entry
stringlengths 6
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stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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O50202
|
ARC_RHOER
|
Proteasome-associated ATPase (AAA ATPase forming ring-shaped complexes) (ARC) (Proteasomal ATPase)
|
MSSTENPDSVAAAEELHALRVEAQVLRRQLAQSPEQVRELESKVDSLSIRNSKLMDTLKEARQQLIALREEVDRLGQPPSGYGVLLSVHEDKTVDVFTSGRKMRLTCSPNIDTDTLALGQTVRLNEALTIVEAGTYEQVGEISTLREVLDDGLRALVVGHADEERIVWLAAPLAAVFADPEADIIAYDADSPTRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVHYDDIGGLGRQIEQIRDAVELPFLHKDLFHEYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKIAEARGQDSKDAKSYFLNIKGPELLNKFVGETERHIRMIFQRAREKASEGTPVIVFFDEMDSIFRTRGSGVSSDVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAESAQDIFSKYLVDGLPINADDLAEFGGDRTACLKAMIVRVVDRMYAESEENRFLEVTYANGDKEVLFFKDFNSGAMIQNIVDRAKKYAIKSVLDTGAPGLRVQHLFDSIVDEFAENEDLPNTTNPDDWARISGKKGERIVYIRTLVTGKNASASRAIDTESNTGQYL
|
ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. {ECO:0000255|HAMAP-Rule:MF_02112, ECO:0000269|PubMed:19481487, ECO:0000269|PubMed:9514743}.
|
O50274
|
CYSNC_PSEAE
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Bifunctional enzyme CysN/CysC [Includes: Sulfate adenylyltransferase subunit 1 (EC 2.7.7.4) (ATP-sulfurylase large subunit) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (APS kinase) (ATP adenosine-5'-phosphosulfate 3'-phosphotransferase)]
|
MSHQSDLISEDILAYLGQHERKELLRFLTCGNVDDGKSTLIGRLLHDSKMIYEDHLEAITRDSKKVGTTGDDVDLALLVDGLQAEREQGITIDVAYRYFSTAKRKFIIADTPGHEQYTRNMATGASTCDLAIILIDARYGVQTQTRRHSFIASLLGIRHIVVAINKMDLKDFDQGVFEQIKADYLAFAEKIGLKTSSLHFVPMSALKGDNVVNKSERSPWYAGQSLMEILETVEIAADRNLDDMRFPVQYVNRPNLNFRGFAGTLASGVVRKGDEVVALPSGKGSKVKSIVTFEGELEQAGPGQAVTLTLEDEIDVSRGDMLVHADNRPLVTDGFDAMLVWMAEEPMLPGKKYDIKRATSYVPGSIPSIVHKVDVNTLERTPGSELKLNEIARVKVSLDAPIALDGYEQNRTTGAFIVIDRLTNGTVGAGMIVSAPPAAHGSSAHHGSNAHVTREERAGRFGQQPATVLFSGLSGAGKSTLAYAVERKLFDMGRAVYVLDGQNLRHDLNKGLPQDRAGRTENWLRTAHVAKQFNEAGLISLCAFVAPSAEGREQARALIGAERLITVYVQASPQVCRERDPQGLYAAGEDNIPGESFPYDVPLDADLVIDTQALSVEDGVKQVLDLLRERQAI
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With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD. APS kinase catalyzes the synthesis of activated sulfate.
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O50406
|
DITCY_MYCTU
|
Type B diterpene cyclase (EC 5.5.1.16)
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METFRTLLAKAALGNGISSTAYDTAWVAKLGQLDDELSDLALNWLCERQLPDGSWGAEFPFCYEDRLLSTLAAMISLTSNKHRRRRAAQVEKGLLALKNLTSGAFEGPQLDIKDATVGFELIAPTLMAEAARLGLAICHEESILGELVGVREQKLRKLGGSKINKHITAAFSVELAGQDGVGMLDVDNLQETNGSVKYSPSASAYFALHVKPGDKRALAYISSIIQAGDGGAPAFYQAEIFEIVWSLWNLSRTDIDLSDPEIVRTYLPYLDHVEQHWVRGRGVGWTGNSTLEDCDTTSVAYDVLSKFGRSPDIGAVLQFEDADWFRTYFHEVGPSISTNVHVLGALKQAGYDKCHPRVRKVLEFIRSSKEPGRFCWRDKWHRSAYYTTAHLICAASNYDDALCSDAIGWILNTQRPDGSWGFFDGQATAEETAYCIQALAHWQRHSGTSLSAQISRAGGWLSQHCEPPYAPLWIAKTLYCSATVVKAAILSALRLVDESNQ
|
Catalyzes the formation of tuberculosinyl diphosphate from geranylgeranyl diphosphate (GGPP). It could also react with (14R/S)-14,15-oxidoGGPP to generate 3alpha- and 3beta-hydroxytuberculosinyl diphosphate.
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O50580
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DT3E_PSECI
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D-tagatose 3-epimerase (DTE) (EC 5.1.3.31) (D-ribulose 3-epimerase) (Ketose 3-epimerase)
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MNKVGMFYTYWSTEWMVDFPATAKRIAGLGFDLMEISLGEFHNLSDAKKRELKAVADDLGLTVMCCIGLKSEYDFASPDKSVRDAGTEYVKRLLDDCHLLGAPVFAGLTFCAWPQSPPLDMKDKRPYVDRAIESVRRVIKVAEDYGIIYALEVVNRFEQWLCNDAKEAIAFADAVDSPACKVQLDTFHMNIEETSFRDAILACKGKMGHFHLGEANRLPPGEGRLPWDEIFGALKEIGYDGTIVMEPFMRKGGSVSRAVGVWRDMSNGATDEEMDERARRSLQFVRDKLA
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Catalyzes the epimerization of various ketoses at the C(3) position. It is able to interconvert D-tagatose and D-ribulose to D-sorbose and D-xylulose, respectively. The enzyme is also able to accept other ketopentoses such as D-psicose with lower efficiency.
|
O50657
|
DCLO_SELRU
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Lysine/ornithine decarboxylase (LDC) (EC 4.1.1.17) (EC 4.1.1.18)
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MKNFRLSEKEVKTLAKRIPTPFLVASLDKVEENYQFMRRHLPRAGVFYAMKANPTPEILSLLAGLGSHFDVASAGEMEILHELGVDGSQMIYANPVKDARGLKAAADYNVRRFTFDDPSEIDKMAKAVPGADVLVRIAVRNNKALVDLNTKFGAPVEEALDLLKAAQDAGLHAMGICFHVGSQSLSTAAYEEALLVARRLFDEAEEMGMHLTDLDIGGGFPVPDAKGLNVDLAAMMEAINKQIDRLFPDTAVWTEPGRYMCGTAVNLVTSVIGTKTRGEQPWYILDEGIYGCFSGIMYDHWTYPLHCFGKGNKKPSTFGGPSCDGIDVLYRDFMAPELKIGDKVLVTEMGSYTSVSATRFNGFYLAPTIIFEDQPEYAARLTEDDDVKKKAAV
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Decarboxylates both L-lysine and L-ornithine with similar catalytic efficiency.
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O51312
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ENO_BORBU
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Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
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MGFHIYEIKARQIIDSRGNPTVEADVILEDGTYGRAAVPSGASTGINEAVELRDGDKSVYMGKGVLKAIENIKNIIAPELEGMSALNQVAIDRKMLELDGTPTKEKLGANAILAVSMATAKAAAKYLGLRPYQYLGAYKANILPTPMCNIINGGAHSDNSVDFQEFMIMPIGAKTFSEAIRMAAEVFHTLKGILSGKGYATSVGDEGGFAPNLKSNEEACEVIIEAIKKAGYEPGKDIAIALDPATSELYDPKTKKYVLKWSTKEKLTSEQMVEYWAKWVEKYPIISIEDGMAEEDWDGWKKLTDKIGNKIQLVGDDLFVTNTSFLKKGIEMGVANSILIKVNQIGTLTETFEAVEMAKKAGYTAIVSHRSGETEDTTIADLVVALGTGQIKTGSLSRTDRIAKYNQLIRIEEELETTAEYHGKSVFYSIKQK
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Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}.
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O51934
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RGYR_THEMA
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Reverse gyrase [Includes: Helicase (EC 3.6.4.12); Topoisomerase (EC 5.6.2.2)]
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MAVNSKYHHSCINCGGLNTDERNERGLPCEVCLPEDSPSDIYRALLERKTLKEYRFYHEFWNEYEDFRSFFKKKFGKDLTGYQRLWAKRIVQGKSFTMVAPTGVGKTTFGMMTALWLARKGKKSALVFPTVTLVKQTLERLQKLADEKVKIFGFYSSMKKEEKEKFEKSFEEDDYHILVFSTQFVSKNREKLSQKRFDFVFVDDVDAVLKASRNIDTLLMMVGIPEEIIRKAFSTIKQGKIYERPKNLKPGILVVSSATAKPRGIRPLLFRDLLNFTVGRLVSVARNITHVRISSRSKEKLVELLEIFRDGILIFAQTEEEGKELYEYLKRFKFNVGETWSEFEKNFEDFKVGKINILIGVQAYYGKLTRGVDLPERIKYVIFWGTPSMRFSLELDKAPRFVLARVLKEMGLIKAQENPDVEELRKIAKEHLTQKEFVEKVKEMFRGVVVKDEDLELIIPDVYTYIQASGRSSRILNGVLVKGVSVIFEEDEEIFESLKTRLLLIAEEEIIEEAEANWKELVHEVEESRRRSERELTDTSRSLLIIVESPTKAETLSRFLGRASSRKERNIIVHEAVTGEGVILFTATRGHVYDLVTKGGIHGVEEENGKFVPVYNSLKRCRDCGYQFTEDRDECPVCSSKNIDDKTETLRALREISLEADEILVATDPDVEGEKISWDVTQYLLPSTRSLRRIEMHEITRYGFKKARESVRFVDFNLVKAQIVRRVQDRWIGFELSGKLQKRFGRSNLSAGRVQSTVLGWIVEREEEYKKSEKDFTLLVLENGVNLEVEGKIADDVVTVVELQEAEEEKNPLPPYTTSSALSEISQKLRLGVQEVMDILQDLFEKGFITYHRTDSTRISLEGQNVARTYLRKIGKEDIFMGRSWSTEGAHEAIRPVKPIDARELEEMIEEGLIADLTKKHLRVYELIFNRFLASQSAAVKVKKQIVTVDVDGKRMGIEQIVEILRDGWNLFVPLTVSPRFEHRTYKIKEKKFYKKHTVPLFTQASIVEEMKKRGIGRPSTYAKIVEVLFRRGYVYEDKYKRVRPTRFGVMVYSYLKERYEKYVTEETTRRLEEIMDKVERGEEDYQATLRLLYEEIKSLMEEG
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Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.
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O52063
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ATZC_PSESD
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N-isopropylammelide isopropyl amidohydrolase (EC 3.5.4.42)
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MSKDFDLIIRNAYLSEKDSVYDIGIVGDRIIKIEAKIEGTVKDEIDAKGNLVSPGFVDAHTHMDKSFTSTGERLPKFWSRPYTRDAAIEDGLKYYKNATHEEIKRHVIEHAHMQVLHGTLYTRTHVDVDSVAKTKAVEAVLEAKEELKDLIDIQVVAFAQSGFFVDLESESLIRKSLDMGCDLVGGVDPATRENNVEGSLDLCFKLAKEYDVDIDYHIHDIGTVGVYSINRLAQKTIENGYKGRVTTSHAWCFADAPSEWLDEAIPLYKDSGMKFVTCFSSTPPTMPVIKLLEAGINLGCASDNIRDFWVPFGNGDMVQGALIETQRLELKTNRDLGLIWKMITSEGARVLGIEKNYGIEVGKKADLVVLNSLSPQWAIIDQAKRLCVIKNGRIIVKDEVIVA
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Transforms N-isopropylammelide to cyanuric acid and isopropylamine.
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O52378
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NAGAA_RALSP
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Naphthalene 1,2-dioxygenase/salicylate 5-hydroxylase systems, ferredoxin--NAD(P)(+), reductase component (NDO/S5H systems, ferredoxin--NAD(P)(+), reductase component) (EC 1.18.1.7) (Ferredoxin reductase NagAa) (Ferredoxin--NAD(P)(+) reductase (naphthalene dioxygenase/salicylate 5-hydroxylase ferredoxin-specific))
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MELVVEPLNLHLNAETGSTLLDVLRSNEVPISYSCMSGRCGTCRCRVIAGHLRDNGPETGRPQAGKGTYVLACQAVLTEDCTIEIPESDEIVVHPARIVKGTVTAIDEATHDIRRLRIKLAKPLEFSPGQYATVQFTPECVRPYSMAGLPSDAEMEFQIRAVPGGHVSNYVFNELSVGASVRISGPLGTAYLRRTHTGPMLCVGGGTGLAPVLSIVRGALESGMSNPIHLYFGVRSEQDIYDEERLHALAARFPNLKVNVVVATGPAGPGRRSGLVTDLIGRDLPNLAGWRAYLCGAPAMVEALNLLVARLGIVPGHIHADAFYPSGV
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Component of two multicomponent enzyme systems which are involved in the catabolism of naphthalene. Plays a role as an electron transfer component for both salicylate 5-hydroxylase (S5H) and naphthalene 1,2-dioxygenase (NDO) systems, by transferring electrons from NAD(P)H to the oxygenase component via the ferredoxin NagAb. The electron transport chain from the two systems can use both NADH and NADPH as electron donors at approximately similar rates.
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O52552
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RIFK_AMYMS
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3-amino-5-hydroxybenzoate synthase (AHBA synthase) (EC 4.2.1.144) (Putative UDP-kanosamine synthase aminotransferase subunit) (EC 2.6.1.-)
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MNARKAPEFPAWPQYDDAERNGLVRALEQGQWWRMGGDEVNSFEREFAAHHGAAHALAVTNGTHALELALQVMGVGPGTEVIVPAFTFISSSQAAQRLGAVTVPVDVDAATYNLDPEAVAAAVTPRTKVIMPVHMAGLMADMDALAKISADTGVPLLQDAAHAHGARWQGKRVGELDSIATFSFQNGKLMTAGEGGAVVFPDGETEKYETAFLRHSCGRPRDDRRYFHKIAGSNMRLNEFSASVLRAQLARLDEQIAVRDERWTLLSRLLGAIDGVVPQGGDVRADRNSHYMAMFRIPGLTEERRNALVDRLVEAGLPAFAAFRAIYRTDAFWELGAPDESVDAIARRCPNTDAISSDCVWLHHRVLLAGEPELHATAEIIADAVARA
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Catalyzes the dehydration and aromatization of 5-amino-5-deoxy-3-dehydroshikimate (aminoDHS) to 3-amino-5-hydroxybenzoate (AHBA), a compound that then serves as the starter unit for the assembly of a polyketide during the biosynthesis of rifamycin B and other ansamycin antibiotics. Cannot utilize 5-deoxy-5-amino-3-dehydroquinate (aminoDHQ), 5-deoxy-5-aminoshikimate (aminoSA), quinate, 3-dehydroquinate, or 3-dehydroshikimate (DHS) as substrate. In a complex with RifL, RifK may have a second function in the AHBA pathway, acting as a transaminase introducing the nitrogen into the first pathway intermediate, UDP-3-keto-D-glucose, to give UDP-kanosamine. Appears to use glutamine as the nitrogen donor NH(4)(+) or asparagine are 30% less effective as nitrogen donors and neither glutamate nor aspartate show activity.
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O52582
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CDR_STAA8
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Coenzyme A disulfide reductase (CoA-disulfide reductase) (CoADR) (EC 1.8.1.14)
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MPKIVVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYVIGEVVEDRRYALAYTPEKFYDRKQITVKTYHEVIAINDERQTVSVLNRKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVSLEVLENLNERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEINAINGNEITFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGFLGNNIVKFFDYTFASVGVKPNELKQFDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNRQILRAAAVGKEGADKRIDVLSMAMMNQLTVDELTEFEVAYAPPYSHPKDLINMIGYKAK
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Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide. Is also active with other disulfide substrates containing at least one 4'-phosphopantethienyl moiety such as 4,4'-diphosphopantethine, but is not able to reduce oxidized glutathione, cystine, pantethine, or H(2)O(2).
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O52623
|
SOPE_SALTM
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Guanine nucleotide exchange factor SopE (Effector protein SopE) (Toxin SopE)
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MTKITLSPQNFRIQKQETTLLKEKSTEKNSLAKSILAVKNHFIELRSKLSERFISHKNTESSATHFHRGSASEGRAVLTNKVVKDFMLQTLNDIDIRGSASKDPAYASQTREAILSAVYSKNKDQCCNLLISKGINIAPFLQEIGEAAKNAGLPGTTKNDVFTPSGAGANPFITPLISSANSKYPRMFINQHQQASFKIYAEKIIMTEVAPLFNECAMPTPQQFQLILENIANKYIQNTP
|
Activator for both CDC42 and RAC1 by directly engaging these Rho GTPases and acting as potent guanine nucleotide exchange factor (GEF). This activation results in actin cytoskeleton rearrangements and stimulates membrane ruffling, promoting bacterial entry into non-phagocytic cells. Also activates MAPK8, indicating that it is capable of stimulating signaling pathways that can lead to nuclear responses. Chaperone InvB is required for secretion and translocation of SopE.
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O52646
|
DNRD_STRGJ
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Aklanonic acid methyl ester cyclase AcmA (AAME cyclase) (EC 5.5.1.23) (Methyl aklanonate cyclase)
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MSEQIAAVRRMVEAYNTGKTDDVADYIHPEYMNPGTLEFTSLRGPELFAINVAWVKKTFSEEARLEEVGIEERADWVRARLVLYGRHVGEMVGMAPTGRLFSGEQIHLLHFVDGKIHHHRDWPDYQGTYRQLGEPWPETEHRRP
|
Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the cyclization of aklanonic acid methyl ester to yield aklaviketone. It is also able to use nogalonic acid methyl ester as substrate, but produces exclusively auraviketone with C9-R stereochemistry.
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O52681
|
HYDC_THEMA
|
Bifurcating [FeFe] hydrogenase gamma subunit (EC 1.12.1.4) (Hydrogenase (NAD(+), ferredoxin) gamma subunit) (Iron-hydrogenase gamma subunit)
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MERHFEKVEEILKKYGYKRENLIKILLEIQEIYRYLPEDVINYVSTAMGIPPAKIYGVATFYAQFSLKPKGKYTIMVCDGTACHMAGSPEVLKAIEEETGLTPGNVTEDLMFSLDQVGCLGACALAPVMVINGEVYGNLTADKVKEILRKIKEKERESANV
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Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2). The gamma subunit might be the site where reduced ferredoxin is oxidized.
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O52793
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EVAA_AMYOR
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dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase (EC 4.2.1.159) (2,3-dehydratase)
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MSSFVVPSLTAVRPRDHHDYADRIALSAATTDGVQMRTEDVRAWIAERRDANVFHVERIPFADLDQWWFEGVTGNLVHRSGRFFTIEGLHVIEHDGPHGDGPYREWQQPVIRQPEVGILGILAKEFDGVLHFLMQAKMEPGNPNLVQLSPTVQATRSNYTKAHGGTNVKLIEYFAPPDPERVIVDVLQAEQGSWFFRKSNRNMIVETVDDVPLWDDFCWLTLGQIAELMHEDETINMNSRSVLSCLPYQDITPRALFSDVQLLSWFTNERSRHDVRVRRIPLADVCGWKQGAEEIEHEDGRYFKVLAVAVKGSNREKISWTQPLVESVDLGVVAFLVRKIDGVPHVLVQARVDGGFLDTVELAPTVQCTPLNYAHLPAEERPPFLDLVQNAPRSRIRYEAIHSEEGGRFLGVRARYLVIDADEAIDPPPGYAWVTPAQLTALTRHGHYVNVEARTLLACINAAAAQPRGGA
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Involved in the biosynthesis of the 2,3,6-trideoxysugar L-epivancosamine, the terminal sugar added to the aglycone scaffold of chloroeremomycin, a member of the glycopeptide antibiotics vancomycin family. Catalyzes the removal of the hydroxyl group at position C-2 of the hexose ring of dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose, and the oxidation of the hydroxyl group at position C-3 to form a carbonyl functionality. The product of the reaction, dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose, is a highly unstable diketosugar, which spontaneously forms dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose.
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O52958
|
KPRS_THEKO
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Ribose-phosphate pyrophosphokinase (RPPK) (EC 2.7.6.1) (5-phospho-D-ribosyl alpha-1-diphosphate synthase) (Phosphoribosyl diphosphate synthase) (Phosphoribosyl pyrophosphate synthase) (P-Rib-PP synthase) (PRPP synthase) (PRPPase)
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MFLLGSGGKHFEDELRNAGAKILEVEIKRFPDGEKYVRVMGNGDEATVVSSTFYPQDEKIVELLLLGDALREKGFEKLKLVVPYFAYSRQDRVTKDGEPISVRAVMRALGIYYEELYIFDTHNPETLRFFPGKAVNVSPARVIGEYFREKLGDGLVLAPDKGALERARAVAEVLGLEYSHFEKRRISPTEVEMHPVDVDVKGKNVLIVDDIISTGGTMVRAAELLRKLGAKKIYVSATHGVFAEGAIERVSRAVDELAVTNTIPTPVSRISIVPELLKLE
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Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). It can also use CTP and GTP as substrates in addition to ATP. {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|Ref.1}.
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O53166
|
ACNA_MYCTU
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Aconitate hydratase A (ACN) (Aconitase) (EC 4.2.1.3) ((2R,3S)-2-methylisocitrate dehydratase) ((2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase) (Iron-responsive protein-like) (IRP-like) (Probable 2-methyl-cis-aconitate hydratase) (EC 4.2.1.99) (RNA-binding protein)
|
MTSKSVNSFGAHDTLKVGEKSYQIYRLDAVPNTAKLPYSLKVLAENLLRNEDGSNITKDHIEAIANWDPKAEPSIEIQYTPARVVMQDFTGVPCIVDLATMREAIADLGGNPDKVNPLAPADLVIDHSVIADLFGRADAFERNVEIEYQRNGERYQFLRWGQGAFDDFKVVPPGTGIVHQVNIEYLASVVMTRDGVAYPDTCVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLIPRVVGFRLTGEIQPGVTATDVVLTVTEMLRQHGVVGKFVEFYGEGVAEVPLANRATLGNMSPEFGSTAAIFPIDEETIKYLRFTGRTPEQVALVEAYAKAQGMWHDPKHEPEFSEYLELNLSDVVPSIAGPKRPQDRIALAQAKSTFREQIYHYVGNGSPDSPHDPHSKLDEVVEETFPASDPGQLTFANDDVATDETVHSAAAHADGRVSNPVRVKSDELGEFVLDHGAVVIAAITSCTNTSNPEVMLGAALLARNAVEKGLTSKPWVKTTIAPGSQVVNDYYDRSGLWPYLEKLGFYLVGYGCTTCIGNSGPLPEEISKAVNDNDLSVTAVLSGNRNFEGRINPDVKMNYLASPPLVIAYALAGTMDFDFQTQPLGQDKDGKNVFLRDIWPSQQDVSDTIAAAINQEMFTRNYADVFKGDDRWRNLPTPSGNTFEWDPNSTYVRKPPYFEGMTAKPEPVGNISGARVLALLGDSVTTDHISPAGAIKPGTPAARYLDEHGVDRKDYNSFGSRRGNHEVMIRGTFANIRLRNQLLDDVSGGYTRDFTQPGGPQAFIYDAAQNYAAQHIPLVVFGGKEYGSGSSRDWAAKGTLLLGVRAVIAESFERIHRSNLIGMGVIPLQFPEGKSASSLGLDGTEVFDITGIDVLNDGKTPKTVCVQATKGDGATIEFDAVVRIDTPGEADYYRNGGILQYVLRNILKSG
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Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA-binding regulatory protein which binds to selected IRE-like sequences present within the UTRs (untranslated regions) of 3' trxC and 5' IdeR mRNA. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate (By similarity).
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O53168
|
RIPA_MYCTU
|
Peptidoglycan endopeptidase RipA (EC 3.4.-.-) (Macrophage invasion and intracellular persistence protein A) (Resuscitation-promoting factor interaction partner A) (Rpf-interacting protein A)
|
MRRNRRGSPARPAARFVRPAIPSALSVALLVCTPGLATADPQTDTIAALIADVAKANQRLQDLSDEVQAEQESVNKAMVDVETARDNAAAAEDDLEVSQRAVKDANAAIAAAQHRFDTFAAATYMNGPSVSYLSASSPDEIIATVTAAKTLSASSQAVMANLQRARTERVNTESAARLAKQKADKAAADAKASQDAAVAALTETRRKFDEQREEVQRLAAERDAAQARLQAARLVAWSSEGGQGAPPFRMWDPGSGPAGGRAWDGLWDPTLPMIPSANIPGDPIAVVNQVLGISATSAQVTANMGRKFLEQLGILQPTDTGITNAPAGSAQGRIPRVYGRQASEYVIRRGMSQIGVPYSWGGGNAAGPSKGIDSGAGTVGFDCSGLVLYSFAGVGIKLPHYSGSQYNLGRKIPSSQMRRGDVIFYGPNGSQHVTIYLGNGQMLEAPDVGLKVRVAPVRTAGMTPYVVRYIEY
|
Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages.
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O53177
|
RPFE_MYCTU
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Resuscitation-promoting factor RpfE (EC 3.-.-.-)
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MKNARTTLIAAAIAGTLVTTSPAGIANADDAGLDPNAAAGPDAVGFDPNLPPAPDAAPVDTPPAPEDAGFDPNLPPPLAPDFLSPPAEEAPPVPVAYSVNWDAIAQCESGGNWSINTGNGYYGGLRFTAGTWRANGGSGSAANASREEQIRVAENVLRSQGIRAWPVCGRRG
|
Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Active in the pM concentration range. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity. Stimulates growth of stationary phase M.bovis (a slow-growing Mycobacterium), reduces the lag phase of diluted fast-growers M.smegmatis and Micrococcus luteus. Sequential gene disruption indicates RpfB and RpfE are higher than RpfD and RpfC in functional hierarchy.
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O53181
|
KORB_MYCTU
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2-oxoglutarate oxidoreductase subunit KorB (EC 1.2.7.3) (Alpha-ketoglutarate oxidoreductase subunit beta) (KG oxidoreductase subunit beta) (KGO subunit beta) (KOR subunit beta)
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MTRSGDEAQLMTGVTGDLAGTELGLTPSLTKNAGVPTTDQPQKGKDFTSDQEVRWCPGCGDYVILNTIRNFLPELGLRRENIVFISGIGCSSRFPYYLETYGFHSIHGRAPAIATGLALAREDLSVWVVTGDGDALSIGGNHLIHALRRNINVTILLFNNRIYGLTKGQYSPTSEVGKVTKSTPMGSLDHPFNPVSLALGAEATFVGRALDSDRNGLTEVLRAAAQHRGAALVEILQDCPIFNDGSFDALRKEGAEERVIKVRHGEPIVFGANGEYCVVKSGFGLEVAKTADVAIDEIIVHDAQVDDPAYAFALSRLSDQNLDHTVLGIFRHISRPTYDDAARSQVVAARNAAPSGTAALQSLLHGRDTWTVD
|
Component of KG oxidoreductase (KOR) that catalyzes the CoA-dependent oxidative decarboxylation of 2-oxoglutarate (alpha-ketoglutarate, KG) to succinyl-CoA. Methyl viologen can act as electron acceptor in vitro the physiologic electron acceptor is unknown. Is involved in the alternative TCA pathway that functions concurrently with fatty acid beta-oxidation. Since a growing body of evidence indicates that lipids (for example cholesterol and fatty acids) are a predominant growth substrate for M.tuberculosis during infection, flux through KOR likely represents an important step in intermediary metabolism in vivo. KOR-dependent decarboxylation of KG also appears to be an important source of CO(2) in M.tuberculosis metabolism.
|
O53223
|
LDT2_MYCTO
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L,D-transpeptidase 2 (LDT 2) (EC 2.3.2.-) (Ldt(Mt2))
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MPKVGIAAQAGRTRVRRAWLTALMMTAVMIGAVACGSGRGPAPIKVIADKGTPFADLLVPKLTASVTDGAVGVTVDAPVSVTAADGVLAAVTMVNDNGRPVAGRLSPDGLRWSTTEQLGYNRRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMPGDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREVRWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATADDNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTYGVPVNSPNGYRTDVDWATQISYSGVFVHSAPWSVGAQGHTNTSHGCLNVSPSNAQWFYDHVKRGDIVEVVNTVGGTLPGIDGLGDWNIPWDQWRAGNAKA
|
Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems. Is essential for virulence in a mouse model of acute infection.
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O53289
|
SERB2_MYCTU
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Phosphoserine phosphatase SerB2 (PSP) (PSPase) (EC 3.1.3.3) (O-phosphoserine phosphohydrolase) (Protein-serine/threonine phosphatase) (EC 3.1.3.16)
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MPAKVSVLITVTGMDQPGVTSALFEVLAQHGVELLNVEQVVIRGRLTLGVLVSCPLDVADGTALRDDVAAAIHGVGLDVAIERSDDLPIIRQPSTHTIFVLGRPITAGAFSAVARGVAALGVNIDFIRGISDYPVTGLELRVSVPPGCVGPLQIALTKVAAEEHVDVAVEDYGLAWRTKRLIVFDVDSTLVQGEVIEMLAARAGAQGQVAAITEAAMRGELDFAESLQRRVATLAGLPATVIDDVAEQLELMPGARTTIRTLRRLGFRCGVVSGGFRRIIEPLARELMLDFVASNELEIVDGILTGRVVGPIVDRPGKAKALRDFASQYGVPMEQTVAVGDGANDIDMLGAAGLGIAFNAKPALREVADASLSHPYLDTVLFLLGVTRGEIEAADAGDCGVRRVEIPAD
|
Catalyzes the dephosphorylation of O-phospho-L-serine into L-serine, a step in the L-serine biosynthetic pathway. Exhibits high specificity for L-phosphoserine compared to substrates like L-phosphothreonine (5% relative activity) and L-phosphotyrosine (1.7% relative activity). In the host, induces significant cytoskeleton rearrangements through cofilin dephosphorylation and its subsequent activation, and affects the expression of genes that regulate actin dynamics. It specifically interacts with HSP90, HSP70 and HSP27 that block apoptotic pathways but not with other HSPs. Also interacts with GAPDH. It actively dephosphorylates MAP kinase p38 and NF-kappa B p65 (specifically at Ser-536) that play crucial roles in inflammatory and immune responses. This in turn leads to down-regulation of Interleukin 8, a chemotactic and inflammatory cytokine. Thus might help the pathogen to evade the host's immune response. Exogenous addition of purified SerB2 protein to human THP-1 cells (that can be differentiated into macrophage-like cells) induces microtubule rearrangements the phosphatase activity is co-related to the elicited rearrangements, while addition of the ACT-domains alone elicits no rearrangements.
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O53353
|
WHB2A_MYCTU
|
Transcriptional regulator WhiB2 (Probable chaperone WhiB2)
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MVPEAPAPFEEPLPPEATDQWQDRALCAQTDPEAFFPEKGGSTREAKKICMGCEVRHECLEYALAHDERFGIWGGLSERERRRLKRGII
|
Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA (By similarity). The apo-form functions as a chaperone, preventing aggregation or helping in correct refolding of a number of substrates this activity does not require ATP or the ability to bind a Fe-S cluster. Chaperone activity is insensitive to the redox state of its cysteine residues. The apo-form has no protein disulfide reductase activity. The apo-form binds to its own promoter.
|
O53361
|
SAPM_MYCTU
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Phosphatidylinositol-3-phosphatase (PI3P phosphatase) (EC 3.1.3.64) (Acid phosphatase SapM) (EC 3.1.3.2) (Secreted acid phosphatase)
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MLRGIQALSRPLTRVYRALAVIGVLAASLLASWVGAVPQVGLAASALPTFAHVVIVVEENRSQAAIIGNKSAPFINSLAANGAMMAQAFAETHPSEPNYLALFAGNTFGLTKNTCPVNGGALPNLGSELLSAGYTFMGFAEDLPAVGSTVCSAGKYARKHVPWVNFSNVPTTLSVPFSAFPKPQNYPGLPTVSFVIPNADNDMHDGSIAQGDAWLNRHLSAYANWAKTNNSLLVVTWDEDDGSSRNQIPTVFYGAHVRPGTYNETISHYNVLSTLEQIYGLPKTGYATNAPPITDIWGD
|
Virulence factor that plays an important role in blocking phagosome-lysosome fusion and thus participates in the intracellular survival of the pathogen. Acts as a phosphatase that dephosphorylates phosphatidylinositol 3-phosphate (PI3P), a membrane trafficking regulatory lipid essential for phagosomal acquisition of lysosomal constituents. Therefore, SapM eliminates PI3P from the phagosomal membrane by catalyzing its hydrolysis, and thus contributes to inhibition of phagosome maturation. Also interferes with autophagy: SapM blocks autophagosome-lysosome fusion in macrophages by binding to the small GTPase RAB7, which prevents RAB7 from being involved in this process and thus negatively regulates autophagy flux. In vitro, displays phosphatase activity with broad specificity can dephosphorylate a variety of phosphoester substrates, with the highest activity against phosphoenolpyruvate, glycerophosphate, GTP, NADPH, phosphotyrosine and trehalose-6-phosphate. In contrast, the enzyme exhibits poor activity against glucose-6-phosphate, phosphothreonine, and a number of nucleotides (NADP, ATP, AMP, and GMP).
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O53423
|
GDSLL_MYCTU
|
GDSL-like esterase Rv1075c (EC 3.1.-.-) (Acetylesterase) (EC 3.1.1.6)
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MPRRSTIALATAGALASTGTAYLGARNLLVGQATHARTVIPKSFDAPPRADGVYTRGGGPVQRWRREVPFDVHLMIFGDSTATGYGCASAEEVPGVLIARGLAEQTGKRIRLSTKAIVGATSKGVCGQVDAMFVVGPPPDAAVIMIGANDITALNGIGPSAQRLADCVRRLRTRGAVVVVGTCPDLGVITAIPQPLRALAHTRGVRLARAQTAAVKAAGGVPVPLGHLLAPKFRAMPELMFSADRYHPSAPAYALAADLLFLALRDALTEKLDIPIHETPSRPGTATLEPGHTRHSMMSRLRRPRPARAVPTGG
|
Esterase that preferentially hydrolyzes short-chain fatty acids, particularly pNP-acetate (C2) and pNP-butyrate (C4). Has also weak activity with pNP-hexanoate (C6) and pNP-octanoate (C8). It can also hydrolyze short-chain tryglycerides such as triacetin and tributyrin. Important for intracellular survival.
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O53424
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LIPU_MYCTU
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Esterase LipU (EC 3.1.1.-)
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MAVRPVLAVGSYLPHAPWPWGVIDQAARVLLPASTTVRAAVSLPNASAQLVRASGVLPADGTRRAVLYLHGGAFLTCGANSHGRLVELLSKFADSPVLVVDYRLIPKHSIGMALDDCHDGYRWLRLLGYEPEQIVLAGDSAGGYLALALAQRLQEVGEEPAALVAISPLLQLAKEHKQAHPNIKTDAMFPARAFDALDALVASAAARNQVDGEPEELYEPLEHITPGLPRTLIHVSGSEVLLHDAQLAAAKLAAAGVPAEVRVWPGQVHDFQVAASMLPEAIRSLRQIGEYIREATG
|
Esterase that shows preference for short chain fatty acids. Contributes to the growth of M.tuberculosis during the nutritive stress. Elicits strong humoral response in both extrapulmonary and relapsed cases of tuberculosis patients.
|
O53493
|
PPMNT_MYCTU
|
Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase [Includes: Apolipoprotein N-acyltransferase (ALP N-acyltransferase) (EC 2.3.1.269); Polyprenol monophosphomannose synthase (PPM synthase) (Polyprenol-P-Man synthase) (Ppm1) (EC 2.4.1.-) (Dolichol-phosphate mannose synthase) (EC 2.4.1.83)]
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MKLGAWVAAQLPTTRTAVRTRLTRLVVSIVAGLLLYASFPPRNCWWAAVVALALLAWVLTHRATTPVGGLGYGLLFGLVFYVSLLPWIGELVGPGPWLALATTCALFPGIFGLFAVVVRLLPGWPIWFAVGWAAQEWLKSILPFGGFPWGSVAFGQAEGPLLPLVQLGGVALLSTGVALVGCGLTAIALEIEKWWRTGGQGDAPPAVVLPAACICLVLFAAIVVWPQVRHAGSGSGGEPTVTVAVVQGNVPRLGLDFNAQRRAVLDNHVEETLRLAADVHAGLAQQPQFVIWPENSSDIDPFVNPDAGQRISAAAEAIGAPILIGTLMDVPGRPRENPEWTNTAIVWNPGTGPADRHDKAIVQPFGEYLPMPWLFRHLSGYADRAGHFVPGNGTGVVRIAGVPVGVATCWEVIFDRAPRKSILGGAQLLTVPSNNATFNKTMSEQQLAFAKVRAVEHDRYVVVAGTTGISAVIAPDGGELIRTDFFQPAYLDSQVRLKTRLTPATRWGPILQWILVGAAAAVVLVAMRQNGWFPRPRRSEPKGENDDSDAPPGRSEASGPPALSESDDELIQPEQGGRHSSGFGRHRATSRSYMTTGQPAPPAPGNRPSQRVLVIIPTFNERENLPVIHRRLTQACPAVHVLVVDDSSPDGTGQLADELAQADPGRTHVMHRTAKNGLGAAYLAGFAWGLSREYSVLVEMDADGSHAPEQLQRLLDAVDAGADLAIGSRYVAGGTVRNWPWRRLVLSKTANTYSRLALGIGIHDITAGYRAYRREALEAIDLDGVDSKGYCFQIDLTWRTVSNGFVVTEVPITFTERELGVSKMSGSNIREALVKVARWGIEGRLSRSDHARARPDIARPGAGGSRVSRADVTE
|
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Transfers mannose from GDP-mannose to lipid acceptors (works best on C20-C95 lipid monophosphate substrates in which the lipid can be modified, tested with the C-terminal domain expressed in M.smegmatis) to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor which adds mannose-phosphate residues to triacylated-phosphatidyl-myo-inositol mannosides (PIM2), eventually leading to generation of the cell wall glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM).
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O53512
|
AROG_MYCTU
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Phospho-2-dehydro-3-deoxyheptonate aldolase AroG (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase) (DAHP synthase) (Phospho-2-keto-3-deoxyheptonate aldolase)
|
MNWTVDIPIDQLPSLPPLPTDLRTRLDAALAKPAAQQPTWPADQALAMRTVLESVPPVTVPSEIVRLQEQLAQVAKGEAFLLQGGDCAETFMDNTEPHIRGNVRALLQMAVVLTYGASMPVVKVARIAGQYAKPRSADIDALGLRSYRGDMINGFAPDAAAREHDPSRLVRAYANASAAMNLVRALTSSGLASLHLVHDWNREFVRTSPAGARYEALATEIDRGLRFMSACGVADRNLQTAEIYASHEALVLDYERAMLRLSDGDDGEPQLFDLSAHTVWIGERTRQIDGAHIAFAQVIANPVGVKLGPNMTPELAVEYVERLDPHNKPGRLTLVSRMGNHKVRDLLPPIVEKVQATGHQVIWQCDPMHGNTHESSTGFKTRHFDRIVDEVQGFFEVHRALGTHPGGIHVEITGENVTECLGGAQDISETDLAGRYETACDPRLNTQQSLELAFLVAEMLRD
|
Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate.
|
O53547
|
CHSB1_MYCTU
|
Hydroxyacyl-CoA dehydrogenase ChsB1 (EC 1.1.1.-)
|
MKLTESNRSPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVVDEIGAAAADAGAKAVAVAGDISQRATADELLASAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRDKAKDAEGGSVFGRLVNTSSEAGLVGPVGQANYAAAKAGITALTLSAARALGRYGVCANVICPRARTAMTADVFGAAPDVEAGQIDPLSPQHVVSLVQFLASPAAAEVNGQVFIVYGPQVTLVSPPHMERRFSADGTSWDPTELTATLRDYFAGRDPEQSFSATDLMRQ
|
A reversible dehydrogenase involved in cholesterol side-chain degradation. Catalyzes the oxidation of hydroxyl-cholesterol-CoA ester metabolic intermediate (22S)-HOCO-CoA (3-oxo-chol-4-ene-(22S)-hydroxy-24-oyl-CoA), the product of ChsH3, has no activity on (22R)-HOCO-CoA (the product of EchA19). Also acts on (3R)-hydroxyoctanoyl-CoA and 17-beta-hydroxyandrost-4-en-3-one, but not on 7-alpha-hydroxyandrost-4-en-3-one, uses NAD(+) but not NADP(+).
|
O53551
|
FAC17_MYCTU
|
Medium/long-chain-fatty-acid--CoA ligase FadD17 (FACL) (EC 6.2.1.2) (EC 6.2.1.3) (Acyl-CoA synthetase) (FACL17) (Steroid-24-oyl-CoA synthetase)
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MTPTHPTVTELLLPLSEIDDRGVYFEDSFTSWRDHIRHGAAIAAALRERLDPARPPHVGVLLQNTPFFSATLVAGALSGIVPVGLNPVRRGAALAGDIAKADCQLVLTGSGSAEVPADVEHINVDSPEWTDEVAAHRDTEVRFRSADLADLFMLIFTSGTSGDPKAVKCSHRKVAIAGVTITQRFSLGRDDVCYVSMPLFHSNAVLVGWAVAAACQGSMALRRKFSASQFLADVRRYGATYANYVGKPLSYVLATPELPDDADNPLRAVYGNEGVPGDIDRFGRRFGCVVMDGFGSTEGGVAITRTLDTPAGALGPLPGGIQIVDPDTGEPCPTGVVGELVNTAGPGGFEGYYNDEAAEAERMAGGVYHSGDLAYRDDAGYAYFAGRLGDWMRVDGENLGTAPIERVLMRYPDATEVAVYPVPDPVVGDQVMAALVLAPGTKFDADKFRAFLTEQPDLGHKQWPSYVRVSAGLPRTMTFKVIKRQLSAEGVACADPVWPIRR
|
Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. Also involved in steroid side-chain degradation. Activates cholesterol metabolites with a C5 side chain, including cholate and chenodeoxycholate.
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O53561
|
ECH19_MYCTU
|
Enoyl-CoA hydratase EchA19 (EC 4.2.1.-)
|
MATVESGPDALVERRGHTLIVTMNRPAARNALSTEMMRIMVQAWDRVDNDPDIRCCILTGAGGYFCAGMDLKAATQKPPGDSFKDGSYGPSRIDALLKGRRLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLYPMGGSAVRLVRQIPYTLACDLLLTGRHITAAEAKEMGLIGHVVPDGQALTKALELADAISANGPLAVQAILRSIRETECMPENEAFKIDTQIGIKVFLSDDAKEGPRAFAEKRAPNFQNR
|
Degradation of the cholesterol side chain involves 3 multistep beta-oxidation cycles, this may be involved in the second cycle (Probable). Hydrates 3-OCDO-CoA ((22E)-3-oxo-chol-4,22-dien-24-oyl-CoA) to make (22R)-HOCO-CoA (3-oxo-chol-4-ene-(22R)-hydroxy-24-oyl-CoA). Also acts on octenoyl-CoA. Not active on (E)-3-OCDS-CoA ((E)-3-oxocholest-4,24-dien-26-oyl-CoA) or 3-OPDC-CoA (3-oxo-4,17-pregnadiene-20-carboxyl-CoA). Hydrates the same substrate as ChsH3, but the 2 enzymes make different stereoisomers of the product.
|
O53580
|
FAA32_MYCTU
|
Long-chain-fatty-acid--AMP ligase FadD32 (FAAL) (EC 6.2.1.20) (Acyl-AMP synthetase) (FAAL32)
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MFVTGESGMAYHNPFIVNGKIRFPANTNLVRHVEKWAKVRGDKLAYRFLDFSTERDGVARDILWSDFSARNRAVGARLQQVTQPGDRVAILCPQNLDYLISFFGALYSGRIAVPLFDPAEPGHVGRLHAVLDDCAPSTILTTTDSAEGVRKFIRARSAKERPRVIAVDAVPTEVAATWQQPEANEETVAYLQYTSGSTRIPSGVQITHLNLPTNVVQVLNALEGQEGDRGVSWLPFFHDMGLITVLLASVLGHSFTFMTPAAFVRRPGRWIRELARKPGETGGTFSAAPNFAFEHAAVRGVPRDDEPPLDLSNVKGILNGSEPVSPASMRKFFEAFAPYGLKQTAVKPSYGLAEATLFVSTTPMDEVPTVIHVDRDELNNQRFVEVAADAPNAVAQVSAGKVGVSEWAVIVDADTASELPDGQIGEIWLHGNNLGTGYWGKEEESAQTFKNILKSRISESRAEGAPDDALWVRTGDYGTYFKDHLYIAGRIKDLVIIDGRNHYPQDLECTAQESTKALRVGYAAAFSVPANQLPQTVFDDSHAGLKFDPEDTSEQLVIVGERAAGTHKLDHQPIVDDIRAAIAVGHGVTVRDVLLVSAGTIPRTSSGKIGRRACRAAYLDGSLRSGVGSPTVFATSD
|
Involved in the biosynthesis of mycolic acids. Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension. Can use dodecanoate (C12), tetradecanoate (C14) and hexadecanoate (C16). In vitro, displays a preference for long-chain over medium and short-chain fatty acid substrates.
|
O53581
|
CULP6_MYCTU
|
Carboxylesterase/lipase Culp6 (EC 3.1.1.-) (Cell wall lipase) (Cutinase-like protein 6) (Culp6)
|
MAKNSRRKRHRILAWIAAGAMASVVALVIVAVVIMLRGAESPPSAVPPGVLPPGPTPAHPHKPRPAFQDASCPDVQMISVPGTWESSPQQNPLNPVQFPKALLLKVTGPIAQQFAPARVQTYTVAYTAQFHNPLTTDNQMSYNDSRAEGTRAMVAAMTDMNNRCPLTSYVLIGFSQGAVIAGDVASDIGNGRGPVDEDLVLGVTLIADGRRQQGVGNQVPPSPRGEGAEITLHEVPVLSGLGLTMTGPRPGGFGALDGRTNEICAQGDLICAAPAQAFSPANLPTTLNTLAGGAGQPVHAMYATPEFWNSDGEPATEWTLNWAHQLIENAPHPKHR
|
Shows esterase and phospholipase A activities. May be involved in cell wall biosynthesis and/or maintenance. Can hydrolyze various substrates, including the p-nitrophenol-linked aliphatic esters pNP-laurate (C12), pNP-myristate (C14), pNP-palmitate (C16), pNP-stearate (C18), pNP-butyrate (C4), phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, 4-methylumbelliferyl heptanoate and palmitic acid and arachidonic acid containing phospholipids. Does not exhibit cutinase activity.
|
O53585
|
GLFT2_MYCTU
|
Galactofuranosyltransferase GlfT2 (GalTr 2) (EC 2.4.1.288) (Arabinogalactan galactosyltransferase 2) (Galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase) (Polymerizing galactofuranosyltransferase GlfT2)
|
MSELAASLLSRVILPRPGEPLDVRKLYLEESTTNARRAHAPTRTSLQIGAESEVSFATYFNAFPASYWRRWTTCKSVVLRVQVTGAGRVDVYRTKATGARIFVEGHDFTGTEDQPAAVETEVVLQPFEDGGWVWFDITTDTAVTLHSGGWYATSPAPGTANIAVGIPTFNRPADCVNALRELTADPLVDQVIGAVIVPDQGERKVRDHPDFPAAAARLGSRLSIHDQPNLGGSGGYSRVMYEALKNTDCQQILFMDDDIRLEPDSILRVLAMHRFAKAPMLVGGQMLNLQEPSHLHIMGEVVDRSIFMWTAAPHAEYDHDFAEYPLNDNNSRSKLLHRRIDVDYNGWWTCMIPRQVAEELGQPLPLFIKWDDADYGLRAAEHGYPTVTLPGAAIWHMAWSDKDDAIDWQAYFHLRNRLVVAAMHWDGPKAQVIGLVRSHLKATLKHLACLEYSTVAIQNKAIDDFLAGPEHIFSILESALPQVHRIRKSYPDAVVLPAASELPPPLHKNKAMKPPVNPLVIGYRLARGIMHNLTAANPQHHRRPEFNVPTQDARWFLLCTVDGATVTTADGCGVVYRQRDRAKMFALLWQSLRRQRQLLKRFEEMRRIYRDALPTLSSKQKWETALLPAANQEPEHG
|
Involved in the galactan polymerization of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacteria cell wall. Thus, successively transfers approximately 28 galactofuranosyl (Galf) residues from UDP-galactofuranose (UDP-Galf) onto the galactofuranosyl-galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-GlcNAc-PP-C50) acceptor produced by GlfT1, with alternating 1->5 and 1->6 links, forming a galactan domain with approximately 30 galactofuranosyl residues.
|
O53638
|
LDT1_MYCTU
|
L,D-transpeptidase 1 (LDT 1) (EC 2.3.2.-) (Ldt(Mt1))
|
MRRVVRYLSVVVAITLMLTAESVSIATAAVPPLQPIPGVASVSPANGAVVGVAHPVVVTFTTPVTDRRAVERSIRISTPHNTTGHFEWVASNVVRWVPHRYWPPHTRVSVGVQELTEGFETGDALIGVASISAHTFTVSRNGEVLRTMPASLGKPSRPTPIGSFHAMSKERTVVMDSRTIGIPLNSSDGYLLTAHYAVRVTWSGVYVHSAPWSVNSQGYANVSHGCINLSPDNAAWYFDAVTVGDPIEVVG
|
Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems. Is thought to play a role in adaptation to the nonreplicative state of M.tuberculosis.
|
O53664
|
HTDX_MYCTU
|
3-hydroxyacyl-thioester dehydratase X (EC 4.2.1.-) (3-hydroxybutyryl-CoA dehydratase) (EC 4.2.1.55) (Enoyl-CoA hydratase 2) (EC 4.2.1.119)
|
MTQPSGLKNLLRAAAGALPVVPRTDQLPNRTVTVEELPIDPANVAAYAAVTGLRYGNQVPLTYPFALTFPSVMSLVTGFDFPFAAMGAIHTENHITQYRPIAVTDAVGVRVRAENLREHRRGLLVDLVTNVSVGNDVAWHQVTTFLHQQRTSLSGEPKPPPQKKPKLPPPAAVLRITPAKIRRYAAVGGDHNPIHTNPIAAKLFGFPTVIAHGMFTAAAVLANIEARFPDAVRYSVRFAKPVLLPATAGLYVAEGDGGWDLTLRNMAKGYPHLTATVRGL
|
Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase activity. Displays a broad chain length specificity, with a predilection for the C8 to C12 substrates.
|
O53666
|
FADE5_MYCTU
|
Broad-specificity linear acyl-CoA dehydrogenase FadE5 (Long-chain-acyl-CoA dehydrogenase) (EC 1.3.8.8) (Medium-chain-acyl-CoA dehydrogenase) (EC 1.3.8.7) (Short-chain-acyl-CoA dehydrogenase) (EC 1.3.8.1)
|
MSHYRSNVRDQVFNLFEVLGVDKALGHGEFSDVDVDTARDMLAEVSRLAEGPVAESFVEGDRNPPVFDPKTHSVMLPESFKKSVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHILGANPAVWMYAGGAGFAQILYHLGTEEQKKWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDVETGEPGERNGVFVTNVEHKMGLKVSATCELAFGQHGVPAKGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGADLTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRALYLYTATFQDAAVAEVVHGVDAKLAVKVNDLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQAQDFFFRKIVRDKGVALAHVSGQIQEFVDSGAGNGRLKTERALLAKALTDVQGMAAALTGYLMAAQQDVTSLYKVGLGSVRFLMSVGDLIIGWLLQRQAAVAVAALDAGATGDERSFYEGKVAVASFFAKNFLPLLTSTREVIETLDNDIMELDEAAF
|
Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates.
|
O53699
|
STF0_MYCTU
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Trehalose 2-sulfotransferase (EC 2.8.2.37)
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MSRAVRPYLVLATQRSGSTLLVESLRATGCAGEPQEFFQYLPSTGMAPQPREWFAGVDDDTILQLLDPLDPGTPDTATPVAWREHVRTSGRTPNGVWGGKLMWNQTALLQQRAAQLPDRSGDGLRAAIRDVIGNEPVFVHVHRPDVVSQAVSFWRAVQTQVWRGHPDPKRDSQAVYHAGAIAHIIRNLRDQENGWRAWFAEEGIDPIDIAYPVLWRNLTAIVASVLDAIGQDPKLAPAPMLERQANQRSDEWVDRYRAEAPRLGLPT
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Catalyzes the sulfuryl group transfer from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to trehalose, leading to trehalose-2-sulfate (T2S). The sulfation of trehalose is the first step in the biosynthesis of sulfolipid-1 (SL-1), a major cell wall glycolipid and the most abundant sulfated metabolite found in Mycobacterium tuberculosis, that is a potential virulence factor thought to mediate host-pathogen interactions.
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O53873
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XPB_MYCTU
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DNA helicase XPB (EC 3.6.4.12)
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MTDGPLIVQSDKTVLLEVDHELAGAARAAIAPFAELERAPEHVHTYRITPLALWNARAAGHDAEQVVDALVSYSRYAVPQPLLVDIVDTMARYGRLQLVKNPAHGLTLVSLDRAVLEEVLRNKKIAPMLGARIDDDTVVVHPSERGRVKQLLLKIGWPAEDLAGYVDGEAHPISLHQEGWQLRDYQRLAADSFWAGGSGVVVLPCGAGKTLVGAAAMAKAGATTLILVTNIVAARQWKRELVARTSLTENEIGEFSGERKEIRPVTISTYQMITRRTKGEYRHLELFDSRDWGLIIYDEVHLLPAPVFRMTADLQSKRRLGLTATLIREDGREGDVFSLIGPKRYDAPWKDIEAQGWIAPAECVEVRVTMTDSERMMYATAEPEERYRICSTVHTKIAVVKSILAKHPDEQTLVIGAYLDQLDELGAELGAPVIQGSTRTSEREALFDAFRRGEVATLVVSKVANFSIDLPEAAVAVQVSGTFGSRQEEAQRLGRILRPKADGGGAIFYSVVARDSLDAEYAAHRQRFLAEQGYGYIIRDADDLLGPAI
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ATP-dependent 3'-5' DNA helicase, unwinds 3'-overhangs, 3'- flaps, and splayed-arm DNA substrates but not 5'-overhangs, 5'-flap substrates, 3-way junctions or Holliday junctions. Not highly efficient in vitro. Requires ATP hydrolysis for helicase activity the ATPase activity is DNA-dependent and requires a minimum of 4 single-stranded nucleotides (nt) with 6-10 nt providing all necessary interactions for full processive unwinding. The ATPase prefers ATP over CTP or GTP, is almost inactive with TTP. DNA helicase activity requires ATP or dATP and only acts when the 3'-overhang is >20 nt. Capable of unwinding a DNA:RNA hybrid if the 3'-overhang is DNA. Also catalyzes ATP-independent annealing of complementary DNA strands annealing requires Mg(2+).
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O53896
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PEPD_MYCTU
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Serine protease PepD (EC 3.4.21.107) (HtrA-like serine protease)
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MAKLARVVGLVQEEQPSDMTNHPRYSPPPQQPGTPGYAQGQQQTYSQQFDWRYPPSPPPQPTQYRQPYEALGGTRPGLIPGVIPTMTPPPGMVRQRPRAGMLAIGAVTIAVVSAGIGGAAASLVGFNRAPAGPSGGPVAASAAPSIPAANMPPGSVEQVAAKVVPSVVMLETDLGRQSEEGSGIILSAEGLILTNNHVIAAAAKPPLGSPPPKTTVTFSDGRTAPFTVVGADPTSDIAVVRVQGVSGLTPISLGSSSDLRVGQPVLAIGSPLGLEGTVTTGIVSALNRPVSTTGEAGNQNTVLDAIQTDAAINPGNSGGALVNMNAQLVGVNSAIATLGADSADAQSGSIGLGFAIPVDQAKRIADELISTGKASHASLGVQVTNDKDTLGAKIVEVVAGGAAANAGVPKGVVVTKVDDRPINSADALVAAVRSKAPGATVALTFQDPSGGSRTVQVTLGKAEQ
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Required for virulence. Acts both as a protease, which degrades and/or refolds damaged substrate targets, and as a chaperone. Plays an important role in the stress response network mediated through the two-component regulatory system MprAB and SigE signaling networks. May utilize its PDZ domain to recognize and process misfolded proteins at the cell membrane, leading to activation of the MprAB and SigE signaling pathways and subsequent establishment of a positive feedback loop that facilitates bacterial adaptation. Interacts with and potentially cleaves several proteins, including the 35 kDa antigen PspA. Proteolytic cleavage of PspA may help to maintain cell envelope homeostasis in Mycobacterium and regulate specific stress response pathways during periods of extracytoplasmic stress. In vitro, exhibits proteolytic activity against the artificial substrate beta-casein.
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O53901
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PKS5_MYCTU
|
Mycocerosic acid synthase-like polyketide synthase (MAS-like PKS) (EC 2.3.1.-) (Polyketide synthase Pks5)
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MGKERTKTVDRTRVTPVAVIGMGCRLPGGIDSPDRLWEALLRGDDLVTEIPADRWDIDEYYDPEPGVPGRTDCKWGAYLDNVGDFDPEFFGIGEKEAIAIDPQHRLLLETSWEAMEHGGLTPNQMASRTGVFVGLVHTDYILVHADNQTFEGPYGNTGTNACFASGRVAYAMGLQGPAITVDTACSSGLTAIHLACRSLHDGESDIALAGGVYVMLEPRRFASGSALGMLSATGRCHAFDVSADGFVSGEGCVMLALKRLPDALADGDRILAVIRGTAANQDGHTVNIATPSRSAQVAAYREALDVAGVDPATVGMVEAHGPGTPVGDPIEYASLAEVYGNDGPCALASVKTNFGHTQSAAGALGLMKAVLALQHGVVPQNLHFTALPDKLAAIETNLFVPQEITPWPGADQETPRRAAVSSYGMTGTNVHAIVEQAPVPAPESGAPGDTPATPGIDGALLFALSASSQDALRQTAARLADWVDAQGPELAPADLAYTLARRRGHRPVRTAVLAATTAELTEALREVATGEPPYPPAVGQDDRGPVWVFSGQGSQWAGMGADLLATEPVFAATIAAIEPLIAAESGFSVTEAMTAPEVVTGIDRVQPTLFAMQVALAATMKSYGVAPGAVIGHSLGESAAAVVAGALCLEDGVRVICRRSALMTRIAGAGAMASVELPAQQVLSELMARGVNDAVVAVVASPQSTVIGGATQTVRDLVAAWEQRDVLAREVAVDVASHSPQVDPILDELAEALAEISPLQPEIPYYSATSFDPREEPYCDAYYWVDNLRHTVRFAAAVQAALEDGYRVFTELTPHPLLTHAVDQTARSLDMSAAALAGMRREQPLPHGLRALAGDLYAAGAAVDFAVLYPTGRLINAPLPTWNHRRLLLDDTTRRIAHANTVAVHPLLGSHVRLPEEPERHVWQGEVGTVTQPWLADHQIHGAAALPGAAYCEMALAAARAVLGEASEVRDIRFEQMLLLDDETPIGVTATVEAPGVVPLTVETSHDGRYTRQLAAVLHVVREADDAPDQPPQKNIAELLASHPHKVDGAEVRQWLDKRGHRLGPAFAGLVDAYIAEGAGDTVLAEVNLPGPLRSQVKAYGVHPVLLDACFQSVAAHPAVQGMADGGLLLPLGVRRLRSYGSARHARYCCTTVTACGVGVEADLDVLDEHGAVVLAVRGLQLGTGASQASERARVLGERLLSIEWHERELPENSHAEPGAWLLISTCDATDLVAAQLTDALKVHDAQCTTMSWPQRADHAAQAARLRDQLGTGGFTGVFVLTAPQTGDPDAESPVRGGELVKHVVRIAREIPEITAQEPRLYVLTHNAQAVLSGDRPNLEQGGMRGLLRVIGAEHPHLKASYVDVDEQTGAESVARQLLAASGEDETAWRNDQWYTARLCPAPLRPEERQTTVVDHAEAGMRLQIRTPGDLQTLEFAAFDRVPPGPGEIEVAVTASSINFADVLVTFGRYQTLDGRQPQLGTDFAGVVSAVGPGVSELKVGDRVGGMSPNGCWATFVTCDARLATRLPEGLTDAQAAAVTTASATAWYGLQDLARIKAGDKVLIHSATGGVGQAAIAIARAAGAQIYATAGNEKRRDLLRDMGIEHVYDSRSVEFAEQIRRDTAGYGVDIVLNSVTGAAQLAGLKLLALGGRFIEIGKRDIYSNTRLELLPFRRNLAFYGLDLGLMSVSHPAAVRELLSTVYRLTVEGVLPMPQSTHYPLAEAATAIRVMGAAEHTGKLILDVPHAGRSSVVLPPEQARVFRSDGSYIITGGLGGLGLFLAEKMANAGAGRIVLSSRSQPSQKALETIELVRAIGSDVVVECGDIAQPDTADRLVTAATATGLPLRGVLHAAAVVEDATLANITDELIERDWAPKAYGAWQLHRATADQPLDWFCSFSSAAALVGSPGQGAYAAANSWLDTFTHWRRAQDLPATSIAWGAWGQIGRAIAFAEQTGDAIAPEEGAYAFETLLRHNRAYSGYAPVIGSPWLTAFAQHSPFAEKFQSLGQNRSGTSKFLAELVDLPREEWPDRLRRLLSKQVGLILRRTIDTDRLLSEYGLDSLSSQELRARVEAETGIRISATEINTTVRGLADLMCDKLAADRDAPAPA
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Polyketide synthase likely involved in the biosynthesis of a polymethyl-branched fatty acid (PMB-FA) that might only be produced during host infection. Is required for the full virulence of M.tuberculosis during host infection.
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O54003
|
REP75_PYRAB
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Replication initiator protein (Rep75 protein) (EC 2.7.7.31) (EC 3.1.21.-) (EC 6.5.1.1) (ORF1)
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MVIYTSKFKNSLLDGLGVGHLSYDDQPILCNEVHPTLTLDTFISGGSSGSRPRPRWVYLDISTTNEGISEEFSSNTESKSPLLKVCGVSSKSSEGDGSSFIWFDKYRSVISRLEHSGFVEVERTVLKLRKISKELRSINKQLSRLFLDDRERAKLLSRKRKYLDFARALIGSISKSLTLYADRFFVEVPQDYAKLIQKLGFSSDTLLLHLFVNSGVLEVFLDDNSSHKFRIAYISKVHAGKYHPVKGISKGSQEAKRVLRDLLVLSELLEGSLVSYRSGGVETIHHLIPVRHFVLTAPKELSFSIWASLKKGDSSLFRAFKDAGAKAIKEFLSYLASKEHISGNLLFGFTINVHVTGDKNPFEPHFHIDAIVTFICYDKSSTKWFRLNPLLSESDLKKLRDIWKNVLLSYFGELLSEDTKSKDFDVWAGDNYYSLPLDVPQVFFELKYASRKLFVNFVNYFEQSNFDESSVSDWDFVRFVFEYSNRTERYGFLTNIKRYLSMSCSHLVEKRVQELEEFISRIEFDLSVNGNKMSDSLKRALLERLEYLKDELSELKERGFEYLFERALEKAEELLSNDNLTLERVIHILETLFTALGKSIVNYNFYVELEDVSFREFVDYLYDNHLSDVLVFSDRHRSITIIRLIPPPDGGVPV
|
Required for rolling circle plasmid replication, has a site-specific endonuclease/ligase activity (nicking and closing). In vitro (no in vivo system yet exists) cleaves the double-stranded origin of replication (dso) site, on an ssDNA template, remaining covalently linked to the 5' end. Religates the appropriate substrates. Has nucleotidyltransferase activity, adding ATP or dATP to the 3' end of the nicked ssDNA site. Both activities require a G nucleotide at the 3' end of the nicking site. Also has topoisomerase activity, nicking and relaxing negatively supercoiled plasmids in a narrow concentration range (25-50 molar ratio of protein:DNA). Topoisomerase is not dependent on a dso sequence. Has no topoisomerase activity on slightly positively supercoiled plasmid.
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O54259
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SNOAB_STRNO
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Deoxynogalonate monooxygenase (EC 1.13.12.22) (12-deoxy-nogalonic acid oxygenase) (Cofactor-independent monooxygenase SnoaB)
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MPTRVNDGVDADEVTFVNRFTVHGGPAEFESVFARTAAFFARQPGFVRHTLLRERDKDNSYVNIAVWTDHDAFRRALAQPGFLPHATALRALSTSEHGLFTARQTLPEGGDTTGSGHR
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Involved in the biosynthesis of the anthracycline (aromatic polyketide) antibiotic nogalamycin. Catalyzes the oxygenation of 12-deoxy-nogalonic acid at position 12 to yield nogalonic acid.
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O54288
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KDGA_SACSO
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2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase (EC 4.1.2.55)
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MPEIITPIITPFTKDNRIDKEKLKIHAENLIRKGIDKLFVNGTTGLGPSLSPEEKLENLKAVYDVTNKIIFQVGGLNLDDAIRLAKLSKDFDIVGIASYAPYYYPRMSEKHLVKYFKTLCEVSPHPVYLYNYPTATGKDIDAKVAKEIGCFTGVKDTIENIIHTLDYKRLNPNMLVYSGSDMLIATVASTGLDGNVAAGSNYLPEVTVTIKKLAMERKIDEALKLQFLHDEVIEASRIFGSLSSNYVLTKYFQGYDLGYPRPPIFPLDDEEERQLIKKVEGIRAKLVELKILKE
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Involved in the degradation of glucose and galactose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal). It is equally active with both D- and L-glyceraldehyde.
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O54329
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LANA_STRMG
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Lantibiotic mutacin-2 (Lantibiotic mutacin H-29B) (Mutacin II)
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MNKLNSNAVVSLNEVSDSELDTILGGNRWWQGVVPTVSYECRMNSWQHVFTCC
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Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria including M.luteus, S.aureus, Streptococcus, P.micros, P.acidilactici, C.sporogenes, C.diphtheriae, A.viscosus, G.vaginalis, P.acnes, L.monocytogenes and M.smegmatis, and Gram-negative bacteria including C.jejuni, H.pylori and N.gonorrhoeae. Transiently and partially depolarizes the transmembrane electrical potential and pH gradient of susceptible cells, inhibits the uptake of amino acids and depletes the intracellular ATP pool.
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O54408
|
RELA_BACSU
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GTP pyrophosphokinase (EC 2.7.6.5) ((p)ppGpp synthase) (ATP:GTP 3'-pyrophosphotransferase) (ppGpp synthase I)
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MANEQVLTAEQVIDKARSYLSDEHIAFVEKAYLYAEDAHREQYRKSGEPYIIHPIQVAGILVDLEMDPSTIAGGFLHDVVEDTDVTLDDLKEAFSEEVAMLVDGVTKLGKIKYKSQEEQQAENHRKMFVAMAQDIRVILIKLADRLHNMRTLKHLPQEKQRRISNETLEIFAPLAHRLGISKIKWELEDTALRYLNPQQYYRIVNLMKKKRAERELYVDEVVNEVKKRVEEVNIKADFSGRPKHIYSIYRKMVLQNKQFNEIYDLLAVRILVNSIKDCYAVLGIIHTCWKPMPGRFKDYIAMPKPNMYQSLHTTVIGPKGDPLEVQIRTFEMHEIAEYGVAAHWAYKEGKAANEGATFEKKLSWFREILEFQNESTDAEEFMESLKIDLFSDMVYVFTPKGDVIELPSGSVPIDFSYRIHSEIGNKTIGAKVNGKMVTLDHKLRTGDIVEILTSKHSYGPSQDWVKLAQTSQAKHKIRQFFKKQRREENVEKGRELVEKEIKNLDFELKDVLTPENIQKVADKFNFSNEEDMYAAVGYNGITALQVANRLTEKERKQRDQEEQEKIVQEVTGEPKPYPQGRKREAGVRVKGIDNLLVRLSKCCNPVPGDDIVGFITKGRGVSVHREDCPNVKTNEAQERLIPVEWEHESQVQKRKEYNVEIEILGYDRRGLLNEVLQAVNETKTNISSVSGKSDRNKVATIHMAIFIQNINHLHKVVERIKQIRDIYSVRRVMN
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In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp, it is probably the hydrolysis activity that is required for optimal growth (Probable). {ECO:0000250, ECO:0000305|PubMed:18067544}.
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O54689
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CCR6_MOUSE
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C-C chemokine receptor type 6 (C-C CKR-6) (CC-CKR-6) (CCR-6) (KY411) (CD antigen CD196)
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MNSTESYFGTDDYDNTEYYSIPPDHGPCSLEEVRNFTKVFVPIAYSLICVFGLLGNIMVVMTFAFYKKARSMTDVYLLNMAITDILFVLTLPFWAVTHATNTWVFSDALCKLMKGTYAVNFNCGMLLLACISMDRYIAIVQATKSFRVRSRTLTHSKVICVAVWFISIIISSPTFIFNKKYELQDRDVCEPRYRSVSEPITWKLLGMGLELFFGFFTPLLFMVFCYLFIIKTLVQAQNSKRHRAIRVVIAVVLVFLACQIPHNMVLLVTAVNTGKVGRSCSTEKVLAYTRNVAEVLAFLHCCLNPVLYAFIGQKFRNYFMKIMKDVWCMRRKNKMPGFLCARVYSESYISRQTSETVENDNASSFTM
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Receptor for the C-C type chemokine CCL20. Binds to CCL20 and subsequently transduces a signal by increasing the intracellular calcium ion levels. Although CCL20 is its major ligand it can also act as a receptor for non-chemokine ligands such as beta-defensins. Binds to defensin DEFB1 leading to increase in intracellular calcium ions and cAMP levels. Its binding to DEFB1 is essential for the function of DEFB1 in regulating sperm motility and bactericidal activity (By similarity). Binds to defensins DEFB4 and DEFB4A/B and mediates their chemotactic effects. The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/memory T-cells and B-cells and plays an important role at skin and mucosal surfaces under homeostatic and inflammatory conditions, as well as in pathology, including cancer and various autoimmune diseases. CCR6-mediated signals are essential for immune responses to microbes in the intestinal mucosa and in the modulation of inflammatory responses initiated by tissue insult and trauma. CCR6 is essential for the recruitment of both the pro-inflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation. Required for the normal migration of Th17 cells in Peyers patches and other related tissue sites of the intestine and plays a role in regulating effector T-cell balance and distribution in inflamed intestine. Plays an important role in the coordination of early thymocyte precursor migration events important for normal subsequent thymocyte precursor development, but is not required for the formation of normal thymic natural regulatory T-cells (nTregs). Required for optimal differentiation of DN2 and DN3 thymocyte precursors. Essential for B-cell localization in the subepithelial dome of Peyers-patches and for efficient B-cell isotype switching to IgA in the Peyers-patches. Essential for appropriate anatomical distribution of memory B-cells in the spleen and for the secondary recall response of memory B-cells. Positively regulates sperm motility and chemotaxis via its binding to CCL20.
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O54692
|
ZW10_MOUSE
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Centromere/kinetochore protein zw10 homolog
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MASFVTEVLAHSGSLEKEDLGTRISRLTRRVEEIKGEVCNMISKKYSEFLPTMQSAQALVTQVDTLSNDIDQLKSRIETEVCRDLHISTVEFTNLKQQLERDSVVLTLLKQLQEFSSAIEEYNSALAEKKYIPAARHLEEAQECLKLLKSRKCFDLKMLKSLSMELTVQKQNILYHLGEDWQKLVVWKFPPAKDTSSLESCLQTELHLCTEQPEKEDMTPLPSISSVLLAFSILGELPTKLKSFGQMLLKYILKPLVTCPSLHAVIERQPSSVSICFESLTTDLEHPSPPEAFAKIRLVLEVLQKQLLDLPLDADLEIGKVPGIVLAEMLGEGIWEDLSECLIRNCLVYSIPTNSSKLQEYEEIIQSTEEFEKFLKEMRFLKGDTTDLLKYARNINSHFANKKCQDVIVAARNLMTSEIHNTVKIGPDCKEALPDLPSPDADHKLQVQTVCKAQFTDAGNLEPETSLDPQSFSLPTCRISEAVKKLMELAYQTLLEATTSSDQCAVQLFYSVRNIFHLFHDVVPTYHKENLRKLPQLAAIHHNNCMYIAHHLLTLGHQFRLRLAPILCDGTTTFVDLVPGFRRLGTECFLAQMQAQKGELLERLSSARSFANMDDEENYSAASKAVRQVLHQLRRLGIVWQDVLPVNIYCKAMGTLLNTAIAEMMSRITALEDISTEDGDRLYSLCKTVMDEGPQVFAPLSDENKNKKYQEEVPVYVSKWMPFKELMIMLQASLQEIGDRWADGKGPLATAFPSSEVKALIRALFQNTERRAAALAKIK
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Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex. Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER) the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER (By similarity).
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O54693
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EDA_MOUSE
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Ectodysplasin-A (EDA protein homolog) (Tabby protein) [Cleaved into: Ectodysplasin-A, membrane form; Ectodysplasin-A, secreted form]
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MGYPEVERREPLPAAAPRERGSQGCGCRGAPARAGEGNSCRLFLGFFGLSLALHLLTLCCYLELRSELRRERGTESRLGGPGAPGTSGTLSSPGSLDPVGPITRHLGQPSFQQQPLEPGEDPLPPDSQDRHQMALLNFFFPDEKAYSEEESRRVRRNKRSKSGEGADGPVKNKKKGKKAGPPGPNGPPGPPGPPGPQGPPGIPGIPGIPGTTVMGPPGPPGPPGPQGPPGLQGPSGAADKTGTRENQPAVVHLQGQGSAIQVKNDLSGGVLNDWSRITMNPKVFKLHPRSGELEVLVDGTYFIYSQVEVYYINFTDFASYEVVVDEKPFLQCTRSIETGKTNYNTCYTAGVCLLKARQKIAVKMVHADISINMSKHTTFFGAIRLGEAPAS
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Cytokine which is involved in epithelial-mesenchymal signaling during morphogenesis of ectodermal organs. Functions as a ligand activating the DEATH-domain containing receptors EDAR and EDA2R. Isoform TAA binds only to the receptor EDAR, while isoform TA-A2 binds exclusively to the receptor EDA2R (By similarity). May also play a role in cell adhesion. Isoform TAA binds only to the receptor EDAR, while isoform TA-A2 binds exclusively to the receptor EDA2R.
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O54695
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SPTC1_CRIGR
|
Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1)
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MAMAAEQWVLVEMVQALYEAPAYHLILEGILILWIIRLVFSKTYKLQERSDLTAKEKEELIEEWQPEPLVPPVSKNHPALNYNIVSGPPTHNIVVNGKECVNFASFNFLGLLANPRVKAAALASLKKYGVGTCGPRGFYGTFDVHLDLEERLAKFMRTEEAIIYSYGFSTIASAIPAYSKRGDIVFVDSAACFAIQKGLQASRSDIKLFKHNDVADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTVCPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGISIDDIDLISANMENALASVGGFCCGRSFVVDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENPGIFAVLKKKCQHIHKSLQGISGLKVVGESLSPALHLQLEESTGSREKDVQLLQEMVIHCMNEGIALTQARYLDKEEKCLPPPSIRVVVTVEQTEEELERAASTIREAAQAVLL
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Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (By similarity). Required for adipocyte cell viability and metabolic homeostasis (By similarity).
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O54697
|
NALDL_RAT
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Aminopeptidase NAALADL1 (EC 3.4.11.-) (100 kDa ileum brush border membrane protein) (I100) (Ileal dipeptidylpeptidase) (N-acetylated-alpha-linked acidic dipeptidase-like protein) (NAALADase L)
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MHWAKILGVGIGAAALLGLGIILGHFAIPKATEPLASSVSDSQDLDLAILDSVMGQLDASRIRENLRELSKEPHVATSARDEALVQLLLGRWKDSASGLDTAKTYEYTVLLSFPSTEQPNSVEVVGPNGTVFHSFQPFEKNLTGEQAEPNVLQPYAAYAPPGTPKGPLVYANRGSEDDFKKLEAEGINLKGTIALTRYGSVGRGAKAINAARHGVVGVLVYTDPGDINDGKSLPNETFPNSWGLPPSGVERGSYYEYFGDPLTPYLPAHPVSFRLDPHNISGFPPIPTQPIGFEDAKNLLCNLNGTSAPDSWQGALGCEYKLGPGFEPNGNFPAGSEVKVSVYNRLELRNSSNVLGIIQGAVEPDRYVIYGNHRDSWVHGAVDPSSGTAVLLEISRVLGTLLKKGTWRPRRSIIFASWGAEEFGLIGSTEFTEEFLSKLQERTVTYINVDISVFSNATLRAQGTPPVQSVIFSATKEISAPGSSGLSIYDNWIRYTNRSSPVYGLVPSMGTLGAGSDYASFIHFLGITSMDLAYTYDRSKTSARIYPTYHTAFDTFDYVEKFLDPGFSSHQAVARTAGSVLLRLSDSLFLPLNVSDYSETLQSFLQAAQENLGALLESHNISLGPLVTAVEKFKAAAAALNQHILTLQKSSPDPLQVRMVNDQLMLLERAFLNPRAFPEERYYSHVLWAPNTASVATFPGLANAYARAQEINSGAEAWAEVERQLSIAVMALEGAAATLQPVTDL
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Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position. Lacks carboxypeptidase activity. Lacks dipeptidyl-peptidase IV type activity.
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O54698
|
S29A1_RAT
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Equilibrative nucleoside transporter 1 (rENT1) (Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter) (Equilibrative NBMPR-sensitive nucleoside transporter) (Nucleoside transporter, es-type) (Solute carrier family 29 member 1)
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MTTSHQPQDRYKAVWLIFFVLGLGTLLPWNFFITATQYFTSRLNTSQNISLVTNQSCESTEALADPSVSLPARSSLSAIFNNVMTLCAMLPLLIFTCLNSFLHQKVSQSLRILGSLLAILLVFLVTATLVKVQMDALSFFIITMIKIVLINSFGAILQASLFGLAGVLPANYTAPIMSGQGLAGFFTSVAMICAVASGSKLSESAFGYFITACAVVILAILCYLALPWMEFYRHYLQLNLAGPAEQETKLDLISEGEEPRGGREESGVPGPNSLPANRNQSIKAILKSIWVLALSVCFIFTVTIGLFPAVTAEVESSIAGTSPWKNCYFIPVACFLNFNVFDWLGRSLTAICMWPGQDSRWLPVLVACRVVFIPLLMLCNVKQHHYLPSLFKHDVWFITFMAAFAFSNGYLASLCMCFGPKKVKPAEAETAGNIMSFFLCLGLALGAVLSFLLRALV
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Uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis. Functions as a Na(+)-independent transporter (By similarity). Involved in the transport of nucleosides such as adenosine, thymidine and uridine. Also transports purine nucleobases (hypoxanthine, adenine, guanine) and pyrimidine nucleobases (thymine, uracil) (By similarity). Mediates basolateral nucleoside uptake into Sertoli cells, thereby regulating the transport of nucleosides in testis across the blood-testis-barrier. Regulates inosine levels in brown adipocytes tissues (BAT) and extracellular inosine levels, which controls BAT-dependent energy expenditure (By similarity).
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O54699
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S29A2_RAT
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Equilibrative nucleoside transporter 2 (rENT2) (Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter) (Equilibrative NBMPR-insensitive nucleoside transporter) (Nucleoside transporter, ei-type) (Solute carrier family 29 member 2)
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MAHGNAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQGRLAGTNSSAETPSTNHTSPTDTFNFNNWVTLLSQLPLLLFTLLNSFLYQCIPESVRILGSLLAILLLFALTAALVKVDLSPGLFFSITMASVWFINSFCAVLQGSLFGQLGTMPSTYSTLFLSGQGLAGIFAALAMLTSLASGVDPQTSALGYFITPCVGILLSIICYLSLPHLKFARYYLTKKPQAPVQELETKAELLGADEKNGIPVSPQQAGPTLDLDPEKELELGLEEPQKPGKPSVFVVFRKIWLTALCLVLVFTVTLSVFPAITAMVTTSSNSPGKWSQFFNPICCFLLFNVMDWLGRSLTSYFLWPDEDSQLLPLLVCLRFLFVPLFMLCHVPQRARLPIIFWQDAYFITFMLLFAISNGYFVSLTMCLAPRQVLPHEREVAGALMTFFLALGLSCGASLSFLFKALL
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Bidirectional uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis. Functions as a Na(+)-independent, passive transporter (By similarity). Involved in the transport of nucleosides such as inosine, adenosine, uridine, thymidine, cytidine and guanosine. Also able to transport purine nucleobases (hypoxanthine, adenine, guanine) and pyrimidine nucleobases (thymine, uracil). Involved in nucleoside transport at basolateral membrane of kidney cells, allowing liver absorption of nucleoside metabolites (By similarity). Mediates apical nucleoside uptake into Sertoli cells, thereby regulating the transport of nucleosides in testis across the blood-testis-barrier. Mediates both the influx and efflux of hypoxanthine in skeletal muscle microvascular endothelial cells to control the amount of intracellular hypoxanthine available for xanthine oxidase-mediated ROS production.
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O54701
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NCKX2_RAT
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Sodium/potassium/calcium exchanger 2 (Na(+)/K(+)/Ca(2+)-exchange protein 2) (Retinal cone Na-Ca+K exchanger) (Solute carrier family 24 member 2)
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MDLHQSATVRLLQEWCSHESPSGCRRHYNTRKKLKLIRVIGLVMGLVAVSTVPFSISAFTETYSQNNRGEASDVTGPRAAPGHRQRTLLDLNDKIRDYTPQPPASQEDRSENGTDHAQGDYPKDVFSLEERRKGAIILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLGISDDVAGATFMAAGGSAPELFTSLIGVFIAHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLIMLIIFFLDNVIMWWESLLLLTAYFAYVVFMKFNVQVERWVKQMINRNKVVKVTVSEAQAKASTAGDKEEPTLPNKPRLQRGGSSASLHNSLMRNSIFQLMIHTLDPLAEELGSYGKLKYYDTMTEEGRFREKASILHKIAKKKCQVDENERQNGAANHVDYAAEKIELPNSTSTEVEMTPSSEASEPVQNGNLSHSIEAADAPQATETAEEDDDQPLSLSWPSNTRKQITFLIVLPIVFPLWITLPDVRKPASKKFFPITFFGSITWIAVFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPLPWLLYTIIHRFKPVTVSSNGLFCAIVLLFIMLIFVILSIALCKWRMNKILGFIMFGLYFAFLVVSVLLEDKVLECPVSI
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Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). Required for learming and memory by regulating neuronal Ca(2+), which is essential for the development of synaptic plasticity (By similarity).
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O54702
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CHSTA_RAT
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Carbohydrate sulfotransferase 10 (EC 2.8.2.-) (HNK-1 sulfotransferase) (HNK-1ST) (HNK1ST) (RaHNK-1ST) (Sul-T)
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MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDGYSAKQEFVFLTAMPEAEKLRGEKHFSEVMKPTGKMLSESHPDQPPVYLERLELIRNACKEEALRNLSHTEVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSKIGIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRKNRTETRGIQFEDFVRYLGDPNRRWLDLQFGDHIIHWVTYVKLCAPCEIKYSVIGHHETLEADAPYILKEAGIDHLVSYPTIPPGITMYNRTKVEQYFLGISKRDIRRLYARFEGDFKLFGYQKPDFLLN
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Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-(1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis. Sulfates terminal glucuronyl residue of the laminin globular (LG)-domain binding epitope on DAG1/alpha-dystroglycan and prevents further polymerization by LARGE1 glycosyltransferase. Likely defines the chain length of LG epitope, confering binding specificity to extracellular matrix components. Plays a role in down-regulating the steroid hormones. Sulfates glucuronidated estrogens and androgens with an impact in hormone cycle and fertility. Has a preference for glucuronyl moiety at the 3-hydroxyl group of a sterol ring rather than the 17-hydroxyl group, showing high catalytic efficiency for 17beta-estradiol 3-O-(beta-D-glucuronate) and dehydroepiandrosterone 3-O-(beta-D-glucuronate) hormones (By similarity).
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O54705
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NOS2_CAVPO
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Nitric oxide synthase, inducible (EC 1.14.13.39) (Inducible NO synthase) (Inducible NOS) (iNOS) (NOS type II) (Peptidyl-cysteine S-nitrosylase NOS2)
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MACPWNFLWKLKSSRYDLTEEKDINNNVGKASHLYSPEIQDDPKYCSPGKHQNGSSQSLTGTAKKVPESQSKPHKPSPTCSQHMKIKNWGNGMILQDTLHTKAKTNFTCKPKSCLGSVMNPRSMTRGPRDTPIPPDELLPQAIEFVNQYYDSFKEAKIEEYLARVETVTKEIETTGTYQLTGDELIFATKLAWRNAPRCIGRIQWSNLQVFDARSCHTAQEMFEHICRHVRYSTNNGNIRSAITVFPQRTDGKHDFRVWNAQLIRYAGYQMPDGTIQGDPANLEFTQLCIDLGWKPRYGRFDVLPLILQADGRDPELFEIPPDLVLEVPMEHPKYEWFQDLGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDAQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHHSAAESFMKHMQNEYRARGGCPADWIWLVPPISGSITPVFHQEMLNYILSPFYYYQVEAWKTHVWQDETRRPKRREIPFRVLAKATLFASLLMRKMMASRVRATILFATETGKSEALAQDLGALFSCAFNPKVLCMDQYQLSSLEEEKLLLVVTSTFGNGDCPGNGETLKKSLFVLKKLTNTFRYAVFGLGSSMYPRFCAFAHDIDIKLSQLGASQLTPVGEGDELSGQEDAFCTWAVQTFQAACAAFDVRGRHHITIPKRYTSSVTWEPYHYRLVQDSQPLDLNKALSRMHATDVFTMRLKSQKNLQSPKSSRTTLLMELSCDDSRSLAYLPGEHLGVFPCNQPALVQGILECVVDNPGPHHTVCLEVLDDSGSYWAKDKRLPPCSLSQALTYFLDITTPPTQLQLQKLARLATEQAERLRLESLSQPSEYNKWKFTNSPTFLEVLEEFPSLRVPAAFLLSQLPILKPRYYSISSSLDHTPAEVHLTVAVVTYRTRDGRGPLHHGVCSTWFSGLKPQDPVPCLVRSVNSFQLPKDPSQPCILIGPGTGIAPFRSFWQQRLHNLKHTGLQGGRMTLLFGCRHPEEDHIYKEEMQEMVQKGVLHEVHTAYSRLPGKPKAYVQDILRQQLAREVLRVLHEEPGHLYVCGNVLMAQDVACTLKQLLAAKLNLNEEQVEDYFFQLKSQKRYHEDIFGAVFPHGVKKDRAERPPGDDKL
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Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8.
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O54707
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KLRD1_MOUSE
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Natural killer cells antigen CD94 (Killer cell lectin-like receptor subfamily D member 1) (CD antigen CD94)
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MAVSRITRWRLMSVIFGIKCLFLMVTLGVLLINSFTIQNIQSTPSPTTTVEFQEVSECCVCLDKWVGHQCNCYFISKEEKSWKRSRDFCASQNSSLLQPQSRNELSFMNFSQTFFWIGMHYSEKRNAWLWEDGTVPSKDLFPEFSVIRPEHCIVYSPSKSVSAESCENKNRYICKKLPI
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Immune receptor involved in self-nonself discrimination. In complex with KLRC1 or KLRC2 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule MHC-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia and non-classical MHC class Ib molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self. Primarily functions as a ligand binding subunit as it lacks the capacity to signal. KLRD1-KLRC1 acts as an immune inhibitory receptor. Key inhibitory receptor on natural killer (NK) cells that regulates their activation and effector functions. Dominantly counteracts T cell receptor signaling on a subset of memory/effector CD8-positive T cells as part of an antigen-driven response to avoid autoimmunity. On intraepithelial CD8-positive gamma-delta regulatory T cells triggers TGFB1 secretion, which in turn limits the cytotoxic programming of intraepithelial CD8-positive alpha-beta T cells, distinguishing harmless from pathogenic antigens. In MHC-E-rich tumor microenvironment, acts as an immune inhibitory checkpoint and may contribute to progressive loss of effector functions of NK cells and tumor-specific T cells, a state known as cell exhaustion. Upon MHC-E-peptide binding, transmits intracellular signals through KLRC1 immunoreceptor tyrosine-based inhibition motifs (ITIMs) by recruiting INPP5D/SHIP-1 and INPPL1/SHIP-2 tyrosine phosphatases to ITIMs, and ultimately opposing signals transmitted by activating receptors through dephosphorylation of proximal signaling molecules. KLRD1-KLRC2 acts as an immune activating receptor. On cytotoxic lymphocyte subsets recognizes MHC-E loaded with signal sequence-derived peptides from non-classical MHC class Ib MHC-G molecules, likely playing a role in the generation and effector functions of adaptive NK cells and in maternal-fetal tolerance during pregnancy. Regulates the effector functions of terminally differentiated cytotoxic lymphocyte subsets, and in particular may play a role in adaptive NK cell response to viral infection. Upon MHC-E-peptide binding, transmits intracellular signals via the adapter protein TYROBP/DAP12, triggering the phosphorylation of proximal signaling molecules and cell activation.
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O54709
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NKG2D_MOUSE
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NKG2-D type II integral membrane protein (Killer cell lectin-like receptor subfamily K member 1) (NK cell receptor D) (NKG2-D-activating NK receptor) (CD antigen CD314)
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MALIRDRKSHHSEMSKCHNYDLKPAKWDTSQEQQKQRLALTTSQPGENGIIRGRYPIEKLKISPMFVVRVLAIALAIRFTLNTLMWLAIFKETFQPVLCNKEVPVSSREGYCGPCPNNWICHRNNCYQFFNEEKTWNQSQASCLSQNSSLLKIYSKEEQDFLKLVKSYHWMGLVQIPANGSWQWEDGSSLSYNQLTLVEIPKGSCAVYGSSFKAYTEDCANLNTYICMKRAV
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Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including RAET1A, RAET1B, RAET1C, RAET1D, RAET1E, H60 and MULT1.
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O54714
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PIAS3_MOUSE
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E3 SUMO-protein ligase PIAS3 (EC 2.3.2.-) (E3 SUMO-protein transferase PIAS3) (Protein inhibitor of activated STAT protein 3)
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MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPGPLAPIPPTLLTPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQLQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTSLRVSLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAPYESLIIDGLFMEILNSCSDCDEIQFMEDGSWCPMKPKKEASEVCPPPGYGLDGLQYSAVQEGIQPESKKRVEVIDLTIESSSDEEDLPPTKKHCPVTSAAIPALPGSKGALTSGHQPSSVLRSPAMGTLGSDFLSSLPLHEYPPAFPLGADIQGLDLFSFLQTESQHYGPSVITSLDEQDTLGHFFQYRGTPSHFLGPLAPTLGSSHRSSTPAPPPGRVSSIVAPGSSLREGHGGPLPSGPSLTGCRSDVISLD
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Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pathway. Repressor of STAT3 signaling via inhibiting STAT3 DNA-binding and suppressing cell growth. Repressor of MITF transcriptional activity. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1 (By similarity). Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus (By similarity).
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O54715
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VAS1_RAT
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V-type proton ATPase subunit S1 (V-ATPase subunit S1) (C7-1 protein) (V-ATPase Ac45 subunit) (V-ATPase S1 accessory protein) (Vacuolar proton pump subunit S1)
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MMAATVVSRIRTGTRWAPVLWLLLSLVAVAAAVAAEQQVPLVLWSSDRDLWAPVADTHEGHITSDMQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAISTLTTYLQEKLGASPLHVDLATLKELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLESEDVPYTAALTAVRPSRVARDVAMVAGGLGRQLLQTQVASPAIHPPVSYNDTAPRILFWAQNFSVAYKDEWKDLTSLTFGVENLNLTGSFWNDSFAMLSLTYEPLFGATVTFKFILASRFYPVSARYWFTMERLEIHSNGSVAHFNVSQVTGPSIYSFHCEYVSSLSKKGSLLVTNVPSLWQMTLHNFQIQAFNVTGEQFSYASDCAGFFSPGIWMGLLTTLFMLFIFTYGLHMILSLKTMDRFDDRKGPTITLTQIV
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Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles. Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity. Involved in membrane trafficking and Ca(2+)-dependent membrane fusion. May play a role in the assembly of the V-type ATPase complex. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). In islets of Langerhans cells, may regulate the acidification of dense-core secretory granules (By similarity).
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O54724
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CAVN1_MOUSE
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Caveolae-associated protein 1 (Cav-p60) (Cavin-1) (Polymerase I and transcript release factor)
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MEDVTLHIVERPYSGFPDASSEGPEPTQGEARATEEPSGTGSDELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSVSKSLKESEALPEKEGDELGEGERPEDDTAAIELSSDEAVEVEEVIEESRAERIKRSGLRRVDDFKKAFSKEKMEKTKVRTRENLEKTRLKTKENLEKTRHTLEKRMNKLGTRLVPVERREKLKTSRDKLRKSFTPDHVVYARSKTAVYKVPPFTFHVKKIREGEVEVLKATEMVEVGPEDDEVGAERGEATDLLRGSSPDVHTLLEITEESDAVLVDKSDSD
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Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues. Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template. The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A.
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O54728
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PLB1_RAT
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Phospholipase B1, membrane-associated (Phospholipase B) (Lysophospholipase) (EC 3.1.1.5) (Phospholipase A2) (EC 3.1.1.4) (Phospholipase B/lipase) (PLB/LIP) (Triacylglycerol lipase) (EC 3.1.1.3)
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MESWPGVSLVGLLLLLLLGQGPSQIHGSSGENTSQPQQVFRTLKNFSFPCKPKKLELSVLSKSVHSLRPSDIKLVAAIGNLETPPAPGSGVVNMEKPQSLESELQNVCIGIMTALSDIIRHFNPSVLMPTCSPGKGTAGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRHLMKHMEMLSGVLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGFSPAPEICKCSEEITKLSKAVMQWSYQEAWEDLLASSKFNKHETFAVVFQSFFSEVELPLERPSPQDSTTLALRIWNSMMEPVGRKDGTLNEAERKTMKCPSQESPYLFTYRNSNYQARQLKPIGKFQMKEGTKFTCPDKDPSDSIPTTVHRLRPADIKVIGAMGDSLTAGNGAGSSPGNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKENTPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKVSCPRMILRSLCPCVLNLGENSAELAQLVERNRQYQEETGKLIESGRYDTRDDFTVVLQPMFENVVMPRTLEGLPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVGRKTRHQNFEIKVPIMCPNQTSPFLSTTKNSNLGHGTSMSCEEKAPSASPPTSVHTLRPADIQVVAALGDSVTAGNGISSQEGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDVNSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDILHKEVPRALVNLVDFMNPSIIRQVFLKNPDKCPVNQTSVLCNCVLTPGEDSHELARLEAFTKSYQSSMLQLVESGRYDTREDFSVVLQPFLFNIRLPILENGNPDTSFFAPDCILLSQKFHTQLARALWANMLEPLGKKMDTLDPKELIALACPTKDKPFLRTFRNSNYTYPIKPAIENWGSDFLCTEQSPSSKVPTSVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENTAGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYEELPRVFINVVEVMELSGLLHDQGGKCAMPLAVQKNCSCLKRSQNLMAMQELKKVNGNLQSALSELSYWHRYMQREDFAVTVQPFFRNTFVPLDERGGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVGKKTTSNNFTYNRTKLKCPSPENPFLYTVRNSQILLDKAKENSNTLYWAVPVAAVGGLVVGILGMMLWRTVRLVQ
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Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (By similarity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates. Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity. May also hydrolyze long chain retinyl esters such as retinyl palmitate (By similarity). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (Probable).
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O54732
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MMP15_MOUSE
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Matrix metalloproteinase-15 (MMP-15) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 2) (MT-MMP 2) (MTMMP2) (Membrane-type-2 matrix metalloproteinase) (MT2-MMP) (MT2MMP)
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MGSDRSALGRPGCTGSCLSSRASLLPLLLVLLDCLGHGTASKDAEVYAAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQSFYGIPVTGVLDEETKTWMKRPRCGVPDQFGVHVKANLRRRRKRYTLTGKAWNNYHLTFSIQNYTEKLGWYNSMEAVRRAFQVWEQVTPLVFQEVSYDDIRLRRRAEADIMVLFASGFHGDSSPFDGVGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGISLFLVAVHELGHALGLEHSSNPSAIMAPFYQWMDTDNFQLPEDDLRGIQQLYGSPDGKPQPTRPLPTVRPRRPGRPDHQPPRPPQPPHPGGKPERPPKPGPPPQPRATERPDQYGPNICDGNFDTVAVLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGNISAAYERQDGHFVFFKGNRYWLFREANLEPGYPQPLSSYGTDIPYDRIDTAIWWEPTGHTFFFQADRYWRFNEETQHGDPGYPKPISVWQGIPTSPKGAFLSNDAAYTYFYKGTKYWKFNNERLRMEPGHPKSILRDFMGCQEHVEPRSRWPDVARPPFNPNGGAEPEADGDSKEENAGDKDEGSRVVVQMEEVVRTVNVVMVLVPLLLLLCILGLAFALVQMQRKGAPRMLLYCKRSLQEWV
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Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.
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O54735
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PDE5A_RAT
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cGMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.35) (cGMP-binding cGMP-specific phosphodiesterase) (CGB-PDE)
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MLPFGDKTRDMVNAWFSERVHNIPVCKEGIRAHTESCSCSLPQSPHADNTTPGAPARKISASEFDRPLRPIVVKDSEGTVSFLSDSGKKEQMPLTSPRFDSDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSKDKFLVSRLFDVAEGSTLEEASNNCIRLEWNKGIVGHVAAFGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCPDSFSRVFQMEWEEVGKSSEPLTREHDANKINYMYAQYVKNTMEPLNIPDVTKDNRFPWTNENMGHINTHCIRSLLCTPIKNGKKNKVIGVCQLVNKMEEKTGKIKAFNQNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQALAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLETLALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSTMEHHHFDQCLMVLNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNEFSFEDPLQKELFLAMLMTACDLSAITKPWPIQQRIAELVAAEFFDQGDRERKELNMEPADLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCLPLLDGCRKNRQKWQALADQQEKTLLNGESGQAKRD
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Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP.
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O54743
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FOXF2_MOUSE
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Forkhead box protein F2 (Protein LUN)
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MSTEGGPPPPPPRPPPAPLRRACSPAPGALQAALMSPPPAATLESTSSSSSSSSASCASSSSNSVSASAGACKSAASSGGAGAGSGGTKKATSGLRRPEKPPYSYIALIVMAIQSSPSKRLTLSEIYQFLQARFPFFRGAYQGWKNSVRHNLSLNECFIKLPKGLGRPGKGHYWTIDPASEFMFEEGSFRRRPRGFRRKCQALKPMYHRVVSGLGFGASLLPQGFDFQAPPSAPLGCHGQGGYGGLDMMPAGYDTGAGAPGHAHPHHLHHHHVPHMSPNPGSTYMASCPVPAGPAGVGAAAGGGGGGGDYGPDSSSSPVPSSPAMASAIECHSPYTSPAAHWSSPGASPYLKQPPALTPSSNPAASAGLHPSMSSYSLEQSYLHQNAREDLSVGLPRYQHHSTPVCDRKDFVLNFNGISSFHPSASGSYYHHHHQSVCQDIKPCVM
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Probable transcription activator for a number of lung-specific genes. Mediates up-regulation of the E3 ligase IRF2BPL and drives ubiquitination and degradation of CTNNB1 (By similarity).
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O54747
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DPOD1_RAT
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DNA polymerase delta catalytic subunit (EC 2.7.7.7) (3'-5' exodeoxyribonuclease) (EC 3.1.11.-)
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MDGKRRQAPSSGVPPKRACKGLWDEDEPSQFEENLALLEEIEAENRLQEAEEELQLPPEGIVGGQFSTADIDPRWLRPTPLALDPSTEPLIFQQLEIDHYVGTSPPLPEGPPASRNSVPILRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGAEHLSELQRELNAAISRDQRGGKELSGPAVLAIELCSRESMFGYHGHGPSPFLRITLALPRLMAPARRLLEQGIRVPGLGTPSFAPYEANVDFEIRFMVDADIVGCNWLELPAGKYVRRAEKKATLCQLEVDVLWSDVISHPPEGQWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPCAPILGAKVQSYEREEDLLQAWATFILAMDPDVITGYNIQNFDLPYLISRAQTLKVDRFPFLGRVTGLRSNIRDSSFQSRQVGRRDSKVVSMVGRVQMDMLQVLLREYKLRSYTLNAVSFHFLGEQKEDVQHSIITDLQNGNEQTRRRLAVYCLKDAFLPLRLLERLMVLVNNVEMARVTGVPLGYLLSRGQQVKVVSQLLRQAMREGLLMPVVKTEGGEDYTGATVIEPLKGYYDVPIATLDFSSLYPSIMMAHNLCYTTLLRPGAAQKLGLKPDEFIKTPTGDEFVKASVRKGLLPQILENLLSARKRAKAELAQETDPLRRQVLDGRQLALKVSPNSVYGFTGAQVGKLPCLEISQSVTGFGRQMIEKTKQLVETKYTLENGYDANAKVVYGDTDSVMCRFGVSSVAEAMSLGREAANWVSSHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRSDAHDRMDCKGLEAVRRDNCPLVANLVTSSLRRILVDRDPDGAVAHAKDVISDLLCNRIDISQLVITKELTRAAADYAGKQAHVELAERMRKRDPGSAPNLGDRVPYVIIGAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQQLAKPLLRIFEPILGEGRAESVLLRGDHTRCKTVLTSKVGGLLAFTKRRNSCIGCRSVIDHQGAVCKFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFYMRKKVRKDLEDQERLLQRFGPPGPEAW
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As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities. Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine, 8oxoG or abasic sites.
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O54748
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STK3_RAT
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Serine/threonine-protein kinase 3 (EC 2.7.11.1) (Mammalian STE20-like protein kinase 2) (MST-2) (STE20-like kinase MST2) [Cleaved into: Serine/threonine-protein kinase 3 36kDa subunit (MST2/N); Serine/threonine-protein kinase 3 20kDa subunit (MST2/C)]
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MEQPPAPKSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDVQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKSPEQRATATQLLQHPFIKNAKPVSILRELITEGMEIKAKRHEEQQRELEDEEENSDEDELDSHTMVKTSSEGVGTMRATSTMSEGAQTMIEHNSTMLESDLGTMVINSEDEEEEDGTMKRNATSPQVQRPSFMDYFDKQDFKNKSHENCDQSMREPCPMSNNVFPDNWRVPQDGDFDFLKNLSLEELQMRLKALDPMMEREIEELHQRYSAKRQPILDAMDAKKRRQQNF
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Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates NKX2-1. Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38 (By similarity).
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O54751
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CRX_MOUSE
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Cone-rod homeobox protein
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MMAYMNPGPHYSVNALALSGPNVDLMHQAVPYSSAPRKQRRERTTFTRSQLEELEALFAKTQYPDVYAREEVALKINLPESRVQVWFKNRRAKCRQQRQQQKQQQQPPGAQTKARPAKRKAGTSPRPSTDVCTDPLGISDSYSPSLPGPSGSPTTAVATVSIWSPASEAPLPEAQRAGLVASGPSLTSAPYAMTYAPASAFCSSPSAYASPSSYFSGLDPYLSPMVPQLGGPALSPLSGPSVGPSLAQSPTSLSGQSYSTYSPVDSLEFKDPTGTWKFTYNPMDPLDYKDQSAWKFQIL
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Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcription. Essential for the maintenance of mammalian photoreceptors.
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O54753
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H17B6_RAT
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17-beta-hydroxysteroid dehydrogenase type 6 (17-beta-HSD 6) (17-beta-HSD6) (EC 1.1.1.105) (EC 1.1.1.209) (EC 1.1.1.239) (EC 1.1.1.53) (EC 1.1.1.62) (3-alpha->beta-hydroxysteroid epimerase) (3-alpha->beta-HSE) (Oxidative 3-alpha hydroxysteroid dehydrogenase)
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MWFYLVTLVGLYYLLRWYRERQVVSHLHDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELKSKTSDRLETVILDVTNTDSISAATQWVKEHVGDKGLWGLVNNAGVFQAFAYIEWCRPEDCMSIFQVNLIGLAQVTLSMLFLVKKARGRIVNVSSVLGRVALFGGFYSCSKYGVEAFSDVLRREIRDFGVKVSIIEPGSFKTRMTDAELIIEKTKKTWEATPEHIRESYGQQFFDDFCNTTRRELKKCSTNLSLVTDCMEHALTSKYPRTRYSAGWDARLFFIPLSYLPTSLVDCLLAISRRKPAQAV
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NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro) (By similarity). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro).
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O54754
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AOXA_MOUSE
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Aldehyde oxidase 1 (EC 1.2.3.1) (Azaheterocycle hydroxylase 1) (EC 1.17.3.-) (Retinal oxidase)
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MDPIQLLFYVNGQKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNPSTKAIRHHPVNACLTPICSLHGTAVTTVEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKASACCQSKENGVCCLDQEINGLAESQEEDKTSPELFSEEEFLPLDPTQELIFPPELMRIAEKQPPKTRVFYGERVTWISPVTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILADIVQKLPEEKTQTYRALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGERRIPLSEEFLRKCPEADLKPQEVLVSVNIPWSRKWEFVSAFRQAQRQQNALAIVNSGMRVLFREGGGVIEELSILYGGVGSTIISAKNSCQRLIGRPWNEGMLDTRCRLVLDEVTLAASAPGGKVEFKRTLIISFLFKFYLEVSQGLKREDPGHSPSLAGNHESALDDLHSKHPWRTLTHQNVDPAQLPQDPIGRPIMHLSGIKHATGEAIYCDDMPAVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHLQEANTFGTETFLATDEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLAPLILTIEEAIQHKSFFKSERKLECGNVDEAFKIVDQILEGEIHIGGQEHFYMETQSMLVVPKGEDGEIDIYVSTQFPKYIQDIVAATLKLSANKVMCHVRRVGGAFGGKVGKTSILAAITAFAASKHGRAVRCILERGEDMLITGGRHPYLGKYKAGFMNEGRILALDVEHYCNGGCSLDESLWVIEMGLLKLDNAYKFPNLRCRGWACRTNLPSNTALRGFGFPQAGLVTEACITEVAIKCGLSPEQVRTINMYKHVDTTHYKQEFSAKALSECWRECMAKCSYFERKAAIGKFNAENSWKKRGMAVIPLKFPVGIGSVAMGQAAALVHIYLDGSALVSHGGIEMGQGVHTKMIQVVSRELRMPMSSVHLRGTSTETVPNTNASGGSVVADLNGLAVKDACQTLLKRLEPIISKNPQGTWKDWAQTAFDQSISLSAVGYFRGYESNIDWEKGEGHPFEYFVFGAACSEVEINCLTGDHKNIRTNIVMDVGHSINPALDIGQVEGAFIQGMGLYTIEELSYSPQGTLYSRGPNQYKIPAICDIPTEMHISFLPPSEHSNTLYSSKGLGESGVFLGCSVFFAIHDAVKAARQERGISGPWKLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPCNIPV
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Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imidacloprid (IMI) via its nitroreduction to nitrosoguanidine (IMI-NNO) and aminoguanidine (IMI-NNH(2)). Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. May also catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. Cannot use xanthine and hypoxanthine as substrate.
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O54766
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ZP1_RAT
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Zona pellucida sperm-binding protein 1 (Zona pellucida glycoprotein 1) (Zp-1) [Cleaved into: Processed zona pellucida sperm-binding protein 1]
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MAWGCFVVLLLLVAAPLRLGQHLHLKPGFQYSYDCGVQGMQLLVFPRPNQTIQFKVLDEFGNRFEVNNCSICYHWVISEAQKPAVFSADYKGCHVLEKQDGRFHLRVFIQAVLPNGRVDTAQDVTLICPKPDHILTPESYLAPPTTPQPFIPHTFALHPISGHTLAGSGHTGLTTLYPETHPTPAPPSSEPGPVGPTVPQSQWGTLGSWELTELDSIGTHLLQERCQVASGHIPCMVKGSSEEACQQAGCCYDNTKEMPCYYGNTVTLQCFRSGYFTLVMSQETALTHGVMLDNVHLAYAPNGCPPTQKTSAFVVFHVPLTLCGTAIQVVGKQLVYENQLVSNIEVQTGPQGSITRDGVFRLHVRCIFNASDFLPIRASIFSPQPPAPVTRSGPLRLELRIATDKTFSSYYQGSDYPLVRLLQEPVYIEVRLLQRTDPGLALMLHQCWATPSASPFEQPQWPILSDGCPFKGDNYRTQMVAADRATLPFWSHYQRFTIATFTLLDSSSQNALRGQVYFFCSASACHPVGSETCSTTCDSEIARHRRSSGHHNSTIRALDIVSSPGAVGFEDAPKLEPSGSTRNSGSRPLLWVLQLLALTLVLGDGVLVGLSWAWAWA
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Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the zona pellucida.
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O54767
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ZP2_RAT
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Zona pellucida sperm-binding protein 2 (Zona pellucida glycoprotein 2) (Zp-2) (Zona pellucida protein A) [Cleaved into: Processed zona pellucida sperm-binding protein 2]
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MARWQRVYWLRSLFFALVTSVNSLSLPQSENPAFPGTLICDKDEVRVEFSSRFDMEKWNPSLVDTFGNEISNCTYALDLEKFILKFPYETCTIKVIGGYQVNIRVQDTNADVSYKDDVHHFFCPAIQAEIHEVSEIVVCMEDLISFSFPQLFSRLADENQNVSEMGWIIKIGNGTRVHTLPLKDAIVQGFNLLIDSQKITLHVPANATGVAHYVQESSYLYTVQLKLLFSSPGQKITFSSQAICAPDLSVACNVTHMSLTIPEFPGKLKSVGFGQRNIPEDQWHANGIDKEATNGLRLHFRKSLLKTKPSEKCPFYQFYFSSLELTFNFQGDMLSTVIDPECHCESPVSIDELCTRDGFMDFEVYSHQTKPALNLESLLVGNSSCQPIFKVQSLGLARFHIPLNGCGTRQKFEGDKVIYENEIHALWENPPSNIIFRNSEFRMTVRCHYIRDSMLLRAHIKSHSSPVASVKPGPLALVLQTYPDISYQRPYRKNEYPLVRYLRQPIYMEVTVLNRNDPNIKLVLDDCWATTFEDPASVPQWQIIMDGCEYELDNYRTTFHAANSSAAHSGHYQRFDVKTFAFVSESRGLSSLIYFHCSALICNQASPLCSVTCPAPLRNKREASKEGTMTVSLPGPIILLSDDSSSKGVMNPDSYEITKDIASKTLGAVAALVGSAVIIGFICYLHKKRIVRFNS
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Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor.
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O54774
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AP3D1_MOUSE
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AP-3 complex subunit delta-1 (AP-3 complex subunit delta) (Adaptor-related protein complex 3 subunit delta-1) (Delta-adaptin) (mBLVR1)
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MALKMVKGSIDRMFDKNLQDLVRGIRNHKEDEAKYISQCIDEIKQELKQDNIAVKANAVCKLTYLQMLGYDISWAAFNIIEVMSASKFTFKRVGYLAASQCFHEGTDVIMLTTNQIRKDLSSPSQYDTGVALTGLSCFVTPDLARDLANDIMTLMSHTKPYIRKKAVLIMYKVFLKYPESLRPAFPRLKEKLEDPDPGVQSAAVNVICELARRNPKNYLSLAPLFFKLMTSSTNNWVLIKIIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECVNTVIAVLISLSSGMPNHSASIQLCVQKLRILIEDSDQNLKYLGLLAMSKILKTHPKSVQSHKDLILQCLDDKDESIRLRALDLLYGMVSKKNLMEIVKKLMTHVDKAEGTTYRDELLTKIIDICSQSNYQHITNFEWYISILVELTRLEGTRHGHLIAAQMLDVAIRVKAIRKFAVSQMSSLLDSAHLVASSTQRNGICEVLYAAAWICGEFSEHLQGPQQTLEAMLRPKVTTLPGHIQAVYVQNVVKLYASILQQKEQAADTEAAQEVTQLLVERLPQFVQSADLEVQERASCILQLVKHVQKLQAKGVPVAEEVSALFAGELNPVAPKAQKKVPVPEGLDLDAWINEPPSDSESEDEKPKAIFHEEEPRHTRRRQPEEDEEELARRREARKQEQANNPFYIKSSPSPQKRYQDAPGVEHIPVVQIDLSVPLKVPGMPMSDQYVKLEEQRRHRQRLEKDKKRKKKEKGKRRHSSLPTESDEDIAPAQRVDIITEEMPENALPSDEDDKDPNDPYRALDIDLDKPLADSEKLPVQKHRNAEAVKSPEKEGVLGVEKKSKKPKKKEKKTKEREREKKDKKGEDLDFWLSTTPPPAAAPIPAPSTEELAASTITSPKDECEVLKGEEEDHVDHDQERKSSRHKKKKHRKEKEKEERPRDKKKAKKKQVAPLENGAAAEEEEEPIPPMSSYCLLAESPYIKVTYDIQASLQKDSQVTVSIILENQSSSFLKNMELNVLDSLNTKMTRPEGSSVHDGVPVPFQLPPGVSNEAQFVFTIQSIVMAQKLKGTLSFIAKDDEGATHEKLDFRLHFSCSSYLITTPCYSDAFAKLLESGDLSMNSIKVDGISMSFQNLLAKICFYHHFSVVERVDSCASMYSRSIQGHHVCLLVKKGESSVSVDGKCSDATLLSSLLEEMKTTLAQC
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Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes (By similarity). Involved in process of CD8+ T-cell and NK cell degranulation (By similarity). In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
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O54775
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CCN4_MOUSE
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CCN family member 4 (ELM-1) (WNT1-inducible-signaling pathway protein 1) (WISP-1)
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MRWLLPWTLAAVAVLRVGNILATALSPTPTTMTFTPAPLEETTTRPEFCKWPCECPQSPPRCPLGVSLITDGCECCKICAQQLGDNCTEAAICDPHRGLYCDYSGDRPRYAIGVCAQVVGVGCVLDGVRYTNGESFQPNCRYNCTCIDGTVGCTPLCLSPRPPRLWCRQPRHVRVPGQCCEQWVCDDDARRPRQTALLDTRAFAASGAVEQRYENCIAYTSPWSPCSTTCGLGISTRISNVNARCWPEQESRLCNLRPCDVDIQLHIKAGKKCLAVYQPEEATNFTLAGCVSTRTYRPKYCGVCTDNRCCIPYKSKTISVDFQCPEGPGFSRQVLWINACFCNLSCRNPNDIFADLESYPDFEEIAN
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Downstream regulator in the Wnt/Frizzled-signaling pathway (By similarity). Associated with cell survival. Adheres to skin and melanoma fibroblasts (By similarity). In vitro binding to skin fibroblasts occurs through the proteoglycans, decorin and biglycan (By similarity). Suppresses tumor growth in vivo.
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O54781
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SRPK2_MOUSE
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SRSF protein kinase 2 (EC 2.7.11.1) (SFRS protein kinase 2) (Serine/arginine-rich protein-specific kinase 2) (SR-protein-specific kinase 2) [Cleaved into: SRSF protein kinase 2 N-terminal; SRSF protein kinase 2 C-terminal]
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MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPLPDPAPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKILEENITSAEASGEQDGEYQPEVTLKAADLEDTTEEETAKDNGEVEDQEEKEDAEKENAEKDEDDVEQELANLDPTWVESPKANGHIENGPFSLEQQLEDEEDDEDDCANPEEYNLDEPNAESDYTYSSSYEQFNGELPNGQHKTSEFPTPLFSGPLEPVACGSVISEGSPLTEQEESSPSHDRSRTVSASSTGDLPKTKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS
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Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (By similarity). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (By similarity). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (By similarity). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (By similarity).
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O54784
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DAPK3_MOUSE
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Death-associated protein kinase 3 (DAP kinase 3) (EC 2.7.11.1) (DAP-like kinase) (Dlk) (MYPT1 kinase) (ZIP-kinase)
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MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERFSRVLEDVAAAEQGLRELQRGRRQCRERVCALRAAAEQREARCRDGSAGLGRDLRRLRTELGRTEALRTRAQEEARAALLGAGGLKRRLCRLENRYDALAAQVAAEVQFVRDLVRALEQERLQAECGVR
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Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in formation of promyelocytic leukemia protein nuclear body (PML-NB). Involved in apoptosis involving PAWR which mediates cytoplasmic relocation in vitro phosphorylates PAWR (By similarity). Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton such as in regulation of cell polarity and cell migration. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2 disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates STAT3 and enhances its transcriptional activity. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis (By similarity). Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition.
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O54785
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LIMK2_MOUSE
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LIM domain kinase 2 (LIMK-2) (EC 2.7.11.1)
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MAALAGDEAWRCRGCGTYVPLSQRLYRTANEAWHGSCFRCSECQESLTNWYYEKDGKLYCHKDYWAKFGEFCHGCSLLMTGPAMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQDQLPYSVTLISMPATTECRRGFSVTVESASSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAIKQTSQTLQLLIEHDPVPQRLDQLRLDARLPPHMQSTGHTLMLSTLDTKENQEGTLRRRSLRRSNSISKSPGPSSPKEPLLLSRDISRSESLRCSSSYSQQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSVDPFPWQQKVRFAKGISSGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRPPVEKATTKKRTLRKSDRKKRYTVVGNPYWMAPEMLNGKSYDETVDVFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCKLEPESRPAFSKLEDSFEALSLFLGELAIPLPAELEDLDHTVSMEYGLTRDSPP
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Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Involved in astral microtubule organization and mitotic spindle orientation during early stages of mitosis by mediating phosphorylation of TPPP. Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. Suppresses ciliogenesis via multiple pathways phosphorylation of CFL1, suppression of directional trafficking of ciliary vesicles to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity).
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O54786
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DFFA_MOUSE
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DNA fragmentation factor subunit alpha (DNA fragmentation factor 45 kDa subunit) (DFF-45) (Inhibitor of CAD) (ICAD)
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MELSRGASAPDPDDVRPLKPCLLRRNHSRDQHGVAASSLEELRSKACELLAIDKSLTPITLVLAEDGTIVDDDDYFLCLPSNTKFVALACNEKWIYNDSDGGTAWVSQESFEADEPDSRAGVKWKNVARQLKEDLSSIILLSEEDLQALIDIPCAELAQELCQSCATVQGLQSTLQQVLDQREEARQSKQLLELYLQALEKEGNILSNQKESKAALSEELDAVDTGVGREMASEVLLRSQILTTLKEKPAPELSLSSQDLESVSKEDPKALAVALSWDIRKAETVQQACTTELALRLQQVQSLHSLRNLSARRSPLPGEPQRPKRAKRDSS
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Inhibitor of the caspase-activated DNase (DFF40).
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O54788
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DFFB_MOUSE
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DNA fragmentation factor subunit beta (EC 3.-.-.-) (Caspase-activated deoxyribonuclease) (CAD) (Caspase-activated DNase) (DNA fragmentation factor 40 kDa subunit) (DFF-40)
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MCAVLRQPKCVKLRALHSACKFGVAARSCQELLRKGCVRFQLPMPGSRLCLYEDGTEVTDDCFPGLPNDAELLLLTAGETWHGYVSDITRFLSVFNEPHAGVIQAARQLLSDEQAPLRQKLLADLLHHVSQNITAETREQDPSWFEGLESRFRNKSGYLRYSCESRIRGYLREVSAYTSMVDEAAQEEYLRVLGSMCQKLKSVQYNGSYFDRGAEASSRLCTPEGWFSCQGPFDLESCLSKHSINPYGNRESRILFSTWNLDHIIEKKRTVVPTLAEAIQDGREVNWEYFYSLLFTAENLKLVHIACHKKTTHKLECDRSRIYRPQTGSRRKQPARKKRPARKR
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Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
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O54790
|
MAFG_MOUSE
|
Transcription factor MafG (V-maf musculoaponeurotic fibrosarcoma oncogene homolog G)
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MTTPNKGNKALKVKREPGENGTSLTDEELVTMSVRELNQHLRGLSKEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFARTVARSPVAPARGPLAAGLGPLVPGKVAATSVITIVKSKTDARS
|
Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1 and NFE2L2, and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NFE2L2 transcription factor. Transcription factor, component of erythroid-specific transcription factor NFE2L2. Activates globin gene expression when associated with NFE2L2 (By similarity). May be involved in signal transduction of extracellular H(+) (By similarity).
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O54794
|
AQP7_MOUSE
|
Aquaporin-7 (AQP-7) (Aquaglyceroporin-7)
|
MAPRSVLETIQSVLQKNMVREFLAEFLSTYVMMVFGLGSVAHMVLGENSGSYLGVNLGFGFGVTMGVHVAGGISGAHMNAAVTFTNCALGRMTWKKFPVYVLGQFLGSFSAAATTYLIFYGAINHFAGGDLLVTGSKATANIFATYLPEYMTLWRGFLDEAFVTGMLQLCLFAITDKKNSPALQGTEPLVIGILVTVLGVSLGMNSGYAINPSRDLPPRLFTFIAGWGKQVFRAGNNWWWVPVVAPLLGAYLGGIVYLGLIHPSIPQDPQRLENFTARDQKVTASYKNAASANISGSVPLEHF
|
Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH. The channel is also permeable to urea (By similarity). Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export from adipocytes. After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia. Required for normal glycerol reabsorption in the kidney.
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O54799
|
NMBR_MOUSE
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Neuromedin-B receptor (NMB-R) (Neuromedin-B-preferring bombesin receptor)
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MPPRSLSNLSFPTEANESELVPEVWEKDFLPDSDGTTAELVIRCVIPSLYLIIISVGLLGNIMLVKIFLTNSAMRNVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWVFGKLGCKLIPAIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGVLLWTSLKAVGIWVVSVLLAVPEAVFSEVARIGSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLVIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFVFCWFPNHVLYLYRSFNYKEIDPSLGHMIVTLVARVLSFSNSCVNPFALYLLSESFRKHFNSQLCCGRKSYPERSTSYLLSSSAVRMTSLKSNTKNVVTNSVLLNGHSTKQEIAL
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Receptor for neuromedin-B (By similarity). Contributes to the maintenance of basal sigh rate through signaling in the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity. Contributes to the induction of sneezing following exposure to chemical irritants or allergens which causes release of NMB by nasal sensory neurons and activation of NMBR-expressing neurons in the sneeze-evoking region of the brainstem. These in turn activate neurons of the caudal ventral respiratory group, giving rise to the sneezing response. Contributes to induction of acute itch, possibly through its activation on dorsal root ganglion neurons by the NMB peptide. Plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6. Plays a role in CSF1-induced proliferation of osteoclast precursors by contributing to the positive regulation of the expression of the CSF1 receptor CSF1R.
|
O54800
|
CADH8_RAT
|
Cadherin-8
|
MPERLAETLLDLWTPLIILWITLPSFVYMAPMNQAHVLTTGSPLELSRQSEEMRILNRSKRGWVWNQMFVLEEFSGPEPILVGRLHTDLDPGSKKIKYILSGDGAGTIFQINDITGDIHAIKRLDREEKAEYTLTAQAVDWETNKPLEPPSEFIIKVQDINDNAPEFLNGPYHATVPEMSILGTSVTNVTATDADDPVYGNSAKLVYSILEGQPYFSIEPETAIIKTALPNMDREAKEEYLVVIQAKDMGGHSGGLSGTTTLTVTLTDVNDNPPKFAQSLYHFSVPEDVVLGTAIGRVKANDQDIGENAQSSYDIIDGDGTALFEITSDAQAQDGVIRLRKPLDFETKKSYTLKVEAANIHIDPRFSGRGPFKDTATVKIVVEDADEPPVFSSPTYLLEVHENAALNSVIGQVTARDPDITSSPIRFSIDRHTDLERQFNINADDGKITLATPLDRELSVWHNISIIATEIRNHSQISRVPVAIKVLDVNDNAPEFASEYEAFLCENGKPGQVIQTVSAMDKDDPKNGHFFLYSLLPEMVNNPNFTIKKNEDNSLSILAKHNGFNRQKQEVYLLPIVISDSGNPPLSSTSTLTIRVCGCSNDGVVQSCNVEPYVLPIGLSMGALIAILACIILLLVIVVLFVTLRRHKNEPLIIKDDEDVRENIIRYDDEGGGEEDTEAFDIATLQNPDGINGFLPRKDIKPDLQFMPRQGLAPVPNGVDVDEFINVRLHEADNDPTAPPYDSIQIYGYEGRGSVAGSLSSLESTTSDSDQNFDYLSDWGPRFKRLGELYSVGESDKET
|
Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells cadherins may thus contribute to the sorting of heterogeneous cell types.
|
O54803
|
P2RX6_MOUSE
|
P2X purinoceptor 6 (P2X6) (ATP receptor) (P2XM) (Purinergic receptor) (Purinergic receptor P2X-like 1)
|
MQLQPAGTGNMASAAAAALVSWGFLDYKTEKYVLTRNCRVGVSQRLLQLAVVVYVIGWALLAKKGYQERDLAPQTSVITKLKGVSVTQVKELENRLWDVADFVKPSQGENVFFLVTNFLVTPAQVQGRCPEHPSVPLANCWADEDCPEGETGTYSHGIKTGQCVVFNGTHRTCEIWSWCPVESGAVPRKPLLAQAKNFTLFIKNTVTFSKFNFSRSNALLTWDNTYFKHCLYDPLSSPYCPVFRIGDLVAMAGGDFEDLALLGGAVGISIHWDCNLDTKGSDCCPQYSFQLQQKGYNFRTANHWWAASGVETRSLLKLYGIRFDILVTGQAGKFALIPTAITVGTGAAWLGMVTFLCDLLLLYVDREAGFYWRTKYEEARAPKTTTNSS
|
Receptor for ATP that acts as a ligand-gated ion channel.
|
O54804
|
CHKA_MOUSE
|
Choline kinase alpha (CK) (EC 2.7.1.32) (CHETK-alpha) (Ethanolamine kinase) (EK) (EC 2.7.1.82)
|
MKTKFCTGGEAEPSPLGLLLSCGGNAAPTPGVGQQRDAAGELESKQLGGRTQPLALPPPPPPPLPLPPPPSPPLADEQPEPRTRRRAYLWCKEFLPGAWRGLREDQFHISVIRGGLSNMLFQCSLPDSIASVGDEPRKVLLRLYGAILKMRSCNKEGSEQAQNENEFQGAEAMVLESVMFAILAERSLGPKLFGIFPQGRLEQFIPSRRLDTEELRLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLNQVLRLKFSREARVQQLHKILSYNLPLELENLRSLLQYTRSPVVFCHNDCQEGNILLLEGQENSERRKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKYPFFRANIQKYPSRKQQLHFISSYLTTFQNDFESLSSEEQFATKEDMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMEYAQARFEAYFDQKRKLGV
|
Plays a key role in phospholipid biosynthesis by catalyzing the phosphorylation of free choline to phosphocholine, the first step in phosphatidylcholine biosynthesis. Also phosphorylates ethanolamine, thereby contributing to phosphatidylethanolamine biosynthesis. Has higher activity with choline. May contribute to tumor cell growth. [Isoform 1]: This isoform plays a key role in lipolysis of lipid droplets following glucose deprivation (By similarity). In response to glucose deprivation, phosphorylated by AMPK, promoting localization to lipid droplets (By similarity). Phosphorylation is followed by acetylation by KAT5, leading to dissociation of the homodimer into a monomer (By similarity). Monomeric CHKA isoform 1 is converted into a tyrosine-protein kinase, which phosphorylates lipid droplet structural proteins PLIN2 and PLIN3, leading to lipolysis of lipid droplets (By similarity).
|
O54814
|
CCR3_RAT
|
C-C chemokine receptor type 3 (C-C CKR-3) (CC-CKR-3) (CCR-3) (CCR3) (CKR3) (CD antigen CD193)
|
MASNEEELKTVVETFETTPYEYEWAPPCEKVSIRELGSWLLPPLYSLVFIVGLLGNMMVVLILIKYRKLQIMTNIYLLNLAISDLLFLFTVPFWIHYVLWNEWGFGHCMCKMLSGLYYLALYSEIFFIILLTIDRYLAIVHAVLALRARTVTFATITSIITWGFAVLAALPEFIFHESQDNFGDLSCSPRYPEGEEDSWKRFHALRMNIFGLALPLLIMVICYSGIIKTLLRCPNKKKHKAIQLIFVVMIVFFIFWTPYNLVLLLSAFHSTFLETSCQQSIHLDLAMQVTEVITHTHCCINPIIYAFVGERFRKHLRLFFHRNVAIYLRKYISFLPGEKLERTSSVSPSTGEQEISVVF
|
Receptor for C-C type chemokine. Binds and responds to a variety of chemokines, including CCL11, CCL26, CCL7, CCL13, RANTES(CCL5) and CCL15. Subsequently transduces a signal by increasing the intracellular calcium ions level. In addition acts as a possible functional receptor for NARS1.
|
O54824
|
IL16_MOUSE
|
Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)]
|
MEPHGHSGKSRKSTKFRSISRSLILCNAKTSDDGSSPDEKYPDPFETSLCQGKEGFFHSSMQLADTFEAGLSNIPDLALASDSAQLAAAGSDRGKHCRKMFFMKESSSTSSKEKSGKPEAQSSSFLFPKACHQRTRSNSTSVNPYSAGEIDFPMTKKSAAPTDRQPYSLCSNRKSLSQQLDYPILGTARPTRSLSTAQLGQLSGGLQASVISNIVLMKGQAKGLGFSIVGGKDSIYGPIGIYVKSIFAGGAAAADGRLQEGDEILELNGESMAGLTHQDALQKFKQAKKGLLTLTVRTRLTTPPSLCSHLSPPLCRSLSSSTCGAQDSSPFSLESPASPASTAKPNYRIMVEVSLKKEAGVGLGIGLCSIPYFQCISGIFVHTLSPGSVAHLDGRLRCGDEIVEINDSPVHCLTLNEVYTILSHCDPGPVPIIVSRHPDPQVSEQQLKEAVAQAVEGVKFGKDRHQWSLEGVKRLESSWHGRPTLEKEREKHSAPPHRRAQKIMVRSSSDSSYMSGSPGGSPCSAGAEPQPSEREGSTHSPSLSPGEEQEPCPGVPSRPQQESPPLPESLERESHPPLRLKKSFEILVRKPTSSKPKPPPRKYFKNDSEPQKKLEEKEKVTDPSGHTLPTCSQETRELLPLLLQEDTAGRAPCTAACCPGPAASTQTSSSTEGESRRSASPETPASPGKHPLLKRQARMDYSFDITAEDPWVRISDCIKNLFSPIMSENHSHTPLQPNTSLGEEDGTQGCPEGGLSKMDAANGAPRVYKSADGSTVKKGPPVAPKPAWFRQSLKGLRNRAPDPRRPPEVASAIQPTPVSRDPPGPQPQASSSIRQRISSFENFGSSQLPDRGVQRLSLQPSSGETTKFPGKQDGGRFSGLLGQGATVTAKHRQTEVESMSTTFPNSSEVRDPGLPESPPPGQRPSTKALSPDPLLRLLTTQSEDTQGPGLKMPSQRARSFPLTRTQSCETKLLDEKASKLYSISSQLSSAVMKSLLCLPSSVSCGQITCIPKERVSPKSPCNNSSAAEGFGEAMASDTGFSLNLSELREYSEGLTEPGETEDRNHCSSQAGQSVISLLSAEELEKLIEEVRVLDEATLKQLDSIHVTILHKEEGAGLGFSLAGGADLENKVITVHRVFPNGLASQEGTIQKGNEVLSINGKSLKGATHNDALAILRQARDPRQAVIVTRRTTVEATHDLNSSTDSAASASAASDISVESKEATVCTVTLEKTSAGLGFSLEGGKGSLHGDKPLTINRIFKGTEQGEMVQPGDEILQLAGTAVQGLTRFEAWNVIKALPDGPVTIVIRRTSLQCKQTTASADS
|
Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4. Isoform 1 may act as a scaffolding protein that anchors ion channels in the membrane. Isoform 2 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.
|
O54825
|
BYST_MOUSE
|
Bystin
|
MPKFKVTRGASNREKHAPLAEQILAGNAVRAGTREKRRGREVEEEEEYVGPRLSRRILQQARQQQEELETDHGAGDRSAPPRERATRLGPGLPQDGSDEEDEEWPTLEKAAKMAGVDHQAEVIVDPEDERAIEMFMNKNPPVRRTLADIIMEKLTEKQTEVETVMSEVSGFPMPQLDPRVLEVYRGVREVLCKYRSGKLPKAFKVIPALSNWEQILYVTEPEAWTAAAMYQATRIFASNLKERMAQRFYNLVLLPRVRDDIAEYKRLNFHLYMALKKALFKPGAWFKGILIPLCESGTCTLREAIIVGSIITKCSIPVLHSSAAMLKIAEMEYSGANSIFLRLLLDKKYALPYRVLDALVFHFLAFRTEKRQLPVLWHQCLLTLAQRYKADLATEQKEALLELLRLQPHPQLSPEIRRELQSAVPRDVEDGGVTME
|
Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits.
|
O54827
|
AT10A_MOUSE
|
Phospholipid-transporting ATPase VA (EC 7.6.2.1) (ATPase class V type 10A) (P-locus fat-associated ATPase) (P4-ATPase flippase complex alpha subunit ATP10A)
|
MERELPAAEESASSGWRRPRRRRWEGRTRTVRSNLLPPLGTEDSTIGAPKGERLLMRGCIQHLADNRLKTTKYTLLSFLPKNLFEQFHRLANVYFVFIALLNFVPAVNAFQPGLALAPVLFILAVTAIKDLWEDYSRHRSDHEINHLGCLVFSREEKKYVNRYWKEIRVGDFVRLCCNEIIPADILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDLSRFRGYIMHSNGEKAGLHKENLLLRGCTIRNTEAVAGIVIYAGHETKALLNNSGPRYKRSQLERQMNCDVLWCVLLLVCISLFSAVGHGLWVRRYQEKKALFDVPESDGSSLSPATAAVYSFFTMIIVLQVLIPISLYVSIEIVKVCQVYFINQDIELYDEETDSQLQCRALNITEDLGQIKYIFSDKTGTLTENKMVFRRCTVSGIEYSHDANAQRLARYQEADSEEEEVVSKVGTISHRGSTGSHQSIWMTHKTQSIKSHRRTGSRAEAKRASMLSKHTAFSSPMEKDITPDPKLLEKVSECDRFLAIARHQEHPLAHLSPELSDVFDFFIALTICNTVVVTSPDQPRQKVRVRFELKSPVKTIEDFLRRFTPSRLASGCSSIGNLSTSKSSHKSGSAFLPSLSQDSMLLGLEEKLGQTAPSIASNGYASQAGQEESWASECTTDQKCPGEQREQQEGELRYEAESPDEAALVYAARAYNCALVDRLHDQVSVELPHLGRLTFELLHTLGFDSIRKRMSVVIRHPLTDEINVYTKGADSVVMDLLLPCSSDDARGRHQKKIRSKTQNYLNLYAVEGLRTLCIAKRVLSKEEYACWLQSHIEAEASVESREELLFQSAVRLETNLHLLGATGIEDRLQEGVPETIAKLRQAGLQIWVLTGDKQETAINIAYACKLLDHGEEVITLNADSQEACAALLDQCLSYVQSRNPRSTLQNSESNLSVGFSFNPVSTSTDASPSPSLVIDGRSLAYALEKSLEDKFLFLAKQCRSVLCCRSTPLQKSMVVKLVRSKLKAMTLAIGDGANDVSMIQVADVGVGISGQEGMQAVMASDFAVPRFRYLERLLIVHGHWCYSRLANMVLYFFYKNTMFVGLLFWFQFYCGFSASAMIDQWYLIFFNLLFSSLPQLVTGVLDKDVPADMLLREPQLYKSGQNMEEYRPRAFWLNMVDAAFQSLVCFFIPYLAYYDSDVDVFTWGTPVTAIALFTFLLHLGIETKTWTWLNWLACGFSTFLFFSVALIYNTSCATCYPPSNPYWTMQTLLGDPLFYLTCLIAPIAALLPRLFFKALQGSLFPTQLQLGRQLAKKPLNKFSDPKETFAQGQPPGHSETELSERKTMGPFETLPRDCASQASQFTQQLTCSPEASGEPSAVDTNMPLRENTLLEGLGSQASGSSMPRGAISEVCPGDSKRQSTSASQTARLSSLFHLPSFGSLNWISSLSLASGLGSVLQLSGSSLQMDKQDGEFLSNPPQPEQDLHSFQGQVTGYL
|
Catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane. Initiates inward plasma membrane bending and recruitment of Bin/amphiphysin/Rvs (BAR) domain-containing proteins involved in membrane tubulation and cell trafficking. Facilitates ITGB1/beta1 integrin endocytosis, delaying cell adhesion and cell spreading on extracellular matrix. Has low flippase activity toward glucosylceramide (GlcCer).
|
O54828
|
RGS9_MOUSE
|
Regulator of G-protein signaling 9 (RGS9)
|
MTIRHQGQQYRPRMAFLQKIEALVKDMQNPETGVRMHNQRVLVTSVPHAMTGGDVLQWITQRLWISNLEAQNLGNFIVKYGYIYPLQDPKNLILKPDSSLYRFQTPYFWPTQQWPAEDTDYAIYLAKRNIKKKGILEEYEKENYDFLNKKINYKWDFVIMQAKEQYRTGKERNKADRYALDCQEKAYWLVHRSPPGMNNVLDYGLDRVTNPNEVKKQTVTAVRKEIMYYQQALMRSTVKSSVSLGGIVKYSEQFSSNDAIMSGCLPSNPWITDDTQFWDLNAKLVEIPTKMRVERWAFNFSELIRDPKGRQSFQYFLKKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMDITVKGLRHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKEMLAKAIEPQETTKRSSTLPFMRRHLRSSPSPVILRQLEEEEKAREAANTVDITQPGQHLAPSPHLAVYTGTCVPPSPSSPFSPSCRSPRKPFASPSRFIRRPSIAICPSPSRVALEGSSGLEPKGEASWSGANSGPSVTENREPSADHSRPQPRAPPKARAALSLGRFLRRGCLASPVFARLSPKCPSVSHGKVQPLGDMGQQLPRLKPKKVANFFQIKMEMPTDSGTCLMDSDDPRAGESGDQTTEKEVICPWESLAEGKAG
|
Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to GNAT1. Involved in phototransduction key element in the recovery phase of visual transduction.
|
O54829
|
RGS7_MOUSE
|
Regulator of G-protein signaling 7 (RGS7)
|
MAQGNNYGQTSNGVADESPNMLVYRKMEDVIARMQDEKNGIPIRTVKSFLSKIPSVFSGSDIVQWLIKNLTIEDPVEALHLGTLMAAHGYFFPISDHVLTLKDDGTFYRFQTPYFWPSNCWEPENTDYAVYLCKRTMQNKARLELADYEAESLARLQRAFARKWEFIFMQAEAQAKVDKKRDKIERKILDSQERAFWDVHRPVPGCVNTTEVDIKKSSRMRNPHKTRKSVYGLQNDIRSHSPTHTPTPETKPPTEDELHQQIKYWQIQLDRHRLKMSKVADSLLSYTEQYVEYDPFLVPPDPSNPWLSDDTTFWELEASKEPSQQRVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKRRPIREVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQELLQAKRKGKTLTSKRLTSLVQSY
|
GTPase activator component of the RGS7-GNB5 complex that regulates G protein-coupled receptor signaling cascades. The RGS7-GNB5 complex acts as an inhibitor signal transduction by promoting the GTPase activity of G protein alpha subunits, such as GNAO1, thereby driving them into their inactive GDP-bound form (By similarity). May play a role in synaptic vesicle exocytosis (By similarity). Glycine-dependent regulation of the RGS7-GNB5 complex by GPR158 affects mood and cognition via its ability to regulate neuronal excitability in L2/L3 pyramidal neurons of the prefrontal cortex. Modulates the activity of potassium channels that are activated by GNAO1 in response to muscarinic acetylcholine receptor M2/CHRM2 signaling (By similarity).
|
O54833
|
CSK22_MOUSE
|
Casein kinase II subunit alpha' (CK II alpha') (EC 2.7.11.1)
|
MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGQDNYDQLVRIAKVLGTDELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCAENTVLSSGLTAAR
|
Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins.
|
O54834
|
RHG06_MOUSE
|
Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Rho-type GTPase-activating protein RhoGAPX-1)
|
MSAQSLLHSVFSCSSPASGGTASAKGFSKRKLRQTRSLDPALIGGCGSEMGAEGGLRGSTVSRLHSPQLLAEGLGSRLASSPRSQHLRATRFQTPRPLCSSFSTPSTPQEKSPSGSFHFDYEVPLSRSGLKKSMAWDLPSVLAGSGSASSRSPASILSSSGGGPNGIFSSPRRWLQQRKFQPPPNSRSHPYVVWRSEGDFTWNSMSGRSVRLRSVPIQSLSELERARLQEVAFYQLQQDCDLGCQITIPKDGQKRKKSLRKKLDSLGKEKNKDKEFIPQAFGMPLSQVIANDRAYKLKQDLQREEQKDASSDFVSSLLPFGNKKQNKELSSSNSSLSSTSETPNESTSPNTPEPAPRARRRGAMSVDSITDLDDNQSRLLEALQLSLPAEAQSKKEKARDKKLSLNPIYRQVPRLVDSCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGVDVCLEEEHSVHDVAALLKEFLRDMPDPLLTRELYTAFINTLLLEPEEQLGTLQLLIYLLPPCNCDTLHRLLQFLSIVARHADDNVSKDGQEVTGNKMTSLNLATIFGPNLLHKQKSSDKEYSVQSSARAEESTAIIAVVQKMIENYEALFMVPPDLQNEVLISLLETDPDVVDYLLRRKASQSSSPDILQTEVSFSMGGRHSSTDSNKASSGDISPYDNNSPVLSERSLLAMQEDRARGGSEKLYKVPEQYTLVGHLSSPKSKSRESSPGPRLGKEMSEEPFNIWGTWHSTLKSGSKDPGMTGSYGDIFESSSLRPRPCSLSQGNLSLNWPRCQGSPTGLDSGTQVIRRTQTAATVEQCSVHLPVSRVCSTPHIQDGSRGTRRPAASSDPFLSLNSTEDLAEGKEDVAWLQSQARPVYQRPQESGKDDRRPPPPYPGSGKPATTSAQLPLEPPLWRLQRHEEGSETAVEGGQQASGEHQTRPKKLSSAYSLSASEQDKQNLGEASWLDWQRERWQIWELLSTDNPDALPETLV
|
GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology (By similarity).
|
O54835
|
SMAD9_RAT
|
Mothers against decapentaplegic homolog 9 (MAD homolog 9) (Mothers against DPP homolog 9) (SMAD family member 9) (SMAD 9) (Smad9) (Smad8)
|
MHPSTPISSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMDELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVETPVLPPVLVPRHSEYNPQLSLLAKFRSASLHSEPLMPHNATYPDSFQQSLGPAPPSSPGHVFPQSPCPTSYPQSPGSPSESDSPYQHSDFRPVCYEEPLHWCSVAYYELNNRVGETFQASSRSVLIDGFTDPSNNRNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECVSDSSIFVQSRNCNYQHGFHPATVCKIPSGCSLKVFNNQLFAQLLAQLLAQSVHHGFEVVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
|
Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD) (By similarity). Has been shown to be activated by activin type I receptor-like kinase-2 (ALK-2) which stimulates heteromerization between SMAD9 and SMAD4. ALK-2 binds TGF-beta, activin and BMP.
|
O54838
|
DUS5_RAT
|
Dual specificity protein phosphatase 5 (EC 3.1.3.16) (EC 3.1.3.48) (MAP-kinase phosphatase CPG21)
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MKVTSLDGRRLRKMLRKEAEARCVVLDCRPYLAFAASSVRGSLNVNLNSVVLRRARGGAVSARYVLADEAARARLLQEGGGGVAAVVVLDQGSRHWQKLREESAARVVLTSLLACLSAGPRVYFLKGGYETFYSQYPECCVDAKPISQEKLEGERGLLSQCGKPILSVAYRPAYDQGGPVEILPFLYLGSAYHASKCEFLANLHITALLNVSRRTSEACTTHLHYKWIPVEDSHTADISSHFQEAIDFIDCVREEGGKVLVHCEAGVSRSPTICMAYLMKTKQFRLKEAFEYIKQRRSVVSPNFGFMGQLLQYESEILPSTPTPQPPSCQGEAASSTFIGHLQTLSPDMQGAYCTFPTSVLAPVPTHATVAELHRSPVATATSC
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Dual specificity protein phosphatase active with phosphotyrosine, phosphoserine and phosphothreonine residues. The highest relative activity is toward ERK1.
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O54839
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EOMES_MOUSE
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Eomesodermin homolog (T-box brain protein 2) (T-brain-2) (TBR-2)
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MQLGEQLLVSSVNLPGAHFYSLESARGGGGGGGGGGGGGGGSVSLLPGAAPSPQRLDLDKASKKFPGSLPCQAGSAEPAGAGAGAPAAMLSDADAGDTFGSTSAVAKPGPPDGRKGSPCAEEELPSAATAAATARYSMDSLSSERYYLPSPGPQGSELAAPCSLFQYPAAAGAAHGPVYPASNGARYPYGSMLPPGGFPAAVCPPARAQFGPAAGSGSGAGSSGGGAGGPGAYPYGQGSPLYGPYAGTSAAGSCGGLGGLGVPGSGFRAHVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNINGLNPTAHYNVFVEVVLADPNHWRFQGGKWVTCGKADNNMQGNKMYVHPESPNTGSHWMRQEISFGKLKLTNNKGANNNNTQMIVLQSLHKYQPRLHIVEVTEDGVEDLNEPSKTQTFTFSETQFIAVTAYQNTDITQLKIDHNPFAKGFRDNYDSMYTASENDRLTPSPTDSPRSHQIVPGGRYGVQNFFPEPFVNTLPQARYYNGERTVPQTNGLLSPQQSEEVANPPQRWLVTPVQQPVTNKLDIGSYESEYTSSTLLPYGIKSLPLQTSHALGYYPDPTFPAMAGWGGRGAYQRKMAAGLPWTSRMSPPVFPEDQLAKEKVKEEISSSWIETPPSIKSLDSSDSGVYNSACKRKRLSPSTPSNGNSPPIKCEDINTEEYSKDTSKGMGAYYAFYTSP
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Functions as a transcriptional activator playing a crucial role during development. Functions in trophoblast differentiation and later in gastrulation, regulating both mesoderm delamination and endoderm specification. Plays a role in brain development being required for the specification and the proliferation of the intermediate progenitor cells and their progeny in the cerebral cortex. Also involved in the differentiation of CD8+ T-cells during immune response regulating the expression of lytic effector genes.
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O54842
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NUPR1_RAT
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Nuclear protein 1 (Protein p8)
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MATLPPTAHTSQQPVNIEDEDGILDEYDQYSLAQSYVVGGGRKGRTKREAAANTNRPSPGGHERKLLTKFQNSERKKAWR
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Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses. Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (By similarity). Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (By similarity). Negatively regulates apoptosis through interaction with PTMA (By similarity). Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter. Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity). Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway. Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (By similarity). Coactivator of PAX2 transcription factor activity, both by recruiting the EP300 cofactor to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (By similarity). Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (By similarity). Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (By similarity). Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (By similarity). Also required for LHB expression and ovarian maturation (By similarity). Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity).
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O54851
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CXD2_MOUSE
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Gap junction delta-2 protein (Connexin-36) (Cx36) (Gap junction alpha-9 protein)
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MGEWTILERLLEAAVQQHSTMIGRILLTVVVIFRILIVAIVGETVYDDEQTMFVCNTLQPGCNQACYDRAFPISHIRYWVFQIIMVCTPSLCFITYSVHQSAKQRERRYSTVFLALDRDPAESIGGPGGTGGGGSGGSKREDKKLQNAIVNGVLQNTETTSKETEPDCLEVKELTPHPSGLRTAARSKLRRQEGISRFYIIQVVFRNALEIGFLVGQYFLYGFSVPGLYECNRYPCIKEVECYVSRPTEKTVFLVFMFAVSGICVVLNLAELNHLGWRKIKLAVRGAQAKRKSVYEIRNKDLPRVSVPNFGRTQSSDSAYV
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One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
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O54852
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KCNH7_RAT
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Potassium voltage-gated channel subfamily H member 7 (Ether-a-go-go-related gene potassium channel 3) (ERG-3) (Eag-related protein 3) (Ether-a-go-go-related protein 3) (Voltage-gated potassium channel subunit Kv11.3)
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MPVRRGHVAPQNTFLGTIIRKFEGQNKKFIIANARVQNCAIIYCNDGFCEMTGFSRPDVMQKPCTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEGVAMMFIINFEYVTDEDNAASPERVNPILPVKSVNRKLFGFKFPGLRVLTYRKQSLPQEDPDVVVIDSSKHSDDSVAMKHFKSPTKESCSPSEADDTKALIQPSQCSPLVNISGPLDHSSPKRQWDRLYPDMLQSSSQLTHSRSRESLCSIRRASSVHDIEGFNVHPKNIFRDRHASEDNGRNVKGPFNHIKSSLLGSTSDSNLNKYSTINKIPQLTLNFSDVKTEKKNTSPPSSDKTIIAPKVKERTHNVTEKVTQVLSLGADVLPEYKLQTPRINKFTILHYSPFKAVWDWLILLLVIYTAIFTPYSAAFLLNDREEQKRRECGYSCSPLNVVDLIVDIMFIIDILINFRTTYVNQNEEVVSDPAKIAVHYFKGWFLIDMVAAIPFDLLIFGSGSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLMLLMCIFALIAHWLACIWYAIGNVERPYLTDKIGWLDSLGTQIGKRYNDSDSSSGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHMQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWTYTNGIDMNMVLKGFPECLQADICLHLNQTLLQNCKAFRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILKDDIVVAILGKNDIFGEMVHLYAKPGKSNADVRALTYCDLHKIQREDLLEVLDMYPEFSDHFLTNLELTFNLRHESAKSQSINDSEGDTCKLRRRRLSFESEGDKDFSKENSANDADDSTDTIRRYQSSKKHFEEKKSRSSSFISSIDDEQKPLFLGTVDSTPRMVKASRHHGEEAAPPSGRIHTDKRSHSCKDITDTHSWEREHARAQPEECSPSGLQRAAWGISETESDLTYGEVEQRLDLLQEQLNRLESQMTTDIQAILQLLQKQTTVVPPAYSMVTAGAEYQRPILRLLRTSHPRASIKTDRSFSPSSQCPEFLDLEKSKLKSKESLSSGKRLNTASEDNLTSLLKQDSDASSELDPRQRKSYLHPIRHPSLPDSSLSTVGILGLHRHVSDPGLPGK
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Pore-forming (alpha) subunit of voltage-gated potassium channel. Channel properties may be modulated by cAMP and subunit assembly.
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O54853
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KCNH6_RAT
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Potassium voltage-gated channel subfamily H member 6 (Ether-a-go-go-related gene potassium channel 2) (ERG-2) (Eag-related protein 2) (Ether-a-go-go-related protein 2) (Voltage-gated potassium channel subunit Kv11.2)
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MPVRRGHVAPQNTYLDTIIRKFEGQSRKFLIANAQMENCAIIYCNDGFCELFGYSRVEVMQRPCTCDFLTGPNTPSSAVSRLAQALLGAEECKVDILYYRKDASSFRCLVDVVPVKNEDGAVIMFILNFEDLAQLLAKSSSRSLTQRLLSHSFLGSEGSHSRPSGQGPGPGRGKYRTVSQIPQFTLNFVEFNLEKHRSGSTTEIEIIAPHKVVERTQNVTEKVTQVLSLGADVLPEYKLQAPRIHRGTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLSDQDESQRGTCGYTCSPLTVVDLIVDIMFVVDIVINFRTTYVNTNDEVVSHPRRIAVHYFKGWFLIDMVAAIPFDLLIFRTGSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNVERPYLEPKIGWLDSLGAQLGKQYNGSDPASGPSVQDKYVTALYFTFSSLTSVGFGNVSPNTNSEKVFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLHRALLQHCPAFRGASKGCLRALAVKFKTTHAPPGDTLVHLGDVLSTLYFISRGSIEILRDDVVVAILGKNDIFGEPASLHARPGKSSADVRALTYCDLHKIHRADLLEVLDMYPAFADTFWNKLEVTFNLRDADGGLQSTPRQAPGHQDPQGFFLNDSQSGAAPSLSISDTSALWPELLQQMPPSPPNPRQDLDCWHRELGFKLEQLQAQMNRLESRVSSDLSRILQLLQHPQGRPSYILGASASSDLASFPETSVTRSSESTLLVGHVPSAQTLSYGDLDDHIQTPRNFSPRTPHVAMAMDKTLVPSSEQEQPGGLLSPLASPLRPLEVPGLGGSRFPSLPEHLSSVPKQLEFQRHGSDPGFTRS
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Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a slowly activating, rectifying current. Channel properties may be modulated by cAMP and subunit assembly.
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