ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9D7F7 | MSKLGKFFKGTRSSRARAAPSAQEALARLRETEEMLAKKQEYLENRIQRELALAKKHGSQNKRAALQALKRKKRFEKQLTQVDGTLSTIEFQREALENSHTNTEVLRNMGFAAKAMKAVHDNMDLNKIDDLMQDITEQQDIAQEISEAFSQRVQFADGFDEAELLAELEELEQEELNKKMTSLELPNVPSSSLPAQPSRKASMPSSVHRSRAASSRRAEEDDDFKQLAAWAT | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: upon phosphorylation by AURKB, together with ZFYVE19/ANCHR, retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ANCHR and VPS4 and subsequent abscission. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
PTM: Phosphorylated at Ser-210 by AURKB during cytokinesis: together with ZFYVE19/ANCHR, phosphorylated CHMP4C retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26280
Sequence Length: 232
Domain: The acidic C-terminus and the basic N-terminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity).
Subcellular Location: Cytoplasm
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P30577 | KMLTSRTLHGVMQNIRDIVNLKKSEFWNKGGPAWQKIAVCLVFDGIDPCDKDTLDVLATIGIYQDGVMKKDVDGKETIAHIFEYTTQLSVTANQQLIRPHDDGPSTLPPVQMMFCLKQKNSKKINSHRWLFNAFGRILNPEICILLDAGTKPGHKSLLALWEAFYNDKDLGGSCGEIHAMLGKGWKNLINPLVA | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21690
Sequence Length: 194
Subcellular Location: Cell membrane
EC: 2.4.1.16
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P30582 | EIGFTRTLHGVMQNITHLCSRSKSRTWGKDGWKKIVVCIIADGRKKVHPRTLNALAALGVYQEGIAKNVVNQKQVNAHVYEYTTQVSLDPDLKFKGAEKGIMPCQVLFCLKEHNKKKLNSHRWFFNAFGRALQPNICILLDVGTKPAPTALYHLWKAFDQNSNVAGAAGEIKAGKGKGMLGLLNPLVAS | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20878
Sequence Length: 189
Subcellular Location: Cell membrane
EC: 2.4.1.16
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P30572 | MSYNNPNNSNSHLRPHAYNNSRRDDSDGDESSIEFLNQRSNTPLTQGTYNYHNTSTNSLNFQQPEPIYRNQTRTSLSDSYYDHPIFDTSQTQIQPPHDNPFTESYEMTDTSYQGNDHHYRTGQPNHLMNPTYNQAFIPHVYDEEDNDEQEYDQRIQYNQFQGDHFDLAAISYADDESQSQLDYVPTERVIPEGEEEEEEGETSFEKEPGSETISGPFGEERSFEEPPPQQEVRSKKLTRATGLNGHLVLDCPVADELLSKFPDYNPAEKSGGLSREFAFMRYTAVTCGPSNFYRDAYILRPVHYPIPRQTELMIVITMYNEDDILLGRTLKGVFKNIKYLESKARSSTWGKDSWKKIVVCIVSDGRTKINERAQALLAGLGVYQEGLAKSRVDDKKVQAHMFEYTTRVGISKVTDDVVKLTTEKVVPVQMLFCLKETNAKKINSHRWCFQAIGQVLDPKIVVLLDCGTQPSGRSLYELWKEFDRDHRVAGACGEITTSLKKRQMITNPLVYGQNFEYKISNILDKPTESSFGFISVLPGAFSAYRFIALQNDINGIGPLEKYFKGEFLHSSGELDPNDDEFQMKHLMLKEEAGIFTSNMYLAEDRILCFELVAKRGCNWLLRYCKSARAETDVPEGLAEFILQRRRWLNGSFFAAIYSLVHFYKVWTSSHSFGRKIFLHIEFFYQLINLIVSWFSIGSYFLVFRILTTSLGDKALGFAPGKILSVIFLWLYLASIVTTFVLSFGNKPKGTEKFYVTIVIFFAILMAYMIFAAIFMAVHSIQDIYRSGTRITVSLFFQNSEFRDLVVATSSTYALYFLASFLYFEPWHMFTSFVQYILLSPSYVNVLNIYAFCNIDDISWGTKGEVGGKSLGEAKLREDGTFDVSVPISKEQINQSYLDQLEKIRDPAPPEEKVLVTNTEDYYAFIRSMTVLVWMFTNFVVIALVLETGGFNQFVEATDLANLKSNRAAVFLTVILWTVAFMALFRFIGCIYYLITRLGREIKASEHATK | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 115586
Sequence Length: 1009
Subcellular Location: Cell membrane
EC: 2.4.1.16
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J9VQ06 | MAYHYSHDSDRRQPHGGYNYPSNYSNPSQYSIPDSVYSGHSTNTPRVPSPGGYHQQPSPTTRAVNPAYYQPQPTASSMTSHDLMYGRPSPGPNQYGAAPADVVRGPGATTVPLSQQAPYQPYPSHTDYSDEDKSFASTTHLVSPQKEWGVGSVVPVTTIPPVNQLPYQPYQAYPPRPSPSPITHRGGTSHWHAMRKQLLERRVIKQIPLHNGNLVMDVPVPKGVIPSTKGLGVMDGEMDSMRYSAATCDPDDFMGSKFSLRQYLYGRKTELFIVMTMYNENSELLLRTLNAVIKNIAHLTTRTRSKTWGPDSWKKVVVCIVADGRKVVDPRVLKVLQLMGVYAEGVMKDHVVDKETQAHIFEYTSQVVVSETGEVGFGSTPIQLLFCLKEQNKKKLNSHRWFFNAFGPLIKPNVCVLLDVGTKPSGHSIYELYKCFEKHPTVGGACGEIFADTGKWGKYLWNPLVAGQNFEYKMSNILDKPFESVFGLISVLPGAFSAYRYDAVANHADGTGPLAAYFRGELMNQPGATATIFDRNKFLAEDRILAFEIVVKKNARWRLQYVKAAKAGTDVPATVPEFISQRRRWLNGSIFAATYAMVCFWRIWTSGHGIFRKFTLTFLTIYNLFNLLFNWLSVSSFYLAFFFLISSSISGSSDPFNGAGDEIFQVFNKVYIALIFVVLVCSLGNRPQGSNYMYTFCIFMFAVCQGILLYCAGWTVYQTVPHTSEGWEDVSGLFENRTFVQLALSLMATYGLYLISSLLYFEPWHMLTSFVQYLLLLPSYVNILLIYAMCNLHDVSWGTKGDNGSSKDLGAAKKVEKDGKEMAEVALPTKQEDVEALWQQARQELRVPVKEKAEKRSPETKRADEDRNFRTNVVLLFLGSNMLIILLFTSSTFTNWVNSHFVDATSSTFNPYLTVIFYAVLGLSALRFAGCLLYLIFRMFGY | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105826
Sequence Length: 942
Subcellular Location: Cell membrane
EC: 2.4.1.16
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P30601 | MAYNRLGSPQRDGPYSPSAQPQYDSRSPSPGRPLQPYIHPDEAYARQQPLHLQMPTASDDRLAMQPTYSVENVHNPQAYGQQYGQHLPDSGDMGYGRNDYIVSPEEHHDAYYTQPYSPHPQGDYALDPYPSHDEPYRPDTDNVPILQPDSAYGPDPHTQPGMDYDDYQEEPRPTPSPAPIRRWKTVKEVQLFNGNLVLDCPVPPKLLANVPHAKPPERDEFTHMRYSAATCDPSDFHNERFTLRQRLFAKPRQTELFIVVTMYNEDEFLFARTMIGVFKNIEFMCNRSSSKTWGKEAWKKIVVCIVSDGRAKINPRTRAVLAGLGVYQDGIAKQQVNGKDVTAHIYEYTTQVGLELKGTQVSLKPRSATPVQLLFCLKEKNQKKINSHRWFFQAFGRVLDPNICVLIDAGTKPGKDSIYQLWKAFDLEPMCGGACGEIKVMLDHGKKLLNPLVATQNFEYKMSNILDKPLESAFGFISVLPGAFCAYRYVALQNDKNGVGPLEKYFKGETMHADAGVFTANMYLAEDRILCFELVSKRNCRWILQYVKSATGETDVPDRIPEFVLQRRRWLNGSFFAAVYAVAHVYQLWRTDHSFLRKLMFLIEFTYQTINMLFAWFAIGNFFLVFRLLTASLGTKETLGTAGTVLGVVFEFVYLGTLLYCFILSMGNRPQGNPKSYMMMVIFWSVLMVWLTFASIFLTVKSIETEVQQKDFSFSTIFNNSTFFGLIVSLASTYVLWFVASFLFFDPWHMFTCFLQYIVLTPTYINVLNIYAFCNTHDITWGTKGDDKAEKLPSANVKPGGKVDVLIPQDDGDLNAQYDSELKKFATKPPKEVKAPNPADKQEDYYKSFRSNVVTAWMITNFILVAAVLNIAGFDRINVHDTQQQNSTIYLAVILWSVAGLSLFRFTGACWFLVVRMVSLEIWSVCKV | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105713
Sequence Length: 928
Subcellular Location: Cell membrane
EC: 2.4.1.16
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Q8H4L3 | MVTSTVKLEEVRRMQRAEGMAAVLAIGTATPANCVYQTDYPDYYFRVTNSEHLTNLKERFQRMCESSQIRKRYTHLTEEILQENPSMCVFTAPSLDARQDMVVAEVPKLGKAAAEEAIKEWGQPMSRITHLVFCTTNGVDMPGADYQVAKMLGLPTSVKRLMMYQQGCFAGGTVLRVAKDLAENNRGARVLVVCSEIMAMAFRGPSESHLDSLVGHALFGDGAAAVIVGSDPDEAADERPLFQIVSASQTILPGTEDAIVGHLREVGLTFHLPKDVPEFISDSVEGALTDAFMPLGVHDWNSIFWVVHPGGPAILDQVEEKVALHKARMRASRNVLSEYGNMASATVLFVLDEMRKLSADDGHATTGEGMDWGVLFGFGPGLTVETIVLHSVPITAAAPLIMQ | Function: The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Catalytic Activity: 4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA
Sequence Mass (Da): 43925
Sequence Length: 403
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 2.3.1.74
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O53547 | MKLTESNRSPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVVDEIGAAAADAGAKAVAVAGDISQRATADELLASAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRDKAKDAEGGSVFGRLVNTSSEAGLVGPVGQANYAAAKAGITALTLSAARALGRYGVCANVICPRARTAMTADVFGAAPDVEAGQIDPLSPQHVVSLVQFLASPAAAEVNGQVFIVYGPQVTLVSPPHMERRFSADGTSWDPTELTATLRDYFAGRDPEQSFSATDLMRQ | Function: A reversible dehydrogenase involved in cholesterol side-chain degradation. Catalyzes the oxidation of hydroxyl-cholesterol-CoA ester metabolic intermediate (22S)-HOCO-CoA (3-oxo-chol-4-ene-(22S)-hydroxy-24-oyl-CoA), the product of ChsH3, has no activity on (22R)-HOCO-CoA (the product of EchA19). Also acts on (3R)-hydroxyoctanoyl-CoA and 17-beta-hydroxyandrost-4-en-3-one, but not on 7-alpha-hydroxyandrost-4-en-3-one, uses NAD(+) but not NADP(+).
Catalytic Activity: (22S)-hydroxy-3-oxo-chol-4-ene-24-oyl-CoA + NAD(+) = 3,22-dioxochol-4-en-24-oyl-CoA + H(+) + NADH
Sequence Mass (Da): 32753
Sequence Length: 317
Domain: The protein surface forms a large groove around the active sites which is larger than homologs, probably to accommodate bulky sterol substrates.
Pathway: Steroid metabolism; cholesterol degradation.
EC: 1.1.1.-
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Q00757 | MAYHGSGPQSPGEHTYDDGHQLRDLSHSNTSYEEEASHGLLSSQQSPFAGPFDDPHQQRGLTASPVQRPTSGYSLTESYAPDAAYHDPYSANQSVYSGHSENPAAAFGVPGRVASPYARSETSSTEAWRQRQAGAAGGGNGLRRYATRKVKLVQGSVLSVDYPVPSAIQNAIQAKYRNDLEGGSEEFTHMRYTAATCDPNEFTLHNGYNLRPAMYNRHTELLIAITYYNEDKTLTARTLHGVMQNIRDIVNLKKSEFWNKGGPAWQKIVVCLVFDGIDPCDKDTLDVLATVGIYQDGVMKRDVDGKETVAHIFEYTTQLSVTPNQQLIRPTDDGPSTLPPVQMMFCLKQKNSKKINSHRWLFNAFGRILNPEVCILLDAGTKPGPKSLLYLWEAFYNDKDLGGACGEIHAMLGKGWKKLLNPLVAAQNFEYKISNILDKPLESSFGYVSVLPGAFSAYRFRAIMGRPLEQYFHGDHTLSKQLGKKGIEGMNIFKKNMFLAEDRILCFELVAKAGSKWHLSYVKASKGETDVPEGAPEFISQRRRWLNGSFAAGIYSLMHFGRMYKSGHNIVRMFFLHLQMLYNWFSTFLTWFSLASYWLTTSVIMDLVGTPSSSNGYTAFPFGKTATPIINTLVKYIYLAFLLLQFILALGNRPKGSKLSYLASFVAFGIIQLYVVVDALYLVVRAFTGGAPMDFNTDDGIGAFLSSFFGSSGAGIIIIALAATFGLYFVASFMYLDPWHMFTSFPAYMAVQSSYINILNVYAFSNWHDVSWGTKGSDKADALPSAKTTGGKGEEAVIEEIDKPQADIDSQFEATVKRALTPYVPPEEKEEKSLDDSYKSFRTRLVTLWLFSNGLLAVCITSEGLDKFGFTNTSTERTSRFFQALLWSNAVVALIRFIGATWFLGKTGLLCCFARR | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101882
Sequence Length: 916
Subcellular Location: Cell membrane
EC: 2.4.1.16
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P48398 | MSTTVTVLTDTWSRRAKRLEGDAKILAIGTATPASWVDQTTYPDFYFRITNSQHLLEHKEKFRRICNKSKIRKRHLVLTEELLKKNPNLCTYNETSLNTRQDILVSEVPKLGKEAAMKAIKEWGRPISEITHLVFCTTSGVDMPGADFQLTKLLGLNSSVKRLMMYQQGCNAGAAMLRLAKDLAESNKGGRVLVVCAEITINIFRGPSLEQDDNLLAQCLFGDGAAAMIVAADPRPGLETPLFELVSSAQTIVPNTDSHLKLHLREMGLTFHCSKAVPSVLAENVEDCLVKAFEPYGISDWNSIFWVFHPGGNAIVDRVEERLGLGPEKLRASRDVLSEYGNLTSACVLFILDEMRKKSKKDEQMTTGEGLEWGVVFGFGPGLTIDTIIIRSVPIN | Function: The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Catalytic Activity: 4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA
Sequence Mass (Da): 43927
Sequence Length: 396
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 2.3.1.74
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P22924 | MKVENGQLQGWWAQRAEGPAKILAIGTATPFHWVDQNSYPDYYFRVTNSQHLVDLKEKFRRICSKTMIKKRHMFLTEELLRKNPTLCSHNEPSLDIRQDILVSEIPKLGKEAALKAIGEWGQPKSTITHLVFCTRSGVDMPGADCQLVKLLGLSPSVQRLMMYQQGCFAGGTMLRLAKDLAENNKGARVLVVCAESSAIGFRGPSEANVDNLIAQALFGDGAAALIIGSDPKPGLERPVFEIFSAAQTFVPNGDCHLALHLREMGLTFHCTKDVPPTIAKNVESCLIKAFEPLGISDWNSLFWILHPGGNAIVDQVESTLGLGPEKLRATRNILSEYGNLSSACCLFILDEIRKKSAREGMRTSGDGLDLGVLLSFGPGLTIETVVLRSVPI | Function: The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Catalytic Activity: 4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA
Sequence Mass (Da): 42957
Sequence Length: 392
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 2.3.1.74
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P30583 | MSYNRLGDPYGDDRDARSPIMNPSSLSNRSPSPGRPLDGYQLSDAPYGHHHHIEMPSSDRLAEQPTYSVERIPQSYGHNEAYEAQHQHYPGYEYSVDPEAHHDAYYTQPYQPTVTPGHDDYDLGQYPGHQHSYQDDEPILQPEDPFQAQNPYSDDYQEDMTIAPTPSPAPLRRWKTVKEVQLFQGNLVLDCPIAPKLLNQIPHAENGQRDEFTHMRYSAATCDPKDFFEERFTLRQKLFAKPRHTELFIVVTMYNEDDFLFARTMVGVFKNIEHMCSRTRSKTWGKDAWKKIVVCVISDGRAKINPRTRAVLAGLGCYQDGIAKQQVNGKDVTAHIYEYTTQVGMELKGNQVHLKPRSGVPVQMIFCLKEKNQKKINSHRWFFQAFGRVLDPNICVLLDAGTQPGKDSIYRLWKAFDVEPMCGGACGEIKVMLDHGKKLFNPLVAGQNFEYKLSNILDKPLESAFGFISVLPGAFSAYRYIALQNDKNGQGPLERYFLGEKMHGANAGIFTANMYLAEDRILCFEIVTKRNCRWLLQYVKSSTGETDVPDQMAEFILQRRRWLNGSFFAAVYAITHFYQLWRSDHSFIRKFMLLIETIYQTINMLFAWFGIGNFFLVFHILTTYLGDADLLGTAGKVLGVVFEWLYLATLVTCFVLSLGNRPGGSNKLYMTMVYLWVFIMIYLAFAAVFVTVRSIQEEVKDGSFTFSTLFTNSTFFSIIVSLGSTYVMWFIASIIFMDPWHMFTCFIQYILLTPTYINVLNIYAFCNTHDITWGTKGDDKAEKLPSANLKPGGKVDVNIPQDDGDLNAQYEAELMKFAQKPPKEIKTISEEERQADYYKGFRSSVVLVWVFCNFALGAVVLSSAGLDRFSDDAEAAETDRNNRAMIYMAVVLWSVAGLSIFKFLGAMWFLVVRMFRGV | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 104831
Sequence Length: 918
Subcellular Location: Cell membrane
EC: 2.4.1.16
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P78746 | MIVLFTLLRWAPISPVFSMRTMHANLAHRGIFLPVMIVTLPLPVHLRRRFPAQMVLMLQWFAFGMFSVLLIIPWLLCVYRLVTHSPGRTKRIKQVLDDRTAPKTVVVMPVYKEAPETLIRAIDSVVDCDYPANCIHVFLSYDGCLIDESYLRLIEHLGIPITLESYPQSIDVTYKDARITVSRFKHGGKRHCQKQTFRLIDMVYADYLERHDNLFVLFIDSDCILDRVCLQNFMYDMELKPGSKHDMLAMTGVITSTTDRGSLLTLLQDMEYVHGQLFERSVESSCGAVTCLPGALTMLRFSAFRKMAKYYFADKAEQCEDFFDYGKCHLGEDRWLTHLFMVGARKRYQIQMCAGAFCKTEAVQTFSSLLKQRRRWFLGFITNEVCMLTDVRLWKRYPLLCLVRFMQNTIRTTALLFFIIALSLITTSSSINDLPVGFIAISLGLNYVLMFYLGAKLKRYKAWLFPLMFILNPFFNWLYMVYGILTAGQRTWGGPRADAATADEHTSPEEAVELAKAQGDELNVDLTTFRSRGDEKSVPIHPSEKIDGRFSAPELPDGYDSNLNDSNAALTELMTPLPSVPRIGIHTYPSSDSILTSDSLSSIHLPLKVEELTGDNDNMKPYPDRQPRDTSSLHQMQRTCSNGIVASDSCSSQDDASEMVNKPEILSPSAHILPHPSQATESSSGEDIYPLHLPSPHQHEAHFAPLNASTRGSMEGNTPEVQRPRRKLPGIPRPIRAQKDPESMV | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84522
Sequence Length: 745
Subcellular Location: Cell membrane
EC: 2.4.1.16
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Q9SA37 | MDPKMLFCLPEGDALFNPLNTMFIQMACILVFSQFFYLFLKPCGQAGPVAQILAGIVLSLLTIIRKVHEFFLQKDSASYYIFFSFLLRTAFVFLIGLEIDLDFMKRNLKNSIVITLGSLVISGIIWLPFLWFLIRFMQIKGDFLTFYLAFLITLSNTAAPVVIRSIIDWKLHTSEIGRLAISCGLFIEITNIFIYTIVLSFISGTMTADIFIYSFATGVIILTNRFLASWLPKRNPKEKYLSKAETLAFIILILIIALTIESSNLNSTLFVFIIGLMFPREGKTYRTLIQRLSYPIHEFVLPVYFGYIGFRFSVNSLTKRHYLVLGMTVALSLLGKLLGVLFACSFLKIPKQYWLFLSTMLSVKGHIGLVLLDSNLMYKKWFTPVVHDMFVAALVIMTLLSGVITSLLLRSQEKSFAHIKTSLELFDTTEELRVLTCVYGVRHARGSISLVSALSGFSPGTSSSPFTPYLMHLIPLPKKRKTELLYHELDEDAGNSNGGDDEFGTNEGLEINDSIDSFTRDRKIMVRQVKLVAPMENMHEEICNATEDLRVSIVFLPFHKHQRIDGKTTNDGEVFRHMNRKVLKQAQCSIGIFVDRNITGFHQLHGSDSVQHVAALFFGGPDDREALSLCKWLTNNSQIHLTVIQFVADDSKTEKIVGDAVTKENNEVFLEIVSEDQTENETDRIFLEEFYHRFVTTGQVGFIEKRVSNGMQTLTILREIGEMYSLFVVGKNRGDCPMTSGMNDWEECPELGTVGDFLASSNMDVNASVLVVQRHRNSFDSFVDE | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88909
Sequence Length: 785
Subcellular Location: Membrane
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Q9M353 | MPFNITSVKTSSNGVWQGDNPLNFAFPLLIVQTALIIAVSRFLAVLFKPLRQPKVIAEIVGGILLGPSALGRNMAYMDRIFPKWSMPILESVASIGLLFFLFLVGLELDLSSIRRSGKRAFGIAVAGITLPFIAGVGVAFVIRNTLYTAADKPGYAEFLVFMGVALSITAFPVLARILAELKLLTTQIGETAMAAAAFNDVAAWILLALAVALAGNGGEGGGEKKSPLVSLWVLLSGAGFVVFMLVVIRPGMKWVAKRGSPENDVVRESYVCLTLAGVMVSGFATDLIGIHSIFGAFVFGLTIPKDGEFGQRLIERIEDFVSGLLLPLYFATSGLKTDVAKIRGAESWGMLGLVVVTACAGKIVGTFVVAVMVKVPAREALTLGFLMNTKGLVELIVLNIGKEKKVLNDETFAILVLMALFTTFITTPTVMAIYKPARGTHRKLKDLSASQDSTKEELRILACLHGPANVSSLISLVESIRTTKILRLKLFVMHLMELTERSSSIIMVQRARKNGLPFVHRYRHGERHSNVIGGFEAYRQLGRVAVRPITAVSPLPTMHEDICHMADTKRVTMIILPFHKRWNADHGHSHHHQDGGGDGNVPENVGHGWRLVNQRVLKNAPCSVAVLVDRGLGSIEAQTLSLDGSNVVERVCVIFFGGPDDRESIELGGRMAEHPAVKVTVIRFLVRETLRSTAVTLRPAPSKGKEKNYAFLTTNVDPEKEKELDEGALEDFKSKWKEMVEYKEKEPNNIIEEILSIGQSKDFDLIVVGRGRIPSAEVAALAERQAEHPELGPIGDVLASSINHIIPSILVVQQHNKAHVEDITVSKIVSESSLSINGDTNV | Function: Operates as a K(+)/H(+) antiporter that maintains K(+) homeostasis in guard cells and could regulate pH. Plays a critical role in osmoregulation through the control of stomates opening.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91553
Sequence Length: 842
Subcellular Location: Endomembrane system
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Q8VYD4 | MSSGAPLNVTNPNYDIEESRFGKIVCYDQSLLFEKREQKGWESGSTLASSLPFFITQLFVANLSYRVLYYLTRPLYLPPFVAQILCGLLFSPSVLGNTRFIIAHVFPYRFTMVLETFANLALVYNIFLLGLGMDLRMVRITELKPVIIAFTGLLVALPVGAFLYYLPGNGHPDKIISGCVFWSVALACTNFPDLARILADLKLLRSDMGRTAMCAAIVTDLCTWVLLVFGFASFSKSGTWNKMMPFVIITTAIFVLLCIFVIRPGIAWIFAKTVKAGHVGDTHVWFILGGVVLCGLITDACGVHSITGAFLFGLSIPHDHIIRNMIEEKLHDFLSGILMPLFYIICGLRADIGFMLQFTDKFMMVVVICSSFLVKIVTTVITSLFMHIPMRDAFAIGALMNTKGTLSLVVLNAGRDTKALDSPMYTHMTIALLVMSLVVEPLLAFAYKPKKKLAHYKHRTVQKIKGETELRVLACVHVLPNVSGITNLLQVSNATKQSPLSVFAIHLVELTGRTTASLLIMNDECKPKANFSDRVRAESDQIAETFEAMEVNNDAMTVQTITAVSPYATMHEDICVLAEDKRVCFIILPYHKHLTPDGRMGEGNSSHAEINQNVLSHAPCSVGILVDRGMAMVRSESFRGESMKREVAMLFVGGPDDREALSYAWRMVGQHVIKLTVVRFVPGREALISSGKVAAEYEREKQVDDECIYEFNFKTMNDSSVKYIEKVVNDGQDTIATIREMEDNNSYDLYVVGRGYNSDSPVTAGLNDWSSSPELGTIGDTLASSNFTMHASVLVIQQYSATKRQAAVTAAAATTVMGAVAGVTGNNLESAGGDAKMTRDAHEPFMKSMYEDEDEDDEEDHQYGIHR | Function: Operates as a K(+)/H(+) antiporter or Na(+)/H(+) antiporter of the chloroplast envelope that functions in pH homeostasis and chloroplast development. Monovalent cation transporter with a preference for Cs(+), K(+) and Rb(+) relative to Na(+) or Li(+). Required for pollen tube guidance, but not for normal pollen development. May also be involved in the development or function of the female gametophyte.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95867
Sequence Length: 867
Subcellular Location: Plastid
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Q1HDT2 | MVRHFPINDQSLLPAHFGFWPGNSTTPGEVSNRVFSPKIPVVCRKLHSKQPFGMFKGENAMNYAFSTFLIEAIIIIFFIKVVSIALRPFRQPRIVSEIIGGMMIGPSMFGGIRNFNYYLFPPIANYICANIGLMGFFYFLFLTAAKTDVGAIGKAPRKHKYIAAIGVIVPIICVGSVGMAMRDQMDENLQKPSSIGGVVFALSFTSFPVIYTVLRDMNLLNSEVGKFAMSVALLGDMAGVYVIVIFEAMTHADVGGAYSVFWFLVSVVIFAAFMLLVVRRAFDWIVSQTPEGTLVNQNYIVMILMGVLASCFLTDMFGLSIAVGPIWLGLLVPHGPPLGSTLAVRSETFIYEFLMPFTYALVGQGTNIHFLRDETWRNQLSPLFYMTVVGFITKFLSTAFAALFFKVPARESITLGLMMNLRGQMDLLVYLHWIDKRIVGFPGYTVMVLHTVVVTAVTTPLINFFYDPTRPYRSSKHRTIQHTPQNTEMGLVLAVSDHETLSGLITFLDFAYPTKSSPLSIFAVQLVELAGRATPLFIDHEQRKEEEEEEYEEEEEEPERKQSGRIDQVQSAFKLYEEKRNECVTLRSYTAHAPKRLMYQDICELALGKKTAFILLPYQKERLEDAAPTELRDSGMLSVNADVLEHTPCSVCIYFDKGRLKNAVVRLSMDLQHSTNSIRMRQETYRFVVLFLGGADNREALHLADRMSTNPDVTLTVIRFLSYNHEGEDEREKKLDDGVVTWFWVKNESNERVSYKEVVVKNGAETLAAIQAMNVNDYDLWITGRREGINPKILEGLSTWSEDHQLGVIGDTVAASVFASEGSVLVVQQQVRNQKGGDGFLNGKFDYKRFLSPWSHSHN | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96681
Sequence Length: 859
Subcellular Location: Membrane
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Q9FGH6 | MVRSFPSDGWSALPTRFGFWPENPTTAGVVSSRVFSARLPEVCRQVHDKQPFGMFKGENGMNYTFSTFLIEAILIIFFIKIVYVLLRPLRQPRIVCEIIGGMMIGPSMLGRNRNFNYYLFPPIANYICANIGLMGFFYFFFLTAAKTDVAEIFKAPRKHKYIAAVSVLVPIACVGSTGAALKHKMDIRLQKPSSIGGVTFALGFTSFPVIYTVLRDMNLLNSEIGKFAMSVTLLGDMVGVYVLVLFEAMAQADGGGGAYSVIWFLISAAIMAACLLLVVKRSFEWIVAKTPEGGLVNQNYIVNILMGVLVSCFLTDMFGMAIAVGPIWLGLVVPHGPPLGSTLAIRSETFVNEFLMPFSFALVGQKTNVNLISKETWPKQISPLIYMSIVGFVTKFVSSTGAALFFKVPTRDSLTLGLMMNLRGQIDILLYLHWIDKQMVGLPGYSVMVLYAIVVTGVTAPLISFLYDPTRPYRSSKRRTIQHTPQNTETGLVLAVTDHDTFSGLITFLDFAYPTKTSPFSVFAIQLVELEGRAQPLFIAHDKKREEEYEEEEEPAERMGSRRVDQVQSAFKLYQEKRSECVTMHAYTAHASKHNMYQNICELALTKKTAFILLPYQKERLQDAALTELRDSGMLSVNADVLAHTPCSVCIYYEKGRLKNAMVRSSMDPQHTTNSSHMRQEMYRFVVLFLGGADNREALHLADRMTENPFINLTVIRFLAHNHEGEDEREKKLDDGVVTWFWVKNESNARVSYKEVVVKNGAETLAAIQAMNVNDYDLWITGRREGINPKILEGLSTWSEDHQLGVIGDTVAGSVFASEGSVLVVQQQVRNQMGGDGFLNGKFDYKKLVSPWSHSHN | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95833
Sequence Length: 857
Subcellular Location: Membrane
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Q9M008 | MNNSVTSNGTHEFVCEAWLGSSSGGLLRGDDPLKYSTPLLLLLISLVSSLSSVFQALLRPLANVDFVTQILAGIFLGPSALGQNIDLVKKLFNTRSYFIIESFEAISFMFISYISTAQVDMGVIKRGGKLAIINGLSLFLFPYVVGAIACTVITSNIRGTVAKNNPEQLHNLLTNQSVVYFQVAYSVLSNLKMLNSEPGRLALSSIMVANCFGWGFFLLLITFDSFLHQNYSKTTYLPTFTKVLLLVGIVVVCRPIFNWIVKRTPEGKKLKASHLCTICVMLCTATFLSETVGFPYVVGSVALGLVTPKTPPFGTGLTDKIGSFCYAVLMPCYVIGIGNKVDFFSFNLRDIISLEFLIFTISAAKFASIVLPSLYFQVPISHAVIVGFIVCIQGIYDVQIFKQLLNYKNISHEAFGIMVISAMVHSTIFTAIVKNLYGWVQRKHITYRRQTVQHYEPNKPLKILTCFYHRETVPPILTVLELSTCPSSASSHSIVSVNLEELEQNNVPLLIQHHPGHNDESSTSSSRRDQISKAFEKFRSGHDLQENVSVECFTAVAPSKTMHEDVCALAFEKETDLIIFGMADGTAAERRLCRNVRNASPSSVAVLMDQGRLPDFKNMGTAMKNGSMRINICSIFLGGADDRETLAFAVRMTNQPYVNLTVLKLVDGENVSHLNDVVEKRLDFRTIEKFRQDTMNKHNVALREVWIKEASDLVNLLREEGNNYDLIMVGIRHEKSFEVLQGLSVWSEIEELGEIGDLLVSRDLKLSASVLAVQQQLSSVVEEV | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87038
Sequence Length: 784
Subcellular Location: Membrane
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Q9M007 | MENITKTFQYGGVDWLCEPWVGAGSLGIGRGENPLKFALPLLLLQISVFSIFSVSFQFLLRPFGKFAFLTQMLAGICLGPSVIGRNKQYMATFFYARSVYIIESFEAICFLFICYITTCQVDTRMIKRVGKLAFINGILLFLIPFVWGQFAAILISKRLKSGPAGIPPVEFHHVAIVQSTMFFQVVYGVLSSLKMLNTEPGRLALASMMVHDCLSWCFFMLNIAIKLNVDLPNKNRAAFLSVLQMIMILVIAYVFRPLMLWMKNRTPEGHSLKASYLSVICVLLFISCLWAEFVGLPYFFGAVVLGLATPKRPPLGTGLSDKIGCFVWSVLMPCYVIGIGLNIDLSLFSWRDVIRFELLFGVVRFAKMIAIALPSLYYKVPLWHAILVGFIVNIQGLYDVQIYKQNFNYTKISSKSFGAMVMSATVNSTIFIVIVKKLYQTMSKRNPYKRRTVQHCRVEAPLRILTCFRNREAVRPVLDLVELSRPAIGSPLSVFAVNLEELNNHSLPLLIHHTQEISPFLVPSRRDQIVKAFHNFEKTNQETVLIECFTAVAPRKTMHEDVCAIAFDQETDIVILTLDAGIELWERLLCRNLLHNCPCSVALFIDRGRLPDFRFVPLKKLTINIGAIFLGGPDDREMLAYATRLASHPSVELQVFRLVDQNGVSPLRDMVERNHDMRVINVFRKENSEKNIIFREVRIEEAVNLLDLLRKEGDDFDLMMVGIRHEENLLMLEGLSEWSDMKELGEVGDVLISKDLELSVSVLAVQQ | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86991
Sequence Length: 767
Subcellular Location: Membrane
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Q8L709 | MNSTTTKNVCGDKWYLNLDRPEEALKILVFIAIFVVRTLLHYLMKPLGQPYLTTDFAIGLILGNIPRFRGAFSGPYSITLNNIIEFGMICHMFVMGLEMNPSVLLRPPTKDAFIAYTSMITTFVLAFVTTPFLHYTKTSPYIFSLALSLMASSTGSPILTRVIANLKIRKSDLGKLASAAGVHTDMISTLLYCFGFIFFPTEKPLARPLHRFFRALLMFCLFLAQVTFTSIVSPIFLNWVNNENPEGKPLKGSHLVMSLAFVVLICSFPTWPPESMYNPILSAFTAGLFLPNKGRMSKWIINKINYLLSTVFYPIFFFWVGFIIHMRNFDITDKMAWVRFFSLLGTVIAGKVTGTVLCGLLLGYHVPETASLGLLLTTKGHFHVYLAALAIRTNRVKSTTGALIIFIIVFTVVYSPFVVMDIIKRARKRVPVHIMALQWLDPTTELRILIGLHGPHNIGSTLNVMEICHGGREPGSIFYATDMVELTDEIAATLKKGGGAGQSNDSVTVTDRSVTEMRESITAAVNGYGELRNGQGVTVRRMLALSTFVTMAHDVCGLADELMVSIIILPFHKRLNPDGTLDAGHAGFRHVNRKILKNAPCSVGILVDRSFGQTEEAWRPGASMGIAIIFIGGRDDREALAFAAQVARHPAVKLKVIRFLEDKSSQNAQKRSSILNRASVVDQEEEMKLDDECFAEFYERYIAGGGRVSYMEKHLTNSSETFTALKSLDGEYGLVIVGRGGGRASSGLTTGLNDWQQCPELGPIGDVLSGSDFSHNTSMLIIQQQRTRGQLEGLHDDFTIL | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88710
Sequence Length: 801
Subcellular Location: Membrane
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Q9FYC1 | MEFNGDRIPYLRDTWRDANMICGILPINPSSSGLWPSPKLPDPQANIEFWNYMFPHVQIIFLIVTILWQFFHFFLRRLGMIRFTSHMLTGILLSKSFLKENTPARKFLSTEDYKETLFGLVGACSYMMFWFLMGVKMDLSLIRSTGRKAVAIGLSSVLLSITVCALIFFLILRDVGTKKGEPVMSFFEIIFIYLIQCLSSFPVIGNLLFELRLQNSELGRLAMSSAVISDFSTSILSAVLVFLKELKDDKSRLGSVFIGDVIVGNRPMKRAGTVVLFVCFAIYIFRPLMFFIIKRTPSGRPVKKFYIYAIIILVFGSAILADWCKQSIFIGPFILGLAVPHGPPLGSAILQKFESVVFGTFLPFFVATSAEEIDTSILQSWIDLKSIVILVSVSFIVKFALTTLPAFLYGMPAKDCIALSLIMSFKGIFEFGAYGYAYQRGTIRPVTFTVLSLYILLNSAVIPPLLKRIYDPSRMYAGYEKRNMLHMKPNSELRILSCIYKTDDIRPMINLLEATCPSRENPVATYVLHLMELVGQANPVLISHRLQTRKSENMSYNSENVVVSFEQFHNDFFGSVFVSTYTALSVPKMMHGDICMLALNNTTSLIILPFHQTWSADGSAIVSDSLMIRQLNKSVLDLSPCSVGIFVYRSSNGRRTIKETAANFSSYQVCMLFLGGKDDREALSLAKRMARDSRITITVVSLISSEQRANQATDWDRMLDLELLRDVKSNVLAGADIVFSEEVVNDANQTSQLLKSIANEYDLFIVGREKGRKSVFTEGLEEWSEFEELGIIGDLLTSQDLNCQASVLVIQQQQQMI | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92008
Sequence Length: 817
Subcellular Location: Membrane
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Q3EDG3 | MESRNEAYEGAYNATFWGDFSYHGYGFSEDGSKFCEQIPILVNSFGVWEKLDLPIRGMKIWDYSLPHLESVIVLVLCLWQFFYLSLKKIGLPVPKITSMMIAGAALSQTNLLPNDWTIQHILFPDDTRPKVPETLGGFAFVFYWFIEGVKMDVGMVRKTGTKVIVTGIATVILPIIAANMVFGKLRETGGKYLTGMEYRTILFMQSISAFTGISRLLRDLRINHSEFGRIVISTAMVADGTGFGVNLFALVAWMDWRVSALQGVGIIGYVIFMVWVVRPAMFWVIKRTPQERPVKECFIYIILILAFGGYYFLKEIHMFPAVGPFLLGLCVPHGPPLGSQLVEKFESFNTGILLPLFLFFSMLQIDGPWLANQIGQLRHFDGQLYEALTIIIVVFVAKIIFSMIPALLAKMPLTDSFVMALILSNKGIVELCYFLYGVESNVLHVKSFTIMATMILVSSTISPVLIHYLYDSSKRFISFQKRNLMSLKLGSELKFLVCIHKADHISGMINLLAQSFPLHESTISCYVIHLVELVGLDNPVFISHQMQKAEPGNRSYSNNVLIAFDNFKHYWKSISLELFTCISNPRYMHQEIYSLALDKQASFLMLPFHIIWSLDQTTVVSDDVMRRNANLNVLRQAPCSVGIFVHRQKLLSAQKSSPSFEVCAIFVGGKDDREALALGRQMMRNPNVNLTVLKLIPAKMDGMTTGWDQMLDSAEVKEVLRNNNNTVGQHSFVEYVEETVNDGSDTSTLLLSIANSFDLFVVGRSAGVGTDVVSALSEWTEFDELGVIGDLLVSQDFPRRGSVLVVQQQQNVACR | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91606
Sequence Length: 815
Subcellular Location: Membrane
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Q8GX92 | MATEEIDMSYWDVSWGEFNEDKNSSIFCESHPHIVNSHGIWEVMTFKRGMNFWEYPLPNLEILIFSTFFIWRLLDISFNKIGLRVPRFTYMMIAGIILGQTCHFSNKSWIHDIFFPDDNRPKVAETLGAFGFVLYWFLKGVTMDAELPFRTEKRSSVIGFITVIIPLICGSLTFRYRERRGDSSILRMEYRLIIFLQSISAFTSIDTLLKDLQIKHSEFGRIALSGAMVTDMLAFGVTFFNAIYYEKLYGFMQTVGFCLFVVVMICVVRPAMYWVIKQTPEGRPVKDFYLYSIFGIAFACFTFFNKVIHLFGPAGSFVFGLTVPNGYPLGTTLIQKFESFNLGSILPLFGSLTMMQVDLLRLFKESGDLIRMEGQIYEVISFILLVNTTKFVVTTITAYAFKMPLRDSFALALVLSNKGIFELAYYTYAVELKLIRPEVFTILAAYTLLNSIFIPMLLELVHDPTKRFRCYRKRNLGILKDGAALQCLMCVYRPDHITSMTDLLETFSPSQDSPMACNILHLVELVGQANPMFISHQLQKPEPGSTSLSDNVIISFRGFQRQFFEYTSLDIFTSVSVSQHMHEDICWLALSRSLSLIVLPFHRTWSVDRSTVISNDDNLRMLNVNVLRRAPCSVGIFVYRKPIVESHMAKSHSKICLIFNGGKDDREALAITNRMRLTEKRTRLTIIRFIPKSSEMDNDEWEQQQSINLKESVTSIVGSNIKENDAKVTYIDKAVSDGSETSRILRAMANDYDLFIVGSGSGIGTEATSGISEWTEFNELGPIGDLLASHEYPSSASVLVVQKQVYIHHTKSQRRKSF | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93395
Sequence Length: 818
Subcellular Location: Membrane
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P0CG16 | MDAENATWRKEFMWNNDEKRAEMGTKMFCDVSPHIMLNSHGVAEKMASGSKGMDFWEYPLPQLEIIILSIFLLWRLFDMLFKKLGVPIPKFTSMMLVGAVLSEMFGSMQIPCLKHIFIHYNQYMTKVPDTIGAFAFVLDWFLRGVTTDVGIMKKSGTKSVVIGITSMIIPWQIGKLLYSSREKSSILTMTEMEYTVMTFTMSMTPFTCVNMLLTDLKIVHTDFGQIAQSAGMVTDLLAFFLTVSAYVSRDETQGVKMGLAFMAFFIFVYLVRQFMLWVIRHTPEGAPVKNVYLYIGLLLAYLSYLYWSRFLFFGPLGAFALGLAVPNGPPLGSVFIQKFDSFNEGIFLPLFGSLSMIKLDWSFLRKEFGNGRHLHGHMYECFSFLPIVYIAKFATSFLAALATKIPLRDSIILGVIMGTKSSFELGYVLTAFEKDRISLEVLSLLGVYILVNSLLTPMAIHFLYDRSKRFVCYGRRNLKEKPEMQTLVCINKPDNITSMISLLRATSPSKDSPMECCVLHLIELLGQATPTFISHQLQKPKPGSRSYSENVISSFQLFQEVYWDSASINMFTSLTSAKEMHEQICWFALSQGSNLILLSFHRTWEPNGNVIISDDQTLRSLNLNVLKRAPCSVGIFVYRKPIWQTKALESPCRVCLIYVGGNDDKEALALADHMRGNQQVILTVLRLIPTSYADESSLRIHSQMVDMNRHEDQRPGDKSTIIDWTVGDGTETSKILHSVSYDYDLFIVGRRSGVGTTVTRGLGDWMEFEELGVIGDLLASEYFPSRASVLVVQQQE | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90112
Sequence Length: 796
Subcellular Location: Membrane
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Q9ZUV9 | MDPFNASWWTNMAWHGYSLSEDGTKFCEMLPTKINSFGLSEKILHKSVGLYFWEYPLPNLELIILSVFFFWQFFEILFKMSNIPIPKMPSMMLGCVVINLFSYTRPGSLLHRMFFPDDGRPKVAETGGAFGFVMYWFLKGVSIDVGMLRKTEPRAALIGFNTLVIPYISGYILMRTRKHFGKLAMTELQYQEIILLQSLSSFAGVNGLLTDLKINHSEFGRMVQSCAAVTDLVIFIMVSGTVLLKGQKGLPHGIVIVLVIGFLVYIVWPVMLWIIKQTPEGRLVKDVYIYLVMATAYFVYMFWLNFFQFSTYGWFIIGLATPAGPPLGSALIQRFECFNVGVLLPLFGSLSMEQLDISWLMREILNLKHMEGFAYEAISVILIVTVVKFVVTAITAFAVRIPYRDSIVLAMVLSNRSIFELGYLGYIVELKMFDNKSFTIAALSVLVSSLLTPIAIEFMYEPQHIFSSYRDRNMLTLKHDSKLKTLVCIHKPDHITSMVNFVELFNPTQESKLECNVLHLVELIGQAIPTFISHKMQKPKVGTRSCSRNVITAFLSLRRHLTKEAISIDIFTSASLVEHMHEDLCWLALDKNVALVVLPFHRSWSVDRSTIVSDDKAMQNLNHKVLKRASCSVGIFVYRKPLWESQMHGSCYKVCAIVVGGKDDKEALAFTNRMRRNKQTSVTILHLIPQLTTEESEDSVQKLDYDDIKEIMKTEDSNENDSWICIEKSVKEGAETSVILRSIAYDYDLFIVGRSSGMNSAVTKGLNEWTEFEELGALGDVIASKEFPSRASVLVLQQQQY | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90990
Sequence Length: 801
Subcellular Location: Membrane
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Q58P71 | MGGGDISHMSPEVKWIFEMAWYGETVRYDGLICEEHPPKLSSDGIWEKLIIKSAGLYFWQYRLPKLEIVILLVFFLWQGFNILFKKLGLSIPKLSSMMLAGLLLNVLVTLSGENSIIADILVTKNRIDVAGCLGSFGFLIFWFLKGVRMDVKRIFKAEAKARVTGVAAVTFPIVVGFLLFNLKSAKNRPLTFQEYDVMLLMESITSFSGIARLLRDLGMNHSSIGRVALSSALVSDIVGLLLLIANVSRSSATLADGLAILTEITLFLVIAFAVVRPIMFKIIKRKGEGRPIEDKYIHGVLVLVCLSCMYWEDLSQFPPLGAFFLGLAIPNGPPIGSALVERLESFNFGIILPLFLTAVMLRTDTTAWKGALTFFSGDDKKFAVASLVLLIFLLKLSVSVIVPYLYKMPLRDSIILALIMSHKGIIELSFYLFSLSLKLVTKDTFSILVLSIVLNSLLIPMAIGFLYDPSKQFICYQKRNLASMKNMGELKTLVCIHRPDHISSMINLLEASYQSEDSPLTCYVLHLVELRGQDVPTLISHKVQKLGVGAGNKYSENVILSFEHFHRSVCSSISIDTFTCIANANHMQDDICWLALDKAVTLIILPFHRTWSLDRTSIVSDVEAIRFLNVNVLKQAPCSVGILIERHLVNKKQEPHESLKVCVIFVGGKDDREALAFAKRMARQENVTLTVLRLLASGKSKDATGWDQMLDTVELRELIKSNNAGMVKEETSTIYLEQEILDGADTSMLLRSMAFDYDLFVVGRTCGENHEATKGIENWCEFEELGVIGDFLASPDFPSKTSVLVVQQQRTVANNN | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90956
Sequence Length: 816
Subcellular Location: Membrane
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Q9FFB7 | MTDSQALVPGPSPPHSKAEICYGATFFNISSYGIMEKYETPTVIFGYALPLLELQIILIFVCIVLSHMFLRRIGIPRFVSNILAGLILGPQLLDLLEYSSDRLSLDIPGNVALEGVARLGLVMFTFLMGVKTNKRAVYQIGKRPIVIAVSSFFVTMISGLAFRNFRLDKVDPLYMPLRLAPTERSVIVSIQAVTLLPVITHLVYELKMSNSELGRIAISTAAVSDFLGFLTLVCISYVGTYRYVSPGIANRDIVALIILVLVILFIFKPMAQRIVDMTPEGKPVPKVYLYVTILTAIAASIYLSVFNQMYILGALLVGLAIPDGPPLGSALEARFESLVTNIFFPISIAVMAMKADVVRALYSFDDISFNILLLGLTVVVKWTASFVPCLIFCELPTRESVIIATIMNYKGFVDLCFFDVALRRRNLSRATYTVMIIYVLLNAGILPTIIKALYDPKRKYIGYVKRDIMHLKTNSDLKILTCLHKPDNISGAISLLELLSSPLNNDNKDRGVIAVTALHLVKLAGRTFPILIPHDKRSKARLLQNSYIQTMMLAFTEFQQENWESTTVSSFTAYSHENLMDQDICNLALDHLTSMIIVPSGRKWSPDGEYESDDIMIRRVNESLLDLAPCSVGILNYRGYNKGKKKTNSIINVGVIFIGGKDDREALSLAKWMGQNSRVCLTVIRFLSGQELDKSKNWDYLVDDEVLNDLKATYSLANNFNYMEKVVNGGPAVATTVRLVAEDHDLMIVGRDHEDYSLDLTGLAQWMELPELGVIGDLLASKDLRARVSVLVVQQQQQHG | Function: May operate as a cation/H(+) antiporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89060
Sequence Length: 800
Subcellular Location: Membrane
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Q5EK40 | MYLTFYLEKVMKKMLLIAGATVISSMAHPTFAVEDELNIFDECRSPCSLTPEPGKPIQSKLSIPSDVVLDEGVLYYSMTINDEQNDIKDEDKGESIITIGEFATVRATRHYVNQDAPFGVIHLDITTENGTKTYSYNRKEGEFAINWLVPIGEDSPASIKISVDELDQQRNIIEVPKLYSIDLDNQTLEQWKTQGNVSFSVTRPEHNIAISWPSVSYKAAQKEGSRHKRWAHWHTGLALCWLVPMDAIYNYITQQNCTLGDNWFGGSYETVAGTPKVITVKQGIEQKPVEQRIHFSKGNAMSALAAHRVCGVPLETLARSRKPRDLTDDLSCAYQAQNIVSLFVATRILFSHLDSVFTLNLDEQEPEVAERLSDLRRINENNPGMVTQVLTVARQIYNDYVTHHPGLTPEQTSAGAQAADILSLFCPDADKSCVASNNDQANINIESRSGRSYLPENRAVITPQGVTNWTYQELEATHQALTREGYVFVGYHGTNHVAAQTIVNRIAPVPRGNNTENEEKWGGLYVATHAEVAHGYARIKEGTGEYGLPTRAERDARGVMLRVYIPRASLERFYRTNTPLENAEEHITQVIGHSLPLRNEAFTGPESAGGEDETVIGWDMAIHAVAIPSTIPGNAYEELAIDEEAVAKEQSISTKPPYKERKDELK | Function: An NAD-dependent ADP-ribosyltransferase (ADPRT), it catalyzes the transfer of the ADP-ribosyl moiety of oxidized NAD onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. It probably uses the eukaryotic prolow-density lipoprotein receptor-related protein 1 (LRP1) to enter mouse cells, although there seems to be at least one other receptor as well. Is active against mouse fibroblasts, Chinese hamster ovary eEF-2, brine shrimp (Artemia spp. nauplii) and upon expression in S.cerevisiae.
PTM: Probably requires further proteolytic processing to generate a fragment with toxic activity.
Catalytic Activity: diphthamide-[translation elongation factor 2] + NAD(+) = H(+) + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2] + nicotinamide
Sequence Mass (Da): 74293
Sequence Length: 666
EC: 2.4.2.36
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Q5HL70 | MEKAKFVIKLILQLALIMLITFIGTEVQKLLHIPLAGSIVGLMLFFLLLQFKIVPESWINVGADFLLKTMVFFFIPSVVGIMDVASNITMNYILFFIVIIIGTCLVALSSGYIAEKMLEKSNTRKGTDHS | Function: Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14514
Sequence Length: 130
Subcellular Location: Cell membrane
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P60639 | MNDYVQALLMILLTVVLYYFAKRLQQKYPNPFLNPALIASLGIIFVLLIFGISYNGYMKGGSWINHILNATVVCLAYPLYKNREKIKDNVSIIFASVLTGVMLNFMLVFLTLKAFGYSKDVIVTLLPRSITAAVGIEVSHELGGTDTMTVLFIITTGLIGSILGSMLLRFGRFESSIAKGLTYGNASHAFGTAKALEMDIESGAFSSIGMILTAVISSVLIPVLILLFY | Function: Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25012
Sequence Length: 229
Subcellular Location: Cell membrane
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A3B529 | MEERSVLMERYVIGRQLGQGTFGKVYYARNLSSGQSVAIKMIDKEKILKVGLMEQIKREISIMRLVRHPNVLQLFEVMATKSNIYFALEYAKGGELFHKMARAKLNEESARNYFQQLISAMDYCHSRGVYHRDLKPENLLLDENETLKVSDFGLSALAESRRQDGLLHTACGTPAYVAPEVLSRKGYSGSKADVWSCGVILFVLVANYLPFHDRNIIQMYRKIAKAEYRCPRHFSAELKELLYGILDPDPSTRMSISRIKRSAWYRKPIAISALNNETGKKSCTSEAPFSGPTICISSERNQEPPNLHNLNAFDIISLSTGFDLSGLFGERYGRRESLFTSRKPAAAVLVKLKELAKALNLKVTKTDNGVLKLATTKEGRKGRLELDAEVSEVAPFLLVELKKTNGDTLEYQRMMKEDIRPSLKDIIWTWQGDQQ | Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 49331
Sequence Length: 435
Domain: The activation loop within the kinase domain is the target of phosphorylation/activation by upstream protein kinases. The PPI motif mediates the interaction with the ABI (abscisic acid-insensitive) phosphatases (By similarity).
EC: 2.7.11.1
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Q7XIW5 | MPPSTGSVPPAASTPAAGDEATAAGRVLLGRYELGGLLGRGASAKVYLARDLLTGRDVAIKSFPNPRHGGGLRGGEEDVLLRPAPIEREAAILPRLRHRHVMRLREILATRKKVHFVLDLAAGGELFSLLDASGRMTEDLARHYFRQLISAVRYCHSRGVYHRDIKPENLLLDDAGDLKVADFGLGAVADGALHHTLCGTPAYVAPEILSRKGYNPAKVDIWSCGVVLFVLAAGYLPFNDASLVNMYRKIYAGKFRCPAWFSPELRCLVRRILDPNPATRIDTEEIITHPWFRQDASHFAMAQLMQHGHDEEAKFKTEFKEDDMARDMTAFDILACSPGSDLSGLFGAEPGKERVFVGEPAAAVLSRVEEAGKKEGYMVTREGKKGTGPVYVKGENGGIVAKVCVFKIADAVSVVEVVKGYGAEAARFWKARLEPAMKPPAAI | Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48213
Sequence Length: 443
Domain: The activation loop within the kinase domain is the target of phosphorylation/activation by upstream protein kinases. The PPI motif mediates the interaction with the ABI (abscisic acid-insensitive) phosphatases (By similarity).
EC: 2.7.11.1
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Q5JLQ9 | MAMETTSQDSQVIMGRYKLGRLLGRGTFAKVYKAYKLATGEAVAIKVFDKEAVQRSGTVEQVKREVDVMRRVHHRHVIRLHEVMATRSRIYFVMEYASGGELFTRLSRSPRFPEPVARRYFQQLITAVEFCHSRGVYHRDLKPENLLLDARGDLKVTDFGLSALDGGLRGDGLLHTTCGTPAYVAPEVLLKRGYDGAKADIWSCGVILFVLLAGYLPFNETNLVILYRNITESNYRCPPWFSVEARKLLARLLDPNPKTRITISKIMDRPWFQQATCPLGDMSLVASAPSVLLARKEASQQHDDEEDDGFAREKKKRSNVIMSSPVIDVRPSSMNAFDIISRSRGLDLSKMFDAEERRSEARFSTRETTTAIVSKLEEIAEAGRFSFKLKEKGRVELEGSQDGRKGALAIEAEIFKVAPEVHVVEVRKTGGDSPDFRDFYKQELKPSLGDMVWAWQGGDSPPLVPAAGRRPITKRS | Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 53563
Sequence Length: 476
Domain: The activation loop within the kinase domain is the target of phosphorylation/activation by upstream protein kinases. The PPI motif mediates the interaction with the ABI (abscisic acid-insensitive) phosphatases (By similarity).
EC: 2.7.11.1
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Q6X4A2 | MYRAKRAALSPKVKRRVGKYELGRTIGEGTFAKVRFAKNTENDEPVAIKILDKEKVQKHRLVEQIRREICTMKLVKHPNVVRLFEVMGSKARIFIVLEYVTGGELFEIIATNGRLKEEEARKYFQQLINAVDYCHSRGVYHRDLKLENLLLDASGNLKVSDFGLSALTEQVKADGLLHTTCGTPNYVAPEVIEDRGYDGAAADIWSCGVILYVLLAGFLPFEDDNIIALYKKISEAQFTCPSWFSTGAKKLITRILDPNPTTRITISQILEDPWFKKGYKPPVFDEKYETSFDDVDAAFGDSEDRHVKEETEDQPTSMNAFELISLNQALNLDNLFEAKKEYKRETRFTSQCPPKEIITKIEEAAKPLGFDIQKKNYKMRMENLKAGRKGNLNVATEVFQVAPSLHVVELKKAKGDTLEFQKFYRTLSTQLKDVVWKCDGEVEGNGAAA | Function: Involved in cold stress tolerance. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 50954
Sequence Length: 449
Domain: The activation loop within the kinase domain is the target of phosphorylation/activation by upstream protein kinases (By similarity). The N-terminal region containing the kinase domain is responsible for the autophosphorylation.
EC: 2.7.11.1
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Q86X95 | MGKSFANFMCKKDFHPASKSNIKKVWMAEQKISYDKKKQEELMQQYLKEQESYDNRLLMGDERVKNGLNFMYEAPPGAKKENKEKEETEGETEYKFEWQKGAPREKYAKDDMNIRDQPFGIQVRNVRCIKCHKWGHVNTDRECPLFGLSGINASSVPTDGSGPSMHPSELIAEMRNSGFALKRNVLGRNLTANDPSQEYVASEGEEDPEVEFLKSLTTKQKQKLLRKLDRLEKKKKKKDRKKKKFQKSRSKHKKHKSSSSSSSSSSSSSSTETSESSSESESNNKEKKIQRKKRKKNKCSGHNNSDSEEKDKSKKRKLHEELSSSHHNREKAKEKPRFLKHESSREDSKWSHSDSDKKSRTHKHSPEKRGSERKEGSSRSHGREERSRRSRSRSPGSYKQRETRKRAQRNPGEEQSRRNDSRSHGTDLYRGEKMYREHPGGTHTKVTQRE | Function: May modulate splice site selection during alternative splicing of pre-mRNAs (By similarity). Regulates transcription and acts as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC). Required for RBPJ-mediated repression of transcription.
PTM: Phosphorylated by NEK6.
Sequence Mass (Da): 52313
Sequence Length: 450
Subcellular Location: Nucleus speckle
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Q9DA19 | MGKSFANFMCKKDFHPASKSNIKKVWMAEQKISYDKKKQEELMQQYLKEQESYDNRLLMGDERVKNGLNFMYEAPPGVKKENKEKEETEGETEYKFEWQKGAPREKYAKDDMNIRDQPFGIQVRNVRCIKCHKWGHVNTDRECPLFGLSGINASSVPTDGSGPSMHPSELIAEMRNSGFALKRNVLGRNLTANDPSQDYVASDCEEDPEVEFLKSLTTKQKQKLLRKLDRLEKKKKKKKSDKKKKKLQKSKNKHKKRKNKSPSSSSSSSSSSSSSSSSSSSSSSSSETSDSSSESDNKEKKREKEKRKKKKKTKCSESKSSDCKEDKPKNMLYEELSSSHSDRGKAQEKLRFPKQESSGENSMWVHSASDRTSRSHRHSPEKKGSDRNRGIRSRSRSRAESSRRSRSRSPYRQKHREVRSRPHRSPSEEQKGRKGTRSHGEGDHRREHVR | Function: Regulates transcription and acts as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC). Required for RBPJ-mediated repression of transcription (By similarity). May modulate splice site selection during alternative splicing of pre-mRNAs.
PTM: Phosphorylated by NEK6.
Sequence Mass (Da): 51838
Sequence Length: 450
Subcellular Location: Nucleus speckle
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P17315 | MFRLNPFVRVGLCLSAISCAWPVLAVDDDGETMVVTASSVEQNLKDAPASISVITQEDLQRKPVQNLKDVLKEVPGVQLTNEGDNRKGVSIRGLDSSYTLILVDGKRVNSRNAVFRHNDFDLNWIPVDSIERIEVVRGPMSSLYGSDALGGVVNIITKKIGQKWSGTVTVDTTIQEHRDRGDTYNGQFFTSGPLIDGVLGMKAYGSLAKREKDDPQNSTTTDTGETPRIEGFSSRDGNVEFAWTPNQNHDFTAGYGFDRQDRDSDSLDKNRLERQNYSVSHNGRWDYGTSELKYYGEKVENKNPGNSSPITSESNTVDGKYTLPLTAINQFLTVGGEWRHDKLSDAVNLTGGTSSKTSASQYALFVEDEWRIFEPLALTTGVRMDDHETYGEHWSPRAYLVYNATDTVTVKGGWATAFKAPSLLQLSPDWTSNSCRGACKIVGSPDLKPETSESWELGLYYMGEEGWLEGVESSVTVFRNDVKDRISISRTSDVNAAPGYQNFVGFETGANGRRIPVFSYYNVNKARIQGVETELKIPFNDEWKLSINYTYNDGRDVSNGENKPLSDLPFHTANGTLDWKPLALEDWSFYVSGHYTGQKRADSATAKTPGGYTIWNTGAAWQVTKDVKLRAGVLNLGDKDLSRDDYSYNEDGRRYFMAVDYRF | Function: Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73896
Sequence Length: 663
Subcellular Location: Cell outer membrane
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Q9DED4 | MSDEGKLFIGGLNFDTNEESLEQVFSKYGQISEVVVVKDRETKRSRGFGFVTFENPDDAKDAMMAMNGKAVDGRQIRVDQAGKSSGDRRGGYRGGSSGGRGFFRGGRGRGGGDRGYGSSRFDNRSGGYGGSSGSRDYYSSGRSQGSYGDRAGGSYRDSYDSYATHE | Function: Cold-inducible mRNA binding protein. Acts cooperatively with elavl1/elrA to stabilize AU-rich element (ARE)-containing mRNAs by binding to them and inhibiting their deadenylation. Essential for embryonic gastrulation and neural development, acting to maintain the expression of a set of adhesion molecules, and cell movement during embryogenesis. Required for pronephros development.
PTM: Methylated on arginine residues within RGG motifs. Methylation by prmt1 promotes cytoplasmic accumulation.
Sequence Mass (Da): 17855
Sequence Length: 166
Domain: The glycine-rich domain, which contains a number of RGG motifs, is necessary to regulate nucleocytoplasmic localization.
Subcellular Location: Nucleus
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Q14011 | MASDEGKLFVGGLSFDTNEQSLEQVFSKYGQISEVVVVKDRETQRSRGFGFVTFENIDDAKDAMMAMNGKSVDGRQIRVDQAGKSSDNRSRGYRGGSAGGRGFFRGGRGRGRGFSRGGGDRGYGGNRFESRSGGYGGSRDYYSSRSQSGGYSDRSSGGSYRDSYDSYATHNE | Function: Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Acts as a translational activator. Seems to play an essential role in cold-induced suppression of cell proliferation. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a translational repressor (By similarity). Promotes assembly of stress granules (SGs), when overexpressed.
PTM: Methylated on arginine residues. Methylation of the RGG motifs is a prerequisite for recruitment into SGs (By similarity).
Sequence Mass (Da): 18648
Sequence Length: 172
Domain: Both the RRM domain and the arginine, glycine (RGG) rich domain are necessary for binding to the TXN 3'-untranslated region. Both the RRM domain and the arginine, glycine (RGG) rich domain (RGG repeats) are necessary for optimal recruitment into SGs upon cellular stress. The C-terminal domain containing RGG repeats is necessary for translational repression (By similarity).
Subcellular Location: Nucleus
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P45410 | MTLILKRVQLLKDKPRREAIDRFLRQHQLSLEADCEMAIIAEYQQRLVGCGAIAGNVLKCIAIDPSLQGEGLSLKLLTELLTLAYELGRSELFLFTKPCNAALFSGAGFWPIAQAGDRAVLMENSRERLTRYCRQLAMYRQPGRKIGAIVMNANPFTLGHRWLVEQAASQCDWLHLFVVKEDASCFSYHDRFKLIEQGITGIDKVTLHPGSAYLISRATFPGYFLKEQGVVDDCHSQIDLQLFRERLAPALQITHRFVGTEPLCPLTRNYNQRMKSLLEAPGDAPPIEVVELARIEKNGGPVSASRVRELYRQRNWQAVAALVPPGTLSFLMQLAESEHQTA | Function: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
Catalytic Activity: acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate lyase ACP] + AMP + diphosphate
Sequence Mass (Da): 38477
Sequence Length: 342
EC: 6.2.1.22
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O53076 | MRRDWQNFLMACGIKNFDDSELNPLDITIAVYENEEIIGTGSIAGDVIKYVAVQETTMSGHSTLFNQLMTKLENFMAVEGRFHQFVLRNQFTKKVLNTLASKRWLSVNKEFCWKKDYQILRNTCQQFPSQTPIDKVASVVINANPFTNGHRFLIEEASRNNELVYVFVLNQEASLFHTDERIALVKAGVQDLSNVIVVNGGAYIISYLTFPAYFLKHNDSAIDYQTTIDVRLFKYKIASALGITSRYVGSEPLSHTTNLYNQKLISELNPQIEVHVIQRKLAAGDLGVISARTVREAIDKGDEAVWQKMVTETTQHFISNNLLELQQRIRKGQKINGN | Function: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
Catalytic Activity: acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate lyase ACP] + AMP + diphosphate
Sequence Mass (Da): 38460
Sequence Length: 338
EC: 6.2.1.22
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A0A142PTM2 | MATVKVIDFIQTPFDFLIVGGGTAGLVLAARLSEEPGIQVGVIEAGSLRLGDPKVDLPTGPGQMLGDPGYDWNFESIPQAGANAKAYHIPRGRMLGGSSGINFMSYNRPSAEDIDDWANKLGVKGWTWSELLPYFKRSENLEPIEPSASCPVSPKVHGTGGPIHTSIGPWQAPIEESLLAAFDEAARLQRPAEPYSGAHLGFYRSLFTLDRTSTPVRSYAVSGYYAPVMGRPNLKVLENAQVCRILLSDASDGIPVAEGVELHHAGARYAVSARREVILSAGSVQSPQLLELSGIGDPSVLEGAGIACRVANTDVGSNLQEHTMSAVSYECADGIMSVDSLFKDPALLEEHQSLYAKNHSGALSGSVSLMGFTPYSSLSTETQVDATMARIFDAPSVSGRLSQQNASYQRRQQEAVAARMQNRWSADIQFIGTPAYFNTAAGYASCAKIMSGPPVGYSACYSIVVSNMYPLSRGSVHVRTSNPMDAPAIDPGFLSHPVDVDVLAAGIVFADRVFRSTLLNGKVRRRVSPPAGLDLSNMDEARQFVRNHIVPYHHALGTCAMGQVVDEKLRVKGVRRLRVVDASVMPMQVSAAIMATVYAIAERASDIIKKDCGFGRRLRAHI | Function: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III . The pathway begins with the synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT) from successive condensations of 4 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit . Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain . Mp11 collaborates with pksCT by catalyzing the hydrolysis of ACP-bound acyl intermediates to free the ACP from stalled intermediates (By similarity). Mpl2 then catalyzes the oxidation of the C-12 methyl of the ketone intermediate to an alcohol intermediate which is further oxidized by the oxidoreductase mpl7 to produce a bisaldehyde intermediate . The fourth catalytic step is catalyzed by the mpl4 aldehyde dehydrogenase . The final transformation is the reduction of C-3 by mpl6 to provide the chemically stable citrinin nucleus .
Sequence Mass (Da): 66811
Sequence Length: 622
Pathway: Mycotoxin biosynthesis.
EC: 1.1.-.-
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P55069 | MLAILGFLMMLVFMALIMTKRLSVLTALVLTPIVFALIAGFGFTEVGDMMISGIQQVAPTAVMIMFAILYFGIMIDTGLFDPMVGKILSMVKGDPLKIVVGTAVLTMLVALDGDGSTTYMITTSAMLPLYLLLGIRPIILAGIAGVGMGIMNTIPWGGATPRAASALGVDPAELTGPMIPVIASGMLCMVAVAYVLGKAERKRLGVIELKQPANANEPAAAVEDEWKRPKLWWFNLLLTLSLIGCLVSGKVSLTVLFVIAFCIALIVNYPNLEHQRQRIAAHSSNVLAIGSMIFAAGVFTGILTGTKMVDEMAISLVSMIPEQMGGLIPAIVALTSGIFTFLMPNDAYFYGVLPILSETAVAYGVDKVEIARASIIGQPIHMLSPLVPSTHLLVGLVGVSIDDHQKFALKWAVLAVIVMTAIALLIGAISISV | Function: Proton motive force-driven secondary transporter that mediates the transport of citrate complexed to Mg(2+). Cotransports at least two protons per Mg(2+)-citrate complex. Can also transport citrate in complex with Ni(2+), Mn(2+), Co(2+), and Zn(2+).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45830
Sequence Length: 433
Subcellular Location: Cell membrane
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P31602 | MTNMSQPPATEKKGVSDLLGFKIFGMPLPLYAFALITLLLSHFYNALPTDIVGGFAIMFIIGAIFGEIGKRLPIFNKYIGGAPVMIFLVAAYFVYAGIFTQKEIDAISNVMDKSNFLNLFIAVLITGAILSVNRRLLLKSLLGYIPTILMGIVGASIFGIAIGLVFGIPVDRIMMLYVLPIMGGGNGAGAVPLSEIYHSVTGRSREEYYSTAIAILTIANIFAIVFAAVLDIIGKKHTWLSGEGELVRKASFKVEEDEKTGQITHRETAVGLVLSTTCFLLAYVVAKKILPSIGGVAIHYFAWMVLIVAALNASGLCSPEIKAGAKRLSDFFSKQLLWVLMVGVGVCYTDLQEIINAITFANVVIAAIIVIGAVLGAAIGGWLMGFFPIESAITAGLCMANRGGSGDLEVLSACNRMNLISYAQISSRLGGGIVLVIASIVFGMMI | Function: Uptake of citrate across the boundary membrane with the concomitant uptake of a sodium ion (symport system).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47558
Sequence Length: 446
Subcellular Location: Cell membrane
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P21608 | MMNHPHSSHIGTTNVKEEIGKLDRIRISGIGLIAYAFMAVLLIIAISTKTLPNTMIGAIFALVLMGHVFYYLGAHLPIFRSYLGGGSVFTILLTAILVATNVIPKYVVTTASGFINGMDFLGLYIVSLIASSLFKMDRKMLLKAAVRFLPVAFISMALTAVVIGIVGVIIGVGFNYAILYIAMPIMAGGVGAGIVPLSGIYAHAMGVGSAGILSKLFPTVILGNLLAIISAGLISRIFKDSKGNGHGEILRGEREKSAAAEEIKPDYVQLGVGLIIAVMFFMIGTMLNKVFPGINAYAFIILSIVLTKAFGLLPKYYEDSVIMFGQVIVKNMTHALLAGVGLSLLDMHVLLAALSWQFVVLCLVSIVAISLISATLGKLFGLYPVEAAITAGLANNSMGGTGNVAVLAASERMNLIAFAQMGNRIGGALILVVAGILVTFMK | Function: Uptake of citrate across the boundary membrane with the concomitant uptake of a sodium ion (symport system).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46629
Sequence Length: 442
Subcellular Location: Cell membrane
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Q07065 | MPSAKQRGSKGGHGAASPSEKGAHPSGGADDVAKKPPPAPQQPPPPPAPHPQQHPQQHPQNQAHGKGGHRGGGGGGGKSSSSSSASAAAAAAAASSSASCSRRLGRALNFLFYLALVAAAAFSGWCVHHVLEEVQQVRRSHQDFSRQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASLEESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKSDSHGPKEDGGFRHSEAFEALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQRLAALQGRLEGLGSSEADQDGLASTVRSLGETQLVLYGDVEELKRSVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPPQDFLDRLSSLDNLKASVSQVEADLKMLRTAVDSLVAYSVKIETNENNLESAKGLLDDLRNDLDRLFVKVEKIHEKV | Function: Mediates the anchoring of the endoplasmic reticulum to microtubules.
PTM: Reversibly palmitoylated. Palmitoylation at Cys-100 by ZDHHC2 is required for its trafficking from the ER to the plasma membrane and for its perinuclear localization. Palmitoylation by ZDHHC2 is also required for its function in APF-mediated antiproliferative signaling .
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 66022
Sequence Length: 602
Subcellular Location: Endoplasmic reticulum membrane
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P25859 | MEKYEKLEKVGEGTYGKVYKAMEKGTGKLVALKKTRLEMDEEGIPPTALREISLLQMLSTSIYVVRLLCVEHVHQPSTKSQSTKSNLYLVFEYLDTDLKKFIDSYRKGPNPKPLEPFLIQKLMFQLCKGVAHCHSHGVLHRDLKPQNLLLVKDKELLKIADLGLGRAFTVPLKSYTHEIVTLWYRAPEVLLGSTHYSTGVDMWSVGCIFAEMVRRQALFPGDSEFQQLLHIFRLLGTPTEQQWPGVSTLRDWHVYPKWEPQDLTLAVPSLSPQGVDLLTKMLKYNPAERISAKTALDHPYFDSLDKSQF | Function: May control G2/M (mitosis) phase progression. Plays a role in regulating seedling growth in darkness via regulation of hypocotyl cell elongation and cotyledon cell development. Plays a role in stomatal development. Required to suppress endoreduplication. Together with CDKB1-2, promotes both the last division in the stomatal cell lineage as well as the number of stomata . In collaboration with MYB124 and MYB88, restrict the G1/S transition and chloroplast and nuclear number during stomatal formation, and normally maintain fate and developmental progression throughout the stomatal cell lineage .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35318
Sequence Length: 309
Subcellular Location: Nucleus
EC: 2.7.11.22
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Q2V419 | MEKYEKLEKVGEGTYGKVYKAMEKTTGKLVALKKTRLEMDEEGIPPTALREISLLQMLSQSIYIVRLLCVEHVIQSKDSTVSHSPKSNLYLVFEYLDTDLKKFIDSHRKGSNPRPLEASLVQRFMFQLFKGVAHCHSHGVLHRDLKPQNLLLDKDKGILKIADLGLSRAFTVPLKAYTHEIVTLWYRAPEVLLGSTHYSTAVDIWSVGCIFAEMIRRQALFPGDSEFQQLLHIFRLLGTPTEQQWPGVMALRDWHVYPKWEPQDLSRAVPSLSPEGIDLLTQMLKYNPAERISAKAALDHPYFDSLDKSQF | Function: Together with CDKB1-1, promotes both the last division in the stomatal cell lineage as well as the number of stomata . In collaboration with MYB124 and MYB88, restrict the G1/S transition and chloroplast and nuclear number during stomatal formation, and normally maintain fate and developmental progression throughout the stomatal cell lineage .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35582
Sequence Length: 311
EC: 2.7.11.22
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Q0J4I1 | MAALHHQAAAAPVTTTTDGGELRAMDLYEKLEKVGEGTYGKVYKAREKATGRIVALKKTRLPEDDEGVPPTALREVSLLRMLSQDSHVVRLLDLKQGQNKEGQTILYLVFEYMDTDLKKFIRAHRQNLQKIPVPTVKILMYQLCKGVAFCHGRGVLHRDLKPHNLLMDRKTMALKIADLGLSRSFTVPLKKYTHEILTLWYRAPEVLLGAAHYSTPVDIWSVGCIFAELATNQPLFAGDSEVQQLLHIFKLLGTPNEQVWPGVSKLPNWHEYPQWNPSKVSDLVHGLDADALDLLEKMLQYEPSKRISAKKAMEHPYFNDVNKELY | Function: Forms a complex with CYCB2-1 or CYCB2-2 that activates CDK kinase in tobacco BY2 cells during G2/M (mitosis) phases. May be involved in the regulation of the cell cycle at the G2/M transition.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 36977
Sequence Length: 326
Subcellular Location: Nucleus
EC: 2.7.11.22
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P46559 | MTAIEKFFTEKSPDSEQVLLKVIELGIDFLGGEWKNVDKSQVNVSRVHGGQSNHMFHVTSSTSATPYLLRIHRQPPSQVFTDTVNLAIFSERGLGPKLYGFFEGGRMEEFLPSKTFDVNDVLVPENSRKIGAIFPLYHSINVPVSKSRRCVHLMREWLNGYESLGGGDYEILPTTVNYSDHPKSVSIKDLNHEIDNFEKWSTEIFEHTLVFSHNDLASTNILELNSTKELVLIDWEFGTYNWRGFDLAMHLSETAIDYRVPFPPGIKMNGDLIDNPPNIQIFCEAYVEADKKLKNRSPSDPTAEVKALIQECQFFWPLTNLFWALSAMKHSLLKFENGVDLDVQARDRLAVYFHLKPRSQKIYEELSKK | Cofactor: Less efficient with Mn(2+).
Function: Catalyzes the first step in phosphatidylcholine biosynthesis. Phosphorylates choline.
Catalytic Activity: ATP + choline = ADP + H(+) + phosphocholine
Sequence Mass (Da): 42264
Sequence Length: 369
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from choline: step 1/1.
EC: 2.7.1.32
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Q8CFC7 | MWHEARKHERKLRGMMVDYKKRAERRREYYEKIKKDPAQFLQVHGRACKVHLDSAVALAAESPVNMMPWQGDTNNMIDRFDVRAHLDHIPDYTPPLLTTISPEQESDERKCNYERYRGLVQNDFAGISEEQCLYQIYIDELYGGLQRPSEDEKKKLAEKKASIGYTYEDSTVAEVEKVAEKPEEEESPAEEESNSDEDEVIPDIDVEVDVDELNQEQVADLNKQATTYGMADGDFVRMLRKDKEEAEAIKHAKALEEEKAMYSGRRSRRQRREFREKRLRGRKISPPSYARRDSPTYDPYKRSPSESSSESRSRSRSPSPGREEKITFITSFGGSDEEAAAAAAAAAASGAAPGKPPAPPQTGGPAPGRNASTRRRSSSSSASRTSSSRSSSRSSSRSRRGYYRSGRHARSRSRSWSRSRSRSRRYSRSRSRGRRHSDGGSRDGHRYSRSPARRGGYVPRRRSRSRSRSGDRYKRGARGPRHHSSSHSRSSWSLSPSRSRSVTRSGSRSQSRSRSRSQSHSQSQSHSPSPPREKLTRPAASPAVGEKLKKTEPAAGKETGAAKPKLTPQERLKLRMQKALNRQFKADKKAAQEKMIQQEHERQEREDELRAMARKIRMKERERREKEREEWERQYSRQSRSPSPRYSREYSSSRRRSRSRSRSPHYRH | Function: Probably functions as an alternative splicing regulator. May regulate the mRNA splicing of genes such as CLK1. May act by regulating members of the CLK kinase family.
PTM: Phosphorylated in vitro by CLK4.
Sequence Mass (Da): 76825
Sequence Length: 668
Subcellular Location: Nucleus
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Q5HZB6 | MWHEARKHERKLRGMMVDYKKRAERRREYYEKIKKDPAQFLQVHGRACKVHLDSAVALAAESPVNMMPWQGDTNNMIDRFDVRAHLDHIPDYTPPLLTTISPEQESDERKCNYERYRGLVQNDFAGISEEQCLYQIYIDELYGGLQRPSEDEKKKLAEKKASIGYTYEDSTVAEVEKVAEKPEEEESPAEEESNSDEDEVIPDIDVEVDVDELNQEQVADLNKQATTYGMADGDFVRMLRKDKEEAEAIKHAKALEEEKAMYSGRRSRRQRREFREKRLRGRKISPPSYARRDSPTYDPYKRSPSESSSESRSRSRSPSPGREEKITFITSFGGSDEEAAAAAAAAAASGAAPGKPPAPPQPGGPAPGRNASARRRSSSSSASRTSSSRSSSRSSSRSRRGYYRSGRHARSRSRSWSRSRSRSRRYSRSRSRGRRHSDGGSRDGHRYSRSPARRSGYAPRRRSRSRSRSGDRYKRGARGPRHHSSSHSRSSWSLSPSRSRSLTRSGSRSQSRSRSRSQSHSQSQSHSPSPPREKLTRPAASPAVGEKLKKTEPAAGKETGAAKPKLTPQERLKLRMQKALNRQFKADKKAAQEKMIQQEHERQEREDELRAMARKIRMKERERREKEREEWERQYSRQSRSPSPRYSREYSSSRRRSRSRSRSPHYRH | Function: Probably functions as an alternative splicing regulator. May regulate the mRNA splicing of genes such as CLK1. May act by regulating members of the CLK kinase family (By similarity).
PTM: Phosphorylated in vitro by CLK4.
Sequence Mass (Da): 76807
Sequence Length: 668
Subcellular Location: Nucleus
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P32756 | MEKEKVDELPPNDNWYETALPKPPVPSLEATLDRYLEYAAVVAVGQKASLATTHDAAHKFVRQATPLQEQLLEIAEKSPNWATKFWLPEMYMRVRMPTPVNSNPGYIFPKVKFETKEDHIKYTALLTRGLLEYKNLIDTKQVCREKSTGAQKLQMCMEQYDRVLSCYREPGVGEDTQIRKQKTNDGNEHVLVMCRNQTFLLHSRINGALVSYADVEYQLAQIEEISKINQNNTANIGASGVGPRDNAALFWQDMLTVEQNSKSYEWVKSALFVVCLDMEDPIDYGKNDTMSISEKEKEFVARGYSTLTGHGSSKFGLNRWYDATIQLVVSSSGVNGLCIEHSTAEGIVIINMAETAIRYAQKYFKSKMVWNDVRNVHPKSLTWHFSENSRNILKKQAEVFDELANELELEVLIFNEFGKDSIKNWRVSPDGFIQLIMQLAHYKTHGHLVSTYESASVRRFGAGRVDNIRANTQEALEWVTAMASKKESKERKLELFKKAVLKQVKVTLENISGYGVDNHLCALFCLAREREETTGEDIPSLFLDPLWSEVMRFPLSTSQVTTSLDIPDCYLTYGAVVRDGYGCPYNIQPDRVIFAPTAFRSDPRTDLQHFKKSLAGAMRDVKELLSN | Function: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses (By similarity). Required in SIA sublateral cholinergic motor neurons for a left-right turning behavior that occurs during the lethargus phase of the normal sleep process called 'flipping' . During 'flipping' animals rotate 180 degrees about their longitudinal axis .
Catalytic Activity: acetyl-CoA + choline = acetylcholine + CoA
Sequence Mass (Da): 71317
Sequence Length: 627
EC: 2.3.1.6
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B2ZGJ1 | MPVSKREQSKDTGDPCALPKLPIPPLKQTLDMYLTCMGHLVPEDQFRKTKAVVEKFGAPGGVGETLQKKLLERSEQKANWVYDYWLEDMYLNNRLALPVNSSPVMVFHKQNFKGQSDVLRFAANLISGVLEYKALIDGRALPVEHARGQLAGTPLCMDQYNKVFTSYRLPGTKTDTLVAQKSTVMPEPEHIIVACKNQFFVLDVMVNFRRLNEKDLYTQLERIRKMADIEEERQPPIGLLTSDGRTQWAEARNILIKDSTNRDSLDMIERCLCLVCLDEETATELNDSNRALLMLHGGGTDKNGGNRWYDKPMQFVIGADGCCGVVCEHSPFEGIVLVQCSEYLLRYMRGSPSKLVRAASMSELPAPRRLRWKCSPDIQTFLSASADRLQKLVKNLDMNVHKFTGYGKEFIKRQKMSPDAYVQVALQFTFYRCHGRLVPTYESASIRRFQEGRVDNIRSSTPEALAFVKAMASGSKITDAEKMELLWTAIKAQTNYTILAITGMAIDNHLLGLREIAKELKLEKPELFSDTTYATSIHFTLSTSQVPTTEEMFCCYGPVVPNGYGACYNPQTDHILFCVSSFRECAETSSDLFVKTLEGCLKEMQDLCRKCNTEVKPADSTQRMEGNPKVMKNGSKS | Function: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
Catalytic Activity: acetyl-CoA + choline = acetylcholine + CoA
Sequence Mass (Da): 71840
Sequence Length: 637
EC: 2.3.1.6
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P51798 | MANVSKKVSWSGRDRDDEEAAPLLRRTARPGGGTPLLNGAGPGAARQSPRSALFRVGHMSSVELDDELLDPDMDPPHPFPKEIPHNEKLLSLKYESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKGNIDKFTEKGGLSFSLLLWATLNAAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPCLQVIEAVLVAAVTATVAFVLIYSSRDCQPLQGGSMSYPLQLFCADGEYNSMAAAFFNTPEKSVVSLFHDPPGSYNPLTLGLFTLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPVTSHSLTAREVMSTPVTCLRRREKVGVIVDVLSDTASNHNGFPVVEHADDTQPARLQGLILRSQLIVLLKHKVFVERSNLGLVQRRLRLKDFRDAYPRFPPIQSIHVSQDERECTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRLGKRGLEELSLAQT | Function: Slowly voltage-gated channel mediating the exchange of chloride ions against protons . Functions as antiporter and contributes to the acidification of the lysosome lumen and may be involved in maintaining lysosomal pH . The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons (By similarity). The presence of conserved gating glutamate residues is typical for family members that function as antiporters (By similarity).
Catalytic Activity: 2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88679
Sequence Length: 805
Subcellular Location: Lysosome membrane
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P0DM29 | MNPKLLIVIGLLLATGVCSFAKALDEESLRKECNHLNEPCDSDGDCCTSSEQCISTGSKYFCKGKQGP | Function: Cell penetrating peptide (CPP) that increases intracellular calcium release through the activation of nuclear inositol 1,4,5-trisphosphate receptors (ITPR) of cardiomyocytes, thereby causing an increase in the contraction frequency of these cells . In vivo, this toxin is not lethal to mice, hovewer anti-CPP serum reduces venom lethality, suggesting that this toxin is lethal when it acts in synergy with other venom components .
Sequence Mass (Da): 7298
Sequence Length: 68
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q8MN58 | MSDPFGEENVEITEEFVEGDINENDLIDGNVEYVDGNGISFETTTFDNSNNNNNNNNHNNNSYNSGFDGDLSSVDGDMKPKETAPAMREYLEKHEKEMQEKKKKSEEKRQKKIAEAKQSLDNFYSEREAKKKTALKNNRDHNKSLETDSTSGNTTHTWESVVSMIDLQAKPNPANKDTSRMREILIRLKNQPIV | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22137
Sequence Length: 194
Subcellular Location: Cytoplasmic vesicle membrane
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Q9VWA1 | MDFGDDFAAKEDVDPAAEFLAREQSALGDLEAEITGGSASAPPAASTDEGLGELLGGTASEGDLLSAGGTGGLESSTGSFEVIGGESNEPVGISGPPPSREEPEKIRKWREEQKQRLEEKDIEEERKKEELRQQSKKELDDWLRQIGESISKTKLASRNAEKQAATLENGTIEPGTEWERIAKLCDFNPKVNKAGKDVSRMRSIYLHLKQNPIQVQKST | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23840
Sequence Length: 219
Subcellular Location: Cytoplasmic vesicle membrane
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Q5E9L0 | MASTASEIIAFMVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYWANLWKTCVTDSTGVSNCKDFPSMLALDGYIQACRGLMIAAVSLGFFGSIFALIGMKCTKVGGSDKAKAKIACLAGIVFILSGLCSMTGCSLYANKITTEFFDPLFVEQKYELGAALFIGWAGASLCLIGGVIFCFSISDNNKAPRMGYTYNGATSVMSSRTKYHGREGDLKTPNPSKQFDKNAYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in the regulation of paracellular epithelia permeability to ions in multiple organs. It acts as a paracellular ion channel probably forming permselective pores; isoform 1 appears to create pores preferentially permeable to cations and isoform 2 for anions. In sweat glands and in the thick ascending limb (TAL) of Henle's loop in kidney, it controls paracellular sodium permeability which is essential for proper sweat production and renal function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24761
Sequence Length: 231
Domain: The fourth transmembrane region (161-181) is necessary for integration into tight junctions.
Subcellular Location: Cell junction
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P78369 | MASTASEIIAFMVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYWANLWKACVTDSTGVSNCKDFPSMLALDGYIQACRGLMIAAVSLGFFGSIFALFGMKCTKVGGSDKAKAKIACLAGIVFILSGLCSMTGCSLYANKITTEFFDPLFVEQKYELGAALFIGWAGASLCIIGGVIFCFSISDNNKTPRYTYNGATSVMSSRTKYHGGEDFKTTNPSKQFDKNAYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in the regulation of paracellular epithelia permeability to ions in multiple organs. It acts as a paracellular ion channel probably forming permselective pores; isoform 1 appears to create pores preferentially permeable to cations and isoform 2 for anions. In sweat glands and in the thick ascending limb (TAL) of Henle's loop in kidney, it controls paracellular sodium permeability which is essential for proper sweat production and renal function .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24488
Sequence Length: 228
Domain: The fourth transmembrane region (161-181) is necessary for integration into tight junctions.
Subcellular Location: Cell junction
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Q9Z0S6 | MASTALEIVAFVVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYFANLWKICVTDSTGVANCKEFPSMLALDGYIQACRGLMIAAVSLGFFGSIFALFGMKCTKVGGSDQAKAKIACLAGIVFILSGLCSMTGCSLYANKITTEFFDPLYMEQKYELGAALFIGWAGASLCIIGGVIFCFSISDNNKTPRMGYTYNGPTSAMSSRTKYQGGEGDFKTTGPSKQFDKNAYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in the regulation of paracellular epithelia permeability to ions in multiple organs. It acts as a paracellular ion channel probably forming permselective pores; isoform 1 appears to create pores preferentially permeable to cations and isoform 2 for anions. In sweat glands and in the thick ascending limb (TAL) of Henle's loop in kidney, it controls paracellular sodium permeability which is essential for proper sweat production and renal function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24695
Sequence Length: 231
Domain: The fourth transmembrane region (161-181), which is missing in isoform 3, isoform 5 and isoform 6, is necessary for integration into tight junctions.
Subcellular Location: Cell junction
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O75508 | MVATCLQVVGFVTSFVGWIGVIVTTSTNDWVVTCGYTIPTCRKLDELGSKGLWADCVMATGLYHCKPLVDILILPGYVQACRALMIAASVLGLPAILLLLTVLPCIRMGQEPGVAKYRRAQLAGVLLILLALCALVATIWFPVCAHRETTIVSFGYSLYAGWIGAVLCLVGGCVILCCAGDAQAFGENRFYYTAGSSSPTHAKSAHV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21993
Sequence Length: 207
Subcellular Location: Cell junction
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Q5REK8 | MVATCLQVVGFVTSFVGWIGVIVTTSTNDWVVTCGYTIPTCRKLDELGSKGLWADCVMATGLYHCKPLVDILPCRALMIAASVLGLPAILLLLTVLPCIRMGQEPGVAKYRRAQLAGVLLILLALCAIVATIWFPVCAHRETTIVSFGYSLYAGWIGAVLCLVGGCVILCCAGDAQAFGENRFYYTAGSSSPTHAKSAHV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21248
Sequence Length: 200
Subcellular Location: Cell junction
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Q0IIL2 | MGCRDVHAATVLSFLCGIASVAGLFAGTLLPNWRKLRLITFNRNEKNLTVYTGLWVKCARYDGGNDCLMYDAAWYSSVDQLDLRVLQFALPLSILIAMGALLLCLIGMCNTAFRSSVPNIKLAKCLVNSAGCHLVAGLLFFLAGTVSLSPSIWVIFYNIHLNRKFEPVFAFDYAVYVTVASAGGLFMTALLLFIWYCACKSLPSPFWQPLYSHPPGMHTYSQPYSARSRLSAIEIDIPVVSHTT | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26951
Sequence Length: 244
Subcellular Location: Cell junction
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P56749 | MGCRDVHAATVLSFLCGIASVAGLFAGTLLPNWRKLRLITFNRNEKNLTVYTGLWVKCARYDGSSDCLMYDTTWYSSVDQLDLRVLQFALPLSMLIAMGALLLCLIGMCNTAFRSSVPNIKLAKCLVNSAGCHLVAGLLFFLAGTVSLSPSIWVIFYNIHLNKKFEPVFSFDYAVYVTIASAGGLFMTSLILFIWYCTCKSLPSPFWQPLYSHPPSMHTYSQPYSARSRLSAIEIDIPVVSHTT | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27110
Sequence Length: 244
Subcellular Location: Cell junction
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Q2G015 | MNMKKKEKHAIRKKSIGVASVLVGTLIGFGLLSSKEADASENSVTQSDSASNESKSNDSSSVSAAPKTDDTNVSDTKTSSNTNNGETSVAQNPAQQETTQSSSTNATTEETPVTGEATTTTTNQANTPATTQSSNTNAEELVNQTSNETTSNDTNTVSSVNSPQNSTNAENVSTTQDTSTEATPSNNESAPQSTDASNKDVVNQAVNTSAPRMRAFSLAAVAADAPVAGTDITNQLTNVTVGIDSGTTVYPHQAGYVKLNYGFSVPNSAVKGDTFKITVPKELNLNGVTSTAKVPPIMAGDQVLANGVIDSDGNVIYTFTDYVNTKDDVKATLTMPAYIDPENVKKTGNVTLATGIGSTTANKTVLVDYEKYGKFYNLSIKGTIDQIDKTNNTYRQTIYVNPSGDNVIAPVLTGNLKPNTDSNALIDQQNTSIKVYKVDNAADLSESYFVNPENFEDVTNSVNITFPNPNQYKVEFNTPDDQITTPYIVVVNGHIDPNSKGDLALRSTLYGYNSNIIWRSMSWDNEVAFNNGSGSGDGIDKPVVPEQPDEPGEIEPIPEDSDSDPGSDSGSDSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSDNDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSDSDSDSDSDSDSDSDSDSDSASDSDSGSDSDSSSDSDSESDSNSDSESVSNNNVVPPNSPKNGTNASNKNEAKDSKEPLPDTGSEDEANTSLIWGLLASIGSLLLFRRKKENKDKK | Function: Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen cell proliferative response in vitro, contributing significantly to the immunostimulatory activity of S.aureus.
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 96448
Sequence Length: 927
Subcellular Location: Secreted
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Q8GHB1 | MSKALANMPGDDYFRHPPVFDTYAEHRAYLKFRHAVALRHFARLGFDQDGLAGLITVADPEHADTYWANPLAHPFSTITPADLIRVDGDSTETVDGQRRVNIAAFNIHAEIHRARPDVQAVIHLHTVYGRAFSAFARKLPPLTQDACPFFEDHEVFDDYTGLVLAKDDGRRIAKQLRGHKAILLKNHGLVTVGETLDAAAWWFTLLDTCCHVQLLADAAGGAEPIPAEVARLTGQQLGSHLLGWNSYQPLHEATLARNPDLAAMAPALPPQTPALAR | Function: Involved in the biosynthesis of ring A of the aminocoumarin antibiotic clorobiocin . Catalyzes two consecutive oxidative decarboxylations of 3-dimethylallyl-4-hydroxyphenylpyruvate (3DMA-4HPP) to yield 3-dimethylallyl-4-hydroxybenzoate (3DMA-4HB) via the 3-dimethylallyl-4-hydroxymandelic acid (3DMA-4HMA) intermediate .
Catalytic Activity: 3-dimethylallyl-4-hydroxyphenylpyruvate + O2 = 3-dimethylallyl-4-hydroxymandelate + CO2
Sequence Mass (Da): 30496
Sequence Length: 277
Pathway: Antibiotic biosynthesis.
EC: 1.13.11.83
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P09870 | MLRRKVSTLLMTALITTSFLNSKPVYANPVTKSKDNNLKEVQQVTSKSNKNKNQKVTIMYYCDADNNLEGSLLNDIEEMKTGYKDSPNLNLIALVDRSPRYSSDEKVLGEDFSDTRLYKIEHNKANRLDGKNEFPEISTTSKYEANMGDPEVLKKFIDYCKSNYEADKYVLIMANHGGGAREKSNPRLNRAICWDDSNLDKNGEADCLYMGEISDHLTEKQSVDLLAFDACLMGTAEVAYQYRPGNGGFSADTLVASSPVVWGPGFKYDKIFDRIKAGGGTNNEDDLTLGGKEQNFDPATITNEQLGALFVEEQRDSTHANGRYDQHLSFYDLKKAESVKRAIDNLAVNLSNENKKSEIEKLRGSGIHTDLMHYFDEYSEGEWVEYPYFDVYDLCEKINKSENFSSKTKDLASNAMNKLNEMIVYSFGDPSNNFKEGKNGLSIFLPNGDKKYSTYYTSTKIPHWTMQSWYNSIDTVKYGLNPYGKLSWCKDGQDPEINKVGNWFELLDSWFDKTNDVTGGVNHYQW | Function: Cysteine endopeptidase with strict specificity.
Catalytic Activity: Preferential cleavage: Arg-|-Xaa, including Arg-|-Pro bond, but not Lys-|-Xaa.
Sequence Mass (Da): 59733
Sequence Length: 526
EC: 3.4.22.8
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Q5ZKJ0 | MLSRSSFTSLAVGVFAVYVAHTCWVMYGIVYTRPCPSGGAAACVWPYLARRPKLQLSVYTTTRSNIGAESNIDLVLNVEDFDIESKFERTVNVSVPKKTRNNGTLYAYIFLHHAGVLPWHDGKQVHIVSPLTTYMVPKPEEINLLTGESTTQQIEAEKQTSALDEPVSHWRSRLTLNVMVEDFVFDGSSLPADVHRYMKMVQLGKTVHYLPILFIDQLSNRVKDLMVINRSTTELPLTVSYDKISLGKLRFWIHMQDAVYSLQQFGFSEKDADEVKGIFVDTNLYFLALTFFVAAFHLLFDFLAFKNDISFWKKKRSMIGMSTKAVLWRCFSTVVIFLFLLDEQTSLLVLIPAGIGAVIELWKVKKALKMTVKWQGIRPKVQFGASNDSEKKTEEYDTQAMKYLSYLLYPLCIGGAAYSLLNVKYKSWYSWLINSFVNGVYAFGFLFMLPQLFVNYKMKSVAHLPWKAFTYKAFNTFIDDIFAFIITMPTSHRLACFRDDVVFLVYLYQRWLYPVDKSRVNEYGESYEEKPKKKSS | Function: Scramblase that mediates the translocation of glucosaminylphosphatidylinositol (alpha-D-GlcN-(1-6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol, GlcN-PI) across the endoplasmic reticulum (ER) membrane, from the cytosolic leaflet to the luminal leaflet of the ER membrane, where it participates in the biosynthesis of glycosylphosphatidylinositol (GPI). GPI is a lipid glycoconjugate involved in post-translational modification of proteins. Can also translocate 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) (phosphatidylinositol or PI), as well as several other phospholipids (1,2-diacyl-sn-glycero-3-phosphocholine, 1,2-diacyl-sn-glycero-3-phosphoethanolamine), and N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI) in vitro.
Catalytic Activity: an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol(in) = an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61649
Sequence Length: 536
Subcellular Location: Endoplasmic reticulum membrane
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Q6DHU1 | MFPKTSFTSLIVGVFLLYVLHTCWVMYGIVYTKPCEKRRAESCISPYLAAKPRLQLSVYTALRPNADGGHSLIHREEEFDVNTKFEKLVNVSLPKKTRKNGTLYAMVFLHQAGVSPWQDPHQVHLVTQLTTYMLPKPPEISLITGQDEPEKPDQQKQSSDSELDRPVSHWRSRLTLNVVSENFLFDREALPGDVHRYMRVYQSGKKMIYLPLLFVDELSNRVKDLMEINSSSTELPLTITYDSIALGKLRFWIHMQDAVYSLQQFGFTEKDADEIKGIFVDTNLYFLALTFFVAAFHLLFDFLAFKNDISFWKHKKSMVGMSSKAVLWRCFSTIVIFLYLLDEQTSLLVLVPAGIGSLIEVWKVKKAFKIHVIWRGLTPTFLFGKLDESEKRTEEYDTLAMKYLSYLLYPLCVGGAVYALVFVKYKSWYSWIINSLVNGVYAFGFLFMLPQLFVNYKLKSVAHLPWKAFMYKAFNTFIDDVFAFIITMPTSHRLACFRDDVVFLVYLYQRWLYPVDRSRVNEYGVSYDEKPKGKSHED | Function: Scramblase that mediates the translocation of glucosaminylphosphatidylinositol (alpha-D-GlcN-(1-6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol, GlcN-PI) across the endoplasmic reticulum (ER) membrane, from the cytosolic leaflet to the luminal leaflet of the ER membrane, where it participates in the biosynthesis of glycosylphosphatidylinositol (GPI). GPI is a lipid glycoconjugate involved in post-translational modification of proteins. Can also translocate 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) (phosphatidylinositol or PI), as well as several other phospholipids (1,2-diacyl-sn-glycero-3-phosphocholine, 1,2-diacyl-sn-glycero-3-phosphoethanolamine), and N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI) in vitro.
Catalytic Activity: an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol(in) = an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62497
Sequence Length: 538
Subcellular Location: Endoplasmic reticulum membrane
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Q96KA5 | MWSGRSSFTSLVVGVFVVYVVHTCWVMYGIVYTRPCSGDANCIQPYLARRPKLQLSVYTTTRSHLGAENNIDLVLNVEDFDVESKFERTVNVSVPKKTRNNGTLYAYIFLHHAGVLPWHDGKQVHLVSPLTTYMVPKPEEINLLTGESDTQQIEAEKKPTSALDEPVSHWRPRLALNVMADNFVFDGSSLPADVHRYMKMIQLGKTVHYLPILFIDQLSNRVKDLMVINRSTTELPLTVSYDKVSLGRLRFWIHMQDAVYSLQQFGFSEKDADEVKGIFVDTNLYFLALTFFVAAFHLLFDFLAFKNDISFWKKKKSMIGMSTKAVLWRCFSTVVIFLFLLDEQTSLLVLVPAGVGAAIELWKVKKALKMTIFWRGLMPEFQFGTYSESERKTEEYDTQAMKYLSYLLYPLCVGGAVYSLLNIKYKSWYSWLINSFVNGVYAFGFLFMLPQLFVNYKLKSVAHLPWKAFTYKAFNTFIDDVFAFIITMPTSHRLACFRDDVVFLVYLYQRWLYPVDKRRVNEFGESYEEKATRAPHTD | Function: Scramblase that mediates the translocation of glucosaminylphosphatidylinositol (alpha-D-GlcN-(1-6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol, GlcN-PI) across the endoplasmic reticulum (ER) membrane, from the cytosolic leaflet to the luminal leaflet of the ER membrane, where it participates in the biosynthesis of glycosylphosphatidylinositol (GPI) . GPI is a lipid glycoconjugate involved in post-translational modification of proteins . Can also translocate 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) (phosphatidylinositol or PI), as well as several other phospholipids (1,2-diacyl-sn-glycero-3-phosphocholine, 1,2-diacyl-sn-glycero-3-phosphoethanolamine), and N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI) in vitro .
Catalytic Activity: an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol(in) = an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62229
Sequence Length: 538
Subcellular Location: Endoplasmic reticulum membrane
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Q8KG79 | MNTADTRQRLLDIEKQIASLREEQATVKAQWEAEKELIHTSRRLKEELEDLRVQAENYERSGDYGKVAEIRYGKIAEIEKALEENNRKIEARQASGDLIMKEEIDAGDIADIVSRWTGIPVSKMLQSERQKLLGIESELHRRVVGQDEAVRAVSDAVKRSRAGMGDEKRPIGSFIFLGPTGVGKTELARTLAEYLFDDEDALIRIDMSEYMEAHTVSRLVGAPPGYVGYEEGGQLTEAVRRKPFSVVLLDEIEKAHPDVFNILLQILDDGRLTDSKGRTVNFKNTIIIMTSNIGAQLIQSEMEHLEGRDADAALAGLKEKLFQLLKQQVRPEFLNRIDEVILFTPLTRENLREIVTIQFNRIKETARRQRITLEISDEALMWLAKTGFDPAFGARPLKRVMQRQITNRLSEMILAGQVGEDDTVEIGLENDAIVMKKK | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Sequence Mass (Da): 49655
Sequence Length: 438
Domain: The N-terminal domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer (By similarity).
Subcellular Location: Cytoplasm
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Q7U637 | MQPTAEQFTEQAWAAIVAAQQLAQASRHQQLETEHLLLALLRQNGLAGRILSKTGVDVTTFEASVEGHLQRLPSLGSAPDSVFLGRSLNKALDRAEQRRDGFGDSFIAIEHLLLALAEDDRCGRQLLSQAGVTTNTLKEAITAVRGNQTVTDQNPEATYESLAKYGRDLTAAARDGQLDPVIGRDEEIRRTIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPQALQNRQLITLDMGALIAGAKYRGEFEERLKAVLKEVTTSDGQIVLFIDEIHTVVGAGASGGAMDASNLLKPMLARGELRCIGATTLDEHRQHIEKDPALERRFQQVLVDQPTVPDTISILRGLKERYEVHHGVRIADSALVAAAMLSSRYITDRFLPDKAIDLVDESAARLKMEITSKPEQIDEIDRKILQLEMEKLSLGRESDSASQERLQRIERELAELGEQQSSLNAQWQSEKGAIDQLSALKEEIERVQLQVEQAKRNYDLNKAAELEYGTLATLQRQLQEQEDLLEDEDGTDKTLLREEVTEDDIAEVIAKWTGIPVARLVQSEMEKLLQLEDDLHQRVIGQNQAVTAVADAIQRSRAGLSDPNRPIASFLFLGPTGVGKTELSKALANRLFDSDDAMVRIDMSEYMEKHTVSRLIGAPPGYVGYEAGGQLTEAVRRRPYAVILFDEVEKAHPDVFNVMLQILDDGRVTDGQGRTVDFTNTVLILTSNIGSQSILELAGDPEQHTAMEQRVNEALKAKFRPEFLNRLDDQIIFRSLEKEELRRIVSLQVERLRSRLEQRKLDLQLSDIAADWLATIGFDPVYGARPLKRAIQRELETPIAKAILAGQLSEGQTVQVDAGDDKLSIS | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Sequence Mass (Da): 95612
Sequence Length: 862
Domain: The Clp repeat (R) domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer (By similarity).
Subcellular Location: Cytoplasm
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P53533 | MQPTNPNQFTEKAWEAIVRTTDVAKQAQHQQIESEHLFLALLQEPGLALNILKKAGLEAAQLQQFTERFIARQPKVSGGNQSVYLGRSLDQLLDQADQFRKDFGDEFISVEHLILSFPRDSRFGRLLSQEFKVDEKQLRQIIQQIRGSQKVTDQNPEGKYEALEKYGRDLTEMARRGKLDPVIGRDDEIRRTIQILSRRTKNNPVLIGEPGVGKTAIAEGLAQRIINGDVPQSLKDRRLIALDMGALIAGAKFRGEFEERLKAVLKEVTDSEGIIILFIDEIHTVVGAGAVQGSMDAGNLLKPMLARGELRCIGATTLDEYRQYIEKDAALERRFQQVFVDQPTVEDTISILRGLKERYEVHHGVRISDNALVAAAVLSTRYISDRFLPDKAIDLVDESAARLKMEITSKPEELDEIDRKILQLEMERLSLQKESDLASQERLQRLEKELADLKEEQRSLSSQWQAEKDVITDIQSVKEEIDQVNLLIQQAERDYDLNKAAELKYGKLTELQRKLNEMEGGLATTHTSGKSLLREEVTEVDIAEIISKWTGIPVSKLVESEMQKLLNLDEELHQRVIGQEEAVSAVADAIQRSRAGLSDPKRPIASFIFLGPTGVGKTELAKALAAYLFDTEDAMIRIDMSEYMEKHAVSRLIGAPPGYVGYDEGGQLTEAVRRRPYSVILFDEIEKAHPDVFNVMLQILDDGRVTDSRGRTVDFKNTILILTSNIGSQYILDVAGDDSRYEEMRSRVTEALRANFRPEFLNRVDETIIFHSLRKDQLQQIVRIQLHRLEERLSDRKLSLSMSPEAIDFLVEIGFDPVYGARPLKRVIQRELETAIAKAILRGQFSDGDTIQVAVENERLVFKAIATPTAVPLS | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary for thermotolerance.
Sequence Mass (Da): 98726
Sequence Length: 874
Domain: The Clp repeat (R) domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer (By similarity).
Subcellular Location: Cytoplasm
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Q8KA87 | MHFDPNKFTVKAQEALQAASMLASSKQNQQIEPEHLLSVMLGDHDNIACQIARKLETPVDTLLSVVDREIDRIPKVTGASATGQYISSDLGKVFDTALKEAEQLKDEYISSEHLFIAMSEAGVKVSKLLKDAGIDRNAILKVLTSFRGSQRVTSQNAEESYQSLKKYSRNLNDLVIKGKLDPVIGRDDEIRRVLQILSRRTKNNPVLIGEPGVGKTAIVEGIAQRIVGGDVPENLKSKQIAALDIAALVAGTKFRGEFEERLKALVKEVQASDGEVILFIDELHLLVGAGSAEGSMDAANILKPALARGELRCIGATTLDEYRKHIEKDAALERRFQTVIVDQPSVEDTVSILRGLKEKYEIHHGVRIKDAALVAAAELSNRYIADRFLPDKAIDLIDEACSRLRLEIDSEPEELDRINRELRRLEIEREALKRELEATGSV | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Sequence Mass (Da): 48929
Sequence Length: 442
Domain: The Clp repeat (R) domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer (By similarity).
Subcellular Location: Cytoplasm
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Q7U3T3 | MTGTPASRGSLTHEPDRFSDPAWELLLAGQDMARRWRHDQLDVEHLIQVLFSDSSFRRWVEPLPLRSDDLLDRLEDVLADQPPARGDQLFIGEDLEQLLETADQVRGRWGDRSIDVPQLIVAVGADPRIGAELFAAQGLAVDRLESLLRQPSVSPAPAPPPVPTAASAPAPTPRSAPAPRVMAPEPEPMVELEREPSALEAYGRDLTEEAEAGSLDPVIGRDSEIRNLIKVLSRRSKNNPVLIGEPGVGKTAIAELLAQRIVAGEVPDSLQGLRLIALDLGALIAGAKFRGQFEERLRSVLEEVSRSDSGVVLFIDELHTVVGSDRSSTDAGSLLKPALARGDLRCIGATTPEEYRRTVEKDPALNRRFQQVLIREPDLELSLEILRGLRERYELHHGVTITDEAIQTANRLADRYISDRCLPDKAIDLIDEAAAQLKIEVTSKPQVVEEAEADLRRVELALLAAEEAPEEERIQLQRQRLEVSSRLDDLRRRWQEERTQLEELGQLLQQDEDLRHAIAEAEREGALEEAARLQYDQLHTVQQRREALEASQAEAQSAGTALLREQVEAGDIADLVARWTGIPVQRLLAGERRKLLALESHLSERVIGQVEAVAAVAAAIRRARAGMKDPRRPVGSFLFLGPTGVGKTELAKALATSLFDEEEALVRLDMSEFMERNASARLIGAPPGYVGYEEGGQLTEAVRRRPYAVLLLDEVEKAHPDVFNLLLQVLDDGRLTDSQGLTVDFRHTVVVMTSNLASPVILEHARSGSSDDAQLQQQVDAALSSQFRPEFLNRIDEVIRFRPLKVKDLVRIVRLQLADLSTLMAEQGLSLEVDDAVADSLARQGHEPEYGARPLRRVLRRQLENPLATQLLEERFRSAHGIRVRCGTDDGASLEFEPLE | Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Sequence Mass (Da): 99782
Sequence Length: 900
Domain: The Clp repeat (R) domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer (By similarity).
Subcellular Location: Cytoplasm
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Q7NEW2 | MPIGIPKVPYRLPGGQSQWIDIFNRLALDRIIFLGREVDDEIANAIIASMLYLDSEDPEKDIFLYINSPGGSVSAGLAIYDTMQHVRADVATMCVGLAASMGSFLLTAGAKGKRTSLPHSRIMIHQPLGGAQGQATDIGIQAKEILYTKDRLNQILSERTGQPLERIERDTDRDFFMSAEDAKQYGLIDQVVQHRPV | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 21757
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 3.4.21.92
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Q5FUR3 | MTIRDRDPLEVFSNSLVPMVVEQTARGERSFDIFSRLLQERIIFLTGPVYDQVSSLICAQLLYLESVNPTKEISFYINSPGGVVSAGLAIYDTMQYIRCPVSTVCIGQAASMGSLLLAGGEKGHRYALPNARVMVHQPSGGAQGQASDIEIQAREILIIRQRLNEIYREHTGQTLEQIEQKLERDSYLSANEAREFGLIDKVVERNPHETTPDPS | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 23969
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 3.4.21.92
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Q5Z0M4 | MSTYTIPNVIAQHPRGGERITDIYSHLLAERIVYLGTPIDSGVANALIAQLLHLESESPDQEINFYINCEGGDLPSMLAVYDTMQHIGAPVHTTCVGQAIAVGAVLLAGGAPGQRAMLPHARVVLHQPAARGQGPIPDLILQADELVRMRSEIEAILSRHTGRSPEQLREDTDRDRVFTATAALEYGLIDTVLSPRG | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 21275
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 3.4.21.92
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Q8YXH5 | MTIPIVIEQSGRGERAFDIYSRLLRERIVFLGQQVDSNLANLIVAQLLFLDAEDPEKDIYLYINSPGGSVTAGMGIFDTMKHIRPDVCTICTGLAASMGAFLLSAGAKGKRMSLPHSRIMIHQPLGGAQGQATDIEIQAREILYHKRRLNDYLAEHTGQPIERIAEDTERDFFMSPDEAKDYGLIDQVIDRHAAGSRPVAMVGQ | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 22570
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 3.4.21.92
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Q928C4 | MNLIPTVIEQTSRGERAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLDAQDPEKDIFLYINSPGGSISAGMAIYDTMNFVKADVQTIGMGMAASMGSFLLTAGANGKRFALPNAEIMIHQPLGGAQGQATEIEIAARHILKIKERMNTIMAEKTGQPYEVIARDTDRDNFMTAQEAKDYGLIDDIIVNKSGLKG | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 21605
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 3.4.21.92
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P26567 | MPIGVPKVPYRIPGDEEATWVDLYNVMYRERTLFLGQEIRCEITNHITGLMVYLSIEDGNSDIFLFINSLGGWLISGMAIFDTMQTVTPDIYTICLGIAASMASFILLGGEPTKRIAFPHARIMLHQPASAYYRARTPEFLLEVEELHKVREMITRVYALRTGKPFWVVSEDMERDVFMSADEAKAYGLVDIVGDEMIDEHCDTDPVWFPEMFKDW | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 24759
Sequence Length: 216
Subcellular Location: Plastid
EC: 3.4.21.92
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Q65RF6 | MALIPMVVEQTSRGERSYDIYSRLLKERVIFLSGEVEDNMANLIVAQLLFLESENPEKDINLYINSPGGSVTAGMAIYDTMQFIKPDVRTLCVGQACSMGAFLLAGGAAGKRAALPHARVMIHQPLGGFRGQASDIQIHAQEILKIKQTLNERLAFHTGQPFEVIERDTDRDNFMSAEDAKNYGLIDSVLVKR | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 21372
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.4.21.92
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Q9MUV8 | MPIGIPKVAYRIPGEAVSTYVDVYNRLYRERILFLGEDLDDEVANQLIGVMVFLNSEDDTKGIFFYINSPGGSMNAGLGVYDMIQHVNVDVTTICMGLAASMASFILAGGTPGQRLMFPHARVMLHQPMGGNGGKAKYMVEESVEVKRLRELIAHLYVKRTGQSLEKIRKDMNRDNFMRPRQAKEYGLIDHMVTNVNELDELDKQSNDLKKLGKVNLTNIETSNKSELK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Sequence Mass (Da): 25717
Sequence Length: 229
Subcellular Location: Plastid
EC: 3.4.21.92
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B7V5T6 | MAATGVDKDRPRAMTSTTYLGLLLVGIQVLGFVAAIHAVLTVRTAQGAIAWATSLVFMPYLTLLPYLVFGRSRFDAYIEARRQANREMHLAAAELDWRPWVEEALAARQVSGYKGLKALVRMTRTPTLANNRVRLLVNGEASFEAMFKAISAARQVILVQFFIVRDDALGQRLQQLLLERAANGVEVFFLYDAIGSHALPHRYVERLRQGGVQMHGFSTGSGMLNRFQVNFRNHRKVVVVDGECGFVGGHNVGVEYLGEKPPLAPWRDTHMELRGPAVACLQESFAEDWYWATHSLPPLILPPQYDSEGALCQVVASGPADAQETCSLFFVEMINAAHERVWITSPYFVPDEAVMAALRLAVLRGVDVRLLIPSRPDHRTVYAASSLYALEAIRAGVKVFRYQPGFLHQKVVLVDRDTAAVGSANLDNRSFRLNFEVMVVTVDEGFAGEVEAMLEADFAESLEFTPEDRRSVRRLQQLGMRVARLVSPIL | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54558
Sequence Length: 490
Subcellular Location: Cell inner membrane
EC: 2.7.8.-
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A0A345BJN2 | MAGDLWLVGDCTNHGGLSDAIIVSPDYRLLPEATGADIFDDVEAFWNWLHTSLPSLAQSYSWQAQPDLTRILCVGQSGGGSMAVHSALLHPEYSIKVIVSLYAPLYHNVPNLTVPRPRRILGTMPPPPRKAEGLIRSYIKQSKGSVRTGGNPFDMWELLLCLLQQGRLISLMNIKPDSRLDTPFLLRQVGKLPPLWLIHGEDDSVVGPSTICVHRVIF | Function: Probable carboxylesterase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8-dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms . These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly reducing polyketide synthase clz14, followed by oxaloacetate extension and product release to generate a tricarboxylic acid containing product . The phenylalanine ammonia lyase (PAL) clz10 and the acyl-CoA ligase clz12 are involved in transforming phenylalanine into benzoyl-CoA . The citrate synthase-like protein clz17 is involved in connecting the C-alpha-carbons of the hexaketide chain and oxaloacetate to afford the tricarboxylic acid unit . The potential hydrolytic enzymes, clz11 and clz13, are in close proximity to pks2 and may participate in product release . On the other side, the tetraketide arm is synthesized by a the squalestatin tetraketide synthase clz2 and enzymatically esterified to the core in the last biosynthetic step, by the acetyltransferase clz6 (By similarity). The biosynthesis of the tetraketide must involve 3 rounds of chain extension (By similarity). After the first and second rounds methyl-transfer occurs, and in all rounds of extension the ketoreductase and dehydratase are active (By similarity). The enoyl reductase and C-MeT of clz2 are not active in the final round of extension (By similarity). The acetyltransferase clz6 appears to have a broad substrate selectivity for its acyl CoA substrate, allowing the in vitro synthesis of novel squalestatins (By similarity). The biosynthesis of SQS1 requires several oxidative steps likely performed by oxidoreductases clz3, clz15 and clz16 (Probable). Finally, in support of the identification of the cluster as being responsible for SQS1 production, the cluster contains a gene encoding a putative squalene synthase (SS) clz20, suggesting a likely mechanism for self-resistance (Probable).
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Sequence Mass (Da): 24100
Sequence Length: 218
Pathway: Secondary metabolite biosynthesis.
EC: 3.1.1.1
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A0A345BJN3 | MVQRSHRSLVLETGGIQDRNSAKPFQVRRLYCTPIFHAFSFPEMVVNTIRLGFPSFYMRRFDESFADKIHEFGITETMAAPAMLLKIIQWTEKHEEKRFKLQGLRTILCAGAALASRLRASFLQLFDSASVRIVQVWGMTEGGWFATFWYPEHDDTGSIGRPLPTCQIRVSEVSRAELPDGRQVGELLVKGPQLLTAYKGHPDATKEALHDGWLRTGDIGYCADGKIYIIDRAKDIIKVNGWTISPAELETVLHQIPGIVDAAALSYGTGTKEHVAMFVVAEGPSLLVADIKHHLLQQVARFKVATCEIHLVDSLPRSPSGKVLRSVLRHQLQAHYDNVDSGTS | Function: Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8-dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms . These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly reducing polyketide synthase clz14, followed by oxaloacetate extension and product release to generate a tricarboxylic acid containing product . The phenylalanine ammonia lyase (PAL) clz10 and the acyl-CoA ligase clz12 are involved in transforming phenylalanine into benzoyl-CoA . The citrate synthase-like protein clz17 is involved in connecting the C-alpha-carbons of the hexaketide chain and oxaloacetate to afford the tricarboxylic acid unit . The potential hydrolytic enzymes, clz11 and clz13, are in close proximity to pks2 and may participate in product release . On the other side, the tetraketide arm is synthesized by a the squalestatin tetraketide synthase clz2 and enzymatically esterified to the core in the last biosynthetic step, by the acetyltransferase clz6 (By similarity). The biosynthesis of the tetraketide must involve 3 rounds of chain extension (By similarity). After the first and second rounds methyl-transfer occurs, and in all rounds of extension the ketoreductase and dehydratase are active (By similarity). The enoyl reductase and C-MeT of clz2 are not active in the final round of extension (By similarity). The acetyltransferase clz6 appears to have a broad substrate selectivity for its acyl CoA substrate, allowing the in vitro synthesis of novel squalestatins (By similarity). The biosynthesis of SQS1 requires several oxidative steps likely performed by oxidoreductases clz3, clz15 and clz16 (Probable). Finally, in support of the identification of the cluster as being responsible for SQS1 production, the cluster contains a gene encoding a putative squalene synthase (SS) clz20, suggesting a likely mechanism for self-resistance (Probable).
Sequence Mass (Da): 38434
Sequence Length: 344
Pathway: Secondary metabolite biosynthesis.
EC: 6.2.1.-
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A0A345BJP6 | MATATLPATVGVIGLWDGTTDGKEGFMDYATGDTNVKQPKEYEIEVHDIRKLDPQPTLLNNGYELVDIPTVVTEEQFSESGKSEKGKAYIKDVYFAECKRIIQEVAGGVDTIIPVSFRMREQKGEKESTTKKLGNIESRYAPRPVAHLDRDTPTAITVLEETVGKEKAQELLSKHKRNPATMWPLCFLNHDRIPTWNYDTHVGHVWSLNDPRVSDRGEKTYDCVVKYDERYDYHYVSDLKPEECLVFCSFDSIPKYAMPHSAFWDNNVPADAPNRRSIEVRSLVFF | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8-dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms . These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly reducing polyketide synthase clz14, followed by oxaloacetate extension and product release to generate a tricarboxylic acid containing product . The phenylalanine ammonia lyase (PAL) clz10 and the acyl-CoA ligase clz12 are involved in transforming phenylalanine into benzoyl-CoA . The citrate synthase-like protein clz17 is involved in connecting the C-alpha-carbons of the hexaketide chain and oxaloacetate to afford the tricarboxylic acid unit . The potential hydrolytic enzymes, clz11 and clz13, are in close proximity to pks2 and may participate in product release . On the other side, the tetraketide arm is synthesized by a the squalestatin tetraketide synthase clz2 and enzymatically esterified to the core in the last biosynthetic step, by the acetyltransferase clz6 (By similarity). The biosynthesis of the tetraketide must involve 3 rounds of chain extension (By similarity). After the first and second rounds methyl-transfer occurs, and in all rounds of extension the ketoreductase and dehydratase are active (By similarity). The enoyl reductase and C-MeT of clz2 are not active in the final round of extension (By similarity). The acetyltransferase clz6 appears to have a broad substrate selectivity for its acyl CoA substrate, allowing the in vitro synthesis of novel squalestatins (By similarity). The biosynthesis of SQS1 requires several oxidative steps likely performed by oxidoreductases clz3, clz15 and clz16 (Probable). Finally, in support of the identification of the cluster as being responsible for SQS1 production, the cluster contains a gene encoding a putative squalene synthase (SS) clz20, suggesting a likely mechanism for self-resistance (Probable).
Sequence Mass (Da): 32615
Sequence Length: 286
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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A0A345BJP7 | MSTTTTTLHTTTGTVYVADGTTDGKIGYYNHTDDSTNVIRKPIPIQVEDARTLSKSPTTKEEGYQLVDFHTKLPEGHFLDSKSPENKKVIEQVYFDECRRLVQEVTGAAEAYPYVYRVRNQEQNAKASNKSNFHTDFVPVVHVDRDDITAPQRLRASLGAEKAEMLLSKYKSYGSINVWRPVKNVVQKWPLMLVDHKSIENWDYSTHMFTLHSSNDERVATRGAKDHETILTHDKRYRYIYASDMTPDEAWLFFAFHSDPALGIPHGAFWDDSTKEEALTRCSIEVRIWVFFD | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8-dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms . These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly reducing polyketide synthase clz14, followed by oxaloacetate extension and product release to generate a tricarboxylic acid containing product . The phenylalanine ammonia lyase (PAL) clz10 and the acyl-CoA ligase clz12 are involved in transforming phenylalanine into benzoyl-CoA . The citrate synthase-like protein clz17 is involved in connecting the C-alpha-carbons of the hexaketide chain and oxaloacetate to afford the tricarboxylic acid unit . The potential hydrolytic enzymes, clz11 and clz13, are in close proximity to pks2 and may participate in product release . On the other side, the tetraketide arm is synthesized by a the squalestatin tetraketide synthase clz2 and enzymatically esterified to the core in the last biosynthetic step, by the acetyltransferase clz6 (By similarity). The biosynthesis of the tetraketide must involve 3 rounds of chain extension (By similarity). After the first and second rounds methyl-transfer occurs, and in all rounds of extension the ketoreductase and dehydratase are active (By similarity). The enoyl reductase and C-MeT of clz2 are not active in the final round of extension (By similarity). The acetyltransferase clz6 appears to have a broad substrate selectivity for its acyl CoA substrate, allowing the in vitro synthesis of novel squalestatins (By similarity). The biosynthesis of SQS1 requires several oxidative steps likely performed by oxidoreductases clz3, clz15 and clz16 (Probable). Finally, in support of the identification of the cluster as being responsible for SQS1 production, the cluster contains a gene encoding a putative squalene synthase (SS) clz20, suggesting a likely mechanism for self-resistance (Probable).
Sequence Mass (Da): 33691
Sequence Length: 293
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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A0A345BJP9 | MNVDTTSPQAPLAGVESKQDGASNEATAKAESTTHDQNESSSFDERPVHSALSERQRSALLAVASFAAAISPASTTTYYPAITTLANDLDVSITQINLSLPAYQIFQGLAPTVAAAFSDRFGRRPVYLVSLSINMAANLGLALQKNYASLMVLRCLQSSSSGGTVALGQAVMDDLITSEERGRYMAYLTLGLVMGPALGPLIGGLLSQYLGWRAIFWFLMILGGFFFLMVLTFFRETNRSIVGDGSVPPQKWNRSLVQIFRKDKLIANPESLAKKRISVNPLASIQILRNKENFIVCMYGALLFGGYASVISIFATQLEERYGYSQVQVGLCYLPFGVGSILSRWTAGKMIDWNFKREADKQGFKIVKNRQQDLSRYDIEKARLTVSFPMIFATCGFVVAYGWLMQYDTHVASVLVVVFLIANVFTGVLIANSALLNDLNPGNGAALGAAMNLTRCLMGAGGVAAVTPLINKIGIGYTATATAGVWVVTLPALYLVYSKGYTWRKAALEASSQDRRENPDVASGSP | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56950
Sequence Length: 526
Subcellular Location: Membrane
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A0A345BJQ0 | MVSTRGVLYYLLRPKELRPILQWKALHGLGHQRDEKNESPDVKACYQYLALTSRSFAAVCQQLDRELLMPICIFYLILRGLDTIEDDMTLSKEVKEPLLRNFYTTIYDQTWTFNDSGTDEKDRELLVHFDCVAREFHKIKDEYKIIITDITKQMGNGMADFVVSGDLTGIQKIKDYELYCHYVAGVVGDGLTRLFVEANVADPSLLKNPRLIESMGQFLQQTNIIRDVREDHDEVRHFWPKEVWSKYAQDFDHLVSPKPQDRKKALQCSSEMVLMALNRADDCLNYMAGVREQTVFNFVAIPQSMAIATLELCFQNPAIFDKNIKITKGATCQLMIDSTQDLQHVCQAFRRYARRIKKKNHPEDPHFHDINAACNKIDRFIDDRYPNLQDEQAKADTMYLAVLVLGVFGVVAAIL | Function: Squalene synthase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . Catalyzes the condensation of 2 two farnesyl pyrophosphate moieties to form squalene (By similarity). The presence of a gene encoding a squalene synthase supports the identification of the cluster as being responsible for SQS1 production and suggests a likely mechanism for self-resistance (Probable).
Catalytic Activity: 2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47890
Sequence Length: 415
Pathway: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.
Subcellular Location: Membrane
EC: 2.5.1.21
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A0A345BJP2 | MPSISTDFDVRPYEDVPAQTIALSVPDAAAPKHCPIQLLFWPVDGKSSFTRGYENLKEGLSRLLSDVPVLAGKLERGWKGDSRYLAVNISSDASVEFVYEDVSAEDIIPSYDNLAQNGFPTTGFRDILSPKMSLGPMVEGSPMMCAKLNMIKGGAILAYGFSHVLADGWANSELGRLWALHAAQVSQGIEFKKHKDATPDEDIRRRLSTLPEYDTDVPLDAFLQITPSEEATNFLHKDVLSAEKAKKKAREKMMATLLAAGEVPELPRFTFWRFTPEKLKELKQAAAGSDPDKWISTMDALAGLFWSRIALIQGQSSNGHQQSRCIFALDIRRRLQPPVPLGYIGNVFSPVDALCPLDELESDSLGLKAAAQSMRQANKGWAQSRWEAWLNKIMSLPLDQTLDTSQEFRLQKHNMYFNDYSAFQLNTASWGAPFGQPTRTRCLRSGLSGGAAGVWVCPKLPDGSLEVWLTSTAALQKSLFEDTMFNHYAEFVCQHT | Function: Acyltransferase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8-dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms . These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly reducing polyketide synthase clz14, followed by oxaloacetate extension and product release to generate a tricarboxylic acid containing product . The phenylalanine ammonia lyase (PAL) clz10 and the acyl-CoA ligase clz12 are involved in transforming phenylalanine into benzoyl-CoA . The citrate synthase-like protein clz17 is involved in connecting the C-alpha-carbons of the hexaketide chain and oxaloacetate to afford the tricarboxylic acid unit . The potential hydrolytic enzymes, clz11 and clz13, are in close proximity to pks2 and may participate in product release . On the other side, the tetraketide arm is synthesized by a the squalestatin tetraketide synthase clz2 and enzymatically esterified to the core in the last biosynthetic step, by the acetyltransferase clz6 (By similarity). The biosynthesis of the tetraketide must involve 3 rounds of chain extension (By similarity). After the first and second rounds methyl-transfer occurs, and in all rounds of extension the ketoreductase and dehydratase are active (By similarity). The enoyl reductase and C-MeT of clz2 are not active in the final round of extension (By similarity). The acetyltransferase clz6 appears to have a broad substrate selectivity for its acyl CoA substrate, allowing the in vitro synthesis of novel squalestatins (By similarity). The biosynthesis of SQS1 requires several oxidative steps likely performed by oxidoreductases clz3, clz15 and clz16 (Probable). Finally, in support of the identification of the cluster as being responsible for SQS1 production, the cluster contains a gene encoding a putative squalene synthase (SS) clz20, suggesting a likely mechanism for self-resistance (Probable).
Sequence Mass (Da): 55032
Sequence Length: 496
Pathway: Secondary metabolite biosynthesis.
EC: 2.3.1.-
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A0A345BJN8 | MAASTKPTTKLSTEEDDVSRRDSESSADFMKSNEELQATMIPEDDGANPATGQPTWTILSDTEIKSVLVVASFAAAISPFSTSTYYPVVTAIARDLGVSVSKINLTMSSYQIFQGVAPTITAAFADTYGRRPMFLVCFVTYFVANVGLALQNDFTTLLVLRCLQSTGSSGTFALAQAVTADITTRAERGRYLIYATLGSTLGPFIGPVIGGLLVKFLGWRSVFWFLLCMGTVFALLIFIFFGETARPIVGDGSIPPQSWNRSYLQMRSKGVSNLKPNLASLERRKSRPNPLTSLALLWDRENFILSVSGGLLYAGYSSVTSVLASQLQQRYKYDAVQVGLCYLPVGFGSLLAYRTTVRLMDWNFEREAKKQGLVIVKNRQTDISRFDLEKARLGFVFPMILVCSGLLVAYGWQMHYHAPLAPILVTMFLIAIILTGVMNAIAALLTDVNRENAAAVGAAMNLTRLLLGAGAVAVVGPLNKSAGIGWTATVTAGFSYNVNTKGIQTKRRAAAIFEVSRATLHRRCDGKRARRDCQPNSKKLIQQEEEVILKYILDLDTRGFLPTYAAERGMADKLLSTRGGSPVGRDWPRNFVKHKAKYSILDEDVYSFDEAGFMMGKITTQLAVTGSERRGRPKAIQPENREWVTLIQGINAAGWAISPFVVFAGQHHLSAWYEEDIPRDWAIAVSDNGWTTNEIGVEWLEHFIKYTDGKAVGVRRLLIFDGHESHHSLKSRELCKENNIYTLYMPPHSSHLLQPLDIGCFSPLKRAYSREIEALICHHINHITKLEFLPAFKAAFQRSFTSANICSSFRGAGLVPLQPDIVLSKLDVRLLTHIPAASPEAPWEAKTPSNRKKKQIQKRGTLTKGEGEDTLAQKEADQQIEREQRQGGEQSGRSRQALARSLEALEVGGVAHSLNGSFV | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 101381
Sequence Length: 919
Subcellular Location: Membrane
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P0DQV5 | CCSALCSRYHCLPCC | Function: Slowly and reversibly inhibits human nicotinic acetylcholine receptors (nAChR) alpha-7/CHRNA7 (IC(50)=45.7 uM). It is unknown whether it inhibits nAChRs by a competitive or a non-competitive mechanism.
PTM: Has a free C-terminus.
Sequence Mass (Da): 1662
Sequence Length: 15
Domain: The cysteine framework is III (CC-C-C-CC). Classified in the M-2 branch, since 2 residues stand between the fourth and the fifth cysteine residues.
Subcellular Location: Secreted
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P0C1T9 | GRCCDVPNACSGRWCRDHAQCC | Function: Mu-conotoxins block voltage-gated sodium channels (Nav). This synthetic toxin moderately blocks rNav1.1/SCN1A, rNav1.2/SCN2A, rNav1.3/SCN3A, rNav1.4/SCN4A, rNav1.5/SCN5A, and mNav1.6/SCN8A . This block is very slowly reversible . Causes seizures when injected intracranially into mice.
Sequence Mass (Da): 2441
Sequence Length: 22
Domain: The cysteine framework is III (CC-C-C-CC). Classified in the M-5 branch, since 5 residues stand between the fourth and the fifth cysteine residues.
Subcellular Location: Secreted
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P01523 | MMSKLGVLLTICLLLFPLTALPMDGDEPANRPVERMQDNISSEQYPLFEKRRDCCTPPKKCKDRQCKPQRCCAGR | Function: Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin potently blocks rat Nav1.4/SCN4A (IC(50)= 19-110 nM) . It also moderately blocks rNav1.1/SCN1A (Kd=260 nM), rNav1.2/SCN2A (IC(50)=2.7-17.8 uM), and mNav1.6/SCN8A (IC(50)=680 nM) . The inhibition is reversible. In vivo, induces paralysis to an isolated skeletal muscle preparation from frog (cutaneous pectoralis) within a few minutes .
PTM: Hydroxylated; hydroxylations improve the ability to block Nav1.4/SCN4A sodium channels but does not affect folding.
Sequence Mass (Da): 8586
Sequence Length: 75
Domain: The cysteine framework is III (CC-C-C-CC). Classified in the M-4 branch, since 4 residues stand between the fourth and the fifth cysteine residues.
Subcellular Location: Secreted
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P85017 | KCCMRPICTCPCCIGP | PTM: Reg12e and reg3e are conotoxins with identical sequences, but different post-translational modifications. Reg12e is C-terminally amidated, while reg3e is not.
Sequence Mass (Da): 1728
Sequence Length: 16
Domain: The cysteine framework is III (CC-C-C-CC). Classified in the M-1 branch, since 1 residue stands between the fourth and the fifth cysteine residues.
Subcellular Location: Secreted
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O85728 | MLVVAFKPGHDGAVAAIDDRRLLYSLESEKDSRPRYSTLLPTTFLDIAERLGAIPDVVALGGWADLRPRGVVYTGAGYEGTQEPTVTTSRFFGKEVKFFTSTHERSHIYMALGMAPKDGAPLKSVLVWEGDVGAFYLVDSEHRIIRTIPVMTGPGARYSFLFGLADPTFPDTGGKPRLNDAGKLMALAAFGDSADASPDIRHVVERVLKQDSMYPAPKAEYRDSVLHNAGVESEECKIAAALLTERLFETFAEVARRELPEGTPLYISGGCGLNCDWNSQWAQLGHFSSVFVAPCTNDSGSALGTAIDALTTFTGDPHIDWNVYSGLEFVHDTRPDPARWESVPLDHAALSSALAAGRVVAWVQGRWEIGPRALGNRSLLAEAFSSASRDRLNTVKMREDYRPIAPVCRVEDLGKVFHEDFEDPHMLYFRRVREESGVRAVTHVDGSARCQTVTGTSNPELHRLLSVFAQGQGLGVLCNTSLNFNGDGFINRMSDLVRYCEWREIQDMVVGDTWYRRIAGS | Function: Catalyzes the carbamoylation reaction in the cephamycin biosynthesis.
Sequence Mass (Da): 57370
Sequence Length: 521
Pathway: Antibiotic biosynthesis; cephamycin C biosynthesis.
EC: 2.1.3.-
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Q04733 | MTSVRGASKTGRTSKTSTATTALVLACTAHFLVVFDTSVITVALPSVRADLGFAPASLQWVVNSYTLAFAGLLLFGGRLADIHGHRRVFLGGLAVFTLTSLIGGLATSPASLIAARAGQGAGAAVLAPLAVTMLTTSFAEGPRRTRALTISTAVALVGGASGNLLGGVFTEFLSWRSVLLVNVPIGIPVLFLAARVLAGPRKRPWGRVRLDLPGAVLATAGLTLLTLGVSQTHEHGWGEAAVAVPLAGGLLALLAFVVVEARFAASPLIPPRLFGLPGVGWGNLAMLLAGASQVPVWFFLTLSMQHVLGYSAAQAGLGFVPHALVMLVVGLRVVPWLMRHVQARVLIAAGAAIGALGFWWQSLLTPDSAYLGGILGPAVLISIGGGLVGTPLARTVTSGVGPLDAGAASGLMNTTRQFGGAFGLAVLLTVTGSGTSGSPAELASHYGDAFVGIAVFMLAIAVLTPVLPALARSTPPGVIHVSPVAR | Function: Involved in cephamycin export.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49325
Sequence Length: 486
Subcellular Location: Cell membrane
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