ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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B3E0Z6 | MHQLGIEWNKLIAQIINFVIVLWVLNRFAFKPVLKILEERRKKIAESLQNAEKIKQELAEAEEARKEILRKANEQASFIVAEAQKVASYQGEKKIQEAVEEAKRVLKKAEESAKLEREKAKEEMRREILNLVIEITSKVVGKTLTLDDQERLKNEVLSKLPQKEGHEAYSRN | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19973
Sequence Length: 172
Subcellular Location: Cell inner membrane
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B0JWU9 | MIIDTILLLATEAKEAAAEGFGINTDILGTNLFNLSILLGLIIFYGRKVLGQILGERQSKIAEALAEAENRKNIAATALAEEQKKLALAKQEAEKIIDNSRSRAKAVTADIAAQAELDIQRMRESAAKDLSAEQDRVLVELRQRITALALANVESQLSTGLEESVQQTLIDRSLANLGGK | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19453
Sequence Length: 180
Subcellular Location: Cellular thylakoid membrane
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P80285 | MISNGLILAAAEGANPLIPNPWEILVVVVGFALLMFIVIKFIVPTLEKSYQDRVEAIEGGLAKAEKAQAEANAMMADYESQLADARTEANRIREDARTEAAEIVAEARERATAEATRVFEQAQAQIAAERQQAAAQLKREVGSLATTLAGKIVGESLEDDARSQRVVDRFLADLDRHQSAGVAE | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19904
Sequence Length: 184
Subcellular Location: Cell membrane
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Q2RFX5 | MQAIFQALNFNPWTFLFQTLNLLVVMGLLYVFLYKPLGKVLADREARIEGNLNDAAAAREKAENILAEYRQQLQGARQEAQAILDRATKMAEETRAEIINRAREEAERTLAQARREIEGEKSKALAAIRSEAASLAILAAGKVLERSLTPDDQERLAREAIAEVERLQ | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18879
Sequence Length: 168
Subcellular Location: Cell membrane
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A5IYE1 | MNLFYNLSLKANTLLSAQSGGIKDELKDKFKTLFPTWPMFLATLIAFILVVLILWFLLHKPIKKAMKARQDYIQKNIDEAKLTNDISKQKLNEANKRLAEAYSEADELIKNAKIHGESVIDEYTHKAKNKSKRIIEKAHMEIESERQKMVDDSKSNIAKAAIEISKKIMQKEVTKESQDEVIKNFLKDK | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21810
Sequence Length: 189
Subcellular Location: Cell membrane
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P33256 | MWSTRVKKLLLLSFNFLIISAIVSSCSIPEELQAKTIVNEFFPNFWVFVAHTIALSIIILLGIFLLWKPTKRFLAKRSELIQAEINNANEIKKQAQFLLDNAKKQKQNAELQAREIINLATNQAYRLKNDLETDAKRKANRIIENAHAEIIKQESILKRELEGRIVDVALEATSTLIQKNVAKEDHERLVNELLRNLD | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22801
Sequence Length: 198
Subcellular Location: Cell membrane
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A8M2J7 | MFFLAAEGGETSHSPILPVWQEIVVGLVAFGLLAFVLMKFVFPRMEQTFQARVDAIEGGIKRAEAAQAEANQLLEQYRAQLSEARSDAAKIRDDARADAEGIRQDILAKAREESDRIIAAGKEQLVAERATIVRELRTEVGTLAVDLASKIVGESLADEARRAGTVDRFLDGLESAGAR | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19483
Sequence Length: 179
Subcellular Location: Cell membrane
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Q2S434 | MTALFAQSLVTPSVGLIFWKTVAFLIFLYILYRFGWGPITESLEEREEEIEHSIQRAEEALEEAKAIQAENEEARREAEQKAQQILREARDSAEELREEEKAKTRREIQEMKEQAQAEIEREKQAALQELRDEVADLAIEAAQKIIENDLDADRHRQLVDDALDDFPTN | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19627
Sequence Length: 169
Subcellular Location: Cell inner membrane
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A4XAW6 | MFLAAEGSHNPILPIWQELVVGTIAFALLVFVLLKFVMPRMETMYQARVDAIEGGLKRAEAAQAEANQLLEQYRAQLAEVRTEAARIRDDARADAEGIRQDILAKAREESDRIIAAGKEQLVAERTTIVRELRTEVGTLAVDLAGKIVGESLADEARRAGTVDRFLNGLESAGAR | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19186
Sequence Length: 175
Subcellular Location: Cell membrane
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Q2GGH2 | MANLKALLLRIKSVKSIQKTTKVMQMISAAKLHRVQQKLENAKKHLLELSSIVDYVPSDGVHNCASIAKKERVLLVVMSSDRGLCGNFNNLIVKFTKSYVEKLESSNKEVKLIFFGKKAYDMMYSQYSDKILNVFSNTKSITDFLYFKLFVYNSGIDFDQFDNVMILFNKFYTTILQKPDAQQLIPCNLGIPMLLKEVYQYEPTYVDVLSTISLGYVLNLMYIAFLENSASEHCSRMVAMESANRNTKDMLNRLALEYNRSRQASITTDLIEIISGFESLN | 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): 32170
Sequence Length: 281
Subcellular Location: Cell inner membrane
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B2KEX2 | MESLKDIRDNIKSVQSTQQVMVTMKMISSARIKKAQNAMLNARPFSLGLEGVIDDLRKDILDENNSFKDPDLSKFFKKPDMEKKNIGVLFITADKGLAGAFNALLLRAALNFIKENQDKNIYFFIIGKKGRDFLSRLKQPNVHIVYDAVGIFPKVGYVHADILGEEIINNFLKLDLCEVRVLYNDFKSMGSQKLENQRLIPFDFEIAQGHTEFGEEEHGFLFEPGKEMIFKLLLYRHIKAGLYRILLESQAAELAARMNAMDSASKNAGEIIDTLKVKLNKVRQSSITNEITEIVGAVEALNK | 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): 34307
Sequence Length: 303
Subcellular Location: Cell inner membrane
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C0QTG6 | MAKLSPRDIKRKIQGIKNTQRITKAMKAVSAAKLNKAKAKLNATRPYSERLYDLINDLAMFVDRDIHPLLKIRDEHKVDIVVVTADRGLAGAFNSYVIKTTLGKVKELQEAGKDVNLILIGRKAVQFFKNKGFNIIAEYEDIYRDHMNLSFTSQVGGIIAERYENEKTDAVYLINNELITTATYETKVRKLFPIEPELDYTKLSEISRYNIEPSSEEVLEQLLKRYINFQLYRALVESSTAEHAARMIAMDNATRNAGEAIKRWTIIFNKARQEAITTELIDIINASNAIE | 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): 33202
Sequence Length: 291
Subcellular Location: Cell inner membrane
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Q41075 | MRSFCIAALLAVASAFTTQPTSFTVKTANVGERASGVFPEQSSAHRTRKATIVMDGKANAIRDRITSVKNTRKITMAMKLVRAAPKVRRAQDAVLATRPFSETLQSVFGGLIQRLGGESVDLPLLTEREVKKVTLLVITGDRGLCGGYNSFMIKKAEARFNELKKNGVEADLILVGKKGIAYFERRGFPIRKKYETGQNPTAKQALAIAEEVSSTFLSGESDAVELLYTKFVSLIASSPSIRTLVPFSASDITAKGDEVFQLTSESGQFGVERTELDVAAPQEFPNDMIFEQDPIQIVNAILPLYLNGQILRTLQESVASELAARMQSMQSASDNAGSLAKQLNLEYNRARQAAVTQELLEIISGASALD | 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): 40217
Sequence Length: 370
Subcellular Location: Plastid
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A1VIV1 | MAAGKEIRGKIKSVENTRKITKAMEMVAASKMRKAQERMRAARPYSDKIRNIAAHLSQANPEYTHPFMESNDAKTTGFIVVTTDKGLCGGLNTNVLRLLTTKLKDMQAAGEDAQAVAIGNKGLGFLNRIGVKVAAHATQLGDKPHLDKLIGPVKVLLDAYSEGKIKAVYLCYTRFINTMKQESVVEQLLPLTADRMQPDKTEHSWDYIYEPDAQTVIDELLVRYVEALVFQAVAENMASEQSARMVAMKSATDNAGSVIGELKLIYNKTRQAAITKELSEIVAGAAAV | 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): 31558
Sequence Length: 288
Subcellular Location: Cell inner membrane
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B7GTY8 | MDIITLAEVAGNLSVIGYGIGTLGPGIGLGILFGKAMESTARQPEMSGKIQTIMFIGLALVEVLALIGFVAALIIR | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7816
Sequence Length: 76
Subcellular Location: Cell membrane
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Q494C8 | MEHLNFDMLYIAAAIMMGLAAIGAAIGIGILGSKFLEGAARQPDLIPILRTQFFIVMGLVDAIPMITVGLGLYVMFSAV | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8385
Sequence Length: 79
Subcellular Location: Cell inner membrane
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Q89B44 | MDNVSMDMLYIAVAVMIGLAAIGAAVGIGILGSKFLEGVARQPDLTSLLRTQFFVVMGLVDAIPMIAVGLGLYMLFAVI | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8275
Sequence Length: 79
Subcellular Location: Cell membrane
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B9MS73 | MTALAAGIAMLAGLGVGIGIGIATGKASESIGRQPEAFGRIFPLFLIGAALAEAVAIYSLVIAFMLISKI | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7005
Sequence Length: 70
Subcellular Location: Cell membrane
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Q4AAW2 | MNSIVNFSQQLIQNFQEVSQRTAADSSNLKAFAYLGAGLAMIGVIGVGAGQGYAAGKACDAIARNPEAQKQVFRVLVIGTAISETSSIYALLVALILIFVG | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10522
Sequence Length: 101
Subcellular Location: Cell membrane
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B3PLV3 | METIVNGFNQPNAQASPLAYGLTMVAAGLAIMGAGVVSVGQGMAVAKAVEAIGRNPEATSKIRSTLIMGLAIVETASIYCFIIALLIIFV | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9212
Sequence Length: 90
Subcellular Location: Cell membrane
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C5CA73 | MELHGSLNMIGYGLAAIGSAIGVGLIFAAYINGVARQPEAQRILQPIALLGFALAEALAILGLVFAFVIGA | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7239
Sequence Length: 71
Subcellular Location: Cell membrane
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Q2RFX4 | MATIGFIGVGLAIGLAALGSGLGQGIASRGALEGMARQPEASGDIRTTLLLALAFMEALTLFSFVIAILMWTKL | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7566
Sequence Length: 74
Subcellular Location: Cell membrane
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A5IYE0 | MEKGLIAIGIGISMISGLGVGLGQGLAAGKAAEAVGRNPEAASKIRTMMLVGQAVAESAAIYALVISILLMFAFN | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7505
Sequence Length: 75
Subcellular Location: Cell membrane
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P63692 | MDPTIAAGALIGGGLIMAGGAIGAGIGDGVAGNALISGVARQPEAQGRLFTPFFITVGLVEAAYFINLAFMALFVFATPVK | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8055
Sequence Length: 81
Subcellular Location: Cell membrane
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P33258 | MNIFLVIHELINQADQVNVTLTNHVGAYIGAGMAMTAAAGVGVGQGFASGLCATALARNPELLPKIQLFWIVGSAIAESSAIYGLIIAFILIFVAR | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10001
Sequence Length: 96
Subcellular Location: Cell membrane
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P47644 | MEHVNEILATVGVILQQTQTTQDVNASAKLGAYIGAGVTMIAGSTVGIGQGYIFGKAVEAIARNPEVEKQVFKLIFIGSAVSESTAIYGLLISFILIFVAGA | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10602
Sequence Length: 102
Subcellular Location: Cell membrane
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Q73HW2 | MDLVALKFIAIGLAVFGMLGAGLGIANIFSAMLNGIARNPESEGKMKSYVYIGAAMVEIMGLLAFVLAMLLIFAA | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7826
Sequence Length: 75
Subcellular Location: Cell membrane
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A1JTD2 | MENLNMDLLYMAAAIMMGLAAIGAAIGIGILGGKFLEGAARQPDLIPLLRTQFFIVMGLVDAIPMIAVGLGLYVMFAVA | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8270
Sequence Length: 79
Subcellular Location: Cell inner membrane
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Q3ZBI7 | MAGPEADAQFHFTGIKKYFNSYTLTGRMNCVLATYGSIALIVLYFKLRSKKTPAVKAT | 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 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. ATP5MK is a minor subunit of the mitochondrial membrane ATP synthase required for dimerization of the ATP synthase complex and as such regulates ATP synthesis in the mitochondria.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6435
Sequence Length: 58
Subcellular Location: Mitochondrion membrane
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Q9VR93 | MSDHFNFNEAFNSQTMRGRANVAKATWASLGLVYVLVKMHRRNTKRRETKLYCKGCQQAMLHG | 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 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. ATP5MK is a minor subunit of the mitochondrial membrane ATP synthase required for dimerization of the ATP synthase complex and as such regulates ATP synthesis in the mitochondria.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7303
Sequence Length: 63
Subcellular Location: Mitochondrion membrane
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Q96IX5 | MAGPESDAQYQFTGIKKYFNSYTLTGRMNCVLATYGSIALIVLYFKLRSKKTPAVKAT | 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 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation . ATP5MK is a minor subunit of the mitochondrial membrane ATP synthase required for dimerization of the ATP synthase complex and as such regulates ATP synthesis in the mitochondria .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6458
Sequence Length: 58
Subcellular Location: Mitochondrion membrane
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Q9JJW3 | MAGPESDGQFQFTGIKKYFNSYTLTGRMNCVLATYGGIALLVLYFKLRPKKTPAVKAT | 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 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. ATP5MK is a minor subunit of the mitochondrial membrane ATP synthase required for dimerization of the ATP synthase complex and as such regulates ATP synthesis in the mitochondria.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6408
Sequence Length: 58
Subcellular Location: Mitochondrion membrane
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P65076 | MTDLITVKKLGSRIGAQIDGVRLGGDLDPAAVNEIRAALLAHKVVFFRGQHQLDDAEQLAFAGLLGTPIGHPAAIALADDAPIITPINSEFGKANRWHTDVTFAANYPAASVLRAVSLPSYGGSTLWANTAAAYAELPEPLKCLTENLWALHTNRYDYVTTKPLTAAQRAFRQVFEKPDFRTEHPVVRVHPETGERTLLAGDFVRSFVGLDSHESRVLFEVLQRRITMPENTIRWNWAPGDVAIWDNRATQHRAIDDYDDQHRLMHRVTLMGDVPVDVYGQASRVISGAPMEIAG | Function: Alpha-ketoglutarate-dependent sulfate ester dioxygenase, which oxidizes medium-chain alkyl-sulfate esters. Thus, catalyzes the oxygenolytic cleavage of 2-ethylhexyl sulfate (2-EHS), leading to the formation of succinate and 2-ethylhexanal. Has likely a role in sulfate scavenging in vivo.
Catalytic Activity: 2-oxoglutarate + a primary linear alkyl sulfate ester + O2 = an aldehyde + CO2 + H(+) + succinate + sulfate
Sequence Mass (Da): 32579
Sequence Length: 295
EC: 1.14.11.77
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Q9WWU5 | MSNAALATAPHALELDVHPVAGRIGAEIRGVKLSPDLDAATVEAIQAALVRHKVIFFRGQTHLDDQSQEGFAKLLGEPVAHPTVPVVDGTRYLLQLDGAQGQRANSWHTDVTFVEAYPKASILRSVVAPASGGDTVWANTAAAYQELPEPLRELADKLWAVHSNEYDYASLKPDIDPAKLERHRKVFTSTVYETEHPVVRVHPISGERALQLGHFVKRIKGYSLADSQHLFAVLQGHVTRLENTVRWRWEAGDVAIWDNRATQHYAVDDYGTQPRIVRRVTLAGEVPVGVDGQLSRTTRKG | Function: Catalyzes the oxygenolytic cleavage of 2-ethylhexyl sulfate (2-EHS) in the presence of alpha-ketoglutarate to yield 2-ethyl-hexanal and succinate, the decarboxylated form of alpha-ketoglutarate. It can accept a wide range of alpha-keto acids including 2-oxo-valerate, 2-oxo-adipate, 2-oxo-octanoate, 3-methyl-2-oxo-butyrate, oxaloacetate-alpha-ketoadipate, and alpha-ketooctanoate. It can catalyze the cleavage of medium-chain alkyl sulfate esters such as butylsulfate, pentylsulfate, hexylsulfate, heptylsulfate, octylsulfate, nonylsulfate, decylsulfate and sodium dodecyl sulfate (SDS).
Catalytic Activity: 2-oxoglutarate + a primary linear alkyl sulfate ester + O2 = an aldehyde + CO2 + H(+) + succinate + sulfate
Sequence Mass (Da): 33201
Sequence Length: 301
EC: 1.14.11.77
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Q5W7F3 | MESSVATHWLSAFVILCSFITTQSLNNKIHEHMTIDELRNVFHVEHHSRVPEYHLVQLTHHLARRNIPTSHPANSNSADSGKTPHLKTEKVTKGGYKAPSLLNDEMFVEAKKRIEDVDIMGDPNSTVSVDFKVQSSEFGDSESLSDKEHSAESQEDGVHKIDLEAFGRQLKLVLKKQEGLIKKDGLKVWKALKNETQPHGVDYEEMITEDDEEFGDLYQDEENGAALLIRRHPKHGKLVVEGSIGHDLVIRPIPDTMTSPAQDDEMFMDPSSMADMVSIDTGLPIMKRKKEEQDRLQEALNGAQHVIIKRDPAEVDHMSDYAFMEPDHIGKRYRRKRSAEAHNRQKREAPYVIYPEILVIVDYDGYRLHGGDNVQIKRYFVSFWNGVDLRYKLLKGPRIRISIAGIIISRGRDATPYLERNRVGRDAIDSAAALTDMGKYLFRERRLPVYDIAVAITKLDMCRRQYANDACNRGTAGFAYVGGACVVNKRLEKVNSVAIIEDTGGFSGIIVAAHEVGHLLGAVHDGSPPPSYLGGPGAEKCRWEDGFIMSDLRHTEKGFRWSPCSVQSFHHFLNGDTATCLYNSPHEDDSLPRVLPGRLLTLDAQCRKDRGTSACFKDERVCAQLFCFDAGSGYCVAYRPAAEGSPCGDGQYCINGQCITEHENIIPDYSQHTPSYVRPETSPFYANITSSRH | 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): 77840
Sequence Length: 693
Subcellular Location: Secreted
EC: 3.4.24.-
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Q2T0V9 | MSRVKWRNEKIIVALGSLWILGFAAWAFLLFDLLGTSVKEGILEGPREGVFWTAAQYRNSFSRFERQLILYATRQDRDFDNVLLQLDSLEASFGFLERPSEVSAYWLSIPKARDDIAELSRFMATLRRDVPALGARAGDSRRVLEDVARHWPKVNALANYFRAIEMEQRDFTFHQLKEKRRAIVMLGGVLGVILGALFLLLFYTIRTRGSLLEQQQAALDAQRKASDRAFEMIAAKNAFLGMVSHELRTPLQAICGSIEVLLARPQSDANMKTIKRLQNSAASLEAQVKDLTDYIKLRSTNRSVQSDPVEIAPLLADVLDPLRGRIRDKHLNASLRVEPPDLVVKSDRKLIQQIASNLVENSIKYTNSGTIAISAELAGTPSNRTMQIAVRDTGVGIAKNLLSKIFEPFFRVNDPGVRHVDGIGMGLAVVQELVVALRGHVDVRSVVGEGSEFVVTLPVELPGSADAPDDDAPPSLQTTHRDLHALVVDDNENARETLGAMLTALGIRADLRGTGKEGLRCFGECQHDIVVLDLELPDISGFEVAEQIRWATSPDAAKKTTILGVSAYESAMLKGDHAVFDAFVPKPIHLDTLNGIVSRLRS | Function: Member of a two-component regulatory system involved in control of gene expression; inhibits synthesis of (at least) the polyketide antibiotic thailandamide. Its two-component partner may be BTH_I0635.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66575
Sequence Length: 602
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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P07893 | MPAAIVHSADPSSTSILVEVEGMKCAGCVAAVERRLQQTAGVEAVSVNLITRLAKVDYDAALIEDPTVLTTEITGLGFRAQLRQDDNPLTLPIAEIPPLQQQRLQLAIAAFLLIVSSWGHLGHWLDHPLPGTDQLWFHALLAIWALLGPGRSILQAGWQGLRCGAPNMNSLVLLGTGSAYLASLVALLWPQLGWVCFLDEPVMLLGFILLGRTLEEQARFRSQAALQNLLALQPETTQLLTAPSSIAPQDLLEAPAQIWPVAQLRAGDYVQVLPGVRIPVDGCIVAGQSTLDTAMLTGEPLPQPCQVGDRVCAGTLNLSHRLVIRAEQTGSQTRLAAIVRCVAEAQQRKAPVQRFADAIAGRFVYGVCAIAALTFGFWATLGSRWWPQVLQQPLPGLLIHAPHHGMEMAHPHSHSPLLLALTLAISVLVVACPCALGLATPTAILVATGLAAEQGILVRGGDVLEQLARIKHFVFDKTGTLTQGQFELIEIQPLADVDPDRLLQWAAALEADSRHPLATALQTAAQAANLAPIAASDRQQVPGLGVSGTCDGRSLRLGNPTWVQVATAKLPTGSAAATSIWLADDQQLLACFWLQDQPRPEAAEVVQALRSRGATVQILSGDRQTTAVALAQQLGLESETVVAEVLPEDKAAAIAALQSQGDAVAMIGDGINDAPALATAAVGISLAAGSDIAQDSAGLLLSRDRLDSVLVAWNLSQMGLRTIRQNLTWALGYNVVMLPLAAGAFLPAYGLALTPAIAGACMAVSSLAVVSNSLLLRYWFRRSLNHSVSV | Function: Involved in copper transport.
Catalytic Activity: ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83657
Sequence Length: 790
Subcellular Location: Cell membrane
EC: 7.2.2.9
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P01513 | MFGKIVFLLLVALCAGVQSRYLIVSEPVYYIEHYEEPELLASSRVRRDAHGALTLNSDGTSGAVVKVPFAGNDKNIVSAIGSVDLTDRQKLGAATAGVALDNINGHGLSLTDTHIPGFGDKMTAAGKVNVFHNDNHDITAKAFATRNMPDIANVPNFNTVGGGIDYMFKDKIGASASAAHTDFINRNDYSLDGKLNLFKTPDTSIDFNAGFKKFDTPFMKSSWEPNFGFSLSKYF | Function: Hemolymph antibacterial protein.
PTM: Attacin F appears to be derived by proteolytic digestion of attacin E.
Sequence Mass (Da): 25438
Sequence Length: 235
Subcellular Location: Secreted
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Q93703 | MQTLMSHSRITPLPGAITKEEIKNQLLVHERRFLSKPNRKDQWNVLPQSAHSKNTVNPVRKIADACAVPPHPEKKVIKLHLGDPSVGGKLPPSEIAVQAMHESVSSHMFDGYGPAVGALAAREAIVERYSSADNVFTADDVVLASGCSHALQMAIEAVANAGENILVPHPGFPLYSTLCRPHNIVDKPYKIDMTGEDVRIDLSYMATIIDDNTKAIIVNNPGNPTGGVFTKEHLEEILAFAHQYKLIIIADEIYGDLVYNGATFYPLASLSPKVPIITCDGIAKRWMVPGWRLGWLIIHNHFGVLTDVKNGIVALSQKIVGPCSLVQGALPKILRETPEDYFVYTRNVIETNANIVDSILADVPGMRVVKPKGAMYMMVNISRTAYGSDVSFCQNLIREESVFCLPGQAFSAPGYFRVVLTCGSEDMEEAALRIREFCYRNFNQHSDSEDSSDEGLDLSAMESD | Function: Transaminase involved in tyrosine breakdown . Converts tyrosine to p-hydroxyphenylpyruvate . Has no transaminase activity towards phenylalanine . Plays protective role against oxidative stress, metabolizing meta-tyrosine and negatively regulating its accumulation . Plays a role in modulating the daf-2/insulin receptor-like transduction pathway through regulating tyrosine levels . Negatively regulates dauer formation . Plays a role in longevity .
Catalytic Activity: 2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-glutamate
Sequence Mass (Da): 51031
Sequence Length: 464
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 2/6.
EC: 2.6.1.5
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Q54HG7 | MIKHLIKNVSNSVKYNNVTSNNILFSTSSSLKFGRKFTTETQQECILERLEGENKGISVISFNRGHVKNALGKNLMNQFRSHLNELRFCPDTRVVIVRSLVDGVFCSGADLKERALMSQVEASQFVHSLRSSFTELETLQMPTIAAIEGVAVGGGTEMVLACDFRVASKSSKMGLPETGLAIIPGAGGTQRLPRLIGIPRAKELIFTGAILDSKRALEIGLVQYETEKGEAFDKAIEIAKQIIPKGPIAIRMAKQAIDRGMNVDQASGMIIEQASYAQVIPTKDRIEGLTAFKEKRKPIYKGE | Function: Catalyzes the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA.
Catalytic Activity: (3S)-hydroxy-3-methylglutaryl-CoA = 3-methyl-(2E)-glutaconyl-CoA + H2O
Sequence Mass (Da): 33245
Sequence Length: 303
Pathway: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 3/3.
Subcellular Location: Mitochondrion
EC: 4.2.1.18
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Q13825 | MAAAVAAAPGALGSLHAGGARLVAACSAWLCPGLRLPGSLAGRRAGPAIWAQGWVPAAGGPAPKRGYSSEMKTEDELRVRHLEEENRGIVVLGINRAYGKNSLSKNLIKMLSKAVDALKSDKKVRTIIIRSEVPGIFCAGADLKERAKMSSSEVGPFVSKIRAVINDIANLPVPTIAAIDGLALGGGLELALACDIRVAASSAKMGLVETKLAIIPGGGGTQRLPRAIGMSLAKELIFSARVLDGKEAKAVGLISHVLEQNQEGDAAYRKALDLAREFLPQGPVAMRVAKLAINQGMEVDLVTGLAIEEACYAQTIPTKDRLEGLLAFKEKRPPRYKGE | Function: Catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3-methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) . Can catalyze the reverse reaction but at a much lower rate in vitro . HMG-CoA is then quickly degraded by another enzyme (such as HMG-CoA lyase) to give acetyl-CoA and acetoacetate . Uses other substrates such as (2E)-glutaconyl-CoA efficiently in vitro, and to a lesser extent 3-methylcrotonyl-CoA (3-methyl-(2E)-butenoyl-CoA), crotonyl-CoA ((2E)-butenoyl-CoA) and 3-hydroxybutanoyl-CoA (the missing carboxylate reduces affinity to the active site) . Originally it was identified as an RNA-binding protein as it binds to AU-rich elements (AREs) in vitro . AREs direct rapid RNA degradation and mRNA deadenylation . Might have itaconyl-CoA hydratase activity, converting itaconyl-CoA into citramalyl-CoA in the C5-dicarboxylate catabolism pathway . The C5-dicarboxylate catabolism pathway is required to detoxify itaconate, an antimicrobial metabolite and immunomodulator produced by macrophages during certain infections, that can act as a vitamin B12-poisoning metabolite .
Catalytic Activity: (3S)-hydroxy-3-methylglutaryl-CoA = 3-methyl-(2E)-glutaconyl-CoA + H2O
Sequence Mass (Da): 35609
Sequence Length: 339
Pathway: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 3/3.
Subcellular Location: Mitochondrion
EC: 4.2.1.18
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G3XSI3 | TADNMLNALFYFLLRNPQCLKRLEEEVSCVGATVNELSDDRLAKLPYLNACINETFRIAPAFNGGILQRVSCGATVDGVYVPPGVAVSVDHYTLGHDPQYWVKPDVFNPERWIDPDCKDNFKASRPFLIGARQCPGRQMAYQMFRVCVAKLVYLYTFEL | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aurasperone B, a dimeric gamma-naphthopyrone . The first step in the biosynthesis of aurasperone B is the production of gamma-naphthopyrone precursor YWA1 by the non-reducing polyketide synthase albA, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units . YWA1 is then methylated by aunE at position C-6 to yield foncesin which is further methylated at position C-8 by aunD to produce fonsecin B (Probable). A key enzyme in the biosynthetic pathway is the cytochrome P450 monooxygenase aunB which catalyzes the oxidative dimerization of fonsecin B to aurasperone B . AunB also catalyzes the oxidative dimerization of rubrofusarin B into aurasperone A .
Catalytic Activity: 2 fonsecin B + H(+) + NADPH + O2 = aurasperone B + 2 H2O + NADP(+)
Sequence Mass (Da): 18003
Sequence Length: 159
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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A2QBE9 | MSDTARISGGSFTSPPGRDVELNSFKEASQTRLYPYSSRKEEEGREDEQQRPEREEDTGALTGYKLVLVTVGLCFCIFCTSLDNTIVATAVPRITQQFHSLDDVGWYASAYLLTTCAVTLPFGRLYTFFPIKWVYLSALFVFELGSFICGITPSSLGLILGRAVAGLGGGGLFSGSLLIITQCVPLRRRPAFSGFIMSIFAVASVIAPLMGGAFTDHISWRWCFYINLPFGLVSAVVIFFTFQTTKPVVQASLREKAAGLDPLGTATFLPAIVCLLLATQWGGAQYPWGDGRIIALFTLFGVLLACFVGLQLWARERATLPPRLLRGRNIWGSALYGFCLNGAMFTFVYYLPIWFQAVQGTSATESGIRNLPLVISNVIFAIISGVLVSATGYFGPFMLLSAAMASIAAGLLSMLHPSSGAGEWIGYQVLLGSSIGMGFQLPVFVVQTTLASTDIPTATALMTFIQLLGGAIFVSVAQNVFRNQLAADIRAALPMLDPKAVINAGPTSLRAMYSGETLTTLVAMYNDAVVHTFYLAIGLAAASFLAATVIQWRPSPKSISHPDSS | Function: Efflux pump; part of the gene cluster that mediates the biosynthesis of aurasperone B, a dimeric gamma-naphthopyrone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60824
Sequence Length: 565
Subcellular Location: Cell membrane
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Q54WX4 | MSYPNNKENSNNIGGGSFSVPSKQPQRVLQQQNTNINNHQTTSTVKSTITKPTTTGATTSTNTSTIPPTTTASSSSSSSSSSSSSSSSSSSSSSSSSQSVPKKKWCIDDFDIGKLLGMGRFGHVYLAREKKSQFIVALKVLFKNQLQTHNIEHQLRREIEIQSHLRHPNILRLFGYFYDDKRVFLIIEFAKGGECFKELQKVGSFNEQTAATYTLQIADALRYCHSKHVIHRDIKPENLLIGVGGEIKIADFGWSVHAPNTKRSTFCGTLEYLPPEVIEKKGYDQTADVWSLGILIFEFLVGRSPFTSDEEKNIFHNIQENDVYYPSSISPEAKDLISRLLVSDPHQRITLKDVINHPWIKKHAHPKSLEPTKLGLPLPSQMTY | Function: Part of a chromosomal passenger complex.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42918
Sequence Length: 384
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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E2RTQ7 | MPQHLVPHTGTGKRTTIEDFEIGRFLGRGKYGLVYLAREQSSKLVVALKVLYKSYIKSERVEGQVRRELDIHLNVRHINIIRLYTWFQDETRVFLVLEVAPYGELYQRLQQFGKFPLPVVSKIIRDVAQAIQYLHRKNIFHRDLKAENILICKGKETKEHTDAHNSDDSISVHEHELVRMAHYTYKIADFGWSVHHPTHGGRRRTQCGTLDYLPPEVMLGQSYDKACDIWSLGALCYELICGTAPFYHDEIKITRQNIANVEYSFTKDFSPASKDFIQRMLIRSPEARISIEDILRHPFLRQTDHRSKVPK | Function: Involved in regulation of the cell cycle. Required for mitotic cell division and cytokinesis. Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar dense rods, may coordinate reorganization and segregation of tubulin-containing structures during mitosis and cytokinesis. May regulate microtubule disassembly by phosphorylating cytoskeletal proteins leading to their destabilization.
PTM: Phosphorylated in mitosis and cytokinesis . Activated by phosphorylation at Thr-205 (Probable).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 36286
Sequence Length: 311
Subcellular Location: Nucleus
EC: 2.7.11.1
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D7UQM5 | MTPTGPSHHSMAPKRVLPAASQSNMYGNIRSASTTSTTASTSSQALRLLQNAKTSKNADNRIAHAERQGPPSAHPAAMQKPAARVAPSNENRPDPAARQHQHQQQLQQQKATGHDRVLKESQAGNSTTTTMTSTQSKEANKWSLANFDIGRPLGKGKFGNVYLAREKKSKFIVALKVLFKSQLQKAKVEHQLRREIEIQSHLRHDHILRLYGYFYDDTRVYLILEYAARGELYKEMQAQKAGHFDEDRSAVYIYQLAKALLYCHEKKVIHRDIKPENLLLDLKGDLKIADFGWSVHAPSSRRATLCGTLDYLPPEMIEGKTHDEKVDLWSLGVLCYEFLVGKPPFESQGNTETYRKITKVEFTFPKHVSEGARDLICKLLKHNPSHRLSLEGVIAHAWIQEKISQRS | Function: Serine/threonine protein kinase that contributes to the regulation of cell cycle progression. Involved in meiotic apparatus formation and polar body extrusion. Contributes to Plk1 activation and phosphorylation of histone H3 at 'Ser-10' during meiosis I. Required for accurate progression of early embryonic M phase. Involved in chromosome alignment and cleavage furrow formation during early embryonic cycles. May be involved in mitotic spindle formation and cytokinesis.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 45947
Sequence Length: 407
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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I1RF64 | MLFRFLALLPFVAGAFAEYKVHDDTFKPDYVLEATLDDIKINCVSRSSIVFNGTSPGPTIYLQEEQTTWIRVYNKIPDNNVTVHWHGLSQRAAPFSDGTPLVSQWPIPAGQFFDYEIRPEIGDAGSYFYHSHVGFQIVTAFGALIVRDARKPEYKYDGDIPLLVGDNYAAEDEVIEQGLLADPFKWSGEPQAITIQGNSGNKSFYEAPDSSCMPHVVHVDPGKTYRLRFISATALSMIKLGIEDHENLTVIEADGSYTKPAKIDHVQVSPGQRYSYLMKTKTSKEVCGGDKSQYWIRYESRDRPKVISGYALLKYRCDKNQKLPKSLPETSPIELSNSTADYLEYALEGLSEKNNQAFPKLSEVTRTVVIQINQILTTGAYVNGTLNGTVAWAQNGLPWKENVQAERRQVPYLIQIYENGTTPNYTLALEHHGFDPETKAFPAKVGEVLDIVWENNNGPTGGWDYHPMHVHGYHVYDLGSGNGTYNATENEAHFENFTPVLRDTTNLYRYAVKGVPHHTAGWRAWRIRITEENIGAWMMHCHIAQHQVMGMATVWVFGDAEQIRGKFPAPPYTQGYLTYGGSAYGTEDDQPWVNEYYSDKNN | Function: Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin . The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 . The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction . The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin . Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ . Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin .
Sequence Mass (Da): 67889
Sequence Length: 602
Pathway: Pigment biosynthesis.
EC: 1.-.-.-
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I1RF55 | MINSFSLFAHITPIIRSSLHSRYSVISSRKAMSSLAAAPYRHVMMPFSPAQDAQVHGNSALTKLTDAIPDLKIYTRSSPHYESLRGVYNKLITAQPLAICRPTSVAQVQAIVKTVSGLGIPLGVRGGGHDVFGRGCIADSVTIDMRELDTQELSQDKKTVKVGGGITSKNLVGFLGSHNLCTSNGFAGEAGWTSWASWGGYGPLGDYVGLGVDNIVGAKIVTASGDVVDAKGDSELLWALRGGGGNFGVIAETDVRVYPMSTIQAGFIVYPWPETADVLLRLQALLDSGVPDKLCLQAGFTKGEWGLGMAITYIWPEAETIGPESEEWLQKLKGLGTCIVDTVAETTFEAFQASISSAISNPVNVTSRHISISKFTSDTLNQLIGACESMPAEADCSITCTILHGKAAQANVLSAFGTRRPHIMLHINAVTEEAAHEHVAIAWADRLVDGVEATGDSIGSTYVSFMESDKDPKGCYGENWERLKAVKKEVDPNDVFRFVHGRIPAA | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin . The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 . The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction . The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin . Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ . Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin .
Sequence Mass (Da): 54117
Sequence Length: 506
Pathway: Pigment biosynthesis.
Subcellular Location: Secreted
EC: 1.-.-.-
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I1RF63 | MSKQKPSLWRALRALSFIISIPLLIQYLVLKWYSTSQNTPTPVFHEPNHETNLTVWEVLSNDDRVSKFVDVIGKLPDIVRGLSAPQARFTVYAPVNEAFDSFYFPPDPPPFFGLFIAGCHMGPGPVPAERLPSMGTVSSFVNGDIFFTYKQRISVQKDKSGLTLNRAARVLPVNASQSIAVNGFVHHIDTVLELPNSTAHALRTRPELSKLRRGLEATKLSESIYDTNAHVSQTIFAPTNAAFDRLGKTATKFLFSHGGRPYLRALLKYHVVANKTLFSDSYWPHGGAKLMDLSLIPNKDSHQFDLPTLHNNLTLQVESRKIHKKWHLNVLKDQVAEGKSHDSIPVSMPDVILMDGVMHFIDSILLPPAKSEQRKTSWLSRLKSSLGHNKQSIEDLVTLLGPYIDEP | Function: Part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin . The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 . The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction . The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin . Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ . Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin .
Sequence Mass (Da): 45574
Sequence Length: 407
Pathway: Pigment biosynthesis.
Subcellular Location: Secreted
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I1RF56 | MTDNTDMEKLDRATTPTPIPNEAPPTSEPSESKPEEAEDESKYPHGLKLAAIILSNMVAMFLVALDRTIIATAIPRITDDFNALGDISWYASAYLITSSATQLLWGRIFTFYPTKTVYLVAIFFFELGSLLCGVAPNSVAFIIGRAIAGAGSAGIYSGSTILITTVTPLSKRAGYVGMMGAVFGIASVIAPLIGGAFTDHVTWRWCFYINLPVGGAAVACLILLFPKFPVNEPVSVKQQIKQLDPWGNLVFLPGVICLILALQWGGEKYAWDSGRIVALLVLACVLLLVFIGIQIWQQENATVPPRLFKIRNVWLGTIFAFCLGSVLIVFLIALPIWFQGIRGTDAITSGIDTLPLVLSLVFGAIVSGGVINGVGWFNPVFFSSVIFMSVGGGLITTFVVDTPTRTWIGYQIILGLGIGQGMQLASLGTQVAVKQSDVPTGVSLMFFAQSLGGSVLVCVAQAVFNNELRSRLTSFDGIDVARIIGTGATQLRHVIPADRLAEVLVEYNAALRSYFYVGLAAACFAVLPSLGIEWKNVKGQEFVH | Function: Rubrofusarin-specific efflux pump; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin . The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 . The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction . The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin . Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ . Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58460
Sequence Length: 544
Pathway: Pigment biosynthesis.
Subcellular Location: Cell membrane
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I1RF59 | MSPHSDTQETSHEATVTGQPDTLVCLTITAYKKPSLSEKEYRHHMTKVHAKLVSPLMEEYGIVRYTMTHNTKETRPMLYQLYDPQFSNQSDYDCIVQFIFKDIKDFLRMKADPRFLEKVAPDHVNFADTKRSTMTVGYYEEFVNDGKVVPKD | Function: Dehydratase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin . The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 . The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction . The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin . Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ . Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin .
Catalytic Activity: naphtopyrone YWA1 = H(+) + H2O + norrubrofusarin
Sequence Mass (Da): 17705
Sequence Length: 152
Pathway: Pigment biosynthesis.
EC: 1.-.-.-
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Q5ATK1 | MAKLYYMPYIFNEGMPLASGPPTLPEDFTPEKSGFRVLVEVRRMKGHFPAQKWRKRNQEWQCINNETLLPDHVRNGHLAKNVPYRPYRPVYVPFAMTVSPTTDAMGTSEETRSKQTKGSNDDILSAKIAGRVARPVYHCTSARLHDLAYDPWPITTIDTHGLSSLKAPSTHTRILIIGAGFGGLLFAVRLLQAGFSRDDLLLVDSAGGFGGTWYWNRYPGLMCDIESYIYMPLLEETGHMPSRKYVPGEELRTHAEGIAAKWELEQRALFRTTIRTLEWDEGGNQWIAHAEQLGVFTDAKQGGNGGGGPLTFTATFAIIASGTLSKPKVPNLHGVDDFQGHIFHTARWDYDYTGGSPANPAMHRLQGKRVGVIGTGSTAVQVIPQLARWSKELIVFQRTPAAVGLQKNQVTDPVWWKGNILKAGSGWQRKRSENFNAFISISNPPCMENLVNDGWTSSPSFSAAIGGALNMQPDFLDLVKAIDRPRLEAAQDHIRSTVRDDTTAEALINLNHGWCKRPCFHQGYFETYNLPHVRLIKTDAAGVTGLSPKGILVGDTLYEVDLVVLATGYDLGSLCPADRAQIQVLGSEGVAMKEKWAGGPTTLHGVMTRGFPNLFFPGTSQAGVTANQSYMFDRAAEHVAYIIQNSTLEAGGYIDKIRIEPTAEGEKHWTTQSVARISAFAATTACGTGDYTISNRYRSSDVDTMARHMPWGEGMASYVKILEAWRESGTMEGLDIRYHSSEGSR | Cofactor: Binds 1 FAD per subunit.
Function: FAD-binding monooxygenase; 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 the polyprenyl transferase ausN . Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A . Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE . Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 . The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide . Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol . Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation . Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional .
Catalytic Activity: AH2 + O2 + protoaustinoid A = A + berkeleyone A + H2O
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 82277
Sequence Length: 745
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.14.13.-
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C8VE79 | MYASNKTYPSSRALPCLVEKVEAQHVDGAIRVRITTLEQKDWRQAKAAAVEAKYEAEREIQLRAHGNVKDIEITRESAFEHFATDPWAQHVGVDIEAQRERLLAEPGSRKILIIGAGFGGLLFAVRLIQTGRFTAEDITMIDSAAGFGGTWYWNRYPGLMCDTESYIYMPLLEETGYMPRNKYASGNEIREHAERIAQTYGLATRAMFRTVVEKLDWNEAEKVWTVAGSMLGIANNGQRDNMMSFQMVSQFTIMASGSFASPRVPDYPNIFDYKGKLFHTARWDYNYTGGSVENPKMLGLADKTVAIIGTGASAVQIVPQLAKYSNKLIVFQRTPAAVDARNNCPTDPVWWETETQAEGTGWQKRRQENFNAFTCNEKPLPSVNKVDDGWTRMPSFSILIGGPQGLDPDYVDRMRAVDMNRQEKIRARAHNIVQSEGSADLLTPWYPGWCKRPCFHDDYLSAFNLPNVELVDIRHNGISHFTANGLVANDIEYELDVIILSTGYTVPVTRASPSSRANIAVSGRNGTTMEAKWANGLATLHGVMTRDLPNLFFAGTSQAGACVNLVYALDQNATHVAYILANAFDRRPSDSARVIIEPTPGSEEAWAMQVLQRAAGFRGIAGCTPGYLNGYGMDASSLSPEQQINAARLAAWGEGIASYVRYLEAWRAKGDLNGIELTFFAKF | Cofactor: Binds 1 FAD per subunit.
Function: FAD-binding monooxygenase; 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 the polyprenyl transferase ausN . Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A . Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE . Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 . The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide . Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol . Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation . Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional .
Catalytic Activity: AH2 + O2 + preaustinoid A = A + H2O + preaustinoid A1
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75879
Sequence Length: 683
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.14.13.-
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P0C1T7 | MSALKFVLICGLVLLLIETIPGVSLNLMRATNRHQCDTNDDCEEDECCVLVGGNVNNPGVQTRICLACSRK | Function: Elicits an uncoordinated twisting syndrome when injected into C.elegans, but has no effect on mice.
Sequence Mass (Da): 7722
Sequence Length: 71
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q92194 | MLLSTHLLFVITTLVTSLLHPIDGHAVKRSGSLQQVTDFGDNPTNVGMYIYVPNNLASNPGIVVAIHYCTGTGPGYYGDSPYATLSEQYGFIVIYPSSPYSGGCWDVSSQATLTHNGGGNSNSIANMVTWTISKYGADSSKVFVTGSSSGAMMTNVMAATYPELFAAATVYSGVSAGCFYSNTNQVDGWNSTCAQGDVITTPEHWASIAEAMYSGYSGSRPRMQIYHGSIDTTLYPQNYYETCKQWAGVFGYDYSAPEKTEANTPQTNYETTIWGDSLQGIFATGVGHTVPIHGDKDMEWFGFA | Function: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.
Catalytic Activity: Deacetylation of xylans and xylo-oligosaccharides.
Sequence Mass (Da): 32729
Sequence Length: 304
Pathway: Glycan degradation; xylan degradation.
Subcellular Location: Secreted
EC: 3.1.1.72
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Q75P26 | MILLSYLLTYLLCALTCSARAIHNGRSLIPRAGSLEQVTDFGDNPSNVKMYIYVPTNLASNPGIIVAIHYCTGTAQAYYQGSPYAQLAETHGFIVIYPESPYEGTCWDVSSQATLTHNGGGNSNSIANMVTWTTKQYNADSSKVFVTGTSSGAMMTNVMAATYPNLFAAGVAYAGVPAGCFLSTADQPDAWNSTCAQGQSITTPEHWASIAEAMYPDYSGSRPKMQIYHGNVDTTLYPQNYEETCKQWAGVFGYNYDAPESTESNTPEANWSRTTWGPNLQGILAGGVGHNIQIHGDEDMKWFGFTN | Function: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone. Displays the greatest hydrolytic activity toward alpha-naphthylacetate (C2), lower activity toward alpha-naphthylpropionate (C3) and no detectable activity toward acyl-chain substrates containing four or more carbon atoms.
Catalytic Activity: Deacetylation of xylans and xylo-oligosaccharides.
Sequence Mass (Da): 33286
Sequence Length: 307
Pathway: Glycan degradation; xylan degradation.
Subcellular Location: Secreted
EC: 3.1.1.72
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A8PB24 | MVFSPRLSAFVALVALTNAATAVPMYGQCGGSGYTGPTQCDPGLVCVKLNDWYSQCQSGGAQPPVTTTSSPPVTVSPPPSTTTVAPPVATGPPAPEIPAGQLTQLRSFGNNPSNISMFVYKPQNVKNRPGLLVALHPCGGTAQQYFSGFPGFRQHADQRGFIVLYGQSPPGSSNCWDIISTASLTREGGDDSTGIASAVKYALQNWNVDPEKVFVTGTSSGAMMTNIMAATYPDLFKAGAVWAGTAVGCLSANTPQFPPDPCQSGTVIRTPQEWGDRVRRAYPGYNGPWPRMQIWHGTNDFALDHKNLAEQMKQWTNVHNISQTPTSTSPSTPRQGWTKQVYGNGLVETFSGQGAGHGLPESGTEVVAMDFFGL | Function: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.
PTM: Glycosylated.
Catalytic Activity: Deacetylation of xylans and xylo-oligosaccharides.
Sequence Mass (Da): 39665
Sequence Length: 374
Domain: Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in serines, threonines, and prolines, and a C-terminal carbohydrate esterase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Pathway: Glycan degradation; xylan degradation.
Subcellular Location: Secreted
EC: 3.1.1.72
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Q81UB2 | MNKTLIINAHPKVDDTSSVSIKVFKHFLESYKELISNNETIEQINLYDDVVPMIDKTVLSAWEKQGNGQELTREEQKVTERMSEILQQFKSANTYVIVLPLHNFNIPSKLKDYMDNIMIARETFKYTETGSVGLLKDGRRMLVIQASGGIYTNDDWYTDVEYSHKYLKAMFNFLGIEDYQIVRAQGTAVLDPTEVLQNAYKEVEEAASRLANKYIFSLEE | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 25369
Sequence Length: 220
EC: 1.6.5.-
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O35022 | MSTVLFVKSSDRTAEEGVSTKLYEAFLAAYKENNPNDEVVELDLHKENLPYLGRDMINGTFKAGQGMEMTEDEKKQAAIADKYLNQFVKADKVVFAFPLWNFTVPAVLHTYVDYLSRAGVTFKYTQEGPVGLMGGKKVALLNARGGVYSEGPMAALEMSLNFMKTVLGFWGVQDLHTVVIEGHNAAPDQAQEIVEKGLQEAKDLAAKF | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones (Probable). Contributes to resistance to 2-methylhydroquinone (2-MHQ) and catechol .
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 22977
Sequence Length: 208
EC: 1.6.5.-
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Q89PW2 | MAKLLHLSCSPRPDSESSAGARVFLDGFRQMRPDWDIDVMDLWRERMPEFAGPIVEAKYARMKAEAFDDAQRDSFAEAERMATRLSLAERVLISTPMWNFGIPYKLKQWFDIIVQPGLTFRYDPASGYLPLLKDRPTLVILASGSDFVTGMNRGRTDMATPYLREALRFIGISDVRFVPIGPTTGPADPILAARETAYRRLREIATWF | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 23682
Sequence Length: 208
EC: 1.6.5.-
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Q97LF7 | MKKLLYISVNTKPEGMSASKTVGREFVDRFVQNYPEYQLIEHDICNEYIPELDHRFLNDNGDIVSGNDYNLLSDNDKKIVDRINDLCNEFVSADVYVIAYPMWSSLFPPRLKMYIDCIVQNGKTIKISEDESSGLLSDKERSVLCIQSSGGVYPKIISWKINHGINYLHDIFRHLGIKKFEKLLVEGVDVQDIGKEKAVEKAFDEIDELIDKMQVRDFVKQ | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 25504
Sequence Length: 221
EC: 1.6.5.-
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Q0KBB2 | MNILQIDSSVLGDNSVSRSLTASVVADLVAATPDAKVTVRDLDQDAPAHLSGNLLPVLGGPKEGLSAIQEAELQRTEQWLAEFLAADVLVVGVPQYNFSIPSQLKAWIDRIAQAGRTFKYTENGPVGLAGGKRVIVVSSRGGVRQDANELDLHEKTVDIVFRFLGITDITYVRAHGLAMGPQFREAGLASARTEIAALNDASRLAA | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 21945
Sequence Length: 206
EC: 1.6.5.-
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Q6ALS1 | MSKLLYIEASPRKNKSFSTRVAQSFINTFLDADPANRIETLDLWDFPLPEVDGSYLSAKYKILHWQDPTEAEARAWTEIANIVSQFKDADSYLFSIPMWNFSIPYKLKHFIDIITQPGLTFMFSPESGYQGLVTGKACTVIYARGAQYRGTKGSTLDFQKTYMELLLSFIGFENIHSIRVEPTLTDSASRERVLATAKLEAISLAKELYSLI | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 24075
Sequence Length: 212
EC: 1.6.5.-
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Q728Q5 | MATILYIKASPRGERSHSVTVADAFVKAYSEANPGDVVRVLDVFEADLPAFGTDAVVARYLSGQGDPLSPAQEAAWAAVKRQVEDFKTADKYVIALPMWNFSIPWRLKQFFDIIIQPGLTFSYDEQGYHGLVTGRPVLVSYARGGAYPAGTPAEGWDFQKRYLEHILGFIGFTDIRSVVVEPTLAGGPDTAQAKRAEAVEQARRMALEF | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 22989
Sequence Length: 209
EC: 1.6.5.-
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Q8X9S9 | MSKVLVLKSSILAGYSQSNQLSDYFVEQWREKHSADEITVRDLAANPIPVLDGELVGALRPSDAPLTTRQQEALALSDELIAELKAHDVIVIAAPMYNFNISTQLKNYFDLVARAGVTFRYTENGPEGLVTGKKAIVITSRGGIHKDGPTDLVTPYLSTFLGFIGITDVKFVFAEGIAYGPEMAAKAQSDAKAAIDSIVAA | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 21646
Sequence Length: 201
EC: 1.6.5.-
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Q8FHN0 | MSKVLVLKSSILAGYSQSNQLSDYFVEQWREKHSADEITVRDLATNPIPVLDGELVGALRPSDAPLTPRQQEALALSDELIAELKAHDVIVIAAPMYNFNISTQLKNYFDLVARAGVTFRYTEKGPEGLVTGKKAIVITSRGGIHKDGPTDLVTPYLSTFLGFIGITDVKFVFAEGIAYGPEMAAKAQSDAKAAIDSIVAE | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 21744
Sequence Length: 201
EC: 1.6.5.-
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Q831B2 | MSKLLVVKAHPLTKEESRSVRALETFLASYRETNPSDEIEILDVYAPETNMPEIDEELLSAWGALRAGAAFETLSENQQQKVARFNELTDQFLSADKVVIANPMWNLNVPTRLKAWVDTINVAGKTFQYTAEGPKPLTSGKKALHIQSNGGFYEGKDFASQYIKAILNFIGVDQVDGLFIEGIDHFPDRAEELLNTAMTKATEYGKTF | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 23221
Sequence Length: 208
EC: 1.6.5.-
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Q2N970 | MSTILHITASIRGDESISRALSSKLVERLSGTDTKVITRDLSQNDIPYVDADRFAANLSPYTERSPEQQELAAIADTLIEELQAADTIVLGVPIYNFSVPATVKAWADTVARAGTTFEYTPTGPKGKLDGKKAYITVASGGTPVGSEVDFMSPWLKFFLGFLGISEVEVVATADGIMGEGGEEKIASAHKQVEQVAA | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 20997
Sequence Length: 197
EC: 1.6.5.-
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C4L0W8 | MTKVLYVSANPKPTELSYSKQVAETFVSTLKAENASIEVEAIELYDVDVQEIDGDVLSAWGKFASGEALTDVEAKKVGTMSGMLEKFMEADLYVFATPMWNFFFPARMKMFLDSVLMAGKTFRYTEQGPVGLLENKQAIHIQGTGGIYTGTDLNFADAYLRQALAFVGVSEVTTVAVEGMNQYPDKIEEIVADAKAKAEALAKEVAGAVTV | Cofactor: Binds 1 FMN per subunit.
Function: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Mass (Da): 22966
Sequence Length: 211
EC: 1.6.5.-
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Q9M9U5 | MPATDFQGSFGRSLLSLRRDQVDSSTVVSGSSSHHEPSTMEVELDSFQRQVAEKFIDLNASSNDLLSLEWIGKLLDSFLCCQEEFRAIVFNHRSQISKSPMDRLISDYFERSIKALDVCNAIRDGIEQIRQWEKLADIVISALDSHRPIGEGQLRRAKKALIDLAIGMLDEKDHPSGTNLAHRNRSFGRVKDSHHRSIGHFRSLSWSVSRSWSASKQLQALASNLATPRPNDVVASNGLAVPVYTMTSVLLFVMWVLVAAIPCQDRGLQVNFFVPRHFQWAAPVMSLHDKIVEESKRRDRKNCCGLLKEIDRIEKSSRLMNELIDSIHFPLNDDKEVEVKQRVDELVQVREALRNGLDPFERKVREVFHRIVRSRTESLDSL | Function: Together with TRANSTHYRETIN-LIKE protein (TTL), prevents plant growth and development, but by opposition to TTL, regulates positively cold tolerance, probably in a brassinosteroid (BR) and allantoin-dependent manner . Controls lateral root initiation by modulating exocytic vesicular trafficking-mediated PIN-FORMED (PIN, e.g. PIN1 and PIN3) auxin efflux carrier proteins recycling, thus influencing polar auxin efflux transport in lateral root primordia . Contributes to freezing acclimation via the C-repeat binding factor (CBF) pathway, probably by stabilizing CBF and promoting the expression of CBF pathway genes; this regulation involves the suppression of ubiquitin-mediated degradation of CBF3 triggered by GRF6/14-3-3lambda and GRF8/14-3-3kappa .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 43541
Sequence Length: 382
Subcellular Location: Cell membrane
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C0JB40 | WIMGHMVNDISLVDEYLNQGANSLELDVSFNSEGIAEKLYHGYPCDCLRSCTKTVAFSTYLDYIRNITTPGDPKFRNELVLLMLDLKLKQIAPEAAYWAGFDTAEKLLDYYWQNGQSGARAYIILSIEILTHYEFVTGFKHQLQNKGHEEYSAKIGWDFSGNENLEEIHKVMSDLDLKEHIWQGDGITNCLPRGDDRLKEALFRRNTDWYKYIDKVYTWSIDKKSSIRNALRLGVDGVMTNYPERVVEVLQEPEFSSKLRLATYEDDPWARTVL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity).
Catalytic Activity: an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline
Sequence Mass (Da): 31760
Sequence Length: 274
Subcellular Location: Secreted
EC: 4.6.1.-
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Q1W694 | MQLFIILCLAGSAVQLEGTELDGVERADNRRPIWNIAHMVNDKGLIDEYLDDGANSVESDVSFDSNGKPEKMLHGSPCDCGRSCKRQMSFADYLDYMRQLTTPGDPKFRENLILVMLDLKLKKLSSEQAYSAGQEVASQMLDKYWKRGESGARAYIVLSIPTITRVTFVNGFYDKLHSEGFDQYREKVGVDFSGNEDLEDTGKILKSRDILDHIWQSDGITNCLFRIMKRLKAAIRKRDSNGYMVKVYTWSVDKYTTMRKALRAGADGMITNFPKRLVSVLNEREFSGKFRLATYNDNPWERYTG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with low activity . It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Has no or weak activities in inducing dermonecrosis, hemolysis, inflammatory response, platelet aggregation and increase in vessel permeability . In vivo, shows no lethality when injected at higher dose into mice .
Catalytic Activity: an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline
Sequence Mass (Da): 34831
Sequence Length: 305
Subcellular Location: Secreted
EC: 4.6.1.-
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C0JB51 | FALAHMVNDLEMVDEFVGKGANGLEIDVTFSSAGQPEYTYHGVPCDCFRNCKRREDFDTYIKYIRHLATPGDPKFRSNLIMLIFDLKLNGLSQDALRSAGKEMADKLVGNYWQDLAEARAYIVLSMPSIEQADFVTAFKDELKDFGYDKNLDRIGYDFSGNEDLGETAKVYEKLNIHEHIWQADGITNCLPRGDSRLKEAISKRDTPGYQYINKVYTWTIDKSGSIANALRLGVDGVMTNYPERVIDALNDSEFSGKLRLATYEDNPWETFKG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity).
Catalytic Activity: an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline
Sequence Mass (Da): 30979
Sequence Length: 273
Subcellular Location: Secreted
EC: 4.6.1.-
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Q96Q91 | MEMKLPGQEGFEASSAPRNIPSGELDSNPDPGTGPSPDGPSDTESKELGVPKDPLLFIQLNELLGWPQALEWRETGSSSASLLLDMGEMPSITLSTHLHHRWVLFEEKLEVAAGRWSAPHVPTLALPSLQKLRSLLAEGLVLLDCPAQSLLELVEQVTRVESLSPELRGQLQALLLQRPQHYNQTTGTRPCWGSTHPRKASDNEEAPLREQCQNPLRQKLPPGAEAGTVLAGELGFLAQPLGAFVRLRNPVVLGSLTEVSLPSRFFCLLLGPCMLGKGYHEMGRAAAVLLSDPQFQWSVRRASNLHDLLAALDAFLEEVTVLPPGRWDPTARIPPPKCLPSQHKRLPSQQREIRGPAVPRLTSAEDRHRHGPHAHSPELQRTGRLFGGLIQDVRRKVPWYPSDFLDALHLQCFSAVLYIYLATVTNAITFGGLLGDATDGAQGVLESFLGTAVAGAAFCLMAGQPLTILSSTGPVLVFERLLFSFSRDYSLDYLPFRLWVGIWVATFCLVLVATEASVLVRYFTRFTEEGFCALISLIFIYDAVGKMLNLTHTYPIQKPGSSAYGCLCQYPGPGGNESQWIRTRPKDRDDIVSMDLGLINASLLPPPECTRQGGHPRGPGCHTVPDIAFFSLLLFLTSFFFAMALKCVKTSRFFPSVVRKGLSDFSSVLAILLGCGLDAFLGLATPKLMVPREFKPTLPGRGWLVSPFGANPWWWSVAAALPALLLSILIFMDQQITAVILNRMEYRLQKGAGFHLDLFCVAVLMLLTSALGLPWYVSATVISLAHMDSLRRESRACAPGERPNFLGIREQRLTGLVVFILTGASIFLAPVLKFIPMPVLYGIFLYMGVAALSSIQFTNRVKLLLMPAKHQPDLLLLRHVPLTRVHLFTAIQLACLGLLWIIKSTPAAIIFPLMLLGLVGVRKALERVFSPQELLWLDELMPEEERSIPEKGLEPEHSFSGSDSEDSELMYQPKAPEINISVN | Function: Electroneutral Cl(-)/HCO3(-) antiporter that favors chloride ion entry and efflux of hydrogencarbonate and sodium ion across the basolateral membrane and may participate in salivary secretion . Also mediates Cl(-)/HCO3(-) exchange activity in the presence of K(+) as well as Cs(+), Li(+), and Rb(+) (By similarity). Does not contribute to Cl(-)/HCO3(-) exchanger in the apical membrane of the upper villous epithelium (By similarity).
Catalytic Activity: chloride(in) + 2 hydrogencarbonate(out) + Na(+)(out) = chloride(out) + 2 hydrogencarbonate(in) + Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 108248
Sequence Length: 983
Subcellular Location: Basolateral cell membrane
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A0A494BA31 | MKLPGQGDFESSDAHENAHSEEPDSGLGPGPGLNGPSGIDIGESQVSKDPLLFIQLNELLGWPQALEWRETGRWLLFEEKLDMGAGRWSAPHVPTLELPSLQKLRSLLAEGIVLLDCQAQSLLELVEQVVSGESLSPELRGQLQALLLQRPQHHIQTMGIRPCRESNAFRKASRDEDAPLKHQNPLRQKLPAGAEAAAVLAGELGFLEQPLGAFVRLRNPIVLEPLTEMILPSRFFCLLLGPPTLGRSYHEMGRAAAVLLSDPQFQWSVRRASHLPDLLAALDAFLQEVTALPPGRWDRTARIPPPKYLPSQHKRFPSKLQEVTSLSRQSAALAEDKHHHGPHTPIPELQRTGRLFGGLIQDVRRKACWYTSDFLDALHPQCFSAVFYIYLATVTNAITFGGLLGDATEGAQGVLESFLGTAVAGAAFCLMAGQPLTILSSTGPVLVFERLLFSFSRDYSLDYLPFRLWVGIWVTAFCLALVATEASLLVRYFTRFTEEGFCALISLIFIYDAMGKMLNLIRAYPIQRPGSSAYGCFCQYPGTGGNTSEWTSAKLKDTEDILSVPGLVNASFLPPPECIRQGGHPLGPSCHTVPDIAFFSLLLFFTSFLCAIALKHIKNSRFFPSVVRKVLGDFSSVLAILLGCGLDTFLGLATPKLLVPTEFKPTLSGRGWLVSPFGANPWWLSVAAALPALLLSILIFMDQQITAVILNRAEYRLQKGAGFHLDLFCVAVLMLFTSALGLPWYVSATVISLAHIDSLRRESKACIPGEAPNFLGIREQRLTGLVVFVLTGVSIFLAPVLKFIPMPVLYGIFLYMGVAALSSIQFVKRVQLLLMPRKHQPDMLLLRHVPLSRVHLFTAIQLACLGLLWVVKSTPAAIVFPLMLLGLVAIRKALEWVFSPQELLWLDELMPEEEETIPENRSEPEHLFSGNDSEDSELMYQPKAPEINISVN | Function: Electroneutral Cl(-)/HCO3(-) antiporter that favors chloride ion entry and efflux of hydrogencarbonate and sodium ion across the basolateral membrane and may participate in salivary secretion . Also mediates Cl(-)/HCO3(-) exchange activity in the presence of K(+) as well as Cs(+), Li(+), and Rb(+) . Does not contribute to Cl(-)/HCO3(-) exchanger in the apical membrane of the upper villous epithelium .
Catalytic Activity: chloride(in) + 2 hydrogencarbonate(out) + Na(+)(out) = chloride(out) + 2 hydrogencarbonate(in) + Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 104989
Sequence Length: 952
Subcellular Location: Basolateral cell membrane
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Q9GKY1 | MKLPGQEELEAACACENVPVGQLDSGPSSGPCPDDPSDTGSRELGPPEDPPLFLQLNELLGWPQTLEWREMGRWVLFEEKLEVDAGRWSAPHVPTLALPSLQNLRSLLAEGLVLLDCPAQNLLELVEQVTRVESLSPELRGQLQALLLQRPQHHTQTTGSRPCWGPAQSRKAAHNKEAPMQQQCQSPLRQKLPPGAEAGAVLAGELGFLAQPLAAFVRLRDPVWLGPLTEVPLPSRFFCLLLGPPMLGKGYHELGRAAAVLLSDPHFQWSVRRASNLHDLLTALDAFLEEVTVLPPGRWDPTARIPPPRCLPSRHKRPPLHLQKVKGLSVPHRTQAEDRHRNGPLAPSPELQRTGRLFGGLVQDVRRKASWYPSDFSDALHPQCVSAVLYIYLATVTNAITFGGLLGDATDGAQGVLESLLGTAVAGAAFCLMAGQPLTVLSSTGPVLVFERLLFAFCRDYSLDYLPFRLWVGIWVAVFCLALVATEASVLVRYFTRFTEEGFCALISLIFIYDAVGKMLNLAHAYPIQRPGSLAYGCLCQFPGPGGNESQWTRPRPQSRDDLLSVDLGLVNASLLPPHECVQQGGYPRGPGCHTVPDIAFFSLLLFLTSFLFAIALKHMKTSRFFPSVVRKVLSDFSSILAILLGCGLDALLGLAMPKLMVPREFKPTLPGRGWLVPPFGANPWWLSVAAALPALLLSILIFMDQQITAVILNRVEYRLRKGAGFHLDLFCVALLMLLTSVLGLPWYVSATVLSLAHMDSLRRESRACAPGEPHSFLGIREQRLTGLAVFTLTGVSIFLAPVLKFIPMPVLYGIFLYMGVAALSSIQFMKRVQLMLMPAKHQPDLLLLRHVPLSRVHLFTAIQLACLGLLWIIKSTPAAIIFPLMLLGLVGVRKALEWVFSPQELLWLDELMPEEERNVPEKGLEPGHSFSGSDSEDSELMYQPKAPEINISVN | Function: Electroneutral Cl(-)/HCO3(-) antiporter that favors chloride ion entry and efflux of hydrogencarbonate and sodium ion across the basolateral membrane and may participat in salivary secretion . Also mediates Cl(-)/HCO3(-) exchange activity in the presence of K(+) as well as Cs(+), Li(+), and Rb(+). Does not contribute to Cl(-)/HCO3(-) exchanger in the apical membrane of the upper villous epithelium (By similarity).
Catalytic Activity: chloride(in) + 2 hydrogencarbonate(out) + Na(+)(out) = chloride(out) + 2 hydrogencarbonate(in) + Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105033
Sequence Length: 955
Subcellular Location: Lateral cell membrane
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P15575 | MEGPGQDTEDALRRSLDPEGYEDTKGSRTSLGTMSNPLVSDVDLEAAGSRQPTAHRDTYEGYVELHELVLDSRKDPCWMEAGRWLHLEESMEPGGAWGSHLPLLTYHSLLELHRAFAKGVVLLDVAANSLAAVAHVLLDQLIYEGQLKPQHRDDVLRALLLRHKHPSEAESVWTLPAAQLQCSDGEQKDADERALLRDQRAVEMRELHGAGQSPSRAQLGPQLHQQLPEDTEATLVLVACAAFLEQPLLALVRLGAPCPDAVLAVPLPVRFVLTVLGPDSPRLSYHEIRRAAATVMADRVFRRDAYLCGGRAELLGGLQGFLEASIVLPPQEVPSEQHLHALIPLQRHAVRRRYQHPDTVRSPGGPTAPKDTGDKGQAPQDDDPLLRTRRPFGGLVRDIRRRYPKYLSDIRDALNPQCLAAVIFIYFAALSPAITFGGLLGEKTRGMMGVSELLLSTSVQCLLFSLLSAQPLLVVGFSGPLLVFEEAFFRFCEDHGLEYIVGRVWIGFWLILLVLLVVACEGTVLVRYLSRYTQEIFSFLISLIFIYETFAKLVTIFEAHPLQQSYDTDVSTEPSVPKPNTALLSLVLMAGTFFLALFLRQFKNSVFLPGKVRRLIGDFGVPISIFVMALADFFIKDTYTQKLKVPRGLEVTNGTARGWFIHPMGSATPFPIWMMFASPVPALLVFILIFLETQITTLIVSKPERKLVKGSGFHLDLLLIVAMGGLAALFGMPWLSATTVRTITHANALTVVGKSAVPGERAHIVEVKEQRLSGLLVAVLIGVSILMEPILKYIPLAVLFGIFLYMGVTSLFGIQLFDRILLLLMPPKYHPKEPYVTRVKTWRITSSPLTQILVVALLWGVKVSPASLRCPFVLVLTVPLRRLLLPRIFSEIELKCLDTDDAVVTFEEAEGQDVYNEVQMPS | Function: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine.
Catalytic Activity: chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102223
Sequence Length: 922
Subcellular Location: Cell membrane
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P02730 | MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLVLPPTDAPSEQALLSLVPVQRELLRRRYQSSPAKPDSSFYKGLDLNGGPDDPLQQTGQLFGGLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPAITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLLVVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILLVVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKLIKIFQDHPLQKTYNYNVLMVPKPQGPLPNTALLSLVLMAGTFFFAMMLRKFKNSSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLSVPDGFKVSNSSARGWVIHPLGLRSEFPIWMMFASALPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRVLLPLIFRNVELQCLDADDAKATFDEEEGRDEYDEVAMPV | Function: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein . Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin . Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine .
PTM: Phosphorylated on Tyr-8 and Tyr-21 most likely by SYK. PP1-resistant phosphorylation that precedes Tyr-359 and Tyr-904 phosphorylation.
Location Topology: Multi-pass membrane protein
Catalytic Activity: chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out)
Sequence Mass (Da): 101792
Sequence Length: 911
Subcellular Location: Cell membrane
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P04919 | MGDMRDHEEVLEIPDRDSEEELENIIGQIAYRDLTIPVTEMQDPEALPTEQTATDYVPSSTSTPHPSSGQVYVELQELMMDQRNQELQWVEAAHWIGLEENLREDGVWGRPHLSYLTFWSLLELQKVFSKGTFLLGLAETSLAGVANHLLDCFIYEDQIRPQDREELLRALLLKRSHAEDLGNLEGVKPAVLTRSGGASEPLLPHQPSLETQLYCGQAEGGSEGPSTSGTLKIPPDSETTLVLVGRANFLEKPVLGFVRLKEAVPLEDLVLPEPVGFLLVLLGPEAPHVDYTQLGRAAATLMTERVFRITASMAHNREELLRSLESFLDCSLVLPPTDAPSEKALLNLVPVQKELLRRRYLPSPAKPDPNLYNTLDLNGGKGGPGDEDDPLRRTGRIFGGLIRDIRRRYPYYLSDITDALSPQVLAAVIFIYFAALSPAVTFGGLLGEKTRNLMGVSELLISTAVQGILFALLGAQPLLVLGFSGPLLVFEEAFFSFCESNNLEYIVGRAWIGFWLILLVMLVVAFEGSFLVQYISRYTQEIFSFLISLIFIYETFSKLIKIFQDYPLQQTYAPVVMKPKPQGPVPNTALFSLVLMAGTFLLAMTLRKFKNSTYFPGKLRRVIGDFGVPISILIMVLVDSFIKGTYTQKLSVPDGLKVSNSSARGWVIHPLGLYRLFPTWMMFASVLPALLVFILIFLESQITTLIVSKPERKMIKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASGPGAAAQIQEVKEQRISGLLVSVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPFVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRLILPLIFRELELQCLDGDDAKVTFDEENGLDEYDEVPMPV | Function: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine.
Catalytic Activity: chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 103136
Sequence Length: 929
Subcellular Location: Cell membrane
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P32847 | MENDLSFGEDVMSYEEESDSAFPSPIRPTPPGHSGNYDLEQSRQEEDSNQAIQSIVVHTDPEAYLNLNTNANTRGDAQAYVELNELMGNSWQETGRWVGYEENFNPGTGKWGPSHVSYLTFKSLIQLRKIMSTGAIILDLQASSLSAVAEKVVDELRTKGEIRAADRDGLLRALLQRRSQSEGAVAQPLGGDIEMQTFSVTKQRDTTDSVEASIVLSGVMDSLEKPAVAFVRLGDSVVIEGALEAPVPVRFVFVLVGPSQGGVDYHESGRAMAALMADWVFSLEAYLAPTNKELTNAIADFMDCGIVIPPTEIQDEGMLQPIIDFQKKMLKDRLRPSDTRIIFGGGAKADEADEEPREDPLARTGIPFGGMIKDMKRRYRHYISDFTDALDPQVLAAVIFIYFAALSPAITFGGLLADKTEHMMGVSELMISTCVQGIIFAFIAAQPTLVIGFSGPLLVFEEAFFAFCKSQEIEYIVGRIWVGLWLVIIVVVIVAVEGSFLVKFISRFTQEIFSILISLIFIYETFSKLGKIFKAHPLVLNYEHLNDSLDNPFHPVVKEHIEYHEDGNKTVHEVIHERAYPNTALLSMCLMFGCFFIAYFLRQFKNGHFLPGPIRRMIGDFGVPIAIFFMIAVDITIEDAYTQKLVVPKGLMVSNPNARGWFINPLGEKKPFPAWMMGACCVPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLILVTMGGIASLFGVPWLSAATVRSVTHANALTVMSKGPKPEIEKVLEQRISGMLVAAMVGVSILLEPILKMIPMTALFGIFLYMGITSLSGIQMWDRMLLLIVPRKYYPADAYAQRVTTMKMHLFTLIQMVCLGALWMVKMSAFSLALPFVLILTIPLRMAITGTLFTDKEMKCLDASDGKVKFEEEPGEDMYESPLP | Function: Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine.
Catalytic Activity: chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101894
Sequence Length: 918
Subcellular Location: Cell membrane
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Q9VTG7 | MKGGNYTSLGTCSGINVSGNVAGTRKMSLGKSIKMYLTIFILTTCIYMALYQYHISREPFAASEVVKHQEKSSSYIASYLWSPISLLMANSSSNTNNNSTTTSTTTTTAPTTPTTTTTTTVGSVGQKLGASSISSIRMVSLAATIPSFKSTLSESRSVSLGGHQKTATVKTSTTITTRTTASGLATTKLSATTRTTAKTSAKLSAATTPTASHMENGYKTRPTFVAASLPPPLYIITPTYRRPEQLAELTRLGYTLKHVVNLLWLVIEDANKTNPLVGHTLDRIGVPYEYMVAPMPEKYKQTKKAKPRGVSNRNRGLEYLREHATEGVLYFADDDNTYDISIFEQMRYISKVAMWPVGLVTKTGVSSPIIQAGKLVGYYDGWIGGRKYPVDMAGFAVSVKFLKERPNAQMPFKPGYEEDGFLRSLAPLDDAEIELLADECRDILTWHTQTKKNAPAQALNRTRYKNTNLEHIDRLLVRP | Function: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. Enzyme has a broad specificity.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 52556
Sequence Length: 479
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.135
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Q53461 | PMILLALGLLADTDIASLFTAITMDIGMCVTGLAAALITSSHLLRWVFYGISCAFFVAVLYVLLVQWPADAEAAGTSEIFGTLKILTVVLWLGYPILWALGSEGVALLSVGVTSWGYSGLDILAKYVFAFI | Function: Light-driven chloride pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13951
Sequence Length: 131
Subcellular Location: Cell membrane
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P33970 | IALAGLSILLFVYMGRNVEDPRAQLIFVATLMVPLVSISSYTGLVSGLTVGFLEMPAGHALAGMGAGPEGGVFTPWGRYLTWAFSTPMILIALGLLAGSNMSKLFTAVVADVGMCITGLAAALTTSSYLLRWVWYGISCAFFVVVLYILLAEWAKDAEVAGTADIFNTLKVLTVVLWLGYPIFWALGAEGLAVLDIAITSWAYSGM | Function: Light-driven chloride pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21871
Sequence Length: 206
Subcellular Location: Cell membrane
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B0R2U4 | MSITSVPGVVDAGVLGAQSAAAVRENALLSSSLWVNVALAGIAILVFVYMGRTIRPGRPRLIWGATLMIPLVSISSYLGLLSGLTVGMIEMPAGHALAGEMVRSQWGRYLTWALSTPMILLALGLLADVDLGSLFTVIAADIGMCVTGLAAAMTTSALLFRWAFYAISCAFFVVVLSALVTDWAASASSAGTAEIFDTLRVLTVVLWLGYPIVWAVGVEGLALVQSVGVTSWAYSVLDVFAKYVFAFILLRWVANNERTVAVAGQTLGTMSSDD | Function: Light-driven chloride pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28874
Sequence Length: 274
Subcellular Location: Cell membrane
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O93742 | MMETAADALASGTVPLEMTQTQIFEAIQGDTLLASSLWINIALAGLSILLFVYMGRNLEDPRAQLIFVATLMVPLVSISSYTGLVSGLTVSFLEMPAGHALAGQEVLTPWGRYLTWALSTPMILVALGLLAGSNATKLFTAVTADIGMCVTGLAAALTTSSYLLRWVWYVISCAFFVVVLYVLLAEWAEDAEVAGTAEIFNTLKLLTVVLWLGYPIFWALGAEGLAVLDVAVTSWAYSGMDIVAKYLFAFLLLRWVVDNERTVAGMAAGLGAPLARCAPADD | Function: Light-driven chloride pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30143
Sequence Length: 282
Subcellular Location: Cell membrane
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O00154 | MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVVYSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHAEPQP | Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels . Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18 . May play an important physiological function in brain .
Catalytic Activity: H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate
Sequence Mass (Da): 41796
Sequence Length: 380
Domain: Both HotDog ACOT-type hydrolase domains are required for efficient activity.
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Cytoplasm
EC: 3.1.2.2
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P69051 | MDPIALTAAVGADLLGDGRPETLWLGIGTLLMLIGTFYFIVKGWGVTDKEAREYYSITILVPGIASAAYLSMFFGIGLTEVQVGSEMLDIYYARYADWLFTTPLLLLDLALLAKVDRVSIGTLVGVDALMIVTGLVGALSHTPLARYTWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLWTAYPILWIIGTEGAGVVGLGIETLLFMVLDVTAKVGFGFILLRSRAILGDTEAPEPSAGAEASAAD | Function: Light-driven proton pump. It may interact with bacterioruberin in the claret membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27852
Sequence Length: 260
Subcellular Location: Cell membrane
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P32370 | MDMKHSRLFSPLQIGSLTLSNRVGMAPMSMDYEAADGTVPKRLADVFVRRAEGGTGYVMIDAVTIDSKYPYMGNTTALDRDELVPQFKEFADRVKEAGSTLVPQIIHPGPESVCGYRHIAPLGPSANTNANCHVSRSISIDEIHDIIKQFGQAARRAEEAGCGAISLHCAHAYMLPGSFLSPLRNKRMDEYGGSLDNRARFVIEMIEEARRNVSPDFPIFLRISGDERMVGGNSLEDMLYLAPKFEAAGVSMLEVSGGTQYEGLEHIIPCQNKSRGVNVYEASEIKKVVGIPVYAVGKINDIRYAAEIVERGLVDGVAMGRPLLADPDLCKKAVEGQFDEITPCASCGGSCISRSEAAPECHCHINPRLGREYEFPDVPAEKSKKVLVIGAGPGGMMAAVTAAERGHDVTVWEADDKIGGQLNLAVVAPGKQEMTQWMVHLNYRAKKAGVKFEFNKEATAEDVKALAPEAVIVATGAKPLVPPIKGTQDYPVLTAHDFLRGKFVIPKGRVCVLGGGAVACETAETALENARPNSYTRGYDASIGDIDVTLVEMLPQLLTGVCAPNREPLIRKLKSKGVHINVNTKIMEVTDHEVKVQRQDGTQEWLEGFDYVLFGLGSRNYDPLSETLKEFVPEVHVIGDAVRARQASYAMWEGFEKAYSL | Function: NADH-dependent flavin oxidoreductase . Stereo-specific NAD(H)-dependent 3-oxo-delta4-cholenoic acid oxidoreductase involved in bile acid 7beta-dehydroxylation .
Catalytic Activity: 7beta-hydroxy-3-oxochol-24-oyl-CoA + NAD(+) = 7beta-hydroxy-3-oxochol-4-en-24-oyl-CoA + H(+) + NADH
Sequence Mass (Da): 72029
Sequence Length: 661
Pathway: Lipid metabolism; bile acid degradation.
EC: 1.3.1.116
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B0NAQ4 | MNRIGIIGGGASGIVAAIAAARSDGDAQVFILEQKENIGKKILATGNGRCNLTNEAMDASCYHGEDPEFARNVLKQFGYGETLEFFASLGLFTKSRGGYIYPRSDQAASVLELLEMELRRQKVKIYTGVRVEALKLSAKGFVIRADGQRFPADRVILACGGKASKSLGSDGSGYALARSMGHTLSPVVPALVQLKVKKHPFAKAAGVRTDAKVAALLGRQVLAEDTGEMQITAYGISGIPVFQISRHIAKGLYEGKEMKVRVDFLPEMEASQVRKAFNTHLDKCPYATCQEFLTGIFPKKLIPRLLELSHIRQNFPASELKPAQWEDLIRACKQTLLTIEDTNGFDNAQVCAGGVRTGEVYPDTLESRYADGLYLTGELLDVEGICGGYNLQWAWATGYLAGRAAAERP | Function: Involved in the secondary bile acid metabolism. Catalyzes two subsequent reductions of the double bonds within the bile acid A/B rings of 3-oxochol-4,6-dien-24-oyl-CoA and 12alpha-hydroxy-3-oxochol-4,6-dien-24-oyl-CoA to yield 3-oxocholan-24-oyl-CoA and 12alpha-hydroxy-3-oxocholan-24-oyl-CoA, respectively.
Catalytic Activity: 3-oxocholan-24-oyl-CoA + NAD(+) = 3-oxochol-4-en-24-oyl-CoA + H(+) + NADH
Sequence Mass (Da): 44417
Sequence Length: 409
Pathway: Lipid metabolism; bile acid degradation.
EC: 1.3.1.114
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Q9UQB8 | MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPAQTASGFKQRPYSVAVPAFSQGLDDYGARSMSRNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR | Function: Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions.
PTM: Phosphorylated on tyrosine residues by INSR in response to insulin treatment.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60868
Sequence Length: 552
Domain: The IMD domain forms a coiled coil. The isolated domain can induce actin bundling and filopodia formation. In the absence of G-proteins intramolecular interaction between the IMD and the SH3 domain gives rise to an auto-inhibited state of the protein. Interaction of the IMD with RAC1 or CDC42 leads to activation.
Subcellular Location: Cytoplasm
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Q6GMN2 | MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTFAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKAFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPNKIPDRAAQLMQQMANSNGSILPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQENVPVMNGVAGADSEDYNPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLALPPPDYGTSSRAFPSQTAGTFKQRPYSVAVPAFSQGLDDYGARSVSRNPFANVHLKPTVTNDRSAPLLS | Function: Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions (By similarity).
PTM: Phosphorylated on tyrosine residues by INSR in response to insulin treatment.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59183
Sequence Length: 535
Domain: The IMD domain forms a coiled coil. The isolated domain can induce actin bundling and filopodia formation. In the absence of G-proteins intramolecular interaction between the IMD and the SH3 domain gives rise to an auto-inhibited state of the protein. Interaction of the IMD with RAC1 or CDC42 leads to activation (By similarity).
Subcellular Location: Cytoplasm
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Q94F62 | MERRLMIPCFFWLILVLDLVLRVSGNAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANLSGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSLTAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGSNRITGAIAGGVAAGAALLFAVPAIALAWWRRKKPQDHFFDVPAEEDPEVHLGQLKRFSLRELQVASDNFSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTQGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPESQPPLDWPKRQRIALGSARGLAYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGVMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEALVDVDLQGNYKDEEVEQLIQVALLCTQSSPMERPKMSEVVRMLEGDGLAERWEEWQKEEMFRQDFNYPTHHPAVSGWIIGDSTSQIENEYPSGPR | Function: Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Controls the expression of genes associated with innate immunity in the absence of pathogens or elicitors. Involved in brassinosteroid (BR) signal transduction. Phosphorylates BRI1. May be involved in changing the equilibrium between plasma membrane-located BRI1 homodimers and endocytosed BRI1-BAK1 heterodimers. Interaction with MSBP1 stimulates the endocytosis of BAK1 and suppresses brassinosteroid signaling. Acts in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) via its interactions with FLS2 and EFR, and the phosphorylation of BIK1. Involved in programmed cell death (PCD) control. Positively regulates the BR-dependent plant growth pathway and negatively regulates the BR-independent cell-death pathway . Phosphorylates BIR2 and thus promotes interaction with BIR2 . This interaction prevents interaction with FLS2 in the absence of pathogen-associated molecular patterns (PAMP) . Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity . Required for PSK promotion of seedling growth and protoplast expansion . CNGC17 and AHAs form a functional cation-translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes . Required during SCOOP small peptides (e.g. RGF1, SCOOP10 and SCOOP12) perception and signaling; associates with MIK2 as a coreceptor upon MIK2 perception of SCOOP peptides, and relays the signaling through the activation of receptor-like cytosolic kinases (RLCKs) BIK1 and PBL1 (Probable) .
PTM: Autophosphorylated on Ser-290, Thr-312, Thr-446, Thr-449, Thr-455 and Tyr-610. Probable autophosphorylation on additional Tyr residues. Transphosphorylated by BRI1. It is not sure whether Thr-589 or Ser-595 is the target of the phosphorylation. The phosphorylations on Thr and Tyr are induced by brassinolide. Phosphorylation at Ser-286, Ser-290 Thr-446 or Thr-449 is not critical for flagellin signaling. Phosphorylated on Ser-612 upon SCOOP12 detection; a post-translational modification required for immune signaling .
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68161
Sequence Length: 615
Domain: Contains one leucine-zipper motif and one pair of conservatively spaced Cys (Cys pair) involved in forming heterodimers.
Subcellular Location: Cell membrane
EC: 2.7.10.1
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Q6Z4U4 | MAAHRWAVWAVLLLRLLVPAARVLANMEGDALHSLRTNLVDPNNVLQSWDPTLVNPCTWFHVTCNNDNSVIRVDLGNAALSGTLVPQLGQLKNLQYLELYSNNISGTIPSELGNLTNLVSLDLYLNNFTGPIPDSLGNLLKLRFLRLNNNSLSGSIPKSLTAITALQVLDLSNNNLSGEVPSTGSFSLFTPISFANNPSLCGPGTTKPCPGAPPFSPPPPYNPPTPVQSPGSSSSTGAIAGGVAAGAALLFAIPAIGFAWYRRRKPQEHFFDVPAEEDPEVHLGQLKRFSLRELQVATDTFSNKNILGRGGFGKVYKGRLADGSLVAVKRLKEERTPGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASRLRERPPSEPPLDWRTRRRIALGSARGLSYLHDHCDPKIIHRDVKAANILLDEDFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGIMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKRLEMLVDPDLQSNYIDVEVESLIQVALLCTQGSPTERPKMAEVVRMLEGDGLAERWEEWQKIEVVRQEVELGPHRNSEWIVDSTDNLHAVELSGPR | Function: LRR receptor kinase involved in defense response . Does not seem to be required specifically for XA21-mediated immunity or basal resistance to Xanthomonas oryzae pv. oryzae (Xoo), or immunity to Magnaporthe oryzae . Involved in brassinosteroid (BR) signaling pathway. Acts as coreceptor of BRI1. Forms at the plasma membrane a receptor complex with BRI1 which is activated in response to brassinolide. Phosphorylates BRI1 . Required for normal plant growth and leaf development . Possesses kinase activity in vitro .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 68702
Sequence Length: 624
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q6ZNE5 | MASPSGKGARALEAPGCGPRPLARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSRLKSKQEEFQKEVLKAMEGKWITDQLRWKIMSCKMRIEQLKQTICKGNEEMEKNSEGLLKTKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTIDLRSHYERLANLRRSHILELTSVIFPIEEVKTGVRDPADVSSESDSAMTSSTVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYSWVEEKKTTQGPDMEQSNPAYTISAALCYATQLVNILSHILDVNLPKKLCNSEFCGENLSKQKFTRAVKKLNANILYLCFSQHVNLDQLQPLHTLRNLMYLVSPSSEHLGRSGPFEVRADLEESMEFVDPGVAGESDESGDERVSDEETDLGTDWENLPSPRFCDIPSQSVEVSQSQSTQASPPIASSSAGGMISSAAASVTSWFKAYTGHR | Function: Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 . Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine . Promotes BECN1 translocation from the trans-Golgi network to autophagosomes . Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1 . Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation PIK3C3 by AMPK . Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion . Modulates the hepatic lipid metabolism (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55309
Sequence Length: 492
Domain: The coiled-coil domain is required for BECN1- and PIK3C3-binding and for autophagy.
Subcellular Location: Cytoplasm
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Q8CDJ3 | MASPSGKGSWTPEAPGFGPRALARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTICKGNEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTIDLKSHYERLARLRRSHILELTSIIFPIDEVKTSGRDPADVSSETDSAMTSSMVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYNWVEEKKTTQGPDMEHNNPAYTISAALGYATQLVNIVSHILDINLPKKLCNSEFCGENLSKQKLTRAVRKLNANILYLCSSQHVNLDQLQPLHTLRNLMHLVSPRSEHLGRSGPFEVRADLEESMEFVDPGVAGESDASGDERVSDEETDLGTDWENLPSPRFCDIPSQPVEVSQSQSTQVSPPIASSSAGGMISSAAASVTSWFKAYTGHR | Function: Required for both basal and inducible autophagy . Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 (By similarity). Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine . Promotes BECN1 translocation from the trans-Golgi network to autophagosomes (By similarity). Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1 (By similarity). Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation of PIK3C3 by AMPK . Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion (By similarity). Modulates the hepatic lipid metabolism .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55388
Sequence Length: 492
Domain: The coiled-coil domain is required for BECN1- and PIK3C3-binding and for autophagy.
Subcellular Location: Cytoplasm
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D4A4K3 | MASPSGKGSWTPEAPGFGPRALAPDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSQLKNKQEEFQKEVLKAMEGKRLTDQLRWKIMSCKMRIEQLKQTICKGNEEMKKNSEGLLKNKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTSDLREHYDRLACLRRLHILELTSVIFPMDEVKTSGRDPADVSSETDSAMTSSMVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYNWVEEKKTTQGPDMEHNNPAYTISAALGYATQLVNIVSHILDINLPKKLCNSEFCGENLSKQRLTRAVRKLNANILYLCSSQHVNLDQLQPLHTLRNLMHLVSPHSEHLGRSGPFEVRADLEESMEFVDPGVAGESDVSGDERVSDEETDLGTDWENLPSPRFCDIPSQPVEVSQSQSTQASPPIASSSAGGMISSAAASVTSWFKAYTGHR | Function: Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex. Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine. Promotes BECN1 translocation from the trans-Golgi network to autophagosomes. Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1. Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation PIK3C3 by AMPK. Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion. Modulates the hepatic lipid metabolism (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55345
Sequence Length: 492
Domain: The coiled-coil domain is required for BECN1- and PIK3C3-binding and for autophagy.
Subcellular Location: Cytoplasm
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Q16611 | MASGQGPGPPRQECGEPALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNGPILNVLVVLGVVLLGQFVVRRFFKS | Function: Plays a role in the mitochondrial apoptotic process. Upon arrival of cell death signals, promotes mitochondrial outer membrane (MOM) permeabilization by oligomerizing to form pores within the MOM. This releases apoptogenic factors into the cytosol, including cytochrome c, promoting the activation of caspase 9 which in turn processes and activates the effector caspases.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23409
Sequence Length: 211
Domain: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family.
Subcellular Location: Mitochondrion outer membrane
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O08734 | MASGQGPGPPKVGCDESPSPSEQQVAQDTEEVFRSYVFYLHQQEQETQGAAAPANPEMDNLPLEPNSILGQVGRQLALIGDDINRRYDTEFQNLLEQLQPTAGNAYELFTKIASSLFKSGISWGRVVALLGFGYRLALYVYQRGLTGFLGQVTCFLADIILHHYIARWIAQRGGWVAALNFRRDPILTVMVIFGVVLLGQFVVHRFFRS | Function: In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23295
Sequence Length: 209
Domain: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family.
Subcellular Location: Mitochondrion outer membrane
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Q961J5 | MDFDEVLREVGSFGLYQKVIICSVLLPAALPCAFHAYSQLFIAATPQHFCRVPELEPWTQDYVQLVKNLSIPRNRNGAYAECSMYSRNYTDIVRYLEYRPPPDLLRQQAEDLLKLQPDTTQVVPCQHGWHYDKSIYSSTVVQEWNLVCDRSFLVTLALVVFGVGGLLGNYVFGYLVDLWGRRPSFYAYLLLEIIACAASAFAWNYYTWLGLRFVVGLTVPAILASPYVLAIELVGPERRVFCTIVSNIAYSLGLVVLAGVIYIVRDWRELSLAVSMPLLMLFSCFFVLPESPRWLMAVGKTRRAIKILKVMARVNGVRVNRDFVERLQRKLVITRAAETKSSMTTHYGILDLFRGPNMRRKTLIITLIWFANTSVYVGLSYYAPALGGDEIWNFFLAGAVELPTYLLLWPGLSYFGRRWILFISMLVGGVACVATFLYPDITLLLYCVGKMGISSSFVVLPLMASELYPTVVRGLGMSFSSVISMVGPIVIPMINHMGQQMLVLPLIVMGALLILGGFASLLLPETRNRNLPQTLEEGEAVPLSFLLCCCVESERKPNNIRASPKKRILPEAGTPVFHRVDTPVSDRVPCKIVCSICKNEMRTL | Function: Beta-alanine transporter required for the uptake of beta-alanine by the glia . Required for the recycling process of the neurotransmitter histamine in photoreceptor neurons of the compound eye and therefore for photoreceptor synaptic transmission . Following histamine release from photoreceptors and its uptake by glia, histamine is conjugated to beta-alanine by e/Ebony to form the inactive metabolite, carcinine .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67905
Sequence Length: 604
Subcellular Location: Cell membrane
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F4JPW1 | MGVISPTETLFLKSQHRLLQPRNYSYALAFHSTRRVANFPRNSFSSLGSCSVDFPLRSNPISQNSKSIHPWRRYVSESDSNELYHKKVSSIMETLKQAYSFIPHGILLSTILALVYPPSFTWFKPRYFVPGLGFMMFAVGINSNERDFLEALKRPDAIFAGYIGQYLIKPLLGYIFGVIAVSLFNLPTSIGAGIMLVSCVSGAQLSNYTTFLTDPSLAALSIVMTSISTATAVLVTPMLSLLLIGKKLPVDVFGMISSILQVVITPIAAGLLLNRLFPRLSNAIKPFLPALTVIDMSCCIGAPLALNIDSILSPFGATILFLVITFHLLAFVAGYFFTGFFFSKAPDVKALQRTISYETGMQSSLLALALATKFFQDPLVGVPPAISTVVMSLMGVSLVTIWKNRKE | Function: Plastidic transporter involved in the biosynthesis of aliphatic glucosinolates by translocating the biosynthetic intermediates of Met-derived glucosinolates across chloroplast membranes. Transports short chain (C2) alpha-keto acids, such as 4-methylsulfanyl-2-oxobutanoic acid, from the cytosol to the chloroplast where they are subjected to chain elongation cycles. Functions also in the transport of chain-elongated (C3 to C8) Met derivatives from the chloroplast to the cytosol. Does not seem to be involved in the transport of indole-derived glucosinolates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44582
Sequence Length: 407
Subcellular Location: Membrane
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