNSILDMRYENNKFIDISGYGSNISINGDVYIYSTNRNQFGIYSSKPSEVNIAQNNDIIYNGRYQNFSISFWVRIPKYFNKVNLNNEYTIIDCIRNNNSGWKISLNYNKIIWTLQDTAGNNQKLVFNYTQMISISDYINKWIFVTITNNRLGNSRIYINGNLIDEKSISNLGDIHVSDNILFKIVGCNDTRYVGIRYFKVFDTELGKTEIETLYSDEPDPSILKDFWGNYLLYNKRYYLLNLLRTDKSITQNSNFLNINQQRGVYQKPNIFSNTRLYTGVEVIIRKNGSTDISNTDNFVRKNDLAYINVVDRDVEYRLYADISIAKPEKIIKLIRTSNSNNSLGQIIVMDSIGNNCTMNFQNNNGGNIGLLGFHSNNLVASSWYYNNIRKNTSSNGCFWSFISKEHGWQEN
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[Botulinum neurotoxin type F]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin F which may have 2 coreceptors complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity). Requires complex gangliosides for full neurotoxicity. Electrical stimulation increases uptake of toxin, presumably by transiently exposing a receptor usually found in eukaryotic target synaptic vesicles. Blocks neurotransitter release by cleaving synaptobrevin-2/VAMP2. It is not clear whether a synaptic vesicle protein acts as its receptor there is evidence for and against SV2 fulfilling this function. [Botulinum neurotoxin F light chain]: Has protease activity. After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '58-Gln-|-Lys-59' bond of synaptobrevin-2/VAMP2 and probably also the equivalent 'Gln-|-Lys' sites in VAMP1 and VAMP3. Substrate specificity is conferred by multiple interactions of LC with substrate. [Botulinum neurotoxin F heavy chain]: Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site it may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation (By similarity). Isolated HC binds to host synaptosomes and neurons, significantly decreases uptake and toxicity of whole BoNT/F. Interferes with uptake of BoNT/E and to a lesser extent BoNT/C. in vitro binds gangliosides GT1b, GD1b and GD1a. Binds to synaptic vesicle glycoproteins SV2A, SV2B and SV2C which may serve as coreceptors with gangliosides. Interaction with SV2 proteins requires SV2 glycosylation. However knockout SV2A/SV2B mice still cleave synaptobrevin, leaving the identification of its receptor unclear.
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A7HD43
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GCHK_ANADF
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Globin-coupled histidine kinase (EC 2.7.13.3) (AfGcHK) (Heme-based oxygen-sensor histidine kinase)
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MTGVPETVFEELKRYVGWGDGDERALRSLHGAAAPHFPRLAEEFYDRILGHEGARTALVGGESQVGHLKVTMIAWLDELLGGPWDEAYWDRRYRIGRVHVRIGLPQHYMFGAMNVHRTGLARLAYERFHGDPPELERVRNALGKVLDLELAVMLHTYREDLLAQQARVERLSTFGQLVGSIGHDLRNPLGVIETSLYILRTRTGEDERARKHLDRIGEQLGVANGIITNLLDMIRDRPLAREPVELAAVVGGAAESVRRPTGVSLALEGLDALPPVEGDPGQLRQVFVNLLENAVFAASPEGVVAVRASRADGLVALDVEDSGPGVDPATRRRLFEPLITTKDKGIGLGLALVKRIAERHGGTVEYSDRPGGGARFTVRLPA
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Member of the two-component regulatory system GcHK/Anae109_2439. Autophosphorylates in response to oxygen availability, and then transfers the phosphate group to a conserved Asp residue in the receiver domains of the cognate response regulator Anae109_2439, resulting in its activation.
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A7IQH5
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HCDS3_XANP2
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2-(S)-hydroxypropyl-CoM dehydrogenase 3 (S-HPCDH 3) (EC 1.1.1.269) (2-[(S)-2-hydroxypropylthio]ethanesulfonate dehydrogenase 3) (Aliphatic epoxide carboxylation component IV) (Epoxide carboxylase component IV) (SHPCDH3)
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MSNRLKNEVIAITGGGAGIGLAIASAALREGAKVALIDLDQGLAERSAAMLSTGGAVAKGFGADVTKAADITAAITSAEQTIGSLTGLVNNAGIAGFGSVHDADAAAWDRIMAVNVTGTFLASKAALAGMLERHKGTIVNFGSVAGLVGIPTMAAYCAAKGAIVNLTRQMAADYSGRGVRVNAVCPGTVTSTGMGQQLLGSDTSPEVQARRLAKYPIGRFGTPEDIAEAVIFLLSDQAAFVTGAAFAVDGGMTAI
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Involved in aliphatic epoxide carboxylation. Catalyzes the reversible oxidation of (2S)-2-hydroxypropyl-coenzyme M (S-HPC) to 2-oxopropyl-coenzyme M (2-KPC). The enzyme is highly specific for the S enantiomers. In vitro can also use the aliphatic ketone 2-butanone and the aliphatic alcohol 2-propanol, and shows an inherent stereoselectivity for 2-butanone reduction.
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A7KAU2
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S47A1_RABIT
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Multidrug and toxin extrusion protein 1 (MATE-1) (Solute carrier family 47 member 1)
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MEAPVELGPGGRQASPERRHWLRCLVLSDFREELRALLVLACPAFLAQLMVFLISFVSSVFCGHLSKLELNAVTLAIAVINVMGVSVGFGLSSACDTLISQTYGSRNLKHVGVILQRGSLILLLCCLPCWALFLNTQHILLLFRQDPAVSRLTQTYVTIFIPALPATFLYTLQVKYLLNQGIVLPQVVTGVAANLVNALANYLFVYQLHLGVMGSALANTVAQFTLALLLFLYILRSKVYQATWGGWSLECLQDWASFFRLAIPSMLMLCMEWWAYEIGSFLSGILGMVELGAQSVTYELAVIVYMIPMGLSVAVNVRVGNALGAGNIEQAKKSSAVALLVTELIAVVFCVMLLSCKDLVGYIFTSDRDIIALVAQVTPIYAVSHLFESLAGTSGGILRGSGNQKFGAIVNAIGYYVVGLPIGIALMFAAKLGVIGLWLGIVVCAVSQAVCFLGFIARLNWTKACQQARVHANLTVNTASNGNSAVLPDQPHPVGPDSHGGIVLRDADRKEGAELNEQVHPELPLPVRPEDSAHLSGKQLALRRGLLLLGVILVLLAGILVKVYVRTQ
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Multidrug efflux pump that functions as a H(+)/organic cation antiporter. Plays a physiological role in the excretion of cationic compounds including endogenous metabolites, drugs, toxins through the kidney and liver, into urine and bile respectively. Mediates the efflux of endogenous compounds such as creatinine, vitamin B1/thiamine, agmatine and estrone-3-sulfate. May also contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (By similarity).
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A7KAX9
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RHG32_HUMAN
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Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (GTPase regulator interacting with TrkA) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP)
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METESESSTLGDDSVFWLESEVIIQVTDCEEEEREEKFRKMKSSVHSEEDDFVPELHRNVHPRERPDWEETLSAMARGADVPEIPGDLTLKTCGSTASMKVKHVKKLPFTKGHFPKMAECAHFHYENVEFGSIQLSLSEEQNEVMKNGCESKELVYLVQIACQGKSWIVKRSYEDFRVLDKHLHLCIYDRRFSQLSELPRSDTLKDSPESVTQMLMAYLSRLSAIAGNKINCGPALTWMEIDNKGNHLLVHEESSINTPAVGAAHVIKRYTARAPDELTLEVGDIVSVIDMPPKVLSTWWRGKHGFQVGLFPGHCVELINQKVPQSVTNSVPKPVSKKHGKLITFLRTFMKSRPTKQKLKQRGILKERVFGCDLGEHLLNSGFEVPQVLQSCTAFIERYGIVDGIYRLSGVASNIQRLRHEFDSEHVPDLTKEPYVQDIHSVGSLCKLYFRELPNPLLTYQLYEKFSDAVSAATDEERLIKIHDVIQQLPPPHYRTLEFLMRHLSLLADYCSITNMHAKNLAIVWAPNLLRSKQIESACFSGTAAFMEVRIQSVVVEFILNHVDVLFSGRISMAMQEGAASLSRPKSLLVSSPSTKLLTLEEAQARTQAQVNSPIVTENKYIEVGEGPAALQGKFHTIIEFPLERKRPQNKMKKSPVGSWRSFFNLGKSSSVSKRKLQRNESEPSEMKAMALKGGRAEGTLRSAKSEESLTSLHAVDGDSKLFRPRRPRSSSDALSASFNGEMLGNRCNSYDNLPHDNESEEEGGLLHIPALMSPHSAEDVDLSPPDIGVASLDFDPMSFQCSPPKAESECLESGASFLDSPGYSKDKPSANKKDAETGSSQCQTPGSTASSEPVSPLQEKLSPFFTLDLSPTEDKSSKPSSFTEKVVYAFSPKIGRKLSKSPSMSISEPISVTLPPRVSEVIGTVSNTTAQNASSSTWDKCVEERDATNRSPTQIVKMKTNETVAQEAYESEVQPLDQVAAEEVELPGKEDQSVSSSQSKAVASGQTQTGAVTHDPPQDSVPVSSVSLIPPPPPPKNVARMLALALAESAQQASTQSLKRPGTSQAGYTNYGDIAVATTEDNLSSSYSAVALDKAYFQTDRPAEQFHLQNNAPGNCDHPLPETTATGDPTHSNTTESGEQHHQVDLTGNQPHQAYLSGDPEKARITSVPLDSEKSDDHVSFPEDQSGKNSMPTVSFLDQDQSPPRFYSGDQPPSYLGASVDKLHHPLEFADKSPTPPNLPSDKIYPPSGSPEENTSTATMTYMTTTPATAQMSTKEASWDVAEQPTTADFAAATLQRTHRTNRPLPPPPSQRSAEQPPVVGQVQAATNIGLNNSHKVQGVVPVPERPPEPRAMDDPASAFISDSGAAAAQCPMATAVQPGLPEKVRDGARVPLLHLRAESVPAHPCGFPAPLPPTRMMESKMIAAIHSSSADATSSSNYHSFVTASSTSVDDALPLPLPVPQPKHASQKTVYSSFARPDVTTEPFGPDNCLHFNMTPNCQYRPQSVPPHHNKLEQHQVYGARSEPPASMGLRYNTYVAPGRNASGHHSKPCSRVEYVSSLSSSVRNTCYPEDIPPYPTIRRVQSLHAPPSSMIRSVPISRTEVPPDDEPAYCPRPLYQYKPYQSSQARSDYHVTQLQPYFENGRVHYRYSPYSSSSSSYYSPDGALCDVDAYGTVQLRPLHRLPNRDFAFYNPRLQGKSLYSYAGLAPRPRANVTGYFSPNDHNVVSMPPAADVKHTYTSWDLEDMEKYRMQSIRRESRARQKVKGPVMSQYDNMTPAVQDDLGGIYVIHLRSKSDPGKTGLLSVAEGKESRHAAKAISPEGEDRFYRRHPEAEMDRAHHHGGHGSTQPEKPSLPQKQSSLRSRKLPDMGCSLPEHRAHQEASHRQFCESKNGPPYPQGAGQLDYGSKGIPDTSEPVSYHNSGVKYAASGQESLRLNHKEVRLSKEMERPWVRQPSAPEKHSRDCYKEEEHLTQSIVPPPKPERSHSLKLHHTQNVERDPSVLYQYQPHGKRQSSVTVVSQYDNLEDYHSLPQHQRGVFGGGGMGTYVPPGFPHPQSRTYATALGQGAFLPAELSLQHPETQIHAE
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GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:12446789, ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:12857875, ECO:0000269|PubMed:17663722}.
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A7L9Z8
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AT2C2_MOUSE
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Calcium-transporting ATPase type 2C member 2 (ATPase 2C2) (EC 7.2.2.10) (Ca(2+)/Mn(2+)-ATPase 2C2) (Secretory pathway Ca(2+)-transporting ATPase type 2) (SPCA2)
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MGRRLKFLQKLAFLGQNHRYKALERDEVETLIDEQCELKAIEREKTVAALPPGEACKCSREELARAFHVDLDSGLSEFAVAQRRLVHGWNEFVTDNAEPVWKKYLDQFRNPLILLLLGSSVVSVLTKEYEDAVSIALAVLIVVTVGFIQEYRSEKSLEELTKLVPPECNCLRDGKLRHMLARDLVPGDIVSLSMGDRIPADIRLTEVTDLLVDESSFTGEVEPCGKTDSPLADGGDLSTLSNVVFMGTLVQCGKGQGVVIGTGEQSQFGEVFKMMRAEETPKTPLQKSMDKLGKQLTIFSFGIIGLLMLVGWVQGKPFLSMFTVGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVIVKKLPIVETLGCCNVICSDKTGTLTANEMTATQLVTSDGFHAEVSGVGYSGEGTVCLLPSKEVIKGFDNVSVGKLVEAGCVANNAVIRKNAVMGQPTEGALVVLAMKMNLGSIKDSYVRKKEIPFSSEQKWMAVRCGPKSEDGEDIYFMKGAFEEVIHHCSMYNNGGIPLPLTPQQKSYCQQEEKKMGSLGLRVLALASGPELGRLTFLGLVGIIDPPRAGVKEAVQVLSESGVSVKMVTGDALETALAIGRTIGLCNEKLKAMSGEEVEGTEQGALAARVRQVSVFFRTSPKHKVKIIKALQESGAIVAMTGDGVNDSVALKSADIGIAMGQTGTDVSKEAANMILVDDDFSAIMSAVEEGKGIFYNIKNFVRFQLSTSIAALSLITLSTVCNLPSPLNAMQILWVNIIMDGPPAQSLGVEPVDRDALRRPPRSVGDTILNRALILRVLMSAAVIIGGTLFIFWREIPANGTSTPRTTTMAFTCFVFFDLFNALSCRSQTKLIFEIGFFRNRMFLYSVLGSLLGQLAVIYAPPLQKVFQTENLSALDLLLLTGLASSVFILSELLKLWEKFLSRARPTQMLPEAV
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ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway. Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to the lumenal side. The transfer of ions across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (By similarity). Induces Ca(2+) influx independently of its ATP-driven pump function. At the basolateral membrane of mammary epithelial cells, interacts with Ca(2+) channel ORAI1 and mediates Ca(2+) entry independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May facilitate transepithelial transport of large quantities of Ca(2+) for milk secretion via activation of Ca(2+) influx channels at the plasma membrane and active Ca(2+) transport at the Golgi apparatus (By similarity).
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A7LCJ3
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SN_PIG
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Sialoadhesin (pSn) (Sialic acid-binding Ig-like lectin 1) (Siglec-1) (p210)
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MDFLLLLLLLASSALAGLASWTVSRPETVQGIKGSCLIIPCTFGFPANVEVPHGITAIWYYDYSGKRLVVSHSRNPKVVENHFQGRALLLGQAEQRTCSLLLKDLQPQDSGSYNFRFEISEGNRWSDVKGTVVTVTEVPSVPTIALPAKLHEGMEVDFNCSTPYVCPTEPVNLQWQGQDPTRSVTSHLQKLEPSGTSHMETLHMALSWQDHGRILSCQVSAAERRMQKEIHLQVQHAPKGVEILFSHSGRNVLPGDLVTLSCQVNSSNPQVSSVQWVKDGTKLKDQKRVLQLRRAAWADAGVYTCQAGNAVGSSVSPPVSLHVFMAEVQVSPVGSILENQTVTLACNTPKEAPSELRYSWCKNHALLEGSHSRTLRLHSVTRADSGFYFCEVQNARGRERSPPVSVVVSHPPLTPDLTAFPETQAGLVGILQCSVVSEPPATLVLSHGGLISASTSGEGDHSPRFSVASAPNSLRLEIQDLGPTDSGEYMCSASSSLGNASSTLDFHANAARLLISPAAEVVEGQAVTLSCRSSLSLMPDTRFSWYLNGALILEGPSSSLLLPAASSTDAGSYHCRAQNSHSTSGPSPPAVLTVLRAPRQPVFTAQLDPDTAGAGAGRQGLLLCRVDSDPPAQLQLLHRGRVVASSLSWGGGCCTCGGCFQRMKVTKAPNLLRVEIRDPALEDEGVYLCEASSALGNASASATLDAQATVLVITPSHTLQEGIEANLTCNVSREASGPANFSWFRDGALWAQGPLDTVTLLPVSRTDAALYACRIVTEAGAGLSTPVALNVLYPPDPPKLSALLDVDQGHTAVFVCTVDSHPLAQLALFRGEHLLAASSALRLPPRGRLQAKASANSLQLEVRDLSLGDSGSYHCEATNILGSANTSLTFQVRGAWVRVSPSPELQEGQAVVLSCQVPIGVLEGTSYRWYRDGQPLQESTSATLRFAAITLSQAGAYHCQAQASGSATTDLAAPVSLHVTYAPRQATLTTLMDSGLGRLGLLLCRVNSDPPAQLRLLHGSRLVASTLQGVEELAGSSPRLQVATAPNTLRLEIHNAVLEDEGVYTCEATNTLGQTLASAALDAQAMRVQVWPNATVQEGQLVNLTRLVWTTHLAQLTYTWYRDQQQLPGAAHSILLPNVTVTDAASYRCGILIPGQALRLSRPVALDVLYAPRRLRLTHLLESRGGQLAVVLCTVDSRPAAQLTLSHAGRLLASSTAASVPNTLRLELWEPRPSDEGLYSCSARSPLGQANTSLELRLEGVQVALAPSATVPEGAPVTVTCEDPAARPPTLYVWYHNSRWLQEGSAASLSFPAATRAHAGAYTCQVQDAQGTRISQPAALHILYAPRDAVLSSFWDSRASPMAVVQCTVDSEPPAEMTLSHDGKVLATSQGVHGLAVGTGHVQVARNALQLRVQNVPSRDKDTYVCMDRNSLGSVSTMGQLQPEGVHVVAEPGLDVPEGTALNLSCRLPSGPGHIGNSTFAWFRNGRQLHTESVPTFTFTHVARAQAGLYHCQAELPAGAATSAPVLLRVLYPPKTPTMTVFVEPEGGIQGILDCRVDSEPLASLTLHLGSRLVASSQPQAAPAKPHIRVSASPNALRVDMEELKPSDQGEYVCSASNALGSASAATYFGTRALHRLHLFQHLLWFLGLLASLLFLLLGLGVWYAWRRGNFHKLRMGEYSVEMVSRKETTQMSTDQEEVTGIGDDAGSVNQAAFDPAHLCENTQSVKSTV
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Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells. Plays a crucial role in limiting bacterial dissemination by engaging sialylated bacteria to promote effective phagocytosis and antigen presentation for the adaptive immune response. Mediates the uptake of various enveloped viruses via sialic acid recognition and subsequently induces the formation of intracellular compartments filled with virions (VCCs). In turn, enhances macrophage-to-T-cell transmission of several viruses including reproductive and respiratory syndrome virus or porcine arterivirus. Acts as an endocytic receptor mediating clathrin dependent endocytosis. Preferentially binds to alpha-2,3-linked sialic acid (By similarity). Binds to SPN/CD43 on T-cells (By similarity). May play a role in hemopoiesis. Plays a role in the inhibition of antiviral innate immune by promoting TBK1 degradation via TYROBP and TRIM27-mediated ubiquitination (By similarity).
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A7LFZ6
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DCL4_ORYSJ
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Endoribonuclease Dicer homolog 4 (EC 3.1.26.-) (Dicer-like protein 4) (OsDCL4) (Protein SHOOT ORGANIZATION 1)
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MGDAAAAAPAAAAAGPSSTRGEPKDPRTIARKYQLDLCKRAVEENIIVYLGTGCGKTHIAVLLIYELGHLIRKPSREVCIFLAPTIPLVRQQAVVIASSTDFKVQCYYGNGKNSRDHQEWENDMREFEVLVMTPQILLQSLRHCFIKMNSIALLILDECHHAQPQKRHPYAQIMKEFYNSNSVEKFPRVFGMTASPIIGKGVMPSHSFTEKGGRSPCQPLIFFLPKGGSNKLNYTKCINSLEELLHAKVCSVDNEELESVVASPDMEVYFYGPVNHSNLTTICIKELDSLKLQSERMLRASLCDFKDSQKKLKSLWRLHENIIFCLQELGSFGALQAARTFLSFDGDKLDRREVDLNGSTSSFAHHYLNGATSILSRNKTDGSHAGSFDLEKLEEPFFSNKFSVLINVLSRYGLQENMKCIVFVKRITVARAISNILQNLKCLEFWKCEFLVGCHSGSKNMSRNKMDAIVQRFSSGEVNLLVATSVGEEGLDIQTCCLVVRFDLPETVASFIQSRGRARMTKSKYVVLLERENQSHEKLLNGYIAGESIMNEEIDSRTSNDMFDCLEENIYQVDNTGASISTACSVSLLHCYCDNLPRDMFFTPSPVFFYIDGIEGIICRLILPPNAAFRQADGQPCLSKDEAKRDACLKACVKLHKLGALTDFLLPGPGSRKNKVSVTNNSSNNKVEDDSLREELHEMLIPAVLKPSGLKLDSLSNLHFYYVKFIPIPEDRRYQMFGLFVINPLPVEAETLQVDLHLARGRIVKAGIKHLGKIAFEKEKMMLAHKFQEMCLKILLDRSEFTSPHVKLGNDVTLEINSTFYLLLPIKQKCYGDRFMIDWPAVERCLSSPIFKDPIDVSVHASYSSNESLRLLDGIFSKTDVVGSVVFSPHNNIFFFVDGILDEINAWSEHSGATYAEHFKERFRIELSHPEQPLLKAKQIFNLRNLLHNRLPETTESEGRELLEHFVELPPELCSLKVIGFSKDMGSSLSLLPSLMYRLENLLVAIELKDVMLSSFPEASQISASGILEALTTEKCLERISLERFEVLGDAFLKYVVGRHKFITYEGLDEGQLTRRRSDVVNNSHLYELSIRKKLQVYIRDQQFEPTQFFAPGRPCKVVCNTDVEVRLHQMDIHPDNRENCNLRCTRSHHWLHRKVIADVVESLIGAFLVEGGFKAAFAFLHWIGIDVDFNNPALYRVLDSSSINLSLMDYTDIAGLEELIGYKFKHKGLLLQAFVHPSFSQHSGGCYQRLEFLGDAVLEYVITSYLYSTYPDIKPGQITDLRSLAVGNDSLAYAAVEKSIHKHLIKDSNHLTSAISKFEMYVKLSNSEKDLLEEPACPKALGDIVESCIGAVLLDSGFNLNYVWKVMLMLLKPVLTFANMHTNPMRELRELCQCHGFELGLPKPMKADGEYHVKVEVNIKSKIIICTAANRNSKAARKFAAQETLSKLKNYGYKHRNKSLEEILIVARKRESELIGYNEDPIDVEADISVKMKSPHIHEENIPFQNTETSFTRSSKFHNQIIAGSGKHDVNNGRNNQPKLATQSGRLPSEATEKSNKKVYHGDMVHKTARSFLFELCAANYWKPPEFKLCKEEGPSHLRKFTYKVVVEIKGASATLLECHSDGKLQKKAAQEHAAQGALWCLKQLGHLPKEEDVRV
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Involved in the RNA silencing pathway. Cleaves double-stranded RNA to produce small interfering RNAs (siRNAs) which target the selective destruction of complementary RNAs. Required for the production of 21 nucleotide siRNAs. Regulates shoot apical meristem (SAM) initiation and maintenance, leaf polarization and lemma polarity through the trans-acting siRNAS (ta-siRNAs) pathway, which probably modulate the expression of the ARF2, ARF3, ARF4, ARF14 and ARF15 genes. Can process endogenous 21 nucleotide siRNAs derived from an imperfect inverted repeat. May not be involved in microRNAs (miRNAs) production.
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A7LXT0
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GH31A_BACO1
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Alpha-xylosidase BoGH31A (EC 3.2.1.177) (Glycosyl hydrolase family protein 31A) (BoGH31A)
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MIMNMKNIFYCLLPGLLLGACSNKVYEKTGDSVIVKVQHKETGGPRLVRLQVMGDKLIHVSATADSKFADPQSLIVVPQKKQTSFAVVQNGDTITVSTEEVKASVLASTGEVWFTDKNGELILQENKGGGKTFTPIEVEGTKGYTVCQVFESPEDEAFYGLGQHQADEFNYKGKNEELFQYNTKVSVPFVVSNKNYGILLDSYSFCRFGNPNDYSQLNRIFKLYDKTGQEGALTGTYVPKKGETLVRREDSIYFENLKTIENLPKKLPLMGAKVTYEGEIEPAQTGEFKFILYYAGYVKVYLNNEPVVPERWRTAWNPNSYKFAAHLEAGKRVPLKIEWQPDGGQSYCGLRALTPVNPEEQGKQSWWSEMTKQLDYYFMAGENMDDVISGYRSLTGKSPVMPKWAMGFWQSREKYNTQEEMLGALKGFRDRKIPLDNIVLDWNHWPENAWGSHEFDKARFPDPKAMVDSIHAMHARMMISVWPKFYVTTEHFKEFDENGWMYQQSVKDSLKDWVGPGYHYGFYDAYDPDARKLFWKQMYEHYYPLGIDAWWMDASEPNVRDCTDLEYRKALCGPTALGSSTEFFNAYALMNAEAIYDGQRGVDNNKRVFLLTRSGFAGLQRYSTATWSGDIGTRWEDMKAQISAGLNFAMSGIPYWTMDIGGFCVENRYVAGQKQWNATKTENADYKEWRELNTRWYQFGAFVPLYRAHGQYPFREIWEIAPEGHPAYQSVVYYTKLRYNMMPYIYSLAGMTWFDDYTIMRPLVMDFTADAEVNDIGDQFMFGPSFMVSPVYRYGDRSREIYFPQAEGWYDFYSGKFQAGGERKVIEAPYERIPLYVRAGAIIPFGDDIQYTDEKPAEHIRLYIYQGADGEFTLYEDEGVNYNYEQGMYAMIPMKYDEATKTLVIGERQGEFPGMLKERTFTVVTVNKEKAQPFDLNAKGVTVKYNGSEQTLKL
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Catalyzes the liberation of alpha-xylose from the non-reducing terminal glucose of xyloglucan oligosaccharides in xyloglucan degradation, converting the 'X' to 'G' units.
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A7LXT7
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BGH5A_BACO1
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Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A (EC 3.2.1.151) (Glycosyl hydrolase family protein 5A) (BoGH5A)
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MEKQSFSDGLFSPLGIKRVIFMLVLLTTSFISCSNSDEKGGSLEVAQEYRNLEFDARGSRQTIQIDGPAEWHISTSESWCKSSHTIGEGKQYVNITVEANDTQKERTATVTVSASGAPDIIINVKQSLYSVPAYDEYIAPDNTGMRDLTSMQLSALMKAGVNVGNTFEAVIVGNDGSLSGDETCWGNPTPNKVLFEGIKAAGFDVVRIPVAYSHQFEDAATYKIKSAWMDKVEAAVKAALDAGLYVIINIHWEGGWLNHPVDANKEALDERLEAMWKQIALRFRDYDDRLLFAGTNEVNNDDANGAQPTEENYRVQNGFNQVFVNTVRATGGRNHYRHLIVQAYNTDVAKAVAHFTMPLDIVQNRIFLECHYYDPYDFTIMPNDENFKSQWGAAFAGGDVSATGQEGDIEATLSSLNVFINNNVPVIIGEYGPTLRDQLTGEALENHLKSRNDYIEYVVKTCVKNKLVPLYWDAGYTEKLFDRTTGQPHNAASIAAIMKGLN
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Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues in xyloglucan degradation. Cleaves the backbone of the 3 major types of natural xyloglucans (seed galactoxyloglucan from tamarind kernel, dicot fucogalactoxyloglucan from lettuce leaves, and solanaceous arabinogalactoxyloglucan from tomato fruit), to produce xyloglucan oligosaccharides.
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A7M7C7
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SKOR2_MOUSE
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SKI family transcriptional corepressor 2 (Fussel-18 homolog) (LBX1 corepressor 1-like protein) (Ladybird homeobox corepressor 1-like protein) (Transcriptional corepressor Corl2)
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MASSPLPGPNDILLASPSSAFQPDALSQPRPGHANLKPNQVGQVILYGIPIVSLVIDGQERLCLAQISNTLLKNFSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITKREAERLCKSFLGENRPPKLPDNFAFDVSHECAWGCRGSFIPARYNSSRAKCIKCSYCNMYFSPNKFIFHSHRTPDAKYTQPDAANFNSWRRHLKLTDKSPQDELVFAWEDVKAMFNGGSRKRALPQPSAHPACHPLSSVKAAAVAAAAAVAGGGGLLGPHLLGAPPPPPPPPPLAELAGAPHAHHKRPRFDDDDDSLQEAAVVAAASLSAAAASLSVAAATGGAGPGAGGPGGGCVAGVGVGASAGAGAAAGTKGPRSYPVIPVPSKGSFGGVLQKFPGCGGLFPHPYTFPAAAAAFGLCHKKEDAGTAAEALGGAGAGSAGAAPKAGLSGLFWPAGRKDAFYPPFCMFWPPRTPGGLPVPTYLQPPPQPPSALGCALGDSPALLRQAFLDLAEPGGAGGSAEAAPPPGQPPPVVANGPGSGPPATGGTGARDTLFESPPGGSGGDCSAGSTPPAEQGVTSGTGSASSGAGSVGTRVPAPHHPHLLEGRKAGGGSYHHSSAFRPVGGKDDAESLAKLHGASAGTPHSAPAHHHHHHHHPHHHHHHPPQPPSPLLLLQPQPDEPGSERHHPAPPPPPPPPPLAPQPHHRGLLSPEGTSCSYPSEDSSEDEEDEEEEQEVDVEGHKPLEGEEEEDGRDPEDEEEEDEETRVLLGDSLVGGGRFLQGRGLSEKGSGRDRTTPAVGAFPLALNSSRLLQEDGKLGDSGGSDLPAPPPPPLAPQKASSSGGSRPGSPVHHPSLEEEPSYKDNQKPKENNQVIISTKDDNFSDKNKGHGFFITDSDSSGDFWRERSGEHTQETNSPHSLKKDVENMGKEELQKVLFEQIDLRRRLEQEFQVLKGNTSFPVFNNFQDQMKRELAYREEMVQQLQIIPYAASLIRKEKLGAHLSKS
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Acts as a TGF-beta antagonist in the nervous system (By similarity). Exhibits transcriptional repressor activity. {ECO:0000250, ECO:0000269|PubMed:18522874}.
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A7MAQ2
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DIOA3_DIOJA
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Dioscorin dioA3 (EC 1.6.5.4) (EC 4.2.1.1) (Dj-dio5) (Dj-dioA3) (Tuber storage protein dioA3)
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MSSSTLLHLLLLSSLLFSCLSCLTNVEDEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGKLRRNYRAVDARLRNSGHDVLVDFKGNAGSLSINRVEYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFRFGRADPFLSDLEDFIKQFSNSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFEQLKSKLGVI
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Storage protein of tuber. Involved in protection against oxidative stress (Probable). Has carbonate dehydratase, trypsin inhibitor, dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA) reductase activities. Catalyzes the reactions of carbonate dehydratase and DHA reductase independently of zinc and glutathione (GSH). The coupled reaction is capable of recycling a plant antioxidant ascorbate using ubiquitous compounds H(2)O and CO(2). Exhibits antioxidant activity. Able to scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical. Exhibits immunomodulatory activity. Activates Toll-like receptor 4 signaling pathways by up-regulating the gene expression of pro-inflammatory cytokines, such as tumor necrosis factor alpha, interleukin-1 beta and interleukin-6, and chemokines RANTES and MCP-1, in mouse RAW 264.7 macrophages. Stimulates the phagocytosis of E.coli by the LPS-treated mouse macrophages.
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A7MB74
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SGK1_BOVIN
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Serine/threonine-protein kinase Sgk1 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 1)
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MTVKTEAARDTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKISPPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEAFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHVLEGLLQKDRTKRLGAKDDFMEIKNHVFFSLINWEDLINKKITPPFNPNVSGPSDLRHFDPEFTEEPVPNSIGRSPDSLLLTASVKEAAEAFLGFSYAPPMDSFL
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Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis (By similarity).
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A7MBB4
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M3K13_BOVIN
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Mitogen-activated protein kinase kinase kinase 13 (EC 2.7.11.25)
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MANPQEHLSCSSSPRLPLSENKTFNGLQDDLAPMGSHASPKLLKDQQEKGMVQTELAEGTNSPITTTVLTSISEDSRDQFENSVLQLREQDESEMAMSHGNSNTVDGEGTSGTEDIKIQFSRSGSGSGGFLEGLFGCLRPVWNIIGKAYSTDYKLQQQDTWEVPFEEISELQWLGSGAQGAVFLGKFRAEEVAIKKVREQNETDIKHLRKLKHPNIIAFKGVCTQAPCYCIIMEYCAHGQLYEVLRAGRKITPRLLVDWSTGIASGMNYLHLHKIIHRDLKSPNVLVTHTDAVKISDFGTSKELSDKSTKMSFAGTVAWMAPEVIRNEPVSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLHLPVPSTCPDGFKILMKQTWQSKTRNRPSFRQTLMHLDIASADVLATPQETYFKSQAEWREEVKKHFEKIKSEGTCIHRLDEELIRRRREELRHALDIREHYERKLERANNLYMELSAIMLQLEMREKELIKREQAVEKKYPGTYKRHPVRPIIHPNAMEKLMKRKGMPHRPGMQAKRPDLLRSEGIPSVEVAPTASPLSGSPKLSSSSSKSRYRSKPRHRRGNSRGSHGDFAAILKNQPAQEDSPHPTSLHQAEPQYPSSQHHNLLQQQYQQPPPAMSQSHHPRLNMHGQDIATCPNNLRYFGPAAALRSPLSNHSQRQMPGSSPDLISTAMAADCWRSSEPDKGQAGPWGCCQADPYDPCLQCRPEQHGSLDVPSAKPVGRSPSLFKPPAHNPLLENAQGSEKMEENEFSGYRSASSLGASHHITPPVLPRKTRPLQKSGDDSSEEEEGEVDSEVEFPRRQRPHRCISSCQSYSTFSSENFSVSDGEEGNTSDHSNSPDELADKLEDHLAEKLDDLLSQTPEIPIEISSHSDGLSDKECAVRRVKTQMSLGKLCAEERGYENPMQFEESDCDSSDGECSDATVRTNKHYSSATW
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Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibitors of NF-kappa-B (By similarity).
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A7MBE0
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S22A1_BOVIN
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Solute carrier family 22 member 1 (Organic cation transporter 1)
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MLTVDDVLEQVGEFGWFQKQTFLILCLLSAAFAPIYVGIVFLAFTPDHRCRSPGVAELSRRCGWSLAEELNYTVPGPGPESQCLRYEVDWNQSTLGCLDPLASLATNGSPLPLGPCEQGWVYDTPGSSIVTEFNLVCDDSWKVDLFQSCVNLGFFLGSLGVGYIADRFGRKVCLLATTLTCASLGVLTAVAPDYTSLLIFRLLQGLVSKGSWTAGYTLITEFVGLGYRRTVAILYQMAFTVGLVLLSGLAYILPHWRWLQLAVSLPIFLLLFRFWFVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKMLSLEEDVTEKLSPSFIDLFRTPNLRKYTFILMYLWFTSSVVYQGLIMHVGATGGNLYLDFLYSALVEFPAGFIILVTIDRFGRRYPLATSNLAAGLACFLMIFIPHDLPWLNIMVACVGRMGITIVFQMVCLVNAELFPTFIRNLGMMVCSSLCDLGGVLTPFLVFRLMEVWQGSPLILFAALGLVAGGMTLLLPETKGVTLPETIEDAENLQRKAKPKENKIYLQVQTSELNTQAAERDASQGTAQQK
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Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (By similarity). Functions as a pH- and Na(+)-independent, bidirectional transporter (By similarity). Cation cellular uptake or release is driven by the electrochemical potential (i.e. membrane potential and concentration gradient) and substrate selectivity (By similarity). Hydrophobicity is a major requirement for recognition in polyvalent substrates and inhibitors (By similarity). Primarily expressed in the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds from the blood by hepatic and renal clearance (By similarity). Most likely functions as an uptake carrier in enterocytes contributing to the intestinal elimination of organic cations from the systemic circulation. Transports endogenous monoamines such as N-1-methylnicotinamide (NMN), guanidine, neurotransmitters dopamine, serotonin, noradrenaline, adrenaline and histamine, and quaternary ammonium compound such as choline. Also transports natural polyamines such as spermidine, agmatine and putrescine at low affinity, but relatively high turnover. Involved in the hepatic and intestinal uptake of the vitamin B1/thiamine, hence regulating hepatic lipid and energy metabolism. Contributes to the influx and efflux of fatty acid carriers carnitines and acylcarnitines across the basolateral membrane of hepatocytes, from the liver to the systemic circulation and inversely and may be involved in regulating the systemic availability of hepatic acylcarnitines (By similarity). Also capable of transporting non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (By similarity). May contribute to the transport of cationic compounds in testes across the blood-testis-barrier (By similarity). Also mediates the uptake of xenobiotics tributylmethylammonium (TBuMA), quinidine, N-methyl-quinine (NMQ), N-methyl-quinidine (NMQD) N-(4,4-azo-n-pentyl)-quinuclidine (APQ), azidoprocainamide methoiodide (AMP), N-(4,4-azo-n-pentyl)-21-deoxyajmalinium (APDA) and 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP) (By similarity).
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A7MBH5
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ODAD3_BOVIN
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Outer dynein arm-docking complex subunit 3 (Coiled-coil domain-containing protein 151)
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MTSPLCWAAASNAMPSQDQISTPSKVKATQVQLKPYRSRGKGLVPVWHSLHSKAGPLHASEGKSAVNMQVAELQRKIQLLEGDRKAFYESTQWNIKKNQETINQLREETRVLQLQLTALLQGDEKVVQAVIREWKSEKPYLKNRTGQQALEHLDYRLNEKVKQLNALRHQLGLRQKWLEELQLQHSLRELEIAEAQDSNTEVAKTMRNLENRLEKARMKAEEAEHITSVYLQLKAYLQEESLHLGNRLDFMEAEVVRTKHELEELHLVNQEALNARDIAKNQLQYLEETVFRERKKRERYLTECKKRAEEKKLQNERMERKTQREHVLLQSDDTLQDSMYSKEEELKRRWSMYQMEVLFGKVKDATGVAETHAVVRRFLAQGDTFTQLEMLKSENEQTLLRLKQEKQRLQQELEDLKYSGEALLVSEQKRQAELQGRLKMEEQRRADAQNQLDRTMRALQITKEGLEHLAGKLNHIVVAGPTYEEGSPGASLDTKGSATPQPQETGRSVGKMDPKVDDYLPNLLGLVEEKLLKLHSQLENHNVPEMLRHIVDLEFYATLEGKLPSYNTRIALPVAGHKDKFFDEEESEEDDSDVVTRAALKMRSQKLIESRSKRRGRSRRS
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Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules.
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A7MBI7
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COMT_BOVIN
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Catechol O-methyltransferase (EC 2.1.1.6)
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MLEAPPLLLVAGGVGLALLALRWLATTDLQFFGRAFIVWNEFIMKPIRNLLMGSSKEQRILQHVLQHAVAGDPQSVVAAIDSYSLEKEWAMHVGEKKGQIVDRVLREQQPSVLLELGAYCGYSAVRMARLLLPGARLLTIEFNPDYAAITQRMVEFAGLQDKVTVVLGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDMLLLEECGLLREGTVLLADNVIYPGAPDFLEYVRGNSRFECSHFSSYLEYSKVVDGLEKVVYKGLSGPARP
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Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
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A7MBL8
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PKN2_DANRE
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Serine/threonine-protein kinase N2 (EC 2.7.11.13) (PKN gamma) (Protein kinase C-like 2) (Protein-kinase C-related kinase 2)
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MAADSVQNDARGPMVSGRLDFDQNLDFSDTMVQKNLDEIKDQIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNMLKKSNKKVEELHQELQELNAHIVVKDPEEVEEYPLTPDTPKSETRMSTNSNRLAALKKQADIELKVKQGAEDMIQMYSNGSSKDRKLLAAAQQMLQDSKTKIEFIRMQILKASQTSEINYENNDVTTSKPIISPLDLRIEELRHHYRIESAVADGAKNVMKLLGTGKVTEKKAHSEAQARLNESSQKLDLLKFSLEQRLSELPKNHPKGTLIMEELAMVASPPNSPRQSIMSTSNQYSTVAKPAALTGTLDVRLMGCQDLLENVPGRSKTASVSLPGWSPSEARSSFMSRGNKNKSGSSRTLSKSDDLSNEISAVLKLDNTVVGQTHWKPVSNQSWDQKFTLELDRSRELEIAVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPSVNTSFSPQAADLGSAMSHETAPMGHPDAHSLPSDPTVTKLDFDKAVTPPSKRNSIEVEIEETAPPDKISDGKEVQDALATFDFLNNTVAKPDYDSLVEHEQPGLELTEIQRKTEIREEEEVQFSLSDFKCVAVLGRGHFGKVLLADYKTTGEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHADVFSETRSVFYAACVVLGLQFLHDHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFKDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIFEMLVGESPFPGDDEEEVFDSIVNDEVRYPKYLSTEAISIMRRLLRRNPERRLGAGERDAEEVKRHPFFRDMDWPGLLAKKIRPPFVPTITSREDVSNFDDEFTSEAPILTPPREPRILTLGEQDLFADFDYIADWC
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Pkc-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. May play a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion and transcription activation signaling processes (By similarity).
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A7MBS7
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THS7A_DANRE
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Thrombospondin type-1 domain-containing protein 7A
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MGLASRAPGKGGTSAGALASLFRVALLFFGLWDVQTQTVANTRPTYIWQTGPWGRCMGSECGPGGSQSRAVWCAHSEGWTTLHTNCQQSERPSNQQSCFRVCDWHKELYDWQLGAWNQCVPVSMRNAGVPRPAVCTRGEEGIQTREVGCVHKSDGVPAEDAICEYFEPKPRLEQACLIPCPRDCVVSEFSPWTSCSKSCGMGLQNRLRSVLAPPLFGGSACPNLTEFRTCQPGKCEGVESLHSLRVGPWGQCMASPIRQARDTGEARVPKAERKAKRDRQARQERQGKRRKNKEKKELRESKGERVRERVKEKKRMRDPETRELIKKKRTRNRQNRQGLKFWDLQVGYQTREVTCVHRSGSTASISQCTQQTLPVTYQACVISKDCEVSEWSDWSVCSKECYDLNGRKGQRTRTRQVQQFPVGGGAECPELEESEPCSPQGEGIPPCVVYNWRSTEWSDCRVDVLLSQQDRRRSNQTGLCGGGVQTREVYCVQAPSETSSNLGSLKSKDALRPVNSDLCLGVPHNTTQLCHIPCPVECEVSAWSAWGPCTFENCQDQSTKKGFKLRKRKIMNEPTGGTGNCPHLTEAIPCEEPSCYDWLLVKLEECVPDNDKVCGPGTQNPQVQCINSDGEFVDRQLCRDAILPMPVLCEVSCPKDCVLSPWTSWSLCSNTCSGKNSEGKQTRARSILAYNAGDGGVQCPNSSALQEVRSCNDHPCTVYHWQTGPWGQCIEDTSVPSANSSISRAVPGTAVNDAFCSVGMQTRKVICVRVNVGQVPPKKCPESLRPETVRPCLLPCKRDCVVTPYSDWTPCPSICQTGGSVKKKQSRKRIIIQLPANGGQDCPEVLFQEKDCDASSVCPGYRWKTHKWRRCQLVPWSIRQDSPGAQETCGPGLQARAVSCKKLDSGPADVAACLKFAGPMPQLTQSCQLPCQDDCQLTAWSKFSTCAADCVGVRTRKRTLVGKSKKREQCKNTQMYPLSETQYCPCNKYNAQPVGNWSDCILPEGRVEGLLGMKVQGDIKECGQGYRYQAMVCYDQDNRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSKWLREKPYNGGRPCPKLDHVNQAQVYEVVPCLSDCSQYVWVAEPWSVWKVSNVDLKENCGEGVQTRKVRCMQNTVDGPSDPVEDYLCDPEEMPLGARESKLPCPEDCVLTDWGSWSRCPLPCNVNSTRQRSASPIRQPSERKQCPSTTEKEICTLNSNCFHYSYNITDWSTCQLSERAVCGVGFKTRMLDCVRSDSKSVDLKFCEELGLEKKWQMNASCVVECPVNCQLSDWSSWSECSHTCGLAGKLWRRRTVIQASQGDGRPCSSQLEQWKPCPVKPCFSWRYSVWSPCKSEGARCGEGLRFRNVSCFVSDGSGKDAGSMVDEELCGDLEQTVDGDKQIILQESCTVPCPGECYLTDWTMWSPCQLSCIGGDDLGFGSVQVRSRAVLAQEPENLLQCPEQEWEARPCTEGQCYDYKWMTGAWRGSSRQVWCQRSDGLNVTGGCQSTTEPVSDRSCDPACDKPRSICTEAGICGCEEGYTEVMTSDGVLDQCTVIPVLEIPTAGDSKADVKTIRALNPTEPTANMPGRAGRTWFLQPFGPDGKLKTWVYGVAAGAFVLLVFIVSMTYLACKKPKKPQRRQMNNRLKPLTLAYDGDADM
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Required for normal sprouting angiogenesis and normal embryonic development of intersegmental vessels (ISV). Required for normal function of the glomerular filtration barrier. Required for normal axon outgrowth on embryonic motor neurons at the level of the horizontal myoseptum. Required for normal expression of notch1b, suggesting that its functions in angiogenesis and neuron outgrowth are due to decreased expression of notch1b. Plays a role in actin cytoskeleton rearrangement (By similarity).
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A7MCT6
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EKI2_MOUSE
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Ethanolamine kinase 2 (EKI 2) (EC 2.7.1.82) (Ethanolamine kinase-like protein)
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MAVPPSAPVPCSPFYLRRQEPCPQCSWSMEEKAVASAGCWEPPGPPRAAVPCFSVTVEQDDILPGALRLIRELRPHWKPEQVRTKRFKDGITNKLLACYVEEDMRDCVLVRVYGERTELLVDRENEVRNFQLLRAHGCAPKLYCTFQNGLCYEYVQGVALGPEHIREPQLFRLIALEMAKIHTIHANGSLPKPTLWHKMHRYFTLVKDEISPSLSADVPKVEVLEQELAWLKEHLSQLDSPVVFCHNDLLCKNIIYDSDKGRVCFIDYEYAGYNYQAFDIGNHFNEFAGVNVVDYSRYPARETQVQWLRYYLEAQKGTAASPREVERLYAQVNKFALASHFFWALWALIQNQYSTISFDFLRYAVIRFNQYFKVKPQVSALEMPK
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Highly specific for ethanolamine phosphorylation. Does not have choline kinase activity.
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A7MCY6
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TBKB1_HUMAN
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TANK-binding kinase 1-binding protein 1 (TBK1-binding protein 1)
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MESMFEDDISILTQEALGPSEVWLDSPGDPSLGGDMCSASHFALITAYGDIKERLGGLERENATLRRRLKVYEIKYPLISDFGEEHGFSLYEIKDGSLLEVEKVSLQQRLNQFQHELQKNKEQEEQLGEMIQAYEKLCVEKSDLETELREMRALVETHLRQICGLEQQLRQQQGLQDAAFSNLSPPPAPAPPCTDLDLHYLALRGGSGLSHAGWPGSTPSVSDLERRRLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRAQDLASNQSERDMAWVKRVGDDQVNLALAYTELTEELGRLRELSSLQGRILRTLLQEQARSGGQRHSPLSQRHSPAPQCPSPSPPARAAPPCPPCQSPVPQRRSPVPPCPSPQQRRSPASPSCPSPVPQRRSPVPPSCQSPSPQRRSPVPPSCPAPQPRPPPPPPPGERTLAERAYAKPPSHHVKAGFQGRRSYSELAEGAAYAGASPPWLQAEAATLPKPRAYGSELYGPGRPLSPRRAFEGIRLRFEKQPSEEDEWAVPTSPPSPEVGTIRCASFCAGFPIPESPAATAYAHAEHAQSWPSINLLMETVGSDIRSCPLCQLGFPVGYPDDALIKHIDSHLENSKI
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Adapter protein which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity.
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A7MD48
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SRRM4_HUMAN
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Serine/arginine repetitive matrix protein 4 (Medulloblastoma antigen MU-MB-2.76) (Neural-specific serine/arginine repetitive splicing factor of 100 kDa) (Neural-specific SR-related protein of 100 kDa) (nSR100)
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MASVQQGEKQLFEKFWRGTFKAVATPRPESIIVASITARKPLPRTEPQNNPVVPAQDGPSEKLGQHLATEPLGTNSWERDKTCRELGATRGHSASHDKDLTPPPSSRGKKKKKKSTRKKRRRSSSYSPSPVKKKKKKSSKKHKRRRSFSKKRRHSSSSPKSKRRDEKRHKKQSRSRPRKSHRHRHHRCPSRSQSSESRPSSCESRHRGRSPEEGQKSRRRHSRRCSKTLCKDSPEAQSSRPPSQPLQMLGYLSARGVITGSGSAADLFTKTASPLTTSRGRSQEYDSGNDTSSPPSTQTSSARSRGQEKGSPSGGLSKSRELNSGNTSDSGNSFTTSSPQNKGAMLENLSPTSRGRESRGFQSPCLECAEVKKSSLVPSTARSSPMKGCSRSSSYASTRSSSHSSRSPNPRASPRYTQSRSTSSEKRSYSRSPSYSSKSGKRSPPSRSSRSRRSPSYSRYSPSRERDPKYSEKDSQQRERERARRRRRSYSPMRKRRRDSPSHLEARRITSARKRPIPYYRPSPSSSGSLSSTSSWYSSSSSRSASRSYSRSRSRSRSRRRSRTRTSSSSSSRSPSPGSRSRSRSRSRSRSRSRSQSRSYSSADSYSSTRR
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Splicing factor specifically required for neural cell differentiation. Acts in conjunction with nPTB/PTBP2 by binding directly to its regulated target transcripts and promotes neural-specific exon inclusion in many genes that function in neural cell differentiation. Required to promote the inclusion of neural-specific exon 10 in nPTB/PTBP2, leading to increased expression of neural-specific nPTB/PTBP2. Also promotes the inclusion of exon 16 in DAAM1 in neuron extracts (By similarity). Promotes alternative splicing of REST transcripts to produce REST isoform 3 (REST4) with greatly reduced repressive activity, thereby activating expression of REST targets in neural cells. Plays an important role during embryonic development as well as in the proper functioning of the adult nervous system. Regulates alternative splicing events in genes with important neuronal functions (By similarity).
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A7MQP0
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FADB_CROS8
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MLYKGDTLYLNWLEDGIAELVFDAPGSVNKLDTATVASLGHALDVLEKQHDLKALLLRSEKAAFIVGADITEFLSLFQVPAEQLSQWLHFANSVFNRLEDLPVPTLCAINGYALGGGCECVLATDFRLATPDARIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIAAGKDITADAALKVGLVDAVVKPEKLIEGALRMLRQAIDGELDWQARRQPKLEPLRLSKIEATMSFTIAKGMVMQTAGKHYPAPMTAVKTIEAAAGLGRDEALALENKSFVPLARSSEARALVGIFLNDQYVKGLAKKLTKETETPKQAAVLGAGIMGGGIAYQSAWKGVPVIMKDINEKSLTLGISEASKLLNKQLERGKIDGLKLAGVIATIHPTLDYAGFERADVVVEAVVENPKVKKAVLAETEEKVRPDTVIASNTSTIPISELASVLKRPENFCGMHFFNPVHRMPLVEVIRGEKTSDATIAKVVSWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRQIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDAGRFGQKNGKGFYAYQEDSKGKPRKVPDDAVDSLLAEVSQPKRAFSDEEIVARMMIPMVNEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTQGSAKYLDMAQHYQHLGPLYEAPAGLRDKASHNAPYYPQVEPAQPVGELQTA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A7MRY4
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LUXN_VIBC1
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Autoinducer 1 sensor kinase/phosphatase LuxN (EC 2.7.13.3) (EC 3.1.3.-)
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MFDFSLEAIVYAKAITLLATVAVVMMWLFYYCYRLKQKNEVIFGTHHAAYIAYSVCIIAWISSNAYFHTDLLPELGASAGMFMAKFANLASFFAFAFAYYFSCQLAAEQRKGKVHRWQQGIFVSLTVYSLFINLRPGLTVEHVDIVGPSQFIIEFGPHTSYFFIGLVSFVVLTLVNLVAMRTNSSKLTLAKTNYMIAGILVFMLSTAVIHLGMTYFMGDFSLTWLPPALSISEMLFVGYALLTSRFYSVKYIAYLALSVLLVCAIFVLPLGAIFIPLTESNQWLIAIPICALIGITWQLLYKKTSRYASFLIYGDKKTPVQQILSLEEDFKLSIDDAMRRLGKLLQIPNDKLRLVTSNYNETFYEEYLSSNRSVLVFDELSEELEYKVSAKRSMKALYDKMSSNNTALVMPLFGQGKSVTHLLISPHKSNNQMFSNEEISAVQTLLTRVQSTIEADRRIRQSRALANSIAHEMRNPLAQVQLQFEALKQHIENHAPVEQITLDIENGQAAIQRGRQLIDIILREVSDSSPEHEPIAMTSIHKAVDQAVSHYGFENEKIIERIRLPQHTDFVAKLNETLFNFVIFNLIRNAIYYFDSYPDSQIEISTKTGPYENTLIFRDTGPGIDETISHKIFDDFFSYQKSGGSGLGLGYCQRVMRSFGGRIECKSKLGTFTEFHLYFPVVPNAPKADTLRTPYFNDWKQNKRSNEHKVAPNVQINNQSPTVLIVDDKEVQRALVQMYLNQLGVNSLQANNGENAVEVFKANHVDLILMDVQMPVMNGFDASQRIKELSPQTPIVALSGESGERELDMINKLMDGRLEKPTTLNALRHVLGNWLNKNTASSACEAERE
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At low cell density, in the absence of AI-1 (autoinducer 1), LuxN has a kinase activity and autophosphorylates on His-471. The phosphoryl group is then transferred on Asp-771 of the response regulator domain. The phosphoryl group is transferred to LuxU, and ultimately to LuxO. At high cell density, in the presence of AI-1, the kinase activity is inactivated, and the response regulator domain has a phosphatase activity. LuxN phosphatase acts on itself. As LuxU could function to establish an equilibrium between the aspartyl-phosphate of LuxN and the aspartyl-phosphate of LuxO, LuxU transfers phosphate from LuxO to LuxN and finally phosphate is drained from the system.
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A7N805
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MPAA_VIBC1
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Murein peptide amidase A (EC 3.4.17.-) (Gamma-D-Glu-Dap amidase) (Zinc metallocarboxypeptidase MpaA)
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MNRYYSNNQEITVSLIPRTERAAFLITPTSYGKSVLGAPLLYFPAQVESNSRGLILAGTHGDETASIAGLSCALRSLPAECLKHDVILSMNPDANQLGTRANANQVDLNRAFPTQNWTEHGTVYRWSSHTPVRDVKVKTGDKEQLEPEVDALISLIELRRPKFVVSFHEPLAFVDDPAHSDLAKWLGKQFNLPIVDDVDYETPGSFGTWCNERQLPCITVELPPISADLTIEKHLDAFIALLQHDPDL
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Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap. Has weak activity with L-Ala-gamma-D-Glu-L-Lys, MurNAc-tripeptide and gamma-D-Glu-meso-Dap. Cannot hydrolyze murein tetrapeptide.
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A7RDN6
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RNLS_MOUSE
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Renalase (EC 1.6.3.5) (Monoamine oxidase-C) (MAO-C) (mMAO-C)
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MSRVLVVGAGLTGSLCAALLRKEITAPLYLGLWDKGGDIGGRMITASSPHNPRCTADLGAQYITCSPHYVKEHQNFYEELLAHGILKPLTSPIEGMKGKEGDCNFVAPQGFSSVIKYYLKKSGAEVSLKHCVTQIHLKDNKWEVSTDTGSAEQFDLVILTMPAPQILELQGDIVNLISERQREQLKSVSYSSRYALGLFYEVGMKIGVPWSCRYLSSHPCICFISIDNKKRNIESSECGPSVVIQTTVPFGVQHLEASEADVQKLMIQQLETILPGLPQPVATICHKWTYSQVTSSVSDRPGQMTLHLKPFLVCGGDGFTHSNFNGCISSALSVMKVLKRYI
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Catalyzes the oxidation of the less abundant 1,2-dihydro-beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+). The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis.
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A7T1N0
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TMP2L_NEMVE
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Transient receptor potential cation channel subfamily M member-like 2 (nvTRPM2)
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MGKDSFTPLYDGGDSSHVHLNKFGSNQLSQSKKSWIARNFSRRECIRFVPKSHDVSRCKCGRPRERHSQQALESGQGSEEWNVASCTTKHPTNAYGEIDFEGYGGQKRAPYLRMSHDTDANLVITLMLKRWNLEIPNLVISVTGGAKSFVLKPRLREMFRRGLIKAAKTTGAWIITGGTNTGVMKHVGEAVKEQQLMFGSDTQVNVIGIATWGIVDKQSDLISEKNGKYPALYSMEPTPGHQGAMLDPNHSHFFLVDDGTEGKYGVEIGMRSRIEEAIMKVKTDSRSEAGSIGVPVVLLVLEGGPNTVATMYELIKKKVPAVVIDGSGRAASVVGFAYNHTIKRNVDGQTINVIDPQYEDEVRAKVVEVFGAKGADKTYSMIKDVLEDEKMISVYSLDGEISQDIDLAILKALLKANRSSPVAQLNLALAWNRIDLAKSDIFTEEQQWTTETLSAAMLTALLDDKAEFAELFLQNGLSMREFLSLDILCKLYAEVPGNTTIKPLLQKEMGKRQVKTIDMDVVGEVIEELMGDMFESYYRKDGHYFGELASYAEGLVLKNRKSSKDLLANINRIDPLPTPYLDVFLWAVLCNRRELARVLWEAGREPMAAALMASRLLKRMASRAQEDNTITDISSDLYDHARLFEERAVGVLDECFNENETLSQTLLVRELDHYSRMTALELAVSAESQDFIAHTSCQVLLTRLWMGTMAMNTRWWKVLVCLYLPVLIFPIIYFVPDEQHERQAAEREHQKSLNQKSSKVKSHKEKNDAPVVPVYRSKEEKAVSNDEEARVGTENEEEDFQLEDYIPEIREDDSMEVIMRNKKLGFCDRIMHFYSAPFSKFVGNVVGYLAFIFLYAYVVLFNFPRFDPAKTLGGIHPTEIVLYFWVFTILIEEIRQLAAKPPKYIKDKVSVYFSDTWNFVDIFSLTVFIIAIILRFFTNSRIFTASRIILSLDIIFFIVRSLQIFSVNRLLGPKLVMIQKMMQDLAQFIIILAVFTIAYGIALHAVMFPSPGIYARNNTWVTITSVVQYPYWQMYGELFLDEIQGEKPKEFGEVDPDGRWLSPLLLAIYMVFTNILLLNLLIAIFNYTFERVQEDSDKVWKFQRYDLVQEYHSRPVFAPPLVLLGHILIFIRWVWRMCRCGHPPRGSTMKIGLSPAEMEQMDNWEFQAAEMYIHQQQQKNSGTLEERVRALGDRVDCINSQLNRVLDSMSGTRAHALTDGNGLEGGHDSEGRLARMEVELSSNSESLQKILALLQQQPPVKGQAAVPIQLTLLHYKARSSPYPGSTAKRFAVQDNMVDWQVPFPDYKPVNYTAPVVLANPVWADKDLMAMSPRPELPYNQMDHTCNVNRVSYNGTYVVKDGLPLNPMGRTGMQGRGLLGRFGPNHAADPVVTRWKRTSAGVMLQGGKKVLEFVAIQRKDNNQWAIPGGMVEPGQLVTQALKAEFGEEAMAKLNVSQEEKERIAKQIERLFQQGQEIYKGYVDDPRNTDNAWMETVAVNFHDDKGDLFGDITLQAGDDAAAVRWQRVSGNIPLYASHVSILEKVAKMRDAAF
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Nonselective, voltage-independent cation channel that mediates Ca(2+) and to a lesser extent Na(+) influx, leading to increased cytoplasmic Ca(2+) levels. Functions as ligand-gated ion channel. Binding of ADP-ribose causes a conformation change the channel is primed but still requires Ca(2+) binding to trigger channel opening. May have ADP-ribose pyrophosphatase activity which reduces ADP-ribose levels induced by oxidative stress, thus preventing the channel activation by reactive oxygen species.
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A7TUE1
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CCLOP_MEDTR
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Protein CYCLOPS (MtCYCLOPS) (DMI3-interacting protein IPD3) (Interacting protein of DMI3) (MtIPD3) (MtSYM1)
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MEGRGFSGLYKNSSEELFLKTVMESPIGMPVPTMEMLGFKTVSQSFRTDSEELFKRWLTNDQEGYNSSSMGLNSRLSKRISTEIANMSNQQHIGVASEGRNNDKSCLQNNFLANDVSSDFNFPIRDPVDRELQSSNLFLAKAWFITDQRMTRSRSSELRRRYTEMQNSQAPQGLDSMFMVPEHDTNTIKEELANFNGFDYLSMCELPSQKGTFMSPSNSSSSTFNTHQLVDVDKVSSCVSMLKGTLQRKKLECQVEKEAAEDGLNEIFCIREPLFQSAFNEEESWNQQKLVNVQGDFTDQVNDPGVMQTLEGTTNFVLDGFANQTNQIQGRTASGEPSQSESSAAAPVISSGLDACEGPSNSNQTLGDSSWKQVGESTQNKVRGVREQIMDNLKDDRKRKSLERYGSVTSAVSDGKMDNTKKRRVERSRKMAEAKERNLTPTIPSDMQAILKRCENLEKEVRSLKLNLSFMNRKDSEQTKQIEDLQKQNEDLADEKERLLEEIERILSETGKI
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Involved symbiotic signaling. Required for root infection by symbiotic rhizobia, infection thread (IT) formation, and nodule development. Required for proper induction of early nodulin gene expression. Probably not involved in nodule organogenesis. Involved in arbuscular mycorrhizal (AM) symbiosis. Required for fungal infection of the outer cortical cell layers, and for arbuscule development during the AM symbiosis. Acts downstream of CCAMK. Required for symbiosome formation (i.e. the release of the bacteria from the ITs) and subsequent symbiosome development. Required for the expression of the nodule-specific RPG gene, which controls proper IT growth and is essential for symbiosome formation. Acts upstream of ERN1, a transcriptional regulator required for nodulation.
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A7TZE6
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SKIT1_MOUSE
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Selection and upkeep of intraepithelial T-cells protein 1 (Skint-1) (Immunoglobulin-like and transmembrane domain-containing protein expressed in skin and thymus protein 1)
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MGSTGLCFYGHCIVMFLLQMVTASSEPFIVNGLEGPVLASLGGNLELSCQLSPPQQAQHMEIRWFRNLYTEPVHLYRDGKDMFGEIISKYVERTELLKDGIGEGKVTLRIFNVTVDDDGSYHCVFKDGDFYEEHITEVKITAINLQVQIHVHPPNTKGVIVECHSGGWFPRPLMQWRDRRGEVIPAASKSHSQGRDKLFNMKISLLISESFFQKVICCLQNPLTGQEERTSVILSDAFFSWNRIWKMILGIILSMMVVSIFVFSCLLHHEHKVCKWKWDAPWIKGLLIMTSSMVTVVLVMVYLHMKQRVPVSDVHFELDTLWVEDISVILCSLMVPATMLVSYTYFRLKDWCQHNHAQRVFTSN
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May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus. Plays a central role in mediating key epithelial-immune interactions by being involved in the selection of Vgamma5(+)Vdelta1(+) T-cells, which constitute 90% of epidermal gammadelta T-cells.
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A7UL74
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CTF7_ARATH
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Protein CHROMOSOME TRANSMISSION FIDELITY 7 (EC 2.3.1.-) (Cohesion establishment factor CTF7) (Protein ESTABLISHMENT OF COHESION 1)
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MQAKINSFFKPSSSSSIAASVTTDTDDGLAVWENNRNAIVNTYQRRSAITERSEVLKGCIEKTLKKGSSSVPKNHKKKRNYTQFHLELGQSDFLLRHCAECGAKYAPGDELDEKNHQSFHKDYMYGLPFKGWQNEKAFTSPLFIKNRIVMVSENDSPAHRNKVQEVVKMMEVELGEDWILHQHCKVYLFISSQRISGCLVAEPIKEAFKLIASPDDERQLQKESSSSPSTSIQFGNIVLQREVSKRCRTSDDRLDNGVIVCEEEAKPAVCGIRAIWVSPSNRRKGIATWLLDTTRESFCNNGCMLEKSQLAFSQPSSIGRSFGSKYFGTCSFLLYKAQLIDTHFS
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Acetyltransferase required for the establishment of sister chromatid cohesion. Involved in preservation of genome integrity and meiosis. Required for DNA repair and for the regulation of chromosome segregation during mitotic cell division. Knock-down mutants are extremely dwarf. Regulator of sister chromatid cohesion in meiosis which negatively regulates cohesin association with chromatin, acting as an antagonist of WAPL1 and WAPL2.
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A7VJC2
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ROA2_RAT
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Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)
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MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIFLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY
|
Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm. Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion. Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity). Also plays a role in the activation of the innate immune response. Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6. In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (By similarity).
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A7WLH8
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SUMO1_PIG
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Small ubiquitin-related modifier 1 (SUMO-1)
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MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV
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Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1 this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3.
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A7WM73
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HEXO1_ARATH
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Beta-hexosaminidase 1 (EC 3.2.1.52) (Beta-GlcNAcase 1) (Beta-N-acetylhexosaminidase 1) (Beta-hexosaminidase 2) (AtHEX2) (N-acetyl-beta-glucosaminidase 1)
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MSTNLLRLILLFITLSITSSLSTPSPADSPPYLWPLPAEFSFGNETLSVDPTVTLIVAGNGGGSLIIRAAFDRYMGIIFKHASGRGSLLSRIRFLKMVEYDITSLKIVVHSDSEELQLGVDESYTLMVSKKNEQSIVGAATIEANTVYGALRGLETFSQLCAFDYITKSVQIYKAPWYIQDKPRFGYRGLLIDTSRHYLPIDVIKQIIESMSFAKLNVLHWHIVDEQSFPLETPTYPNLWKGAYSRWERYTVEDASEIVRFAKMRGINVMAEVDVPGHAESWGTGYPDLWPSLSCREPLDVTKNFTFDVISGILADMRKIFPFELFHLGGDEVNTDCWKNTTHVKEWLQGRNFTTKDAYKYFVLRAQQIAISKNWTPVNWEETFSSFGKDLDPRTVIQNWLVSDICQKAVAKGFRCIFSNQGYWYLDHLDVPWEEVYNTEPLNGIEDPSLQKLVIGGEVCMWGETADTSVVLQTIWPRAAAAAERMWSTREAVSKGNITLTALPRLHYFRCLLNNRGVPAAPVDNFYARRPPLGPGSCYAQ
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Has a broad substrate specificity. Can use synthetic substrates such as pyridylaminated chitotriose, pyridylaminated chitobiose, p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc-6SO(4)) as substrates. Removes terminal GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Required for the presence of paucimannosidic N-glycans in glycoproteins of roots and, to a lower extent, of leaves.
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A7WPL6
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BBLB_TOBAC
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Berberine bridge enzyme-like B (NtBBLb) (EC 1.1.1.-)
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MFPLIILISFSLTSLSATATSGAGGGVANLYTCLIDHNVHNFSIYPTKNDQSSSNYFNLLDFSLQNLRFAASYMPKPTVIILPNSKEELVSTILCCRQASYEIRVRCGGHSYEGTSYVSFDGSPFVIVDLMKLDEVSVDLDSETAWAQGGATIGQIYYAIAKVSDVHAFSAGSGPTVGSGGHISGGGFGLLSRKFGLAADNVVDALLIDADGRLLDRKAMGEDVFWAIRGGGGGNWGIIYAWKIRLLKVPKIVTTCMIYRPGSKQYVAQLLQKWQIVTPNLVDDFTLGVLLRPADLPADMKYGNSTPIEIFPQFNALYLGPKTEVLSISNEEFPELGVKNDECKEMTWIESALFFSELADINGNSSNDISRLKERYMDGKGFFKGKTDYVKKPVSMDGMLTFLVELEKNPKGYLVFDPYGGAMDKIDDQAIAFPHRKGNLFAIQYLAQWNEEDDYKSDVYMEWIRGFYNTMTPFVSSSPRGAYINYLDMDLGVNMDDDYLLRNASSRNSSSSVDAVERARAWGEMYFLHNYDRLVKAKTQIDPLNVFRHEQSIPPMLGSTQEHKYSSE
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Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins) nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids.
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A7WYY0
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HCHA_STAA1
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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A7X5R6
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BAG6_ORNAN
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Large proline-rich protein BAG6 (BCL2-associated athanogene 6) (HLA-B-associated transcript 3)
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MDPGGGGGGGGPGPGPDMEEPADLEVSVKTLDSQTRTFTVGAEMTVKEFKEHIAAAVSIPPDKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTQGPSSGGASRAGSPSAPHAGAPPAGPRGPGAPVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMLRDIQALLARLEPQPGQQGQQGQQQGQALLAESGPPRPGPPGQTDGETSPREPTETREPTETREPEDGVAARGTGPAPGPAPAPAPEGNAAPNHPSPAEYAEVLQELQRVESRLQPFLQRYRAILGAAATTDYNNNTEGREEDQRVINLVGESLRLLGNTFVALSDLRCNLSATAPRHLHVVRPMSHYTAPMVLQQAAIPIQINVGTTVTMTGSGARPGPTDTTPTSGQTSSPTPSPTSGEPGPDGAPSGPAPPQAAGPPRLIRISHQSVEPVVMMHMNIPDSGSQTGGTSSASTASTGLPGQGLGQQVSGFPAAPTRVVIARPTPPQARPPHPGGPPPAPGATIPVPGSNASLAQMVSGLVGQLLMQPVLVAQGASGLGAPQAPATASASAGTTNTATTAGPAPGGPAQPPPPPPPGPPQAEVQFSQLLGSLLGPGVPGGPGTAGGATSVGSPTITVAMPGVPAFLQGMTDFLQATQTAPPPPPPPPPPPAPEQAPAAAPPGSPPAGPGGAGGGPEALPPEFFTSVVQGVLSSLLGSLGARAGSGESIAGFIQRLSGSSNIFEPGADGALGFFGALLSVICQNLSMVDVVMLLHGHSQPLQRLQPQLRGFFHQHYLGGREPTGPAIRRATHTLITGLEEYVRDSFASVQVQPGVDITRTNLDFLQEQFNGIAAHVLHCTDSSFGVRLLELCNQGLFECLALNLHCLGGQQSALTNVINGRIRRLSGGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDQVLRYVRRLGEPPQPPPEEPMDVQGAERAPPEPERENASPAPGTTAEEAMSRGPPPAPEGPPPLEEQDGAAAAESEPWAAAVPPEWVPIIRQDLQTQRKVKPQPPLSDAYLSGMPAKRRKLRSDLQQRLRADPNYSPQHFPNAQRAFMDEP
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ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome. SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response. BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis. Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2). Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC).
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A7X657
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ITPK1_SOYBN
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Inositol-tetrakisphosphate 1-kinase 1 (GmItpk1) (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase 1) (Inositol-triphosphate 5/6-kinase 1) (Ins(1,3,4)P(3) 5/6-kinase 1) (EC 2.7.1.159) (Inositol-hexakisphosphate 5-kinase) (EC 2.7.4.21)
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MAEKRFGVIGYALAPKKQNSFIRDSLVSLAKSRGIELVRVDSDKPLADQGPFDCVLHKLYGDDWKRQLQEFHTLYPNAVILDAPEAIERLHNRISMLQVVSELRIEDRPETFGIPKQIVIYDKATLLDPQAWESLKFPVIAKPLVADGSAKSHKMALVFTRDALNKLKPPIVLQEFVNHGGVIFKVYVVGEHVRCVKRKSLPDVSDEEKALGGVSEDLMSFSQVSNLATVNDCDGYYRLMHLDDDTEMPPDAFVVDIAGGLRRALKLNLFNFDVIRDARYGNRYLIIDINYFPGYAKMPGYEAVLTQFFCEVMLKKKQQEEQQQEEGNAPKEKEESLQA
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Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3. May participate in an inositol lipid-independent pathway of InsP6 synthesis. Able to add a beta-phosphate to InsP6 to yield 5-InsP7, thus exhibiting InsP6 kinase activity. Has also some Ins(1,3,4,5,6)P5 phosphatase activity.
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A7X665
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ITPK2_SOYBN
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Inositol-tetrakisphosphate 1-kinase 2 (GmItpk2) (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase 2) (Inositol-triphosphate 5/6-kinase 2) (Ins(1,3,4)P(3) 5/6-kinase 2) (EC 2.7.1.159) (Inositol-hexakisphosphate 5-kinase) (EC 2.7.4.21)
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MSESEVAGQRYRVGYALQGKKVESFIQPSLLDHAKQHSIDLVQIDPTAPLQQQGPFHCIIHKLHTQHWKNLLQQFSSKHPNTVIIDPPELVDRLHNRVSMLDAVTHLQFSLENATIGVPKQVVVNEPKSFDLHKFEEEQGLRFPVIAKPLAADGGAGSHELCLVFDEEGLHALSVPMVLQEFVNHGGVVFKIYVAGQRVNCVKRKSLGDITEEKLKVLRGSLPFSRVSSLGVEDEGGGAVEDAEMPPQSLVGELARGLREALGLNLFNVDVIRDGKEPTRYLVIDINYFPGYAKLPSYEPFITDFLLDIVRSKTA
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Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3. May participate in an inositol lipid-independent pathway of InsP6 synthesis. Barely able to add a beta-phosphate to InsP6 to yield 5-InsP7, thus exhibiting negligible InsP6 kinase activity. Has also Ins(1,3,4,5,6)P5 phosphatase activity. Probably involved in the regulation of drought and salinity tolerance by diverting the flux of inositol phosphate pool towards phytate biosynthesis.
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A7X672
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ITPK3_SOYBN
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Inositol-tetrakisphosphate 1-kinase 3 (GmItpk3) (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase 3) (Inositol-triphosphate 5/6-kinase 3) (Ins(1,3,4)P(3) 5/6-kinase 3) (EC 2.7.1.159)
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MRLREEVACKNDDVCEKEEVVIENDVTVAQNHWCPVVNAGFSSPKRVVVVGYALTTKKIKSFLQPKLEGLARNKGILFVAIDHNRPLSDQGPFDIVLHKLSGKEWRQVLEDYRLSHPEVTVLDPPDAIQHLRNRQYMLQAVADMNLSDSYGIVGVPRQLVIKRDALAIPELVNKAGLTLPLVAKPLVADGSAKSHELSLAYEHFSLQNLEPPLVLQEFVNHGGVLFKVYIVGDAIKVVRRFSLPDVSKWELSKDAGIYRFPRVSCAAASADDADLDPTVAELPPRPLLEKLAKELRWRLGLRLFNLDIIREYGTRNHFYVIDINYFPGYGKMPEYEHIFTDFLLSLGQGKYKKK
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Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3. May participate in an inositol lipid-independent pathway of InsP6 synthesis.
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A7X680
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ITPK4_SOYBN
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Inositol-tetrakisphosphate 1-kinase 4 (GmItpk4) (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase 4) (Inositol-triphosphate 5/6-kinase 4) (Ins(1,3,4)P(3) 5/6-kinase 4) (EC 2.7.1.159)
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MRLNGEISSGEEEEEEKQTGTTTFSSQKVVVGYALTSKKKKSFLQPSFTGLARNRGINFVAIDLNKPLPEQGPFDIILHKLSGEVWREIIEDYREKHPEVTVLDPPDAIQHLHNRQSMLQDVLDLNLSDCHGKVGVPRQLVITKEKDPSSIPYEVTKAGMKLPLVAKPLVVDGTAKSHELFLAYDEFSLSAVEPPLVLQEFVNHGGLLFKIYIVGETIKVVRRFSLPNISKRELSKVAGVFRFPRVSCAAASADDADLDPNIAEHPPRPLLERLARELRHRLGLHLFNIDMIREYGTKDVFYVIDINYFPGYGKMPGYEHVFTDFLLSLVESKCSNKKLAA
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Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4, Ins(3,4,6)P3 and Ins(1,3,4)P3. May participate in an inositol lipid-independent pathway of InsP6 synthesis.
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A7X8B3
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PRGR_PANTR
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Progesterone receptor (PR) (Nuclear receptor subfamily 3 group C member 3)
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MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSNEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPLMSRSGCKAGDSSGTAAAHKVLPRGLSPSRQLLLPASGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPXRSPLATTMMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAXSAFAPPRSSPSASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRAPPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGIPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK
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The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation.
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A7X8B7
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PRGR_GORGO
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Progesterone receptor (PR) (Nuclear receptor subfamily 3 group C member 3)
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MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPYPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLETLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPLMSRSGGKAGDSSGTAAAHKVLPRGLSPSRQLLLPVSGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPSASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRAPPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGIPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK
|
The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation.
|
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