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B8NFL5
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CP51B_ASPFN
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Sterol 14-alpha demethylase (EC 1.14.14.154) (Cytochrome P450 monooxygenase 51B) (Ergosterol biosynthesis protein cyp51B)
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MGILAVILDSVCERCSGSSLWMLSTVALLSILVVSVVINVLRQLLFKNYKEPPLVFHWFPFIGSTISYGMDPYRFFFNCREKYGDIFTFVLLGKKTTVYLGTKGNDFILNGKLRDVCAEEVYSPLTTPVFGRHVVYDCPNAKLMEQKKGPNGVFDVCKTIAEITIYTASRSLQGKEVRSRFDSTFAELYHDLDMGFAPINFMLPWAPLPHNRKRDAAQKRMTETYMEIIKERRKAGSKKDSEDMVWNLMSCMYKDGTPVPDEEIAHMMIALLMAGQHSSSSTAAWIVLHLAASPEITEELYQEQLRILGHDMPPLTYENLQKLDLHAKVIKETLRIHAPIHSIIRAVKNPMPVEGTPYVIPTSHNVLSSPGVTARSEEHFPDPLEWKPHRWDEAIAVSSEDEEKVDYGYGLVTKGTNSPYLPFGAGRHRCIGEQFAYVQLGAITAALVRLFKFSNLPGVQTLPDTDYSSLFSKPLGNSKIQFEKREPVTKA
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Sterol 14alpha-demethylase, encoded by cyp51A, cyp51B and cyp51C, that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (By similarity). Can also use susbtrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity). As a target of azole drugs, plays a crucial role in azole susceptibility.
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B8NSJ0
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SKP1_ASPFN
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E3 ubiquitin ligase complex SCF subunit sconC (Sulfur controller C) (Sulfur metabolite repression control protein C)
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MATPTLTFTSSDGVDIPVERDVAERSQLIKNMLEDLGETGEPIPIPNVNEAVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKGLLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEDR
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Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity).
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B8NUK6
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CP51C_ASPFN
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Sterol 14-alpha demethylase (EC 1.14.14.154) (Cytochrome P450 monooxygenase 51C) (Ergosterol biosynthesis protein cyp51C)
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MSWPRIGAYALLAFVAIMALNVTYQFLFRMLNKTRPPLVFHWIPFIGSTIHYGMDPYGFFFSCREKYGDIFTFILLGRPTTVYLGTQGNEFILNGKLKDVNAEEVYSPLTTPVFGSDVVYDCPNSKLIEQKKFIKFGLSQAALEAHVPLIEKEVEDYLAMSPNFHGTSGEVDIPAAMAEITIFTAGSALQGEEVRSKLTTEFAVLYHDLDKGFTPINFMLPWAPLPHNKKRDAAHARMRSIYIDIINKRRNAGDNVPEKLDMIGNLMQCTYKNGQPLPDKEIAHIMITLLMAGQHSSSSISSWIMLRLASQPAVVEELYQEQLANLERTGPNGSLAPLQYKDFDNLPLHQNVIRETLRLHSSIHSLLRKVKNPLPVPGTPYVIPTSHVLLAAPGVTALSDEYFPNAMAWDPHRWETQAPQENNKDDIVDYGYGAMSKGTSSPYLPFGAGRHRCIGEKFAYLNLAVIVATMVRHLRFSNLDGQTGVPDTDYSSLFSGPMKPARIRWERRAAKSG
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Sterol 14alpha-demethylase, encoded by cyp51A, cyp51B and cyp51C, that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-demethylase catalyzes the three-step oxidative removal of the 14alpha-methyl group (C-32) of both these sterols in the form of formate, and converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol, respectively, which are further metabolized by other enzymes in the pathway to ergosterol (By similarity). Can also use susbtrates not intrinsic to fungi, such as 24,25-dihydrolanosterol (DHL), producing 4,4'-dimethyl-8,14-cholestadien-3-beta-ol, but at lower rates than the endogenous substrates (By similarity). As a target of azole drugs, plays a crucial role in azole drug susceptibility.
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B8PYG1
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NSMF_DANRE
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NMDA receptor synaptonuclear signaling and neuronal migration factor (Nasal embryonic luteinizing hormone-releasing hormone factor) (Nasal embryonic LHRH factor)
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MGTVVSKKENLRNDAISSVAAKVRAARAFGEYLSHTRPENRNRSDHLLSDTFIGQETDSPDISRLNNNNSLQPYSQHTLIVKPSQEELQQGSQSAPLPTSSKRRLSVERSLSSEDQQNQRRTESSVKPARVYTITRERDMLGGQGSEESLELEVLKRTSEPSQINPPTGLRGSHHRGSQHRGNNGPTHQHHYGHAPMAQPLQSSGSTHNIRDWGSRRSRSREDCTPDCVACIRPHCQSQRSLDLDTSPHGGGKQHKKLERMYSEDRVSSEDREDHTNSWFPKENMFSFQTATTTMQAISNFRKHLRMVGSRRVKAQTFVDRKAKSFSRSWSDPTPVKPDSLHDSRDSGDLQASSGNLDEEDCDDVDWEEERELERVACEGDDFIPPKLMLISSKVPKAEYVPNIIRRDDPSIIPILYDHEHATFDDILEEIEKKLTAYRKGCKIWNMLIFCQGGPGHLYLLKNKVATFAKVEKEEGMMQFWKKLGRFMSLLNPEPNLIHIMGCYVLGNANGEKLFQNLKRLMKPHGIEFKSPLELSAQGKEMIEMYFDFRLYRLWKTRQHSKLHDYDDLL
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Stimulates outgrowth of olfactory axons and migration of hypophysiotropic gonadotropin-releasing hormone 3 (GnRH3) neurons. May couple NMDA-sensitive glutamate receptor signaling to the nucleus and trigger long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes.
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B8Q0B2
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POPD1_PIG
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Blood vessel epicardial substance (Popeye domain-containing protein 1) (Popeye protein 1)
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MNYTESSPLAESTAIGFTPELGSITPVPSNETTCENWREIHHLVFHVANVFFAIGLVLPTTLHLHMILLRGMLTIGCTLYIVWATLYRCALDIMIWNSVFLGINVLHLSYLLYKKRPVKIEKELKGIYQRLFEPLRVPPDLFKRLTGQFCMIQTLKKGQAYAAEDKTSVDDRLSILLKGKMKVSYRGHFLHNIYPCAFIDSPEFRSTQMHKGEKFQVTIIADDNCRFLCWSRERLTYFLESEPFLYEVFRYLIGKDITNKLYSLNDPTLNDKTIKKLDHQLSLCTQLSMLEMRNSIVSTSDSEDGLHQFLRGTSSVSSLYVPSPHQRASAKMKPIEEGVEDDDEVFEPETPNTFKVRQLP
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Cell adhesion molecule involved in the establishment and/or maintenance of cell integrity. Involved in the formation and regulation of the tight junction (TJ) paracellular permeability barrier in epithelial cells. Plays a role in VAMP3-mediated vesicular transport and recycling of different receptor molecules through its interaction with VAMP3. Plays a role in the regulation of cell shape and movement by modulating the Rho-family GTPase activity through its interaction with ARHGEF25/GEFT. Induces primordial adhesive contact and aggregation of epithelial cells in a Ca(2+)-independent manner. Important for skeletal muscle and heart development. Also involved in striated muscle regeneration and repair and in the regulation of cell spreading (By similarity). Important for the maintenance of cardiac function. Plays a regulatory function in heart rate dynamics mediated, at least in part, through cAMP-binding and, probably, by increasing cell surface expression of the potassium channel KCNK2 and enhancing current density. Is a caveolae-associated protein important for the preservation of caveolae structural and functional integrity as well as for heart protection against ischemia injury (By similarity).
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B8QHP1
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CP52M_STABO
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Cytochrome P450 52-M1 (CYP52-M1) (EC 1.14.14.80) (Cytochrome P450 monooxygenase CYP52-M1)
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MLIKDIILTPMSLSAVAGLLPLLFVAFLVLHEPIWLLWYRYAARRHKCSMPRFIEKSFPLGIQRTMDMIKTAKSYTLLEVQYDRVFNKFKARTYLRQAPLQYQIFTIEPENIKTILATKFNDFGLGARFHTVGKVFGQGIFTLSGNGWKQSRSMLRPQFTKDQVCRIDQISSHAAELIKEMNRAMKVDQFIDVQHYFHKLTLDTATEFLFGESCESLNPENQSCIVARDGSEITAEQFVESYNFLLNYAFKRTLSSKVYWLFNSKEFRDHKKRAQSYIDYYVDKALYATSFAAENSIAEKDAAAESSGIYVFSLEMAKVTRDPVTIRDQIFNILIAGRDTTAATLSFAIHFLARNPDVFNKLREEVLDHFGTKEEQRPLSFELLKQAPYLKQVINEVLRLAPVLPLNFRTAVRDTTLPIGGGPEQKDPIFVPKGTAVYYSIYMVHRDIKYWGPDAHEFNPNRWENLKLDNVWAFLPFNGGPRICLGQQFALTELSLTLVRLLQEYSKIEMGPDFPESPRFSTTLTAQHAPPGVVVRFS
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Catalyzes the first step of sophorolipid biosynthesis. Catalyzes the terminal (at the omega-position) or subterminal (at the omega(-1)-position) hydroxylation of a fatty acid. This converts the fatty acid to a substrate for the subsequent glycosyltransferase reactions. Oleic acid is the preferred substrate, but it acts on various other C-16, C-18 and C-20 saturated and unsaturated fatty acids, namely palmitic, palmitoleic, stearic, linoleic, cis-9,10-epoxystearic, trans-9,10-epoxystearic and arachidonic acid.
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B8X8Z0
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TOXN_PECAT
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Endoribonuclease ToxN (EndoRNase) (EC 3.1.-.-) (Toxin ToxN)
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MKFYTISSKYIEYLKEFDDKVPNSEDPTYQNPKAFIGIVLEIQGHKYLAPLTSPKKWHNNVKESSLSCFKLHENGVPENQLGLINLKFMIPIIEAEVSLLDLGNMPNTPYKRMLYKQLQFIRANSDKIASKSDTLRNLVLQGKMQGTCNFSLLEEKYRDFGKEAEDTEEGE
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Toxic component of a type III toxin-antitoxin (TA) system. An endoribonuclease which is active independently of the ribosome, cleaving between the second and third A of AAA(U/G) sequences, although not all occurrences of this tetranucleotide are cleaved. Digests many mRNA species, including its own transcript and its cognate antitoxin RNA ToxI. ToxI has 5.5 nearly identical 36 nucleotide-long repeats (a single repeat neutralizes the toxin in vivo) a single repeat folds into a pseudoknot which binds the toxin. The ToxI precursor RNA is a preferential target in vivo and is progressively degraded to single repeat lengths as ToxN-ToxI complex self-assembly occurs. In vivo expression of ToxI antitoxin inhibits endonuclease activity of ToxN. The toxin alone inhibits growth when expressed in E.coli without causing cell lysis this bacteriostatic effect is neutralized by cognate RNA antitoxin ToxI. Non-cognate antitoxin RNA from B.thuringiensis does not inhibit this toxin. The RNA antitoxin is less stable than the proteinaceous toxin synthesis of ToxI in the absence of new ToxN synthesis restores growth and also detectable accumulation of the ToxN protein. Negatively regulates its own operon in complex with ToxI. The toxin-antitoxin system functions in plasmid maintenance (a plasmid addiction system). The TA system protects P.atrosepticum strain 1043 against phage phiM1 and phiA2, E.coli against some but not all coliphages and S.marcescens against some bacteriophages, causing an abortive infection (Abi phenotype). Also protects P.atrosepticum strain 1043 against phage phiTE phage that escape Abi and grow in this bacterium have evolved a pseudo-ToxI RNA by expanding a pre-existing sequence similar to the bona fide ToxI repeats.
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B8XCH5
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QKY_ARATH
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Protein QUIRKY (Multiple C2 domain and transmembrane region protein 15)
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MNTTPFHSDPPPSRIQRKLVVEVVEARNILPKDGQGSSSAYVVVDFDAQKKRTSTKFRDLNPIWNEMLDFAVSDPKNMDYDELDIEVYNDKRFGNGGGRKNHFLGRVKIYGSQFSRRGEEGLVYFPLEKKSVFSWIRGEIGLKIYYYDEAADEDTAGGGGGQQQQQQQQQFHPPQQEADEQQHQQQFHPPPQQMMNIPPEKPNVVVVEEGRVFESAQSQRYTETHQQPPVVIVEESPPQHVMQGPNDNHPHRNDNHPQRPPSPPPPPSAGEVHYYPPEVRKMQVGRPPGGDRIRVTKRPPNGDYSPRVINSKTGGGETTMEKKTHHPYNLVEPMQYLFVRIVKARGLPPNESAYVKVRTSNHFVRSKPAVNRPGESVDSPEWNQVFALGHNRSDSAVTGATLEISAWDASSESFLGGVCFDLSEVPVRDPPDSPLAPQWYRLEGSGADQNSGRISGDIQLSVWIGTQVDEAFPEAWSSDAPHVAHTRSKVYQSPKLWYLRVTVLEAQDLHIAPNLPPLTAPEIRVKAQLGFQSARTRRGSMNNHSGSFHWHEDMIFVAGEPLEDCLVLMVEDRTTKEATLLGHAMIPVSSIEQRIDERFVPSKWHTLEGEGGGGGGGGGPGGGGGGGPYCGRISLRLCLEGGYHVLEEAAHVCSDFRPTAKQLWKPPIGILELGILGARGLLPMKAKNGGKGSTDAYCVAKYGKKWVRTRTITDSFDPRWHEQYTWQVYDPCTVLTVGVFDNWRMFSDASDDRPDTRIGKIRIRVSTLESNKVYTNSYPLLVLLPSGMKKMGEIEVAVRFACPSLLPDVCAAYGQPLLPRMHYIRPLGVAQQDALRGAATKMVAAWLARAEPPLGPEVVRYMLDADSHAWSMRKSKANWYRIVGVLAWAVGLAKWLDNIRRWRNPVTTVLVHILYLVLVWYPDLVVPTAFLYVVMIGVWYYRFRPKIPAGMDIRLSQAETVDPDELDEEFDTIPSSRRPEVIRARYDRLRILAVRVQTILGDFAAQGERIQALVSWRDPRATKLFIAICLVITIVLYAVPAKMVAVALGFYYLRHPMFRDTMPTASLNFFRRLPSLSDRLI
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May be involved in Ca 2(+)-dependent signaling and membrane trafficking. Plays a role in fruit dehiscence (Probable). Components of the machinery involved in organ development mediated by the receptor-like kinase STRUBBELIG (SUB). Collaboratively with SUB and POQ, regulates cell growth anisotropy during gynoecium development, thus linking together cell-cell communication and cellular growth. Together with SUB/SCM, links RLK-dependent signal transduction and intercellular communication mediated by plasmodesmata (PD) to regulate tissue morphogenesis. May function as a signaling molecule by regulating the trafficking of other regulators.
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B8XIA5
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MYC_MACMU
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Myc proto-oncogene protein (Proto-oncogene c-Myc) (Transcription factor p64)
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MDFFPVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSPRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASPDSSAFSPSSDSLLSSTESSPQASPEPLVLHEETPPTTSSDSEEEQEEEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEKDLLRKRREQLKHKLEQLRNSCA
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Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate 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).
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B8XTP8
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POLG_COSAA
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Genome polyprotein [Cleaved into: Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Rho) (Virion protein 4); Capsid protein VP2 (Beta) (P1B) (Virion protein 2); Capsid protein VP3 (Gamma) (P1C) (Virion protein 3); Capsid protein VP1 (Alpha) (P1D) (Virion protein 1); Protein 2A (P2A) (G); Protein 2B (I) (P2B); Protein 2C (C) (P2C) (EC 3.6.4.13); Protein 3A (P3A); VPg (P3B) (H) (Protein 3B); Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C) (p22); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
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MGANNSKESVSSNGNEGTIVNNFYSNQYYASIDASAQGVGTSTTPENGNVSGFLGLAGSAFNALSLLASPRTETGMMMEDRVLSRTAGNTSVNSQAAEGVLQAYGTETDSNSPTSCGDDPSKGTHATDRAFVIQLLPWKQTTNSYFAQWVRLTQKLSNNLHGNVMAKNIKSHAFAKMGFEVMLQANTSPFHNGILGLFLVPEFVRKGEITDEWIDLTPTSSLVSNTELYNPQTYANFPFDAKHSFDYSDITPEQFMIFPHQLINPKDTNVATVRVPYINIAPTNDTTVHTVWTAVVMVLVPLNFSSGASPTVSLTLTITPINSVFNGLHHTAQGPIPVRPFHNFQQFSTTVPLRTEPCYGMTVTPPVDYMPLPITDLVELAKVPSFVTVANSDTTSERSFPYFSVSNTEQGRNLFKSSVVLSDLHYQHTLVANLARYFCNYRGSLQFDFIAATTAMTRGKLLISYTPPGAGEPQSIDQAMMGTYAIWDLGLQSTFNFVVPFISASDFRFNTSSVSNALNSDGWITVWLMNPLTYPPSTPPTQQILMLMSAGSDFSYRLPISPGFAEGETSEHPMDNAECGKIDDKDAGMFSGHSVGLPTPHTSTSFFYDRYRFVGIVKSVVNNTPKPVNIYDDTGKVKNLQQVFPTSDTLLPHSLMSLSPCASVCGQPISSFLFAQRANPKKTLKLRSGDEFLYRCCPFSYIKCDLEFTVVPPANSTRDYIVHWYPPGATLDAGEVAVGNTSGSNGFDDNGMNAGSSLFSYNPTFHARAPSKVSAVIPFCLPVSLLPLYFDGFPDYSTTKGMYGCSPSFSFGTIYIESGLQETYSVYIRYKDFKGYAPRPLIRTPHIRLSERARYIMADSVLPRPLTRAERDVARDLLLIAGDIESNPGPAFNPEYTAHGPVTELIQLARKPETVDNVNRLLTTLNTLMAKWNNLKDTVTDAVFLRDMVCLLVKLTSLMYLVHGQGPGAYFAAASILLADGITFFDWYEKIKIFMARKLRVSPPFFPAAQGPDLRDFVTFFNAARGAQWMIDSLKSLITCIKQWLELEEENEAVQLEKMLIDSPRHCKAINDYNRGDSFQRPTNSFEFMDRLVECATKLGKVQIATYFRNFTTADSDTSRPEPVVVVLRGKPGVGKSAAATVMAAAVSKLLVGSQSVYTLSPDTEHMDGYHGQFVTLMDDLGQNPDGEDFRCFCQMVSCAQYRPAMADLKDKGILFTSRLLIATTNLPDFNPVTISDPRALDRRITFDILVTPGSAATKNGKLDLAAALKPDGPGEHPYTSDCPILHTTGLLLKNLRNNQTMNLKDLVDMIVKRIKHKKEVGNMLDSLVAQGPTMIVGYTKDDDGIAIVDCLEEWNKIKDKKKKQLALEMVAQELKDKHEEHKGTIKLLKMFVTGLGVVAAVAGAYATMKYFTKDKPKEEEEEPEEKKEKKTEESKEAAGPYNGPTKKEIKTLKLKAQSPLMDMEKKIAQNVMPFQIFYNGKRYTQSCLAIGKRVILVNKHAFESVEHKFVVDQKEYTLDQVTAISLDCGSGVTDVCAVCLPPGPDFKSIKKHFLPFNTTMFPGTRLTILSNDHYPMSREGSFLRFEDEVPTNVGNMPFVMLYKSTSYFGMCGSVVCSRFVDGGGIIGMHCAGGGGVSVGTRLTARMIESVFDYFYPPVAQGIIENTETGPRVHVPRTSKLKRTNATYPATEKYGPAALSRYDPRLNEGVNLDEVIFSKHTQNTLVEKGSTFRSALDMAAEIYGEKFRGNDFSPLSVEDAILGIPGLDRLDPNTASGLPYTKTRRQMIDFNTGQILDDTLKCRLGQWLAGRPPQEVHYQTFLKDEIRPIEKVKAGKTRIIDVPPLDHVIAFRMLFGRFIAHYHLNFGFKTGSAIGCDPDVAWASFGFELSGFPYLYDFDYSNFDASHSTSIFEILEQKFFSPELGFDPRCSLLLKSLAVSTHCYENKRLQIAGGLPSGTAGTSVLNTVINNIIFHGALYHTYTNFERDDISMLAYGDDIVVASKFELDLVMVKAFMNRIGYKITPADKSDEFRPKCMDDICFLKRRFVKVAGVWAPVMETENLEAMLSWYKPGTLNEKLQSVSRLAHFSGRDVYDHLFKPFIRDGFDVTPWKQLHLEWLNKLSA
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[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. [Capsid protein VP4]: Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity). After genome has been released, the channel shrinks (By similarity). [Protein 2C]: Associates with and induces structural rearrangements of intracellular membranes (By similarity). It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Interacts with IFIH1/MDA5 to inhibit the induction of the IFN-beta signal pathway (By similarity). [VPg]: Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains. [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease. Cleaves host PABP1, this cleavage is important for viral replication (By similarity). Cleaves host TANK and disrupts the TANK-TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the IFN-beta signal pathway (By similarity).
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B8XX90
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STING_PIG
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Stimulator of interferon genes protein (poSTING) (Transmembrane protein 173)
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MPYSSLHPSIPQPRGLRAQVAALVLLGACLVALWGLGELPEYTLRWLVLHLASQQIGLLVKGLCSLAEELCHVHSRYQSSYWRAARACLGCPIRCGALLLLSCYFYFSIRDKAGLPLPWMLALLGLSQALNILLGLQHLAPAEVSAICEKRNFNVAHGLAWSYYIGYLRLILPGLRARIQAYNQRHKNVLGGIGNHRLHILFPLDCGVPDDLSVADPNIRFLHELPQQSADRAGIKGRVYTNSIYELLENGQPAGVCVLGYATPLQTLFAMSQDGRAGFSREDRLEQAKLFCRTLEDILADAPEAQNNCRLIVYQEPTEGGSFSLSQEILRHLRQEEREVTMGSAETSVVPTSSTLSQEPELLISGMEQPLPLRSDIF
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Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol. Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state. In addition to promote the production of type I interferons, plays a direct role in autophagy. Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome. The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (By similarity). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'-cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP. The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free-ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (By similarity). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (By similarity).
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B8XY56
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RNT2_DANRE
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Ribonuclease T2 (EC 4.6.1.19) (RNase Dre2)
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MRFIAFAVIFSAVYLCSSAFTHPRGEWTKLILTQHWPQTFCKMEHCKTDFSYWTLHGLWPNTGVRCNTSWHFNASLIEDILPEMEKFWPDLLEPSSPKFWNYEWTKHGTCAAKSESLNSEHKYFGKALELYHKFDLNSVLLKNQIVPSEKHYTLEDVEEAITSAYGVKPKIQCVHPGQGGQVQILGQIEICVDRDFQLMGCEKSSEDTWSNDLPTVPVSGQSGLSVCDHSMPVYYPPVQA
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Has ribonuclease activity, with higher activity at acidic pH. Probably is involved in lysosomal degradation of ribosomal RNA.
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B8YG19
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XS20E_NEOPA
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Bifunctional acetylxylan esterase/xylanase XynS20E [Includes: Acetylxylan esterase (EC 3.1.1.72); Endo-1,4-beta-xylanase (Xylanase) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase)]
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MRLGVALSTIAVLLTATSARNLDKRQWGWPNFGGGNGGNGGNGGKTINDYKREQGAGRDIHVYAPSNLAPNSPLLLSLHGMDQDPNYQQSNTHWETLADSEGFVVVYPRGGTGMSTWDIQGTKDTQWVSQIIDQMKKEYNIDTKRVYLSGFSMGGMFTYHAMSQIANKIAAFAPCSGPNVFGASKAQRPVPIFHVHGTNDDVLNYQQVEGFLKNYRDQFHCPSQADTKTNYPNRENPNATLYTWGPCDKGVYIKHLKLQGRGHSPSSADIQDIWDFVSQWTVDGPVSASGNGGGNTTPTNPSTGGNGNGNGGGNTTPTNPSTGGNGNGNGGSTDKCSSNITKQGYKCCASNCEVVYTDSDGDWGVENDQWCGCGNRVTVGSGTCSAKILQQGYKCCPSGCIIYYTDEDGTWGVNGEEWCGCGSGSSSTGGGNDAPSSGSGYQGANGTNFCNNAKHSGESVTVTSNKVGDINGIGYELWADSGNNSATFYDDGSFSCSFQRAKDYLCRSGLSFDSTKTHKQIGHIYAEFKLVKQNIQNVDYSYVGIYGWTRNPLVEFYVVDNWLSQWRPGDWVGNKKHGDFTIGGAQYTVYENTRYGPSIDGDTNFKQYFSIRQQPRDCGTIDITAHFEQWEKLGMTMGKMHEAKVLGEAGSNNGGTSGTADFPFAKVYVKN
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Bifunctional acetylxylan esterase/xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades xylan from acetylxylan, beechwood, birchwood, and oat spelt, and releases acetate from 4-methylumbelliferyl acetate and beta-D-xylose tetraacetate. No activity is observed against carboxy methyl cellulose, beta-glucan, p-nitrophenol acetate, p-nitrophenol laurate, p-nitrophenol myristate, p-nitrophenol, palmitate, or beta-naphthol acetate.
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B8ZXI1
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QTRT2_MOUSE
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Queuine tRNA-ribosyltransferase accessory subunit 2 (Queuine tRNA-ribosyltransferase domain-containing protein 1)
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MKLSLIKVVNGCRLGKIQNLGKAGDCTVDIPGCLLYTRTGSAPHLTHQTLRNIHGVPGIAQLTLSSLAEHHEVLAEYKKGVGSFIGMPESLFYCSLHDPVTPGPAGYVTSKSVSVWGFGGRVEMTVSKFMAIQEALQPDWFQCLSDGEASCAETTSIKRARKSVDRSLLFLDSCLRLQEESEVLQKSVIIGVIEGGDVMEERLRSARETAKRPVGGFLLDGFQGDPAVTETRLHLLSSVTAELPEDKPRLICGVSRPDEVLECIERGVDLFESFFPYQVTERGCALTFTFDCQLNPEETLLQQNGIQEKIKGLDQAKKIEATGCNQEMTSFEINLKEKKYQEDFDPLVRGCSCYCCKNHTRAYIHHLLMTNELLAGVLLMMHNFEHYFGFFCSIREALKNDTLAQLKELICRQMF
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Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587}.
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B9DFA8
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INVC_ARATH
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Alkaline/neutral invertase C, mitochondrial (A/N-INVC) (EC 3.2.1.26)
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MNSRSCICVSAMKPCCRFLISFRSSSLFGFSPPNSGKFINSSKLHCTKIDSRSIRSGIHCRRIVLDRNAFCDSDSISWGGGGSRVLRARGSSRGRGRGVLVIPHVASDFRNYSTSSLDSHVNDKSFESMFVKPLVFKEVEKTEGIPKRERGNVGGGKDANFGNVGVRKETERCLSQTEVEKEAWKLLRGAVVNYCGFPVGTVAANDPGDTQTLNYDQVFIRDFVPSAYAFMLDGEGEIVRNFLLHTLQLQSWEKTVDCHSPGPGLMPASFKVKSAPLEGNDGSFEEFLDPDFGGSAIGRVSPVDSGLWWIILLRAYGKLTGDYTLQERIDVQTGIKLILKLCLADGFDMFPTLLVTDGSCMVDRRMGIHGHPLEIQALFYSALRCAREMLIVNDGTKSLVTAVNNRLSALSFHIREYYWVDIKKINEIYRYNTEEYSADATNKFNIYPEQIPTWLVDWIPDKGGYFIGNLQPAHMDFRFFTLGNLWAVISSLGNQEQNEGVMTLIEEKWDDLVANMPLKICFPALEKDEWRIITGSDPKNTPWSYHNGGSWPTLLWQFTLACIKMGKLELAKKAVAVAEKRLKEDEWPEYYDTKSGRFVGKQSRLYQTWTIAGFLAAKKLIEQPEKASLLFWEEDYQLLETCVCGLSKSSGRKNKCSRFTPPRS
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Mitochondrial invertase that cleaves sucrose into glucose and fructose and is involved in the regulation of aerial tissue development and floral transition. May be modulating hormone balance in relation to the radicle emergence.
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B9DFG3
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ISE2_ARATH
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DExH-box ATP-dependent RNA helicase DExH15 chloroplastic (EC 3.6.4.13) (ATP-dependent RNA helicase ISE2) (Protein EMBRYO DEFECTIVE 25) (Protein INCREASED SIZE EXCLUSION LIMIT 2) (Protein PIGMENT DEFECTIVE 317)
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MNTLPVVSLTASSSFKFFHFPSLHRSLSHSPNFSFTKSLILNPNHLSFKSTLNSLSPSQSQLYEEEDDEEEEEEDEDDDDEAADEYDNISDEIRNSDDDDDDEETEFSVDLPTESARERVEFRWQRVEKLRSLVRDFGVEMIDIDELISIYDFRIDKFQRLAIEAFLRGSSVVVSAPTSSGKTLIAEAAAVSTVAKGRRLFYTTPLKALSNQKFREFRETFGDDNVGLLTGDSAINKDAQIVIMTTEILRNMLYQSVGMASSGTGLFHVDAIVLDEVHYLSDISRGTVWEEIVIYCPKEVQLICLSATVANPDELAGWIGEIHGKTELVTSTRRPVPLTWYFSTKHSLLPLLDEKGINVNRKLSLNYLQLSASEARFRDDDDGYRKRRSKKRGGDTSYNNLVNVTDYPLSKNEINKIRRSQVPQISDTLWHLQGKNMLPAIWFIFNRRGCDAAVQYVENFQLLDDCEKSEVELALKKFRVLYPDAVRESAEKGLLRGIAAHHAGCLPLWKSFIEELFQRGLVKVVFATETLAAGINMPARTAVISSLSKKAGNERIELGPNELYQMAGRAGRRGIDEKGYTVLVQTAFEGAEECCKLVFAGVKPLVSQFTASYGMVLNLVAGSKVTRKSSGTEAGKVLQAGRSLEEAKKLVEKSFGNYVSSNVTVAAKQELAEIDNKIEILSSEISDEAIDKKSRKLLSARDYKEITVLKEELREEKRKRAEQRRRMELERFLALKPLLKGMEEGNLPFICLEFKDSEGREQSVPAVYLGHIDSFQGSKLQKMMSLDESFALNLIEDELAADEPGKPNVKPSYYVALGSDNSWYLFTEKWVRTVYRTGFPNIALALGDALPREIMKNLLDKADMQWDKLAESELGSLWRLEGSLETWSWSLNVPVLSSLSDEDEVLHMSEEYDNAAQKYKEQRSKISRLKKKMSRSEGFREYKKILENANLTVEKMKRLKARSRRLINRLEQIEPSGWKDFMRISNVIHESRALDINTHLIFPLGETAAAIRGENELWLAMVLRNKALVDLKPPQLAGVCASLVSEGIKVRPWRDNNYIYEPSDTVVDMVNFLEDQRSSLIKLQEKHEVMIPCCLDVQFSGMVEAWASGLSWKEMMMECAMDEGDLARLLRRTIDLLAQIPKLPDIDPVLQRSAAAAADIMDRPPISELAG
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RNA helicase involved in group II intron splicing. Essential protein required during embryogenesis. Involved in post-transcriptional gene silencing. Modulates the determination of cell fate. Necessary for normal plasmodesmata (PD) development and aperture regulation.
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B9DFK5
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RETIC_ARATH
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Protein RETICULATA, chloroplastic (Protein LOWER CELL DENSITY 1)
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MAGCAMNLQFSSVVKVRNEISSFGICNRDFVFRDLAKAMKVPVLRIRGGSGRQRSRLFVVNMSQSPIEPQSGGFAATEQIKGEGDNSILGKDNVRNLGTDQLENLDIDGNVGDGFNGSDGNGGGGGGGNGGEGDGEGEDYEEKEFGPILKFEEVMKETEARGATLPSDMLEAAKNYGIRKVLLLRYLDLQSSAGLLGFAIRSWAMLRNRMLADPSFLFKIGAEIVIDSCCATVAEVQKRGKDFWAEFELYVADLLVGTVVNIALVGMLAPYVRFGQPSASPGFLGRMVFAYNALPSSVFEAERPGCRFSAQQRLATYFYKGIMYGAVGFGCGIVGQGIANLIMTAKRNINKSEENIPVPPLIKSAALWGVFLSVSSNTRYQIINGLERVVEASPFAKKFPPAAMAFTVGVRLANNIYGGMQFVDWARLSGCQ
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May play a role in leaf development. Required for leaf mesophyll cell division in the early stages of leaf organogenesis. Acts in a developmental pathway that involves PPT1/CUE1 but does not include ASE2/DOV1.
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B9DFS6
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SNX2B_ARATH
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Sorting nexin 2B
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MMGSENDEESHLHSSKEEMEKLFLREDGDPLTKSNVNGDKSNSNYRSAMSTLFDSRHPSIVVTPADSDPLFAPPSYYSESRSPRSKPNGGDRVSSYLEPPSYADVIFSPFDDISEINGSEDGHSQSSDSLSRSPSSLSSDYIKITVSNPQKEQEATNSMIPGGSTYITYQITTRTNLSDYGGSEFSVRRRFRDIVTLADRLAESYRGFCIPPRPDKSIVESQVMQKQEFVEQRRVALEKYLRRLVAHPVIRNSDELKVFLQAQGKLPLATSTDVASRMLDGAVKLPKQLFGEGGGASSVEVVQPGRGGRDFLRMFKELRQSVSNDWGGSKPPVVEEDKEFLEKKEKMYDLEQQIINASQQAESLVKAQQDMGETMGELGLAFIKLTKFENEEAVFNSQRARANDMKNLATSAVKASRFYRELNSQTVKHLDTLHDYLGLMMAVQGAFADRSSALLTVQTLLSELSSLEARAEKLEVASSKVFGGDKSRIKKIEELKETIKVTEDSKNVAIREYEQIKENNWSEVERLDRERRADFLNMMKGFVANQVGYAEKIANVWTKVAEETRQYDRESS
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Plays a role in vesicular protein sorting. Acts at the crossroads between the secretory and endocytic pathways. Is involved in the endosome to vacuole protein transport and, as component of the membrane-associated retromer complex, is also involved in endosome-to-Golgi retrograde transport.
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B9DFU2
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MAX1_ARATH
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Cytochrome P450 711A1 (EC 1.14.-.-) (Protein MORE AXILLARY BRANCHES 1)
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MKTQHQWWEVLDPFLTQHEALIAFLTFAAVVIVIYLYRPSWSVCNVPGPTAMPLVGHLPLMAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTSLIPTMHSFITSATHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKDVEVTDFINQHVYSTTQLKMDLSGSLSIILGLLIPILQEPFRQVLKRIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETDSKDFLSLILKARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQHKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDYGIILSFKNGVKLRTIKRF
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Converts carlactone to carlactonoic acid by catalyzing consecutive oxidations at C-19 to convert the C-19 methyl group into carboxylic acid. Prefers 11R-carlactone to 11S-carlactone as substrate. Acts downstream of CCD7/MAX3 and CCD8/MAX4 in strigolactone signaling pathway and may be implicated in synthesis of carotenoid-derived branch regulators. Acts as a positive regulator of the flavonoid pathway in the late vegetative stage plant. Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute to the regulation of shoot architectural response to phosphate-limiting conditions and function as rhizosphere signal that stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger seed germination of root parasitic weeds.
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B9DFX7
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HMA8_ARATH
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Copper-transporting ATPase PAA2, chloroplastic (EC 7.2.2.9) (Protein HEAVY METAL ATPASE 8)
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MASNLLRFPLPPPSSLHIRPSKFLVNRCFPRLRRSRIRRHCSRPFFLVSNSVEISTQSFESTESSIESVKSITSDTPILLDVSGMMCGGCVARVKSVLMSDDRVASAVVNMLTETAAVKFKPEVEVTADTAESLAKRLTESGFEAKRRVSGMGVAENVKKWKEMVSKKEDLLVKSRNRVAFAWTLVALCCGSHTSHILHSLGIHIAHGGIWDLLHNSYVKGGLAVGALLGPGRELLFDGIKAFGKRSPNMNSLVGLGSMAAFSISLISLVNPELEWDASFFDEPVMLLGFVLLGRSLEERAKLQASTDMNELLSLISTQSRLVITSSDNNTPVDSVLSSDSICINVSVDDIRVGDSLLVLPGETFPVDGSVLAGRSVVDESMLTGESLPVFKEEGCSVSAGTINWDGPLRIKASSTGSNSTISKIVRMVEDAQGNAAPVQRLADAIAGPFVYTIMSLSAMTFAFWYYVGSHIFPDVLLNDIAGPDGDALALSLKLAVDVLVVSCPCALGLATPTAILIGTSLGAKRGYLIRGGDVLERLASIDCVALDKTGTLTEGRPVVSGVASLGYEEQEVLKMAAAVEKTATHPIAKAIVNEAESLNLKTPETRGQLTEPGFGTLAEIDGRFVAVGSLEWVSDRFLKKNDSSDMVKLESLLDHKLSNTSSTSRYSKTVVYVGREGEGIIGAIAISDCLRQDAEFTVARLQEKGIKTVLLSGDREGAVATVAKNVGIKSESTNYSLSPEKKFEFISNLQSSGHRVAMVGDGINDAPSLAQADVGIALKIEAQENAASNAASVILVRNKLSHVVDALSLAQATMSKVYQNLAWAIAYNVISIPIAAGVLLPQYDFAMTPSLSGGLMALSSIFVVSNSLLLQLHKSETSKNSL
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Mediates copper transfer across the chloroplast thylakoid membrane. Required for copper delivery into the thylakoids lumen, which is essential for the function of copper proteins.
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B9DFZ0
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NTH2_ARATH
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Endonuclease III homolog 2, chloroplastic (AtNTH2) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 2) (DNA glycosylase/AP lyase 2)
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MILTGAASTFPIVARVLNAMNRRMYAATTLSSAKSISAESLNLRSDSNSEAAHGASESETRVSLRKKRIKQDDLEPVKKCSARETKARKDMCGLPDIEDSPYKKTNGTASSRTRKLNSYIKSTEASPSASSIKTAGLGIPPENWEKVLEGIRKMKPSEEAPVNAVECDRTGSFLPPKERRFYVLIGTLLSSQTKEHITGAAVERLHQNGLLTPEAIDKADESTIKELIYPVGFYTRKATNVKKVAKICLMEYDGDIPRTLEELLSLPGVGPKIAHLVLHVAWNDVQGICVDTHVHRICNRLGWVSKPGTKQKTSSPEETRVALQQWLPKGEWVAINFLLVGFGQTICTPLRPHCGTCSITEICPSAFKETPSTSSKLKKSIKSKKL
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Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:19372224}.
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B9DGD6
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ACS_ARATH
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Acetyl-coenzyme A synthetase, chloroplastic/glyoxysomal (EC 6.2.1.1) (Acetate--CoA ligase) (Acetyl-CoA synthetase)
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MKIGSPSSPILSVVSSSGSLDPKISGSLGSRILPATQRSSPSENLLLHRKMSSNSLRHVESMSQLPSGAGKISQLNAVVLGESLASEENDLVFPSKEFSGQALVSSPQQYMEMHKRSMDDPAAFWSDIASEFYWKQKWGDQVFSENLDVRKGPISIEWFKGGITNICYNCLDKNVEAGLGDKTAIHWEGNELGVDASLTYSELLQRVCQLANYLKDNGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSADSLAQRIVDCKPNVILTCNAVKRGPKTINLKAIVDAALDQSSKDGVSVGICLTYDNSLATTRENTKWQNGRDVWWQDVISQYPTSCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMIYTATTFKYAFDYKSTDVYWCTADCGWITGHSYVTYGPMLNGATVVVFEGAPNYPDPGRCWDIVDKYKVSIFYTAPTLVRSLMRDDDKFVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGNEIEGECSGYLCVKGSWPGAFRTLFGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVLHPQCAEAAVVGIEHEVKGQGIYAFVTLLEGVPYSEELRKSLVLMVRNQIGAFAAPDRIHWAPGLPKTRSGKIMRRILRKIASRQLEELGDTSTLADPSVVDQLIALADV
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Catalyzes the production of acetyl-CoA, an activated form of acetate that can be used for lipid synthesis or for energy generation. May play a limited role in the biosynthesis of lipids.
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B9DGI8
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BZP63_ARATH
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Basic leucine zipper 63 (AtbZIP63) (bZIP protein 63) (Basic leucine zipper OPAQUE 2 homolog 3) (Basic leucine zipper O2 homolog 3)
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MEKVFSDEEISGNHHWSVNGMTSLNRSASEWAFNRFIQESSAAADDGESTTACGVSVSSPPNVPVDSEEYRAFLKSKLNLACAAVAMKRGTFIKPQDTSGRSDNGGANESEQASLASSKATPMMSSAITSGSELSGDEEEADGETNMNPTNVKRVKRMLSNRESARRSRRRKQAHLSELETQVSQLRVENSKLMKGLTDVTQTFNDASVENRVLKANIETLRAKVKMAEETVKRLTGFNPMFHNMPQIVSTVSLPSETSNSPDTTSSQVTTPEIISSGNKGKALIGCKMNRTASMRRVESLEHLQKRIRSVGDQ
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Transcription factor involved in controlling responses to starvation. BZIP2-BZIP63-KIN10 complex binds to the ETFQO promoter to up-regulate its transcription.
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B9DGT7
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TBA2_ARATH
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Tubulin alpha-2 chain (EC 3.6.5.-)
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MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVSILLDNEAIYDICRRSLSIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPVISAEKAFHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVGTIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTSVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAEGGDDEDDEGEEY
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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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B9DGU7
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TPK1_ARATH
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Thiamine pyrophosphokinase 1 (AtTPK1) (EC 2.7.6.2) (Thiamine kinase 1)
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MSAMDVMIHSSSFLLPCDETSTGTRYALVVLNQSLPRFTPLLWEHAKLRLCADGGANRIYDELPLFFPNEDALAIRNRYKPDVIKGDMDSIRRDVLDFYINLGTKVIDESHDQDTTDLDKCILYIRHSTLNQETSGLQILATGALGGRFDHEAGNLNVLYRYPDTRIVLLSDDCLIQLLPKTHRHEIHIQSSLEGPHCGLIPIGTPSAKTTTSGLQWDLSNTEMRFGGLISTSNLVKEEKITVESDSDLLWTISIKKTGLSIQDHTP
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Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate (TPP). TPP is an active cofactor for enzymes involved in glycolysis and energy production. Plant leaves require high levels of TPP for photosynthesis and carbohydrate metabolism.
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B9DGY1
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AB1K7_ARATH
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Protein ACTIVITY OF BC1 COMPLEX KINASE 7, chloroplastic (ABC1-LIKE KINASE 7) (EC 2.7.11.1) (Salt-induced ABC1 kinase 1, chloroplastic) (AtSIA1)
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MAALLASQSCCYGGETARVTKAIGFSSSLENHFTGEATQCYGSKSKRFRIEMRQSELPSKVGINGRSVKMVPASEVVKRKDGVNGSAGKGVNGASLVSSRNINGAASTLVKAPKKTTESYLPPPVEGVRVLPSDEGFSWADENYSSLQRSIDVWSFVISLRIRILFDNSKWAYVGGFTEEKQKSRRRETASWLRESVLQLGPTFIKLGQLSSTRSDLFPREFVDELSKLQDRVPAFSPEKAKRFIEAELGAPISVMYKEFEEQPIAAASLGQVHRAVLHNGEKVVVKVQRPGLKKLFDIDLRNLKLIAEYFQKSESFGTNDWVGIYEECALILYQEIDYINEAKNADRFRRDFRNINWVRVPLVYWDYSAMKVLTLEYVPGVKINNLDALAARGFNRSRIASRAIEAYLIQILKTGFFHADPHPGNLAIDVDESIIYYDFGMMGEIKTFTRKRLLDLFYSVYEKDAKKVMQNLIDLEALQPTGDLSSVRRSVQFFLDNLLSQSPDQQQTLAAIGEDLFAISQDQPFRFPSTFTFVIRAFSTLEGIGYILDPEFSFVKVAAPYAQELLDLKQRQRSGTQLVQEIRKQADDARSSTLSMPYRVQRIEEFVKELDSGDLKLRVRVLESERAARKATILQMATMYTVLGGTLLNIGVTFSNQGSQLVANGSFIGAGIFMLLVLRSMQRVNKLDKFEKMI
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Involved in resistance to oxidative stress. Influences responses to reactive oxygen species (ROS) production. Regulates plastoglobules formation in thylakoids. Together with OSA1, regulates iron distribution within the chloroplast and mediates the oxidative stress response. Together with ABC1K8, influences chloroplast lipid synthesis/accumulation and modulates chloroplast membrane composition in response to stress.
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B9DHQ0
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TBA5_ARATH
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Tubulin alpha-5 chain (EC 3.6.5.-)
|
MREIISIHIGQAGIQVGNSCWELYCLEHGIQPDGMMPSDTTVGVAHDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTVGKEIVDLCLDRVRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQIISSLTTSLRFDGAINVDITEFQTNLVPYPRIHFMLSSYAPVISAAKAYHEQLSVPEITNAVFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVGTIKTKRTVQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNNTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAEGGDDEEDEGEDY
|
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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B9DHT4
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ARIA_ARATH
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ARM REPEAT PROTEIN INTERACTING WITH ABF2 (ARIA)
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MDQQPERREGRSFPERKGQKRKLEEGAAAVEDREISAVSTDGGQALLSEVAAQVSVLNSAFSWQESDRAAAKRATQVLAELAKNEDLVNVIVDGGAVPALMTHLQAPPYNDGDLAEKPYEHEVEKGSAFALGLLAIKPEYQKLIVDKGALPHLVNLLKRNKDGSSSRAVNSVIRRAADAITNLAHENSSIKTRVRVEGGIPPLVELLEFSDSKVQRAAAGALRTLAFKNDDNKNQIVECNALPTLILMLGSEDAAIHYEAVGVIGNLVHSSPHIKKEVLTAGALQPVIGLLSSCCPESQREAALLLGQFASTDSDCKVHIVQRGAVRPLIEMLQSPDVQLKEMSAFALGRLAQDAHNQAGIAHSGGLGPLLKLLDSRNGSLQHNAAFALYGLADNEDNVSDFIRVGGIQKLQDGEFIVQATKDCVSKTLKRLEEKIHGRVLRHLLYLMRISEKSIQRRVALALAHLCSPEDQRTIFIDDNGLELLLGLLGSLNTKQQLDGAAALYKLANKSMALSPVDAAPPSPTQRVYLGEQYVNNATLSDVTFLVEGRTFYAHRICLLASSDAFRAMFDGGYREKDARDIEIPNIKWEVFELMMRFIYTGSVDITNEISKDLLRAADQYLLEGLKRLCEYTIAQDITLESIGDMYELSEAFHAMSLRQACIMFILEHFDKLSSMPWQNELVQRTIPEIREYFCRALTKSTTNLQSLRL
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May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2, a transcription factor which controls ABA-dependent gene expression via the G-box-type ABA-responsive elements. Negative regulator of seed germination and young seedling growth. {ECO:0000250, ECO:0000269|PubMed:15516505}.
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B9E972
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OLHYD_MACCJ
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Oleate hydratase (EC 4.2.1.53) (Fatty acid double bond hydratase) (Fatty acid hydratase)
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MYYSNGNYEAFARPKKPEGVDNKSAYLVGSGLASLAAASFLIRDGQMKGENIHILEELDLPGGSLDGILNPERGYIMRGGREMENHFECLWDLFRSVPSLEVEDASVLDEFYWLNKEDPNYSKCRVIENRGQRLESDGKMTLTKKANKEIIQLCLMKEEQLNDVKISDVFSKDFLDSNFWIYWKTMFAFEPWHSAMEMRRYLMRFIHHIGGLADFSALKFTKFNQFESLVMPLIEHLKAKNVTFEYGVTVKNIQVECSKESKVAKAIDIVRRGNEESIPLTENDLVFVTNGSITESTTYGDNDTPAPPTSKPGGAWQLWENLSTQCEEFGNPAKFYKDLPEKSWFVSATATTNNKEVIDYIQKICKRDPLSGRTVTGGIVTVDDSNWQLSFTLNRQQQFKNQPDDQVSVWIYALYSDERGERTNKTIVECSGKEICEEWLYHMGVPEEKISALAAECNTIPSYMPYITAYFMPRKEGDRPLVVPHGSKNIAFIGNFAETERDTVFTTEYSVRTAMEAVYKLLEVDRGVPEVFASVYDVRILLHALSVLNDGKKLDEIDMPFYERLVEKRLLKKASGTFIEELLEEANLI
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Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate. Cannot catalyze the reverse reaction. Is not active with saturated fatty acids and trans-, cis-5-, cis-6-, cis-8-, cis-11-, cis-13-, cis-14-, and cis-15-double bond unsaturated fatty acids as substrate is only active on cis-9- and/or cis-12-double bond of unsaturated fatty acids without any trans-configurations, producing 10-hydroxy and 10,13-dihydroxy fatty acids. The hydration of unsaturated fatty acids is suggested to be a detoxification mechanism and a survival strategy for living in fatty acid-rich environments.
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B9EHT4
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CLIP3_MOUSE
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CAP-Gly domain-containing linker protein 3 (Cytoplasmic linker protein 170-related 59 kDa protein) (CLIP-170-related 59 kDa protein) (CLIPR-59)
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MTKTDPAPMAPPPRGEEEEEEEEDEPVPEAPSPTQERRQKPVVHPSAPAPLPKDYAFTFFDPNDPACQEILFDPKTTIPELFAIVRQWVPQVQHKIDVIGNEILRRGCHVNDRDGLTDMTLLHYACKAGAHGVGDPAAAVRLSQQLLALGADVTLRSRWTNMNALHYAAYFDVPDLVRVLLKGARPRVVNSTCSDFNHGSALHIAASNLCLGAAKCLLEHGANPALRNRKGQVPAEVVPDPMDMSLDKAEAALVAKELRTLLEEAVPLSCTLPKVTLPNYDNVPGNLMLSALGLRLGDRVLLDGQKTGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLFASVSKVSKAVDAPPSSVTSTPRTPRMDFSRVTGKGRREHKGKKKSPSSPSLGSLQQREGAKAEVGDQVLVAGQKQGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCAPRHGVFAPASRIQRIGGSTDPPGDSVGAKKVHQVTMTQPKRTFTTVRTPKDIASENSISRLLFCCWFPWMLRAEMQS
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Functions as a cytoplasmic linker protein. Involved in TGN-endosome dynamics. May modulate the cellular compartmentalization of AKT kinase family and promote its cell membrane localization, thereby playing a role in glucose transport in adipocytes (By similarity).
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B9EJ57
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MTF1B_MOUSE
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Transcription termination factor 1b, mitochondrial (Mitochondrial transcription termination factor 1b) (mTERF1b)
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MASRNIWCVRRNFLFDLRGWMLQYSAEVFLKSISFRTFSVECDSKDKESLEEEREDLLSNLVTMGVDIDMARRRQPGVFNKAVTNEQELKIFLLSKGASDKVIGSIISRYPRAITRTPESLSKRWDLWRKIMASDLEIVNILERSPESFFRSNNNLNLENNIKFLCSVGLTHKCLCRLLTNAPRTFSNSLNLNKQMVEFLQETGMSLGHNDPRDFVRKIISKNPSILIQSTKRVKTNIEFLQSTFNLNKQDLLLLICGPGARILDLSNDCTKKNYTNIRERLLSLGCSEEEVQRFVLSYLNMVFLSEKKFNDKIDCLIEEKISASQIIENPRILDSSINTLKTRIRELSHAGYDLSTSSIALLSWSQRRYEAKLKRLCG
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Transcription termination factor. Binds to a 28 bp region within the tRNA(Leu(uur)) gene at a position immediately adjacent to and downstream of the 16S rRNA gene this region comprises a tridecamer sequence critical for directing accurate termination. Binds DNA along the major grove and promotes DNA bending and partial unwinding. Promotes base flipping. Transcription termination activity appears to be polarized with highest specificity for transcripts initiated on the light strand.
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B9EJ80
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PDZD8_MOUSE
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PDZ domain-containing protein 8
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MGLLLLILASAVLGSFLTLLAQFLLLYRRQPEPRADEAARAGDGFRYLKPVPGLPLREYLYGGGAEELAACSSEAGASSTPTPDSPAPPTLETCYFLNATILFLFRELRDTALARRWVTKKIKVEFEELLQTKTAGRLLEGLSLRDVFLGDTVPFIKTIRLVRPVVASGTGEPDDPDGDALPATCPEELAFEAEVEYNGGFHLAIDVDLVFGKSAYLFVKLSRVVGRLRFVLTRVPFTHWFFSFVEDPLIDFEVRSQFEGRPMPQLTSIIVNQLKKIIKRKHTLPSYKIRFKPFFPYQALQGFEEDEELIHIQQWALTEGRLKVTLLECSRLFIFGSYDRETNVHCTLELSSGVWEEKQRSSIKTVELIKGNLQSVGLTLRLVQSTDGYAGHVIIETVAPNSPAAMADLQRGDRLIAIGGVKITSTLQVLKLIKQAGDRVLVYYQRPAGQSSQDSLGQLEESFLSSSCQAAYEEDAAGLSADTENRDLDSEFEDLASDVRVQTELKEETQPLSHSPKRTPTTLSIKPLGAISPVLNRKLISGIHPPPQKLPSKEGNKPSTLKTSETTEAAQVSKPQGPTFKPPVPPRPQGRVPLPPTDTSAQADPEAPEKPDKVLLPPPPADKPAEKQVKSVDQGEDVAAGKQSSAKQEGVKDLPSESSAPTKDSSDDPQMWESSEVLYRNKVGKWSRTRASCVFDIEACHRYLNIALWCRDPFKLGGLICLGHVSLKLEEVALGCLATSNMEYLTKFRLEPPTPKAMVTRTALRNLSMQKGFNDKFCFGDITIHFKYLKEGEPDHHIVPNVEKEKELHLVEEVSTLPKEEHFVGQMSLSENKHSFQDTQFQNPTWCDYCKKKVWTKAASQCMFCAYVCHKKCQEKCLAETPLCGATERRIDRTLKNLRLEGQDPLLGLPPRVEIEANKSVNKTTGLTRHIINTSSRLLNLRQVSKTRLSEPGTDLVEPSPKHTPNTSDNEGSDTEVCGSNSPSKRGNSAGIKLMRKEGGLDDSVFIAVKEIGRDLYRGLPTEERIQKLEFMLDKLQNEIDQELEHNNSLVREEKETNDTRKKSVLSAALAKSGERLQALTLLMIHYRAGIEDIETLENLSLDQHSKKMNKYADDTEEDLDSEISQLIDSQPFSNISDDLFGPSESV
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Molecular tethering protein that connects endoplasmic reticulum and mitochondria membranes. PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for endoplasmic reticulum-mitochondria Ca(2+) transfer. In neurons, involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons.
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B9EJ86
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OSBL8_MOUSE
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Oxysterol-binding protein-related protein 8 (ORP-8) (OSBP-related protein 8)
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MEAALADGEPDRSSLLGDSKDVLGPSTVVANSDEPQHLTPGKMSQRQGRDANPTPTRDLPQPSLSPASLHSQGFERGKEDISQNKDDSSLSMSKSKSESKLYNGSEKDSSTSSKLTKKESLKVQKKNYREEKKRATKELLSTITDPSVIVMADWLKIRGTLKSWTKLWCVLKPGVLLIYKTQKNGQWVGTVLLNACEIIERPSKKDGFCFKLFHPLEQSIWAVKGPKGEAVGSITQPLPSSYLIIRATSESDGRCWMDALELALKCSSLLKRTMVREGKEHDLSISSDSTHVTLYGLLRANNLHSGDNFQLNDSEIERQHFKDQDLYSDKSDKENDPEHDESDNEVLGKSEESDTDTSERQDDSYIDPEPVEPLKETTYMEQSHEELGEAGEASQTETVSEENKSLIWTLLKQVRPGMDLSRVVLPTFILEPRSFLDKLSDYYYHADFLSEAALEENPYFRLKKVVKWYLSGFYKKPKGLKKPYNPILGETFRCLWIHPRTNSKTFYIAEQVSHHPPISAFYVSNRKDGFCLSGSILAKSKFYGNSLSAILEGEARLTFLNRGEDYVMTMPYAHCKGILYGTMTLELGGTVNITCQKTGYSAILEFKLKPFLGSSDYVNQISGKLKLGKEVLATLEGHWDSEVFINDKKTDNSEIFWNPTPDIKQWRLIRHTVKFEEQDDFESEKLWQRVTKAINAKDQTEATQEKYVLEEAQRQAARDRKTKTQEWVCKLFELDPLTGEWHYKFSDTRPWDPLNDMIQFEKDGVIQTKVKHRTPMVSVPKMKHKPTRQQKKVVKGYSSPEPDIQDSSGSEAQSVKPSTRRKKGIDLGDIQSSIESIKQTQEEIKRNIMALRNHLLSSTPATDYFLQQKDYFVIFLLILLQVIINFIFK
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Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner. Binds oxysterol, 25-hydroxycholesterol and cholesterol.
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B9EJA2
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CTTB2_MOUSE
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Cortactin-binding protein 2 (CortBP2)
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MATDSASCEPDLSRTPGDTEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKKGSDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTESTDPVKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALLIRPGIDRQSSHSDLGPSPPTALPSSANRIEENGPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGNSLSSEEPKSGLFSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQPSNDVSDDFECEHTICTLNIRKQTSWEDFSKAVSQALTNHFQAISSDGWWSLEDGTFNNATDSCIGLGTSSIRSIMLGSMPWSTGQSFSQSPWDFLKKKKVEQVLALLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIANQLALCMKYRQMAAGFPCEIVRAEVDSGFSKEQLVDVFIRNACLIPVKQFPVKKKIIVILENLEKSSLSELLGDFLAPLENRSTESPCTFQKGNGTSECYYFHENCFLVGTIAKACLQGSDLLVQQHFRWVQLRWDCEPIQGLLQRFLRRKVVSKFRGQLPAPCDPVCKIVDWALSVWRQLNSCLARLGTPEALLGPKYFLSCPVVPGHAQATVKWMSKLWNAVIAPRVQEAILSRASMNKQPGTGQTASKKYPSQGQQAVVRAALSILLNKAVLHGCPLPRAELDQQIADFKGGSFPLSIVSSYSKKKVESGAWRKVNTSPRKKPGHFSSPTWNKPDPKREGMRNKTIPHLNTNRNSSLSKQQSLENDLSVTLTLDHRLSLGSDDEADLVKELQSMCSSKSESDISKIADSRDDLRKFDSSRTNPGTSAPLNLRTPVPQKEASPPSSRQTAECSNSKSKTEMGVSSVKSFLPVPRSKVAQCSQNTKRNSSSSNTRQLEINNNSKEENWTLDKHEQVEKPNK
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Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance.
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B9EJV3
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GRB1L_MOUSE
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GREB1-like protein
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MGNSYAGQLKSARFEEALHNSIEASLRCSTAVPRPIFSQLYLDPDQHPFSTADVKPKVEDLDKDLVHPYTQNGSVDFSHNVAMNEMEDDEDEEEMSDSNSPPIPYSQKPAPEGSCTTDGFCQAGKDLRLVSLCMEQIDIPAGFLLVGAKSPNLPEHILVCAVDKRFLPDDHGKNALLGFSGNCIGCGERGFRYFTEFSNHINLKLTTQPKKQKHLKYYLVRTSQGVLSKGPLICWKECRSRQSSALCHSTKPISSVSSAVAPENGTANGYKAGFTVTEAANGTSGHGGKSSSCSSTPSRPGNYSLSPRPTFTSVDQANMFISGPPKKRHRGWYPGSPVSQSALVVPAPTVRPLSRTEPLLSTPVPQTPLTGILQPRPVLAGETVIVPENLLSNSGVRPVILIGYGTLPYFYGNVGDIVVSPLLVNCYKIPQLENKDLEQLGLTSTHLLSVENMILLTIQYLVRLGPDQIPLREEFEQIMLTAMQEFSVRERALPLGAPCAPMSPAQLPWLARLAASVSQDLVHVIVTQNSLAEGISETLRLLSEMKHYQRLPDYVVAICASKIRGNEFCVVVLGQHQSRALAESMLTTSEFLKEISYELITGKVSFLASHFKTTSLGDDLDKLLEKMQQRRGDSVVTPFNGDLDECVSPQEAAAMIPTQNLDVDNETFQIYQPQLTVARRLLSQVCAIADSGSQSLDLGHFSKVDFIIIVPRSEVLVQQTLQRVRQSGVLVDLGLEESGLAHQRAERYVVRLDNEIQSKFEVFMRRVKQNPYTLFVLVHDNSHVELTSVISGSLSHGEPTHGLADRVINCREVLEAFNLLVLQVSSFPYTLQTQQSRISSSNEVHWIQLDTMEDAGCEKLYFGLDEYSKSLQWGITSPLLRCDETFEKMVSTLLERYPRLHSMVVRCYLLIQQYSEALMALTTMASLRDHSTPETLSIMDDLITSPGKNKSGKGHMLVIRVPSVQLAMLAKERLQEVRDKLGLQYRFEIILGSPASELTVETHFVTRLKTWRGNDQDEWIPRTYQDLEGLPCIVILTGKDPLGETFPRSLKYCDLRLIDSSYLTRTALEQEVGLACCYVSKEVIRGPAAALDLSAKEAERVPASENDSEELLIDLERPQSNSSAVTGTSGSIMENGVSSSSTAGKPQQQLLTPTSSIRLDEGVSASTAVVGEILKQECDSLDPPMASSTTSKPSSSSSSSAQALAWSRQPRGLHTALPPVIILSKAAYSLLGSQKGGRLPSSSSLLPHADVAWVSSLRPGLHKDMSSEEQSLYYRQWTSARQHHADYSNQPDPISGARTLHPRRLLLTGPPQVGKTGSYLQFLRILFRMLIRLLEVDVYNEEEINTDHSDDSELSQSEGEPWPDIETFSKMPFDVSVHDPKYRLMSLVYSEKLAGIKQEVIKEYKVEEPRQRETMSMMLTQYAAYNTFHHCEQCQQYMAFTPASQMSDSTLHAFTFSSSMLGEEVQLYFIIPKSKESHFVFSKQGRHLESMRLPLVSDKNLNAVKSPIFTPSSGRHEHGLLNLFHAMEGISHLHLLVVKEYEMPLYRKYWPNHIMLVLPGMFNNAGVGAARFLIKELSYHNLELERNRLEELGVKRQCVWPFIVVMDDSCVLWNIHSVQEQTSQPTEAGISSKNVSLKSVLQHIEATPKIIHYAILGIQKWNSKLTSQSLKAPFSRCHVHDFILLNIDLTQNVQYDFNRYFCEDVDFNLRTNSSGLLICRFNNFSLMKKHVQVGGQRDFIIKPKLMVSENVVPILPLQYVCAPDSEHTLLAAPAQFLLEKFLQHASYKLFPKAIHNFKSPVLAIDCYLNIGQEVAICYVSSRPHSSNVNCEGVFFSGLLLYLCDSFVGADLLKKFKFLKGATLCVICQDRSSLRQTIVRLELEDEWQFRLRDEFQTANSSDDKPLYFLTGRHV
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Plays a major role in early metanephros and genital development.
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B9EKI3
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TMF1_MOUSE
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TATA element modulatory factor (TMF) (Androgen receptor coactivator 160 kDa protein) (Androgen receptor-associated protein of 160 kDa)
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MSWFNASQLSSFAKQALSQAQKSIDRVLDIQEEEPSAWAEAIPYGEPGISPPVSGGWDTSTWGLNSTSSEPQSPPTASQAITKPVRRTVVDESENFFSAFLSPSDAHTIQKSPVVSKPPSKSQRPEEEVKSSLQESSSPGQSRVSETAEVRDSVCVSGETSAVGTPSPVPEDKHEETAGEESEVKVPTVRLKASENVVNVNTTEDVSTTSTQSLTAETKDMALEPKEQKHEDRQSNTPSPPVSSFSSGTSTTSDIEVLDHESVISESSASSRQETSDAKSSLHLMQTSFQLLSASACPEYSRLDDFQKLNESCCSSDAFERIDSFSVQSLDSRSVSEINSDDELPGKGYALVPIIVSPSTPKTKVVESTEENAEEEEGNETLVAPSEEAELEESGRSATPVNCDQPDILASPTAGSGGHSASGPATEQCEAVENQPKAPPEKEDVCKTVEFLNEKLEKRETQLLSLSKEKALLEEAYDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEMKTIKEELATRLNSSQTADLLKEKDEQIQGLMEEGEKLSKQQLHNSNIIKKLRAKDKDNENVIAKLNRKAKELEEELQHLRQVLDGKEEVEKQHRENIKKLNSVVERQEKDLGRLQVDMDELEEKSRSTQAALDSAYRELTDLHKANAAKDSEVQEAALRREMKAKEELSGALEKAQEEARQQQEALVLQVGDLRLALQRAEQAAARKEDYLRHEISELQQRLQEAENRNQELSQSVSSTARPLLRQIENLQATLGSQTSSWETLEKSLSDRLGESQTLLAAAVERERAATEELLANKIQMSSVESQNTLLRQENSRLQAQLESEKNKLRKLEDENSRYQVELENLKDEYVRTLEESRKEKTLLSSQLEMERMKVEQERKKTIFTQEALKEKDHKLFSVCSTPTMSRSSSISGVDAAGLQASFLSQDESHDHSFGPMSTSASGSNLYEAVRMGAGSSIIENLQSQLKLREGEISHLQLEISNLEKTRSIMSEELVKLTNQNDELEEKVKEIPKLRVQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDELLRQRLS
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Potential coactivator of the androgen receptor. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER (By similarity). Mediates STAT3 degradation. {ECO:0000250, ECO:0000269|PubMed:15467733}.
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B9EKR1
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PTPRZ_MOUSE
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Receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta) (EC 3.1.3.48)
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MRILQSFLACVQLLCLCRLDWAYGYYRQQRKLVEEIGWSYTGALNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLSGGLSEKVFKASKITFHWGKCNVSSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMDYLQNNFREQQYKFSRQVFSSYTGKEEIHEVVCSSEPENVQADPENYTSLLVTWERPRVVYDAMIEKFAVLYQPLAGNDQAKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVCSNGLYGKYSDQLIVDMPTEDAELDLFPELIGTEEIIKEEEYGKDNEEDTGLNPGRDSVTNQIRKKEPQVSTTTHYNHMGTKYNEAKTNRSPTRGSEFSGKSDVPNTSPNSTSQHVAEFETERGISLPSQTGTNLPPHNVEGTSASLNSGSKTLFIFPQMNLSGTAESLNTVPITEYKEVSADVSEEENFLTDFKLDTGADDSSGSSPSTSTVPFSSDNLSHGYITSSDMPEAITYDVLKPGSTRNAPEDSAPSGSEESLKDPSLEGSVWFPGSTDLTTQSETGSGRESFLQVNSTDIQIDESRETTESFSPDATVSQDPSVTDMGMPHYSTFAYLPTEVTPQAFTPSSRPLDLAPTINILHSQTTQPVYNGETPLQPSYSSEVFPLATPLLLDNQTLNTTPAASSSDSALHATPVSPSVGVSFESILSSYDDAPLLPFSSASFSSEMFRHLHTVSQTLPQVTSAAERDELSLHASLLVARGDLLLEPSLVQYSDVASHQATTRAASDTLGFGSESAVFYKTSMVSQIESPRSDVVMHAYSSGPEPSYTVEGSHHVPTVSYSSAMPLHGSVDVSDQGSLLINPSHISMPESSFITPTASLLQPPPALSGDGEWSGASSDSELLLPDADGLRTLNISSPVSVAEFTYTTSVFADGIKPLSKSEMMYGNETELKMSSFSDMAYPSKSTVVPKMSDVVHKWSESLKETSVSISSMKSVFPESLVYPTTKGFEQGVSHVPEIIFPVQPTHTASQASGDTWLKPGLSANSEAAFSDTASREVVHPSTQPLLYEAATPFNTEALLQPSFQASDVDTLLKTALPSVPSDPILAGTPQVEQSSSSVSHPMASESGSSESMLHFTSVPILDISPSKVHSTPLQGLTVPHSSKKFSEQGLLKSKSPQQVLPSLFSNDEFFQSAHLDVSQAYPPKGRHAFVTPVLSIDEPQNTLINKLVYSEDIFSSTEISITDKVLTGLPTLASDVLSSTDHSVPLGSGPISLTMVSPNRDDSVTTAKLLLPSTATSKLTQSARSDADLVGGGEDGDDYDDDDYDDIDRGRFPVNKCMSCLPYRESREKVMNDSDTQESSLVDQSDPISPLLFENTEEENGGTGVTRVDKSPPPSMLPQNHNDGKEDSDIQMGSAVLPHTPGSKAWAVLTSDEESGSGQGTSDSLNDNETSTDFSFPDVNEKDTDGVLETDDTGIAPGSPRSSTPSVTSGHSGVSNSSEAEASNSSHESRIGLAEGLESEKKAVIPLVIVSALTFICLVVLVGILIYWRKCFQTAHFYLEDNTSPRVISTPPTPIFPISDDIGAIPIKHFPKHVADLHASNGFTEEFETLKEFYQEVQSCTADLGITADSSNHPDNKHKNRYVNIVAYDHSRVKLTQLAEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPTDGSEEYGSFLVNQKSVQVLAYYTVRNFTLRNTKLKKGSQKGRSSGRLVTQYHYTQWPDMGVPEYSLPVLAFVRKAAQAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEVPDSHIHSYVNTLLIPGPTGKTKLEKQFQLLSQSNILQSDYSTALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMSEEHKCLSNEEKLIVQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENAMDVYQVAKMINLMRPGVFTDIEQYQFLYKVVLSLVSTRQEENPSTSLDSNGAALPDGNIAESLESLV
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Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades.
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B9F1C0
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SHOC1_ORYSJ
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Protein SHORTAGE IN CHIASMATA 1 homolog (OsSHOC1)
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MRTRFLATDYFAPSSSSAAGKALALEFFSFPSLPVPALPPDPHFLPFTSADELPAATVADDGLGPLPIASALSDFLAAVIPQALPVPTVPAADEVLDDFLYDRGGYGEDFSSWEFGAFRIPKASEGYGVINREKDEKGEGSRSDGLEISSVMKRWEQLKELRFEVVEVDLLMALQEDIASFGEEESGGGVTLLLRVPDMKIHLDFIDIETDIKIRYQSDLPESVYQVEKVPVKDNDGNGHSSLREDCCLEIAALDHGAVIPRLEVSRNSWELDDCLTETDRYGVFDNVVRHLDEAQIQHSVFKSTEFLRSTDMDMLTFVCEDAPCHDIQVDKPAEIKAAVEMDVVRINGNILLEKNSALYPLKPDGTCSDLPCSILLEEVQIIDFPSDNVFKMLVQSETNKMNISDEIFKDDFDPARRLYESMVSCELALVDDTFRSLPTPILNDDIAVRSRVPPIQEILCSLKPHPLSASDGIYLDWHLLLEGPCNREICCSYASMVEEAKTCHLSSELQRSCQSTSVFVSDFLEDFQRSPKLQDEDKHSDIYVPAPLSHDPQKLEATQKCEQEGGTRNHSSMKRPSPEKSSSFPELISHSGDLNFYLNVRSATKSGTNNENTSTLDVPHSEEQALSLSTRAKVDKLIEIHPVSPSNLIQGLIEQIHASYTSALQESTYWRHSFSDEQGLGISKQKLLELITGEGSEGSYNHCEHKDKMELIVLYALKQVAYYLCFFGLHAAHLYISNLTRSLENTPERLKHILWSISEAQRKSERQLFESHPSLSCIETILRSNKQIDQKILIVADRAFWLPLGQKLASMRMTFVEFGQNPATTFVDLVNKTNSTAWVLEELLKSDCILLDNKNIPASFPFDKFGIILEYGGPNKSSTLLSLAPKLDGLPPLHFLYVKVDGKDFPAALVEDNHKDQDLKSTLDKVLLTLQKDLQERMNKMRIVDSLNFIPATNQLQGLQEKRSKHFAADATKELLPDDQPHRLQNLNKKNTFDSHNVVLADEQLHIQQTLSNKPVVNSQCVPTVEKSSSTSSVSANVLKDPQENQSTTDLPSCVKNDCIMPGRLSVPDVVIVVNTGNHGKTMLVSRRSSYQQILALEKGGMQVVERDIDLPVDLILSAAVCLVWYETALFEANELTTSAETSGIKENVENIATNILMSVSFSFTGCIMVFEGEADFLSAVMDSSDSLYTAAASLDMNLQLFFSHTPRSTDEIILNCITNVTSCYKAPLPDIPESESLAESFLTSFPSINPVSAYMLLSSGGSLVEFLSWPHERRIQAVGKYLLSPKIISLFNALCKFGELGESRSVMTECSSVDSDISSAFLQSPRKRKQRSLQACAVPTNKLLFSDSLNQIPGDYAEHAEVFSPSKLRKFSDMDNTIPELPDVFTFDESLNMRSEGFSYQQKKHDVDAIPGNQVINDDFSNGLTPNNQAYNRRTGNMVDTFDLPWQPEFGGTHPSKSTFHTSRPSCSRTHSNPVFSTAFEINDDPGEWNISGGTKQTWKGLAHGGTVDDSYRYDMDNRYHEPRDEIMQHPASSLAFQKLDFGSHATSQGSCWEIDYLRQMSAKRKARQERSRCSNSPGMSIPRMRDSNSKILNPPPKESFRYRGDRDTPSRDQSPSIGTQHYGKGKEGAKAQNRRARKDFNVQPTSHKKRIEPSIDPTWTPIDKRARQKLSFVTYGKEKQSKLVWRNQNSPGVGCGFRKRFREEGT
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Essential for normal crossover (CO) formation during meiosis. Essential component for the formation of class I meiotic COs. Interacts with PTD, another meiotic component, to regulate CO formation, possibly by stabilizing the recombination intermediates during meiosis. SHOC1 and PTD may form transient heterotrimeric or heterotetrametric complexes with HEI10 and/or ZIP4 to promote class I COs formation. Does not seem to be involved in early meiotic recombination steps involving double-strand break (DSB) formation, processing, and single-strand invasion. Does not seem to be involved in homologous pairing or synaptonemal complex (SC) assembly.
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B9FDE0
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BSK3_ORYSJ
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Probable serine/threonine-protein kinase BSK3 (EC 2.7.11.1) (Brassinosteroid-signaling kinase 3) (OsBSK3) (Receptor-like cytoplasmic kinase 173) (OsRLCK173)
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MGGRVSKAVACCCCRSQHHGVVVESSEKTAEEDHGESYELPAFQEFSFEQLRLATSGFAVENIVSEHGEKAPNVVYKGKLDAQRRIAVKRFNRSAWPDPRQFLEEAKSVGQLRSKRLANLLGCCCEGDERLLVAEYMPNDTLAKHLFHWEAQAMKWPMRLRVVLYLAEALEYCTSKGRALYHDLNAYRVLFDDDCNPRLSCFGLMKNSRDGKSYSTNLAFTPPEYMRTGRITPESVIYSFGTLLLDVLSGKHIPPSHALDLIRDRNFNMLTDSCLEGQFSNEEGTELVRLASRCLHYEPRERPNVRSLVQALAPLQKDLETPSYELMDIPRGGATSVQSLLLSPLAEACSRKDLTAIHEILEKTGYKDDEGTANELSFQMWTNQMQDTLNSKKKGDNAFRQKDFSSAIDCYSQFIEVGTMVSPTIYARRCLSYLMNDKAEQALSDAMQALVISPTWPTAFYLQAAALLSLGMENEAQEAIKDGCAHETSSSSGH
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Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of BRI1.
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B9J3S4
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COLQ1_BACCQ
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Collagenase ColQ1 (EC 3.4.24.3) (Microbial collagenase)
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MNKKSKINKVMLSISTMALSLGALQAPASAEEKVPYNVLKTKPVGIEKPVDEIGHVSKAEETLSFQERLKVGDFSQRPASIPNKAAVKQVKESYSMADLNKMNDQELVETLGCIKWHQITDLFQFNEDAKAFYKDKGKMQVIIDELAHRGSTFTRDDSKGIQTFTEVLRSAFYLAFYNNELSELNERSFQDKCLPALKAIAKNPNFKLGTAEQDTVVSAYGKLISNASSDVETVQYASNILKQYNDNFNTYVNDRMKGQAIYDIMQGIDYDIQSYLIEARKEANETMWYGKVDGFINEINRIALLNEVTPENKWLVNNGIYFASRLGKFHSNPNKGLEVVTQAMHMYPRLSEPYFVAVEQITTNYNGKDYSGNTVDLEKIRKEGKEQYLPKTYTFDDGSIVFKTGDKVSEEKIKRLYWAAKEVKAQYHRVIGNDKALEPGNADDILTIVIYNSPEEYQLNRQLYGYETNNGGIYIEETGTFFTYERTPEQSIYSLEELFRHEFTHYLQGRYEVPGLFGRGDMYQNERLTWFQEGNAEFFAGSTRTNNVVPRKSIISGLSSDPASRYTAERTLFAKYGSWDFYNYSFALQSYLYTHQFETFDKIQDLIRANDVKNYDAYRENLSKDPKLNKEYQEYMQQLIDNQDKYNVPAVADDYLAEHAPKSLTAVEKEMTETLPMKDAKMTKHSSQFFNTFTLEGTYTGSVTKGESEDWNAMSKKVNEVLEQLAQKEWSGYKTVTAYFVNYRVNSSNEFEYDVVFHGIAKDDGENKAPTVNINGPYNGLVKEGIQFKSDGSKDEDGKIVSYLWDFGDGRTSTEVNPVHVYEREGSYKVALIVKDDKGKESKSETTVTVKDGSLTESEPNNRPEEANRIGLNTTIKGSLIGGDHTDVYTFNVASAKDIDISVLNEYGIGMTWVLHHESDMQNYAAYGQANGNHIEANFNAKPGEYYLYVYKYDNGDGTYKLSVK
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Acts as a true collagenase, which is highly active and cleaves natively folded collagen. In vitro, can also cleave gelatin and the synthetic peptide FALGPA (furylacryloyl-Leu-Gly-Pro-Ala). Causes damage on dermal collagen (COL), resulting in gaps in the tissue, which might lead to an accelerated bacterial infiltration and penetration into deeper sites of the host.
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B9J8S0
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PDA_AGRRK
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Pterin deaminase (PDA) (EC 3.5.4.11)
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MSYSFMSPPNAARFVLSNATVPAVTVVGFTGPSSEGLMKADIVVADGLIKDILPAGTAPAELAKADMRDGMVWPTFADMHTHLDKGHIWERRANPDGSFMGALDAVRSDREANWSAADVRKRMEFSLRAAYAHGTSLIRTHLDSLAPQHRISFEVFSEVREAWKDKIALQAVALFPLDFMVDDAFFADLTTVVREAGGLLGGVTQMNPDIDAQLDKLIRAAAANGLDIDLHVDETEDREVLTLKAIAAAVLRNGFTGKVTAGHCCSLARQDENVAAATIDLVAKAGISIVALPMCNMYLQDRHPGRTPRWRGVTLLHELAAAGVPTAVASDNTRDPFYAYGDLDPVEVFREAVRILHLDHPLDTAARVVTTSPASILGRPDIGRIAVGGPADLVLFSARRWSEFLSRPQSDRVVLRKGKVIDRSLPDYRELDTVIGA
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Catalyzes the deamination of many pterin metabolites, such as formylpterin, pterin-6-carboxylate, pterin-7-carboxylate, pterin, hydroxymethylpterin, biopterin, D-(+)-neopterin, isoxanthopterin, sepiapterin, folate, xanthopterin, and 7,8-dihydrohydroxymethylpterin. May be involved in a degradative pathway for catabolizing pterin rings.
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B9K712
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IYD_THENN
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Iodotyrosine deiodinase (EC 1.21.1.1) (Halotyrosine dehalogenase)
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MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF
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Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine. Activity towards 2-iodophenol is weak.
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B9K7M5
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BGLA_THENN
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1,4-beta-D-glucan glucohydrolase (Glucan glucohydrolase) (EC 3.2.1.74) (Beta-D-glucoside glucohydrolase) (Beta-glucosidase) (EC 3.2.1.21) (Glucan 1,4-beta-glucosidase)
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MKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGDVACDHYNRWKEDIEIIEKIGAKAYRFSISWPRILPEGTGKVNQKGLDFYNRIIDTLLEKNITPFITIYHWDLPFSLQLKGGWANRDIADWFAEYSRVLFENFGDRVKHWITLNEPWVVAIVGHLYGVHAPGMKDIYVAFHTVHNLLRAHAKSVKVFRETVKDGKIGIVFNNGYFEPASEREEDIRAARFMHQFNNYPLFLNPIYRGEYPDLVLEFAREYLPRNYEDDMEEIKQEIDFVGLNYYSGHMVKYDPNSPARVSFVERNLPKTAMGWEIVPEGIYWILKGVKEEYNPQEVYITENGAAFDDVVSEGGKVHDQNRIDYLRAHIEQVWRAIQDGVPLKGYFVWSLLDNFEWAEGYSKRFGIVYVDYNTQKRIIKDSGYWYSNVIKNNGLTD
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Broad substrate specificity glycosidase. Releases glucose from soluble glucooligomers, with a preference for longer oligomers acts more readily on cellotetraose than on cellobiose. Displays similar activities towards the disaccharides lactose and cellobiose. Is also able to hydrolyze various aryl-beta-glycosides in vitro.
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B9KDD4
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PGLB_CAMLR
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Undecaprenyl-diphosphooligosaccharide--protein glycotransferase (EC 2.4.99.19) (Protein glycosylation B)
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MKLQQNFTDNNSIKYTCILILIAFAFSVLCRLYWVAWASEFYEFFFNDQLMITTNDGYAFAEGARDMIAGFHQPNDLSYFGSSLSTLTYWLYSILPFSFESIILYMSAFFASLIVVPIILIAREYKLTTYGFIAALLGSIANSYYNRTMSGYYDTDMLVLVLPMLILLTFIRLTINKDIFTLLLSPVFIMIYLWWYPSSYSLNFAMIGLFGLYTLVFHRKEKIFYLTIALMIIALSMLAWQYKLALIVLLFAIFAFKEEKINFYMIWALIFISILILHLSGGLDPVLYQLKFYVFKASDVQNLKDAAFMYFNVNETIMEVNTIDPEVFMQRISSSVLVFILSFIGFILLCKDHKSMLLALPMLALGFMALRAGLRFTIYAVPVMALGFGYFLYAFFNFLEKKQIKLSLRNKNILLILIAFFSISPALMHIYYYKSSTVFTSYEASILNDLKNKAQREDYVVAWWDYGYPIRYYSDVKTLIDGGKHLGKDNFFSSFVLSKEQIPAANMARLSVEYTEKSFKENYPDVLKAMVKDYNKTSAKDFLESLNDKDFKFDTNKTRDVYIYMPYRMLRIMPVVAQFANTNPDNGEQEKSLFFSQANAIAQDKTTGSVMLDNGVEIINDFRALKVEGASIPLKAFVDIESITNGKFYYNEIDSKAQIYLLFLREYKSFVILDESLYNSSYIQMFLLNQYDQDLFEQITNDTRAKIYRLKR
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Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (GalNAc(2)GlcGalNAc(3)Bac(NAc)(2) in eubacteria, where Bac(NAc)(2) is di-N-acetyl bacillosamine) from the lipid carrier undecaprenol-pyrophosphate to an asparagine residue within an Asp/Glu-Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.
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B9NAE4
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NRP31_POPTR
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Metal transporter Nramp3.1 (PotriNRAMP3.1) (PtNRAMP3.1) (Natural resistance-associated macrophage protein 3.1)
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MPSPEEDPQPLLKDQEETAYDSDGKVLSFGIDYDTESGGSTVVPSFSWRKLWLFTGPGFLMCIAFLDPGNLEGDLQAGAIAGYSLLWLLLWATAMGLLVQLLSARLGVATGRHLAELCREEYPTWARMILWIMAELALIGADIQEVIGSAIAIQILSNGVLPLWAGVIITASDCFIFLFLENYGVRKLEAAFGILIGIMAVTFAWMFADAKPSAPELFLGILIPKLSSKTIKQAVGVVGCIIMPHNVFLHSALVQSREIDHNKKGQVQEALRYYSIESTAALAISFMINLFVTTIFAKGFHGTELANSIGLVNAGQYLQDKYGGGFFPILYIWGIGLLAAGQSSTITGTYAGQFIMGGFLNLGLKKWLRALITRSCAIIPTIIVALVFDTSEDSLDVLNEWLNMLQSIQIPFALIPLLCLVSKEQIMGTFTVGPILKMVSWLVAALVMLINGYLLLDFFSNEVTGVVFTTVVCAFTGAYVTFIIYLISREVTISTWYCPT
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Divalent metal transporter. Can transport manganese (Mn) and iron (Fe). Involved in the control of cell-to-cell transport of manganese (Mn) between organs and tissues to monitor Mn homeostasis.
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B9TSP7
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FACR6_ARATH
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Fatty acyl-CoA reductase 6, chloroplastic (AtFAR6) (EC 1.2.1.84)
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MATTNVLATSHAFKLNGVSYFSSFPRKPNHYMPRRRLSHTTRRVQTSCFYGETSFEAVTSLVTPKTETSRNSDGIGIVRFLEGKSYLVTGATGFLAKVLIEKLLRESLEIGKIFLLMRSKDQESANKRLYDEIISSDLFKLLKQMHGSSYEAFMKRKLIPVIGDIEEDNLGIKSEIANMISEEIDVIISCGGRTTFDDRYDSALSVNALGPGRLLSFGKGCRKLKLFLHFSTAYVTGKREGTVLETPLCIGENITSDLNIKSELKLASEAVRKFRGREEIKKLKELGFERAQHYGWENSYTFTKAIGEAVIHSKRGNLPVVIIRPSIIESSYNEPFPGWIQGTRMADPIILAYAKGQISDFWADPQSLMDIIPVDMVANAAIAAMAKHGCGVPEFKVYNLTSSSHVNPMRAGKLIDLSHQHLCDFPLEETVIDLEHMKIHSSLEGFTSALSNTIIKQERVIDNEGGGLSTKGKRKLNYFVSLAKTYEPYTFFQARFDNTNTTSLIQEMSMEEKKTFGFDIKGIDWEHYIVNVHLPGLKKEFLSKKKTE
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Catalyzes the reduction of fatty acyl-CoA and -ACP (acyl carrier protein) substrates to fatty alcohols. Triggers the accumulation of C16 and, to a lower extent, of C18 fatty alcohols converts palmitoyl-acyl carrier protein to the corresponding C16:0 alcohol with NAD(P)H as electron donor. Triggers also the formation of some C16:0 and C18:0 aldehydes. May be involved in the generation of C30 primary alcohol.
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B9U3F2
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DISP3_CHICK
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Protein dispatched homolog 3 (Patched domain-containing protein 2) (Thyroid hormone receptor up-regulated protein 1) (TRUP1)
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MDTEDDPLLQDAWLDEEDEEVAFSSRKRREGALLCGKSSCRVRPLRVTLPVSGFWNIVGWIFTNPYCAGFILFLGCAIPAVLAVVMFLHYPALDIDISYNAFEIRNHESSQRFDALALALKSQFGSWGRNRRDLADFTSETLQRLIFEQLQQLHLNASHLQVSTRAKRSAPQGRTSSPEPRAHPHPGNETSRVTRGAPRWDYSNTYISANTQTHAHWRIELIFLARGDSENNIFTTERLVTIHEVERKIMDHPRFREFCWKPHEVLKDLPLGSYSYCSPPSSLMTYFFPTERGGKIYYDGMGQDLADIQGSLELAMTHPEFYWYVDEGLSAENKKSSLLRSEILFGAPLPNYYSVEDRWEEQRHKFQNFVVTYVAMLAKQSTSKVQVLYGGTDLFDYEVRRTFNNDMLLAFISSSCIAVLVYILTSCSVFLSFFGIASIGLSCLVALFLYHVVFGIQYLGILNGVAAFVIVGIGVDDVFVFINTYRQATHLKDLRLRMIHTIQTAGKATFFTSLTTAAAYAANIFSQIPAVHDFGLFMSLIVSCCWVAVLFTMPAALGIWTLYVSPLESSCQNSCSQKCTKKSTLHLAEDLFVASEGTSRAGRETLPYLDDDIPLLSVEEEPVSLEMGDVPLVSVMPENLQLPVEKSNRGHLIAHLQELLEHWVLWSAVKSRWVIVGLFLLVLLLSIFFASRLRPASRAPVLFRPDTNIQVLLDLKYNLSAEGISCITCSGLFQEKPHSLQNNFRTSLEKKKRGSASPWGSKGSISDTGQQDLQGTVYISKSRSKGRPAIYRFSLNASIPAPWQMVSPGDGEVPSFQVYRVPFGNFTRKLTACVSTVGLLKQTSPRKWMMTTLSCDSKRGWKFDFSFYVAAKEQQRTRKLYFAQSHKPPYHGRVCVAPPGCLLSSSPDGPTKGILYVPSEKAAPKARLSATSGFNPCMNMGCGKPAVRPLVDTGAMVFVVFGIRGVNRTKNSDNHVIGDMGSVIYDDSFDLFKEIGNLCRLCKAIASNTELVKPGGAQCLPSGYSISSFLQMLHPECKNIPEPNLLPGQLSHGAVGVKDGKVQWISMAFESTTYKGKSSFQTYADYLKWETFLQQQLQLFPEGSALRHGFQTCEHWKQIFMEIIGVQSALYGLILSLVICVAAVAVFTTHILLLLPVLLSILGVVCLVVTIMYWSGWEMGAVEAISLSILVGSSVDYCVHLVEGYLLAGENLPLHHAEDPTACRQWRTIEAIRHVGVAIVSSAVTTVIATVPLFFCIIAPFAKFGKIVALNTGVSILYTLTVSTALLSIMGPGTFTRSRTSCLKAVAGVLLAGLLGLCICLALLKGGFKIPLPNGTAL
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Plays a role in neuronal proliferation and differentiation (By similarity). Plays a role in the accumulation of cellular cholesterol. Involved in intracellular lipid droplet formation. May contribute to cholesterol homeostasis in neuronal cells.
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B9VRJ2
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COR15_PAPSO
|
NADPH-dependent codeinone reductase 1-5 (NADPH-dependent codeinone reductase B) (PsCor1.5) (EC 1.1.1.247)
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MESNGVPMITLSSGIRMPALGMGTVETMEKGTEREKLAFLKAIEVGYRHFDTAAAYQTEECLGEAIAEALQLGLIKSRDELFITSKLWCADAHADLVLPALQNSLRNLKLDYLDLYLIHHPVSLKPGKFVNEIPKDHILPMDYKSVWAAMEECQTLGFTRAIGVCNFSCKKLQELMATANSPPVVNQVEMSPTLHQKNLREYCKANNIMITAHSVLGAVGAAWGTKAVMHSKVLHQIAVARGKSVAQVSMRWVYQQGASLVVKSFNEARMKENLKIFDWELTAEDMEKISEIPQSRTSSAAFLLSPTGPFKTEEEFWDEKD
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NADPH-dependent codeinone reductase involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products. Reduces codeinone to codeine in the penultimate step in morphine biosynthesis. Can use morphinone, hydrocodone and hydromorphone as substrate during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrate during oxidative reaction with NADP as cofactor. Converts morphinone to morphine, and neomorphinone to neomorphine (By similarity). Reduces irreversibly neopinone, a spontaneous isomer of codeinone, to neopine in planta, neopine levels are limited to low levels.
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B9VUU3
|
POLG_HE71
|
Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
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MGSQVSTQRSGSHENSNSATEGSTINYTTINYYKDSYAATAGKQSLKQDPDKFANPVKDIFTEMAAPLKSPSAEACGYSDRVAQLTIGNSTITTQEAANIIVGYGEWPSYCSDSDATAVDKPTRPDVSVNRFYTLDTKLWEKSSKGWYWKFPDVLTETGVFGQNAQFHYLYRSGFCIHVQCNASKFHQGALLVAVLPEYVIGTVAGGTGTEDSHPPYKQTQPGADGFELQHPYVLDAGIPISQLTVCPHQWINLRTNNCATIIVPYINALPFDSALNHCNFGLLVVPISPLDYDQGATPVIPITITLAPMCSEFAGLRQAVTQGFPTELKPGTNQFLTTDDGVSAPILPNFHPTPCIHIPGEVRNLLELCQVETILEVNNVPTNATSLMERLRFPVSAQAGKGELCAVFRADPGRNGPWQSTLLGQLCGYYTQWSGSLEVTFMFTGSFMATGKMLIAYTPPGGPLPKDRATAMLGTHVIWDFGLQSSVTLVIPWISNTHYRAHARDGVFDYYTTGLVSIWYQTNYVVPIGAPNTAYIIALAAAQKNFTMKLCKDASDILQTGTIQGDRVADVIESSIGDSVSRALTQALPAPTGQNTQVSSHRLDTGKVPALQAAEIGASSNASDESMIETRCVLNSHSTAETTLDSFFSRAGLVGEIDLPLEGTTNPNGYANWDIDITGYAQMRRKVELFTYMRFDAEFTFVACTPTGEVVPQLLQYMFVPPGAPKPDSRESLAWQTATNPSVFVKLSDPPAQVSVPFMSPASAYQWFYDGYPTFGEHKQEKDLEYGACPNNMMGTFSVRTVGTSKSKYPLVVRIYMRMKHVRAWIPRPMRNQNYLFKANPNYAGNSIKPTGTSRTAITTLGKFGQQSGAIYVGNFRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCNCQTGVYYCNSRRKHYPVSFSKPSLIYVEASEYYPARYQSHLMLAQGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQGVSDYIKGLGDAFGTGFTDAVSREVEALKSYLIGSEGAVEKILKNLIKLISALVIVIRSDYDMVTLTATLALIGCHGSPWAWIKAKTASILGIPIAQKQSASWLKKFNDMANAAKGLEWVSNKISKFIDWLKEKIVPAAKEKVEFLNNLKQLPLLENQISNLEQSAASQEDLEVMFGNVSYLAHFCRKFQPLYATEAKRVYALEKRMNNYMQFKSKHRIEPVCLIIRGSPGTGKSLATGIIARAIADKYHSSVYSLPPDPDHFDGYKQQVVTVMDDLCQNPDGKDMSLFCQMVSTVDFIPPMASLEEKGVSFTSKFVIASTNATNIIVPTVSDSDAIRRRFYMDCDIEVTDSYKTDLGRLDAGRAAKLCSENNTANFKRCSPLVCGKAIQLRDRKSKVRYSVDTVVSELIREYSNRSAIGNTIEALFQGPPKFRPIRIGLEEKPAPDAISDLLASVDSEEVRQYCRDQGWIIPETPTNVERHLNRAVLVMQSIATVVAVVSLVYVIYKLFAGFQGAYSGAPKQVLKKPALRTATVQGPSLDFALSLLRRNVRQVQTDQGHFTMLGVRDRLAVLPRHSQPGKTIWIEHKLVNVLDAVELVDEQGVNLELTLITLDTNEKFRDITKFIPENISTASDATLVINTEHMPSMFVPVGDVVQYGFLNLSGKPTHRTMMYNFPTKAGQCGGVVTSVGKVIGIHIGGNGRQGFCAGLKRSYFASEQGEIQWVKPNKETGRLNINGPTRTKLEPSVFHDVFEGSKEPAVLHSKDPRLEVDFEQALFSKYVGNTLHVPDEYIREAALHYANQLKQLDIDTTQMSMEEACYGTDNLEAIDLHTSAGYPYSALGIKKRDILDPTTRDVSKMKFYMDKYGLDLPYSTYVKDELRSIDKIKKGKSRLIEASSLNDSVYLRMAFGHLYETFHANPGTVTGSAVGCNPDVFWSKLPILLPGSLFAFDYSGYDASLSPVWFRALELVLREIGYSEEAVSLIEGINHTHHVYRNKTYCVLGGMPSGCSGTSIFNTMINNIIIRALLIKTFKGIDLDELNMVAYGDDVLASYPFPIDCLELAKTGKEYGLTMTPADKSPCFNEVNWENATFLKRGFLPDEQFPFLIHPTMPMKEIHESIRWTKDARNTQDHVRSLCLLAWHNGKQEYEKFVSSIRSVPIGKALAIPNYENLRRNWLELF
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[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1, together with VP2, interacts with host cell receptor SCARB2 to provide virion attachment to target host cells (By similarity). This attachment induces virion internalization. This attachment induces virion internalization (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity). [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP2, together with VP1, interacts with host cell receptor SCARB2 to provide virion attachment to target host cells (By similarity). [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). [Capsid protein VP4]: Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity). [Capsid protein VP0]: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step (By similarity). [Protease 2A]: Cysteine protease that cleaves viral polyprotein and specific host proteins (By similarity). It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (By similarity). Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (By similarity). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity). Cleaves and inhibits host IFIH1/MDA5, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (By similarity). Cleaves and inhibits host MAVS, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (By similarity). [Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell (By similarity). In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity). Activates also the mitochondrial apoptotic pathway by activating host BAX (By similarity). [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. [Protein 3AB]: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity. [Protein 3A]: Localizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity). [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity). [Protease 3C]: Major viral protease that mediates proteolytic processing of the polyprotein (By similarity). Cleaves host EIF5B, contributing to host translation shutoff (By similarity). Cleaves also host PABPC1, contributing to host translation shutoff (By similarity). Disassembles host cytoplasmic stress granules by cleaving host G3BP1, although this effect is less prononced than the inhibition induced by protease 2A (By similarity). Cleaves host RIGI and thus contributes to the inhibition of type I interferon production (By similarity). Cleaves host IRF7 and thus contributes to the inhibition of type I interferon production (By similarity). Cleaves host HNRNPA1 thereby increasing the translation of apoptosis protease activating factor APAF1, leading to apoptosis of the host cell (By similarity). Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (By similarity). [RNA-directed RNA polymerase]: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated.
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B9W4V6
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APO1_CYCAE
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Aromatic peroxygenase (AaP) (EC 1.11.2.1)
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MKYFPLFPTLVFAARVVAFPAYASLAGLSQQELDAIIPTLEAREPGLPPGPLENSSAKLVNDEAHPWKPLRPGDIRGPCPGLNTLASHGYLPRNGVATPVQIINAVQEGLNFDNQAAVFATYAAHLVDGNLITDLLSIGRKTRLTGPDPPPPASVGGLNEHGTFEGDASMTRGDAFFGNNHDFNETLFEQLVDYSNRFGGGKYNLTVAGELRFKRIQDSIATNPNFSFVDFRFFTAYGETTFPANLFVDGRRDDGQLDMDAARSFFQFSRMPDDFFRAPSPRSGTGVEVVIQAHPMQPGRNVGKINSYTVDPTSSDFSTPCLMYEKFVNITVKSLYPNPTVQLRKALNTNLDFFFQGVAAGCTQVFPYGRD
|
Aromatic peroxidase that oxidizes aryl alcohols into the corresponding aldehydes and then into the corresponding benzoic acids. Oxidizes toluene and naphthalene. Catalyzes the regioselective peroxide-dependent hydroxylation of propranolol and diclofenac to 5-hydroxypropranolol and 4'-hydroxydiclofenac. Catalyzes the regioselective peroxide-dependent hydroxylation of naphthalene to 1-naphthol or 2-naphthol via a naphthalene 1,2-oxide intermediate. Catalyzes the regioselective peroxide-dependent oxidation of pyridine to pyridine N-oxide. Halogenates monochlorodimedone and phenol. Oxidizes the sulfur-containing heterocycle dibenzothiophene to yield ring-hydroxylation products and to a lesser extent sulfoxidation products.
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B9W5G6
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ACTPC_ACTFR
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DELTA-actitoxin-Afr1a (DELTA-AITX-Afr1a) (Alpha-helical pore-forming toxin) (PFT) (Cytolysin) (Fragaceatoxin C) (fraC)
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SADVAGAVIDGAGLGFDVLKTVLEALGNVKRKIAVGIDNESGKTWTAMNTYFRSGTSDIVLPHKVAHGKALLYNGQKNRGPVATGVVGVIAYSMSDGNTLAVLFSVPYDYNWYSNWWNVRVYKGQKRADQRMYEELYYHRSPFRGDNGWHSRGLGYGLKSRGFMNSSGHAILEIHVTKA
|
Pore-forming toxin (PFT) that consists of a crown-shaped octamer or nonamer that forms cation-selective hydrophilic pores of about 1.5 nm (inside) and 13 nm (outside). It causes cardiac stimulation and cytolysis (EC(50)=1.6 nM on erythrocytes). Interestingly, the Phe-16 is crucial for hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers. It is probable that a dimeric form is an assembly intermediate before the complete oligomerization. The formation of stable pores occurs only in vesicles composed of DOPC/SM (there is no oligomerization when the PFT is treated with vesicles of DOPC or SM alone). The transmembrane pore displays 8 lateral perforations, one at each subunit-subunit interface, partially occupied by the acyl-chain region of a bridging lipid. Each pore contains 24 lipid molecules, firmly bound to each subunit, that is, 3 lipids (L1, L2, L3, L4 and/or L5) are associated to each subunit. Lipid L1 bridges 2 subunits, whereas lipids L2 and L3 bind to sites at single subunit.
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B9WFG1
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ARO1_CANDC
|
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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MSIERVPILGKETIHVGYGIADHIVNEVIANLASSTYVIVTDTNMARTPQYSKLTDDFKTNLSKKRPESRLLTYCVSPGENNKNRVTKAAVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQVPTTLLAMVDSSVGGKTAIDTPLGKNFIGAFHQPEYVFCDVSFLETLPARQFINGMAEVVKTAAIWNEEEFTRLENFSKKFLSVVTSKKPDLQSIKAELVKTVLESVRVKAGVVSSDEKEAGLRNLLNFGHTIGHAIEAVLTPEALHGECVSIGMIKEAELSRYLGILPPVAVARLSKCLVAYGLPVSIDDKEFLKKVGPKRHYVEIDILLKKMAIDKKNDGSKIRCVLLEKIGKCYQLKAHQVSKQDLSFVLTDEVLVHPFTNPPKENIIVPPGSKSISNRALILAALGNGTVRVKNLLHSDDTKHMLDAVASLKGAEISTEDNGETIVVKGNGGNLVTCGEELYLGNAGTASRFLTTVASLVGKSPASDDVILTGNARMQERPIGPLVDALRSNGSEIEYLNKQGSLPLKISAGNGLKGGRIELAATISSQYVSSILMCAPYAKEPVTLALVGGKPISQLYIDMTCAMMKSFGIEVTKSTTEEYTYHIPKGIYKNPTEYVIESDASSATYPLAFAAMTGTSCTIPNIGSSSLQGDARFAVDVLKPMGCKVEQTATSTTVTGPPRGHLKPLPHVDMEPMTDAFLTASVVAAVAKGGSTSITGIANQRVKECNRIEAMVTELAKFGVSANELPDGIEIHGIDIKDLKTPEISDRGVCSYDDHRVAMSFSLLAGLCKEPVLILERSTTGKTWPGWWDILHSKFKIELDGYEPPFNTDKHVIKSSDKGVIVIGMRGTGKSTLSEWLASFLGFKMLDMDKYLEEKLGTDIKSLIKAKGWEHFRKEEAIVAKECFTKFSKGYVLSTGGGIVEGEDARQQLKSYADNGGIVLHLHRDLDETVTFLAADTTRPAYSSEVQEVWLRREKWYHECSNYHFYSSHCSTEDEFNHLRKSFVNYIKLITGAERSVVPTGRSTAVVLTLPDLNNVAGDLESITIGADAVELRVDLLKDTSAAFVAAQIATTRKHADLPIIYTVRTVSQGGKFPDENVDELKSLLLLGIRLGVAYIDLQLTAPNELIEEISSKKGFTRIIGTYQDINGELKWNNVEWKNKYNQGVSMNADIVRLVGRANSIQDNLDLEDFKKQNTLKPLIAFNLGTQGKLSQVLNGTFTPISHQLLPNDDGLLTIGEINQTYFDIGGFTAKKFWVIGSPIEHSRSPNLHNAGYKALNLPYQFGRFEATDVDVVYDNLINKSDFGGLAITMPLKLDIMKFATKLSDAAETIGAVNTLIPVEGGYFGDNTDWVGISNSFIRAGVPPKSSSNGLVVGAGGTSRAAIYALHQMGCTKIYLVNRTVAKLEELVKSFPKDYNLEIVETEQQADKVNKVLLAVSCIPADKPLDSDVLKKIERILSNGSEQVAGFKPTLLEASYKPRVTPIMKLAEEQYKWKVIPGVEMLVNQGDRQFKLHTGFSAPYEIIHRAVVEE
|
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
|
B9X187
|
NMP1A_XENLA
|
Nuclear envelope integral membrane protein 1a
|
MAGDVEGGGCRVSWGALLTLLLLPLPSLCTLASGKEPHVIKLYEGKVVRYNESKNFCYQRTYEPKWSDVWTKIQIRVNSTKMIRVTQVENEEKLKEMETFNMFDLFSSFLKEKLNDTFIYVDLYSNKTCIKVHVIDTDTYYSVALSRGFDPRLCFLFLCGLLLFFYGDALSRSQLFFYSTGITIGMLASMLILVFMLSKLMPKKSPFVALLLGGWSVSIYIIQLVFKNLQAICSEYWQYLLGYLGIVGFVSFAFCYKYGPLENDRSINILTWTLQLIGLLLMYISVQIQHIAVTMVVIAFCTKQIEYPVQWIYILYRKIKRKRAKPSPPRLLTEEEYRKQGEIETRKALEELRGYCSSPDFATWKMISRIQSPKRFADFVEGSSHLTPNEVSVHEHEYGLGGSFLEDELFGEDSDIEVEMDIEQPLYLVPRSCF
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In concert with ran, required for proper eye development. May be involved in the expression of early eye marker genes. Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (By similarity).
|
C0H5F4
|
RH2B_PLAF7
|
Reticulocyte-binding protein homolog 2b (PfR2Hb) (PfRH2b) [Cleaved into: Reticulocyte-binding protein homolog 2b 85 kDa form; Reticulocyte-binding protein homolog 2b 297 kDa form]
|
MKTTLFCSISFCNIIFFFLELSHEHFVGQSSNTHGASSVTDFNFSEEKNLKSFEGKNNNNDNYASINRLYRKKPYMKRSLINLENDLFRLEPISYIQRYYKKNINRSDIFHNKKERGSKVYSNVSSFHSFIQEGKEEVEVFSIWGSNSVLDHIDVLRDNGTVVFSVQPYYLDIYTCKEAILFTTSFYKDLDKSSITKINEDIEKFNEEIIKNEEQCLVGGKTDFDNLLIVLENAEKANVRKTLFDNTFNDYKNKKSSFYNCLKNKKNDYDKKIKNIKNEITKLLKNIESTGNMCKTESYVMNNNLYLLRVNEVKSTPIDLYLNRAKELLESSSKLVNPIKMKLGDNKNMYSIGYIHDEIKDIIKRYNFHLKHIEKGKEYIKRITQANNIADKMKKDELIKKIFESSKHFASFKYSNEMISKLDSLFIKNEEILNNLFNNIFNIFKKKYETYVDMKTIESKYTTVMTLSEHLLEYAMDVLKANPQKPIDPKANLDSEVVKLQIKINEKSNELDNAISQVKTLIIIMKSFYDIIISEKASMDEMEKKELSLNNYIEKTDYILQTYNIFKSKSNIINNNSKNISSKYITIEGLKNDIDELNSLISYFKDSQETLIKDDELKKNMKTDYLNNVKYIEENVTHINEIILLKDSITQRIADIDELNSLNLININDFINEKNISQEKVSYNLNKLYKGSFEELESELSHFLDTKYLFHEKKSVNELQTILNTSNNECAKLNFMKSDNNNNNNNSNIINLLKTELSHLLSLKENIIKKLLNHIEQNIQNSSNKYTITYTDINNRMEDYKEEIESLEVYKHTIGNIQKEYILHLYENDKNALAVHNTSMQILQYKDAIQNIKNKISDDIKILKKYKEMNQDLLNYYEILDKKLKDNTYIKEMHTASLVQITQYIPYEDKTISELEQEFNNNNQKLDNILQDINAMNLNINILQTLNIGINACNTNNKNVEHLLNKKIELKNILNDQMKIIKNDDIIQDNEKENFSNVLKKEEEKLEKELDDIKFNNLKMDIHKLLNSYDHTKQNIESNLKINLDSFEKEKDSWVHFKSTIDSLYVEYNICNQKTHNTIKQQKNDIIELIYKRIKDINQEIIEKVDNYYSLSDKALTKLKSIHFNIDKEKYKNPKSQENIKLLEDRVMILEKKIKEDKDALIQIKNLSHDHFVNADNEKKKQKEKEEDDEQTHYSKKRKVMGDIYKDIKKNLDELNNKNLIDITLNEANKIESEYEKILIDDICEQITNEAKKSDTIKEKIESYKKDIDYVDVDVSKTRNDHHLNGDKIHDSFFYEDTLNYKAYFDKLKDLYENINKLTNESNGLKSDAHNNNTQVDKLKEINLQVFSNLGNIIKYVEKLENTLHELKDMYEFLETIDINKILKSIHNSMKKSEEYSNETKKIFEQSVNITNQFIEDVEILKTSINPNYESLNDDQIDDNIKSLVLKKEEISEKRKQVNKYITDIESNKEQSDLHLRYASRSIYVIDLFIKHEIINPSDGKNFDIIKVKEMINKTKQVSNEAMEYANKMDEKNKDIIKIENELYNLINNNIRSLKGVKYEKVRKQARNAIDDINNIHSNIKTILTKSKERLDEIKKQPNIKREGDVLNNDKTKIAYITIQINNGRIESNLLNILNMKHNIDTILNKAMDYMNDVSKSDQIVINIDSLNMNDIYNKDKDLLINILKEKQNMEAEYKKMNEMYNYVNETEKEIIKHKKNYEIRIMEHIKKETNEKKKKFMESNNKSLTTLMDSFRSMFYNEYINDYNINENFEKHQNILNEIYNGFNESYNIINTKMTEIINDNLDYNEIKEIKEVAQTEYDKLNKKVDELKNYLNNIKEQEGHRLIDYIKEKIFNLYIKCSEQQNIIDDSYNYITVKKQYIKTIEDVKFLLDSLNTIEEKNKSVANLEICTNKEDIKNLLKHVIKLANFSGIIVMSDTNTEITPENPLEDNDLLNLQLYFERKHEITSTLENDSDLELDHLGSNSDESIDNLKVYNDIIELHTYSTQILKYLDNIQKLKGDCNDLVKDCKELRELSTALYDLKIQITSVINRENDISNNIDIVSNKLNEIDAIQYNFEKYKEIFDNVEEYKTLDDTKNAYIVKKAEILKNVDINKTKEDLDIYFNDLDELEKSLTLSSNEMEIKTIVQNSYNSFSDINKNINDIDKEMKTLIPMLDELLNEGHNIDISLYNFIIRNIQIKIGNDIKNIREQENDTNICFEYIQNNYNFIKSDISIFNKYDDHIKVDNYISNNIDVVNKHNSLLSEHVINATNIIENIMTSIVEINEDTEMNSLEETQDKLLELYENFKKEKNIINNNYKIVHFNKLKEIENSLETYNSISTNFNKINETQNIDILKNEFNNIKTKINDKVKELVHVDSTLTLESIQTFNNLYGDLMSNIQDVYKYEDINNVELKKVKLYIENITNLLGRINTFIKELDKYQDENNGIDKYIEINKENNSYIIKLKEKANNLKENFSKLLQNIKRNETELYNINNIKDDIMNTGKSVNNIKQKFSSNLPLKEKLFQMEEMLLNINNIMNETKRISNTDAYTNITLQDIENNKNKENNNMNIETIDKLIDHIKIHNEKIQAEILIIDDAKRKVKEITDNINKAFNEITENYNNENNGVIKSAKNIVDKATYLNNELDKFLLKLNELLSHNNNDIKDLGDEKLILKEEEERKERERLEKAKQEEERKERERIEKEKQEKERLEREKQEQLKKEALKKQEQERQEQQQKEEALKRQEQERLQKEEELKRQEQERLEREKQEQLQKEEELRKKEQEKQQQRNIQELEEQKKPEIINEALVKGDKILEGSDQRNMELSKPNVSMDNTNNSPISNSEITESDDIDNSENIHTSHMSDIESTQTSHRSNTHGQQISDIVEDQITHPSNIGGEKITHNDEISITGERNNISDVNDYSESSNIFENGDSTINTSTRNTSSTHDESHISPISNAYDHVVSDNKKSMDENIKDKLKIDESITTDEQIRLDDNSNIVRIDSTDQRDASSHGSSNRDDDEISHVGSDIHMDSVDIHDSIDTDENADHRHNVNSVDSLSSSDYTDTQKDFSSIIKDGGNKEGHAENESKEYESQTEQTHEEGIMNPNKYSISEVDGIKLNEEAKHKITEKLVDIYPSTYRTLDEPMETHGPNEKFHMFGSPYVTEEDYTEKHDYDKHEDFNNERYSNHNKMDDFVYNAGGVVCCVLFFASITFFSMDRSNKDECDFDMCEEVNNNDHLSNYADKEEIIEIVFDENEEKYF
|
[Reticulocyte-binding protein homolog 2b]: During the asexual blood stage, binds to a chymotrypsin sensitive, neuraminidase and trypsin resistant receptor on the surface of the host erythrocyte and thus is involved in merozoite invasion. The various processed forms have different binding affinities for the erythrocyte receptor full length form binds with higher affinity followed by the 250 kDa form and finally the 300 kDa form while the 160 kDa form does not bind erythrocytes. After merozoite attachment and reorientation, RH2b binding to its erythrocyte receptor triggers an increase in intracellular Ca(2+) within the parasite resulting in the release of microneme proteins such as EBA175 which in turn leads to the formation of the tight junction between parasite and host cell. [Reticulocyte-binding protein homolog 2b 85 kDa form]: During the asexual blood stage, binds to a trypsin-resistant and chymotrypsin and neuraminidase sensitive receptor on the surface of the host erythrocyte and thus is involved in merozoite invasion.
|
C0H9B6
|
ZPLD1_SALSA
|
Zona pellucida-like domain-containing protein 1 (ZP domain-containing protein 1) (Cupulin) [Cleaved into: Zona pellucida-like domain-containing protein 1, secreted form]
|
MEQICLIILLISKALSVGAQFNGYNCDANFHSRFPAERDISVYCGVQTITLKINFCPVLFSGYTDTDLALNGRHGDAHCRGFINNNTFPTVVLFSISLATLETCGNALVVSTAQGPNAYGNLSLVQIGNISGYIDTPDPPTIISYLPGLLYKFSCSYPLEYLVNNTQLASSAAAISVKDSNGTFVSTLSLLLYNDSSYVQQLSIPMAGLTLKTRVFAAVKATNLDRRWNVLMDYCYTTASGNPNDELRYDLFFSCDKDPQTTVFENGKSQMGRFAFEVFRFVKHKNQKMSTVFLHCVTKLCRADDCPMLMPICGSRKKRDVSERTESNSASGNAIITAGPIITRSDDTPMNNSQLAQLNSPVFRMNTVTSALISGIIILGVMSLCFFILSLTLLKGKRAPPTILSGARNPAFN
|
Glycoprotein which is a component of the gelatinous extracellular matrix in the cupulae of the vestibular organ.
|
C0HJB3
|
MANA_CANEN
|
Alpha-mannosidase (JBM) (Jbalpha-man) (EC 3.2.1.24) [Cleaved into: Alpha-mannosidase, heavy subunit; Alpha-mannosidase, light subunit]
|
MKYNTGAGTVPEQLNVHLVPHSHDDVGWLKTVDQYYVGSENYIQEACVENVLDSVVMSLQRDPNRKFVFGEMAFFHRWWLEQTPETKELXXKLVKAGQLEFVNGGWCMHDEATTHYIDMIDHTTLGHRFLQEQFNKIPRAGWQIDPFGHSAVQGYLLGAELGFDSVHFARIDYQDREKRKGEKSLEVVWRGSKTFGSSAQIFANAFPGHYGPPNGFNFEVRNNFVPLQDDPRLFDTNVEERVQNFLDAALTQAKLTRTNHLMWTMGDDFQYQYAESWFKQMDKLLHHVNKDGRVNALYSTPSLYTEAKNAANQTWPLKIDDYFPYADGRNAYWTGFYTSRXXXXXXXXMLSGYYLATRHSGFFAGKKSTKYHAFDLADALGIAQHHDAVSGTAKQHTTNDYAKRLALGASKAEAVVSSSLACLTSKQSADQCSAPASAFSQCHLFNISYCPPTESSLPDDKSLVVVVYNPLGWSRNEIVRIPVNDANLVVKDSSGNKLEVQYVEMDDVTANLRSFYVKXXXXXXXXXXXXYWSLFKASVPPLGWSTYFISEATGKGTRNALTLSQKGETLNIGPGDLKMSFSSLTGQLKRMYNSKTGVDLPIQQNYLWYESSEGDFSDYQASGAYLFRPNGQPPPHTVSRSSVTRVTRGPLVDEVHQKFNSWISQVTRLYKDKDHAEIEFTIGPIPTDDGVGKEVITRMTSTMATNKEFYTDSNGRDFLKRVRDYREDWPLEVTQPVAGNYYPLNLGLYTKDEKSEFSVLVDRATGGASIKDGEVELMLHRRTLRDDGRGVGEPLDEQVCMNKEYTCEGLTVRGNYYLSIHKPAGGSRWRRTTGQEIYSPMLLAFTQENMENWKSSHSTKAYAMDPNYSLPPSVALITLEELDDGLVLLRLAHLYEPSEDAEYSTLTKVELKKLFATQKLEELREVSLSANQEKSEMKKMKWSVEGDNEQEPQAVRGGPVSNADFVVELGPMEIRTFLLQF
|
Liberates mannose from p-nitrophenyl-alpha-D-mannoside. Liberates mannose from further alpha-D-mannosides including methyl-, benzyl-alpha-D-mannoside, 1-6-linked di-, tri- and tetrasaccharides of alpha-D-mannose and mannosyl-rhamnose. Liberates mannose from various glycoproteins like ovalbumin and ovomucoid. Does not hydrolyze beta-D-mannosides. Has glycosyltransferase activity, forming disaccharides from mannose and lyxose but not from glucose, galactose, ribose, xylose or arabinose.
|
C0HJD3
|
3NB_OXYFU
|
Fulgimotoxin (FTx)
|
QAIGPPFGLCFQCNQKTSSDCFNAKRCPPFHRTCYTLYKPDGGEEWAVKGCAKGCPTAGPDERVKCCHTPRCNN
|
Reptile-specific three-finger toxin that is lethal at low doses for lizards, but not for mice. Probably acts as a neurotoxin.
|
C0HJD9
|
K6TX1_ACTBE
|
Potassium channel toxin AbeTx1
|
RCKTCSKGRCRPKPNCG
|
Potassium channel inhibitor that is the most potent on Kv1.1/KCNA1 (IC(50)=671.95 nM), Kv1.2/KCNA2 (IC(50)=167.36 nM), and Kv1.6/KCNA6 (IC(50)=115.68 nM), and less potent on Kv1.3/KCNA3 (20% inhibition at 3 uM) and on shaker IR (15% inhibition at 3 uM). It inhibits potassium currents, not only by blocking the potassium current of Kv1.2/KCNA2, but by altering the energetics of activation of Kv1.1/KCNA1 and Kv1.6/KCNA6.
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C0HJE7
|
OXLA_CRODU
|
L-amino acid oxidase bordonein-L (LAAO) (LAO) (EC 1.4.3.2)
|
MNVFFMFSLLFLAALGSCAHDRNPLEECFRETDYEEFLEIARNGLTVTSNPKHVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKKDWYANLGPMRLPTKHRIVREYIRKFGLQLNEFFQENENAWYFIKNIRKRVREVKNNPGILEYPVKPSEEGKSAAQLYVESLRKVVKELKRTNCKYILDKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVGGMDQLPTSMYEAIKEKVQVHFNARVIEIQQNDRETKVTYQTSANEMSSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCKRKFWEDDGIRGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHQLPKEDIQTFCRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEF
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Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Is highly active on L-Met, L-Leu, L-Trp, and L-Phe, moderately active on L-Ile, L-His, and L-Arg, and weakly or not active on L-Gln, L-Val, L-Asn, L-Ala, L-Lys, L-Ser, L-Thr, L-Pro, L-Asp, L-Gly, L-Tyr, L-Cys and L-Glu. This enzyme exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions. In vitro, the enzyme exhibits cytotoxicity against fibroblast cell line and kills Leishmania amazonensis promastigotes, intensified by substrate addition.
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C0HJL8
|
PA2B_BOTNI
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Phospholipase A2 nigroviriditoxin basic subunit B (Ngvtx-B) (svPLA2) (EC 3.1.1.4) (Phospholipase A(2))
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NLLQFNRMIKLETKKNAVPFYAFYGCYCGWGGQGQPKDATDRCCFEHDCCYGKLTKCNTKSDLYSYSSKYGFLLCGKGTWCEEQICECDRIAATCLRRSLDTYKLKYMFYLDSYCKGPSEKC
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Heterodimer A-B: Nigroviriditoxin possesses phospholipase A2 (PLA2) activity. It consists of a non-covalent association of a basic PLA2 subunit B with a non-enzymatic subunit A.
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C0HJM9
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SCX2_TITFA
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Toxin Tf2
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MKRFLLFISILMMIGTIVVGKEGYAMDHEGCKFSCFIRPSGFCDGYCKTHLKASSGYCAWPACYCYGVPSNIKVWDYATNKCGK
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Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active against hNav1.3/SCN3A.
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C0HJQ2
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KA192_BUTOC
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Potassium channel toxin alpha-KTx 19.2 (Toxin Kbot21)
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AACYSSDCRVKCRAMGFSSGKCIDSKCKCYK
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Blocks voltage-gated potassium channels rKv1.1/KCNA1, rKv1.2/KCNA2, hKv1.3/KCNA3, rKv1.6/KCNA6 (IC(50)=75.9 nM) and, to a lesser extent, Shaker IR (with the inactivation domain removed).
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C0HJQ3
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H2A_ACIGU
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Histone H2A [Cleaved into: Acipensin 1 (Ac1); Acipensin 2 (Ac2); Acipensin 3 (Ac3); Acipensin 4 (Ac4); Acipensin 5 (Ac5); Acipensin 6 (Ac6)]
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MSGRGKTGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAQRVGAGAPVYLILELAGNAARDNKKTRIIPRHLQL
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Acipensins are antimicrobial peptides. Acipensins 1 and 2 have antibacterial activity against Gram-positive bacteria L.monocytogenes EGD (MIC are 1.1 uM and 1.0 uM, respectively) and S.aureus ATCC 33591 (MIC are 0.9 uM and 0.6 uM, respectively), against Gram-negative bacterium E.coli ML-35p (MIC are 0.7 uM and 0.3 uM, respectively) and antifungal activity against C.albicans 820 (MIC are 1.0 uM and 0.9 uM, respectively). Acipensin 6 has antibacterial activity against Gram-negative bacterium E.coli ML-35p (MIC=2.5 uM). Antimicrobial activity is reduced by high ionic strength. Acipensins 1, 2 and 6 have no hemolytic (up to 40 uM) or cytotoxic (up to 20 uM) effects on human cells in vitro.
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C0HJU3
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PA2A1_BOTPA
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Acidic phospholipase A2 (Bp-PLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
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NLVQFKTLIMKIAGRSVVYKYFYYGCYCGWGGIGQPRDATDRCCFVHD
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Snake venom phospholipase A2 (PLA2) that shows myotoxicity and induces paw edema in mice. Exhibits indirect hemolytic activity. Inhibits platelet aggregation induced by ADP and collagen. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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C0HJY1
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CONV_CANCT
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Concanavalin V (ConV)
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ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFVFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
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D-mannose/D-glucose-binding lectin which binds alpha-methyl-D-mannoside, D-mannose and D-glucose in that order. Also binds to serum fetuin and ovalbumin. Has hemagglutinating activity towards rabbit erythrocytes. Is not toxic towards larvae of the brine shrimp Artemia. Induces relaxation in rat endothelized aorta. Shows a transient edematogenic effect in rat.
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C0HJY4
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PON1A_ANOEM
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U1-poneritoxin-Ae1a (U1-PONTX-Ae1a) (Poneratoxin)
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WCASGCRKKRHGGCSC
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Weakly inhibits human L-type voltage-gated calcium channel Cav1 (CACNA1S, CACNA1C, CACNA1D, CACNA1F) (IC(50)=4.6 uM). In vivo, it induces reversible paralysis in blowfly L.cuprina.
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C0HK05
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PA2BC_CROOL
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Basic phospholipase A2 ColTx-1 (svPLA2) (EC 3.1.1.4) (Basic phospholipase A2 ColTx-I) (Phosphatidylcholine 2-acylhydrolase)
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HLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVH
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Snake venom phospholipase A2 (PLA2) that shows edema-inducing activity and local and systemic myotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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C0HK25
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ADEL_APLDA
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Lectin ADEL
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DPDKCKTIRVESWSYKYAEKVVEDASYVLNMTVVDRQSAAACTLGESFGYQKATLWVDHGCRADFKVCYLPVMPTECQTLRVESWNYKYAEKVVEGAALFINMTVEDRQSEASCDLDKSFGFYNQNSTVWVNHGCRADFNICYLKGAVTTSTINVSSWNYQYATKVLPAASCIYSMRVVNQQSAAPCTLGTTYGFVANTMWVDDGCRADFKPSYYSP
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Binds in decreasing order of affinity: galacturonic acid, D-galactosamine, methyl-alpha-D-galactopyranoside and further galactose-containing carbohydrates. Has hemagglutinating activity against human and rabbit erythrocytes.
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C0HK27
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LECA_DIOLA
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Lectin (DlyL)
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MGISKKSQLVPLLAFITMFLMVVSRVSSSIADANSLHFSFSQFSQNPKDLILQGDATTDSDGNLQLTRVSSDGSPQGSSVGRALFYAPVHIWEKSAVVASFDATFTFLIKSPDRDPADGITFFIANTDTSIPSGSGGRLLGLFPDANIIKNSTNLDFNAAYNADTIVAVELDSYPNTDIGDPSYPHIGIDIKSIRSKSTARWNMQTGKVGTAHISYNSVAKRLSAVVSYSGTSSTTVSYDVDLNNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKTNQLQDLRIASVV
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D-mannose-binding lectin that also binds alpha-methyl-D-mannoside with even higher affinity. Has hemagglutinating activity against rabbit erythrocytes. Shows toxicity against the brine shrimp A.nauplii. Induces reversible paw edema and hypernociceptivity in rats.
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C0HK44
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LL3_LASLA
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Lasioglossin-3 (LL-III)
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VNWKKILGKIIKVVK
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Antimicrobial peptide which assumes an amphiphilic alpha-helix conformation upon contact with membranes. Insertion into membranes involves Trp-3 (By similarity). Penetrates into cells once membrane has been permeated. Active against Gram-negative bacteria E.coli (MIC=1.4 uM), P.aeruginosa (MIC=18.7 uM) and Gram-positive bacteria S.aureus (MIC=3.9 uM) and B.subtilis (MIC=0.7 uM). Has cytotoxic but no hemolytic activity. Binds DNA in vitro (By similarity).In the context of inflammation and cancer tests, a 3-residues C-terminally truncated lasioglossin-3 is weakly cytotoxic to normal cells, induces calcium signaling but does not impact cAMP production. In addition, this truncated peptide prevents LPS-induced nitric oxid (NO) synthesis but does not affect the IP3 signaling and pro-inflammatory activation of endothelial cells. This truncated peptide does not show significant antiproliferative activity on the breast cancer cell line MDA-MB-231.
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C0HK49
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DEF_NICSU
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Defensin NsD7
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KDCKRESNTFPGICITKPPCRKACIREKFTDGHCSKILRRCLCTKPC
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Plant defense peptide (Probable). Disrupts membranes containing phosphatidic acid (PA) via a PA-dependent oligomerization process.
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C0HK69
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SCXD_CENLI
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Beta-toxin Cl13 (CliNaTxBet37)
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KEGYLVDYHTGCKYTCAKLGDNDYCVRECRLRYYQSAHGYCYAFACWCTHLYEQAVVWPLPNKRCKGK
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Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). Inhibits sodium channels Nav1.4/SCN4A, Nav1.5/SCN5A and Nav1.6/SCN8A. Also has a weak inhibitory effect on Nav1.2/SCN2A. Is lethal to mice.
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C0HK98
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SC1A_DROME
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Peptidoglycan-recognition protein SC1a (EC 3.5.1.28)
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MVSKVALLLAVLVCSQYMAQGVYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPGTHIWNEIRGWSHWSG
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N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity.
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C0HK99
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SC1B_DROME
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Peptidoglycan-recognition protein SC1b (EC 3.5.1.28)
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MVSKVALLLAVLVCSQYMAQGVYVVSKAEWGGRGAKWTVGLGNYLSYAIIHHTAGSYCETRAQCNAVLQSVQNYHMDSLGWPDIGYNFLIGGDGNVYEGRGWNNMGAHAAEWNPYSIGISFLGNYNWDTLEPNMISAAQQLLNDAVNRGQLSSGYILYGHRQVSATECPGTHIWNEIRGWSHWSG
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N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity.
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C0HKC4
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PA2B1_AGKPC
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Basic phospholipase A2 APC-D49 (svPLA2) (EC 3.1.1.4) (ApcP3) (Phosphatidylcholine 2-acylhydrolase)
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NLFQFEKLIKKMTGKSGMLWYSAYGCYCGWGGQGRPKDATDRCCFVHDCCYGKVTGCNPKMDIYTYSVDNGNIVCGGTNPCKKQICECDRAAAICFRDNLKTYDSKTYWKYPKKNCKEESEPC
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PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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C0HKE1
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H2A1B_MOUSE
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Histone H2A type 1-B
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MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HKE2
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H2A1C_MOUSE
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Histone H2A type 1-C (H2A-clustered histone 6)
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MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HKE3
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H2A1D_MOUSE
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Histone H2A type 1-D
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MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HKE4
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H2A1E_MOUSE
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Histone H2A type 1-E
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MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HKE5
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H2A1G_MOUSE
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Histone H2A type 1-G
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MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HKE6
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H2A1I_MOUSE
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Histone H2A type 1-I
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MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HKE7
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H2A1N_MOUSE
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Histone H2A type 1-N
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MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HKE8
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H2A1O_MOUSE
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Histone H2A type 1-O
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MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HKE9
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H2A1P_MOUSE
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Histone H2A type 1-P
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MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
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Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HKG7
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TX1A_CHEPU
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DELTA-miturgitoxin-Cp1a (DELTA-MGTX-Cp1a) (Double-knot toxin) (DkTx) (Toxin CpTx1) (Toxin CpTx1a)
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MKFSLFFSVFFLAVLHACLSESEIDLEDEEHFMSSDSFLSEIQDESRGKTCIERNKECTNDRHGCCRGKIFKDKCTCVKNGKTEKCVCTQKKWAKIIESYIGDIPALPKPVDDKCVPKHADCSKRKDDCCKGGIFKYQCKCYDMYDDDGEKTDLCGCVSPVEHQAIEGALRIAKKLIGDRWGR
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Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane. Lethal to insect larvae. Causes instant paralysis and death in the larvae of the flesh fly (S.carnaria) at doses of 20 ug/g, at doses of less than 10 ug/g causes reversible paralysis. Has cytolytic activity against insect Sf9 cells. Causes stable and irreversible depolarization of fly muscle fibers, leading to contracture at higher toxin concentrations. Destabilizes membranes.
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C0HKG8
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TX1B_CHEPU
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DELTA-miturgitoxin-Cp1b (DELTA-MGTX-Cp1b) (Toxin CpTx1) (Toxin CpTx1b)
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MKFSLFFSVFFLAVLHACLSESEIDLEDEEHFMSSDSFLSEIQDESRGKTCIERNKECTNDRHGCCRGKIFKDKCTCVKNGKTEKCVCTQKKWAKIIESYIGDIPALPKPVDDKCVPKHADCSKRKDECCKGGIFKYQCKCYDMYDDDGEKTDLCGCVSPVEHQAIEGALRIAKKLIGDRWGR
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Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane. Lethal to insect larvae. Causes instant paralysis and death in the larvae of the flesh fly (S.carnaria) at doses of 20 ug/g, at doses of less than 10 ug/g causes reversible paralysis. Has cytolytic activity against insect Sf9 cells. Causes stable and irreversible depolarization of fly muscle fibers, leading to contracture at higher toxin concentrations. Destabilizes membranes.
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C0HKG9
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TX1C_CHEPU
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DELTA-miturgitoxin-Cp1c (DELTA-MGTX-Cp1c) (Toxin CpTx1) (Toxin CpTx1c)
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MKFSLFFSVFFLAVLHACLSESEIDLEDEEHFMSSDSFLSEIQDESRGKTCIERNKECTNDRHGCCRGKIFKDKCTCVKSGKTEKCVCTQKKWAKIIESYIGDIPALPKPVDDKCVPKHADCSKRKDDCCKGGIFKYQCKCYDMYDDDGEKTDLCGCVSPVEHQAIEGALRIAKKLIGDRWGR
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Spider venom toxin that exhibits cytolytic activity by forming an alpha-helix across the membrane. Lethal to insect larvae. Causes instant paralysis and death in the larvae of the flesh fly (S.carnaria) at doses of 20 ug/g, at doses of less than 10 ug/g causes reversible paralysis. Has cytolytic activity against insect Sf9 cells. Causes stable and irreversible depolarization of fly muscle fibers, leading to contracture at higher toxin concentrations. Destabilizes membranes.
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C0HKM3
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HYAL_CONPU
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Hyaluronidase conohyal-P1 (EC 3.2.1.35) (Hyaluronoglucosaminidase)
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MRVVVVVTGLVVVVVATALSLPDHDVKSASSPLSSSSVYQGSSGDDCDEGLPPPDRPFYVVWNHPDTCKRNRIPLHLDHYGFIFNKNRLFLGEEIQTLYNTGLWPNISETGEFFNGGLPQLFTHHDYSETVEILGRYRTENFTGLGILDFEEWRAIYDTNFGIMRKYQDESIKLAKQRYPSYNKKELTMVAEQEWDQAAREIMSTKLAIGQALMPGGHWGYYGYPRTWGSKRNTQLRNNRIDWLWRQSTGLYPSIYIKDPNMTESAIAEFVSGNVEEAVRVQDEFSPPNTPIYPYAMLQSGDHIFFQVDHLKISLGLPAKMGTSGVILWASSNRYKNATRQCSRMRVHIDNVLGPYVENLTQVMADCSTTLCGGHGRCVHNSHDVLLGETDSQRLSGLCTPRHSRFRDYHCRCYSDWEGACCQTVRPSRCHKQQQGNVHEGGDLQEGHVVNVVNPLIG
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Hyaluronidase catalyzes the hydrolysis of hyaluronic acid (HA), an anionic, nonsulfated glycosaminoglycan distributed widely throughout connective, epithelial, and neural tissues. In venom, they are known to enhance diffusion of the venom by degrading the extracellular matrix (Probable).
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C0HKQ7
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CECA1_DROME
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Cecropin-A1
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MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATARG
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Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Functions in the imd/NF-kappa-B (Imd) epithelial and humoral immune response to Gram-negative bacteria.
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C0HKQ8
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CECA2_DROME
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Cecropin-A2
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MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATARG
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Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
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C0HL12
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AGRB1_RAT
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Adhesion G protein-coupled receptor B1 (Brain-specific angiogenesis inhibitor 1) [Cleaved into: Vasculostatin-120 (Vstat120); Vasculostatin-40 (Vstat-40)]
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MRGQAAAPGPIWILAPLLLLLLLLGRWARAASGADIGPGTEQCTTLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPAPCSGPGRVRTYQFDSFLESTRTYLGVESFDEVLRLCDPSAPLAFLQASKQFLQMQRQQPPQDGDLGPQGSGDDFSVEYLVVGNRNPSHAACQMLCRWLDACLAGSRSSHPCGIMQTPCACLGGEAGDTASSPLVPRGDVCLRDGVAGGPENCLTSLTQDRGGHGSAGGWKLWSLWGECTRDCGGGLQTRTRTCSPTLGVEGRGCEGVLEEGRLCNRKACGPTGRTSSRSQSLRSTDARRREEFGDELQQFGFPSPQTGDPAAEEWSPWSVCSSTCGEGWQTRTRFCVSSSYSTQCSGPLREQRLCNNSAVCPVHGAWDEWSPWSLCSSTCGRGFRDRTRTCRPPQFGGNPCEGPEKQTKFCNIALCPGRAVDGNWNEWSSWSTCSASCSQGRQQRTRECNGPSYGGAECQGHWVETRDCFLQQCPVDGKWQAWASWGSCSVTCGGGSQRRERVCSGPFFGGAACQGPQDEYRQCGAQRCPEPHEICDEDNFGAVVWKETPAGEVAAVRCPRNATGLILRRCELDEEGIAFWEPPTYIRCVSIDYRNIQMMTREHLAKAQRGLPGEGVSEVIQTLLEISQDGTSYSGDLLSTIDVLRNMTEIFRRAYYSPTPGDVQNFVQIISNLLAEENRDKWEEAQLMGPNAKELFRLVEDFVDVIGFRMKDLRDAYQVTDNLVLSIHKLPASGATDISFPMKGWRATGDWAKVPEDRVTVSKSVFSTGLAEADDSSVFVVGTVLYRNLGSFLALQRNTTVLNSKVISVTVKPPPRSLLTPLEIEFAHMYNGTTNQTCILWDETDGPSSSAPPQLGPWSWRGCRTVPLDALRTRCLCDRLSTFAILAQLSADATMDKVTVPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTGRLRSRLVRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAGASLWSSCVVLPLLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVDRQEEGNGDSGGSFQNGHAQLMTDFEKDVDLACRSVLNKDIAACRTATITGTFKRPSLPEEEKMKLAKGPPPTFNSLPANVSKLHLHGSPRYPGGPLPDFPNHSLTLKKDKAPKSSFIGDGDIFKKLDSELSRAQEKALDTSYVILPTATATLRPKPKEEPKYSINIDQMPQTRLIHLSMAPDASFPTRSPPAREPPGGAPPEVPPVQPPPPPPPPPPPQQPIPPPPSLEPAPPSLGDTGEPSAHPGPSSGAGTKNENVATLSVSSLERRKSRYAELDFEKIMHTRKRHQDMFQDLNRKLQHAAEKEKEVPGVDNKPEKQQTPNKRAWESLRKPHGTPAWVKKELEPLPPSPLELRSVEWEKAGATIPLVGQDIIDLQTEV
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Phosphatidylserine receptor which enhances the engulfment of apoptotic cells (By similarity). Also mediates the binding and engulfment of Gram-negative bacteria (By similarity). Stimulates production of reactive oxygen species by macrophages in response to Gram-negative bacteria, resulting in enhanced microbicidal macrophage activity (By similarity). In the gastric mucosa, required for recognition and engulfment of apoptotic gastric epithelial cells (By similarity). Promotes myoblast fusion (By similarity). Activates the Rho pathway in a G-protein-dependent manner (By similarity). Inhibits MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity (By similarity). Required for the formation of dendritic spines by ensuring the correct dendritic localization of PARD3 and TIAM1. Potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53/TP53 signal in suppression of glioblastoma (By similarity).
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C0HL13
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LRP2_PIG
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Low-density lipoprotein receptor-related protein 2 (LRP-2) (Glycoprotein 330) (gp330) (Megalin)
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MERWAAAAACTLLLAFAACLAPASGRECLGNEFRCSNGHCITESWRCDGTRDCLDGSDEIGCPPSTCGSTQFHCENEDVCIPLYWVCDGEEDCSNGADEHQRCPPGRTCSSHHFTCTNGECIPVEYRCDHSTDCLDGTDEINCRYPVCQQQTCHNGACYNTSQRCDGEIDCRDASDELNCTQRCLRNEFQCGSGECIPRDYVCDHDPDCSDSSDEHSCSVYQPCKGNEFACSNGFCINQNWVCDGMADCLDNSDEDGCESSIIRTHECYPNEWACPEDGKCIPLSRVCDGIADCPRGGDENKQGRVCDVNMCPSLGCEYQCHKSPSGGTCNCPPGFIVNKNNTRSCVDFNDCQIWGICDHFCEDRIGHHQCFCAEGYVLEHEQHCRANSSSGQAFVIFSNGRNLLLGDIQGQSFEYLVRSQNRGSPVGVDFHYRLSKVFWTDTMQNKVFSLDIDGLVIREVLSVSIEDPENLAVDWINNKLYIVETNVNRIDLANLDGSHRITLITENLGRPRGIALDPTVGYLFFSDWQSISGQPKIERAYMDGSNRKDLVKIKLGWPGGITLDLVAKRVYWVDARFDYIETVTYDGTQRKTVLQGGSNIPHPFGITLFEDNLFFTDWTKFSVMKANKFTETNPRVYFRSSTRPFGVTVYHAIRQPSVRNPCGNNNGGCEHICVLSHRTDNGGLGYRCKCKLGYIPGLDDYSCVATKQFLFFSTDVAVRGIPLTPSNQKDVILPVTGSPSVFVGIDFDAKENAIFFSDTSKDMIFRQKINGTGREIITANRVPSVESLSFDWISRNLYWTDASYRSVTVMRLADKSRRTIVQNLNNPRSIVVHPIAGYIFFTDWFRPAKILRAWSDGSHMLPIVNTTLGWPNGLAIDWGSSRLYWVDAFLDKIEHTTFDGLDRRALNHLQQMTHPFGLTVFGEYVYFTDWRQRSIVRVRKTDGGEMTILRNGVGNVMRVKIFETSIQVGSNACNRPTNPNGDCSHFCFPVPNLQRVCGCPYGMRLASNRLNCVNDSSREPPMEQCGALSFPCNNGRCVPLHYRCDGVDDCHDNSDEVQCGAFNTSCAPSAFACGHGGGECIPSYWRCDNHNDCVDGSDEQNCSSQAQTSCRADYFTCDNHMCIPKNWLCDTDNDCGDGSDEKRCDLGETCSPTQFHCPNHRCIDLAFVCDGDKDCADGSDESACVINCTDSQFKCVGSNKCISNTYRCDGVSDCSDHSDEIDCPTRPPGMCRQDEFQCREDGICIPDSWECDGHPDCLTGSDEHSGCPPRTCPXSRFLCANGNCIFRDWLCDGDNDCRDMSDEKDCPTQPFLCPSWQWQCPGHSICVNLSSVCDGISDCPHGTDESPLCNQESCLHSNGGCTHLCIQGPFGAQCECPLGYRLANDSKTCEDIDECRIPGFCSQHCYNMRGSFRCWCDIEYSLEADQRTCKATASESLLLVVANQNQLIADNITKSMDHMRALIQDGSHIVAVDFDSVRGRIFWSDKTLGKIFSAFQNGTDRKPVFNSGNIMTESIAVDWVGRNLYWADFALETIEVSKLDGTLRTVLLSENVTSPRGIVLDPRVNDRVIFWTNWGSYPRIERASMDGEMRTVIVQQKIFWPNGLAIDYPTRLLYFADGNLDHIHFCKYDGSNRKQVISSGEGSGHLFAITIFEDSIYWTDRNSQDVRKANKWHGGNESVVLSASQPLGIVAVHPARQPTARNPCTIARCSHLCLLSSERLYSCACPSGWSLSQDSMTCVRDDDAFLIVVRRTTIFGISLNPEVNTDNAMVPISGMESGYDVEVDYSEQFLYYADYPGEIYKVKTDGTNRTLFDPLTKVGSTTTLALDWLSRNLYYTDSEARSIKVLTLRGNVRYRKTLITNDGTTLGIGVPVSITVDPAKGKLYWSDLGIEGRVPAKIACANMDGTSRKNLFTGHLENVGFITLDIQEQKLYWTVRSYISIERGNVDGTDRMSLVNSLPRPRGIAVYGPYLYYADEQNQVIERVDKATGANKVVVREGLPNLRALRIYRRRGSESSNGCSNNINACQQICLPVPGGLFTCACAVGFKLNPDNRTCSSHDSFIVVSMLTAIRGYSLDVSDHSEAMVPVELEGQNTLHVDVDVSSGFVYWADFNRNVQTDNAIRRIKIDGSGFADIITDGIGKDGIRGIAVDWVAGNLYFINAFVSETLIEVLRINTTHRRVLLKTTEDVPRDIVVDPKNRYLFWSDIGQTPKIERSFLDCTNRTVLVSEMVASPRGLALDHNSGYIYWVDDSLDLIARVSIHGGNSETIRFGSSYPTPYAIAVFGNSIIWVDRDLKTIFQASKEPFKTDPPTVIRNNINWLRDVTVFDKQAQPRSPAEVNYNPCLQNNGGCTHFCFALPQLRTPKCGCAFGVLQGDGRSCAISREDFLIYALDNSVRSLHFDPEDYNVPFTAISVEETAVAVDYDSIDNRIYFTQVLASGKGQISYISLNSRSHSPTVVISNLGSPDGIAFDWIGRRIYYSDYTNQTIQSMNMDGSRRTVVARVTKPRAIVLDPCQGYMYWTDWSTNAQIERATMAGNFRNSIVNRDLVWPNGLTLDYKENLLYWADASLQKIERSSVTGTGREVIVSRANAPFGLTVYGQYIYWTDWLTQKIYRANKYDGSGQTAMTTALPFLPNGIRAVVNNQELCHNPCGRFNGGCSHVCAPGPNGPECKCPHEGRWYLANNNKYCIVDDGKRCNSTQFTCLSGYCILESLKCNDIDECGDSSDELETLCAYHTCPPTSFTCANGRCIQRHFRCDHYNDCGDNSDESGCRFRSCNITTEFSCNNGKCLPLQLVCDGIDHCNDNNTSDEKNCAQHTCLPDYIKCANSNVCIPRLFLCDGDNDCGDMSDENPIYCVSPTCKNNEFQCTSGSCIPELWHCDGERDCDDGSDEPATCVYSPSTCSSDEFKCDNNRCIQMEWICDGDNDCGDMSDEDGRHHCENHNCSSYAFHCVNSAPPSRRCIPLSWVCDGDADCSDAYDEHQNCTRRNCSGTEFRCSNGLCIPNWFRCDRRNDCGDYSDERNCKYPACDENLFTCQNGICTYKSYICDGENDCGDNSDELEHLCHKEETTCPPHQFRCNNGNCIEMVKVCNHQADCSDNSDEERCGVNECNDPLLSGCDQNCTDTLTSFYCSCKPGYRLLPDKRTCVDIDECKETPSVCSQKCENLLGSYICKCAPGYTREPDGRSCRQNTNIEPYLIFSNRYYLRNLTIDGHIYSLILQGLGNAVALDFDRVEERLYWLDIENKVIERMFLNKTNREAVIKYNIPGTESLAVDWVTRKLYWSDSYLNCLSVSDLNGRYRRKLAEHCVDVNNTFCFDKPRGIALHPRYGYVYWADWTDRAYIGRVGMDGRNKSLIISSKIKWPNGITIDYTNDLLYWTDAHLGYIEYSDLEGSHRHTVYETGTLSHPFAVTIFEDTIYWTDWNTKTVEKGNKYNGSNREVLVNTTHRPYDIHVYHPYRQPFVSNPCGTNNGGCSHLCLIKAGGNGFTCECPDNFYTIQHGDTTQCLPMCSSTQFLCANNEMCIPIWWKCDGQKDCLDGSDEPNTCPQRFCRLGQFQCSDGNCTSSNFICNARQDCPDGSDEDAVLCEHHRCESNQWQCANKRCIPESWQCDSLNDCGDNSDEDSSHCARRTCLPGYFKCANGHCIPQSWKCDVDNDCGDYSDEPLQECMGPAYRCDNYTEFDCKTNYRCIPKWAVCNGFDDCRDNSDEQNCESLTCKPSGEFRCTNHHCIPLRWRCDGHNDCGDNSDEENCVPRQCSESEFRCDDQTCIPSRWICDQNNDCGDNSDERDCEVMTCHPGYFQCSSGHCIPDQMRCDGFADCLDASDEATCPTRFPNGAYCPATLFECKNHVCVQPSWKCDGDNDCGDGSDEELHLCLNITCDLTNRFRCDNNRCIYRHELCNHEDDCGDGSDEKKENCLAPTPRPCTEGEFKCSNGHCISQHLVCDDVDDCGDHFDETGCNTGEERSCAENLCEHNCTQLIGGGFICSCRPGFKASSLNRNSCEDINECEQFGVCPQNCHNTKGSYECTCAEGFRSMSEHYGERCAAEGNPPLLLLPENVRVRKYNLSSEKFSDYLEDQERIQALDYDWDPEGTGLSVVYYTVLGHGSKFGAIKRAYIPNFESGSNNPVKEVNLGLKYIVQPDGIAVDWVGRHIYWSDAKTQRIEVAELDGRYRKWLITTLLDQPAAIVVNPKQGLMYWTDWGKNPKIEIAWMDGQHRKVLVQEDLGWPTGLSIDYVNSDRIYWSDLKEDVIETIKHDGTDRKVVVTAAMNPYSLDIFESQLYWISKDKGEIWVQDKFERDRKEKLLIVNPWLTQVRIFHQRRYNQSVPNRCKKVCSHLCLLKPEGYTCACPQGSRFIAGSVTECDAAIESPVTMPPPCRCMNEGNCYFDKNNLPKCKCPSGYMGEYCEIGLSKGISPGTTVAVLVTLILIIIIGGLVALGFFHYRKTGSILISMPRLPSLSNLSKYTENGNGVTFRSGEDVNMDIGVSGFGPESAIDRSMAMSEHFAMDLEKPPIIFENPMYTSKDGTIRMAQPTTTQVSESGNVYNKNYGSPVNPDELAPDTKPASPSADETQVTKWNIFKRKPKQNTNFENPIYAETENEPKVGAAVTPPPSPSPPAKKTQKKGTTPAYSATEDTFKDTANLVREDSEA
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Multiligand endocytic receptor (By similarity). Acts together with CUBN to mediate endocytosis of high-density lipoproteins (By similarity). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and clearance of leptin (By similarity). Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (By similarity). Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells (By similarity). Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP (By similarity). Mediates renal uptake of metallothionein-bound heavy metals (By similarity). Together with CUBN, mediates renal reabsorption of myoglobin (By similarity). Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (By similarity). Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (By similarity). Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity). Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (By similarity). Also mediates ShhN transcytosis (By similarity). In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon (By similarity). Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH (By similarity). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (By similarity). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (By similarity). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity). Involved in neurite branching (By similarity). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (By similarity). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (By similarity). Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG (By similarity). Mediates endocytosis of angiotensin-2 (By similarity). Also mediates endocytosis of angiotensis 1-7 (By similarity). Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation. Required for embryonic heart development (By similarity). Required for normal hearing, possibly through interaction with estrogen in the inner ear (By similarity).
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C0HL58
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NDB4B_ISOMC
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Peptide Im-5
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FLGSLFSIGSKLLPGVIKLFQRKKQ
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Probably forms pores in target membranes. Has antibacterial activity against Gram-negative bacterium E.coli NBRC 3972 (MIC=10 uM) and against Gram-positive bacteria S.aureus NBRC 13276 (MIC=2.5-5 uM) and B.subtilis NBRC 3009 (MIC=0.5-1 uM). Toxic to cricket A.domestica. Has hemolytic activity against sheep erythrocytes.
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C0HL66
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H33A_DROME
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Histone H3.3A (H3.A)
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MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
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Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HL67
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H33B_DROME
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Histone H3.3B (H3.B)
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MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
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Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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C0HL84
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PNG1_PANCL
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Panurgin 1 (PNG-1)
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LNWGAILKHIIK
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Antimicrobial peptide active against Gram-positive bacteria M.luteus (MIC=1.5 uM), B.subtilis (MIC=1.3 uM) and S.aureus (MIC=10.6 uM), against Gram-negative bacteria E.coli (MIC=3.7 uM) and P.aeruginosa (MIC=51.7 uM) as well as against yeast C.albicans (MIC=7.3 uM). Has weak hemolytic activity against human erythrocytes. Probably acts by disrupting membranes of target cells.
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C0HL98
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MAC1_MACFV
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Macropin (MAC-1)
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GFGMALKLLKKVL
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Antimicrobial peptide with activity against Gram-positive bacteria (B.subtilis, S.aureus and L.monocytogenes) and Gram-negative bacteria (E.coli and P.aeruginosa) (MIC=1.3-35 uM). Also active against fungus C.albicans (MIC=6.3 uM). Has little hemolytic activity. Acts by disrupting membranes and bacterial cell wall structures. Binds to peptidoglycan and lipopolysaccharide (LPS). In the context of inflammation and cancer tests, is weakly cytotoxic to normal cells, induces calcium signaling but does not impact cAMP production. In addition, prevents LPS-induced nitric oxid (NO) synthesis but does not affect the IP3 signaling and pro-inflammatory activation of endothelial cells. Does not show significant antiproliferative activity on the breast cancer cell line MDA-MB-231.
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C0HLF7
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PA2B_OPHSH
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Basic phospholipase A2 sphenotoxin subunit B (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
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HLLQFNKMIKEETGKNAIPFYAFYGCYCGWGGSGKPKDATDRCCFEHDCCYGKLTNCNTKWDIYSYSLKDGYITCGKGTWCEKEVCECDKCLRRNLRTYKYGYMFYL
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Heterodimer A-B: Sphenotoxin is a potent neurotoxin that possesses phospholipase A2 (PLA2) activity. It consists of a non-covalent association of a basic PLA2 subunit B with a non-enzymatic subunit A. Monomer B: Not found in vivo. In vitro, potent neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. Induces paralysis of the hind legs and neuromuscular blockade in mouse phrenic nerve-diaphragm preparations. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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C0HLG3
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RNAG_CYCAE
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Ribonuclease ageritin (EC 4.6.1.23) (Ribotoxin)
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MSESSTFTTAVVPEGEGVAPMAETVQYYNSYSDASIASCAFVDSGKDKIDKTKLVTYTSRLAASPAYQKVVGVGLKTAAGSIVPYVRLDMDNTGKGIHFNATKLSDSSAKLAAVLKTTVSMTEAQRTQLYMEYIKGIENRSAQFIWDWWRTGKAPA
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Fungal ribonuclease involved in fungal defense. Highly specific and highly toxic fungal endonuclease that cleaves a single phosphodiester bond in the 28S RNA of eukaryotic ribosomes at a universally conserved GAGA tetraloop of the sarcin-ricin loop (SRL). The damage of the SRL inhibits the binding of translation elongation factors and halts protein biosynthesis, ultimately resulting in the death of the target cells. Shows antitumor activity. Exerts cytotoxicity and induces apoptosis towards rat glial cells and human glioma cells, and also displays some activity towards human neurolastoma cell lines. Shows a strong entomotoxicity against Aedes aegypti larvae, yet no nematotoxicity against nematodes.
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C0HLG4
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KKX1U_UROMN
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Wasabi receptor toxin (WaTx)
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MKYFTLALTLLFLLLINPCKDMNFAWAESSEKVERASPQQAKYCYEQCNVNKVPFDQCYQMCSPLERS
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Cell-penetrating peptide (CPP) with defensive purpose that induces pain by specifically activating mammalian sensory neuron TRPA1 channels. It non-covalently binds to the same region than other TRPA1 agonists (irritants), but acts via a distinct biochemical mechanism. Its binding stabilizes the TRPA1 open state and diminishes calcium-permeability. Consequently, it produces pain and pain hypersensitivity, but fails to trigger efferent release of neuropeptides (CGRP) and neurogenic inflammation typically produced by noxious electrophiles. Is not active on voltage-gated potassium channels and other TRP channels.
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