ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q6K332 | MGSDFKAIPLIDISPLVGKIDDPSMVNDEDLLQVVQMLDDACREAGFFYVKGHGIADSLMKQVRDVTQKFFQLPYEEKLKIKMTPQSGYRGYQRVGENITKGKPDMHEAIDCYTPIEPGKYGDLAKPMVGSNLWPKYPSNFDVLLENYISLLRDLSRKIMRGIALALGAPVDAFEGTTAGDPFWVCRLIGYPVSTDIPEEQRTDTGCGAHTDYGLLTLVNQDDDICALEVRNQSGEWIYAKPIPGTFVCNIGDMLKVWSNGIYQPTLHRVVNNSPRYRVSVAFFYESNFDAAVEPVEFCRERTGGVAKYEKVVYGEHLVQKVLTNFVM | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Involved in melatonin degradation . Catalyzes the hydroxylation of melatonin to produce 2-hydroxymelatonin .
Catalytic Activity: 2-oxoglutarate + melatonin + O2 = 2-hydroxymelatonin + CO2 + succinate
Sequence Mass (Da): 36835
Sequence Length: 328
Subcellular Location: Cytoplasm
EC: 1.14.11.-
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Q5BJF6 | MSASSSGGSPRFPSCGKNGVTSLTQKKVLRAPCGAPSVTVTKSHKRGMKGDTVNVRRSVRVKTKVPWMPPGKSSARPVGCKWENPPHCLEITPPSSEKLVSVMRLSDLSTEDDDSGHCKMNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHENTVLRHNIERMKEEKDFTILQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERLMEQQGALLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRSKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKESLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKEKGDLELEIIVLNDRVTDLVNQQQTLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKILKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSLKVDELERKLEATSAQNIEFLQVIAKREEAIHQSQLRLEEKTRECGTLARQLESAIEDARRQVEQTKEHALSKERAAQNKILDLETQLSRTKTELSQLRRSRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQFLKSSYANVFGDGPYSTFLTSSPIRSRSPPA | Function: Seems to be a major component of sperm tail outer dense fibers (ODF). ODFs are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail and may help to maintain the passive elastic structures and elastic recoil of the sperm tail. May have a modulating influence on sperm motility. Functions as a general scaffold protein that is specifically localized at the distal/subdistal appendages of mother centrioles. Component of the centrosome matrix required for the localization of PLK1 and NIN to the centrosomes. Required for the formation and/or maintenance of normal CETN1 assembly.
PTM: Tyrosine phosphorylated. Phosphorylated by TSSK4 on Ser-95.
Sequence Mass (Da): 95401
Sequence Length: 829
Subcellular Location: Cytoplasm
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Q6P6Z8 | MFNLRTCASKLRPLTASQTIRSLKHNRPAAPRTFQQFRCLSTPVAAEPFLSGTNSNYVEEMYYAWLENPKSVHKSWDIFFRNANAGASPGAAYQSPPSLGSSLSTLTQAQSLLHSQPNVDKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSCVPADIVTSSDKLGFYGLQESDLDKVFHLPTTTFIGGNEMALPLREIIRRLENAYCQHIGVEFMFINDLEQCQWIRQKFEAPGIMQFNNEEKRTLLARLVRSTRFEEFLHRKWSSEKRFGLEGCEVLIPALKTIIDKSSGNGVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEATDEGSGDVKYHLGMYHRRINRVTDRNITLSLVANPSHLEAADPVVQGKTKAEQFYCGDTEGKKVMAILLHGDAAFAGQGIVYETFHLSDLPSHTTHGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVMYVCNVAAEWRSTFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIRKQKAVLQKYAETLISQGVVNQLEYEEEISKYDKICEEAFARSKDEKILHIKHWLDSPWPGFFTLDGQPRSMTCPSTGLTEEDLTHIGNVASSVPVEDFMIHGGLSRILKGRGEMVKNRTVDWALAEYMALGSLLKEGIHIRLSGQDVERGTFSHRHHVLHDQNVDKRTCIPMNHLWPNQAPYTVCNSSLSEYGVLGFELGFAMASPNALVLWEAQFGDFHNTAQCIIDQFVCPGQAKWVRQNGIVLLLPHGMEGMGPEHSSARPERFLQMCNDDPDVWPKASEDFAVGQLYDCNWIVVNCSTPANFFHVIRRQILLPFRKPLIVFTPKSLLRHPEARSSFDDMLPSTHFQRIIPEAGPASQNPEGVKRLIFCTGKVYYELTKERSGRDMEGDVAIARVEQLSPFPFDLVEKEVQKYPNADLVWCQEEHKNQGYYDYVKPRLRTTIHRTKPVWYAGRDPAAAPATGNKKTHLTELRRFLDTAFNLDAFKGHF | Function: 2-oxoglutarate dehydrogenase (E1o) component of the 2-oxoglutarate dehydrogenase complex (OGDHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids. Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate. Mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2
Sequence Mass (Da): 115633
Sequence Length: 1021
Subcellular Location: Mitochondrion
EC: 1.2.4.2
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P20967 | MLRFVSSQTCRYSSRGLLKTSLLKNASTVKIVGRGLATTGTDNFLSTSNATYIDEMYQAWQKDPSSVHVSWDAYFKNMSNPKIPATKAFQAPPSISNFPQGTEAAPLGTAMTGSVDENVSIHLKVQLLCRAYQVRGHLKAHIDPLGISFGSNKNNPVPPELTLDYYGFSKHDLDKEINLGPGILPRFARDGKSKMSLKEIVDHLEKLYCSSYGVQYTHIPSKQKCDWLRERIEIPEPYQYTVDQKRQILDRLTWATSFESFLSTKFPNDKRFGLEGLESVVPGIKTLVDRSVELGVEDIVLGMAHRGRLNVLSNVVRKPNESIFSEFKGSSARDDIEGSGDVKYHLGMNYQRPTTSGKYVNLSLVANPSHLESQDPVVLGRTRALLHAKNDLKEKTKALGVLLHGDAAFAGQGVVYETMGFLTLPEYSTGGTIHVITNNQIGFTTDPRFARSTPYPSDLAKAIDAPIFHVNANDVEAVTFIFNLAAEWRHKFHTDAIIDVVGWRKHGHNETDQPSFTQPLMYKKIAKQKSVIDVYTEKLISEGTFSKKDIDEHKKWVWNLFEDAFEKAKDYVPSQREWLTAAWEGFKSPKELATEILPHEPTNVPESTLKELGKVLSSWPEGFEVHKNLKRILKNRGKSIETGEGIDWATGEALAFGTLVLDGQNVRVSGEDVERGTFSQRHAVLHDQQSEAIYTPLSTLNNEKADFTIANSSLSEYGVMGFEYGYSLTSPDYLVMWEAQFGDFANTAQVIIDQFIAGGEQKWKQRSGLVLSLPHGYDGQGPEHSSGRLERFLQLANEDPRYFPSEEKLQRQHQDCNFQVVYPTTPANLFHILRRQQHRQFRKPLALFFSKQLLRHPLARSSLSEFTEGGFQWIIEDIEHGKSIGTKEETKRLVLLSGQVYTALHKRRESLGDKTTAFLKIEQLHPFPFAQLRDSLNSYPNLEEIVWCQEEPLNMGSWAYTEPRLHTTLKETDKYKDFKVRYCGRNPSGAVAAGSKSLHLAEEDAFLKDVFQQS | Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + CO2
Sequence Mass (Da): 114416
Sequence Length: 1014
Subcellular Location: Mitochondrion
EC: 1.2.4.2
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Q8H107 | MMMRAVIRRAASNGSSPSLFAKSLQSSRVAASSPSLLSGSETGAYLHRGNHAHSFHNLALPAGNSGISRSASLVSSTLQRWVRPFSAETGDTVEAVVPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVNEGDTVEPGTKVAIISKSEDTASQVTPSQKIPETTDTKPSPPAEDKQKPRVESAPVAEKPKAPSSPPPPKQSAKEPQLPPKERERRVPMTRLRKRVATRLKDSQNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKHGVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTINSLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLLDI | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA
Sequence Mass (Da): 50059
Sequence Length: 464
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
Subcellular Location: Mitochondrion
EC: 2.3.1.61
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P20708 | MAIDIKAPTFPESIADGTVATWHKKPGEPVKRDELIVDIETDKVVMEVLAEADGVIAEIVKNEGDTVLSGELLGKLTEGGAATAAPAAAPAPAAAAPAAAEAPILSPAARKIAEENAIAADSITGTGKGGRVTKEDAVAAAEAKKSAPAGQPAPAATAAPLFAAGDRVEKRVPMTRLRAKVAERLVEAQSSMAMLTTFNEVNMKPVMELRAKYKDLFEKTHNGVRLGFMSFFVKAAVEALKRQPGVNASIDGNDIVYHGYQDIGVAVSSDRGLVVPVLRNAEFMSLAEIEGGINEFGKKAKAGKLTIEEMTGGTFTISNGGVFGSLLSTPIVNPPQTAILGMHKIQERPMAVNGQVVILPMMYLALSYDHRLIDGKEAVTFLVTMKDLLEDPARLLLDV | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA
Sequence Mass (Da): 42003
Sequence Length: 399
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
EC: 2.3.1.61
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P16263 | MAEIKVPELAESISEGTIAQWLKQPGDYVEQGEYLLELETDKVNVELTAEESGVLQEVLKDSGDTVQVGEIIGTISEGAGESSAPAPTEKTESKESVKEEKQAEPAAQEVSEEAQSEAKSRTIASPSARKLAREKGIDLSQVPTGDPLGRVRKQDVEAYEKPASKPAPQQKQQPQAQKAQQSFDKPVEVQKMSRRRQTIAKRLVEVQQTSAMLTTFNEVDMTAVMNLRKRRKDQFFEQNEVKLGFMSFFTKAVVAALKKYPLLNAEIQGDELIVKKFYDIGIAVAADEGLVVPVVRDADRLTFAGIEKEIGELAKKARNNKLTLSELQGGSFTITNGGTFGSLMSTPILNSPQVGILGMHKIQLRPVAIDEERFENRPMMYIALSYDHRIVDGKEAVGFLVTIKNLLEDPEQLLLEG | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA
Sequence Mass (Da): 46003
Sequence Length: 417
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
EC: 2.3.1.61
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Q6FYD4 | MTTGIRVPTLGESVTEATIGKWFKKLGEAVAVDEPLVELETDKVTVEVPSPVMGKLTEIIAKEGDIVEVNAVLGFVESGAAGISQSFSPSATSIPEAPSELEQSPSSSATPSGTMPPAPSAAKLMAENNIAKSDISGSGKRGQILKEDVLGALAQGTKASTSVATLTASSSSAAPIQEMREERVRMTKLRQTIARRLKDAQNTAAMLTTFNEVDMSAVMDLRKRYKDLFEKKHGVKLGFMGFFTKAVCHALKEFPTVNAEIDGTDIVYKNYVNAGIAVGTDKGLVVPVVRDADQMSLAEIEKEISRLGRLARDGKLAVSDMQGGTFTITNGGVYGSLMSTPILNAPQSGILGMHAIKERAMVVGGQIIICPMMYLALSYDHRIVDGQEAVTFLVRVKESLEDPERLVLDL | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA
Sequence Mass (Da): 43763
Sequence Length: 410
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
EC: 2.3.1.61
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Q8GCY1 | MTTEIRVPTLGESVTEATVGKWFKKLGEAVAIDEPLVELETDKVTVEVPSPVAGKLFEIIAKEGDTVEVNALLGAVEAGAASVAKSPSSSETSVSAAPSELEQSSSSNTMPPAPSAAKLMAENNIAKSDILGSGKRGQILKEDVLNVLAQGVKTSPPAVSASSSTPVSVSSSAVAPVQEMREERVRMTKLRQTIARRLKDAQNTAAMLTTFNEVDMSAVMGLRKRYKDLFEKKHGVKLGFMGFFTKAVCHALKELPAVNAEIDGTDIIYKNYVNAGIAVGTDKGLVVPVVRDADQMSLAEIEKEIGRLGRLARDGKLAVSDMQGGTFTITNGGVYGSLMSTPILNAPQSGILGMHAIKERAMVVDGQIAIRPMMYLALSYDHRIVDGQEAVTFLVRVKESLEDPERLVLDL | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA
Sequence Mass (Da): 43841
Sequence Length: 411
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
EC: 2.3.1.61
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P11179 | MLSRSRCASRAFSRSLSAFQKGNCPLVRRSLPGISLCQGPGYPDSRKTVINSSNIFSVRFFRTTAVCKDDVITVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAAAPAAAAPKAEPTVSAVPPPPAAPIPTQMPPVPSPSQPLTSKPVSAVKPTAAPPRAEAGAGVGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKDAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTISELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIVDRPVVIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex (By similarity). The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA
Sequence Mass (Da): 48973
Sequence Length: 455
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
Subcellular Location: Mitochondrion matrix
EC: 2.3.1.61
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P57389 | MKKINILVPDLPESISDATVVKWHKKIGDTVHCDDNIVDIETDKVMLEVSSPCDGILQSILEKEGKVVISQQTLGEINKSTVVDNHLSNNHIIEKEDNLLKKEEKYITTEEKKEIEYLLKDNHKHLTPSMRRSVKIHNINNGFLNQVIETSKKTNFENIIKEEKKESNQILFNHNIFNANENNKNNNNKVTNRVKMTRLRQRIAERLLDSKNNTAMLTTFHEVNMKPIILLRKKYGEDFEKKHNVRIGFMSFFVKAVIQALKNFPEINAYIDQTDIVFYKNFDISIAISTPRGLITPVIRNADTMTMAEIEKKIKDFSIKGLQNKINIKELMGGNFTITNGGVFGSLMSTPIINPPQTAILGMHVIQERPVVVNGQIKILPMMYLALSYDHRLIDGKESVGFLINIKNILEDFNRIAIDV | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA
Sequence Mass (Da): 48092
Sequence Length: 420
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
EC: 2.3.1.61
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P52993 | MAIVDVKVPQLSESVAEATMLNWKKKPGEAVAQDEILIEIETDKVVLEVPAPSAGVLSIIVKNDGDTVVADEIIAKIDTEATAGAAAPAAAAPAPAAAAPAPAAAVAAPAAAGGVAMPSAAKLMAEAGLSAGQVAGTGKDGRITKGDALAAAAAPAAKAAPAPAAAKPALQQVSAPVDFAALGDRPEERVPMSRLRARIAERLLQSQSTNAILTTFNEVNMKPVMDLRNKYKDRFEKEHGVKLGFMSFFVKAAVHALKKFPLINASIDGNDIVYHGYFDIGIAVGSPRGLVVPILRNADQMSLADIEKKIAEFGVKARDGKLSLEELTGGTFSISNGGVFGSMLSTPIINPPQSAILGVHATKDRPVVEDGQIVIRPMNYLAMSYDHRIIDGREAVLGLVAMKDALEDPARLLLDL | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA
Sequence Mass (Da): 43250
Sequence Length: 416
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
EC: 2.3.1.61
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P83708 | AIVEVKVPXLXE | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA
Sequence Mass (Da): 1319
Sequence Length: 12
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
EC: 2.3.1.61
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Q869Y7 | MRSATKLIKNVNINRCVQSNVVRSTSRLINNNSINTVRQFTSSSSSSFTSLFNNNNVNNTNIKYQRFYSSANDVVIKVPSMGDSISEGTIVAWTKNVGDSVRVDEVVCSIETDKVTIDINAPVSGTIVELFAKEGENVTVGNDLYKIAKGEVAAAPKVEAPKAAEAPKAAAPTPAPKAAETPKAAPAPKSEAPTPAPKSTTTTTSTGPSETRVKMTRIRQRTAQRLKDSQNTAAMLTTFNELDMSALMNMRKTYKDEFEKKHGVKFGFMSAFVKASTIALKEQPIVNASVEENDIVYHNNVNINVAVSAPRGLVVPVIRNCENLSFADIEKEIGRLSGLARNDALAIEDSIGGTFTISNGGVFGSMFGTPIINPPQSAILGMHAIKDRPYVVNGQVVVRPIMYLALTYDHRIIDGREAVTFLKKIKDVLENPERILLEL | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA
Sequence Mass (Da): 47633
Sequence Length: 439
Pathway: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
Subcellular Location: Mitochondrion
EC: 2.3.1.61
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P16387 | MLAASFKRQPSQLVRGLGAVLRTPTRIGHVRTMATLKTTDKKAPEDIEGSDTVQIELPESSFESYMLEPPDLSYETSKATLLQMYKDMVIIRRMEMACDALYKAKKIRGFCHLSVGQEAIAVGIENAITKLDSIITSYRCHGFTFMRGASVKAVLAELMGRRAGVSYGKGGSMHLYAPGFYGGNGIVGAQVPLGAGLAFAHQYKNEDACSFTLYGDGASNQGQVFESFNMAKLWNLPVVFCCENNKYGMGTAASRSSAMTEYFKRGQYIPGLKVNGMDILAVYQASKFAKDWCLSGKGPLVLEYETYRYGGHSMSDPGTTYRTRDEIQHMRSKNDPIAGLKMHLIDLGIATEAEVKAYDKSARKYVDEQVELADAAPPPEAKLSILFEDVYVKGTETPTLRGRIPEDTWDFKKQGFASRD | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
PTM: Phosphorylated at Ser-313 by pyruvate dehydrogenase kinases PKP1 (PDK1) and PKP2 (PDK2), and dephosphorylated by pyruvate dehydrogenase phosphatases PTC5 and PTC6.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 46343
Sequence Length: 420
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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Q9C6Z3 | MSSIIHGAGAATTTLSTFNSVDSKKLFVAPSRTNLSVRSQRYIVAGSDASKKSFGSGLRVRHSQKLIPNAVATKEADTSASTGHELLLFEALQEGLEEEMDRDPHVCVMGEDVGHYGGSYKVTKGLADKFGDLRVLDTPICENAFTGMGIGAAMTGLRPVIEGMNMGFLLLAFNQISNNCGMLHYTSGGQFTIPVVIRGPGGVGRQLGAEHSQRLESYFQSIPGIQMVACSTPYNAKGLMKAAIRSENPVILFEHVLLYNLKEKIPDEDYVCNLEEAEMVRPGEHITILTYSRMRYHVMQAAKTLVNKGYDPEVIDIRSLKPFDLHTIGNSVKKTHRVLIVEECMRTGGIGASLTAAINENFHDYLDAPVMCLSSQDVPTPYAGTLEEWTVVQPAQIVTAVEQLCQ | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 44245
Sequence Length: 406
Subcellular Location: Plastid
EC: 1.2.4.1
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Q0J0H4 | MLGAARRQLGSGPMLGQVLRRLRPATAAAADAARAYSAAAKEMTVREALNSALDEEMSADPSVFLMGEEVGEYQGAYKISKGLLDKYGPERVLDTPITEAGFTGIAVGAAYQGLRPVVEFMTFNFSMQAIDHIINSAAKSNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCYAAWYAHVPGLKVLVPYSAEDARGLLKAAIRDPDPVVFLENELLYGESFPISAEVLDSSFALPIGKAKIEREGKDVTITAYSKMVGYALQAADILSKEGISAEVINLRSIRPLDRATINASVRKTNRLVTIEESFPQHGIGAEICMSVVEESFEYLDAPVERIAGADVPMPYAANLERMAVPQVDDIVRAAKRACYRAVPMAATA | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 40251
Sequence Length: 376
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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Q2QM55 | MATAAAASLQYALHGAASASAKPRSAAPGRSVRVVAARRSVRARGGAVVARAAVTASADATAESKSGGHEVLLFEALREALIEEMKEDPTVCVFGEDVGHYGGSYKVTKGLAEMFGDLRVLDTPIAENSFAGMGVGAAMKGLRPIVEGMNMGFLLLAYNQISNNCGMLHYTSGGQFKIPIVIRGPGGVGRQLGAEHSQRLESYFQSIPGLQMVACSTPYNAKGLMKAAIRSENPVVLFEHVLLYNLKEKIPDEEYICCLEEAEMVRPGEHVTILTYSRMRYHVMQAAKTLVNKGYDPEVIDIRSLKPFDLHTIGNSIKKTHRVLIVEECMRTGGIGASLRSAIIDNFWDYLDAPIMCLSSQDVPTPYAATLEDATVVQPAQIVAAVEQICQ | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 42121
Sequence Length: 391
Subcellular Location: Plastid
EC: 1.2.4.1
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P35488 | MAIITLLEAINQAIDQAMEKDESIVVFGEDAGFEGGVFRVTAGLQKKYGETRVFDTPIAESAIVGSAVGMAINGLKPIAEIQFDGFIFPGYTDLVTHAARMRNRSRGQFTVPMVLRLPHGGGIRALEHHSEALEVLFGSIPGLKVVTPSTPYDAKGLLLAAINDPDPVVFLEPKRIYRAGKQEVPAEMYEIPIGKAKVVKQGTDMTVVAWGSIVREVEKAVKLVEAEGISVEIIDLRTISPIDEETILNSVKKTGKFMVVTEAVKSYGPAAELITMVNEKAFFHLEAAPVRFTGFDITVPLARGEHYHFPQPEKIAAYIRKLAKARP | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 35682
Sequence Length: 327
EC: 1.2.4.1
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P26269 | MAVNGCMRLLRNGLTSACALEQSVRRLASGTLNVTVRDALNAALDEEIKRDDRVFLIGEEVAQYDGAYKISKGLWKKYGDGRIWDTPITEMAIAGLSVGAAMNGLRPICEFMSMNFSMQGIDHIINSAAKAHYMSAGRFHVPIVFRGANGAAVGVAQQHSQDFTAWFMHCPGVKVVVPYDCEDARGLLKAAVRDDNPVICLENEILYGMKFPVSPEAQSPDFVLPFGQAKIQRPGKDITIVSLSIGVDVSLHAADELAKSGIDCEVINLRCVRPLDFQTVKDSVIKTKHLVTVESGWPNCGVGAEISARVTESDAFGYLDGPILRVTGVDVPMPYAQPLETAALPQPADVVKMVKKCLNVQ | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 39136
Sequence Length: 361
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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P21882 | MAQMTMIQAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLALGLGLNGFRPVMEIQFFGFVYEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLISAIRDNDPVVFLEHMKLYRSFRQEVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAADELEKDGISAEVVDLRTVSPLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFPFSQAESVWLPNHKDVLETARKVLEF | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 35474
Sequence Length: 325
EC: 1.2.4.1
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O44451 | MALRKCGNLFVARLAGTSTRAASTMTVRDALNQAMDEEIKRDDRVFLMGEEVAQYDGAYKISKGLWKKHGDKRVVDTPITEMGFAGIAVGAAFAGLRPICEFMTFNFSMQAIDQIINSAAKTYYMSAGRVPVPIVFRGPNGAAAGVAAQHSQDFSAWYAHCPGLKVVCPYSAEDAKGLLKAAIRDDNPVVFLENEILYGQSFPVGDEVLSDDFVVPIGKAKIERAGDHVTIVSYSRGVEFSLEAAKQLEAIGVSAEVINLRSLRPFDFESIRQSVHKTHHLVSVETGWPFAGIGSEIAAQVMESDVFDQLDAPLLRVTGVDVPMPYTQTLEAAALPTAEHVVKAVKKSLNIA | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Mass (Da): 38141
Sequence Length: 352
Subcellular Location: Mitochondrion matrix
EC: 1.2.4.1
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P53397 | MSYKFGKLAINKSELCLANVLQAGQSFRWIWDEKLNQYSTTMKIGQQEKYSVVILRQDEENEILEFVAVGDCGNQDALKTHLMKYFRLDVSLKHLFDNVWIPSDKAFAKLSPQGIRILAQEPWETLISFICSSNNNISRITRMCNSLCSNFGNLITTIDGVAYHSFPTSEELTSRATEAKLRELGFGYRAKYIIETARKLVNDKAEANITSDTTYLQSICKDAQYEDVREHLMSYNGVGPKVADCVCLMGLHMDGIVPVDVHVSRIAKRDYQISANKNHLKELRTKYNALPISRKKINLELDHIRLMLFKKWGSYAGWAQGVLFSKEIGGTSGSTTTGTIKKRKWDMIKETEAIVTKQMKLKVELSDLHIKEAKID | Function: DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 42781
Sequence Length: 376
Subcellular Location: Nucleus
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P21258 | MAKGKKLSFSFHTYQDSVTGTEVVRLTPPDVICHRNYFYQKCFSNDGSKLLFGGAFDGPWNYYLLDLKTQQATQLTEGTGDNTFGGFLSPDDDALYYVKNVRNLMRVDLNTLEETNIYQVPDDWVGYGTWVANSDCTKMVGIEIKKEDWKPLTDWKKFQEFYFTNPCCRLIRIDLKTGEATTILKENQWLGHPIYRPGDDNTVAFCHEGPHDLVDARMWFINEDGSNMRKVKEHAPGESCTHEFWVPNGSALAYVSYLKGSTNRFICSVDPVTLENRQLTEMPPCSHLMSNYDGTLMVGDGCNAPVDVKDDGGYKIENDPFLYVFNMKTGKHFQVAQHNTSWEVLEGDRQVTHPHPSFTPDDKHILFTSDVDGKPALYLAKVPDSVWQ | Function: Involved in degradation of pectin, which causes soft-rod disease in plants.
Catalytic Activity: 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate
Sequence Mass (Da): 44186
Sequence Length: 388
Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 3/5.
Subcellular Location: Periplasm
EC: 4.2.2.6
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Q15743 | MGNITADNSSMSCTIDHTIHQTLAPVVYVTVLVVGFPANCLSLYFGYLQIKARNELGVYLCNLTVADLFYICSLPFWLQYVLQHDNWSHGDLSCQVCGILLYENIYISVGFLCCISVDRYLAVAHPFRFHQFRTLKAAVGVSVVIWAKELLTSIYFLMHEEVIEDENQHRVCFEHYPIQAWQRAINYYRFLVGFLFPICLLLASYQGILRAVRRSHGTQKSRKDQIQRLVLSTVVIFLACFLPYHVLLLVRSVWEASCDFAKGVFNAYHFSLLLTSFNCVADPVLYCFVSETTHRDLARLRGACLAFLTCSRTGRAREAYPLGAPEASGKSGAQGEEPELLTKLHPAFQTPNSPGSGGFPTGRLA | Function: Proton-sensing receptor involved in pH homeostasis. May represents an osteoblastic pH sensor regulating cell-mediated responses to acidosis in bone. Mediates its action by association with G proteins that stimulates inositol phosphate (IP) production or Ca(2+) mobilization. The receptor is almost silent at pH 7.8 but fully activated at pH 6.8. Also functions as a metastasis suppressor gene in prostate cancer (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41077
Sequence Length: 365
Subcellular Location: Cell membrane
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O34777 | MENKFDHMKLENQLCFLLYASSREMTKQYKPLLDKLNITYPQYLALLLLWEHETLTVKKMGEQLYLDSGTLTPMLKRMEQQGLITRKRSEEDERSVLISLTEDGALLKEKAVDIPGTILGLSKQSGEDLKQLKSALYTLLETLHQKN | Function: Organic peroxide sensor . Represses the expression of the peroxide-inducible gene ohrA by cooperative binding to two inverted repeat elements .
PTM: Cys-15 is oxidized by organic peroxides to cysteine sulfenic acid (Cys-SOH). This can react with the alpha-amido of the following residue to form the sulfenamide cross-link. Oxidation or cross-linking results in the loss of DNA-binding activity and the inactivation of repressor function. Both the cysteine sulfenic acid and the sulfenamide cross-link can react with free cysteine or bacillithiol (BSH) to form mixed disulfides. Further reduction of OhrR by free sulfhydryl compounds restores repressor activity.
Sequence Mass (Da): 17003
Sequence Length: 147
Subcellular Location: Cytoplasm
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Q6D8V4 | MAIGLSTYAFFWRASSRVPNPLGLAAMLEQTAESGAGVFQICDYAAVEALSPAELEKLRQRAVDLGIQLELGTRGLATDHLTRYLTMARALDVRFIRTMFNSATHKPTQDEALALLRCVLPEFEQYNIQLGLETYEQVKTRDVLAVVDAIDSPALGICLDPGNCVAALEYPHEVIELTASRVVNLHIKDFAFARQEGWVGFTYSGCLLGTGLLDYDALHQTIRPNERNINQIVEHWLPWQASAEETCRLEDAWTRHSLNYLYTRNPYANRSSHIL | Function: Involved in catabolism of D-apiose. Catalyzes decarboxylation of 3-oxo-isoapionate to L-erythrulose.
Catalytic Activity: 3-oxoisoapionate + H(+) = CO2 + L-erythrulose
Sequence Mass (Da): 30871
Sequence Length: 275
Pathway: Carbohydrate metabolism.
EC: 4.1.1.120
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B1G889 | MNGTEPAEPTNGTNATAWPAGLLLAYYGDDFTGSTDAMEAMQAAGVPTVLCLQKPTPELLARFPEVRCVGMAGSSRGRSSAWMDDELPDVLASLAALGAPILQYKVCSTFDSSPEVGSIGRAIDIGVRHMPGNWSPMVIGAPRLKRYQMFGNLFAAVDGVGYRLDRHPTMSRHPVTPMNEADLRLHLARQTARRIELIDMLELRGADVATRVRALCAPDMPVVLIDVLDEETLAEAGRLVWEQRGEGIFTASSSGLQYALAAHWRARGLLPPTPSLPAADPVQAIAAVSGSCSPVTAAQIGWARAHGFHTERLDLPRALDSRDGAAEIERVVTAATQALTRGISVIVHSAEGPDDPAVTGFDAIASAAGFARHDAARKVGRALAEVMRRLLDSVELTRVVVAGGDSSGEVASVLGIDALSVMAGLVPGAPLCRAWSAEPRRDGLQIVLKGGQIGDATFFGMVREGRLAGA | Function: Involved in catabolism of D-apiose. Catalyzes the phosphorylation of 3-oxo-isoapionate to 3-oxo-isoapionate 4-phosphate.
Catalytic Activity: 3-oxoisoapionate + ATP = 3-oxoisoapionate 4-phosphate + ADP + H(+)
Sequence Mass (Da): 49606
Sequence Length: 470
Pathway: Carbohydrate metabolism.
EC: 2.7.1.231
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A7IJG7 | MSERVYATYWMETGGDPARTAEVIAGEQSSGTFVALATETAELKERSGARVERLDILDTADIPSLPGGMASDRYTRAILELSWPVENFGPSLPNLMSTIAGNLFELHQVSGLRLIDLKLPPSFTNAFAGPAFGIAGTRKLAGVAQGPIIGTIIKPSIGLTPEETAQQVRELIAGDIDFIKDDELQADGARCPFEARVKAVMRVVNDAADRRGRKVMVAFNITGDLDEMRRRHDLVLAEGGTCVMVCLNSIGLVGVREIRRHTQLPIHGHRAGWGYLYRCPSLGWDYAPWQQLWRLAGVDHLHVNGLDNKFSEANASVIAAARAVLSPLNHAAPMGAMPVFSSGQTGRQAAETYAAIGCADLIHTAGGGIFGHPAGVPAGVEALRAAWRAAMAGASLEDEATRSPALRSALGFWR | Function: Involved in catabolism of D-apiose. Catalyzes the conversion of 3-oxo-isoapionate 4-phosphate to 3-phosphoglycerate and glycolate.
Catalytic Activity: 3-oxoisoapionate 4-phosphate + H2O = (2R)-3-phosphoglycerate + glycolate + H(+)
Sequence Mass (Da): 44329
Sequence Length: 414
Pathway: Carbohydrate metabolism.
EC: 3.7.1.28
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B9JK73 | MSITITYRIETPGSIEAMADKIASDQSTGTFVPVPGETEELKSRVAARVLGIRQLEDAKRPTWPEVAEGHGPLRRADVDIAFPLDAIGTDLSALMTIAIGGVFSIKGMTGIRIVDMKLPNAFRGAHPGPQFGVAGSKRLTGVEGRPIIGTIVKPALGLRPVETAELVGELINSGVDFIKDDEKLMSPAYSPLKERVAAIMPRILDHEQKTGKKVMYAFGISHADPDEMMRNHDLVLEAGGNCAVVNINSIGFGGMSFLRKRSGLVLHAHRNGWDVLTRDPGAGMDFKVYQQFWRLLGVDQFQINGIRVKYWEPDESFIESFKAVSTPLFDPSDCPLPVAGSGQWGGQAPETYQRTGRTTDLLYLCGGGIVSHPSGPAAGVRAVQQAWEAAVADIPLANYAKDHPELAASIAKFSDGKGA | Function: Involved in catabolism of D-apiose. Catalyzes the decarboxylation of 3-oxo-isoapionate 4-phosphate to L-erythrulose 1-phosphate.
Catalytic Activity: 3-oxoisoapionate 4-phosphate + H(+) = CO2 + L-erythrulose 1-phosphate
Sequence Mass (Da): 45085
Sequence Length: 419
Pathway: Carbohydrate metabolism.
EC: 4.1.1.121
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Q13516 | MDSDASLVSSRPSSPEPDDLFLPARSKGSSGSAFTGGTVSSSTPSDCPPELSAELRGAMGSAGAHPGDKLGGSGFKSSSSSTSSSTSSAAASSTKKDKKQMTEPELQQLRLKINSRERKRMHDLNIAMDGLREVMPYAHGPSVRKLSKIATLLLARNYILMLTNSLEEMKRLVSEIYGGHHAGFHPSACGGLAHSAPLPAATAHPAAAAHAAHHPAVHHPILPPAAAAAAAAAAAAAVSSASLPGSGLPSVGSIRPPHGLLKSPSAAAAAPLGGGGGGSGASGGFQHWGGMPCPCSMCQVPPPHHHVSAMGAGSLPRLTSDAK | Function: Required for oligodendrocyte and motor neuron specification in the spinal cord, as well as for the development of somatic motor neurons in the hindbrain. Functions together with ZNF488 to promote oligodendrocyte differentiation. Cooperates with OLIG1 to establish the pMN domain of the embryonic neural tube. Antagonist of V2 interneuron and of NKX2-2-induced V3 interneuron development.
Sequence Mass (Da): 32385
Sequence Length: 323
Domain: The bHLH is essential for interaction with NKX2-2.
Subcellular Location: Nucleus
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Q9EQW6 | MDSDASLVSSRPSSPEPDDLFLPARSKGGSSSGFTGGTVSSSTPSDCPPELSSELRGAMGASGAHPGDKLGGGGFKSSSSSTSSSTSSAATSSTKKDKKQMTEPELQQLRLKINSRERKRMHDLNIAMDGLREVMPYAHGPSVRKLSKIATLLLARNYILMLTNSLEEMKRLVSEIYGGHHAGFHPSACGGLAHSAPLPTATAHPAAAAHAAHHPAVHHPILPPAAAAAAAAAAAAAVSSASLPGSGLSSVGSIRPPHGLLKSPSAAAAAPLGGGGGGSGGSGGFQHWGGMPCPCSMCQVPPPHHHVSAMGAGTLPRLTSDAK | Function: Required for oligodendrocyte and motor neuron specification in the spinal cord, as well as for the development of somatic motor neurons in the hindbrain . Functions together with ZNF488 to promote oligodendrocyte differentiation . Cooperates with OLIG1 to establish the pMN domain of the embryonic neural tube . Antagonist of V2 interneuron and of NKX2-2-induced V3 interneuron development .
Sequence Mass (Da): 32407
Sequence Length: 323
Domain: The bHLH is essential for interaction with NKX2-2.
Subcellular Location: Nucleus
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Q00650 | MGILRKKKHERNASFKSVLTSILATQAATFLLLISGVSLAGTAAAFIATMPLFVVFSPILVPAGITTGLLTTGLAAAGGAGATAVTIILWLYKRATGKEPPAVLSKVLKKIIPGAAAAPRAAPAAAPAAAPAAAPAAAPAPKPAAAPAPKPAAPPAL | Function: Many of the major pollen coat proteins are derived from endoproteolytic cleavage of oleosin-like proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15309
Sequence Length: 157
Subcellular Location: Lipid droplet
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P29526 | QASIFSRFFRMFSFIFPFVNVIKLIIASVTSLVCLAFSCVALGGSAVALIVSTPLFIMFSPILVPATIATTLLASGLMAGTTLGLTGIGLIMGLVRTAGGVSLLQSPLRKIIVNRIKARLGGGGGGSRLARLKKILGLLNKLRGMGAGGAAAPAAEPAPAAEAAPAAEAAPAAAPAAAPAAAP | Function: Many of the major pollen coat proteins are derived from endoproteolytic cleavage of oleosin-like proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18149
Sequence Length: 183
Subcellular Location: Lipid droplet
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Q42626 | MRNEIQNETAQTDQTQGSMFSFFNLFPFLLPMFEVIKMVVASVASVVYLGFAGVTLSGSAVALAVSTPLFIIFSPILLPAIAATTVLAAGLGSKKVAAAPAASPSLSLLGIPESIKPSNVIPESIKPSNIIPESIKPSNIIPVSIKPSNIKDKIKDTIGKVKNKIKAKQEEKSKGKSEDSSKGKGKSKGEDTTTDEDKHGKGESKHGKGESKHGKGESTHGKGGKHGSEGSSMDEGKHGGKHGSGGSPMGGGKHGSGGKHESGGSPMGGGKHGSGGKHESGGASMGGGKHESVGKHGSGGKHESGGSPMGGGKHGSGGKHESGGASMGGGKHGSGGRHEGGGSAMGGGKHGSGGKHGSEGKHGGEGSSMGKNSLSKNKKEFHYRGQAMDASSTSESSDGSSSDGSSSDGSSSDGSSHGSGGKHI | Function: Many of the major pollen coat proteins are derived from endoproteolytic cleavage of oleosin-like proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42086
Sequence Length: 424
Subcellular Location: Lipid droplet
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Q42627 | MRNEIQNETAQTDQTQGSMFSFFNLFPFLLPMFEVIKMVVASVASVVYLGFAGVTLSGSAVALAVSTPLFIIFSPILLPAIAATTVLAAGLGGKKVAAAPEASPAASPSLSLLGIPESIKPSNIIPESIKPSNIIPEGIKPSNIKDKIKDTIGKVKNKIKAKKEEKSKGKSEDSSKGKGKSKGEDTTTDDDTTTDEDKHGSGAKHGKGESKHGKGESTHGKGGKHGSEGKHGSGGSSMGGGKHGSGGKHETGGKHGSGGKHESGGSPMGGGKHGSEGKHGSGGASMGGGKHGSGGKHESGGSAMGGGKHGSGGKHGSEGKHGGEGSSMGKNSLSKKKKEFHYRGQAMDASSTSESSDGSSDGSSSDGSSHGSGGKHI | Function: Many of the major pollen coat proteins are derived from endoproteolytic cleavage of oleosin-like proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37647
Sequence Length: 377
Subcellular Location: Lipid droplet
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Q43402 | MKEEIQNETAQTQLQREGRMFSFLFPVIEVIKVVMASVASVVFLGFGGVTLACSAVALAVSTPLFIIFSPILVPATIATTLLATGLGAGTTLGVTGMGLLMRLIKHPGKEGAASAPAAQPSFLSLLEMPNFIKSKMLERLIHIPGVGKKSEGRGESKGKKGKKGKSEHGRGKHEGEGKSKGRKGHRMGVNPENNPPPAGAPPTGSPPAAPAAPEAPAAPAAPAAPAAPAAPAAPAAPEDPAAPAAPEAPATPAAPPAPAAAPAPAAPAAPPAPAAPPRPPSFLSLLEMPSFIKSKLIEALINIPGFGKKSNDRGKSKGGKKSKGKGKSNGRGKHEGEGKSKSRKSKSRGKDKEKSKGKGIFGRSSRKGSSDDESS | Function: Many of the major pollen coat proteins are derived from endoproteolytic cleavage of oleosin-like proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37993
Sequence Length: 375
Subcellular Location: Lipid droplet
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P30691 | MKKSLIALTLAALPVAAMADVTLYGTIKAGVETYRTVKHTDGKVTEVKTGSEIADFGSKIGFKGQEDFGNGLKAIWQLEQSASIAGTNSGWGNKQSFIGLKGGFGTVRAGNLNSILKSTGDNVNAWESGKATEDVLQVSKISAPEHRYASVRYDSPEFAGFSGSVQYAPKDNSGANGESYHVGLNYQNSGFFAQYAGLFQRHGEGTKATVGEPVEKLQVHRLVGGYDNDALYASVAVQQQDAKLAAAPNSHNSQTEVAATVAYRFGNVTPRVSYAHGFKGTVAKADGDNRYDQVVVGAEYDFSKRTSALVSAGWLQEGKGAGKTVSTASTVGLRHKF | Function: Serves as a slightly cation selective porin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35710
Sequence Length: 337
Subcellular Location: Cell outer membrane
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Q8CVW1 | MKVKVLSLLVPALLVAGAANAAEVYNKDGNKLDLYGKVDGLHYFSDDKSVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNAPESENNSWTRVAFAGLKFQDIGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGQNGSVSGENDPDFTGHGITNNGRKALRQNGDGVGGSITYDYEGFGVGAAVSSSKRTWDQNNTGLIGTGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSVAYLQSKGKNLGVVAGRNYDDEDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRAAGINTDDIVALGLVYQF | Function: Forms pores that allow passive diffusion of small molecules across the outer membrane, including some antibiotics. Variation of the residues in the constriction zone modifies the transverse electric field in the zone, altering antibiotic resistance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41225
Sequence Length: 375
Subcellular Location: Cell outer membrane
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P06996 | MKVKVLSLLVPALLVAGAANAAEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGNPSGEGFTSGVTNNGRDALRQNGDGVGGSITYDYEGFGIGGAISSSKRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF | Function: Forms pores that allow passive diffusion of small molecules across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40368
Sequence Length: 367
Domain: Loop L3 (residues 116-133) extends along the inner side of the beta barrel wall and may constrict the pore mid-length.
Subcellular Location: Cell outer membrane
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P09888 | MQPAKNLLFSSLLFSSLLFSSAARAASEDGGRGPYVQADLAYAAERITHDYPKPTGTGKNKISTVSDYFRNIRTHSVHPRVSVGYDFGSWRIAADYARYRKWNNNKYSVSIKELLRNDNSASGVRGHLNIQTQKTEHQENGTFHAVSSLGLSTIYDFDTGSRFKPYIGMRVAYGHVRHQVRSVEQETEIITTYPSNGGGKVSLSSKMPPKSAHHQSNSIRRVGLGVIAGVGFDITPNLTLDTGYRYHNWGRLENTRFKTHEASLGMRYRF | Function: This protein serves as a porin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30269
Sequence Length: 270
Subcellular Location: Cell outer membrane
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A0A0C1C354 | MARKFGRRFRRNSRASLPSLKFLTLGSTDSVFGPHNQQHREEEANAPQEIALKPVEENVQTLLGSEGDVECRAPPQQQDYAPTWKCVAIMIALCLAVLCMALDNTILATAIPKITEEFNSVHDMGWYVSAYMLAQSSMTLVYGKLLTYYTVKWVYIAALLLFEGGSLICGVSPNSIALIIGRAISGTGGSGILVSSFLIVTIIVPVEKRPLYNGILSSLYAISGVFGPLLGGAFTDYATWRWCFYINLPVGGVTGFFILLLFRADKPTKQWPTGAVSQLLELDIIGLFLFIPALVSLLLVLQWGGSKYPWDDAHIIALIAVFGVTILAFAAVEYWQQDRATIPPSMIRNRDIWGSLLFTFCLSGSVIIFNYYLPIWFQSIKNASATMSGVMNIPLILAVALTSILSGWAVTTLGYYIPFMYATPVIASVGAGLLSTFKVSSAHPAWIGFQILYGIGVGLGFGLPLVVVQATLTAHTISSGTALVTLTQGLAGALFNFVAQSVFQTKLVQALFAEAPSLDAGKIAEAGATVVRDIVDPDMVPAVLRAYNYAITRVYLVGAALAAAALLGVVPIRWGSVKGKKIEAGAA | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of oxepinamides, derivatives of anthranilyl-containing tripeptides that share an oxepin ring and a fused pyrimidinone moiety.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63189
Sequence Length: 587
Subcellular Location: Membrane
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A0A0C1EFK1 | MGPLRVFTDNKVKVMLLNPIGGAGFNDFVVETVLNHKDPSTHVTITSLANRIGGNQTLAYPSIRPLLYGEMIRVCLQARKENYDVLIINCFGDPMVDELQQIAGDDMVILGARQVAVQTASKISSKYAVLLPYDMKSSPDPLHQRVVADTRTAVAHPVVDMAFNDDLTPMDGESLGERLATQGKLAIKENGAEVLVLGCTAMVGCWQGLMRAVGVPVIDPTVAALRAAGKAGRLKRELVGGASTKRSGTFPTEKELKMIAESEPSYPFSGRIEI | Function: Epimerase; part of the gene cluster that mediates the biosynthesis of oxepinamides, derivatives of anthranilyl-containing tripeptides that share an oxepin ring and a fused pyrimidinone moiety . The nonribosomal peptide synthetase (NRPS) opaA assembles the quinazolinone core with D-Phe incorporation . The first adenylation domain (A1) of opaA loads and activates anthranilic acid whereas the second A domain (A2) is for activating of L-Phe, which is then converted to D-form by the E domain . The third A domain (A3) is responsible for L-Ile activation and the terminal condensation domain C3 for cyclization and releasing the NRPS product protuboxepin K . The cytochrome P450 monooxygenase opaB then catalyzes alone the oxepin ring formation to convert protuboxepin K into protuboxepin A . The flavoenzyme opaC installs subsequently one hydroxyl group at the oxepin ring, accompanied by double bond migration, to form 15-epi-oxepinamide E . The epimerase opaE changes the D-Phe residue back to L-form, leading to oxepinamide E, which is further methylated at the hydroxyl group at C-12 by the O-methyltransferase OpaF to yield oxepinamide F .
Sequence Mass (Da): 29551
Sequence Length: 274
Pathway: Secondary metabolite biosynthesis.
EC: 5.1.-.-
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A0A0C1E5J2 | MARGAAELTQTRKVMIKEQLANLTALIDLRIADTPCNGLDDDMPMQPAIDNTITHELAKETYALLHAIKGPSLSVFNFGEQVMHVSAVRALFGLGVFSALPQDRQAMTATALAEKLGCDEELLVRLMRMCTIWGPFKEVGTETYSHTQFSLAYLDPQVTNQFQAFVDEFLPACLQLHKFLEINNGKPPVDATNCPYTLAHQTSGKDMWEHLAQFPKRSKVVNSAMYAISSAHPWPVALYPFREALLQLPPTSSNAPLVIDIGGGQGQAISVIRKMCGGINGRFILEDRPEVLAGIPHTLRGIEKIECDLFKPQPVKGAAIYFLRHVLHDWAEDACVRILQNIASAITDKSTQRVVISEMVLPEKGVTAECATQDLVTLSTTGAERSRKQWERLIPAAGFRVENIYSSEASCEAAIECYLE | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of oxepinamides, derivatives of anthranilyl-containing tripeptides that share an oxepin ring and a fused pyrimidinone moiety . The nonribosomal peptide synthetase (NRPS) opaA assembles the quinazolinone core with D-Phe incorporation . The first adenylation domain (A1) of opaA loads and activates anthranilic acid whereas the second A domain (A2) is for activating of L-Phe, which is then converted to D-form by the E domain . The third A domain (A3) is responsible for L-Ile activation and the terminal condensation domain C3 for cyclization and releasing the NRPS product protuboxepin K . The cytochrome P450 monooxygenase opaB then catalyzes alone the oxepin ring formation to convert protuboxepin K into protuboxepin A . The flavoenzyme opaC installs subsequently one hydroxyl group at the oxepin ring, accompanied by double bond migration, to form 15-epi-oxepinamide E . The epimerase opaE changes the D-Phe residue back to L-form, leading to oxepinamide E, which is further methylated at the hydroxyl group at C-12 by the O-methyltransferase OpaF to yield oxepinamide F .
Sequence Mass (Da): 46354
Sequence Length: 420
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
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Q7M750 | MSFSLNFTLPSNTTSSPVVTSAKATDCGPSIGLAAGIPSLLATALLVALLFTLIQRRRTIDDEPVEETEIPCEISELYDNPKISENPRRSPTHEMNPRGSQEGHIYVKTVSGSEEPLPDTYRPPEELERRRGLWWLVPSLSLE | Function: Central nervous system-specific myelin protein that increase myelin genes expression during oligodendrocyte differentiation. Promotes oligodendrocyte terminal differentiation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 15833
Sequence Length: 143
Subcellular Location: Cell membrane
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Q8Z765 | MNRRRFIKGSMAMAAVCGSSGIASLFSQAAFAAESDIADGKIVRFDFAGLQSMAQALAKKPWGGAPGPLPDTLANLTPQAYNSIQYDAAHSLWNGVANRQLDIQFFHVGMGFRRRVRMFSVDTTTHLAREIHFRPELFKYNDAGVDTTQLEGQSDLGFAGFRVFKAPELARRDVVSFLGASYFRAVDDTYQYGLSARGLAIDTYTDGQEEFPDFTAFWFDTAKPGDTTFTVYALLDSASVTGAYKFVIHCEKTQVIMDVENHLYARKDIKQLGIAPMTSMFSCGNNERRVCDTIHPQIHDSDRLAMWRGNGEWICRPLNNPQKLQFNAYMDDNPKGFGLLQLDRDFSHYQDVMGWYNKRPSLWVEPRSKWGKGAVSLMEIPTTGETLDNVVCFWQPEKAIKAGDTLAFNYRLYWSAQPPVQSPLARVMATRTGMGGFPEGWAPGEHYPDKWARRFAIDFVGGDLKAAAPKGIEPVITLSSGEAKQVEILYVEPFDGYRIQFDWYPTSDSTAPVDMRMFLRCQGEAISETWLYQYFPPAPDKRRYVDDRIMR | Function: Probably involved in the control of the structural glucose backbone of osmoregulated periplasmic glucans (OPGs).
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 62199
Sequence Length: 551
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Periplasm
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Q83R85 | MDRRRFIKGSMAMAAVCGTSGIASLFSQAAFAADSDIADGQTQRFDFSILQSMAHDLAQTAWRGAPRPLPDTLATMTPQAYNSIQYDAEKSLWHNVENRQLDAQFFHMGMGFRRRVRMFSVDPATHLAREIHFRPELFKYNDAGVDTKQLEGQSDLGFAGFRVFKAPELARRDVVSFLGASYFRAVDDTYQYGLSARGLAIDTYTDSKEEFPDFTAFWFDTVKPGATTFTVYALLDSASITGAYKFTIHCEKSQVIMDVENHLYARKDIKQLGISPMTSMFSCGTNERRMCDTIHPQIHDSDRLSMWRGNGEWICRPLNNPQKLQFNAYTDNNPKGFGLLQLDRDFSHYQDIMGWYNKRPSLWVEPRNKWGKGTIGLMEIPTTGETLDNIVCFWQPEKAVKAGDEFAFQYRLYWSAQPPVHCPLARVMATRTGMGGFPEGWAPGEHYPEKWARRFAVDFVGGDLKAAAPKGIEPVITLSSGEAKQIEILYIEPIDGYRIQFDWYPTSDSTDPVDMRMYLRCQGDAISETWLYQYFPPAPDKRQYVDDRVMS | Function: Probably involved in the control of the structural glucose backbone of osmoregulated periplasmic glucans (OPGs).
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 62784
Sequence Length: 551
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Periplasm
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P46025 | MKKTLAALIVGAFAASAANAAVVYNNEGTNVELGGRLSIITEQSNSTVDDQEQQHGALRNAGSRFHIKATHNFGDGFYAQGYLETRLVSDYPESSSDHFGGITTKYAYVTLGNKAFGEVKLGRAKTIADGITSAEDKEYGVLNNKKYIPTNGNTVGYTYKGIDGLDGLVLGANYLLAQSRVPGGPSPFPRKQGEVYPQQISNGVQVGAKYDANNIIAGIAFGRTNYKTAGADFDPYGDFGLGRKEQVEGVLSTLGYRFSDLGLLVSLDSGYAKTKYYTTTDSSSGSQTITNPAYDEKRSFVSPGFQYELMEDTNVYGNFKYERTSVNQGKNTREQAVLFGVDHKLHKQVLTYIEGAYARTKTNDKGKTEKTGKEKSVGVGLRVYF | Function: Forms pores that allow passive diffusion of small molecules across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41787
Sequence Length: 385
Subcellular Location: Cell outer membrane
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P24141 | MKKRWSIVTLMLIFTLVLSACGFGGTGSNGEGKKDSKGKTTLNINIKTEPFSLHPGLANDSVSGGVIRQTFEGLTRINADGEPEEGMASKIETSKDGKTYTFTIRDGVKWSNGDPVTAQDFEYAWKWALDPNNESQYAYQLYYIKGAEAANTGKGSLDDVAVKAVNDKTLKVELNNPTPYFTELTAFYTYMPINEKIAEKNKKWNTNAGDDYVSNGPFKMTAWKHSGSITLEKNDQYWDKDKVKLKKIDMVMINNNNTELKKFQAGELDWAGMPLGQLPTESLPTLKKDGSLHVEPIAGVYWYKFNTEAKPLDNVNIRKALTYSLDRQSIVKNVTQGEQMPAMAAVPPTMKGFEDNKEGYFKDNDVKTAKEYLEKGLKEMGLSKASDLPKIKLSYNTDDAHAKIAQAVQEMWKKNLGVDVELDNSEWNVYIDKLHSQDYQIGRMGWLGDFNDPINFLELFRDKNGGNNDTGWENPEFKKLLNQSQTETDKTKRAELLKKAEGIFIDEMPVAPIYFYTDTWVQDENLKGVIMPGTGEVYFRNAYFK | Function: This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, It binds peptides up to five amino acids long with high affinity. Also required for sporulation and competence.
Location Topology: Lipid-anchor
Sequence Mass (Da): 61525
Sequence Length: 545
Subcellular Location: Cell membrane
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Q9CEK0 | MKKLKVTLLASSVVLAAALLSACGSNQNSSTSTKKLKAGNFDVAYQNPDKAIKGGNLKIAYQSDSPMKAEWLAPLSDDATFGSMSSPGGGQDGLFFTNSSFKYINGGPANVSLYKDAKTATITLRKDLKWSDGSEVTAKDYEFSYDLTANPAYGSDRWTDSLANIVGLSDYHAGKAKTISGITFPDGENGKVIKVQFKEMTPGMNQTGNGYFLETVAPYQYLKDVAPKDLASSPKSTTKPLVTGPFKPENVVAGESIKYVPNPYYWGEKPKLNSITYEIVSTAKSVAALSAHKYDYINDMRASQYKQVKDVKGYKVLGQQELYISLMYYNLGHYDVKKSISVQDRKTPLQDQNVREALGYARNVAAVQAKFSNGLATPANGLIPPIFKEFTSPSVKGYEKQDLDKANKLLDEDGWKLNKSTGYREKDGKELSLVYAARVGDANSETIAQNYIQQWKKIGVKVSLYHGKLMEFNSWVDHMTTPPGSDDWDITDGAWSLSGEPSQQDLFSAAAPYNFGHFNDPEITKDLNDIDSTKAEDSTYRKAAFIKYQEDMNKKAYVVPTAYAINYTPVNKRVVGMTLDYGAMNTWSEIGVSSDKMATK | Function: This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, it binds peptides up to five amino acids long with high affinity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 66045
Sequence Length: 600
Subcellular Location: Cell membrane
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P22328 | MNGTEGQDFYVPMSNKTGVVRSPFEYPQYYLAEPWKFSALAAYMFMLILLGFPVNFLTLYVTIQHKKLRTPLNYILLNLVVADLFMVFGGFTTTMYTSMNGYFVFGVTGCYIEGFFATLGGEIALWSLVVLAVERYVVVCKPMSNFRFGENHAIMGVAFSWIMAMACAAPPLFGWSRYIPEGMQCSCGIDYYTLKPEINNESFVIYMFVVHFMIPLAVIFFCYGNLVCTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTNQGSDFGPIFMTIPAFFAKSSAIYNPVIYIVMNKQFRNCMITTLCCGKNPLGDEDTSAGKTETSSVSTSQVSPA | Function: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity).
PTM: Contains one covalently linked retinal chromophore. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. After hydrolysis of the Schiff base and release of the covalently bound all-trans-retinal, active rhodopsin is regenerated by binding of a fresh molecule of 11-cis-retinal.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39327
Sequence Length: 351
Subcellular Location: Membrane
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Q90305 | CGIDYYTRAPGYNNESFVIYMFIVHFLIPLFIISFCYGNLLCAVKAAAAAQEESETTQRAEREVTRMVIMMVISYLVSWVPYASVAWYIFSNQGSEFGPVFMTIPAFFAKSSALYNPLIYVLMNKQFRHCM | Function: Photoreceptor required for image-forming vision at low light intensity. While most salt water fish species use retinal as chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of retinal and 3-dehydroretinal (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity).
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15037
Sequence Length: 131
Subcellular Location: Membrane
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O42307 | YLVNPAAYAALGAYMFLLILIGFPINFLTLYVTLEHKKLRTPLNYILLNLAVGNLFMVLGGFTTTMYTSMHGYFVLGRLGCNLEGFFATLGGEIALWSLVVLAIERWIVVCKPISKFRFTEDHAIMGLAFSWVMGLACAVPPLVGWSRYIPEGMKCSCGVDYYTRAEGFNNESFVIYMFIVHFLIPLSVIFFCYGRLLCAVKEAAAAQQESETTQRAEKEVSRMVVIMVIGFLVCWLPYASVAWWIFCNQGSDFGPIFMTLPSFFAKRPAIYNPMIYICMNKQFRHCMI | Function: Photoreceptor required for image-forming vision at low light intensity. While most salt water fish species use retinal as chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of retinal and 3-dehydroretinal (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity).
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32753
Sequence Length: 289
Subcellular Location: Membrane
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P35359 | MNGTEGPAFYVPMSNATGVVRSPYEYPQYYLVAPWAYGLLAAYMFFLIITGFPVNFLTLYVTIEHKKLRTPLNYILLNLAIADLFMVFGGFTTTMYTSLHGYFVFGRLGCNLEGFFATLGGEMGLWSLVVLAIERWMVVCKPVSNFRFGENHAIMGVAFTWVMACSCAVPPLVGWSRYIPEGMQCSCGVDYYTRTPGVNNESFVIYMFIVHFFIPLIVIFFCYGRLVCTVKEAAAQQQESETTQRAEREVTRMVIIMVIAFLICWLPYAGVAWYIFTHQGSEFGPVFMTLPAFFAKTSAVYNPCIYICMNKQFRHCMITTLCCGKNPFEEEEGASTTASKTEASSVSSSSVSPA | Function: Photoreceptor required for image-forming vision at low light intensity. While most salt water fish species use retinal as chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of retinal and 3-dehydroretinal (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity).
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39706
Sequence Length: 354
Subcellular Location: Membrane
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P46921 | MDRLPRIPLADIIDRFVDWITMTFGGFFDGIANGLAAFVNGIVTGLGFIPSILLTIIFAALAWWISTRGIALFTLIGFLLIDYLGYWDPMLQTLALVLTSVIISIVVGVPIGIWASQKETVRRIVTPILDLMQTMPAFVYLLPAIFFFNIGVVPGVVASVIFAMPPTIRMTVLGIKQVPADLIEATEAFGSTTAQRLFKVQLPLATKTILAGINQSIMLALSMVVIAAMVGAPGLGSEVYSAVTQLKTGVGVEAGIAIVIVAITLDRITQNIKVKKKSRGNA | Function: Involved in a multicomponent binding-protein-dependent transport system for glycine betaine; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30247
Sequence Length: 282
Subcellular Location: Cell membrane
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P46922 | MLKKIIGIGVSAMLALSLAACGSENDENASAAEQVNKTIIGIDPGSGIMSLTDKAMKDYDLNDWTLISASSAAMTATLKKSYDRKKPIIITGWTPHWMFSRYKLKYLDDPKQSYGSAEEIHTITRKGFSKEQPNAAKLLSQFKWTQDEMGEIMIKVEEGEKPAKVAAEYVNKHKDQIAEWTKGVQKVKGDKINLAYVAWDSEIASTNVIGKVLEDLGYEVTLTQVEAGPMWTAIATGSADASLSAWLPNTHKAYAAKYKGKYDDIGTSMTGVKMGLVVPQYMKNVNSIEDLKK | Function: Involved in a multicomponent binding-protein-dependent transport system for glycine betaine.
Location Topology: Lipid-anchor
Sequence Mass (Da): 32215
Sequence Length: 293
Subcellular Location: Cell membrane
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Q45461 | MHHIVQFLQTNGGELLYKTYEHITISLIAVILGVLVAVPLGVVLTRMKKGAGTIIGIVNIIQTLPSLAILAFFIPLLGVGKVPAIVALFFYSVLPILRNTYTGIRGVNKNLLESGKGIGMTPAEQVRLVELPLAAPVIMAGIRTSTIYLIGWATLASFIGGGGLGDYIFIGLNLYQPEYIIGGAVPVTILAIVIDYVLAVAERKLTPAGMQRLKELS | Function: Involved in a high affinity multicomponent binding-protein-dependent transport system for choline; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23163
Sequence Length: 217
Subcellular Location: Cell membrane
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Q45462 | MKRKYLKLMIGLALAATLTLSGCSLPGLSAAADQTIKIGAQSMSESEIIASMLGQLIEHHTDLKTTTIKNLGSNAVQQQALMNGEIDIAATRYTGDALTGTLRMEPEKDPDKALALTQREFKKRYDLKWYDSYGFDNTYAFTVSKELADQYHLETVSDVKKWAPQLKLGVDNYWMKLKGNGYQDFTKTYGMTFGGTYPMQIGLVYDAVKSGKMDIVLAYSTDGRIKSYGLKMLKDDKQFFPPYDCSPVVPEKVLKEHPELEGIIKKMLGKIDTATMQELNYEVDGNLKEPSVVAKEYLEKHRYFES | Function: Member of a high affinity multicomponent binding-protein-dependent transport system for choline.
Location Topology: Lipid-anchor
Sequence Mass (Da): 34401
Sequence Length: 306
Subcellular Location: Cell membrane
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P39775 | MNVLEQLMTYYAQNGSYVMDEFGRHFLMSAYGVLFAAVVGVPAGILIAHFRRLSAWVFAVTNVIQTIPALAMLAVLMLVMGLGANTVILSLFLYSLLPIIRNTYTGIISIEHAYLESGKAMGMTKFQVLRMVELPLALSVIMAGLRTALVIAIGITAIGTFVGAGGLGDMIVRGSNATNGTAIILAGAIPTAVMAVGADLLMAWLERALSPVKKKRTGAKHVQSAA | Function: Involved in a high affinity multicomponent binding-protein-dependent transport system for choline; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23928
Sequence Length: 226
Subcellular Location: Cell membrane
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O34878 | MNQMMTFLQTNGGELLYKTGEHLYISLIAVVLGIIVAVPLGVALTRMKKGAGAVIGFVNIVQTLPSLAILAFFIPLLGVGKVPAIVALFFYSVLPILRNTYTGIKGVNKNLLESGKGIGMTGWEQIRLVEIPLAIPIIMAGIRTSTIYLIGWATLASFIGGGGLGDYIFIGLNLYQPEYIIGGAVPVTILAIIIDYVLAVTERKVTPKGLQGMKEVS | Function: Involved in a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine and choline; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23149
Sequence Length: 217
Subcellular Location: Cell membrane
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G2JZ42 | MKKKFIALFSVLLLTSSLFLSSCSLPGLGGSSKDTIRIGAMATTESQIVSNILKELIEHDTGLKVEIVNNLGSTIVQHQAMLNGDVDITATRYTGTDLVGPLGEEAIKDPEKALAAVKKGFEERFHQTWFDSYGFANTYVFMVRQDTAKKYNLNTVSDMRKVENELTAGVDNSWMEREGDGYKAFSKAYDIEFKKIFPMQIGLIYTALKNNQMDVALGYSTDGRIPTYNLKLLKDDKKFFPPYDASALATDEILKKHPELKTTINKLKGKISTEEMQKLNYEADGKLKEPSIVAQEFLQKNNYFEGKN | Function: Part of the ABC transporter complex OpuCABCD involved in carnitine uptake. Involved, with BetL and GbuABC, in osmoprotection and cryoprotection of Listeria. Can also mediate weak glycine betaine transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 34549
Sequence Length: 308
Subcellular Location: Cell membrane
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Q9V589 | MYPRFLSRNYPLAKHLFFVTRYSFGLLGLRFGKEQSWLHLLWLVFNFVNLAHCCQAEFVFGWSHLRTSPVDAMDAFCPLACSFTTLFKLGWMWWRRQEVADLMDRIRLLIGEQEKREDSRRKVAQRSYYLMVTRCGMLVFTLGSITTGAFVLRSLWEMWVRRHQEFKFDMPFRMLFHDFAHRMPWFPVFYLYSTWSGQVTVYAFAGTDGFFFGFTLYMAFLLQALRYDIQDALKPIRDPSLRESKICCQRLADIVDRHNEIEKIVKEFSGIMAAPTFVHFVSASLVIATSVIDILLYSGYNIIRYVVYTFTVSSAIFLYCYGGTEMSTESLSLGEAAYSSAWYTWDRETRRRVFLIILRAQRPITVRVPFFAPSLPVFTSVIKFTGSIVALAKTIL | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to anisole.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46324
Sequence Length: 396
Subcellular Location: Cell membrane
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P81919 | MSKGVEIFYKGQKAFLNILSLWPQIERRWRIIHQVNYVHVIVFWVLLFDLLLVLHVMANLSYMSEVVKAIFILATSAGHTTKLLSIKANNVQMEELFRRLDNEEFRPRGANEELIFAAACERSRKLRDFYGALSFAALSMILIPQFALDWSHLPLKTYNPLGENTGSPAYWLLYCYQCLALSVSCITNIGFDSLCSSLFIFLKCQLDILAVRLDKIGRLITTSGGTVEQQLKENIRYHMTIVELSKTVERLLCKPISVQIFCSVLVLTANFYAIAVLSDERLELFKYVTYQACMLIQIFILCYYAGEVTQRSLDLPHELYKTSWVDWDYRSRRIALLFMQRLHSTLRIRTLNPSLGFDLMLFSSIVNCSYSYFALLKRVNS | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44068
Sequence Length: 381
Subcellular Location: Cell membrane
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Q9V3N2 | MVTEDFYKYQVWYFQILGVWQLPTWAADHQRRFQSMRFGFILVILFIMLLLFSFEMLNNISQVREILKVFFMFATEISCMAKLLHLKLKSRKLAGLVDAMLSPEFGVKSEQEMQMLELDRVAVVRMRNSYGIMSLGAASLILIVPCFDNFGELPLAMLEVCSIEGWICYWSQYLFHSICLLPTCVLNITYDSVAYSLLCFLKVQLQMLVLRLEKLGPVIEPQDNEKIAMELRECAAYYNRIVRFKDLVELFIKGPGSVQLMCSVLVLVSNLYDMSTMSIANGDAIFMLKTCIYQLVMLWQIFIICYASNEVTVQSSRLCHSIYSSQWTGWNRANRRIVLLMMQRFNSPMLLSTFNPTFAFSLEAFGSIVNCSYSYFALLKRVNS | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44451
Sequence Length: 384
Subcellular Location: Cell membrane
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P81921 | MDSFLQVQKSTIALLGFDLFSENREMWKRPYRAMNVFSIAAIFPFILAAVLHNWKNVLLLADAMVALLITILGLFKFSMILYLRRDFKRLIDKFRLLMSNEAEQGEEYAEILNAANKQDQRMCTLFRTCFLLAWALNSVLPLVRMGLSYWLAGHAEPELPFPCLFPWNIHIIRNYVLSFIWSAFASTGVVLPAVSLDTIFCSFTSNLCAFFKIAQYKVVRFKGGSLKESQATLNKVFALYQTSLDMCNDLNQCYQPIICAQFFISSLQLCMLGYLFSITFAQTEGVYYASFIATIIIQAYIYCYCGENLKTESASFEWAIYDSPWHESLGAGGASTSICRSLLISMMRAHRGFRITGYFFEANMEAFSSIVRTAMSYITMLRSFS | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. Complexes with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. They are necessary and sufficient to promote functional reconstitution of odor-evoked signaling in sensory neurons that normally respond only to carbon dioxide. Involved in the behavioral responses to esters. Involved in the behavioral responses to pentyl acetate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43966
Sequence Length: 385
Subcellular Location: Cell membrane
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P81922 | MNDSGYQSNLSLLRVFLDEFRSVLRQESPGLIPRLAFYYVRAFLSLLCQYPNKKLASLPLYRWINLFIMCNVMTIFWTMFVALPESKNVIEMGDDLVWISGMALVFTKIFYMHLRCDEIDELISDFEYYNRELRPHNIDEEVLGWQRLCYVIESGLYINCFCLVNFFSAAIFLQPLLGEGKLPFHSVYPFQWHRLDLHPYTFWFLYIWQSLTSQHNLMSILMVDMVGISTFLQTALNLKLLCIEIRKLGDMEVSDKRFHEEFCRVVRFHQHIIKLVGKANRAFNGAFNAQLMASFSLISISTFETMAAAAVDPKMAAKFVLLMLVAFIQLSLWCVSGTLVYTQSVEVAQAAFDINDWHTKSPGIQRDISFVILRAQKPLMYVAEPFLPFTLGTYMLVLKNCYRLLALMQESM | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Plays an important role in sociosexual interactions since its enhances courtship in a pheromone-dependent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47913
Sequence Length: 412
Subcellular Location: Cell membrane
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Q9V6A9 | MEKLRSYEDFIFMANMMFKTLGYDLFHTPKPWWRYLLVRGYFVLCTISNFYEASMVTTRIIEWESLAGSPSKIMRQGLHFFYMLSSQLKFITFMINRKRLLQLSHRLKELYPHKEQNQRKYEVNKYYLSCSTRNVLYVYYFVMVVMALEPLVQSCIMYLIGFGKADFTYKRIFPTRLTFDSEKPLGYVLAYVIDFTYSQFIVNVSLGTDLWMMCVSSQISMHLGYLANMLASIRPSPETEQQDCDFLASIIKRHQLMIRLQKDVNYVFGLLLASNLFTTSCLLCCMAYYTVVEGFNWEGISYMMLFASVAAQFYVVSSHGQMLIDLSTNLAKAAFESKWYEGSLRYKKEILILMAQAQRPLEISARGVIIISLDTFKILMTITYRFFAVIRQTVEK | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to butanol and 2-heptanone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46463
Sequence Length: 396
Subcellular Location: Cell membrane
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Q9V6H2 | MFEDIQLIYMNIKILRFWALLYDKNLRRYVCIGLASFHIFTQIVYMMSTNEGLTGIIRNSYMLVLWINTVLRAYLLLADHDRYLALIQKLTEAYYDLLNLNDSYISEILDQVNKVGKLMARGNLFFGMLTSMGFGLYPLSSSERVLPFGSKIPGLNEYESPYYEMWYIFQMLITPMGCCMYIPYTSLIVGLIMFGIVRCKALQHRLRQVALKHPYGDRDPRELREEIIACIRYQQSIIEYMDHINELTTMMFLFELMAFSALLCALLFMLIIVSGTSQLIIVCMYINMILAQILALYWYANELREQNLAVATAAYETEWFTFDVPLRKNILFMMMRAQRPAAILLGNIRPITLELFQNLLNTTYTFFTVLKRVYG | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43899
Sequence Length: 375
Subcellular Location: Cell membrane
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Q8NH83 | MRQNNNITEFVLLGFSQDPGVQKALFVMFLLTYLVTVVGNLLIVVDIIASPSLGSPMYFFLACLSFIDAAYSTTISPKLIVGLFCDKKTISFQGCMGQLFIDHFFGGAEVFLLVVMACDRYVAICKPLHYLTIMNRQVCFLLLVVAMIGGFVHSAFQIVVYSLPFCGPNVIVHFSCDMHPLLELACTDTYFIGLTVVVNSGAICMVIFNLLLISYGVILSSLKTYSQEKRGKALSTCSSGSTVVVLFFVPCIFIYVRPVSNFPTDKFMTVFYTIITHMLSPLIYTLRNSEMRNAIEKLLGKKLTIFIIGGVSVLM | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34915
Sequence Length: 315
Subcellular Location: Cell membrane
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P0C604 | MRQNNNITEFVLLGFSQYPDVQNALFVMFLLIYIVTMVGNLLIVVSIIASPFLGSPVYFFLACLSFIDAVYSTTISPVLIVDLLCDKKTISFPACMGQLFIEHLFGDTDVFLLVVMAYDRYVATCKPLRYLTIMNRQVCILLLVVAVTGGFLHSVFQILVVYSLPFCGPNVIYHFFCNIYPLLDLECTDTYFVGLAVVFNGGAICMVIFTLLLISYGVILNSLKTYSPEGRHKAPFICSSHFIMVILFFVPCIFLYVRPVSNFPIDKFLTVFYSVITPKLNPFIYMLRNSEMRNAIENLLGYQSGKTGFRCSKLN | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35621
Sequence Length: 315
Subcellular Location: Cell membrane
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Q8NGF8 | MASTSNVTELIFTGLFQDPAVQSVCFVVFLPVYLATVVGNGLIVLTVSISKSLDSPMYFFLSCLSLVEISYSSTIAPKFIIDLLAKIKTISLEGCLTQIFFFHFFGVAEILLIVVMAYDCYVAICKPLHYMNIISRQLCHLLVAGSWLGGFCHSIIQILVIIQLPFCGPNVIDHYFCDLQPLFKLACTDTFMEGVIVLANSGLFSVFSFLILVSSYIVILVNLRNHSAEGRHKALSTCASHITVVILFFGPAIFLYMRPSSTFTEDKLVAVFYTVITPMLNPIIYTLRNAEVKIAIRRLWSKKENPGRE | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34456
Sequence Length: 309
Subcellular Location: Cell membrane
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Q8NH72 | MENQNNVTEFILLGLTENLELWKIFSAVFLVMYVATVLENLLIVVTIITSQSLRSPMYFFLTFLSLLDVMFSSVVAPKVIVDTLSKSTTISLKGCLTQLFVEHFFGGVGIILLTVMAYDRYVAICKPLHYTIIMSPRVCCLMVGGAWVGGFMHAMIQLLFMYQIPFCGPNIIDHFICDLFQLLTLACTDTHILGLLVTLNSGMMCVAIFLILIASYTVILCSLKSYSSKGRHKALSTCSSHLTVVVLFFVPCIFLYMRPVVTHPIDKAMAVSDSIITPMLNPLIYTLRNAEVKSAMKKLWMKWEALAGK | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34558
Sequence Length: 309
Subcellular Location: Cell membrane
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Q6IEV9 | MQQNNSVPEFILLGLTQDPLRQKIVFVIFLIFYMGTVVGNMLIIVTIKSSRTLGSPMYFFLFYLSFADSCFSTSTAPRLIVDALSEKKIITYNECMTQVFALHLFGCMEIFVLILMAVDRYVAICKPLRYPTIMSQQVCIILIVLAWIGSLIHSTAQIILALRLPFCGPYLIDHYCCDLQPLLKLACMDTYMINLLLVSNSGAICSSSFMILIISYIVILHSLRNHSAKGKKKALSACTSHIIVVILFFGPCIFIYTRPPTTFPMDKMVAVFYTIGTPFLNPLIYTLRNAEVKNAMRKLWHGKIISENKG | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35003
Sequence Length: 310
Subcellular Location: Cell membrane
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Q8NGM1 | MQNQSFVTEFVLLGLSQNPNVQEIVFVVFLFVYIATVGGNMLIVVTILSSPALLVSPMYFFLGFLSFLDACFSSVITPKMIVDSLYVTKTISFEGCMMQLFAEHFFAGVEVIVLTAMAYDRYVAICKPLHYSSIMNRRLCGILMGVAWTGGLLHSMIQILFTFQLPFCGPNVINHFMCDLYPLLELACTDTHIFGLMVVINSGFICIINFSLLLVSYAVILLSLRTHSSEGRWKALSTCGSHIAVVILFFVPCIFVYTRPPSAFSLDKMAAIFYIILNPLLNPLIYTFRNKEVKQAMRRIWNRLMVVSDEKENIKL | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35667
Sequence Length: 316
Subcellular Location: Cell membrane
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Q8NGL9 | MQLNNNVTEFILLGLTQDPFWKKIVFVIFLRLYLGTLLGNLLIIISVKTSQALKNPMFFFLFYLSLSDTCLSTSITPRMIVDALLKKTTISFSECMIQVFSSHVFGCLEIFILILTAVDRYVDICKPLHYMTIISQWVCGVLMAVAWVGSCVHSLVQIFLALSLPFCGPNVINHCFCDLQPLLKQACSETYVVNLLLVSNSGAICAVSYVMLIFSYVIFLHSLRNHSAEVIKKALSTCVSHIIVVILFFGPCIFMYTCLATVFPMDKMIAVFYTVGTSFLNPVIYTLKNTEVKSAMRKLWSKKLITDDKR | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34991
Sequence Length: 310
Subcellular Location: Cell membrane
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Q9VCS9 | MDKHKDRIESMRLILQVMQLFGLWPWSLKSEEEWTFTGFVKRNYRFLLHLPITFTFIGLMWLEAFISSNLEQAGQVLYMSITEMALVVKILSIWHYRTEAWRLMYELQHAPDYQLHNQEEVDFWRREQRFFKWFFYIYILISLGVVYSGCTGVLFLEGYELPFAYYVPFEWQNERRYWFAYGYDMAGMTLTCISNITLDTLGCYFLFHISLLYRLLGLRLRETKNMKNDTIFGQQLRAIFIMHQRIRSLTLTCQRIVSPYILSQIILSALIICFSGYRLQHVGIRDNPGQFISMLQFVSVMILQIYLPCYYGNEITVYANQLTNEVYHTNWLECRPPIRKLLNAYMEHLKKPVTIRAGNFFAVGLPIFVKTINNAYSFLALLLNVSN | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46052
Sequence Length: 387
Subcellular Location: Cell membrane
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Q9VAZ3 | MLFNYLRKPNPTNLLTSPDSFRYFEYGMFCMGWHTPATHKIIYYITSCLIFAWCAVYLPIGIIISFKTDINTFTPNELLTVMQLFFNSVGMPFKVLFFNLYISGFYKAKKLLSEMDKRCTTLKERVEVHQGVVRCNKAYLIYQFIYTAYTISTFLSAALSGKLPWRIYNPFVDFRESRSSFWKAALNETALMLFAVTQTLMSDIYPLLYGLILRVHLKLLRLRVESLCTDSGKSDAENEQDLIKCIKDHNLIIDYAAAIRPAVTRTIFVQFLLIGICLGLSMINLLFFADIWTGLATVAYINGLMVQTFPFCFVCDLLKKDCELLVSAIFHSNWINSSRSYKSSLRYFLKNAQKSIAFTAGSIFPISTGSNIKVAKLAFSVVTFVNQLNIADRLTKN | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45437
Sequence Length: 397
Subcellular Location: Cell membrane
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Q9VAW0 | MLTDKFLRLQSALFRLLGLELLHEQDVGHRYPWRSICCILSVASFMPLTIAFGLQNVQNVEQLTDSLCSVLVDLLALCKIGLFLWLYKDFKFLIGQFYCVLQTETHTAVAEMIVTRESRRDQFISAMYAYCFITAGLSACLMSPLSMLISYQRTGELQPKFPFPSVYPWDNMKLSNYIISYFWNVCAALGVALPTVCVDTLFCSLSHNLCALFQIARHKMMHFEGRNTKETHENLKHVFQLYALCLNLGHFLNEYFRPLICQFVAASLHLCVLCYQLSANILQPALLFYAAFTAAVVGQVSIYCFCGSSIHSECQLFGQAIYESSWPHLLQENLQLVSSLKIAMMRSSLGCPIDGYFFEANRETLITVSKAFIKVSKKTPQVND | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43644
Sequence Length: 384
Subcellular Location: Cell membrane
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Q8NGU1 | MLGNYSSATEFFLLGFPGSQEVCRILFATFFLLYAVTVMGNVVIIITVCVDKCLQSPIYFFLGHLCVLEILITSTAVPFMLWGLLLPSTQIMSLTACAAQLYLYLSLGTLELALMGVMAVDRYVAVCNPLRYNIIMNSSTFIWVIIVSWVLGFLSEIWPVYATFQLTFCKSSVLDHFYCDRGQLLKVSCEDTLFREFILFLMAVFIIIGSLIPTIVSYTYIISTNLKIPSASGWRKSFSTCASHFTYVVIGYGSCLFLYVKPKQTQAAEYNRVVSLLVLVVTPFLNPFIFTLRNDKFIQAFGDGMKHCYKLLKN | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35431
Sequence Length: 314
Subcellular Location: Cell membrane
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Q9W2U9 | MSDKVKGKKQEEKDQSLRVQILVYRCMGIDLWSPTMANDRPWLTFVTMGPLFLFMVPMFLAAHEYITQVSLLSDTLGSTFASMLTLVKFLLFCYHRKEFVGLIYHIRAILAKEIEVWPDAREIIEVENQSDQMLSLTYTRCFGLAGIFAALKPFVGIILSSIRGDEIHLELPHNGVYPYDLQVVMFYVPTYLWNVMASYSAVTMALCVDSLLFFFTYNVCAIFKIAKHRMIHLPAVGGKEELEGLVQVLLLHQKGLQIADHIADKYRPLIFLQFFLSALQICFIGFQVADLFPNPQSLYFIAFVGSLLIALFIYSKCGENIKSASLDFGNGLYETNWTDFSPPTKRALLIAAMRAQRPCQMKGYFFEASMATFSTIVRSAVSYIMMLRSFNA | Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44623
Sequence Length: 392
Subcellular Location: Cell membrane
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Q8NH87 | MQRSNHTVTEFILLGFTTDPGMQLGLFVVFLGVYSLTVVGNSTLIVLICNDSCLHTPMYFFTGNLSFLDLWYSSVYTPKILVTCISEDKSISFAGCLCQFFFSAGLAYSECYLLAAVAYDRYVAISKPLLYAQAMSIKLCALLVAVSYCGGFINSSIITKKTFSFNFCRENIIDDFFCDLLPLVELACGEKGGYKIMMYFLLASNVICPAVLILASYLFIITSVLRISSSKGYLKAFSTCSSHLTSVTLYYGSILYIYALPRSSYSFDMDKIVSTFYTVVFPMLNLMIYSLRNKDVKEALKKLLP | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34071
Sequence Length: 305
Subcellular Location: Cell membrane
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Q8NGQ1 | MIFPSHDSQAFTSVDMEVGNCTILTEFILLGFSADSQWQPILFGVFLMLYLITLSGNMTLVILIRTDSHLHTPMYFFIGNLSFLDFWYTSVYTPKILASCVSEDKRISLAGCGAQLFFSCVVAYTECYLLAAMAYDRHAAICNPLLYSGTMSTALCTGLVAGSYIGGFLNAIAHTANTFRLHFCGKNIIDHFFCDAPPLVKMSCTNTRVYEKVLLGVVGFTVLSSILAILISYVNILLAILRIHSASGRHKAFSTCASHLISVMLFYGSLLFMYSRPSSTYSLERDKVAALFYTVINPLLNPLIYSLRNKDIKEAFRKATQTIQPQT | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36344
Sequence Length: 327
Subcellular Location: Cell membrane
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Q8NGQ6 | MAKNNLTRVTEFILMGFMDHPKLEIPLFLVFLSFYLVTLLGNVGMIMLIQVDVKLYTPMYFFLSHLSLLDACYTSVITPQILATLATGKTVISYGHCAAQFFLFTICAGTECFLLAVMAYDRYAAIRNPLLYTVAMNPRLCWSLVVGAYVCGVSGAILRTTCTFTLSFCKDNQINFFFCDLPPLLKLACSDTANIEIVIIFFGNFVILANASVILISYLLIIKTILKVKSSGGRAKTFSTCASHITAVALFFGALIFMYLQSGSGKSLEEDKVVSVFYTVVIPMLNPLIYSLRNKDVKDAFRKVARRLQVSLSM | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34908
Sequence Length: 314
Subcellular Location: Cell membrane
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Q8NGE7 | MLGSKPRVHLYILPCASQQVSTMGDRGTSNHSEMTDFILAGFRVRPELHILLFLLFLFVYAMILLGNVGMMTIIMTDPRLNTPMYFFLGNLSFIDLFYSSVIEPKAMINFWSENKSISFAGCVAQLFLFALLIVTEGFLLAAMAYDRFIAICNPLLYSVQMSTRLCTQLVAGSYFCGCISSVIQTSMTFTLSFCASRAVDHFYCDSRPLQRLSCSDLFIHRMISFSLSCIIILPTIIVIIVSYMYIVSTVLKIHSTEGHKKAFSTCSSHLGVVSVLYGAVFFMYLTPDRFPELSKVASLCYSLVTPMLNPLIYSLRNKDVQEALKKFLEKKNIIL | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37746
Sequence Length: 335
Subcellular Location: Cell membrane
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Q8NGQ5 | MAEMNLTLVTEFLLIAFTEYPEWALPLFLLFLFMYLITVLGNLEMIILILMDHQLHAPMYFLLSHLAFMDVCYSSITVPQMLAVLLEHGAALSYTRCAAQFFLFTFFGSIDCYLLALMAYDRYLAVCQPLLYVTILTQQARLSLVAGAYVAGLISALVRTVSAFTLSFCGTSEIDFIFCDLPPLLKLTCGESYTQEVLIIMFAIFVIPASMVVILVSYLFIIVAIMGIPAGSQAKTFSTCTSHLTAVSLFFGTLIFMYLRGNSDQSSEKNRVVSVLYTEVIPMLNPLIYSLRNKEVKEALRKILNRAKLS | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34757
Sequence Length: 310
Subcellular Location: Cell membrane
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A0A0R4IM31 | MDLCVTIKGVSFLLQAGLGILANALVLLAYAHIRLAEARLQPVDAILCHLALVDLLLLLTRGVPQTMTVFGMRNLLDDTGCKVVIYTYRIARALSVCITCMLSVFQAVTVAPAAGPLLSGVKARLPQLLAPTFAALWFINMAVCIAAPFFSVAPRNGTVPPFTLNLGFCHVDFHDNLSYVLNGVAVSVRDFAFVGAMLASSGFILLLLHRHRRQVRAVRRSQGSTMETRAARTVLMLVILYSVFFGIDNVIWIYMLTVAQVPPVVADMRVFFSSCYASLSPFLIISSNRKLKARMVCATSEQERQAEDGKNSSGKN | Function: Probable pheromone receptor. Shows high specificity for 4-hydroxyphenylacetic acid. Activation of the receptor stimulates intracellular calcium release.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34498
Sequence Length: 316
Subcellular Location: Cell membrane
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A0A0R4IP11 | MSEVLTVDAVLFGLLVFSGIIGNIMVIYVVFDCAKLCASRHLPPSDTILVHLCLANLLTSVFRTVPIFVSDLGLQVWLTAGWCRVFMLLWVWWRAVGCWVTLALSAFHCATLRRQHVSMGPLGHSRERRRVWVVLAVVWAANLLFSLPALVYTTQVRGNATVELMVISCTTRPLLGCVWEFPTFQQGYAFASSSLALNEVLPLVLMVGTNLATLQALGKHIRTVRAGGSTGAELDRHVSSERKAGHVIMALVALFVGCWVLQVAAVTYYNHNRGAHAEGLLTVAHFSASLFVGFSPLVVALGHGKLRRRISGILQSCMHRLKQTQDKPAEITEKDGRTTQSAMK | Function: Probable olfactory receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37804
Sequence Length: 344
Subcellular Location: Cell membrane
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Q8BH10 | MSAELNVPMDPSAPACPEPGHKGMDYRDWVRRSYLELVTSNHHSVQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLETKYQYPQPLLIAFSACTTVLVAVHLFALLISTCILPNVEAVSNIHNLNSISESPHERMHPYIELAWGFSTVLGILLFLAEVVLLCWIKFLPVDAKDQPGSHSHTGWQAALVSTIIMVPVGLIFVVFTIHFYRSLVRHKTERHNREIEELHKLKVQLDGHERSLQVV | Function: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel subunit which mediates Ca(2+) influx and increase in Ca(2+)-selective current by synergy with the Ca(2+) sensor, STIM1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28199
Sequence Length: 250
Subcellular Location: Membrane
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E3PY99 | MEKVKVIIMGLGAMGGGMADMLLKKQGVEIVGVVGRGKMLGTSMYDHISTPRGDREDVIVGAMEDVITEKAADVVLLCTDSFTRKAFDKIKFIVEKKINVISSAEEMAYPMAQEPELAKEIDRLAKENGVSVLGTGINPGLIMDLLVILMTGCCEEVHSILSRRVNSLSPFGPAVMEEQGIGITVEEFNKGVQEGTLAGHVGFHESIGMIADAIGWKLSAPITQSMEPIVTDVDRKSPYGFAKAGNVAGCAMKGFGYVDGELKIEMDHPQQIEPEQVGVQTGDYVIINGVPNINMVNSPEVPGGIGTIAMCVNMIPQIINARPGLHTMIDLPVPRAIMGDFRDLISEEAKIVK | Function: Involved in the ornithine fermentation pathway. Catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate (DAP) to yield 2-amino-4-ketopentanoate (AKP).
Catalytic Activity: (2R,4S)-2,4-diaminopentanoate + H2O + NAD(+) = (2R)-2-amino-4-oxopentanoate + H(+) + NADH + NH4(+)
Sequence Mass (Da): 37896
Sequence Length: 353
EC: 1.4.1.12
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C1FW05 | MGKNVKTLIWGFGAMGSGMASILLEKGGYELVSVIDTHPQKAGKDVGELLGRAPLGVKVTMDHLKAFGSHPDVALIATSSFVEEVSPQIEFALENDANVITIAEEMSYPWIDSKEIAERLDALALNRGKTVLGTGINPGFVLDTLVVSLSGVCKEVRHIHAKRVNDLAPFGPTVMRTQGVGTTPEKFEEGIRSGNIVGHIGFRQSIMLIAKALGWTIEDIVEERQPIITNVRRKTNYVDVTPGNVAGCRHTARAYSCGREVIFLEHPQQVCPEAEGVRTGDYVVIDGDPPVNLRIEPEIPGGTGTMAMAVNMIPLVVNAPPGLLTMIDLPVPRSISNGF | Function: Involved in the ornithine fermentation pathway. Catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although Ord is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Ord is specific for NAD as hydrogen acceptor.
Catalytic Activity: (2R,4S)-2,4-diaminopentanoate + H2O + NAD(+) = (2R)-2-amino-4-oxopentanoate + H(+) + NADH + NH4(+)
Sequence Mass (Da): 36466
Sequence Length: 339
EC: 1.4.1.26
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O43612 | MNLPSTKVSWAAVTLLLLLLLLPPALLSSGAAAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRSGPPGLQGRLQRLLQASGNHAAGILTMGRRAGAEPAPRPCLGRRCSAPAAASVAPGGQSGI | Function: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested.
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
Sequence Mass (Da): 13363
Sequence Length: 131
Subcellular Location: Rough endoplasmic reticulum
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O77668 | MNPPFAKVSWATVTLLLLLLLLPPAVLSPGAAAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRPGPPGLQGRLQRLLQASGNHAAGILTMGRRAGAEPAPRLCPGRRCLAAAASSVAPGGRSGI | Function: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested.
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
Sequence Mass (Da): 13457
Sequence Length: 131
Subcellular Location: Rough endoplasmic reticulum
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O55232 | MNLPSTKVPWAAVTLLLLLLLPPALLSLGVDAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRPGPPGLQGRLQRLLQANGNHAAGILTMGRRAGAELEPYPCPGRRCPTATATALAPRGGSRV | Function: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions . A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested . A modulation effect on luteinizing hormone-releasing hormone (LHRH) secretion also suggests a more minor contribution to the regulation of reproductive function .
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides.
Sequence Mass (Da): 13645
Sequence Length: 130
Subcellular Location: Rough endoplasmic reticulum
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Q6F6K2 | MATVHYSRRPGTPPVTLTSSPSMDDVATPIPYLPTYAEAVADAPPPYRSRESLVFSPPLFPHVENGTTQQSYDCLDCAYDGIHRLQLAFLRIRKCCVPAFLILFGILTLTAVVVAIVAVFPEEPPNSTT | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14092
Sequence Length: 129
Domain: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. Contains one L domain: a PPXY motif which is involved in the interaction with ITCH, a member of the NEDD4 family.
Subcellular Location: Host Golgi apparatus membrane
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Q9E2H5 | MATVHYSRRPGTPPVTLTSSPGMDDVATPIPYLPTYAEAVADAPPPYRSRESLVFSPPLFPHVENGTTQQSYDCLDCAYDGIHRLQLAFLRIRKCCVPAFLILFGILTLTAVVVAIVAVFPEEPPNSTTRNYCPEGEGIYSRLQLVARVCTTKAIYVTKANVAIWSTTPSTLHNLSICIFSCADAFLRDRGLGTSTSGIRTAGGLARTTSGDALFCISSVC | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23825
Sequence Length: 221
Domain: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. Contains one L domain: a PPXY motif which is involved in the interaction with ITCH, a member of the NEDD4 family.
Subcellular Location: Host Golgi apparatus membrane
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P22059 | MAATELRGVVGPGPAAIAALGGGGAGPPVVGGGGGRGDAGPGSGAASGTVVAAAAGGPGPGAGGVAAAGPAPAPPTGGSGGSGAGGSGSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQTYHLKASSEVERQRWVTALELAKAKAVKMLAESDESGDEESVSQTDKTELQNTLRTLSSKVEDLSTCNDLIAKHGTALQRSLSELESLKLPAESNEKIKQVNERATLFRITSNAMINACRDFLMLAQTHSKKWQKSLQYERDQRIRLEETLEQLAKQHNHLERAFRGATVLPANTPGNVGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLGHKRTGSNISGASSDISLDEQYKHQLEETKKEKRTRIPYKPNYSLNLWSIMKNCIGKELSKIPMPVNFNEPLSMLQRLTEDLEYHELLDRAAKCENSLEQLCYVAAFTVSSYSTTVFRTSKPFNPLLGETFELDRLEENGYRSLCEQVSHHPPAAAHHAESKNGWTLRQEIKITSKFRGKYLSIMPLGTIHCIFHATGHHYTWKKVTTTVHNIIVGKLWIDQSGEIDIVNHKTGDKCNLKFVPYSYFSRDVARKVTGEVTDPSGKVHFALLGTWDEKMECFKVQPVIGENGGDARQRGHEAEESRVMLWKRNPLPKNAENMYYFSELALTLNAWESGTAPTDSRLRPDQRLMENGRWDEANAEKQRLEEKQRLSRKKREAEAMKATEDGTPYDPYKALWFERKKDPVTKELTHIYRGEYWECKEKQDWSSCPDIF | Function: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum . Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol . Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly . Regulates cholesterol efflux by decreasing ABCA1 stability .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 89421
Sequence Length: 807
Domain: The FFAT motif is required for interaction with VATA and proper localization of the protein.
Subcellular Location: Cytoplasm
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Q969R2 | MGKAAAPSRGGGCGGRSRGLSSLFTVVPCLSCHTAAPGMSASTSGSGPEPKPQPQPVPEPERGPLSEQVSEAVSEAVPRSEPVSETTSEPEPGAGQPSELLQGSRPGSESSSGVGAGPFTKAASEPLSRAVGSATFLRPESGSLPALKPLPLLRPGQAKTPLGVPMSGTGTTSSAPLALLPLDSFEGWLLKWTNYLKGYQRRWFVLGNGLLSYYRNQGEMAHTCRGTINLSTAHIDTEDSCGILLTSGARSYHLKASSEVDRQQWITALELAKAKAVRVMNTHSDDSGDDDEATTPADKSELHHTLKNLSLKLDDLSTCNDLIAKHGAALQRSLTELDGLKIPSESGEKLKVVNERATLFRITSNAMINACRDFLELAEIHSRKWQRALQYEQEQRVHLEETIEQLAKQHNSLERAFHSAPGRPANPSKSFIEGSLLTPKGEDSEEDEDTEYFDAMEDSTSFITVITEAKEDSRKAEGSTGTSSVDWSSADNVLDGASLVPKGSSKVKRRVRIPNKPNYSLNLWSIMKNCIGRELSRIPMPVNFNEPLSMLQRLTEDLEYHHLLDKAVHCTSSVEQMCLVAAFSVSSYSTTVHRIAKPFNPMLGETFELDRLDDMGLRSLCEQVSHHPPSAAHYVFSKHGWSLWQEITISSKFRGKYISIMPLGAIHLEFQASGNHYVWRKSTSTVHNIIVGKLWIDQSGDIEIVNHKTNDRCQLKFLPYSYFSKEAARKVTGVVSDSQGKAHYVLSGSWDEQMECSKVMHSSPSSPSSDGKQKTVYQTLSAKLLWKKYPLPENAENMYYFSELALTLNEHEEGVAPTDSRLRPDQRLMEKGRWDEANTEKQRLEEKQRLSRRRRLEACGPGSSCSSEEEKEADAYTPLWFEKRLDPLTGEMACVYKGGYWEAKEKQDWHMCPNIF | Function: Binds 7-ketocholesterol.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 101266
Sequence Length: 916
Subcellular Location: Membrane
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Q5QNQ6 | MGKAAALSRGGGCAGRSRGLSSLFTVVPCLSCHTAAPGMNSSAFGSGPASKPQLQPVQAPERELLSKQVCQPISEPASRSEPGSQTTSVPRPSGVGQESELQGLWPGSENGTRSVSIIKASPELAMPSPLQSTVGSLPVTKPESKLVPKTQSFLRQGQAKISVGTPVSGIGVQMVSPPLDSYKGWLLKWTNYLKGYQRRWFVLGNGLLSYYRNQGEMAHTCRATINLASTHFETEDSCGILLCNGARTYHLKASSEVDRQHWITALELAKAKAIRVMKTQSDDSGDDDEEPAAPADNSELHHTLKTLSLKLNDLSTCNDLIAKHGAALQRSLNELDSLKIPSECGEKLKVVNERATLFRITSNAMINACRDFLELAETHSRKWQRALNYEQEQRVHLEETIEQLAKQHNSLERAFCNTPGGPASSSKSFSEGSFLTSKGENSEEDEDTEYFDAMEDSTSFITVVTEAKEDRKPESGPGTTTVDWTSADNVLDGASFMPKNSCKVKRRVRIPDKPNYSLNLWSIMKNCIGRELSRIPMPVNFNEPLSMLQRLTEDLEYHHLLDKAVNCTSSVEQMCLVAAFSVSSYSTTVHRIAKPFNPMLGETFELDRMEDMGLRSLCEQVSHHPPSAAHHVFSKHGWSLWQEITIASKFRGKYISIMPLGAIHLEFQASGNHYVWRKSTSTVHNIIVGKLWIDQSGDIEIVNHKTKDRCQLKFVPYSYFSKEAARKVTGVVSDSQGKAHYVLSGSWDDQMECSKIVHSSPSSDGRQKTVYQTLPAKLLWRKYPLPENAENMYYFSELALTLNEQEDGVAPTDSRLRPDQRLMERGRWDEANTEKQRLEEKQRLSRRRRLESCTAGCGGEEEKESDGYVPLWFEKRLDPLTGEMACMYKGGYWEAKEKKDWHMCPNIF | Function: Binds 7-ketocholesterol.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 101353
Sequence Length: 908
Subcellular Location: Membrane
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Q8IYS5 | MALVLILQLLTLWPLCHTDITPSVPPASYHPKPWLGAQPATVVTPGVNVTLRCRAPQPAWRFGLFKPGEIAPLLFRDVSSELAEFFLEEVTPAQGGIYRCCYRRPDWGPGVWSQPSDVLELLVTEELPRPSLVALPGPVVGPGANVSLRCAGRLRNMSFVLYREGVAAPLQYRHSAQPWADFTLLGARAPGTYSCYYHTPSAPYVLSQRSEVLVISWEGEGPEARPASSAPGMQAPGPPPSDPGAQAPSLSSFRPRGLVLQPLLPQTQDSWDPAPPPSDPGV | Function: Regulator of osteoclastogenesis which plays an important bone-specific function in osteoclast differentiation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 30481
Sequence Length: 282
Subcellular Location: Secreted
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Q8VBT3 | MVLSLILQLSTLWPACRADFTPTAPLASYPQPWLGAHPAAVVTPGINVTLTCRAPQSAWRFALFKSGLVTPLLLRDVSVELAEFFLEEVTPAQGGSYHCRYRKTDWGPGVWSQPSNVLELLVTDQLPRPSLVALPGPVVAPGANVSLRCAGRIPGMSFALYRVGVATPLQYIDSVQPWADFLLIGTHTPGTYCCYYHTPSAPYVLSQRSQPLVISFEGSGSLDYTQGNLIRLGLAGMVLICLGIIVTCDWHSRSSAFDGLLPQQN | Function: Regulator of osteoclastogenesis which plays an important bone-specific function in osteoclast differentiation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 28726
Sequence Length: 265
Subcellular Location: Cell membrane
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