ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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C8V329 | MAGAFDFDLEKNPPVVQSTADNSSDGAVPGETFTYGDSTYAKIQRLAAELNIEQRGIERVPAAEQTDTSVFNIGSMWLAANMVVSSFAIGVLGKSVYSLGFVDAILTVLFFNLLGIMTVCFFSCFGPFGLRQMVFSRLWFGWYVTKGFAVLNILACLGWSAANAIVGAQMLHAVNSDVPGFAAILIISICTLLVTFAGYKVVHLYEYWSWIPTFIVFMIILGTFAHSGDFQNIPMGVGTSEMGSVLSFGSAVYGFATGWTSYAADYTVYQPANRSKRKIFLSTWLGLIVPLLFVEMLGVAVMTATDIKGSKYDVGYATSGNGGLIAAVLQPLGGFGDFCLVILALSIVANNCPNFYSVALTVQVLSRYAQRVPRFIWTLFGTGVSIAIAIPGYSHFETVLENFMNFIAYWLAIYSAIAIMDHFVFKRGFSGYVVENFDKREKLPVGIAATIAFGFGVAGMITGMSQPWYVGPIARHAAGGDVGFELGFAFAAFSYLCLRPFEIKFFGR | Function: This permease has a broad specificity towards purines, and also transports cytosine, but neither uracil nor thymine. Contributes very little in purine uptake. Its major role may be the uptake of cytosine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55197
Sequence Length: 508
Subcellular Location: Cell membrane
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P17064 | MLEEGNNVYEIQDLEKRSPVIGSSLENEKKVAASETFTATSEDDQQYIVESSEATKLSWFHKFFASLNAETKGVEPVTEDEKTDDSILNAASMWFSANMVIASYALGALGPMVFGLNFGQSVLVIIFFNIMGLIFVAFFSVFGAELGLRQMILSRYLVGNVTARIFSLINVIACVGWGIVNTSVSAQLLNMVNEGSGHVCPIWAGCLIIIGGTVLVTFFGYSVIHAYEKWSWVPNFAVFLVIIAQLSRSGKFKGGEWVGGATTAGSVLSFGSSIFGFAAGWTTYAADYTVYMPKSTNKYKIFFSLVAGLAFPLFFTMILGAASAMAALNDPTWKAYYDKNAMGGVIYAILVPNSLNGFGQFCCVLLALSTIANNIPNMYTVALSAQALWAPLAKIPRVVWTMAGNAATLGISIPATYYFDGFMENFMDSIGYYLAIYIAISCSEHFFYRRSFSAYNIDDWDNWEHLPIGIAGTAALIVGAFGVALGMCQTYWVGEIGRLIGKYGGDIGFELGASWAFIIYNILRPLELKYFGR | Function: This permease has a broad specificity towards purines, and also transport cytosine and 5-methylcytosine but neither uracil nor thymine.
PTM: Not N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58201
Sequence Length: 533
Subcellular Location: Membrane
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O59834 | MSSTELSEKDLAYLREAIKVSQQARDEGQHPFGCIIVDENDNVIMSAGNRVPDGDVTQHAETRAVGLITKTRRDLEKCTLYTSTEPCAMCSGAIFWSGIRRMIFGLSNENLIKLTQKSGECPPLYINSRDILGAASHPIEVVGPYIEDEAIIPHKGFWDGGR | Function: Catalyzes the hydrolytic deamination of cytosine to uracil or 5-methylcytosine to thymine. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis.
Catalytic Activity: cytosine + H(+) + H2O = NH4(+) + uracil
Sequence Mass (Da): 17882
Sequence Length: 162
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from cytosine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.4.1
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O04584 | MAVSFQTKNPLRPITNIPRSYGPTRVRVTCSVTTTNPQLNHENLVVEKRLVNPPLSKNNDPTLQSTWTHRLWVAAGSTTIFASFAKSIIGGFGSHLWLQPALACYAGYVFADLGSGVYHWAIDNYGGASTPIVGAQLEASQGHHKYPWTITKRQFANNSYTIARAITFIVLPLNLAINNPLFHSFVSTFAFCILLSQQFHAWAHGTKSKLPPLVMALQDMGLLVSRKDHPGHHQAPYNSNYCVVSGAWNKVLDESNLFKALEMALFFQFGVRPNSWNEPNSDWTEETETNFFTKI | Function: Fatty acid desaturase involved in the production of chloroplast-specific phosphatidylglycerol molecular species. Catalyzes the formation of a trans double bond introduced close to the carboxyl group of palmitic acid, which is specifically esterified to the sn-2 glyceryl carbon of phosphatidylglycerol (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32954
Sequence Length: 295
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.-
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Q8WSF3 | MSLAVSLRRALLVLLTGAIFILTVLYWNQGVTKAQAYNEALERPHSHHDASGFPIPVEKSWTYKCENDRCMRVGHHGKSAKRVSFISCSMTCGDVNIWPHPTQKFLLSSQTHSFSVEDVQLHVDTAHREVRKQLQLAFDWFLKDLRLIQRLDYVGSSSEPTVSESSSKSRHHADLEPAATLFGATFGVKKAGDLTSVQVKISVLKSGDLNFSLDNDETYQLSTQTEGHRLQVEIIANSYFGARHGLSTLQQLIWFDDEDHLLHTYANSKVKDAPKFRYRGLMLDTSRHFFSVESIKRTIVGMGLAKMNRFHWHLTDAQSFPYISRYYPELAVHGAYSESETYSEQDVREVAEFAKIYGVQVIPEIDAPAHAGNGWDWGPKRGMGELAMCINQQPWSFYCGEPPCGQLNPKNNYTYLILQRIYEELLQHTGPTDFFHLGGDEVNLDCWAQYFNDTDLRGLWCDFMLQAMARLKLANNGVAPKHVAVWSSALTNTKCLPNSQFTVQVWGGSTWQENYDLLDNGYNVIFSHVDAWYLDCGFGSWRATGDAACAPYRTWQNVYKHRPWERMRLDKKRKKQVLGGEVCMWTEQVDENQLDNRLWPRTAALAERLWTDPSDDHDMDIVPPDVFRRISLFRNRLVELGIRAEALFPKYCAQNPGECI | Function: Involved in brain restructurization via hormonal control during metamorphosis. Implicated in N-glycan processing.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 75486
Sequence Length: 660
EC: 3.2.1.52
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Q52078 | MAGNKSVVYHGTRDLRVETVPYPKLEHNNRKLEHAVILKVVSTNICGSDQHIYRGRFIVPKGHVLGHEITGEVVEKGSDVELMDIGDLVSVPFNVACGRCRNCKEARSDVCENNLVNPDADLGAFGFDLKGWSGGQAEYVLVPYADYMLLKFGDKEQAMEKIKDLTLISDILPTGFHGCVSAGVKPGSHVYIAGAGPVGRCAAAGARLLGAACVIVGDQNPERLKLLSDAGFETIDLRNSAPLRDQIDQILGKPEVDCGVDAVGFEAHGLGDEANTETPNGALNSLFDVVRAGGAIGIPGIYVGSDPDPVNKDAGSGRLHLDFGKMWTKSIRIMTGMAPVTNYNRHLTEAILWDQMPYLSKVMNIEVITLDQAPDGYAKFDKGSPAKFVIDPHGMLKNK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Active against a range of primary alcohols as well as some secondary alcohols. Exhibits higher activity against alcohols with longer carbon chains.
Catalytic Activity: 2 formaldehyde + H2O = formate + H(+) + methanol
Sequence Mass (Da): 42981
Sequence Length: 399
EC: 1.2.98.1
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Q9EY50 | MPVLNLNDPQAVERYEEFMRQSPYGQVTQDLGWAKVKNNWEPVDVYLEDDQGAIIAAMSMLLGDTPTDKKFAYASKGPVMDVTDVDLLDRLVDEAVKALDGRAYVLRFDPEVAYSDEFNTTLQDHGYVTRNRNVADAGMHATIQPRLNMVLDLTKFPDAKTTLDLYPSKTKSKIKRPFRDGVEVHSGNSATELDEFFKTYTTMAERHGITHRPIEYFQRMQAAFDADTMRIFVAEREGKLLSTGIALKYGRKIWYMYAGSMDGNTYYAPYAVQSEMIQWALDTNTDLYDLGGIESESTDDSLYVFKHVFVKDAPREYIGEIDKVLDPEVYAELVKD | Function: Involved in the synthesis of the bacterial cell wall. Catalyzes the addition of alanine into the interchain peptide bridge of peptidoglycan precursor using aminoacyl-tRNA(Ala) as amino acid donor. This alanine is added to the epsilon-amino group of the L-lysine of the peptidoglycan UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, in a ribosome-independent mechanism . Specific for UDP-N-acetyl-muramoyl-pentapeptide. Has no activity toward UDP-N-acetyl-muramoyl-tetrapeptide or UDP-N-acetyl-muramoyl-tripeptide . Also acts on L-seryl-tRNA(Ser) .
Catalytic Activity: L-alanyl-tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine = H(+) + tRNA(Ala) + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-N(6)-(L-alanyl)-L-lysyl-D-alanyl-D-alanine
Sequence Mass (Da): 38284
Sequence Length: 336
EC: 2.3.2.10
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Q9SXQ6 | MGIKGLTKLLADNAPKAMKEQKFESYFGRRIAVDASMSIYQFLIVVGRTGMETLTNEAGEVTSHLQGMFNRTIRLLEAGIKPVYVFDGKPPDLKKQELAKRYSKREDATKELTEAVEEGDKDAIEKFSKRTVKVTKQHNEECKRLLRLMGVPVVEAPCEAEAECAALCINDMVYAVASEDMDSLTFGAPRFLRHLMDPSSKKIPVMEFEVAKVLEELELTMDQFIDLCILSGCDYCDSIKGIGGQTALKLIRQHGSIESILENINKDRYQIPEDWPYQEARRLFKEPNVTLDIPELKWNAPDEEGLVEFLVKENGFNQDRVTKAIEKIKFAKNKSSQGRLESFFKPVVSTSVPLKRKDTSEKPTKAVANKKTKGAGGKKK | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA (By similarity). May be required for cell proliferation.
PTM: Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.
Sequence Mass (Da): 42792
Sequence Length: 380
Subcellular Location: Nucleus
EC: 3.1.-.-
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B8AMS4 | MGIKGLTKLLAEHAPGAAVRRRVEDYRGRVVAIDTSLSIYQFLIVVGRKGTEVLTNEAGEVTSHLQGMLNRTVRILEAGIKPVFVFDGEPPDMKKKELAKRSLKRDGSSEDLNRAIEVGDEDLIEKFSKRTVKVTKKHNEDCKRLLSLMGVPVVQAPGEAEAQCAALCENHKVFAIASEDMDSLTFGARRFLRHLTDLSFKRSPVTEFEVSKVLEELGLTMDQFIDLCILSGCDYCENIRGIGGQRALKLIRQHGYIEEVVQNLSQTRYSVPEDWPYQEVRALFKEPNVCTDIPDFLWTPPDEEGLINFLAAENNFSPDRVVKSVEKIKAANDKFSLGRGKLLAPVANLTGSTSTAGKEPKCILGGPGQVMKARSPLQVCKSSSLNFIHDNSKAFMLGRRSGFLRISTYASI | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
PTM: Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.
Sequence Mass (Da): 45690
Sequence Length: 412
Subcellular Location: Nucleus
EC: 3.1.-.-
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O04397 | MAHSALSQVSVAVPLQTDSSFRRSTFKATSITFSDRSSWISMPPIDLKAAPSRNQHIVCMSVQQASKAKVSVSPLSLEDAKEPPLNIYKPKEPYTATIVSVERLVGPKAPGETCHIVIDHDGNLPYWEGQSYGVIPPGENPKKPGNPHNVRLYLIASTRYGDSFDGKTASLCVRRAVYYDPETGKEDPSKNGVCSNFLCDSKPGDKVKITGPSGKIMLLPEEIPNATHIMIGTGTGVAPFRGYLRRMFMESVPTKFNGLAWLFLGVANTDSLLYDDEFTKYLNDYPGNFRYDRALSREQKNNKGGKMYVQDKIEEYSDEIFKLLDEGAHIYFCGLKGMMPGIQDTLKRVAERRGESWEQKLSQLKKNKQWHVEVY | Function: May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. Is involved in nitrate assimilation.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 41958
Sequence Length: 375
Pathway: Energy metabolism; photosynthesis.
Subcellular Location: Plastid
EC: 1.18.1.2
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B1HW35 | MQHVYDVTIIGGGPAGLYSAFYSGLRGLKTKLIESQSQLGGKVLLYPEKLIWDIGGQPPILGEKFVKQLIQQAKTFDPTILTNTKVDFIERQEHLFIVHTATGERHYSKTVLLAVGGGIINPQKLTLEGAEKYEMSNLHYTVQSYKRFVNRDILISGGGNAAIDWAVELSPLAKSVTVVYRKDTLSAHEATVKEAIDAGVLIECNTTITKLLANDDKTAIQLVRCENSKTKESYTRQIDEVIISHGYNCEASLTFDEAISIPKKDDYYFEGKATGETAQPGIFAAGDILSFEGKINLLLGTFQDAANAVNSIKTYLEPTAYRHGMVSSHNELFKEKNRSIIEKELVPSH | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 38560
Sequence Length: 349
EC: 1.18.1.2
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A9NFF6 | MLEVLIIGAGPTGLYAAFLAGLRNLKAAVIESSAEPGGQLTAVYKDKYIYDIPGFPKITAKDYIDGQVLQYERFKSDLPIYYNEEAIDIKKHDDHFIVTTTTKTIETKFVLIAHGGGGFVPQKLKIDEHYDNILYFIKDLNQFKDKKIVVLGGGDSALDWAIDLSEYTKDVTLVHRRDEFRALQSSVDHFREKGTILTPYIVDTVEGNDKLVHTLVLKHAKTHERLNLDADYIVVNYGFVLTKSRLDEWGIEGEKGLIKVDYTMKTSLDGIYAAGNGIDYPGKVKLISTGQGEAATAIQSITTLLYPEKTRKFEHSTALIKE | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36026
Sequence Length: 322
EC: 1.18.1.2
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A1TRN6 | MENARLIEADAVVIGAGPVGLFQVFQLGLQGIAAHVVDALPHVGGQCAELYADKPIYDIPGVPVCTGRELVALLNRQIAPFSPQLHLSQRVETLQPAPDGGFLFATDAGAALHARTVFIAAGVGAFVPRTLKIDGIERFHGTQVFHHEEPAPTRGRQVVVLGGEDTAVARAIACAEPGPEAAASVTLVHRRDAFQAAPQDLARLQALRDSGRIRVLAAQVTGIEAAAQAGTPEPGRLTGVRLLASDGTEQGLPLDTLLLCLGVSPRLGPVADWGLALERKQVKVDTATFSAGVPGLYAVGDINTYPGKRKLILCGFHEATLAAFAAAEHLAGSPVALQYTTTSTRLKERLGVAGAGTP | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 37297
Sequence Length: 358
EC: 1.18.1.2
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A0LT79 | MLIVGAGPAGLYAAYYAGFRAMSVVVLDSLTEPGGQLAALYPEKVIYDVGGIPAILGRELAADLYKQAMTYNPVMLLGHGADQLFRLDDGSFLVTTTTGLLIHAKAIIVTAGIGVFTPRRLPVGQEYEGRGLRYFVPNPQELAGKRILVVGGGDSAVDYALMLEKVAASVTLIHRRHEFRAHEASVEQLRASSVRILTPYQVSAVYGDDRVTAVDVTDHDTKHVERLDVDEIVAALGFVAELGPLAEWGMELRQRHIVVDTTMATSVPRIYAAGDIADYPGKVKLISVGFGEAAIAVNNAAVAIDPSKKLFPGHSSDPDRHPTER | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 34930
Sequence Length: 325
EC: 1.18.1.2
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A1W6V2 | MHPSPSSPTPQAADAVVIGAGPVGLFQVFQLGLQGIAAHLVDALPHVGGQCAELYPDKPIYDIPGIPVCTGLGLVELLQRQIAPFAPTLHLGQQIHALAAQADGRILLTTTAGTALLARSVFIAAGVGAFVPRAIKAEGVEALAPGQLLYHPDAATATRAATGKRVVVHGGDEAAVQAALDCVDAAAQVLLLHRRDAFQAAPAPLAQLQALREAGRIQVVIGQITGVETAPDGTLQALALLDPQGQPQRQPLDLLLAYLGISPRLGPIADWGLAMDRKQLAVDTATFATSVPGIYAVGDINTYPGKRKLILCGFHEATLAAFAEAERQAGHKLPLEYTTSSERLQARLGVAPAR | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36785
Sequence Length: 354
EC: 1.18.1.2
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Q5PAR7 | MAIIGAGPVGLFTVFQAGMLGMSACVIDALSEVGGQCAVLYPEKPIYDIPAYPVTLARDLVNNLKRQADPFKPTYLLGHTAEQVLEEGEHFVVVTDKKVGVRCRAIVIAAGSGGFGPNRPPLDGITEYEDKSVFYHVSDVSRFRGKRVVIAGGGDSAADWAVSLSEVADSVHVIHRRHSFRCAPNTLRNLESLAERGQIKLLVPYQLAGLAGSDGMLNGVIIRNISSKEETRIDADFLLPFFGISAKLGPIANWGLGVESFYIPIDQSTCRTARTRIYAVGDVAHYQGKLKLILVGFSESALACHDIYKVLFPETPLNFQYSTSKKMPC | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 35705
Sequence Length: 329
EC: 1.18.1.2
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Q2FNC9 | MGVALRDILTDLKRPAETDELKGVAAIDAFNALYQFLSIIRQPDGTPLMDDSGRITSHLSGIFFRTANFLTQGIRPVFIFDGKSPEMKGRTIQERRDVREESKEKWDQAKKEGDLAGAFRYAMSSTAIDAYILSSARQLIQLMGLPVVDAPSEGEAQGAYMVLKGDADYVVSQDYDTLLFGTPVLVRNLTISGKRRLHGRQITVQPERIVLSDVLSTLDITREQLIEIAILTGTDFNPGIRGIGAKTGLKKIKSGEFDSIIREKLPDFDPEPVRSFFLNPPVTDSYTLDPGRIDRDGIRAFLCGEHGFSQDRVDPVLDKISKKEKQKTLESWF | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity).
Sequence Mass (Da): 37157
Sequence Length: 333
EC: 3.1.-.-
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Q58839 | MGVQFGDFIPKNIISFEDLKGKKVAIDGMNALYQFLTSIRLRDGSPLRNRKGEITSAYNGVFYKTIHLLENDITPIWVFDGEPPKLKEKTRKVRREMKEKAELKMKEAIKKEDFEEAAKYAKRVSYLTPKMVENCKYLLSLMGIPYVEAPSEGEAQASYMAKKGDVWAVVSQDYDALLYGAPRVVRNLTTTKEMPELIELNEVLEDLRISLDDLIDIAIFMGTDYNPGGVKGIGFKRAYELVRSGVAKDVLKKEVEYYDEIKRIFKEPKVTDNYSLSLKLPDKEGIIKFLVDENDFNYDRVKKHVDKLYNLIANKTKQKTLDAWFK | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA.
Sequence Mass (Da): 37527
Sequence Length: 326
EC: 3.1.-.-
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A5UL52 | MGVKLKDIIQPEQIDFKDLKGRAISIDAFNTLYQFLSTIRQRDGRPLSDSNGNITSHLSGILYRNSSMIEKDIKPIYVFDGTPSYLKQETIDQRRQTREESEKKWKEALAKQDTQEARKYAMRSSKLSPYIIESSKKLLTMMGIPYIEAYGEGEAQAAYLVENGDAWAVASQDYDCLLFGAKRVVRNLAINSNLGDLEYYNLKRVLDELDINREQLIDMGILIGTDFSEGLKGVGAKTALKLAKKGELENKLAKLQEESSHDISEVREIFLNHNVNTNYKIRWKKPAKNDIIDFLCEEHGFSQDRVSKACDKLKNLNSSQKSLEDWF | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity).
Sequence Mass (Da): 37365
Sequence Length: 327
EC: 3.1.-.-
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Q2NFD4 | MGVKFKDITNPEPIEMKELEGKILTVDASNVIYKFLSSMRQTDGTPLRDLNGHITSHLNGIMFQTSTLIEKDIKPVYVFDGKAPDLKKETQEERINIKKESEKKYLEAKEVGDVVAARKYAARTTHLNKEIIKSSKKLLDLMGIPYVQARTEGEAQASYMVSQNDAWAVVSQDYDCLQFGATRMIRNLKLSKSNSKNLELISLEKTLKELNLTREQLVDVAMLVGTDFNKGVYGIGAKKGIKLIHKYGTLEKALESLNETMEVDAELIREIFLNPNVVHNYTIEFKRPKKSQLLDFLCGEHDFDERRTISAIKKLQAKTAQSSLEDWF | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity).
Sequence Mass (Da): 37297
Sequence Length: 328
EC: 3.1.-.-
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O27670 | MGVKLRDVVSPRRIRLEDLRGRTVAVDAANTLYQFLSSIRQRDGTPLMDSRGRVTSHLSGILYRTAAVMEREIRVIYVFDGRSHHLKGETVSRRADIRKKSEVEWKRALEEGDIDRAKKYAVRSSRMSSEILESSKRLLELLGIPYVQAPGEGEAQASYMVKMGDAWAVASQDYDCLLFGAPRVVRNLTLSGKLEDPEIIELESTLRELSISHTQLVDMALLVGTDFNEGVKGIGARRGLKLIREKGDIFKVIRDLEADIGGDPQVLRRIFLEPEVSEDYEIRWRKPDVEGVIEFLCTEHGFSEDRVRAALKKFEGASSTQKSLEDWF | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity).
Sequence Mass (Da): 37170
Sequence Length: 328
EC: 3.1.-.-
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Q3IPG8 | MGNADLRTLAAIEPKPFDELGGSVVAVDAHNWLYRYLTTTVKFTRSEAYTTADGEEVANLIGVVQGLPKFFEHDVTPVFVFDGGVSDLKADEVEKRRDQRERYEAQLEAAKERDETDAAEIAALESRTQRLTDTIVETTRELLARLDVPVVEAPAEGEAQAAHMARRGDADYVGSEDYDALLLGAPYTLRGLTSNGDPECMDFEATLSTHDLSWEGLVDAAILMGTDFNEGLSGVGPKTAVKLIHEHGDLRSVLAARDDDIPHADRIRELFLDPAVTDDYDYDTDIDPDFERAREFVTETWGVPADEVERGFERIEESVIQTGLDRWT | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity).
Sequence Mass (Da): 36413
Sequence Length: 328
EC: 3.1.-.-
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A9A4B0 | MGLNLKDLVVREKTTLEAFSNKVIAIDAYNAIYQFLASIRGPDGLQLSDSEGRITSHLSGLLYRNVNFLSLGIKPVYVFDGKPPSLKTAEIERRKQIKMDATIKYEKAIADGNMEDARKYAQQTTSMKDGMVKESKQLLTYFGIPYIEAPSEGEATAAHLTNTGQAYASASQDFDSILCGAKRLVRNFTNSGRRKIPNKNTYIDIVPEIIETQKTLDSLELTREELIDVGILIGTDFNPNGFERVGPKTALKMIKQHSKLEEIPQIQEQLEEIDYQEIRKIFLNPEVADVKEIVFENVNYEGMSNYLVRERSFSEDRVNSTLNRLKKALEKKSQNLDQWF | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity).
Sequence Mass (Da): 38589
Sequence Length: 340
EC: 3.1.-.-
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P00240 | AYKVTLKTPSGDQTIEVSPDAYILDAAEEAGLDLPYSCRAGACSSCAGKVEAGTIDQSDQSFLDDDQQGRGFVLTCVAYATSDCTISTHQEESLY | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 10065
Sequence Length: 95
Subcellular Location: Plastid
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P00237 | AYKVTLKTPDGDITFDVEPGERLIDIGSEKADLPLSCQAGACSTCLGKIVSGTVDQSEGSFLDDEQIEQGYVLTCIAIPESDVVIETHKEDEL | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 9962
Sequence Length: 93
Subcellular Location: Plastid
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P70451 | MGFGSDLKNSQEAVLKLQDWELRLLETVKKFMALRIKSDKEYAYTLQNLCNQVDKESTVQVNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYVGIHQQIEAEMIKVTKTELEKLKSSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQSQYYDTTLPLLLDSVQKMQEEMIKALKGIFDDYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTADSLQVMLKTLAEELTQTQQMLLHKEAAVLELEKRIEESFETCEKKSDIVLLLGQKQALEELKQSVQQLRCTEAKCAAQKALLEQKVQENDGKEPPPVVNYEEDARSVTSMERKERLSKFESIRHSIAGIIKSPKSVLGSSTQVCDVISVGERPLAEHDWYHGAIPRIEAQELLKQQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQFVDNLYRFEGTGFSNIPQLIDHHFNTKQVITKKSGVVLLNPIPKDKKWVLNHEDVSLGELLGKGNFGEVYKGTLKDKTPVAIKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVPGGDFLTFLRKRKDELKLKQLVRFSLDVAAGMLYLESKNCIHRDLAARNCLVGENNTLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQNCPEEVFTIMMKCWDYKPENRPKFNDLHKELTVIKKMIT | Function: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3 according to PubMed:10878010 and PubMed:19159681, but clearly plays a redundant role in STAT3 phosphorylation. According to PubMed:11134346, cells where wild type FER has been replaced by a kinase-dead mutant show no reduction in STAT3 phosphorylation. Phosphorylates TMF1. Isoform 3 lacks kinase activity.
PTM: Autophosphorylated.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 94579
Sequence Length: 823
Domain: The coiled coil domains mediate homooligomerization and are required for location at microtubules.
Subcellular Location: Cytoplasm
EC: 2.7.10.2
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P85121 | ATYYKVKLLTPEGEKEFECPDDVYILDNAEEIGIDLPYSCRAGSCSSCAGKVVSGKVDNSDNSFLNDDNMDAGYVLTCHAYANSDVVIETHKEEEV | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 10521
Sequence Length: 96
Subcellular Location: Plastid
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O04166 | MAAAAMTSIVPVASIAPVSKVANVRPSSVSVAKAFGLKSRSMGRLTCMATYKVTFLDGETGAENVVECSDEEYVLDAAERAGMDLPYSCRAGACSSCAGIIKAGEVDQSDQSFLDDSQIDDGFVLTCVAYPASDCIILTHQEENM | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 15217
Sequence Length: 145
Subcellular Location: Plastid
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Q8IED5 | MNIVILLLILTFSIKHSNTYKLKNTYIPINYMYHNNKNILRSQKSKLFLNFLSNNQLANSNKQTCFFKSNIKSSISNIDNYDYIRKRYINTSNKNKLFYNITLRTNDGEKKIECNEDEYILDASERQNVELPYSCRGGSCSTCAAKLVEGEVDNDDQSYLDEEQIKKKYILLCTCYPKSDCVIETHKEDELHDM | Cofactor: Binds 1 2Fe-2S cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions . By transferring electrons to 4-hydroxy-3-methylbut-2-enyl diphosphate reductase LytB/IspH, plays a role in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis .
Sequence Mass (Da): 22721
Sequence Length: 194
Subcellular Location: Plastid
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P18820 | AKKYKVRLLSEAEGIDVTIDSADDVYILDAAEE | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 3641
Sequence Length: 33
Subcellular Location: Plastid
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P34806 | MVSGVSRNAARTSSGCIVALVSTDDDYTSQDVTTIPQAIRFPSSCLVTYSCVSCYLAIPSGKLHAASSFEHVLECTVAPVSEYVKSVFVGSSIECTGRSGSVTFALV | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 11179
Sequence Length: 107
Subcellular Location: Hydrogenosome
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O15552 | MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKVVCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGNEITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQPLVGAQRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQVLRNQGSSLLGRRGKDTAEGTNEDRGVGQGEGMPSSDFTTE | Function: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins but also to the Gq family . Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. May play a role in glucose homeostasis by regulating the secretion of GLP-1, in response to short-chain fatty acids accumulating in the intestine. May also regulate the production of LEP/Leptin, a hormone acting on the central nervous system to inhibit food intake. Finally, may also regulate whole-body energy homeostasis through adipogenesis regulating both differentiation and lipid storage of adipocytes. In parallel to its role in energy homeostasis, may also mediate the activation of the inflammatory and immune responses by SCFA in the intestine, regulating the rapid production of chemokines and cytokines. May also play a role in the resolution of the inflammatory response and control chemotaxis in neutrophils. In addition to SCFAs, may also be activated by the extracellular lectin FCN1 in a process leading to activation of monocytes and inducing the secretion of interleukin-8/IL-8 in response to the presence of microbes . Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably acetate, propionate and butyrate . Exhibits a SCFA-independent constitutive G protein-coupled receptor activity .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37144
Sequence Length: 330
Subcellular Location: Cell membrane
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Q8VCK6 | MTPDWHSSLILTAYILIFLTGLPANLLALRAFMGRVRQPQPAPVHILLLNLTLADLLLLLLLPFRIVEAASNFRWYLPKIVCALTGFGFYSSIYCSTWLLAGISMERYLGVAFPVQYKLSRRPLYGVIAALVAWIMSFGHCTIVIIVQYLNSTEQVGTENQITCYENFTQEQLDVVLPVRLELCLVLFFVPMAVTIFCYWRFVWIMLTQPHVGAQRRRRAVGLAVVTLLNFLVCFGPYNMSHLVGFYLRQSPSWRVEAVVFSSLNASLDPLLFYFSSSVVRRAFGKGLLLIRNPASSMLGRGAKETVEGTKMDRGGSQAEGVQSSEFVTE | Function: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins but also to the Gq family . Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. May play a role in glucose homeostasis by regulating the secretion of GLP-1, in response to short-chain fatty acids accumulating in the intestine . May also regulate the production of LEP/Leptin, a hormone acting on the central nervous system to inhibit food intake . Finally, may also regulate whole-body energy homeostasis through adipogenesis regulating both differentiation and lipid storage of adipocytes . In parallel to its role in energy homeostasis, may also mediate the activation of the inflammatory and immune responses by SCFA in the intestine, regulating the rapid production of chemokines and cytokines . May also play a role in the resolution of the inflammatory response and control chemotaxis in neutrophils . In addition to SCFAs, may also be activated by the extracellular lectin FCN1 in a process leading to activation of monocytes and inducing the secretion of interleukin-8/IL-8 in response to the presence of microbes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37124
Sequence Length: 330
Subcellular Location: Cell membrane
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Q7TMA4 | MSPECAQTTGPGPSHTLDQVNRTHFPFFSDVKGDHRLVLSVVETTVLGLIFVVSLLGNVCALVLVARRRRRGATASLVLNLFCADLLFTSAIPLVLVVRWTEAWLLGPVVCHLLFYVMTMSGSVTILTLAAVSLERMVCIVRLRRGLSGPGRRTQAALLAFIWGYSALAALPLCILFRVVPQRLPGGDQEIPICTLDWPNRIGEISWDVFFVTLNFLVPGLVIVISYSKILQITKASRKRLTLSLAYSESHQIRVSQQDYRLFRTLFLLMVSFFIMWSPIIITILLILIQNFRQDLVIWPSLFFWVVAFTFANSALNPILYNMSLFRNEWRKIFCCFFFPEKGAIFTDTSVRRNDLSVISS | Function: G-protein-coupled receptor for long-chain fatty acids (LCFAs) with a major role in adipogenesis, energy metabolism and inflammation. Signals via G-protein and beta-arrestin pathways . LCFAs sensing initiates activation of phosphoinositidase C-linked G proteins GNAQ and GNA11 (G(q)/G(11)), inducing a variety of cellular responses via second messenger pathways such as intracellular calcium mobilization, modulation of cyclic adenosine monophosphate (cAMP) production, and mitogen-activated protein kinases (MAPKs) . After LCFAs binding, associates with beta-arrestin ARRB2 that acts as an adapter protein coupling the receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis . In response to dietary fats, plays an important role in the regulation of adipocyte proliferation and differentiation . Acts as a receptor for omega-3 polyunsaturated fatty acids (PUFAs) at primary cilium of perivascular preadipocytes, initiating an adipogenic program via cAMP and CTCF-dependent chromatin remodeling that ultimately results in transcriptional activation of adipogenic genes and cell cycle entry . Induces differentiation of brown and beige adipocytes probably via autocrine and endocrine functions of FGF21 hormone . Contributes to the thermogenic activation of brown adipose tissue and the browning of white adipose tissue . Activates brown adipocytes by initiating intracellular calcium signaling leading to mitochondrial depolarization and fission, and overall increased mitochondrial respiration . Consequently stimulates fatty acid uptake and oxidation in mitochondria together with UCP1-mediated thermogenic respiration, eventually reducing fat mass . Regulates bi-potential differentiation of bone marrow mesenchymal stem cells toward osteoblasts or adipocytes likely by up-regulating distinct integrins . In response to dietary fats regulates hormone secretion and appetite . Stimulates GIP and GLP1 secretion from enteroendocrine cells as well as GCG secretion in pancreatic alpha cells, thereby playing a role in the regulation of blood glucose levels . Negatively regulates glucose-induced SST secretion in pancreatic delta cells . Mediates LCFAs inhibition of GHRL secretion, an appetite-controlling hormone . In taste buds, contributes to sensing of dietary fatty acids by the gustatory system . During the inflammatory response, promotes anti-inflammatory M2 macrophage differentiation in adipose tissue . Mediates the anti-inflammatory effects of omega-3 PUFAs via inhibition of NLRP3 inflammasome activation (By similarity). In this pathway, interacts with adapter protein ARRB2 and inhibits the priming step triggered by Toll-like receptors (TLRs) at the level of TAK1 and TAB1 . Further inhibits the activation step when ARRB2 directly associates with NLRP3, leading to inhibition of pro-inflammatory cytokine release (By similarity). Mediates LCFAs anti-apoptotic effects .
PTM: Phosphorylated at two clusters of Ser and Thr residues located in the intracellular C-terminus, a prerequisite for FFAR4 internalization via an ARRB2-dependent pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40813
Sequence Length: 361
Subcellular Location: Cell membrane
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S0ECT9 | MVPSLITPPPSRSGEATPQKDACLNPVNIAEPEGHWIKLPEALFSSIMAVEPEVNPLYRTSKALSDEWLKTALRMNDKTAVIWSRLDIAYMSAICAPHADLETLKLMNDWNGWVFAFDDPFDEGTFANDPIKAAEEVIYTLATLDNIHPVVSPDENPLRHTLQSCWMRFRERSSPSLQYRWKKHLTMYCVGVLQQVGVQHRATRPTIEEYMDMRAGCVGAYPCIGLMEFAEGIDIPQNVMDHPSMQAISRITCDLVTLQNDLCSYRKDLIQGEESNIIFILKDQGMTDQQAVDQIGEMLYDCYRRWHMALANLPFWGEGIDRDVIKFVTGCRNIALGNLHWSLYTFRYLGNDGPEVKRTRMMKLP | Cofactor: Binds 3 Mg(2+) ions per monomer.
Function: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to the sesquiterpene koraiol.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = diphosphate + koraiol
Sequence Mass (Da): 41636
Sequence Length: 365
Domain: The 2 conserved active-site motifs D(D/E)XX(D/E) and NSE are required for coordinating the divalent metal ions that stabilize the PPi moiety of the substrate.
Pathway: Sesquiterpene biosynthesis.
EC: 4.2.3.-
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S0EGZ9 | MPHKDLPIRPLVRAFDPVGPDTLGPPDLDFASLFRERNVPEDAPLTLYPEQLNVPWHTSLPWTRQSKWWVQGEAAGRDLVNRISADKASERGALPVEFMDERRKGKIDELVEDAVSCAVYLYPSSSPTRIELLTQALLLLFFHDDVMERGATQDDATVCDDFVTMIPKNKHMKRYFAEVLECDPILGPGLLRAIGLFVNAGRKKSPFKQDKYATLAEYLDYRRHDIAKPFMIAAIRFGSGVRQTPEETAPFAELEDLYVQHSILINDLYSYDKEMYEARTINGSVVNAVHVIEKLMCVPPHLAKTITRTMSFDVEKKYYAESERFMRDPALNDKQRTYVIALFDCLTGNLFHHATLGRYSRYAEYVFDCKT | Cofactor: Binds 3 Mg(2+) ions per monomer.
Function: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to the spirocyclic sesquiterpene alpha-acorenol.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = (-)-alpha-acorenol + diphosphate
Sequence Mass (Da): 42495
Sequence Length: 371
Domain: The 2 conserved active-site motifs D(D/E)XX(D/E) and NSE are required for coordinating the divalent metal ions that stabilize the PPi moiety of the substrate.
Pathway: Sesquiterpene biosynthesis.
EC: 4.2.3.-
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A0A7L8UVG6 | MTQIKLLLLSLAITAQSITYDLPSQWDHQWLTQQPLGSDTTCTTSHLTAFQMSKTKDPIFFSTGGTDPFLSPKMLPLNSTAGEQWEFDGVSPDAKMAFVFGFYRDPNYAILGSGNLRVSVEMLWPNGTRFAQVDYPTDSVIEECEWGTRGVWRADEFSYSFEVSRDLQTARVAMHTPQVTGVVYLDSESKPRYPDGKIYPSETSTSEALPYFHFVEPIPVAKSQVDLMILGESYVWSDGVGGMERLWGAFSWFTCLQGMNVVRLHAGPYALSLLSFTSNIKKGNEYPSIALFENGEPVFSSQRTEDSDTADYFTFTKTYDGKVTGTLRDKVTGYELELVSPGEKKHWTFIIDHESLAFEYILGGGHGGSGFAGFVQGGRVGLEQFRGIALTEALTFPKKSPLFRSQYSETS | Function: Diels-Alderase; part of the gene cluster that mediates the biosynthesis of the cytotoxic leucine-containing cytochalasans, including aspochalasin C, aspochalasin E, TMC-169, flavichalasine F, aspergillin PZ, aspochalasin M and flavichalasine G . The first step in the pathway is catalyzed by the hybrid PKS-NRPS ffsA that utilizes 8 units of malonyl-CoA to iteratively assemble the octaketide chain before addition of L-leucine by the C-terminal NRPS modules . Because ffsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase fssC (Probable). The methyltransferase (MT) domain of ffsA catalyzes the alpha-methylation at C10 and C14 using S-adenosyl-L-methionine as the methyl-donating cosubstrate (Probable). Reduction by the hydrolyase ffsE, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ffsF then yield the required isoindolone-fused macrocycle (By similarity). A number of oxidative steps catalyzed by the tailoring cytochrome P450 monooxygenase ffsD, the FAD-linked oxidoreductase ffsJ and the short-chain dehydrogenase/reductase ffsI, are further required to afford the final products (Probable).
Sequence Mass (Da): 45809
Sequence Length: 411
Pathway: Mycotoxin biosynthesis.
EC: 5.5.1.-
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A0QNG6 | MQGLVLQLTRVGFLLLLWLFIWSVLRILRTDIYAPTGAVMVRRGLALRGSLLPNRQRRHVARQLVVTEGALAGTRITLGNQPVLIGRADDSTLVLTDDYASTRHARLSPRGSEWYVEDLGSTNGTYLDRAKVTTAVKVPIGAPVRIGKTVIELRP | PTM: Phosphorylated by PknB (By similarity). Dephosphorylated by PstP (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17125
Sequence Length: 155
Subcellular Location: Cell membrane
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P35077 | MTDATNRFRPGLVGRALVRAGLLFAVAACAQAQLLPGARDLNRIDDRQRKEQLQRDIERALTRPPVELNPQSEAAAPARKPDATSGHTVTVHAVDLDFGVEGRLFDPAPLVQDYLNRPLDNEQLFLLVKALSAALYDRGYATSIVTFVPPGVVDGVLKLKVEWGRIKGWLIDGKPLEGTRDRMMVFSAMPGWQDKVLNVFDIDQAIYNINNGGKTGNITIVPADEYGYSYLDLQLQRRALPRVSLGMDNSGPGTPENGRYKYNASVTANDLLGLNDTLGLYIGNRYYRDAGHDAERNYDLMYSVPLGRTRLDLQTGYSTYRNLLKTRYGQYQSAGNSRSFGLKATRLLYRDTRSQFSVYGGLKLRQNKNYLAGTRLDVSSKHYSDVTVGMQYSTQRGANAYFGDLSFTRGVGVNNGKYAAYDERGPQGNVSRFNGSLAWTRYMALAGQPIQWASQLGFQYSRQQLLNSYQITVGDEYTVRGYNLRTSQSGDSGVYLSNTLTVPVQFSLLGKQASVAPFVGADVGALKSNHPDARTIRMAGLAAGVRFDLPYARMSFTYSKPVGAQPGGAPRAPVWLYINAGLSF | Function: Member of a two partner secretion pathway (TPS) in which it mediates the secretion of filamentous hemagglutinin FHA (fhaB).
Sequence Mass (Da): 64446
Sequence Length: 584
Domain: In the crystal structure alpha helix H1 passes through the middle of the pore with its C-terminus in the periplasm and loop L6 also blocks the channel. Both of the POTRA domains are periplasmic; POTRA stands for polypeptide-transport associated.
Subcellular Location: Cell outer membrane
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Q54D73 | MLSQKSIQIIKSTVPLLEKYGVEITSLFYKNMFEAQPQFLNIFNHSNQRNQKQPVALANTILQSAIHIEKLNEINLMPIVHKHVALGITPEMYPIVGAHLLGAMKTVMQDEATPEIMAAWTEAYRAVAQAFMDAEEDLYFETEEQIGGWKDTREFVVDRIEEETPLIKSFYFKAYDGKEIATYIPGQYITVKITLPGDGVDVPTDKMRTYVRHYSLSDKPNDEYYRISIKKELGKNTPNGIVSNHFHNNIKVGDVVPMSVPAGDFVVNNDSETPILLICGGVGINPLFSMLKETLVQQPDRKINFIFSTHCESSQPFKEELKQLEDDYKETGNLKINLVYSENQGHINKEIIEKYSTQHVDQAEIAETDVYICGPVPFMMQVNKDLLQLGFHKENVHYELFGPLTPVLEENQMLRGVKNIIEN | Cofactor: Binds 1 FAD per subunit.
Function: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the cell from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
Catalytic Activity: NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate
Sequence Mass (Da): 48206
Sequence Length: 423
Domain: Consists of two distinct domains; a N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Subcellular Location: Cytoplasm
EC: 1.14.12.17
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Q9JXV4 | MNRTAFCCLSLTTALILTACSSGGGGVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTGKLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAKRQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKSPELNVDLAAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGGKAQEVAGSAEVKTVNGIRHIGLAAKQ | Function: A bacterial surface lipoprotein that binds host (human) complement factor H (fH, gene CFH), binding contributes to the avoidance of complement-mediated lysis by N.meningitidis. Binding of fH to the bacteria surface is independent of bacterial sialic acid moieties . fH binding affinity is high enough that it may sequester plasma fH, depleting its circulating levels and de-regulating complement in the host (Probable). This protein induces high levels of bactericidal antibodies in mice .
PTM: Protein is lipidated in N.meningitidis upon growth in radioactive palmitic acid, probably on Cys-20.
Location Topology: Lipid-anchor
Sequence Mass (Da): 28990
Sequence Length: 274
Domain: Divided into 3 domains by antibody recognition; domain A (27-119), domain B (120-183) and domain C (184-274). Domain A contains linear epitopes that are common to the three GNA 1870 (fHbp) variants, antibodies against it recognize N.meningitidis cells. Domain B contains linear epitopes common to variant 1 proteins but antibodies against it do not give a robust signal against N.meningitidis cells. Domain C does not have linear epitopes but antibodies against it recognize N.meningitidis cells. Bactericidal antibodies are directed against conformational epitopes located in the BC domain . Structures show there are 2 beta barrel domains, 51-156 and 167-274 each form an 8-stranded antiparallel beta-barrel joined by linker between 157-166 .
Subcellular Location: Cell outer membrane
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C5B137 | MLTRIHGGRVVDPTAGRDAVGDVWIEDGRVVAPSERAPDQTIDATGCVVMAGGVEVHSHIAGGNVVMSRLLLPDLYVSESAPNGHPFAHAGGSGSWIGANYARMGYTTAVEPALPPSNALATHLELADIPLLDRGGLAVLGNDDHLLQLLRDGEGKQAVRDLVQQTLAHSRGLGVKCINAGGASAFKDGVLKLSLDDEIPCYGLSTRKIMSALLDAVEEIGVPHPLHVHCNNLGLPGADDSLVATLEAAEGRRIHFAHAQFYAYGVVDPENPMTGGFRSAAERINAAMEAHPNATYDVGQVVFGQTVTISLDILRQFGGRKGAKPKKWVISAGDAEGGGVVPFLYRPRGPVSSLQWAIGLELMLLSSNPERTILTTDHPNGGVFTEYPRIIHLLMDAEERAKEIATLPAIVGERSGLPKIEREYSFSEIAQLTRSGPAKLLGLTDRGHLREGAKADVAIYRDDKDRTAMFSRAKLVLKDGQPIVEDGEVVAWFSGKTLSLDVEADAGMEKRAESYLQDRFGAGLDTFAVPDAAFPENTGTFEDVACRA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR). May be catalyze the hydrolysis of formylmethanofuran (formyl-MFR) to yield formate and MFR.
Catalytic Activity: H2O + N-formylmethanofuran = formate + methanofuran
Sequence Mass (Da): 58480
Sequence Length: 548
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 4/5.
Subcellular Location: Cytoplasm
EC: 3.5.1.-
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C5B138 | MAAWVKGGAADVDAAVEAAADLLAASRVPVLAGLSAEVSALRAAYRLAETLGASLDPVSGPSVYAELGALSAGGAMSTTRAETIGRADVILIVGNRPWDGELIAEIAAAAPSRGRAAGSERALLSLGGPQNGAIRHVAYAADAGGLTISLGHLRAFAKGHLAGEAAFADLAKRLFAAQYGVIVYDPEEVGELGAEMLQGLIRDLNESTRFFALTLADPFQGRAAVQLSAWTTGQAPRVGFGRHQPEHDSWRFDSARQIAAGEADAALWLASLPAPRPAWLGSLPTIAIVGEGSQEAAGETAEVVITVGVPGQSVGGALWNDRRGVIAYAEASDPAKTPAETETAAGVLTRIRDRLIEKGVSC | Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR).
Sequence Mass (Da): 37145
Sequence Length: 362
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 4/5.
Subcellular Location: Cytoplasm
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C5B135 | MSTLRLRGDLPERVDLLNITPLALSGLSEAEAGKLAIGTSRRGLTLGDVFEISLDGSDSLVIEGGSARLDRVGAALSQGSIRVEGDVGQRLGEGMAAGSLTVTGSAGPYAGTGATGGTITIEGDAGDHAGGAVYAAKAGLDGATLVIKGAAGDHLGDRMRRGMILAGSAGAFAASRMIAGTIVVSGALGDHPGYGMRRGTLIAGSHGTLLPTFVETGTPDLVFVRLLAQSLKHLGAAQASLLSGTLRRYSGDLATLGKGELFVPA | Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR).
Sequence Mass (Da): 26463
Sequence Length: 265
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 4/5.
Subcellular Location: Cytoplasm
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Q49118 | MSDFTLNGIKVEDTFAEAFDVAGTAIIVTNDTPKWAMIAATVMTGFATSVIGCGAEAGIDAELSPDETPDGRPGVRILLFGFEPNGLKDQLLKRVGQCILTCPGTACFAGVEGPTKIKLGGAIRYFGDGFAVAKRLPDHEGKMRRYWRIPVMDGEFLCEDSVRAVDGAVGGGNLLFLGRKHADTLIVAEIAVEAAKAIPGAILPFPGGIVRSGSKVGGRTKGMMASTNDAYCPTLKGRAGSALPPECGVVLEIVIDALTSAAVAESMRAALHAATEIGAQHGLVAVTAGNYGGNLGRHHYHLRDLLEKPAA | Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the intermediate formylmethanofuran (formyl-MFR). Catalyzes the transfer of a formyl group from 5-formyl-H(4)MPT to MFR to produce tetrahydromethanopterin (H(4)MPT) and formyl-MFR, which is then hydrolyzed to formate and MFR.
Catalytic Activity: 5,6,7,8-tetrahydromethanopterin + H(+) + N-formylmethanofuran = methanofuran + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 32374
Sequence Length: 311
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 4/5.
Subcellular Location: Cytoplasm
EC: 2.3.1.101
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P14463 | EDGSGEFLAEGGGVR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
Sequence Mass (Da): 1480
Sequence Length: 15
Domain: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
Subcellular Location: Secreted
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P14536 | TKATEGEFLAEGGGVR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
Sequence Mass (Da): 1622
Sequence Length: 16
Domain: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
Subcellular Location: Secreted
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Q7LZT3 | EDTGTFEEGHGGVR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots.
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
Sequence Mass (Da): 1491
Sequence Length: 14
Domain: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
Subcellular Location: Secreted
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P68212 | TNSKEGEFIAEGGGVR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
Sequence Mass (Da): 1651
Sequence Length: 16
Domain: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
Subcellular Location: Secreted
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P14465 | QPSYDYDEEEDDRAKLRLDAR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot.
Sequence Mass (Da): 2585
Sequence Length: 21
Domain: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
Subcellular Location: Secreted
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P68123 | ATDYDEEEDDRVKVRLDAR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot.
Sequence Mass (Da): 2295
Sequence Length: 19
Domain: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
Subcellular Location: Secreted
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P68118 | QHSTDYDEEEEDRAKLHLDAR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.
PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot.
Sequence Mass (Da): 2558
Sequence Length: 21
Domain: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
Subcellular Location: Secreted
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Q23544 | MSVRRRTHSDDFSYLLEKTRRPSKLNVVQEDPKSAPPQGYSLTTVIIISVLVSLICQHFVPYAVSTLHTVIKNSPKQKSSPPPSNRLNIGFISGNSPEKYAPAVQKPTFLVDPIYDEKWKGIQTAVPVMSTQTDEKRENDPAKVKEAILAAKAAGRSRKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTTPLVSAIDRKMLRSVHDLRDEFNHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLSKEHDEISIDDILEMHRRVLGNADPVEAGRIRTTQVYVGRFTPVSPEYVMEQLKDIVDWLNDESTLTIDPIERAAIAHYKLVLVHPFTDGNGRTARLLLNLIMMRSGFPPVILPVETRAEYYASLHVANLGDLRPFVRYVAKHSEASIQRYIGAMKTSSDNILNSGDSKLTPEESEVSEKIEAECRAGN | Function: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-274 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins . In vivo target proteins include the heat-shock 70 family proteins hsp-1 and hsp-3 and the translation elongation factors eef-1A, eef-1G and eef-2 . Can AMPylate core histone H3 in vitro . Can also act as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from target proteins (By similarity). Decreases susceptibility to P.aeruginosa-mediated killing and might therefore play a role in the innate immune response .
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56979
Sequence Length: 508
Domain: The fido domain mediates the adenylyltransferase activity.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.7.108
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B3MK83 | MGATDQALEAESKTTEPPKTPPVPEQHDRPFLGRQANLCHLLVLLFSGGLAAITLHIFTSSNVGWRLRQLHHLPTAHYLQTRDEFAVYSVDELNAFKEFYDRSISDSVGSSYSEAEETNIKEALGALRLAQDMYLAGKDDKAARLFQHSLALAPRHPTVLLRYGEFLEHSQRNIVLADQYYFQALSISPSNSEALANRQRTADVVQSLDERRLESLDSKRDALSAIHESSAALRRAKKEAYFQHIYHTVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKMEITIKDILELHRRVLGHVDPIEGGEFRRNQVYVGGHVPPGPGDLALLMQRFERWLNSEHSSSMHPVNYAALAHYKLVHIHPFIDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSKYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPHQIPMLIQSTSEAGEGVPQLQSSQMGGGASIPEFHESGSGSLP | Function: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-252 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55739
Sequence Length: 497
Domain: The fido domain mediates the adenylyltransferase activity.
Subcellular Location: Membrane
EC: 2.7.7.108
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Q8SWV6 | MGTEAEQPSPPAQQQDQENPPLCKAQNPKPARLYRFVLIFVAGSLAAWTFHALSSTNLVWKLRQLHHLPTAHYLQTRDEFALYSVEELNAFKEFYDKSVSDSVGASYTEAEQTNIKEALGALRMAQDLYLAGKDDKAARLFEHALALAPRHPEVLLRYGEFLEHNQRNIVLADQYYFQALTISPSNSEALANRQRTADVVQSLDERRLESLDSKRDALSAIHESNGALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKIDITIKDILELHRRVLGHVDPIEGGEFRRNQVYVGGHIPPGPGDLALLMQRFERWLNSEHSSTLHPVNYAALAHYKLVHIHPFVDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSKYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTESEAGERLAQMQSPNVAQRSSILEFYESGSGDLP | Function: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context . The side chain of Glu-247 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP . In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it . In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity .
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55725
Sequence Length: 492
Domain: The fido domain mediates the adenylyltransferase activity.
Subcellular Location: Membrane
EC: 2.7.7.108
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Q09920 | MNKFFSFPILGLLLTCVRFVVAKERLFEWNVTDVYDVDPDGSGNSRWVIGVNNKWPIDPLVVDYGDQVIIKMTNSLANNRTTSLHSHGLFQKFTPYMDGVPQSTQCEIPPGATFYYNYTALQNGTYWVHSHDMSQYPDGLRTPFIINALEEPYDYDEEYIISMTDWYYTPFNILVPDEFKTWKNPTGAEPVPDTGLFNDTANATFAMEPGKTYRLRFINIGAFNNYDVMIEDHNMTIIEVDGEYTEPQEVSSIHLTVAQRYSVLVTAKNSTDRNYAITAYMDESLFDTIPDNYNPNVTAWLSYNSDASYDLGPDIDEIDSYDDAELNPLYSWDVTESNHSINIWFDFFTLGDGANYAEINDSSYVFPKVPSIMIANSTNVDGYNLEPVTYGPYTNAYIFEYGDVVDVIIDNHDTGKHPFHLHGHTFQVLERGEENAGLYSDQESHTYYDNPMRRDTVEIEPGSFIVIRFIADNPGAWVIHCHIEWHMESGLLATFIEAPEMIPSISSPDFVKEQCMLDGVPTIGNGAGNYKNISDLSGAPSPPGEMPAGWTSKAIGTMAACVISACIGMGSIIFYGASIHPVPTEELDENDDLQEAALENAAMFLDTDKAVEKVVEGKDEIK | Cofactor: Binds 4 Cu cations per monomer.
Function: Could be an iron transport multicopper oxidase, which is required for Fe(2+) high affinity uptake. May be required to oxidize Fe(2+) and release it from the transporter. Essential component of copper-dependent iron transport.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 69908
Sequence Length: 622
Subcellular Location: Cell membrane
EC: 1.-.-.-
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Q54Y27 | MNLSLPLNKDNSGNSGNSGNSGGSVCSSNNTLSPILSNSILSSPISSPRLISSSNNNNNNNNNNNNNNNNNNNNNNNNTINSDSNNNNNINNKPRKAGIQLDSDGCLIKRIIKEGYGEIPPPRSIVTVHYEGYLSNQVLFDSSVQRNSPFTFQMGTKSVIDAIELSISTMKVGQEAEIVTTQRYAFGKLGLPPFIPPNVSVIYKIKLLSYKLKSNDFTNFESLINKSKEEKEIGNQFFQKSNYKKSIRHYVKSIWILNDPEQTLGLNEMENKLLKDTLIILYLNLASCNIKLKDGKRGISNCEKILELGGNTTAKFYYRMGQAYSLNKQYDSAKRCLVQAIRLEPNDKLLRDELENIKKLQEENNK | Function: PPIases accelerate the folding of proteins by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 40987
Sequence Length: 366
EC: 5.2.1.8
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Q9Y680 | MPKTMHFLFRFIVFFYLWGLFTAQRQKKEESTEEVKIEVLHRPENCSKTSKKGDLLNAHYDGYLAKDGSKFYCSRTQNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYAEGKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLQREFEKDEKPRDKSYQDAVLEDIFKKNDHDGDGFISPKEYNVYQHDEL | Function: PPIases accelerate the folding of proteins during protein synthesis.
PTM: Glycosylated.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 25794
Sequence Length: 222
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.2.1.8
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Q14318 | MASCAEPSEPSAPLPAGVPPLEDFEVLDGVEDAEGEEEEEEEEEEEDDLSELPPLEDMGQPPAEEAEQPGALAREFLAAMEPEPAPAPAPEEWLDILGNGLLRKKTLVPGPPGSSRPVKGQVVTVHLQTSLENGTRVQEEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAVDGPDLEMLTGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSSAKVDMTFEEEAQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN | Function: Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis. Involved in the inhibition of viral infection by influenza A viruses (IAV) .
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Location Topology: Single-pass membrane protein
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 44562
Sequence Length: 412
Subcellular Location: Mitochondrion
EC: 5.2.1.8
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O35465 | MASWAEPSEPAALRLPGAPLLEGFEVLDGVDDAEEEDDLSGLPPLEDMGQPTVEEAEQPGALAREFLAATEPEPAPAPAPEEWLDILGNGLLRMKTLVPGPKGSSRPLKGQVVTVHLQMSLENGTRVQEEPELAFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAEDGPDLEMLSGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSNTKVDMTCEEEEELLQLKVKCLNNLAASQLKLDHYRAALRSCSQVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKRAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN | Function: Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis (By similarity). Required for normal embryonic development.
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
Location Topology: Single-pass membrane protein
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 43529
Sequence Length: 402
Subcellular Location: Mitochondrion membrane
EC: 5.2.1.8
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O95302 | MAFRGWRPPPPPLLLLLLWVTGQAAPVAGLGSDAELQIERRFVPDECPRTVRSGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDIWNSEDQVQIHTYFKPPSCPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLVFDVALLDLHNPKDSISIENKVVPENCERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVIDFHNPSDSISITSHYKPPDCSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAVLVFDIELLELVAGLPEGYMFIWNGEVSPNLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLAPGFDAELIVKNMFTNQDRNGDGKVTAEEFKLKDQEAKHDEL | Function: PPIases accelerate the folding of proteins during protein synthesis.
PTM: Phosphorylated.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 63084
Sequence Length: 570
Subcellular Location: Endoplasmic reticulum
EC: 5.2.1.8
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Q9Z247 | MALGARGWRRRSLLLLLLWVTGQAAPVLGLAVSSELQIQQSFVPDECPRTVHSGDFVRYHYVGTFLDGQKFDSSYDRDSTFNVFVGKGQLIAGMDQALVGMCVNERRLVTIPPNLAYGSEGVSGVIPPNSVLHFDVLLVDIWNSEDQVHIQTYFKPPSCPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEEGDGKDIPGQASLVFDVALLDLHNPKDTISIENKVVPENCERRSQSGDFLRYHYNGTLLDGTLFDSSYSRNHTFDTYIGQGYVIPGMDEGLLGVCIGERRRIVVPPHLGYGEKGRGSIPGSAVLVFDIHVIDFHNPSDSISITSHYKPPDCSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAVLVFDIELLELVSGLPEGYMFIWNGEVSPNLFEEIDRDGNGEVLLEEFSEYIHAQVATGKGKLAPGFNAEMIVKNMFTNQDRNGDGKVTAEEFKLKDQEAKHDEL | Function: PPIases accelerate the folding of proteins during protein synthesis.
PTM: Phosphorylated.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 62995
Sequence Length: 570
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.2.1.8
|
Q10175 | MSKEETLYSVKVDQERVPLFDEDFYKGFRSELSVRFTMAALDPRAKSNDAVTVNVITRLEHPEEDGEESDEELFQEEKFTLCTLKKGSVYQQPIDIIFSPGEEVFFERVGGDIPVYLSGTCIITNIPEEEDSSDLENDFLYGADEFSSDEEEMDDISVTSSEEEEEENGARIEELNSDEEDAEQAEEEILEKPVPKDEVAEKHSKDKLKKEEKEKKTAVDVSDSVNGKKRKTEPAGEGEQTEKKSKSTKTYPKQVLEGNVTVQDKVKGDGPAAKRKKRVSMRYIGRLTNGKVFDKNITGKPFTFNLGLEEVIKGWDVGIVGMQVGGERTIHIPAAMAYGSKRLPGIPANSDLVFDVKLLAVN | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 40540
Sequence Length: 362
EC: 5.2.1.8
|
Q58235 | MVEKGKMVKISYDGYVDGKLFDTTNEELAKKEGIYNPAMIYGPVAIFAGEGQVLPGLDEAILEMDVGEEREVVLPPEKAFGKRDPSKIKLIPLSEFTKRGIKPIKGLTITIDGIPGKIVSINSGRVLVDFNHELAGKEVKYRIKIEEVVDDKKNIVKEIVKMYVPRLSDVKVTIRNGTVKIELPEFAPFIPNIQTAKMAIANEILKRLEDAEKVSFVETFERKKETKEENK | Function: Catalyzes the cis-trans isomerization of peptidyl prolyl bonds and accelerates protein folding (By similarity). Also exhibits chaperone-like activity .
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 25947
Sequence Length: 231
Domain: Contains an N-terminal PPIase domain, an IF (Insert in the Flap) domain and a C-terminal domain (CTD). The CTD mediates dimerization. Chaperone activity requires both the IF domain and the CTD.
EC: 5.2.1.8
|
O27197 | MAVNKGDFIKIEFTGKVKETGEVFDTTYEEVAREAGLGIKKIFGPIPVVVGGGHLIKGLDEAVIGMEEGEEKHVEIEPEDAFGNRDPKLVQLIPMGEFKRQGIKPYPGMTLTVEGHEGRVLNVSGGRVRVDFNHELAGKTLEYDLKVKEIITDDAEKVKSMIQLHYPSQNMDIDKTEVKIEDGKVIIHMDEMTRFDNRSYMDVTLARFRIARDIWENIEGVEKVEFADVFEKRDMEAEEKEEEVEDAGED | Function: Catalyzes the cis-trans isomerization of peptidyl prolyl bonds and accelerates protein folding. Also exhibits chaperone-like activity . In vitro, can use oligopeptides such as N-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as substrates. The PPIase activity is much lower than those of other FKBPs reported against oligopeptidyl substrates. As a chaperone, protects green fluorescent protein (GFP) and rhodanese from thermal denaturation or aggregation, and suppresses the aggregation of chemically unfolded rhodanese and elevates the yield of its refolding .
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 28318
Sequence Length: 250
Domain: Contains an N-terminal PPIase domain, an IF (Insert in the Flap) domain and a C-terminal domain (CTD). Aggregation suppressing activity against chemically unfolded protein is exerted mainly by the CTD while N- and C-terminal domains contribute to thermal protein aggregation suppression. The CTD probably contributes to hexamerization.
EC: 5.2.1.8
|
Q52081 | MNRLLSVFALGGAVLLAGCVAPTPSPTTRTMRRCCRAPRCRQRPTTVRSTRPVSSRTCTATARRSGWVTSSPSRSMSATSASKNAGSQIAKTSKTDIGLTSLFGSTPNTNNPFGGGDLSLEAGYSGDRATKGDSKATQGNTLTGSITVTVAEVLPNGNHRRARQKWLTLNTGEELVRIAGMVRADDIATDNTVPSTRVADARITYSGTGSFADASQPGWLDRFFISPLWPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24489
Sequence Length: 231
Subcellular Location: Cell outer membrane
|
Q3IDW1 | MRNIILFAAGTLLLSGCVSTQNSDVVQDDPYYAPMYPEPNVEPAVANGSLFNTYLSNDLYADKKALRTGDIITVKLQESTQASKAAKTETDKQSDAKLDPVIGLGGLPVNIGGDSIQFGIGSDASFKGDSKSNQSNSLAGDISVNVMRVLPNGNLVIRGEKWLTLNSGEEFIRLEGLVRPEDVTADNTVQSNRIANARIQYSGKGQTQEAQSAGWLTRFFSSSLFPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24430
Sequence Length: 227
Subcellular Location: Cell outer membrane
|
Q8XSW9 | MRILRLAALGTASLLAAACGMLPPPEPIVQGPTTARPPMPVMAPRQNGAIYQEVASGSGGFRGMFEDRRAHMVGDTITIVITENTAASKQTSGSVDRSGSKTTSVPTFAGMNPGVLSLLGVSASDANKFDSKGANGATNNFTATITVTVVEVLSNGNLVVSGEKQMAVGQGTESIKFSGVVNPTTVNNQNTVLSTQVADARMEYRGTGYVAEAQQMGWLSRFFLSVSPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23835
Sequence Length: 229
Subcellular Location: Cell outer membrane
|
Q98HD3 | MIRRTLILCAVAALSGCGTNLREVGKEPSLSPVGSGIDGGNTSALYKYPEPPRAPVKKFSLWDDRQSRLFTDPRALSQGDILTVRIKINDRANFKNQNDRSRTANRKLGFDLSAQWDKWSTAGKGAGALNSATDTTADGEIKRSETLELNVAAIVTDVLPNGNLMITGSQEVRVNAELRVLTIAGIVRPADIGAENTIPYERIAEARISYGGRGRISEIQQPAYGQQVLDQVLPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25524
Sequence Length: 235
Subcellular Location: Cell outer membrane
|
Q52950 | MRTRITAVLAAGLLAGCQNQAFNEIGRAPAMSPIGSGLQYTQTPQLAMYPKQPRHVTNGYSLWNDQQAALFKDARAINIGDILTVDIRIDDKASFENETDRSRKNSSGFNLGASGQSQTSDFAWSGDLEYGSNTKTEGDGKTERSEKLRLLVAAVVTGVLENGNLLISGSQEVRVNHELRILNVAGIVRPRDVDADNVISYDRIAEARISYGGRGRLTEVQQPPWGQQLVDLVSPL | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25730
Sequence Length: 236
Subcellular Location: Cell outer membrane
|
Q6N2Z5 | MSKSVPLQRIVLVAALMATGGLAGGCSSIDRLAAIGERPALTPIENPTTQPGYKPVQMPMPKPEVASYNANSLWRNGSRAFFKDQRAAKVGDILTVTVNFTDKANIANETQRSRTSKEDSGITDFIGSKTITTPATAVLPGRILTTDSTSSSDGKGSVQRQEALQTNVAAVVTQVLPNGNLVVEGKQEIRVNFEIRELIVAGIVRPEDIQSDNTIDSSKIAQARIAYGGRGQITDVQQPRYGQQVMDVLLPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 27024
Sequence Length: 252
Subcellular Location: Cell outer membrane
|
Q2RQF3 | MRRHSTRKTVARVAVVALAVGVLAGCNTFKRLSEIGDGPAMSGVDNPTLRPDYRPVSMPMPAPMVAEPNPSSLWVPGARSFFKDQRAGEVGDLLTVIVDISNEKATFANNLSRTRGNKEGANLTSFLGFEGTLADVLPDGVDPASLTSFGSDSKHTGNGSMARSETVSMRLAAVVLQILPNGNFVIAGKQEVRVNGELRELTVTGVIRPEDIRSDNTIFWHQIAEARISYGGRGTVTDMVEPRYGQQVYDILFPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 27550
Sequence Length: 255
Subcellular Location: Cell outer membrane
|
Q5LWX7 | MMQKCLSPKTLIAALVVLSACGRADHLGKAPSFTPNTESPEHVAMLWPGLPLHTQPQRSVDRASLWSGGQNSLLGDQRAMKKGDILTVVIEIDEKAEISNDTNRSRSGSESLGVPHLLGLPQRIDEKLPEGASMSNAVAVDSSSASGGKGSVKRKEKLTLRVAATVVDVLPNGVLSITGSQELRVNFELRELLVSGYVRPEDISRQNEITYDKIASARVSYGGRGQITDVQQPRYGQQVLDMVLPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 26569
Sequence Length: 246
Subcellular Location: Cell outer membrane
|
Q57QH8 | MQKYALHAYPVMALMVATLTGCAWIPAKPLVQGATTAQPIPGPVPVANGSIFQSAQPINYGYQPLFEDRRPRNIGDTLTIVLQENVSASKSSSANASRDGKTSFGFDTVPRYLQGLFGNSRADMEASGGNSFNGKGGANASNTFSGTLTVTVDQVLANGNLHVVGEKQIAINQGTEFIRFSGVVNPRTISGSNSVPSTQVADARIEYVGNGYINEAQNMGWLQRFFLNLSPM | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24709
Sequence Length: 232
Subcellular Location: Cell outer membrane
|
O85806 | MGNMGTSELLKHIYDINLSYLLLAQRLINDEKASAMFRLGIDETMADALAQLTLPQMVKLAETNQLVCHFRFNESQTIERLTKESRVDDLQQIHTGILLSSHLLQELSSKDASPTKKRA | Function: Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways.
Sequence Mass (Da): 13456
Sequence Length: 119
Domain: The C-terminal region contains a putative helix-turn-helix (HTH) motif, suggesting that this region may bind DNA.
Subcellular Location: Cytoplasm
|
P74931 | MMTQGAVLGLIREGVFQVVLLVAPVLCTALVVGLIVAIFQAVTSIQEQTLTFVPKMLTILGMIALLGGWMLTMLQNYTVRLFDIIPQLVRSGPV | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10186
Sequence Length: 94
Subcellular Location: Cell membrane
|
O67773 | MDKVTSEEFLITLLLSYFRIVSFLFTFPFYGSFLIPNTIRLYLAFALSFAVLSFINITPVKVNTFVEFLVYALNELLFGFSAGLILRLLFDALIIAGELIALHTGLGFLQMFIPGMTQMSLFSGFFTLYGTLIFLSLGGGEFIILGLAESFKRLPVGSFNIFYLNPEVFLNFFYESFRLGVKIAMPLILTALILNLVLAVVNRFIPQMNVFMVGLPLQVSIGLIILLLSLPLITITMSNHFQDFFKVFEYFIQSFKSP | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29178
Sequence Length: 258
Subcellular Location: Cell membrane
|
P35537 | MNSIIDLFPAFLLVFIRISAFFVTIPLFGHRNVPAVHRIGFAFFLAVICFSTIDKPPSLEIDEHYMLLAFKEALVGLCLGLIAYMMIAAVQIAGSFIDFQMGFSIANVIDPQTGAQSPLIGQFIYTMALLFMLSVNAHHLLLDGIYYSFQYISVDQAFPNFGDEKFAYFIAKSFNAMFIIAFQMSAPVVASLFLVDLALGIVARTVPQLNVFVVGLPLKIAVSFIMLIVCMSVIFVVVRNVFSLTIETMRNLLALVGVS | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28636
Sequence Length: 259
Subcellular Location: Cell membrane
|
Q44907 | MYYWDEILNLNFLVLKSFTILPVLVRIFMFLKFSPFFSTIKIGYFNFFFSLILSVIVVEKIKIIYPLDNMLSFALILLGEAILGLIQAFFVNIIFNVFHLVGFFFSNQIGLAYANIFDVFSEEDSMIISQIFAYLFLLLFLSSDFLLRFFVIGIHDSVLNIRVEHLVNMRNSGFVKLLLMSFGFLFEKALLISFPILSLLLLFYLVLGILSKSSPQINLLIISFSTSLFLGLLILYIGFPSLAISSKRVIELSLDSLASFLKLFSRVLK | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30876
Sequence Length: 269
Subcellular Location: Cell membrane
|
P57186 | MLTFNSLQLITLISNFFWPMIRVLSFFSVAPIFKEKLINRKSKILLSGMISWLVWPFLPEVHTVLFSYFGFLLILQQILIGIVLGFTAQLLFATINLSGEIIGLQMGLSFATFFNNNSQIGTSIISRFLNILALFVFITLNMHLYLISIVIDSFYSMPIDGYFLNVNIFFILLKFSSSIFLNGLLLVLPIMIILLSISFVMSLLNRLSPQISIFSIGFPLNLILGMLMLYFLIPVMLPFLKKILDDLIFFMNNNLLHI | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29518
Sequence Length: 258
Subcellular Location: Cell membrane
|
Q89AZ0 | MFQFNFNDFILFIYNLFFPAVRILALFSTAPLFNSKFIEKKIKLIMAFVISWIFSSFLPKVNIAIFSVDGILIIIEQMLIGILLGLTMQLIFSSIFMSGEIISLQMGLSFSSLFDFNSRSNLSALSHFVHIFLLLLFLEWNGHIWMLSALFDTFITIPIQKIYLDPNIFLKVVNFSKYIFFDSIMLLFPIIIVQLLLNLSIGILNRVAPQISILSLGFTVTLLVGIILLYFFIPIFPSSCIVIFRRLQSFVLTLFNS | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29536
Sequence Length: 257
Subcellular Location: Cell membrane
|
Q45975 | MNAFATAFQVYVAALVFARVGAMVMTMPGIGDQAIPARIRLSFALLMALILAPLVQNTVGPIPSTLGGLGGAVIHEVLIGLMIGSVLRLFMTSLTTAGEIISMQTTLSFAQSTNPSMEGSSTAVATFLSMLGLTLVMATDLHHLFIAAIVKSYTIFPFTRAVPVNDAAALAVQTVAQSFSLGVQLAAPVIVFSLVFNLATGLVGRIMPAFQIFFVASPLSVILGLSLLALSLSGIAMVWTDRYRELLDIFT | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26413
Sequence Length: 251
Subcellular Location: Cell membrane
|
P33135 | MLQVTSEQWLSWLNLYFWPLLRVLALISTAPILSERSVPKRVKLGLAMMITFAIAPSLPANDVPVFSFFALWLAVQQILIGIALGFTMQFAFAAVRTAGEIIGLQMGLSFATFVDPASHLNMPVLARIMDMLALLLFLTFNGHLWLISLLVDTFHTLPIGGEPLNSNAFLALTKAGSLIFLNGLMLALPLITLLLTLNLALGLLNRMAPQLSIFVIGFPLTLTVGISLMAALMPLIAPFCEHLFSEIFNLLADIISELPLI | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28543
Sequence Length: 261
Subcellular Location: Cell inner membrane
|
P54702 | MIQVTSEQWLYWLHLYFWPLLRVLALISTAPILSERAIPKRVKLGLGIMITLVIAPSLPANDTPLFSIAALWLAMQQILIGIALGFTMQFAFAAVRTAGEFIGLQMGLSFATFVDPGSHLNMPVLARIMDMLAMLLFLTFNGHLWLISLLVDTFHTLPIGSNPVNSNAFMALARAGGLIFLNGLMLALPVITLLLTLNLALGLLNRMAPQLSIFVIGFPLTLTVGIMLMAALMPLIAPFCEHLFSEIFNLLADIVSEMPINNNP | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28925
Sequence Length: 264
Subcellular Location: Cell inner membrane
|
P74932 | MERSFDALFSQASLFFLAAVRVFALMFTVPLLSVRSVSRVVRVALAGLIAFLVLPLAYPAPMQVREFSAYYVLLLLGEGLLGILTGFFISVIFTTFSAAGQFFSYQMGFGTSEMYDTFAQIENPLMGQFLNFVAMLVFLQIKGFQILFLGGVLRSFQAVNCFVFLRKQEALLLFFTKALSALFLHAMTIALPIMGALLLIHVSMGLLTKAAPQMNLLSEGLPLTIVVTFVLLSVILPYMINLFVSILFGGFEMFEQLLVKLGKAL | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29313
Sequence Length: 265
Subcellular Location: Cell membrane
|
P15286 | MIQPISGPPPGQPPGQGDNLPSGTGNQPLSSQQRTSLESLMTKVTSLTQQQRAELWAGIRHDIGLSGDSPLLSRHFPAAEHNLAQRLLAAQKSHSARQLLAQLGEYLRLGNNRQAVTDYIRHNFGQTPLNQLSPEQLKTILTLLQEGKMVIPQPQQREATDRPLLPAEHNALKQLVTKLAAATGEPSKQIWQSMLELSGVKDGELIPAKLFNHLVTWLQARQTLSQQNTPTLESLQMTLKQPLDASELAALSAYIQQKYGLSAQSSLSSAQAEDILNQLYQRRVKGIDPRVMQPLLNPFPPMMDTLQNMATRPALWILLVAIILMLVWLVR | Function: Acts as a regulator of flagellar gene expression by modulating the protein level of the anti sigma factor FlgM upon sensing ring completion or hook elongation. Flk could inhibit FlgM secretion by acting as a braking system for the flagellar-associated type III secretion (T3S) system. Plays a role in hindering to flip the flagellar T3S specificity switch from the rod and hook-type substrates to filament-type substrates prior to hook-basal body (HBB) completion possibly by preventing interaction of FliK with FlhB (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36668
Sequence Length: 331
Subcellular Location: Cell inner membrane
|
Q1EMV2 | MKDGMRVGERFTHDFVVPPHKTVRHLYPESPEFAEFPEVFATGFMVGLMEWACVRAMAPYLEPGEGSLGTAICVTHTAATPPGLTVTVTAELRSVEGRRLSWRVSAHDGVDEIGSGTHERAVIHLEKFNAKVRQKTPAG | Function: Hydrolyzes fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance. Cannot use acetyl-CoA as substrate.
Catalytic Activity: fluoroacetyl-CoA + H2O = CoA + fluoroacetate + H(+)
Sequence Mass (Da): 15257
Sequence Length: 139
EC: 3.1.2.29
|
Q3IUS7 | MKPRAVALVAGGGFAGALCRHGIAVVLPGTFPWGTLVVNVAGAFLLGAIVYGTERLRSVPESTRLVVATGFLSSFTTYSTFAGETIALAPRLAALNVVGNYALGFVAVLVAREVIRWRS | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12393
Sequence Length: 119
Subcellular Location: Cell membrane
|
Q1QRN0 | MKWTFILAVAAGGSLGSVARYLVGIGFGRLLGPKFPWGTLFINITGSLLIGLFAGLFAIRWNLPQAVRIFLIVGICGGYTTFSTFSLDSFYLIERGEVAAAGAYMIASVVLSVGALIAGIQIVRVL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13333
Sequence Length: 126
Subcellular Location: Cell inner membrane
|
Q5YR86 | MVRRRHDGRGSDDRPTVRGGARVNIALVLLGGMLGAPVRYLIDRAVTARIDSPLPLGTLTVNIVGSAVLGGLIGASANGWLLTAAGTGFCGALTTFSTFGYETIRLVTDGAYGYALGNVVISVAASVGAVYAAVSLTNWVTP | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14521
Sequence Length: 142
Subcellular Location: Cell membrane
|
Q318B0 | MKIKIYIYILLACYIASFLRLFINNNFIVSIIGSLLFGFFIDKRLSYSIEKIILSGFFSCFTSFSGFIYFLYKVFNQGDLMKFIIFCNLIIIINLLVMYFGFWISRKIT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12905
Sequence Length: 109
Subcellular Location: Cell inner membrane
|
Q7V9N6 | MHSKLNIQSKQLYKIFLLIVGSILGAILRWKLNNYFWVNISGAALLGLIVGLRAGSRIQFFLVIGFCGSFTTFSGWILDVFDLFRTGFFWKAAGLICSNLLGGFTALSVTFWIGRKIRHLFIPQ | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13979
Sequence Length: 124
Subcellular Location: Cell inner membrane
|
Q46IH8 | MGIDIKNNTFFLISLGAFLGALFRWQIDEIFIVNLIGCFLLGFFNSLNILKRYKLTLCVGLCGSMTTFSSWMSHLYKLLNQGLYKLFLLNSLSIVLMGVLSIALGHIFAKRLNA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12845
Sequence Length: 114
Subcellular Location: Cell inner membrane
|
Q0S2P9 | MCAVSLTKPVAVVALGGALGASARFLLAELWPGIWTVLLINVVGSLLLGYLAETVGPDRLSRLFLGVGVLGGFTTFSTFAVDAVREDAVTATLYVVATLIPALLAARLGMLAGHRHRLARKAVA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12870
Sequence Length: 124
Subcellular Location: Cell membrane
|
Q214E8 | MSLDELRDRAALYALIAAGSVIGGCARYLVGVAQLSLLGTDFPWATLFVNVTGSFVIGFYAAIAGPDGRLFASSRQRQFVMTGICGGYTTFSGFSLETFQLLRTGHALAALINLGVSPMSWLVAVWLGHLVATRLNRLKGT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15033
Sequence Length: 141
Subcellular Location: Cell inner membrane
|
Q1AYN2 | MAPAELALTLAAAGAGSVLRYLLGGWVAHRMGPEFPWGTLAVNALGCLGLGLLQGAAPHDRALLLVLGSGLLAGFTTFSTLMLETANLATAGERDRAFSNIVGTLALGLFALSAGARAGAWAAG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12403
Sequence Length: 124
Subcellular Location: Cell membrane
|
Q82LR8 | MRADESGPERESREPTHIPGAEPELGGEPTPRGEPGPGFEPGPGGEPAPSRAPFRSRLRKGVLAAVALGGVLGGSARYALGLTFPTPRGTFPVTTFAVNVSGAFLLALLLVYVLEIWPPTRYVRPFAAVGFLGSFTTFSTWMVDTDRLLGHGHYAVAAFNVFGSLFAGLAATGLGLAIGRMALARRVRLAARHGRARRYGWWVR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21754
Sequence Length: 204
Subcellular Location: Cell membrane
|
Q8ZDB1 | MTAIDVMWVGLGGGIGSLLRWWIGLSIGKVYKGNFPLGTFLINISGAFVIGYLSILFSVDWRDRYGDLMNTAVLTGILGGYTTFSSMQLDAAKLATARGRAIAAGYLIISVLVGLAAAAFGAWLAY | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13345
Sequence Length: 126
Subcellular Location: Cell inner membrane
|
A1TSC2 | MLLNIAVICLAACVGALMRWGFALWLNPGGLIPWGTLAVNLIGGYCIGIALAVFTSRPDIDPAWRLLVITGFLGTLTTFSSFSGEVVTMLMQQRFGLAFGTIALHLGGSLALTWAGMRSALWWLAR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13514
Sequence Length: 126
Subcellular Location: Cell inner membrane
|
Q6FF10 | MYSSLLSIACGAVLGAWLRWFVGLKFNSTFQNFPLGTILVNLVGGFIIGFAIALFANMQLSSNYKLFVITGFCGALTTFSTFSAEVIDLLQQQKYGFAIALITIHLMGSLLCTVLGLLSYQWLSQH | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13799
Sequence Length: 126
Subcellular Location: Cell inner membrane
|
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