ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q04G23 | MAFNENRVINNYAEALMEVSGKQTAKVLSELQVIELVFERNKELAQTLDDVSVSSQQQEAFIGILGKGCSTTTKNFLETLADNRHFSLLEEIVENLDQRVSASNNHSLVIAKTAIPITAEQSKRLSKIAQKKFGYQHVEVKNVVDPNVIAGVILTAGSKTIDGSIKNKLVQLNNHIKQAVGKE | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A5CD08 | MHKLNNVAVLYAKILFKQAIKLNIVSKVKQDLKALKQFCKFLAKQNMSLQLIALMKNKINLMDYLSSTYGLNHLTYNFLKLLQKNNRLTYLSHIIIAFDAQVRNYQGVTLGYLITTKKWSKSAIKEIKDIFERKLNRKLIISNIVDKSIVGGIILRYEDYEYDLSMLGAINRFKSRIKLNY | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A6L8N6 | MDIGTISSRYAKALFSLAKDKEQESRVYDDMKMLADSFSMEPELRGALSNPIVSVPEKVKLLTAAGGIEVCELYSRFINLVLAHKRETLLPFIAYIYIHLYRKEKKITRVRFDTAVAVDDAVKSHLQDKLRKETGCTIEFSGHVEPELIGGFRLRIGNYRIDASYATQLRDIRTGLLENR | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
P50008 | MSGMHGASREALAAARERLDALTDSTSVDAGSLADELAAVTALLHREVSLRRVLTDPAQSARPRPSSPSVSSAPRSAAPVDLVAGTVRSRWSQSRDLVDALEQLANIADLTAAQKRGRLDNVEDELFRFGRIISSNTELRAALTSRSATTAAKSELLAGLLGSRAERTTERLVTRLVTAPRGRSLESGLESLSKLAADRRDRMVAVVTSAVPLSDTQKQRLGAALAKVYGRPMHLNLDVDPEVLGGIRVQVGDEVINGSIADRLEDAGRRLAS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
B2FHZ1 | MSQALTLARPYARAAFATARDEGAFAPWSDALAFSAHVAVDPRVAALLANPELGRDDAVALLAPVSHGETYSRFLAILAESHRLPLLPEISGMFDALRAEAEHVVKATVTSAAELSAGELDAIKVALRKRFNREVDVTTAVDASLIGGAVIDAGDVVIDGSLKGKLARLQTALAN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
P95786 | MDKKTQAVTEIYAKSLVEVALERDSVPIIYDEVRAILSVLDDQQVQDFLASKAIDLSAKSEVVRLFQESCSNYMKQFLEIILQNERQQLLYLIMKEVLKELSLKTHIFDIEVTTAVALSDDQKERLTALVEKKFALTKRNLIEKIDDEIIGGFIIKANNKVIDTSIRSQLQELKMNLK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q9A0J0 | MTKKEQALIEQYAKSLVEVASEHHSLDALQADVLAILETFVTTNLDQSLSSQAVPHAEKIKLLTLLKGNNSVYMNNFLNLILQNEREAYLYQMLQAVLNEIAIVSNQYDVTVTSSLPLTEEQKSRVRAVVAKKFAVTAGRLIEKVDPSLIGGFIISVNNKVIDTSIRRQLQAFKMNLK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q04HT6 | MDKKTVKVIEKYSMPFVQLVLEKGEEDRIFSDLTQIKQVVEKTGLPSFLKQVAVDESDKEKTIAFFQDSVSPLLQNFIQVLAYNHRANLFYDVLVDCLNRLEKETNRFEVTITSAHPLTDEQKTRLLPLIEKKMSLKVRSVKEQIDESLIGGFVIFANHKTIDVSIKQQLKVVKENLK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A7HIX6 | MALTLDIVTPERRVLSVTVDEVRAPGAAGGFGIRVNHEPFMTALEPGRLTYVEGGREHHYAIGGGFLQVAENRVIVLADTAEAAGDIDVERAKRAFQDAQDRLLRMTEQDEHHPAESARVKRAAARISVAGR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14369
Sequence Length: 132
Subcellular Location: Cell inner membrane
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O66903 | MIQVEIVSPQGMVYSGEVESVNVPTVEGEVGILENHMYLMTLLKPGLVYFNGDDKNGIAVTYGVLDVTPQKVLILAEEAYEVGKLPPASKLKEEFEEAVKKMATAQTMEELKEWEKEAEKARTLLELVEKYR | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14806
Sequence Length: 132
Subcellular Location: Cell inner membrane
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P09468 | MTLNLCVLTPNRIVWDSEVKEIILSTNSGQIGVLANHAPIATAVDIGILKIRLANQWLTMALMGGFARIGNNEITILVNDAEKNSDIDPQEAQQTLEIAEANLRKAEGKRQTIEANLALRRARTRVEALNTI | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14499
Sequence Length: 132
Subcellular Location: Plastid
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Q5P4E1 | MAMTVHVDIVSAEEQIFSGLAEFVALPGEAGELGILPGHMPLMTRIKPGAVRVKRPDQAEEELVFVAGGILEVQPGLVTVLADTAIRGKDLDEAKALEAKRIAEEALKNQSTEIDYAKAQAELAEAIAQIAAIQKLRKRGH | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15104
Sequence Length: 141
Subcellular Location: Cell inner membrane
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P31477 | MTLDVSIIIPERVFWEKRVEEIILPTLSGQMGVLKDHIPILTGLDIGIILVRQKSSSDWTSLVVTGGFALINSNNVTILVNEAEFGSEINVEQAQISYNSSKHALEMNKDIKRKFELTLNLKKARARFQVTQLKK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15222
Sequence Length: 135
Subcellular Location: Plastid
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Q2J6N4 | MPIRVAIVSPEQEVWSGDADMVVARTTDGDLGVLPGHVPLLGLLAPGGTVRVKTGGREISASVDGGFISVTHQGVSILAETAKLT | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 8676
Sequence Length: 85
Subcellular Location: Cell membrane
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Q14K05 | MTKKYLKVDVVSPLGSVFKGEADMVSLRGSAGEMGIAYGHTELLSTLPAGVVNVRKDQHTDVLYVSGGIVEVTPTRVTIMVDDMERAENLNQAEAEKARARAKEVLKNPDASKLDIEAANKRLKEADARLKALNSSNGLYYSKDD | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15767
Sequence Length: 145
Subcellular Location: Cell inner membrane
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Q8RGE3 | MPSFDVSVVTQVKKILEQEAGYLRLRTSEGDIGILPNHAPFVAELSMGKMEIESPNKDRRDIYFLSGGFLEISDNQATVIADEVFPIEKIDVESEQALVENLKKELEKVSTEEEKRKLQKKIKISLAKIDAKNN | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15134
Sequence Length: 134
Subcellular Location: Cell inner membrane
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A7HT53 | MAEKLNFDLVSPERLLFSGQVDMVVIPGSEGDMGIMAGHAPVMSTLRPGIIEVENEGAPRQRIFVRGGFAEVTPAGLTVLAEFTVPLADLDATALDREIALADKDVADAKNDDKRQSALEKLDHLKELRHTV | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14292
Sequence Length: 132
Subcellular Location: Cell inner membrane
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Q6MAK8 | MLYPLSILTSEKNVFNEDVYSVNVPGADGYFEVLAHHATVIALLQPGKLTIINKDHQKLYFGITTGFIEVSHNSATIIADAIESVQEIDVERAKQSYERAKMRLESPDKHVDKERAKRSLNRAKNRIKLFLEIHPQVSFIPLKALLI | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16669
Sequence Length: 147
Subcellular Location: Cell inner membrane
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Q4FP39 | MSEEFKIEIVNPEKSFLSKEDVTEVVVPAFEGEMGILKDHISIISFLKPGIIKIFSKSGEDNYYVEDGIVEFKNNNLSVLTSSIFNIKDIDKDKISELLTQAEENSKNSDITDQNKYLVDQKIDVLKTLN | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14749
Sequence Length: 130
Subcellular Location: Cell inner membrane
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Q85X21 | MTLNLRVLSPNRVIWDSEVQEIIISTNSGQMGVLPNHVSLVTAVDIGVMKIRLNGKWSTMALMGGFAKIDKDRITILVNNAERDVDIDLQKAQETFRRAKACLVQAEGKRQVIEADVALKRARTLLEAINASPSDSN | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15128
Sequence Length: 137
Subcellular Location: Plastid
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B2IGK9 | MAQERAEHESADQHTTSTGVPHEGQGEPFPPFDSSNFAPLLIWLAISFLLLYALMSKLVLPRIGGILHTRNEKLRSDMHEATALHAQAKEAAALQEKTIADAKAKAIALAQENQAKLRAESDAKQHAVEAELAAKLTAAEARITETKAAAMSNVTAIAQEAASAIVQQFTGKAPDAKKLTAALKAKA | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q89V70 | MAESHGGAKGPAAGAHTGAEGGHGGGFPPFESSTYASQLVSLAIFFVVLYVIVSKLALPKVGGAIEARQNKIEGDLAEAQTLRDQSDAALKAYESELASARSRAQAIGNESRDKANAQAETERKALEEQLAAKLAGAEKTIASTRTAAMSNVRGIAADAAGQIVQQLTGVVPDAASVNAAVDASLKG | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A6WW80 | MDATFWALIGLIIFLAILAYLKVPGMVGRSLDERADRIKNELEEARTLREEAQQLLAEYHRKRKEAEKEAGDIVASAEREAKALLEDAKRATEEYVARRNKLAEQKIATAEVDAINAVRASAVDLAVAAAGKIVADKVDTKVAGNLFKDALSQVKSNLN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A4WNY8 | METEVHEAAGAAGHAGQAVGMPQLNFDYWPNQIFWLLVTLVAIYFLLTRVALPRIGAVLAERRGTITNDLAAAEELKQKAVLAEKAYNEALAKARAEAQAIIAETRAAIQAELAVATAKADAEIAAKSAESESRISEIRAGALQSVTEVAKDTAEALVAALGGKSDAASVDAAVAARMKG | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A8J785 | MASLLARPQQAVVRAAKPAAARPLRLVVRASAQKPQQQLAQLAKPALSAIVANALMAMPAAAEAGKIFDFNLTLPVMAGEFLLLMVFLEKTWFTPVGKVLDERDNLIRSKLGSVKDNTGDVDKLVLEAETILKSARSDVSAMINTKKAAKQSELDKTYNEAKAKITAEVESSIAGLEQESASMLKSLDAQVDKISAEVLKRVLPEGVRV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q65DX0 | MSFLPQVMGAGVGFNAGTMLFQLVAMLILLALLKKYALGPLLNIMKEREDYITGEISSAEKKNEEAKKLIEEQQALLKEAREESQSLIENAKKLGEQQKDEIIKAARQEAERMKESARSEIVKERDQAVTALREQVASLSVMIASKVIEKELDEQAQEKLIQDYLKEVGESR | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
P09221 | MLWKANVWVLGEAAHGISGGTIIYQLLMFIILLALLRKFAWQPLMNIMKQREEHIATKSTRRKNDRQEAEKLLEEQRELMKQSRQEAQALIENAASLAEEQKEQIVASARAEAERVKEAAKKEIEREKEQAMAALREQVASLSVLIASKVIEKELTEQDQAAS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q8A9U9 | MSLLLPDSGLLFWMFVAFGVVFVILAKYGFPIIIKMVEGRKTYIDQSLEVAREANAQLAHLKEEGEALVAAANKEQGRILKEAMEERDKIVHEARKQAEIAAQKELDAVKQQIQIEKDEAIRDIRRQVAVLSVDIAEKVLRKNLQDKESQMGMIDRMLDEVLTPNKN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q6MGM3 | MHMKLILNLLVLLAPAAVFAAGGGHGDGHIPTSTIMFQAINLTILFAAIIYFTKDAIVSFFAGRKAAYLEAAQKSAFAREQAEKEFVDIKNKLANLDQTREENLRKAQTHAEDLKKQILEEANDVTKRIKNDAELTARLEVQRAQKELRTQLLQDSVEAARIVLTKDLGSSDQQKLQKDFINNVGV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q8G7A9 | MMTQAASGIDLFIPEVYDIVWSLIILVIVAVFFYKFFMPKFNAIFDERAAKIQGNIAKAEQARKDADEAKAKYEAQLSTARVDAAKIRDDARAEASHIIADARSRAESDAAQITASAQRSIESQHQQAIVSLKGEVGALATALAGKILGAKLEDNDVQSSMIDSMIDDLGAKK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q06J69 | MNDLFLFNNSFQDSFEINTDLFDTNIINLSIVLFVVIRFLGEALSDTLENRKQTIIDSLQNSNKKVYIVKNKLVEVKSKLELTQTEVENVYSSRFSYFKTRKQTLLEQVQSYLTQLQSLQKDSIEGQTKKVLSDVYDTTISKTFDTLYINLASAFKKSGNFSNKKKAITYSYLKRLN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A6W7G5 | MLVAAFAAAGEEVEGNPTYPILPHLGELIVGIIFAIIIYAVIAKKVVPRLEAMYEERRAAIEGNVEKAEKAQAEAQVALEQYKAQLADARGEANRIREEARQQGAQILAEMREQAQAESERITTAARATIEAERVQATAQLRAEVGRLATDLAGRIVGESLQDSARQSGVVDRFLADLERSESGASSR | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q1IIG4 | MYAQEAQQKPEAQQSAPAAEQPKPAEEQAKPEQHVTNPNAAVGKELSEASHAAEGEEEAGEHMELKHSTMVKTLAKWLGVSVETSYWIAMAFNFAIVFALLGWAMKKNLPGVFKARNESIQRGIAEARAASDDAKRRLADIEARLSKMDGEVAAIRAVTEKESAAEEVRIREAAEADVKRILESAENEIDAATKQARRDLKSLAAGLAIDLATRKLHVDQQTDESLVRSFVAQLGKDGK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q9RGY5 | MTIQTLFAASHHIYLGNAIWYLLCFAILMLLIKHYAWGPVSDMMEKRRQKIISDLDSAASDRKKAETLANEREAALKNSRQEATQILSDAKTNAQNTSKEIVASANEDAAAIRKKANEEAAKAKSDALDAARDQVADISVAIAEKVIAKNLSAEDQKDLVDQFIKGLDD | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
P0A2Z0 | MSTLLLEAAPNTVLGNIIVVSGAFIILLVLLRLFAWNAITSVFASRAKKISDDIDAAEANNKQAADLVKQRQAELAGSKEEAANIIQVANDTASQNRAKVLATANEEATSLKKRAQEDIEQERKEALNTVKGDVADISVQIAEKLIGQSLDASAQQELIDSYLAKLGE | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A9KK96 | MYSTTVLATGTKDTSLVNRIFGLDMQLVVDVAIMGLAIFVLFLILSYLLFNPARELLQKRQDRIKEEMDSSAKDKKEATQLKTNYEAKIKEASKEVDEILSEGRKKALKRENDIVDEAKVEASRIVDRANKEIELNKSKMKDEVKQEMIAVASVMAGKIIAGNIDETKQKQLIDEALNEMGDETWQN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q88UT9 | MLSHLIIGASGLYLGDMLFIGISFIVLMALISVVAWKPITKMMADRADKIANDIDSAQKSRQEASDLADQRRDALSHSRAEASEIVADAKKSGEKQRSSIVADAQNEATQYKQNARKDIEQERQDALKNVQSDVADISVAIATKIIKKQLDPEGQQALINSYIEGLGKHES | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A8F3J8 | MGFVELNLTGIIQLLNFLILLFVLYKFLYKPFLQIADKRREKIQSDLASAEKELKEAQEMKKQAHDALESARKSADGIISEARQKSEEIINQAKVKAREEAEKVLNSARNEIEREKKQALQEIEKRAGEIAVTLALKILQGVLDEKAKREYLINILNKEKEK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q88BX0 | MNINATLIGQSVAFLIFVLFCMKYVWPPVITALQERQKKIADGLDAANRAARDLELAQEKAGQQLREAKAQAAEIIEQSKKRAAQLVDEAREQARVEADRVKAQALAEIEQELNSAKDALRAQVGALAVGGAEKILGATIDQNAHAELVNKLAAEI | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
B0U5A2 | MDITFTIFAQSIAFAALIWIVATKIWPPLIKVIEERQQKIAEGLAAADLGQKELAQAQEEIKKTLKNAREKANEIIEQAHARAHQIIEAAKAEAITETNRQQNLAQVEIEAAAKRAREELRKHVSILAVNGAEKLLKREIDVNTHKMLLDELAAEI | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q6C105 | MPFARVGALSARHYSNQVDPKVKATSILDSIPGNNVLSKTGVLATGVLGSIYAISNELYIVNDESIVLGVFAAFVVVVAKLGGPGYTSWADGYIENMRNILNTTRDKHTDAVKERIGDVSKLKDVVKTTQDLFAVSKDTVKLEAEVFETKQQVVLAAEAKSVLDSWVRYENSVRQREQKLLTETVISKIEKDLKDPKFQQKILQQSVEDIEKLFAKA | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain . F-type ATP synthases consist of two structural domains, F(1) - containing the ex... |
A1JTD1 | MNLNATILGQAIAFVLFVLFCMKYIWPPIMAAIEKRQKEIADGLSSAERAKKDLDLAQANATDQLKKAKAEAQVIIEQASKRKAQILDEAKAEAEQERNKIVAQAQAEIDAERKRAREELRKQVAMLAIAGAEKIIERSVDEAANSDIVDKLVAEL | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q9Z688 | MAGAGLIIIKRRIKSITNTKKITNAMGLIATSNLRKSRQNLEANKAYYEAFNDVINKIVSSSSKSNLYVAGNKSDKKLYIALTSDSGLCGGFNGAVVTAADNVMRGDKDKSLLITVGQKGISYFKRLKYETLSEYVDIPNEPGLKEAKEIADRALSLYEKGEIGEVHVIYTQFLSTVNQKVEVKKVLPIEPKKMEKVSVAEFEPDAEIILEKAIRLHIEQQLFNLLLNSKASEQASRMSSMDSATKNANDLLDALNIKYNRIRQSAITQEITEIVGGAEALK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31137
Sequence Length: 282
Subcellular... |
A0LDA1 | MANLKALKVRIGSVKNTRQITKAMKMVAAAKLRKATEQAESARPYSKRMSRMMHSLAPAAAGRDNAPELLVGRGDVKKVNLVVYTADRGLCGSFNSVVIRATRARIAELEKQGFQVMLTFIGRKAYDVLKRSHGHLVRKVYTEMSRHMSFAYVEKNIVKELIKDFHEGQFDACYLVFNQFKSAMSQELTWAQSIPQPIDTEGASTQTGYQFEPVEEELLEELLPRNLAVQVFQALAESEASEHGSRMTAMDNAVRNAGDMVKKLQTKYNRSRQAAITTELIEIISGAESLKG | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32634
Sequence Length: 292
Subcellular... |
Q8EWY9 | MASLNEIKKRIKIIESTSKITNAMKLVSSAKLKKQKELFLNESIYYKKFYDLFTYIKSNSDSEILSLKKSEEGKTIWLAFFSSMGLCGSFNLNIVKELQKHIKSNDEIWLIGKKGKNLIKSKGIEAEISLDLELDDKDINFDLFHIIAENLLAKYKNDYNIKSIKVIYSKFVNSLSFTPSVFSLLPLDKAIEKPRLDKPNNGADFSIQPNANDVFESILIDYLATCIHGAIVESKVCENASRRNAMDSATKNANELIKNYKLEFNRKRQSEITQEITEIVSGAKGE | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32516
Sequence Length: 286
Subcellular... |
Q6F203 | MANLSNLKTQISNTQDIGKITNAMQLVASAKLRRIGKKVTETQEYVSEVYAIFNEIIKHSSESIYLKNSANDIKKTLWVVVNSNLGLCGGYNANVNKLVISNFKKEDQIYAIGSKAVSAYNSKKIKIKNECTDVDIDFSPAQAKQIGNELLSYYSSGEFDEIQIVYTKFINNVTFEPTKLRVFPIIKEETQETSSSYYSFEPSAEEVLNNAVTLYLSTIIFGTIVESQVSEQASRRLAMENATNNGKELEYNLSIQYNRERQASITQEISEIVSGANALMG | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31416
Sequence Length: 281
Subcellular... |
Q6KI81 | MAELQKLSSRLKSVKVTRKITKAMELVAASKIRRAKESFFSNKEYFQIIQDIFDNLASKTEQIFLKKQMKFDKENNTNSILYIVINSDLGLCGAYNSSIAKEIKKEIKSKDKLFLIGKKGLLFLGKFKTQITNLDKVKEISTNYKNIKKISEKILSMFKSGDYKSIKIVYTKYVNAFTYLPTIKHALPILKSEKNINEATFSNLEFEPDPITIFQKAIPLYFSSLLYSCVLESHVSEVSSRRIAMENATKNADELGDQLKIELNTIRQSKITQEITEIVAGSETEI | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32672
Sequence Length: 286
Subcellular... |
Q1AVH8 | MASLRDLKRQIQSVKNIAKVTDALQAVSAVKFRKAEARVKQARPYAENMEEVMRAIASKASTRNPMLAGREQVRRVAVATLTSDRGLCGSFNAQVLRRTVRFREQQGAEALQVASGRKGIAFFRFRRIGLAESYSGFTDDPSYEDAQRIGRGLTRLFEREEADEVYLVYNRFVNPAVQRPVVVRLLPAAPEGGEEGEGGTVSGAPFDFIPDADTILRRLIPQYVETLVWQALLESAAGEHGARMTAMKNATDNANELVDTLTLQMNKARQAQITREISEIAAGAEALAAG | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31900
Sequence Length: 290
Subcellular... |
O50141 | MANMKDVKRRIKSVESTMQITKAMQLVASSKMRKAKERAEAVHPFFEGVFQVMADISRDHEFTSVFTKKKFKNSVLLIVIAGDRGLAGGFNTNVLKLAKAKADAITESGGEAVIMAIGKKAVEYFEKREYKLIDGFPQIAEGIELIDAMMIANKVIERFKIGDFDAVELVYTTFVSVMTQEPQHLRILPVENLEYLGQKHPMTIYDPSPEEVFDSLIPEYMGGMLYSAIVDSFASEQAARRTAMESASDNANEMIEKLSLLYNRARQAQITQEITEISSASLNDNS | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31970
Sequence Length: 286
Subcellular... |
B3EA02 | MASLKSIKKRIVSVKNTRQITKAMKMVSAAKLRRAQENVVAARPYAQKMGEVLQSLAGNLEGNLHPLLEKRDAKKLLLIVVTSDRGLCGGFNTNLCKAGERYIKEKQAEFDQISIMTVGRKGYEFLKSRHTVYKNFANMLSKPNYQAAAMLAQDVIEGYLAEEYDQVVMLFNSFRTVMSQDITFQQLLPIEPEEKIAADENGVEYIYEPSVSDLLTEILPKNIEVQIFKAMLESVAGEHGARMTAMDSASKNASEMIGKLTLQYNRARQAAITTELMEIISGAESIKG | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32124
Sequence Length: 288
Subcellular... |
A0A161CFW5 | MSGKLRLYKEKLEGYNRFYSIVKTIKMVTLAKYRAAQGRIRTRDFSLRYTELAFSKPQASRDAVAAAKNALVYIPITTNRGSCGALNSNIVRCIDSVVSSKMVLMPVGKRGIDSFSKLYPDEFRYGIINDMKESMHFGYATFVIENAYEVSKDADRYQVIFNRFVSAGVQRNAVYNIPSYEKWKEDLADAASSDNQKNRYLFANALQNEEEQLIRDFFDFHAALAVLNAVGENELSEQAARLVAVEGQLTNISSLQQRTSSLYNKTRQFGITAALIEILSAMSSLEGNAMKGVRRNKFWEGAVTK | Function: Mitochondrial membrane ATP synthase (F(1)F(o) ATP synthase) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain . F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous cata... |
B5ZAW2 | MSLDAIKRKISSVQTTAKITNAMKLVATAKLKRQRDRLAAIKEYCHDYYDVIGLLLSVVNDIEFLKIPNAKNRTLYITINSTMGLAGSYNYNVNKLVSKIINEDDITFTIGKKGHDFMRLSNRLHQVNTYLNLNDNDLTFDMSLQIAREALELYSNGEVNKICIIYTKFINAITFEVNNIDVLPFDKTVLTKDNLAETIELAKDNIIFQPNKVELVKKILPTYIATVLYGSLIESKISENASRRNAMDAATKNAKALAEDYKLIYNTLRQGKITREITEIVAGSDD | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32343
Sequence Length: 286
Subcellular... |
Q2LGZ2 | DPLYTKFVSLVKSDPVIHTLLPLSPKGEICDINGVCVDAAEDEFFRLTTKEGKLTVERDVVRTKTTDYSPILQFEQDPVQILDALLPLYLNSQILRALQESLASELAARMSAMSNAAA | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13024
Sequence Length: 118
Subcellular... |
Q8D3J4 | MYNIKDIRQKIIGIKKTQSITSAMEKISAIKMKKSQNLLNSTKPYYEKISLLLNKLLFQNIKYKHPYLKKRQIKCIGYIVVSTDRGLAGSLNINLFKKLLYEINKSKEKKINTKLVLIGSKAISFFRFFEDEIISTISGIGDTPKISELIKPVQIMLKEYDSNIIDKIYIISNKFINTMTYVPDIKKVLPISIKKSSIKFKNLNYLYEPDFSSLFESILPRYIESLIYQSIVENISSEQSARMVAMKSAMDNSKNLIEELSLIYNKARQSNITKELTEIIAGSNNIY | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33088
Sequence Length: 287
Subcellular... |
B3TN45 | MNIIPCSIKTLKGLYDISGVEVGQHFYWQIGGFQIHAQVLITSWVVITILLGSVLIAVRNPQTIPTDGQNFFEYILEFIRDLSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGALLPWKIIELPHGELAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFEKYIKPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27320
Sequence Length: 247
Subcellular Location: Plastid
|
O63075 | MNPLLEIAEVSVGQHYYWELGGYELHGQVLITSWVVLGILAVLSFLGNTNLKSTPDGFQNFTELVTEFIRDLAKTQIGEEDYLKWVPFLGTIFLFIFVSNWSGALLPYRLIEIPNGELAAPTNDINTTVALALLTSISYFYAGISKKGLGYFSRYVEPAAFLLPINVLEDFTKPLSLSFRLFGNILADELVVGVLVALVPLIIPIPIMLLGVFTSAIQALVFATLAGAYINEALADHH | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
P22483 | MAFLGAAIAAGLAAVAGAIAVAIIVKATIEGTTRQPELRGTLQTLMFIGVPLAEAVPIIAIVISLLILF | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
O66564 | MMKRLMAILTAIMPAIAMAAEGEASVAKGLLYLGAGLAIGLAGLGAGVGMGHAVRGTQEGVARNPNAGGRLQTLMFIGLAFIETIALYGLLIAFILLFVV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q5P4E7 | MENVLGFVALAAGLIIGLGAIGACIGIGIMGSKYLEASARQPELMNALQTKMFLLAGLIDAAFLIGVGIAMMFAFANPFQLV | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
B6YR09 | MLLSILLQVATGTGLAKLGEALGAGLAVIGAGLGIGKIGESAMEGIARQPEAAGDIRMNMIIAAALVEGVSLFAVVVCGFLL | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q98QU0 | MENIISLLALKNDPTSATTGAGLVAVGAGLASIGNFGTGLGQGLSAGRAAEAVGRNPEAIKKIRSLMIIGMAISESASLYSFIIAILLVFVY | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q4A5Z9 | MNQLQNLAEALSASSPVSGTVQTVVDGNTTTTTTTNTGLGVVAVGAGLAMIGAIGSGLGQGYAAGKTVEAVGRNPEMISKIRATFIIGAGIAETASIYSFIVALLLIFVGK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
B2A3G7 | MIDGQSLVLAASAIGAGLAMIAGIGAGIGQGFAAGKGAESVGRQPDAQGDIIRTMLLGAAVAETTGIYALVIALLLLFANPLIGML | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q3J6M6 | MDPELLVSIYASTAVSVGIILAAAGLGSALGWGLICSKYLEGIARQPEMRPQLMGQMLFTGGLMEAFPMIVLGMSMWFIFANPFTGAALAAIGS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q04G25 | MNYIAAGIALCGSAIGAGIGNGMLMAKLIESIARQPELEGNLRTNMFISMALVEAMPIIVIAMSFVLINE | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q8DLP7 | MNPLIASASVLAAALAIGLASLGPGLAQGNASGQALEGIARQPEAEGKIRGTLLLSLAFMESLTIYGLVIALVLLFANPFAS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
B5YGC8 | MRKFFVILMVALVVVLTASAVFAADSDPAKLNYYGYATAGALIGLGAAAGGGGAGMGQGLRGILEGSARNPGVTGKLMTLFIVGLALIESLVIYVLVFVLITFYANPFVK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q83HY5 | MGSVLAEVAGSLASIGYGLAAIGSAIGVGIVVGKTVESVARQPELAKRLTVLMYVGVAFTEALALIGIGTYFLFR | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
B5ZAW9 | MSSFIDITNVISSHVEANLPAVSAENVQSLANGAGIAYLGKYIGTGITMLAAGAVGLMQGFSTANAVQAVARNPEAQPKILSTMIVGLALAEAVAIYALIVSILIIFVA | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A1WF53 | MEIILGFVALACGLIVGLGAIGASIGIGLMGGKFLESSARQPELINELQTKMFILAGLIDAAFLIGVAIALMFAFANPFVSTLLANMPK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
P0A309 | METLLSFSAIAVGIIVGLASLGTAIGFALLGGKFLEGAARQPEMAPMLQVKMFIIAGLLDAVPMIGIVIALLFTFANPFVGQLG | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
Q8D3J8 | MNSINADLLYISAAIIMGFASIGAAIGIGILGGKFLEGAARQPDLIPTLRTQFFIVMGLVDAIPMISVGLGLYLIFAAS | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
P59384 | MLLLGISILALAWRPAGSSEPEWEVVVPIRRDPDINGRHYYRRGTEDSGDQGLIFQITAFQQDFYLHLTPDAQFLAPAFATEYLGVPLQRLTGSSLDLRRCFYSGYVNAEPDSFAAVSLCGGLRGAFGYRGAEYVISPLPNTSAPEAQRHSQGAHLLQRRGAPVGPSGDPTSRCGVASGWNPAILRALDPYKPRRTGAGESHNRRRSGRAKRFVSIPRYVETLVVADESMVKFHGADLEHYLLTLLATAARLYRHPSILNPINIVVVKVLLLGDRDTGPKVTGNAALTLRNFCAWQKKLNKVSDKHPEYWDTAILFTRQD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease which has proteolytic activity against the proteoglycan VCAN, cleaving it at the 'Glu-1401-|-1402-Ala' site . Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle de... |
Q5W7F4 | MPCCLWAALSLLLAVVGAGAWTPPRQPLLLTPRHRRHAQETHHLRLLGWDLKLKENKAIRSPYYKECQFFTGRVLHEEGSAVTVTECDGQLYGLLQVGGEEFVLQPTRTQEKHVLRRRDVTHSERSAEYNLTGDTVIDLDLDFDEDDDLLPTSHVHPRHSDHSDKEYFHDMHLFRRPASGVKGLWLELAIVADNTMLKFHGRERVKHYILALMNIVSAIFNDPSLGSNITLVINKLFLYEDKDIILKYGNIKKSLEAINKWNYRHLMKLPEGSTGWDATIWLTRSQLGGPSGFAPVGGVCTKTRSAAIDRDEGLTSAFVI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in larval molting and metamorphosis. May degrade extracellular matrix (ECM) and basement membrane (BM) during the development of organs to allow degeneration and remodeling of tissues.
Sequence Mass (Da): 113853
Sequence Length: 1007
Subcellular Location: Secre... |
Q9UHI8 | MQRAVPEGFGRRKLGSDMGNAERAPGSRSFGPVPTLLLLAAALLAVSDALGRPSEEDEELVVPELERAPGHGTTRLRLHAFDQQLDLELRPDSSFLAPGFTLQNVGRKSGSETPLPETDLAHCFYSGTVNGDPSSAAALSLCEGVRGAFYLLGEAYFIQPLPAASERLATAAPGEKPPAPLQFHLLRRNRQGDVGGTCGVVDDEPRPTGKAETEDEDEGTEGEDEGAQWSPQDPALQGVGQPTGTGSIRKKRFVSSHRYVETMLVADQSMAEFHGSGLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIHDEQKGPE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Cleaves aggrecan, a cartilage proteoglycan, at the '1938-Glu-|-Leu-1939' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover (By similarity). Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with... |
P97857 | MQPKVPLGSRKQKPCSDMGDVQRAARSRGSLSAHMLLLLLASITMLLCARGAHGRPTEEDEELVLPSLERAPGHDSTTTRLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSPGSEAQHLDPTGDLAHCFYSGTVNGDPGSAAALSLCEGVRGAFYLQGEEFFIQPAPGVATERLAPAVPEEESSARPQFHILRRRRRGSGGAKCGVMDDETLPTSDSRPESQNTRNQWPVRDPTPQDAGKPSGPGSIRKKRFVSSPRYVETMLVADQSMADFHGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Cleaves aggrecan, a cartilage proteoglycan, at the '1691-Glu-|-Leu-1692' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover. Has angiogenic inhibitor activity (By similarity). Active metalloprotease, which may be associated with... |
A0A0U5GGX2 | MVDKSNKVALVLGATGISGWALAKNALSYPSRSTFQRVIGLMHRPRTVEETGLPNDPRLELYSGVDLQGDLNHVVVKLKEKIPRIEEVTHVYYLAYMTLQTCSGDMRQFRDANVAMTYTAVHACDRLCPNMEFFVLQTGTNAYGVACFDYLRQTQLQVPLRESNPRVPRPWSDTLFYYAQADLIKEANKGKAWKWCEVRPDQIVGHTPAQVSVPYVAPMALYLALYRYINGPGARVQFPGTVRNYHHTYTDVRPDTMARAELYLSLVKSDESHGEAFNIADTDTPGPWSAKWPSICRYFGLEASETIDDEWTDIDGWWYA... | Function: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl t... |
A0A0U5GJ41 | MTILDKRQIQRFASDTDIETLSKAIDDDGVAIVRSVVSRDVIQRLQKEVESSDQPVWLEDNPSLKDSKFPSQARHANNLVPASKTYRDDILNNSAVHTTCKAVFRDVGDYWLTTGILRTTKPGSPAQGFHRDALLYPVLQYQPPTSPPLTVALLVSMTDATVANGATRVILGSHKWETVGTPSEDQAVRAELDAGDMLVIHQRLVHAGGEHTHQAPDTRRMLLMFLTSCQLVALESPLALSRELVETMTPLAQKMVGWRTVRPVEPNTVGLNTHRSGCLEDGLKLRAAKPLEGQDGH | Function: Iron/alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsellinic acid is then prenylate... |
A0A1U8QGE6 | MTIIPKRSYNVLTTCKAVFRDVGDYWLTTGNLRTTKPQSPAQGFHRDTLLYPVLQYQPATSPSLIVTLLVSMTDATVANGATRVILSSQNGRLLNTIGGPGRASRAKRWGHAGNPSAAAARWWEAYESGTEYKTNATNFLHKMLASCS | Function: Iron/alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsellinic acid is ... |
A0A0U5GHD4 | MYNLKNQVIVITGSSSGIGLAASTIALSSGAKVFGVDIRPPPSTLTSQSNYACLQYDLSSSSTVSDIVAACEGAFGPRIDGLLNIAGVMDLNQSADTLADEIWERCIAVNLTAPVKLMREVLPVMQRQGGGSIVNVASKAALSGAVSGVAYTASKHGLVGATKNVAWRFKHERIRCNVVCPGGVGATSIRDGVDVTQFDAAALETMALIHQAHGCDREKGVELQPQDIAHMLLFLLDERSRGVSGAVIPVDNAWSTI | Function: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl t... |
P9WEP2 | MFIISQYREHRSLSILTQTCTIFRSMQVSSKHENLSVSFHLTPLQVLIITGTSSGIGLAAATMALEEGAKVLGVDISKPPDSLARHANYQFFQADLSHPEAPARVVEACSRTYGDRIDGLLNIAGVMDLNQSADSLSDNVWERCISINLTAPVKLMREVIPIMKLRGKGSIVNVASKAALSGAVSGVAYTASEHPWP | Function: Short chain dehydrogenase; part of the gene cluster A that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsellinic acid is then prenylated by th... |
A0A0U5GJZ5 | MQPSLLDRISSVTGNRSKRHAKFRLGRLQQPPTESTTRLAISDGAQAIDETKSPRQSEPGATQCKSEGSGDDIADGPQPMPAPNEGDTPTLDELQQGPNPRGSGIVSGWKLAAVLTALSLAVFCMALDSTVLSTAIPKITAEFNSLHDMGWYVSAYNLTISSFSLIYGKLYSLYRVKWVYLSTLFLFEAGSLVCGAAPSSLALIIGRAIAGVGGAGVFLGSMIIVHEIMPLHHVPLFLSLISGLYGIASVVGPLLGGVFTDYVSWRWCFYINLPIGGVTALIIVLFVRPRARDQATVKKTVWAQFLELDPLGMVLILPAV... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65630
Sequence Length: 614
Subcellular Location: Membrane
|
Q96247 | MSEGVEAIVANDNGTDQVNGNRTGKDNEEHDGSTGSNLSNFLWHGGSVWDAWFSCASNQVAQVLLTLPYSFSQLGMLSGIVLQIFYGLLGSWTAYLISVLYVEYRARKEKEGKSFKNHVIQWFEVLDGLLGSYWKALGLAFNCTFLLFGSVIQLIACASNIYYINDHLDKRTWTYIFGACCATTVFIPSFHNYRIWSFLGLGMTTYTAWYLAIASIIHGQAEGVKHSGPTKLVLYFTGATNILYTFGGHAVTVEIMHAMWKPQKFKYIYLMATLYVFTLTIPSAAAVYWAFGDALLDHSNAFSLMPKNAWRDAAVILMLI... | Function: Carrier protein involved in proton-driven auxin influx. Mediates the formation of auxin gradient from developing leaves (site of auxin biosynthesis) to tips by contributing to the loading of auxin in vascular tissues and facilitating acropetal (base to tip) auxin transport within inner tissues of the root ape... |
P57094 | MSMSVNEKGICYLPDLGSSFTEDAPRPPVPGEEGDLVSSDGRQYNHSFYSSKSDSLKNEASIATPRRPDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGIHLFRTFLKQEECADMLDFWFACSGFRKQEANDGNEKMLKLAKAIYKKYILDNNGIVSRQIKPATKSFIKDCVTKLHIDPAMFDQAQTEIQTMMEENTYPLFLKSDIYLEYTRTGGESPKLFSDQSSVSGNGKVLPGYLPTVIEDVEWRCDQEEEQIAESDPTPSNRLTQKLPLETVPQRVANSKRYQDNREYRHASWREPVNPYYVNSGYALAPATS... | Function: Component of the beta-catenin destruction complex required for regulating ctnnb1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling . Controls dorsoventral patterning via two opposing effects: down-regulates ctnnb1 to inhibit the Wnt signaling pathway and ventralize embryos, but a... |
O15169 | MNIQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDPRPASYSFCSGKGVGIKGETSTATPRRSDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACTGFRKLEPCDSNEEKRLKLARAIYRKYILDNNGIVSRQTKPATKSFIKGCIMKQLIDPAMFDQAQTEIQATMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGISGYLPTLNEDEEWKCDQDMDEDDGRDAAPPGRLPQKLLLETAAPRVSSSRRYSEGREFRYGSWREPVNPYYVNAGYALAPATSAND... | Function: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling . Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but a... |
P57095 | MNRTLTDPMVSSFREDDPRPPVPGEEGETTCHHPSKLAMMRPKDPVKTIMADLRCSTARRDEDGLGEPEGSASPDSPLARWTKSLHFLLGDQDGAQLFRAYLEREKCVDTLDFWFACNGFRQMDLKDTKTHRVAKAIYKRYIENNSIVAKQLKPATKTFIRDNIKRQQIDSAMFDQAQMEIQTAMEENAYQMFLTSDIYLEYVRTGCENPSHVNPNGLGGLKLVCGYLPTLNEEEEWSCNDFKAKALATVVGLSAKTLRSPPLRAVEALEKGYRSYRRSDPGNPNRFTSGYSFAPATSANDSEVSSDALTDDSMSMTDSS... | Function: Component of the beta-catenin destruction complex required for regulating ctnnb1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). Controls dorsoventral patterning by down-regulating ctnnb1 to inhibit the Wnt signaling pathway and ventralize embryos .
PTM: ADP-ri... |
Q9Y2T1 | MSSAMLVTCLPDPSSSFREDAPRPPVPGEEGETPPCQPGVGKGQVTKPMPVSSNTRRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGIKKQQIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVVCGYLPTLNEEEEWTCADFKCKLSPTVVGLSSKTLRATASVRSTETVDSGYRSFKRSDPVNPYHIGSGYVFAPATSANDSEISSDALTDDSMSMTDSSVD... | Function: Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B.
PTM: Probably phosphorylated by GSK3B and dephosphorylated by PP2A.
Sequence Mass (Da): 93568
Sequence Length: 843
Domain: The tankyrase-binding motif (also named TBD)... |
O70240 | MSSAVLVTLLPDPSSSFREDAPRPPVPGEEGETPPCQPSVGKVQSTKPMPVSSNARRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSVVSKQLKPATKTYIRDGIKKQQIGSVMFDQAQTEIQAVMEENAYQVFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVLCGYLPTLNEEEEWTCADLKCKLSPTVVGLSSKTLRATASVRSTETAENGFRSFKRSEPVNPYHVGSGYVFAPATSANDSELSSDALTDDSMSMTDSSVD... | Function: Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B.
PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination and subsequent activation of the Wnt... |
Q9ZV69 | MAEPKTKYDRQLRIWGELGQSALETASICLLNCGPTGSEALKNLVIGGIGSITIVDGSKVEIGDLGNNFMVDAKSVGQSRAKTVCGFLQELNDSVKANFVEENPDTLISTDPSFFSQFTLVIATQLVEDSMVKLDRICREANVMLVLARSYGLTGFVRISVKEHTAIETKPDHSLDDLRLNSPWPELKSYVESIDLNVEEPAAHKHIPYVVILVKVAEEWAQHHSGNLPSTREEKNEFKDLVKSKMVSADEENYKEALLAAFKVFAPTGISQEIQDINHDSCAEVGSNSSDFWVMVAALKEFISNEGGGEVPLEGSMPDM... | Function: Regulatory subunit of the dimeric ECR1-AXL1 E1 enzyme. E1 activates RUB1/NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a RUB1-ECR1 thioester and free AMP. E1 finally transfers RUB1 to the catalytic cyst... |
P38928 | MTQLQISLLLTATISLLHLVVATPYEAYPIGKQYPPVARVNESFTFQISNDTYKSSVDKTAQITYNCFDLPSWLSFDSSSRTFSGEPSSDLLSDANTTLYFNVILEGTDSADSTSLNNTYQFVVTNRPSISLSSDFNLLALLKNYGYTNGKNALKLDPNEVFNVTFDRSMFTNEESIVSYYGRSQLYNAPLPNWLFFDSGELKFTGTAPVINSAIAPETSYSFVIIATDIEGFSAVEVEFELVIGAHQLTTSIQNSLIINVTDTGNVSYDLPLNYVYLDDDPISSDKLGSINLLDAPDWVALDNATISGSVPDELLGKNS... | Function: Required for haploid cells axial budding pattern. Acts as an anchor to help direct new growth components and/or polarity establishment components like the BUD5 GTP/GDP exchange factor to localize at the cortical axial budding site. Regulates septin organization in late G1 independently of its role in polarity... |
P50080 | MKGEPKTYSMSDLSYYGEKAQQQNEKQQKQYVVRRNSTQSTSKQNVSVVLEDNASESNELPKGFILYASLIALALSLFLAALDIMIVSTIIEEVAKQFGSYSEIGWLFTGYSLPNALLALIWGRIATPIGFKETMLFAIVIFEIGSLISALANSMSMLIGGRVIAGVGGCGIQSLSFVIGSTLVEESQRGILIAVLSCSFAIASVVGPFLGGVFTSSVTWRWCFYVNLPIGGLAFFLFLFFYNPGLSTFQETMDNIRKFPSQFIEIVRNVAYHLLKIKGFSKLNGWRKPFMELIFMYDIIEFVFCSAGFTCILLAFTFGG... | Function: Transporter protein required for adaptation to high stress imposed by low-chain organic acids, in particular by acetic acid, and for resistance to azoles, especially to ketoconazole and fluconazole.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67169
Sequence Length: 613
Subcellular Locat... |
A1B2F3 | MKDWLFRIATCSIMTFSSLAAAQAEPLDVVATFSIIGDFAAKVGGDRIRLNVLVGPDSDTHVYEPRPADAIALAGADVVLTNGLEFEGFLTRLIAASGTDAAVATLTDGVETMEEPGGGHYHYIDGKAVFHAGAHDPHAWQAVPNAKVYVQNIAAAFCAADAEGCAAYQANAARYIGELDALDTEIRAAIAALPQDRRTVVVAHNAFRYFEAAYGVHFLSPQGVSTESEAAAADVAGLIREIRARNASAIFAENISDTRLLEQIAREAGLPLAGTLYSDALSGPDGPASNYIAMMRHNAGAIAAALAAR | Function: Part of the ATP-binding cassette (ABC) transport system AztABCD involved in zinc import . Binds zinc with high affinity and specificity and delivers it to the membrane permease for translocation into the cytoplasm .
Sequence Mass (Da): 32387
Sequence Length: 309
Domain: The D-loop is required for the efficien... |
P04377 | MRNIAIKFAAAGILAMLAAPALAENIEVHMLNKGAEGAMVFEPAYIKANPGDTVTFIPVDKGHNVESIKDMIPEGAEKFKSKINENYVLTVTQPGAYLVKCTPHYAMGMIALIAVGDSPANLDQIVSAKKPKIVQERLEKVIASAK | Cofactor: Binds 1 copper ion per subunit.
Function: This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen. Serves as a direct electron donor to the nitrite reductase.
Sequence Mass (Da): 15647
Sequence Length: 146
Subcellular Loca... |
P80401 | MFHHSLAAAAAALLALAAPGFAATHEVHMLNKGESGAMVFEPAFVRAEPGDVINFVPTDKSHNVEAIKEILPEGVESFKSKINESYTLTVTEPGLYGVKCTPHFGMGMVGLVQVGDAPENLDAAKTAKMPKKARERMDAELAQVN | Cofactor: Binds 1 copper ion per subunit.
Function: This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen.
Sequence Mass (Da): 15446
Sequence Length: 145
Subcellular Location: Periplasm
|
Q52825 | MPLKFGLIVATAALIASAASLMAADHQVQMLNKGTDGAMVFEPGFLKIAPGDTVTFIPTDKSHNVETFKGLIPDGVPDFKSKPNEQYQVKFDIPGAYVLKCTPHVGMGMVALIQVGDNPANLEPIKIAKVPNMVRKRLDADLAQITPAQITQ | Cofactor: Binds 1 copper ion per subunit.
Function: This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen.
Sequence Mass (Da): 16283
Sequence Length: 152
Subcellular Location: Periplasm
|
Q6P3P5 | MLISARRLRRCQFFQLLTSCFVLSLMALLVQEDNSLINHVKSYSYRYLINSYDFVNDSLSVPRDRPDGAPSYRYLINNRDKCQNEDVLLLLFVKTSPENRRRRNAIRKTWGNEDYIRSQYAANIKVVFALGIEADPVKSHQTQKDLVIENKRFNDLIQQDFKDTFHNLTLKLLLQFGWVNSYCPSAKFIMSADDDIFVHTPNLVSYLKSLPIETQDFWIGRVHRGSPPIRSKTSKYYVPYEMYPWSSYPDYTAGAAYVVSKDVAAKVYEASQTLNTSLYIDDVFMGICANKMGVVPQYHVYFAGEGKAPYHPCIYNKMIT... | Function: Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids.
Catalytic Activity: a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-N-acetyl-alpha-D-glucosamine = a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1... |
Q6ZMB0 | MAFPCRRSLTAKTLACLLVGVSFLALQQWFLQAPRSPREERSPQEETPEGPTDAPAADEPPSELVPGPPCVANASANATADFEQLPARIQDFLRYRHCRHFPLLWDAPAKCAGGRGVFLLLAVKSAPEHYERRELIRRTWGQERSYGGRPVRRLFLLGTPGPEDEARAERLAELVALEAREHGDVLQWAFADTFLNLTLKHLHLLDWLAARCPHARFLLSGDDDVFVHTANVVRFLQAQPPGRHLFSGQLMEGSVPIRDSWSKYFVPPQLFPGSAYPVYCSGGGFLLSGPTARALRAAARHTPLFPIDDAYMGMCLERAG... | Function: Beta-1,3-N-acetylglucosaminyltransferase that synthesizes the core 3 structure of the O-glycan, an important precursor in the biosynthesis of mucin-type glycoproteins. Plays an important role in the synthesis of mucin-type O-glycans in digestive organs.
Catalytic Activity: 3-O-[N-acetyl-alpha-D-galactosaminyl... |
Q8NFL0 | MSLWKKTVYRSLCLALALLVAVTVFQRSLTPGQFLQEPPPPTLEPQKAQKPNGQLVNPNNFWKNPKDVAAPTPMASQGPQAWDVTTTNCSANINLTHQPWFQVLEPQFRQFLFYRHCRYFPMLLNHPEKCRGDVYLLVVVKSVITQHDRREAIRQTWGRERQSAGGGRGAVRTLFLLGTASKQEERTHYQQLLAYEDRLYGDILQWGFLDTFFNLTLKEIHFLKWLDIYCPHVPFIFKGDDDVFVNPTNLLEFLADRQPQENLFVGDVLQHARPIRRKDNKYYIPGALYGKASYPPYAGGGGFLMAGSLARRLHHACDTL... | Function: N-acetyl glucosamine (GlcNAc) transferase that catalyzes the transfer of GlcNAc via a beta1->3 linkage from UDP-GlcNAc to the non-reducing terminal galactose (Gal) in the linearly growing chain of N- and O-linked keratan sulfate proteoglycans. Cooperates with B4GALT4 galactosyltransferase and CHST6 and CHST1 ... |
Q8K0J2 | MSLWKKTLYKSVCLALALLVAVTVFQRSVTPGQFLQDPLPPTPGPAKTGNLVNPNSFWKSSKDVAAPTPTVPRGPQVWDVITTNCSININLTHQPWFQSLEPHFRQFLAYRHCRYFPMLLNHPEKCAGDVYMLVVVKSVITQHDRREVIRQTWGHEWESAGLGRGAVRTLFLLGTASKQEERTHYQQLLAYEDRLYADILQWDFLDSFFNLTLKEIHFLKWLDIYCPNVPFVFKGDDDVFVNPTNLLEFLSDRQPQENLFVGDVLKHARPIRKKDNKYYIPAVMYGKATYPPYAGGGGFLMSGSLARQLHHACDTLELFP... | Function: N-acetyl glucosamine (GlcNAc) transferase that catalyzes the transfer of GlcNAc via a beta1->3 linkage from UDP-GlcNAc to the non-reducing terminal galactose (Gal) in the linearly growing chain of N- and O-linked keratan sulfate proteoglycans. Cooperates with B4GALT4 galactosyltransferase and CHST6 and CHST1 ... |
Q7Z7M8 | MRCPKCLLCLSALLTLLGLKVYIEWTSESRLSKAYPSPRGTPPSPTPANPEPTLPANLSTRLGQTIPLPFAYWNQQQWRLGSLPSGDSTETGGCQAWGAAAATEIPDFASYPKDLRRFLLSAACRSFPQWLPGGGGSQVSSCSDTDVPYLLLAVKSEPGRFAERQAVRETWGSPAPGIRLLFLLGSPVGEAGPDLDSLVAWESRRYSDLLLWDFLDVPFNQTLKDLLLLAWLGRHCPTVSFVLRAQDDAFVHTPALLAHLRALPPASARSLYLGEVFTQAMPLRKPGGPFYVPESFFEGGYPAYASGGGYVIAGRLAPWL... | Function: Beta-1,3-N-acetylglucosaminyltransferase that plays a role in the elongation of specific branch structures of multiantennary N-glycans. Has strong activity towards tetraantennary N-glycans and 2,6 triantennary glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 43396
Sequence ... |
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