ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q8TUQ0 | MTIRALVVDDSALIRKVLSDILNEDPKIRVVGTAVNGKDGLEKVIKLRPDVVLLDNVMPVLDGLKTLARIMKEQPTPVVIVSALGERAEEITLTAFEYGAVDVIEKPSGILSQSMPEMAEEICRKVRTAPKANLKNLECMRDSEPLNPEKRETKENRVLKKAAPRNILAIGASTGGPRALEKLICSLPAELPAAVLVVQHMPPGFTASLSKRLDSKSALRVKEAQEGDRVEDGTVLIAPGNYHMEIVRNKVNSLEEETIHLSCGPKELGSRPSVNVLFRSIASVYGSRVISLVLTGMNCDGADGAEEIKKMGGKVIAEARSSCVVYGMPGEIVRRNLADLVLPLDKMAEEIIRIIG | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 38594
Sequence Length: 356
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
|
Q2FQU2 | MIRVLLVDDSPVTLMVLQSILEKEPDISVIGQAKNGKEAIILASRLAPDIITMDINMPDLDGFATTRQIMERTPVPIIIVSGIDNLEEIRASFRAVEAGALAVFRKPPAYGDPDYEEAVSEFVNAIRTYSEVKVIRRRSNHLKVPKPEASTIQIPFQIHQDIRVIVIGASTGGPQVIQEIISNLPLGFPLPLVLVQHMSPGFIEGLALWLTESTGFPVSIAREGEVLQPGKLYVAPDGIHTGVTSDLRFSFSISPPEHNLRPSVSYLFRSAAKNLGSHVLGILLSGMGSDGAEELLQIRQNGGCTIIQDRDSSFVYGMPGAAEMLNAGMFSLPPVEIARFLRSLSERRQL | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 38184
Sequence Length: 350
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
|
Q1D225 | MGKKVSVLVVDDSLICRQLICEALSKDPDIEVVGTCADGKQAVEMTKELRPHVITMDVDMPVMDGLTATEHIMAECPTPILVLTADPRSQAPELTYRALELGALALQIKPAIDAGPDAWNLVREIRLLSSVRVIRHLRRPQRGPLLPPRVATSVLPAVSMGVVVVAASTGGPQVLFKMLSELPADFPAPIVIVQHINAAFAESLAGWLAGASKLKVRLAQDGEPLMPGHVLIAPPGQHTVIPFRGRVGIKLGVERDGHMPSGTVLLESAARTYGRRAVGLVLTGMGADGADGLLAIKQAGGLAVAQNEESCVVFGMPGAAVERKAVDHLIHGDEVAATLVRLARGESLSVGR | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 37118
Sequence Length: 352
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
|
Q6LTM2 | MTVKVLVVDDSSFFRRRVSEIINADPRLEVIGNAVNGKEAVELVKKLQPDVITMDIEMPVMDGITAVREIMKVLPTPILMFSSLTQEGAKATLDALDAGALDFLPKKFEDIARNRDEAISLLQKRVGELARKRMFMRRPLRTTPAVAPASRYSAPVNAALTREAALTTAARTTAARVTPTSTTRQTMHSAVAAKPMARFKASGKKYQLMAIGTSTGGPVALQKILTQLPANFPYPIVLVQHMPATFTAAFAARLNNLSKISVKEAEDGDTLRAGVAYLAPGGKQMMLEGRPGSARLRILDGGDRMNYKPCVDVTFGSAAKVYNDKVLSMILTGMGADGREGARMLKTHGSTVWAQDEESCVVYGMPQAVAKAGISTEDLPLERFAERILVEVGR | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 42665
Sequence Length: 394
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
|
Q9I6V9 | MPISVLVVDDSALIRSLLKEIIQADPELRLVGCAPDAFVARDLIKQHAPDVISLDVEMPRMDGLTFLDKLMKARPTPVLMISSLTERGSEATLRALELGAVDFIAKPRLGIAEGMQAYAEEIRAKLKTVARARLRRRAADAPAPPESAAPLLSTEKIIALGASTGGTEALKEVLLGLPAHSPGVVITQHMPPGFTRSFAERLDRLTRLSVSEARDGDRILPGHALVAPGDHHMEVQRSGANYVVRLNRQAQVNGHRPAVDVMFESLARCAGRNLLAGLLTGMGKDGARGLLAIRQAGGYTLAQDEATCVVYGMPREAVELGAAEDVLPLERIAAALLQQAARRGSGNRL | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid (By similarity) . Acts on the methyl-accepting chemotaxis protein McpB (Probable). May be involved in a specific chemotactic response, which takes place during infection and is required for P.aeruginosa pathogenicity .
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 37347
Sequence Length: 349
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
|
Q1MC14 | MAKKIRVLIIDDSASIRQTLTHVLEQDPDIEIMAVASDPFMAARKLQEEIPDVITLDVEMPRMDGITFLRKLMSQRPIPVVMCSSLTEAGSETLLQALEAGAVDVILKSKIGAADSLSDDAMRIREVVKSASHARLSNVRRAAGTIRSASVEGPAKKLTADVMLPPPTGRAMAKTTEMVVCVGASTGGTEALREFLEELPANAPGMVIVQHMPEKFTAAFAKRLNGLCEVEVKEAVDGDPVLRGHVLIAPGDKHMLLERQGARYYVSVKTGPLVSRHRPSVDVLFRSAARSAGSNAMGIIMTGMGDDGARGMLEMHQAGAYTVAQDEASSVVFGMPKEAIAKGGVDRILPLDQIAREVLITQQKF | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 39206
Sequence Length: 365
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
|
Q8TLH2 | MSDDILFVSNGNGKAIFLTSRAVLVKSFCSLSKTCSFKDSCQSCEIVDAAKSYLMGKKSDLNVKSLDGELSAGIGEYKIGKNVLLKVMGLGSCIGVILSDVSTGICGIAHVLLPGASNSGEAKYAETAIENMFEDMIRMGARKNRITAKFAGGAQVFKHMSLDILKIGDRNAISVEETLVKRNIPILAKDVGGEVGRNVIFNPVDGSMIVKYTKGEVLWL | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 23520
Sequence Length: 220
EC: 3.5.1.44
|
Q1GM98 | MDKVEVSELHVRIGQVKIGSPGQVLTAILGSCVGIGFFFPQRQIYGLAHCLLSQSSSQPVASSAAQTGRTREDGQLVGNGRHVDKAIESLLKMMDIQDEERRQLRVVLAGGANMSMPFDTPPSQLVGSVNAKFARQAIRSAGLRLLGDDLGGLNGRRISINCDSGEYDIQQIPRLGGTV | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 19173
Sequence Length: 179
EC: 3.5.1.44
|
Q8EEQ1 | MENMAFNQRTVVMIGPGEHYVTAKNEVIKTLLGSCVAVCLYDPKAQVIGMNHFLLAADRRKFTHFLDSRAGYYGVHAMEILINAMLKRGAQRKYLQSKIFGGANVLSLCADNILNHYDIGGMNIDFVRHFLQRERIPIISEDIGGHCGRVIYFDPTDYSVYRSLIEHKYEEIASLQDEEYRYFNQASEDIHSSGVPVVIWSD | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 23028
Sequence Length: 202
EC: 3.5.1.44
|
Q2LSL4 | MNSKAIKPSCEYFLLPGYIFMSPEPYLISTVVGSSVAVALWDADSKLGGMLSFLYPFRESSAESTAIYGNVAITYMVRMFREEGAKKKNLRSQIFGGAESDCCEADQIAHENVKTARSVLKKHGIKVISEDVGGRLGRKIVYNTFQNEALIYKVNTLRNSDWYPYDGQGRQA | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 19184
Sequence Length: 172
EC: 3.5.1.44
|
Q47GX8 | MSAAPSELHEVFLNPGEFHFGESNTRISTLLGSCVSITLWHPRKRIGGMCHYMLTERKRPPNAALDGRFGSEAFELFLQHVAAAGTRPGEYQAKLFGGANMLTGPTGKQMDIGPRNVALGRQLLAANHIALMVEHVGGSGRRKLHFDVWSGDVWLAFPQGADAEIRNAHG | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 18515
Sequence Length: 170
EC: 3.5.1.44
|
Q747R4 | MSRIVSVGISEFKIASAPTILMTYGLGSCVGIALHDPVALTGGLAHTLLPAPVRGMDSMVKSAKFTCWAVDLMVEELIKCGCVAERLVAKLAGGATMFEPQHRTTHSGIGERNVTAAKEALERRGIPLVASDTGDDYGRSLEFNTVTGVITVRALQRPIKRM | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 17253
Sequence Length: 162
EC: 3.5.1.44
|
A5G222 | MTPVAAASPDYARRINIVQGEHRVEHDPEAVLCTILGSCVAACLWDPGASVGGMNHFLLPGDAHAQAGGGGAAMRYGAYAMELLINDLLRHGARRDRLKAKLFGGACLMKGLTDIGRLNADFAERFLAAEGIEIVGGSLRGERGRRIQFWPVSGRARQTLLAADQPALLRAEPDLRTLRAPPPSGAVELF | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 20278
Sequence Length: 190
EC: 3.5.1.44
|
Q5WFS5 | MTKGETISIGEWKVVKGEGVLRTCGLGSCIGIVLYDQERVIAGMVHVMLPDSTKARKGANPWRYADTAIASLQAELKKQGARKLCAKMAGGAQMFKHAVKREFMQIGERNAAAARETLARLGITLVAEDIGGTKGRTIQYDVKTGELAVRTVHHGQMIL | Function: Deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity).
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 17208
Sequence Length: 159
EC: 3.5.1.44
|
O29224 | MGSEILVGIGEFRVAKGAVLKTIGLGSCVGIALYDPKLRLGGLAHVMLPQSGNGTKRSAKYADHAVEMMTEAMERLGSDRKRIVAKMAGGAQIFKHMTMDMLRIGDRNAEAIRTILRDYGIRIVSEDLGGDEGRTVYFFTNDGRMLVKYSRGGELWI | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 17196
Sequence Length: 157
EC: 3.5.1.44
|
P40404 | MSTTEAVVIKVGIADVKIARFPDTIRTSGLGSCVGLVLYDKEKQTAGLVHVMLPDSTLSKTAELNRAKYADTAVQTTIDMLIEAGCRKFALKAKLAGGSEMFKFKSTNDLMKIGPRNVLAIKEQLSLFNIPIISEDTGGSSGRTIEFEPKSCMLHIRTVKQGEKTI | Function: Deamidates 'Gln-593' and 'Gln-594' of the chemoreceptor McpA. In addition, deamidates other chemoreceptors, including McpB and McpC. CheD-mediated MCP (methyl-accepting chemotaxis proteins) deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase. CheD is absolutely required for a behavioral response mediated by McpC but is not required for the response to asparagine mediated by McpB. CheD is necessary for the generation of wild-type prestimulus CheA autophosphorylation levels. Also required for methylation of MCPs by CheR. In addition, enhances the activity of CheC 5-fold in vitro.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 18008
Sequence Length: 166
EC: 3.5.1.44
|
Q6MJE9 | MLPVEHHVRIGQILIAENGEVLKTVLGSCVGIALVWRRQNKWALAHCLLPYPETFKEDKEARYVSQTIPRMLERMGATMADVSELEAIVAGGGRMMDGDKNYIKFVVGDENLKAAKAVLEKHRIRIVAFEPGGEQGTKMRIAGDGDYSIEKLPKTA | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 17304
Sequence Length: 156
EC: 3.5.1.44
|
O51551 | MLNHFNFKLKRDVTIIVPGEAFVSNKRVISTILGSCVAVVLCDESNNLIGMNHYVLVKSDLDISPDQRGRYGIYAIPMLINAMLENGASKSNLKAKLFGGTNFMAKGSVKVGLENSEFAVNTLNKYRIPILAKDFDQSKSRKIFAFPENFKVIVEYPDGTKVF | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 18141
Sequence Length: 163
EC: 3.5.1.44
|
P07364 | MTSSLPCGQTSLLLQMTERLALSDAHFRRISQLIYQRAGIVLADHKRDMVYNRLVRRLRSLGLTDFGHYLNLLESNQHSGEWQAFINSLTTNLTAFFREAHHFPLLADHARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVLEKARSGIYRHEELKNLTPQQLQRYFMRGTGPHEGLVRVRQELANYVDFAPLNLLAKQYTVPGPFDAIFCRNVMIYFDQTTQQEILRRFVPLLKPDGLLFAGHSENFSHLERRFTLRGQTVYALSKD | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32849
Sequence Length: 286
EC: 2.1.1.80
|
Q9KCB8 | MADDYNWFIEQVKERTGIDLNLYKETQMKRRLIALREKRNYQDFRSYFTAMTNDDTLQNEFLERMTINVSEFFRNRKRWDVLDETIIPQLLKEKKRLKVWSAACSTGEEPYTLAMILQKHLPLKDVSILATDIDRAILQQAKVGYYTERSLKEIPVELKEGFFTKDRAGYYVSNELKQAVTFKQHNLLADRFERDCDLIVCRNVLIYFTEEAKRELYHKFSEALRPGGVLFVGSTEQIFEASKYGLETNETFFYRKV | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30546
Sequence Length: 257
EC: 2.1.1.80
|
B0R4J5 | MTDFQTLLEFIETETGFATSYYDESYLDRRVSARMRRRGVEEYAGYLTLLEEDDDDERAELLDTLSVNVTEFFRDEKVWTALRDVLLELADTVRSIDIWSAACADGREPYSLAMLALDAGLDPRNVSILATDIDEDALARARAGRYESTRTADISDQLGFLDNPQEYVDREGDRAFVVNDRVKDLVTFERHDLITGDPKSGFDLVACRNVCIYIDKQYKLPILDTVSKSLREGGHLVLGQTETLPGEVKERFEAEDPRIRIYSRVADT | Function: Catalyzes the methylation of several Htr transducer proteins (methyl-accepting chemotaxis proteins) to form gamma-glutamyl methyl ester residues.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30533
Sequence Length: 268
EC: 2.1.1.80
|
Q9XDE8 | MIPDLEKDYLYFTRVVKRDLGLDLALYKETQMKRRILSFIVKKKYITFGEFFKHLKKDAVLLDEFISLITINVSSFFRNRNRWDALEKQVLPRLLEDSRGKLRVWSAACSSGEEPYSLAMMMERSVGTRHYDILATDLEPAILKRAVIGEYQSRQMEELSEQERHTAFVEKGDTYQILPKYRKSIRFRRHDLLTDYYEKGFDLIVCRNVLIYFTAEGKHQAYQKFAESLRRGGVLFIGGSEQILNPADYGLATLNNFFYIKT | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30820
Sequence Length: 262
EC: 2.1.1.80
|
Q2KCH9 | MIYSDAGIFLNETKASLVYSRLSKHIRNLGLSGFREYCELVASPAGAAARREMLSHLTTNFTRFFRENHHFEHLRDHVLPELLQRARSGGRVRIWSAASSDGQEPYSIALTVLSLMPNVADYDFKILATDIDPKILAIARAGAYDESALETVSPAMRKQWFSEVEVQGRRKFQVDDRVKRLITYNELNLMAQWPFKGKFDVIFCRNVVIYFDEPTQMKIWQRFAGLLPEGGHLYIGHSERVSGEAKHVFDNIGITTYRYTTKGLGRKA | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30638
Sequence Length: 268
EC: 2.1.1.80
|
Q9WYT5 | MQEERSEKKIGPFKFQSNFEWKEFPQEEFEWFVKEVEKRFGLNLSSYKPQRVKRRTELLLRKYNVGYREYLNMLIKDKKYLDEFMDKMTINVTEFFRNPEKWWELRDEIIPLIAKNSLRMKFWSAGCSSGEEPYSLAILVHELNLSYKTRILATDIDIGVLRRAQEGIYEERAFVSTPKEYLEKYFEKLPDGRYRIKDSVKKIVEFKRHDLLKDPFEKNFDLIVCRNVVIYFEPEAKNELYRKFAESLKPGGFLFVGNTERIFNYKELGFEIYKPFIYRKVK | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34225
Sequence Length: 282
EC: 2.1.1.80
|
P37599 | MSLQQYEILLDSGTNELEIVKFGVGENAFGINVMKVREIIQPVEVTSVPHSHQHVEGMIKLRGEILPVISLFSFFGVEPEGSKDEKYIVTEFNKRKIVFHVGSVSQIHRVSWEAIEKPTSLNQGMERHLTGIIKLEDLMIFLPDYEKIIYDIESDSGVDTYNMHTEGFDERRTDKKLIIVEDSPLLMRLLQDELKEAGYNNIASFENGKEAYEYIMNLAENETDLSKQIDMIITDIEMPKMDGHRLTKLLKENPKSSDVPVMIFSSLITDDLRHRGEVVGADEQISKPEISDLIKKVDTYVIE | Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl-accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis.
PTM: Phosphorylated by CheA.
Sequence Mass (Da): 34634
Sequence Length: 303
Domain: Consists of two domains: an N-terminal CheW-like coupling domain and a C-terminal two-component receiver domain.
|
P21227 | EQCGRQAGGATCPNNLCCSQYGY | Function: Defense against chitin-containing fungal pathogens.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 2424
Sequence Length: 23
EC: 3.2.1.14
|
Q9D9G3 | MADFDEIYEEEEDEERALEEQLLKYSPDPVVVRGSGHVTVFGLSNKFESEFPSSLTGKVAPEEFKASINRVNSCLRKNLPVNVRWLLCGCLCCCCTLGCSMWPVICLSKRTRRSIEKLLEWENNRLYHKLCLHWRLSKRKCETNNMMEYVILIEFLPKTPIFRPD | PTM: Palmitoylation in the CHIC motif is required for membrane association.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19282
Sequence Length: 165
Subcellular Location: Membrane
|
O81862 | MSSTKLISLIVSITFFLTLQCSMAQTVVKASYWFPASEFPVTDIDSSLFTHLFCAFADLNSQTNQVTVSSANQPKFSTFTQTVQRRNPSVKTLLSIGGGIADKTAYASMASNPTSRKSFIDSSIRVARSYGFHGLDLDWEYPSSATEMTNFGTLLREWRSAVVAEASSSGKPRLLLAAAVFYSNNYYSVLYPVSAVASSLDWVNLMAYDFYGPGWSRVTGPPAALFDPSNAGPSGDAGTRSWIQAGLPAKKAVLGFPYYGYAWRLTNANSHSYYAPTTGAAISPDGSIGYGQIRKFIVDNGATTVYNSTVVGDYCYAGTNWIGYDDNQSIVTKVRYAKQRGLLGYFSWHVGADDNSGLSRAASQAWDATTATTRTIQKV | Function: Can hydrolyze glycol chitin and chitin oligosaccharides (e.g. N-acetylglucosamine) (GlcNAc)4, (GlcNAc)5 and (GlcNAc)6 . Hydrolyzes N-acetylglucosamine oligomers producing dimers from the non-reducing end of the substrates .
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 41128
Sequence Length: 379
Pathway: Glycan degradation; chitin degradation.
EC: 3.2.1.14
|
Q9FRV0 | MRSLAVVVAVVATVAMAIGTAHGSVSSIISHAQFDRMLLHRNDGACQAKGFYTYDAFVAAANAFPGFGATGSTDARKRDVAAFLAQTSHETTGGWATAPDGAFAWGYCFKQERGAAADYCTPSAQWPCAPGKRYYGRGPIQLSHNYNYGPAGRAIGVDLLRNPDLVATDPTVSFKTALWFWMTAQAPKPSSHAVITGKWSPSGADRAAGRAPGFGVITNIINGGLECGHGQDSRVADRIGFYKRYCDILGVGYGDNLDCYNQRPFA | Function: Defense against chitin-containing fungal pathogens. Binds the hyphal tips of fungi and degrades nascent chitin.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 28302
Sequence Length: 266
EC: 3.2.1.14
|
Q6YXN5 | MKLAYWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTASIVDRHVLARGSQEKVVDNINRKDKEERPDLIVLTPTCTSSILQEDLQNFVDRASTTSNSDVILADVNHYRVNELQAADRTLEQVVRYYLEKARRQGTLDQSLTKEPSANIIGIFTLGFHNQHDCRELKRLLQDLNIKVNKVIPEGGSVKDLQSLPKAWFNLVPYREIGLMTAIYLEKNFGMPYVSITPMGIVDTAECIRQIQKHVNNLIPNKKVDYEPYIDQQTRFVSQAAWFSRSIDCQNLTGKKAVVFGDATHAASITRILAREMGIRVGCTGTYCKHDTEWFKEQVQGFCDEILTTDDHTEVGDMIARIEPSAIFGTQMERHIGKRLDIPCGVISSPVHIQNFPLGYRPFLGYEGTNQIADLIYNSFTLGMEDHLLEIFGGHDTKEVITKSLSTDTDLTWNYESQLELNKIPGFVRGKIKRNTEKFARQNNITTITVEIMYAAKEALSA | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
Catalytic Activity: 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 57830
Sequence Length: 510
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
Subcellular Location: Plastid
EC: 1.3.7.7
|
P29683 | MKPLKLKRLIMENNKSHATNLSLGGPFQGNCMPINQYFSKNQPNRGSSSSEKRSSLLPLWESKNAADGFSIVSHNVLLDGATTILNLNSFFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNALGVMIFAEPRYAMAELEESDISAQLNDYKELKRLCLQIKQDRNPSVIVWIGTCTTEIIKMDLEGMAPRLETEIGIPIVVARANGLDYAFTQGEDTVLSAMALASLKKDVPFLVGNTGLTNNQLLLEKSTSSVNGTDGKELLKKSLVLFGSVPSTVTTQLTLELKKEGINVSGWLPSANYKDLPTFNKDTLVCGINPFLSRTATTLMRRSKCTLICAPFPIGPDGTRVWIEKICGAFGINPSLNPITGNTNLYDREQKIFNGLEDYLKLLRGKSVFFMGDNLLEISLARFLTRCGMIVYEIGIPYLDKRFQAAELALLEQTCKEMNVPMPRIVEKPDNYYQIRRIRELKPDLTITGMAHANPLEARGITTKWSVEFTFAQIHGFTNTREILELVTQPLRRNLMSNQSVNAIS | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
Catalytic Activity: 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 60868
Sequence Length: 545
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
Subcellular Location: Plastid
EC: 1.3.7.7
|
Q20EX8 | MRNTVLNTLNAFPTQLGSNKSTLSSKIFHSYLGVLRPPTPLNTSMEVLGEGAHQNREAKRSSLRFEFCSALKECQKGKVPFGSSLRLEAAENLTFECETGNYHTFCPISCVRWLYQQIADSFFLVIGTKTCGYFLQNAMGVMIFAEPRYAMAELEEGDIAAQLNDYKELKRLCLQIKHDRNPSVIVWIGTCTTEIIKMDLENLAKLIEAELKVPIVVARANGLDYAFTQGEDTVLASLVNRCPSSHESSLDSMKLPSGGREKQINDVNTSKPEGYLSEVISLTSNGDDINKKSCTKPVPKKSLVLFGSVPNSVQTQLTLELAKQGINVDGWLPSRYSELPVLNKDVYVCGINPFLSRTATSLMRRRKCHLISAPFPIGPDGTRRWIEKICTVLNTDKSSTSLEEVQKNLQQREEKVWKSLQSYLDLVKKKSVFFMGDNLLEISLARFFIRCGMIVYEIGIPYMDRRYQAAELALLEQTCLEMNVPLPRIVEKPDNYNQIQRIRELQPDIVVTGLAHSNPLEARGVTTKWSTEFTFAQIHGFANSRDVLELITRPVRRNQNLDALGFTSLVKN | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
Catalytic Activity: 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 64369
Sequence Length: 572
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
Subcellular Location: Plastid
EC: 1.3.7.7
|
C4QXE9 | MVKESKFSYNSKDEKKYSLGKTFRGDIFNVPETHDMVRSLFDPTVKKSVSDYLIVLSLFINGIVYYYSPVTWRIPVFIVLYSFWRLGYNLGIGILLYKQSKSHSMFHWLKQIQINGGWAKKFVELELSSKLNAQQLNSVPDEFKTWIVFRSLVNLILMNDFTTYMCLVFACSDGAFNQSLSLIFLRWVLGISFFIFNIIVKLNAHLIVKDYAWYWGDFFFRLHNNEELIFDGVFDLAPHPMYSIGYAGYYGCALMTKSYTVLIMSIFGHLLQFLFLNYVETPHIEKIYGDDNLSENTISVNKRDDSVFIGTGGKPLVMLTKNFNWLRTNDIFTVVLALYASIVPIFLPASYNNSIIILAIVVKIGTSFVLNSVLYLQSRFKSWTLSFIKNYGTINISILDNKELLERLSFQNWTLLQNNTLVLNYSMLFTISVREVMYNEKFWQTEWLPLRFILAALMILGQFLTVHQMIDSIGLFGWYYGDFFIGVLSSHKSEVTTLSRSGIYHFLNNPERVTSNLTVWALYLLFNNSNKIFLVIALLFTMNNLIVLNFIEKPHMVKLYGEQNVLKHTSGIEKSINSLFLPNHVQGTIVKLSGSIDKVIQDSSKVIDEFIRNKHNQKPKELSLKKRRNSFQQVIELIRGSTDDTLTINLQELNDQGQLQLLNLLRKDDTDFYNLGDPIKVEWNMEDHKGKDKAWIGLYNIFQTSETRTKTLVSSKGYWIPIHREKYINLSDKIRNEEDCILEDELNRGVVQFSAELLPWVPGTYELRLHANEKHEVLAISKPFDIVVKKIDVPTSDDIGDERLEDFANKLYQGFVSKLFPAVESIEDESNWFLQMHIKENARQVEKLCSTLSQSCGVHLTKKAIVDEKCLKDLSFKISKLRKMLDELML | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 103146
Sequence Length: 890
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.1.1.17
|
B0D4E6 | MTSSQSFLRQRKPQANDETESELHNTPEPTKQDVVWGKTPGGEVFRVPTTHDVITTLFNPRYKKSHLDLLNLTLLGFQLVLFFILPRRASQIFFLFYFAFWRGAYDAGLGWVLTKQSKKKWIVREVQRLGWLDEKRRPAVRNWIRKQLADKMGKDYSFDDLPLEYNTWLLFRQAVDVILVNDFLSYCMFAFSCFRVPEGLSVLALLILRRWLGGFLLIAFNLWVKTEAHNVVKDYGWYWGDVFFQRGNLVFDGVFELAPHPMYSVGYAGYYGLSLIAGSYAVLFVSLAAHAAQFAFLVFFENPPVAASYKKISRHVSQPSNASSNGDIEMDPNTRSLISSPRKSATSQHDLLNKYFRRDVVVLRNLDLLRSTDAMLVLIIAYALMISFLPTLSARTMLALHFLHALAWCMIHYVGLGLILQAQSKTKFLVRHFMKNYHYSQNDGGGGAIVEAFTNWKAIYNLSMCMTYVSCVGVVWKSYSLPHDWTVGNELLRHTLGALLVGLHVWASMESFEVLGVFGWFFGDFFMEEFPTHLEYTGIYRYLNNPEAMGGAAWFGLALISGSKLVLSLAVIRHLANWWFLSSVENPHMRKLYGDSLRKDAGFVKVIKNHAPELKRVAREVKGTFDKVFEETADAVEDFLAKCERSSGPRISEVVQETKVLLQQSRERLVITRVSNDISAYDSSKYHVSISPSSLTGERTFHLGEPITIKWQAPHKHSRKDWIGLYRVGANKSNTVTKTSSMGMWLPVHGEEWDGDVPLGLKRVPSKHLESENGVVTFKGNTLPWLVGHYEVRYHHDGKYNVMSMDGPLEIFVDKPSDMTFSSVRNSLMRIVPLCLDSDPSLIPFSCKDRDPDDFSFWSEHQAKRICAAIKQVFNVDYAPEVVVADANLTALANRILISKEILSTRSDT | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 103544
Sequence Length: 909
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.1.1.17
|
C5DGB6 | MIKERKPSKSRAPGKGHKQIPGVAKESQPIARTRTGNVEFTPAKTHDMVRSLFDPTLKKSFLECWISLAILSNVVLCYFMATKFGASFTKKFFLWQYVFWRLCYNVGIGVVLHFQSNYETLTNFAKMRSLFSKKNQQWLARFCRFEIESKMPNTYCLEEYPEEFNVWLLFRQFVDLILMQDFTTYILFVVLSIPKTVLSSHTVSFALGVIMILFNVWVKVDAHRVVKDYAWYWGDFFFFQDSKLVFDGVFNVSPHPMYSIGYMGYYGLSLISGDYKVLLVSIGGHLLQFLFLKYCENPHIEKIYGSDAVENDNAHIDELLVKENPNYSKPLITKGLWFTNVDKLRLTDYFTILTVASIVLFTFFLKPSTKALFWATLVAKITTSLFISLVLHKQSTSKWFTRLFLKNGYTQVHSFYQWQFLYNYCLTVSYTLLILQTWSQFRHLESRNYTQIIFGFLLCWLQKWCDDEILTAISEFGWFYGDFFLTNYISSRKLNSRGIYRYLSNPERFLGVAGCWGAVLITHFSPYNLILAALWTAANIALVKLVEEPHVSKVYGTSERKSGVSKTLMGFKPIRRFSEIMDKMELRLVRHLTSNDSPFEEEAPTSEEAQWNEVVQLALQSVTANLAPNCEFKLGDGKCDTFIIPGPVEAHWKLPSKLYNNDDWIGLYKVFETGEDRQRTRVSSNGRWTGTNEAAFPYSGRPKKSIVKFQRTGDFVNGTVKFDHSLMFYEEGVYELRYHSGNTHKVLMISQPFRLSLPIVKAESAEELSEGLHQFLAEVHALDGNSFNPNSNRYLGDRFLKGLIKKASGVDLSVKYLRRINYDVSIIGKRVQEIKAVLENLE | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 97438
Sequence Length: 842
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.1.1.17
|
A8PRN6 | MKAESSSMAEWHASEGLRQRYALDEAKQGDASRKESVQDELTDTKDDPAAEAMGGSPSMVLGRTPDGRLFHVIDTPDMVTSIFRLDRPKAPLDILTLVLLLWQVCLFCVLPRKQAQVFFAVYFAFWRIMYNVGLGYVLTKQSRSRWIVRMLDSSGWLDACKNPRMHAWVQYHFKTKLGASSQRIAAAPIDFQAWILFRSVVDVILLNDVTAYAFFALSNIQGLGEHGVLLFVIRWLLGLLLLAFNAWVKLDAHRVVKDYAWYWGDCFFLCLQKLKFDGVYEVAPDPMYSIGYIGYYGLSLLTGSYAVLYVSLAAHASQLLFLVLFENPHMDRVYGERVPIAARVSERRPSDVPPATGVQRSREEIRTPQLAGAASAANGSYATSERGTAAVPSPPCTNVHDLHHRLFRNDNVVLSHIDLFRSSDFLLVLCLIYALSPLVLTRCGPRALLLFATIHAVAWRLFHSFGLGFALRWQSEERWIVHHFLKHYHFADGQAAVTESFSHWKTIYNTSLIMTYVSFALLAIRSYTSWTDNIYRLRYVLGVLLILVHMWSARSSYRVLGPFGWLYGDFFIDAYPKRLSYTGIYRFLNNPERSMGSAAFFGMALLSGSLTATVVAQLAHLSHWWFLGCVEGPHMRRLYGADVRQDSGVTKQLRQLCQSQWLRAAQPSIEELQGILQRAQGVVRQLLEQSRPRLERLADDTCALLQQKAEHVLTMHTGDSVQQIDQAKYRVTPVASPHTHEQRFHVGEPIIVQWMAAENHSRRDWIGLYAVNALDAHPDEHHGSLLVTRTTSRGKWLGVAEDEWEGHVHVGLTQSPLGTHGVSSVDTDTHQVSGVSVFQGSRLPWAAPGTYELRYHHDNTHYVLAKSERFTIYADSPEDPYSFDETFMILSKILRYALVEAPSTTSAAAHEYESADKADLTLWTQDQAQHIRDGIWSAFHVDFTKDVVIASANTTLLTRDILMARQLLSR | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 109788
Sequence Length: 970
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.1.1.17
|
Q7SAJ6 | MSSSAADPFAARLNSDVRQRHPTASATSKNVEGTSQQKQQQQQQQSEANAAASRVKKTYGKTPDGTVFVVPTTHDMVTQLLDPREPKNLSDVAVLAIIALHFLAAYYLPWGVKRPLFAAIFMFWRLAYNVGIGYLLTIQSKYKLLVTWAKRWKLFENPATGKNPRPWLYNLLKKELETKIPQDYKFEEAPIEYNTWLTFRRVVDLILMCDFISYCLFAIVCAHKPDGEGLFMCFARWAAGITLVGFNLWVKLDAHRVVKDYAWYWGDFFYLIEQELTFDGVFELAPHPMYSIGYAGYYGISMMAASYDVLFISIIAHAAQFAFLVIVENPHIEKTYNPPQPRVRCESEAGSQLQEFASEYSVPSTTGRHDNTPLPVHNLIGLKNLDFFRITDVAIVLLCAYLAVVTMVTPNTRFYQALFVLHALAWRLWYSAGLGVILTMQSEEKMFTRHFLKYGESVGEAWRQWKGIYHLSNCLCHASFIAASYKMYEFPADWTYGWALLKHVVGLSLIALQVWTATSIYESLGEFGWFYGDFFFDSKRQLTYTSIYRFLNNPERVFGTAGLWGAALITWSRAIFLMALAGHFLTLAFLAYVEKPHMQKVYGRNLRDDAGVTKFIKRSLPPPVTEWQQSIDKVLDETKHFIDEFVDAARSRLATGSSTIVKDTSALFNKYPARLTLSKISPDLAGYDPKHYGLSLAGTRVVGTNEKATGKESPNARVLKDVKTQAFEYGAPIRVKWTAPANHSKKDWVGLYMVTDNRSREVTEVPSLGRWVPTNPGEYDTTTDQGILVWDQPVEKKSEDTDLVEGEMVFEGDKLWWTQGVFEFRYHHGGGHHVMSISEPFEIQIPKFDDEHMGVDISGEVGERAVEAALLPVIRNCLDRDPDIAPSNAEERFGGHVERDGKYARRVVYAIRHMFGIDFAPAVVLADGNVRRLAWRICHAKEVLAPFSMSHTNGRTTPVDSKFSE | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 109552
Sequence Length: 965
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.1.1.17
|
B6HJA3 | MDQGLSTGAHQDTDGLRERNTRVDSTVGREALTAVGEGEIKDKDGKASKTFGRTPDGTVFTVPQTHDMVSQLLLPSEPKNFGDLVVLILLAGHIMFLWALPAGAKIPIFAVTYLFWRLAYNAGIGWLLHNQSHHKTLIRWAEKTKVFVNPATGENPHPKLYNWIKRELETKIPQDYSFDNAPIEYNTWLVFRRLVDLILMCDFTSYCLFAIACGHQPVDESILMTVLRWSAGIVLVLFNLWVKLDAHRVVKDYAWYWGDFFYLIDQELTFDGVFEMAPHPMYSVGYAGYYGISLMAASYKVLFISIIAHAAQFAFLVLVENPHIDKTYNPPPPRKRSSTCADSSSTLPTDLDTPTAPTPSEDQTPNATYSYSVKPPQPVHNLLGLHNLDLYRTTDSSIMLVQLLVFSITALTPSTPWYQLLFVVLAAISRIWYSVGIGYILRNQSNTKSWTRHFVKYGDTPQEAWNQWKGTYHLSMILCYSSFIAAVWKMYTFPADWGYGLVLFRHVLGAGLISLQIWTSVSIYESLGEFGWFYGDFFFDDSPKLTYNGIYRFLNNPERVLGLAGVWGAVLITSSGAVTFLALLSHILSLAFIQFVERPHMQKLYGRSLRQDAGLVKSLKRSLPPSLKQLHGSVDKMFDDSFEFIEEMLDNARPKLAAGVNTFVKDTTALFQKYPARVTIARIDADLAGFDVRDYALSVEGTSALSFEESEKNKGREGANARMPLDRRGDLKDLTFEYGSPIRVKWTAPLHHSKKDWIGLYRVTDNTSREVTRVSSQGRWVATNEGAYDNLTCEKGILTSDVVIPSSERQGQDPCEFASGEIVFAGDKLFWTQGVFELRYHHNGMHNVMAISRPFEIRIRRSDEDETISDGDSFVESAVENALLPVVRNCFDRDPEIAPETVDEQFGTLVERDGKFAKRVVFAVHQMFGIELAAEVVKADGNVRNLAWRICNAKKVLAPYSMSRSNGTTTPLEESKE | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 110184
Sequence Length: 977
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.1.1.17
|
O74787 | MTNQIPSASSAADFGSSKSTSVDAVPNMDKSSSVRRKNIDSNGLQQTNQIEQAESSLNAEADHSEPERYGCTPSGKVFLLPKEQENRRSILETVDPRFSKTPWDWIVISSILAQVLLFFMTTGAVRRYSMMLCFFFWRISYDAGIGFLLHMQSNHRKVVTWISDFGFFDKENHPKLYDLTKKQLISKMDSSYNYDTSPLEFNSWLVFRHFVDLILMCDFCSYILMGLAWTCWPKVNIILQFLRIFGGIALIVFNYWVKMDAHRVVRDYAWYWGDFFFLLRSSLVFNGVFELAPHPMYSVGYAGYYGMSLLTGSYAVLFASILAHAAQFGFLLFVENPHIERTYGTDINHARLSPRGEDNEFELPPEHDLVGFVNFDFTRISDVALLIIALYSIFIILLSSNSHYSQFWAIFQAFVWRFLHSIIHAFILFYQSKSKAWTKHFIRNGESAAYAWSQWKGLYNLTLNMSYISFVMAAWKLYHLPSNWTYGLVSLRHALGFGLIALHIYTSVSIYEDLGQYGWFYGDFFLPSRSPKLVYQGIYRYVNNPERFLGCSAYWGLALISSSAWIFLIAILAQLSNLAIIRLVEQPHMQKVYGNTLRKEAGISKLIKQATSEKGNILPKTVETHMKALTTSVDKVLDQTAEALEEFVNTAPPKVQELLKGTESNLRKNAQLAILKLFAPQLSSSTHFDYKLEIKGIDNNQVLLGHPITVCWTASPNHEINDWIGLYKLSDNASDLYTQTSSEGRWSAIDANGYTSHCSSIKSLSNDKNSGEVEFSGDLLFWETGTFEFRYHYGGKHLVMAKTEPFVITATSMNTTDVDEVSAYLLKSIKFCDPNITPHDGDASLCDISEGSARKLTSIIKYSFGIDLSYRVVQVDGSCSALSRRIVNSLKILQSFDGPSGAKDD | Function: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102762
Sequence Length: 905
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.1.1.17
|
Q9Z0E2 | MPSLPAPPAPRLLLGLLLLGSRPASGTGPEPPALPIRSEKEPLPVRGAAGCSFGGKVYALDETWHPDLGEPFGVMRCVLCACEAPQWARRGRGPGRVSCKNIKPQCPTLACRQPRQLPGHCCQTCPQERSNLDPQPAGLVFEYPRDPEHRSYSDRGEPGVGERTRADGHTDFVALLTGPRSQAVARARVSLLRSSLRFSVSYQRLDRPSRVRFTDPTGNILFEHPATPTQDGLVCGVWRAVPRLSVRLLRAEQLRVALVTSTHPSGEVWGPLIWQGALAAETFSAILTLEDPLQRGVGGIALLTLSDTEDSLHFLLLFRGLLGGLAQAPLKLQILHQGQLLRELQANTSAQEPGFAEVLPSLTDQEMDWLELGELQMVLEKAGGPELRISGYITTRQSCDVLQSVLCGADALIPVQTGAAGSASFILLGNGSLIYQVQVVGTGSEVVAMTLETKPQRKNQRTVLCHMAGLQPGGHMAVGMCSGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVTALCYSGHSARYDRLPVPLAGALVLPPVRSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQGTVTAHLLGPPGMPGPQRLLKGFYGSEAQGVVKDLEPVLLRHLAQGTASLLITTKSSPRGELRGQVHIASQCEAGGLRLASEGVQMPLAPNGEAATSPMLPAGPGPEAPVPAKHGSPGRPRDPNTCFFEGQQRPHGARWAPNYDPLCSLCICQRRTVICDPVVCPPPSCPHPVQALDQCCPVCPEKQRSRDLPSLPNLEPGEGCYFDGDRSWRAAGTRWHPVVPPFGLIKCAVCTCKGATGEVHCEKVQCPRLACAQPVRANPTDCCKQCPVGSGTNAKLGDPMQADGPRGCRFAGQWFPENQSWHPSVPPFGEMSCITCRCGAGVPHCERDDCSPPLSCGSGKESRCCSHCTAQRSSETRTLPELEKEAEHS | Function: Dorsalizing factor. Key developmental protein that dorsalizes early vertebrate embryonic tissues by binding to ventralizing TGF-beta family bone morphogenetic proteins (BMPs) and sequestering them in latent complexes.
PTM: Cleaved by tolloid proteases; cleavage participates in dorsoventral patterning during early development.
Sequence Mass (Da): 101513
Sequence Length: 948
Subcellular Location: Secreted
|
Q91713 | MQCPPILLVWTLWIMAVDCSRPKVFLPIQPEQEPLQSKTPAGCTFGGKFYSLEDSWHPDLGEPFGVMHCVLCYCEPQRSRRGKPSGKVSCKNIKHDCPSPSCANPILLPLHCCKTCPKAPPPPIKKSDFVFDGFEYFQEKDDDLYNDRSYLSSDDVAVEESRSEYVALLTAPSHVWPPVTSGVAKARFNLQRSNLLFSITYKWIDRLSRIRFSDLDGSVLFEHPVHRMGSPRDDTICGIWRSLNRSTLRLLRMGHILVSLVTTTLSEPEISGKIVKHKALFSESFSALLTPEDSDETGGGGLAMLTLSDVDDNLHFILMLRGLSGEEGDQIPILVQISHQNHVIRELYANISAQEQDFAEVLPDLSSREMLWLAQGQLEISVQTEGRRPQSMSGIITVRKSCDTLQSVLSGGDALNPTKTGAVGSASITLHENGTLEYQIQIAGTMSTVTAVTLETKPRRKTKRNILHDMSKDYHDGRVWGYWIDANARDLHMLLQSELFLNVATKDFQEGELRGQITPLLYSGLWARYEKLPVPLAGQFVSPPIRTGSAGHAWVSLDEHCHLHYQIVVTGLGKAEDAALNAHLHGFAELGEVGESSPGHKRLLKGFYGSEAQGSVKDLDLELLGHLSRGTAFIQVSTKLNPRGEIRGQIHIPNSCESGGVSLTPEEPEYEYEIYEEGRQRDPDDLRKDPRACSFEGQLRAHGSRWAPDYDRKCSVCSCQKRTVICDPIVCPPLNCSQPVHLPDQCCPVCEEKKEMREVKKPERARTSEGCFFDGDRSWKAAGTRWHPFVPPFGLIKCAICTCKGSTGEVHCEKVTCPKLSCTNPIRANPSDCCKQCPVEERSPMELADSMQSDGAGSCRFGRHWYPNHERWHPTVPPFGEMKCVTCTCAEGITQCRRQECTGTTCGTGSKRDRCCTKCKDANQDEDEKVKSDETRTPWSF | Function: Potent dorsalizing factor. Has potent axis-forming activities including the ability to recruit neighboring cells into secondary axes. Regulates cell-cell interactions in the organizing centers of head, trunk and tail development.
PTM: Cleaved by bmp1; cleavage participates in dorsoventral patterning during early development. Cleavage by bmp1 is enhanced by the interaction with olfml3/ont1.
Sequence Mass (Da): 104947
Sequence Length: 941
Subcellular Location: Secreted
|
P40685 | MTIRHHVSDALLTAYAAGTLSEAFSLVVATHLSLCDECRARAGALDAVGGSLMEETAPVALSEGSLASVMAQLDRQIQRPAPARRADPRAPAPLADYVGRRLEDVRWRTLGGGVRQAILPTGGEAIARLLWIPGGQAVPDHGHRGLELTLVLQGAFRDETDRFGAGDIEIADQELEHTPVAERGLDCICLAATDAPLRFNSFLPKLVQPFFRI | Cofactor: Binds 2 Zn(2+) ion per subunit. The Zn(2+) bound by the N-terminus is required for anti-sigma function, the function of the Zn(2+) bound by the C-terminus is unknown.
Function: Anti-sigma factor that inhibits the activity of the extracytoplasmic function (ECF) sigma-E factor (RpoE), thereby indirectly regulating the transcription of the cycA and rpoE genes. ECF sigma factors are held in an inactive form by a cognate anti-sigma factor.
Sequence Mass (Da): 22865
Sequence Length: 213
Domain: The N-terminal anti-sigma domain (residues 1-85) is necessary and sufficient to bind sigma-E and inhibit its activity. The C-terminal domain (residues 86-194) is required to respond to singlet oxygen .
|
P0AGE7 | MSEKLQVVTLLGSLRKGSFNGMVARTLPKIAPASMEVNALPSIADIPLYDADVQQEEGFPATVEALAEQIRQADGVVIVTPEYNYSVPGGLKNAIDWLSRLPDQPLAGKPVLIQTSSMGVIGGARCQYHLRQILVFLDAMVMNKPEFMGGVIQNKVDPQTGEVIDQGTLDHLTGQLTAFGEFIQRVKI | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the reduction of quinones. Acts by simultaneous two-electron transfer, avoiding formation of highly reactive semiquinone intermediates and producing quinols that promote tolerance of H(2)O(2). Quinone reduction is probably the primary biological role of ChrR. Can also reduce toxic chromate to insoluble and less toxic Cr(3+). Catalyzes the transfer of three electrons to Cr(6+) producing Cr(3+) and one electron to molecular oxygen without producing the toxic Cr(5+) species and only producing a minimal amount of reactive oxygen species (ROS). Chromate reduction protects the cell against chromate toxicity, but is likely a secondary activity.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 20376
Sequence Length: 188
EC: 1.6.5.2
|
Q88FF8 | MSQVYSVAVVVGSLRKESYNRKVARALSELAPSSLALKIVEIGDLPLYNEDIEAEAPPETWKRFRDEIRRSDAVLFVTPEYNRSVPGCLKNAIDVGSRPYGQSAWSGKPTAVVSVSPGAIGGFGANHAVRQSLVFLDMPCMQMPEAYLGGAASLFEDSGKLNDKTRPFLQAFVDRFASWVKLNRAV | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the reduction of quinones. Acts by simultaneous two-electron transfer, avoiding formation of highly reactive semiquinone intermediates and producing quinols that promote tolerance of H(2)O(2). Quinone reduction is probably the primary biological role of ChrR . Can also reduce toxic chromate to insoluble and less toxic Cr(3+). Catalyzes the transfer of three electrons to Cr(6+) producing Cr(3+) and one electron to molecular oxygen. This reaction produces transiently a minimal amount of the toxic Cr(5+) species and reactive oxygen species (ROS). Chromate reduction protects the cell against chromate toxicity, but is likely a secondary activity . Can also reduce potassium ferricyanide and 2,6-dichloroindophenol . During chromate reduction, displays an eightfold preference for NADH over NADPH .
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 20354
Sequence Length: 186
EC: 1.6.5.2
|
F4I902 | MSTSYSFLLAGRELDVFLSFSGKIALDVDFGYDLSRNGIKAFKSESWKESSFKPIDLRTLEALTESKVAVVMTSDEEVSSVGFLEELIVIIEFQEKRSLTVIPVFLTKHPLDVEKVSQIFPERAKIWRTAIAKLDNIAAQYSFSRNLAVMHGTHRIKQIADDIRLMFLSSASSDFKGLAGMDRHMKALYALLALESDEKVRTIGIWGSSGVGKTTLARYTYAEISVKFQAHVFLENVENMKEMLLPSENFEGEDLRSVNHEMNEMAEAKQKHRKVLLIADGVNNIEQGKWIAENANWFAPGSRVILITQEKSLLVQSGVNHVYEVGSLRYDEALQLFSRFAFKQPYPSPDFERLSVRAVQLAGFLPVTIRLFGSFLTGRDKEEWEATLLKLNAKQGKDIKEVWKIMEALEDKDIVEASQR | Function: Confers resistance to low temperatures by limiting chloroplast damage and cell death, thus maintaining growth homeostasis . Regulates steryl-esters and sterols accumulation . Limits leaf necrosis associated with virulent bacterial infection (e.g. Pseudomonas syringae pv. tomato DC3000) .
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Sequence Mass (Da): 47577
Sequence Length: 420
Domain: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
Subcellular Location: Cytoplasm
EC: 3.2.2.6
|
Q7LGC8 | MEKGLTLPQDCRDFVHSLKMRSKYALFLVFVVIVFVFIEKENKIISRVSDKLKQIPQALADANSTDPALILAENASLLSLSELDSAFSQLQSRLRNLSLQLGVEPAMEAAGEEEEEQRKEEEPPRPAVAGPRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVSFEPGGANAAGSALVYRDVLKQLFLCDLYVLEHFITPLPEDHLTQFMFRRGSSRSLCEDPVCTPFVKKVFEKYHCKNRRCGPLNVTLAAEACRRKEHMALKAVRIRQLEFLQPLAEDPRLDLRVIQLVRDPRAVLASRMVAFAGKYKTWKKWLDDEGQDGLREEEVQRLRGNCESIRLSAELGLRQPAWLRGRYMLVRYEDVARGPLQKAREMYRFAGIPLTPQVEDWIQKNTQAAHDGSGIYSTQKNSSEQFEKWRFSMPFKLAQVVQAACGPAMRLFGYKLARDAAALTNRSVSLLEERGTFWVT | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin . Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices . Catalyzes with a lower efficiency the sulfation of Gal residues of keratan sulfate, another glycosaminoglycan . Can also catalyze the sulfation of the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides (By similarity). May play a role in the maintenance of naive T-lymphocytes in the spleen (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate = n adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate + 2 H(+)
Sequence Mass (Da): 54706
Sequence Length: 479
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.17
|
O88199 | MEKGLALPQDFRDLVHSLKIRGRYVLFLAFVVIVFIFIEKENKIISRVSDKLKQIPHFVADANSTDPALLLSENASLLSLSELDSTFSHLRSRLHNLSLQLGVEPAMESQEAGAEKPSQQAGAGTRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVFFQQRGASAAGSALVYRDVLKQLLLCDLYVLEPFISPPPEDHLTQFLFRRGSSRSLCEDPVCTPFVKKVFEKYHCRNRRCGPLNVTLAGEACRRKDHVALKAVRIRQLEFLQPLVEDPRLDLRVIQLVRDPRAVLASRIVAFAGKYENWKKWLSEGQDQLSEDEVQRLRGNCESIRLSAELGLRQPAWLRGRYMLVRYEDVARRPLQKAREMYSFAGIPLTPQVEDWIQKNTQATRDSSDVYSTQKNSSEQFEKWRFSMPFKLAQVVQAACGPTMHLFGYKLARDAASLTNRSISLLEERGTFWVT | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin . Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices . Catalyzes with a lower efficiency the sulfation of Gal residues of keratan sulfate, another glycosaminoglycan . Can also catalyze the sulfation of the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides (By similarity). May play a role in the maintenance of naive T-lymphocytes in the spleen .
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate = n adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate + 2 H(+)
Sequence Mass (Da): 53997
Sequence Length: 472
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.17
|
Q8NCG5 | MLLPKKMKLLLFLVSQMAILALFFHMYSHNISSLSMKAQPERMHVLVLSSWRSGSSFVGQLFGQHPDVFYLMEPAWHVWMTFKQSTAWMLHMAVRDLIRAVFLCDMSVFDAYMEPGPRRQSSLFQWENSRALCSAPACDIIPQDEIIPRAHCRLLCSQQPFEVVEKACRSYSHVVLKEVRFFNLQSLYPLLKDPSLNLHIVHLVRDPRAVFRSRERTKGDLMIDSRIVMGQHEQKLKKEDQPYYVMQVICQSQLEIYKTIQSLPKALQERYLLVRYEDLARAPVAQTSRMYEFVGLEFLPHLQTWVHNITRGKGMGDHAFHTNARDALNVSQAWRWSLPYEKVSRLQKACGDAMNLLGYRHVRSEQEQRNLLLDLLSTWTVPEQIH | Function: Sulfotransferase involved in SELL/L-selectin ligand biosynthesis pathway. Catalyzes the transfer of the sulfate group from 3'-phospho-5'-adenylyl sulfate (PAPS) onto the hydroxyl group at C-6 position of the non-reducing N-acetylglucosamine (GlcNAc) residue within O-linked mucin-type glycans. Contributes to generate sialyl 6-sulfo Lewis X determinant (also known as MECA-79 epitope) for SELL recognition, a prerequisite for continuous lymphocyte homing into peripheral lymph nodes and antigen immune surveillance . Transfers the sulfate group primarily on core 2 GlcNAcbeta1-6(Galbeta1-3)GalNAcalphaSer/Thr and extended core 1 GlcNAcbeta1-3Galbeta1-3GalNAcalphaSer/Thr based O-linked glycans on CD34 and GLYCAM1 peripheral node addressins (PNAds) expressed on the lumenal side of high endothelial venules (HEVs) . The recognition of PNAds by SELL initiates a multistep process comprising tethering and rolling of blood lymphocytes on HEVs against the blood flow, followed by chemokine signaling, integrin-mediated lymphocyte adhesion onto endothelial cells and lymphocyte transendothelial migration. Modulates rolling velocity and differential T and B lymphocyte recruitment into peripheral lymph nodes, with a major role in B lymphocyte homing. Might be redundant in sulfation of MADCAM1 and lymphocyte trafficking to mesenteric lymph nodes (By similarity). Can also sulfonate core 3 GlcNAcbeta1-3GalNAc-R based glycans as well as GlcNAcbeta1-3Galbeta1-Glc, GlcNAcbeta1-6ManOMe and GlcNAcbeta1-2Man oligosaccharides, which might be ectopically expressed during tumorigenesis .
Catalytic Activity: 3'-phosphoadenylyl sulfate + 3-O-{N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] = 3-O-{6-O-sulfo-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + adenosine 3',5'-bisphosphate + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 45134
Sequence Length: 386
Pathway: Protein modification; carbohydrate sulfation.
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.-
|
Q9GZS9 | MGMRARVPKVAHSTRRPPAARMWLPRFSSKTVTVLLLAQTTCLLLFIISRPGPSSPAGGEDRVHVLVLSSWRSGSSFLGQLFSQHPDVFYLMEPAWHVWTTLSQGSAATLHMAVRDLMRSIFLCDMDVFDAYMPQSRNLSAFFNWATSRALCSPPACSAFPRGTISKQDVCKTLCTRQPFSLAREACRSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREAAGPILARDNGIVLGTNGKWVEADPHLRLIREVCRSHVRIAEAATLKPPPFLRGRYRLVRFEDLAREPLAEIRALYAFTGLTLTPQLEAWIHNITHGSGIGKPIEAFHTSSRNARNVSQAWRHALPFTKILRVQEVCAGALQLLGYRPVYSADQQRDLTLDLVLPRGPDHFSWASPD | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues and O-linked sugars of mucin-type acceptors. Acts on the non-reducing terminal GlcNAc of short carbohydrate substrates. However, it does not transfer sulfate to longer carbohydrate substrates that have poly-N-acetyllactosamine structures. Has no activity toward keratan. Not involved in generating HEV-expressed ligands for SELL. Its substrate specificity may be influenced by its subcellular location.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46161
Sequence Length: 411
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.-
|
Q9QUP4 | MRLPRFSSTVMLSLLMVQTGILVFLVSRQVPSSPAGLGERVHVLVLSSWRSGSSFVGQLFSQHPDVFYLMEPAWHVWDTLSQGSAPALHMAVRDLIRSVFLCDMDVFDAYLPWRRNISDLFQWAVSRALCSPPVCEAFARGNISSEEVCKPLCATRPFGLAQEACSSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREQTAKALARDNGIVLGTNGTWVEADPRLRVVNEVCRSHVRIAEAALHKPPPFLQDRYRLVRYEDLARDPLTVIRELYAFTGLGLTPQLQTWIHNITHGSGPGARREAFKTTSRDALSVSQAWRHTLPFAKIRRVQELCGGALQLLGYRSVHSELEQRDLSLDLLLPRGMDSFKWASSTEKQPES | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues of keratan. Mediates sulfation of keratan in cornea. Keratan sulfate plays a central role in maintaining corneal transparency. Acts on the non-reducing terminal GlcNAc of short and long carbohydrate substrates that have poly-N-acetyllactosamine structures. May also have activity toward O-linked sugars of mucin-type acceptors.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 44537
Sequence Length: 395
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.-
|
Q9GZX3 | MWLPRVSSTAVTALLLAQTFLLLFLVSRPGPSSPAGGEARVHVLVLSSWRSGSSFVGQLFNQHPDVFYLMEPAWHVWTTLSQGSAATLHMAVRDLVRSVFLCDMDVFDAYLPWRRNLSDLFQWAVSRALCSPPACSAFPRGAISSEAVCKPLCARQSFTLAREACRSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREQTAKALARDNGIVLGTNGTWVEADPGLRVVREVCRSHVRIAEAATLKPPPFLRGRYRLVRFEDLAREPLAEIRALYAFTGLSLTPQLEAWIHNITHGSGPGARREAFKTSSRNALNVSQAWRHALPFAKIRRVQELCAGALQLLGYRPVYSEDEQRNLALDLVLPRGLNGFTWASSTASHPRN | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues of keratan . Cooperates with B4GALT4 galactosyltransferase and B3GNT7 N-acetylglucosaminyltransferase to construct and elongate the sulfated disaccharide unit [->3Galbeta1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer. Involved in biosynthesis of keratan sulfate in cornea, with an impact on proteoglycan fibril organization and corneal transparency . Involved in sulfation of endothelial mucins such as GLYCAM1 .
Catalytic Activity: 3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-bisphosphate + keratan 6'-sulfate.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 44099
Sequence Length: 395
Subcellular Location: Golgi apparatus membrane
|
Q9NS84 | MKGRRRRRREYCKFALLLVLYTLVLLLVPSVLDGGRDGDKGAEHCPGLQRSLGVWSLEAAAAGEREQGAEARAAEEGGANQSPRFPSNLSGAVGEAVSREKQHIYVHATWRTGSSFLGELFNQHPDVFYLYEPMWHLWQALYPGDAESLQGALRDMLRSLFRCDFSVLRLYAPPGDPAARAPDTANLTTAALFRWRTNKVICSPPLCPGAPRARAEVGLVEDTACERSCPPVAIRALEAECRKYPVVVIKDVRLLDLGVLVPLLRDPGLNLKVVQLFRDPRAVHNSRLKSRQGLLRESIQVLRTRQRGDRFHRVLLAHGVGARPGGQSRALPAAPRADFFLTGALEVICEAWLRDLLFARGAPAWLRRRYLRLRYEDLVRQPRAQLRRLLRFSGLRALAALDAFALNMTRGAAYGADRPFHLSARDAREAVHAWRERLSREQVRQVEAACAPAMRLLAYPRSGEEGDAEQPREGETPLEMDADGAT | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide and N-acetyllactosamine oligomer with a lower efficiency. Has weak or no activity toward keratan sulfate and oligosaccharides containing the Galbeta1-4GlcNAc. Catalyzes 6-O-sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc.
Catalytic Activity: n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate = n adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate + 2 H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 54266
Sequence Length: 486
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.-
|
Q9H2A9 | MTLRPGTMRLACMFSSILLFGAAGLLLFISLQDPTELAPQQVPGIKFNIRPRQPHHDLPPGGSQDGDLKEPTERVTRDLSSGAPRGRNLPAPDQPQPPLQRGTRLRLRQRRRRLLIKKMPAAATIPANSSDAPFIRPGPGTLDGRWVSLHRSQQERKRVMQEACAKYRASSSRRAVTPRHVSRIFVEDRHRVLYCEVPKAGCSNWKRVLMVLAGLASSTADIQHNTVHYGSALKRLDTFDRQGILHRLSTYTKMLFVREPFERLVSAFRDKFEHPNSYYHPVFGKAILARYRANASREALRTGSGVRFPEFVQYLLDVHRPVGMDIHWDHVSRLCSPCLIDYDFVGKFESMEDDANFFLSLIRAPRNLTFPRFKDRHSQEARTTARIAHQYFAQLSALQRQRTYDFYYMDYLMFNYSKPFADLY | Function: Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Required for biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Only active against terminal GalNAcbeta1,GalNAcbeta. Not active toward chondroitin.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48834
Sequence Length: 424
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.-
|
Q7L1S5 | MQPSEMVMNPKQVFLSVLIFGVAGLLLFMYLQVWIEEQHTGRVEKRREQKVTSGWGPVKYLRPVPRIMSTEKIQEHITNQNPKFHMPEDVREKKENLLLNSERSTRLLTKTSHSQGGDQALSKSTGSPTEKLIEKRQGAKTVFNKFSNMNWPVDIHPLNKSLVKDNKWKKTEETQEKRRSFLQEFCKKYGGVSHHQSHLFHTVSRIYVEDKHKILYCEVPKAGCSNWKRILMVLNGLASSAYNISHNAVHYGKHLKKLDSFDLKGIYTRLNTYTKAVFVRDPMERLVSAFRDKFEHPNSYYHPVFGKAIIKKYRPNACEEALINGSGVKFKEFIHYLLDSHRPVGMDIHWEKVSKLCYPCLINYDFVGKFETLEEDANYFLQMIGAPKELKFPNFKDRHSSDERTNAQVVRQYLKDLTRTERQLIYDFYYLDYLMFNYTTPFL | Function: Catalyzes the transfer of sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. Participates in biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures. Has a higher activity toward carbonic anhydrase VI than toward lutropin. Only active against terminal GalNAcbeta1,GalNAcbeta. Isoform 2, but not isoform 1, is active toward chondroitin.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 52055
Sequence Length: 443
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.-
|
O43529 | MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDVYSAKQEFLFLTTMPEVRKLPEEKHIPEELKPTGKELPDSQLVQPLVYMERLELIRNVCRDDALKNLSHTPVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSDAEIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRRNRTETRGIQFEDFVRYLGDPNHRWLDLQFGDHIIHWVTYVELCAPCEIMYSVIGHHETLEDDAPYILKEAGIDHLVSYPTIPPGITVYNRTKVEHYFLGISKRDIRRLYARFEGDFKLFGYQKPDFLLN | Function: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-(1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis . Sulfates terminal glucuronyl residue of the laminin globular (LG)-domain binding epitope on DAG1/alpha-dystroglycan and prevents further polymerization by LARGE1 glycosyltransferase. Likely defines the chain length of LG epitope, confering binding specificity to extracellular matrix components . Plays a role in down-regulating the steroid hormones. Sulfates glucuronidated estrogens and androgens with an impact in hormone cycle and fertility. Has a preference for glucuronyl moiety at the 3-hydroxyl group of a sterol ring rather than the 17-hydroxyl group, showing high catalytic efficiency for 17beta-estradiol 3-O-(beta-D-glucuronate) and dehydroepiandrosterone 3-O-(beta-D-glucuronate) hormones .
Catalytic Activity: 3'-phosphoadenylyl sulfate + 3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] = 3-O-{O-3-S-beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + adenosine 3',5'-bisphosphate + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 42207
Sequence Length: 356
Pathway: Steroid metabolism.
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.-
|
Q6PGK7 | MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDGYSAKQEFVFLTTMPEAEKLRGEKHFPEVPKPTGKMLSDSRPDQPPVYLERLELIRNTCKEEALRNLSHTEVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSKIGIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRKNRTETRGIQFEDFVRYLGDPNRRWLDLQFGDHIIHWVTYVELCAPCEIKYSVVGHHETLEADAPYILKEAGIDHLVSYPTIPPGITMYNRTKVEQYFLGISKRDIRRLYARFEGDFKLFGYQKPDFLLN | Function: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-(1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis . Sulfates terminal glucuronyl residue of the laminin globular (LG)-domain binding epitope on DAG1/alpha-dystroglycan and prevents further polymerization by LARGE1 glycosyltransferase. Likely defines the chain length of LG epitope, confering binding specificity to extracellular matrix components (By similarity). Plays a role in down-regulating the steroid hormones. Sulfates glucuronidated estrogens and androgens with an impact in hormone cycle and fertility. Has a preference for glucuronyl moiety at the 3-hydroxyl group of a sterol ring rather than the 17-hydroxyl group, showing high catalytic efficiency for 17beta-estradiol 3-O-(beta-D-glucuronate) and dehydroepiandrosterone 3-O-(beta-D-glucuronate) hormones (By similarity).
Catalytic Activity: 3'-phosphoadenylyl sulfate + 3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] = 3-O-{O-3-S-beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + adenosine 3',5'-bisphosphate + H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 42055
Sequence Length: 356
Pathway: Steroid metabolism.
Subcellular Location: Golgi apparatus membrane
EC: 2.8.2.-
|
A0A1U8QH20 | MERFPRSAADAQQLLQLAELFKQSAEIIAEEWNKEDFSRIKAETNSIKSNLGSLDTARILPSPRLHEATRTVLAITGAATELVAEPYSRIQEVACQYFESRALFVAAERRIPDLLAGAGEYGLSVGEIAEATGIEERKLSRILRCLCSIHIFRQIGTDRFANNRISAALKNNEPLRAYVQLFNLDIYTASDQLPKYLLSSQGASYKVHETAWQKAVGTTKARWDWLAERVSLDEVRPKEAPYPGLPDVRHLQPGPDGKYARPELDNFGLAMVGGGKVSGAAHAYDFPWASLGDALVVDVGGGVGGFVLQLLPAYPQLRYIVQDRAEVLQQAQEEIWPVEAPEAVADGRVQFMEHNFFQPNPVKGADVYWLRGIFYCVQILSALRTSMAPTSRILVCDQVMNTTAGCDEIPPAPSPLPANYGYYMRYPHHRDLAMMSIINGIERTPAQFTELVKQAGLKVNKIWNCRSMVGIVEIGLKNEKDRHHRRLSYMGFGNYTQLGIGFFSSAKGPVRDELQADEQA | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans . The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units . PkbA also catalyzes one methylation step to produce 3-methylorsellinate . The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3-methylorsellinate into nidulol . CicB converts 3-methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorine .
Sequence Mass (Da): 57889
Sequence Length: 520
Pathway: Phytotoxin biosynthesis.
EC: 2.1.1.-
|
C8V0D4 | MAILVRLFFALFVVSVYFFRVRLRLSHIPGPFLASLTNINRRQWVTTGRAHTIHTELHRQYGKVVRAGPNTVFVSDPAAIPAIYRFNEPYQKSEFYDALMPYVRGKSIPDVFATRDEHIHRTMKQPIAAIYSMSNLVSFEPYVKSTIEYFFSRLDSLFVETGKVCNFGLWLHLFASDVMGEITFSRRLGFLETGGDMENVMANNWKFFVQAAPATQMPWLDYFWKRNPLLPGSVKPNKVIEFGVARIQERLHLSEKHPDHVNSRDFLSRFIAAKEKNSQIGPDAIMTWANSNIQAGSDTTAILLSALFYHLLKNPTSLAALCTEIDAAAKRGCLSSILTWKETRDLPYLDACVKEAARLHPPISLPLERVIPESGTVIGGFKIPGGTRVAMNPWAVHRDRDVFGADADTWRPERWLEGEEKAKTLYNSLLTFGGGHRSCLGKNISYLEIYKLVPSILLRYEIGLAEPEKEWHLENRWFVMPSRFYVRLKARNGVTKL | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans . The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units . PkbA also catalyzes one methylation step to produce 3-methylorsellinate . The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3-methylorsellinate into nidulol . CicB converts 3-methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorine .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56706
Sequence Length: 497
Pathway: Phytotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
|
P35522 | MSHEKNEASGNPEAQSWKAQEAMLGVKTEVSRWRAVKNCLYRHLVKVLGEDWIFLLLLGALMALVSWAMDFIGSRGLRFYKYLFAMVEGNLGLQYLVWVCYPLILILFSSLFCQIVSPQAVGSGIPELKTIIRGAVLHEYLTLRTFVAKTVGLTVALSAGFPLGKEGPFVHIASICATLLNQLLCFISGRREEPYYLRADILTVGCALGISCCFGTPLAGVLFSIEVTCSHFGVRSYWRGFLGGAFSAFIFRVLSVWVKDTVTLTALFKTNFRGDIPFDLQELPAFAIIGIASGFFGALFVYLNRQIIVFMRKKNFVTKILKKQRLIYPAVVTFVLATLRFPPGVGQFFGAGLMPRETINSLFDNYTWTKTIDPRGLGNSAQWFIPHLNIFIVMALYFVMHFWMAALAVTMPVPCGAFVPVFNLGAVLGRFVGELMALLFPDGLVSNGNLYHILPGEYAVIGAAAMTGAVTHAVSTAVICFELTGQISHVLPMMVAVILANMVAQGLQPSLYDSIIQIKKLPYLPELSWSSANKYNIQVGDIMVRDVTSIASTSTYGDLLHVLRQTKLKFFPFVDTPETNTLLGSIERTEVEGLLQRRISAYRRQPATAAEAEEEGRNGERGASFTGDVPGEAETSFAYIDQEEAEGQQQREGLEAVKVQTEDPRPPSPVPAEEPTQTSGIYQKKHKGTGQVASRFEEMLTLEEIYQWEQREKNVVVNFETCRIDQSPFQLVEGTSLQKTHTLFSLLGLDRAYVTSMGKLVGVVALAEIQAAIEGSYQKGFRLPPPLASFRDAKNARNSGRTATSNSSGK | Function: Voltage-gated chloride channel. This channel is thought to ensure the high conductance of the non-innervated membrane of the electrocyte necessary for efficient current generation caused by sodium influx through the acetylcholine receptor at the innervated membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89447
Sequence Length: 810
Subcellular Location: Membrane
|
Q8N5K1 | MVLESVARIVKVQLPAYLKRLPVPESITGFARLTVSEWLRLLPFLGVLALLGYLAVRPFLPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Contributes to BIK-initiated autophagy, while it is not involved in BIK-dependent activation of caspases. Involved in life span control, probably via its function as regulator of autophagy.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15278
Sequence Length: 135
Subcellular Location: Endoplasmic reticulum membrane
|
Q9CQB5 | MVLDSVARIVKVQLPAYLKQLPVPDSITGFARLTVSDWLRLLPFLGVLALLGYLAVRPFFPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Contributes to BIK-initiated autophagy, while it is not involved in BIK-dependent activation of caspases. Involved in life span control, probably via its function as regulator of autophagy (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15242
Sequence Length: 135
Subcellular Location: Endoplasmic reticulum membrane
|
B3RML8 | MEAIAKLIKVQLPNYLQKLPVPSSLSGFAELSPSDAIAVVFPFAVVSWLIGYSTYKFFQPKAVELPPSPKAKDTNCVNKCIDKTCKKVVHTVDIEDVGEKLVFCRCWRSKKFPYCDGSHNNHNEQEQDNVGPLIVKGKAN | Cofactor: Binds 1 [2Fe-2S] cluster.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15597
Sequence Length: 140
Subcellular Location: Endoplasmic reticulum membrane
|
P0C7P0 | MRGAGAILRPAARGARDLNPRRDISSWLAQWFPRTPARSVVALKTPIKVELVAGKTYRWCVCGRSKKQPFCDGSHFFQRTGLSPLKFKAQETRMVALCTCKATQRPPYCDGTHRSERVQKAEVGSPL | Cofactor: Binds 2 [2Fe-2S] clusters per subunit.
Function: Can transfer its iron-sulfur clusters to the apoferrodoxins FDX1 and FDX2. Contributes to mitochondrial iron homeostasis and in maintaining normal levels of free iron and reactive oxygen species, and thereby contributes to normal mitochondrial function.
Sequence Mass (Da): 14216
Sequence Length: 127
Subcellular Location: Mitochondrion
|
B1AR13 | MGFRRLSFPTDFIFLFPNHICLPALSKPYQRREISSWLARWFPKDPAKPVVAQKTPIRLELVAGKTYRWCVCGRSKNQPFCDGSHFFQRTGLSPLKFKAQETRTVALCTCKATQRPPYCDGTHKSEQVQKAEVGSPL | Cofactor: Binds 2 [2Fe-2S] clusters per subunit.
Function: Can transfer its iron-sulfur clusters to the apoferrodoxins FDX1 and FDX2. Contributes to mitochondrial iron homeostasis and in maintaining normal levels of free iron and reactive oxygen species, and thereby contributes to normal mitochondrial function.
Sequence Mass (Da): 15676
Sequence Length: 137
Subcellular Location: Mitochondrion
|
Q2HJ53 | MVLCVQGLCPLLAVEQIGQRPLWAQSLELPQQVMQPLSAGAFLEEAVEESPAQPEREPKVVDPEEDLLCIAKTFSYLRESGWYWGSITASEARQHLQKMPEGTFLVRDSTHPSYLFTLSVKTTRGPTNVRIEYADSSFRLDSNCLSRPRILAFPDVVSLVQHYVASCAADTRSDSPDLATTPALPTPKEDAPGDPALPATAVHLKLVQPFVRRSSTRSLQHLCRLVINRLVVDVDCLPLPRRMADYLRQYPFQL | Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. CIS is involved in the negative regulation of cytokines that signal through the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin 3 (IL3) receptor. Inhibits STAT5 trans-activation by suppressing its tyrosine phosphorylation (By similarity). May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
Sequence Mass (Da): 28397
Sequence Length: 254
Domain: The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes.
Pathway: Protein modification; protein ubiquitination.
|
Q9NSE2 | MVLCVQGPRPLLAVERTGQRPLWAPSLELPKPVMQPLPAGAFLEEVAEGTPAQTESEPKVLDPEEDLLCIAKTFSYLRESGWYWGSITASEARQHLQKMPEGTFLVRDSTHPSYLFTLSVKTTRGPTNVRIEYADSSFRLDSNCLSRPRILAFPDVVSLVQHYVASCTADTRSDSPDPAPTPALPMPKEDAPSDPALPAPPPATAVHLKLVQPFVRRSSARSLQHLCRLVINRLVADVDCLPLPRRMADYLRQYPFQL | Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. CIS is involved in the negative regulation of cytokines that signal through the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin 3 (IL3) receptor. Inhibits STAT5 trans-activation by suppressing its tyrosine phosphorylation. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
PTM: Association with EPOR may target the protein for proteolysis by the ubiquitin-dependent proteasome pathway. CIS is mainly monubiquitinated (37 kDa form) but may also exist in a polyubiquitinated form (45 kDa).
Sequence Mass (Da): 28663
Sequence Length: 258
Pathway: Protein modification; protein ubiquitination.
|
A0A0S3QTD0 | MKLKERLAELIPQWRAEVAEIRKKYGNRKTMDCTIGHAYGGMRGLKALVCDTSEVFPDEGVKFRGYTIPELREGPHKLPTAEGGFEPLPEGLWYLLLTGELPTEEDVKEISAEFTKRMQNVPQYVFDVLRAMPVDTHPMTMFAAGILAMQRESVFAKRYEEGMRREEHWEAMLEDSLNMLAALPVIAAYIYRRKYKGDTHIAPDPNLDWSANLAHMMGFDDFEVYELFRLYMFLHSDHEGGNVSAHTNLLVNSAYSDIYRSFSAAMNGLAGPLHGLANQEVLRWIQMLYKKFGGVPTKEQLERFAWDTLNSGQVIPGYGHAVLRVTDPRYVAQRDFALKHLPDDELFKIVSLCYEVIPEVLKKHGKAKNPWPNVDAHSGVLLWHYGIREYDFYTVLFGVSRALGCTAQAILVRGYMLPIERPKSITTRWVKEVAESLPVAGS | Function: Catalyzes both citrate generation and citrate cleavage. Part of a reversible tricarboxylic acid (TCA) cycle that can fix carbon dioxide autotrophically and may represent an ancestral mode of the conventional reductive TCA (rTCA) cycle. The direction is controlled by the available carbon source(s).
Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 50337
Sequence Length: 442
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
EC: 2.3.3.16
|
Q28DK1 | MSLITAGRLCARILGAKNSPCALIAARQASSSANLKDVLSDLIPKEQTRIKNFRQQYGKNVIGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAPGGEEPLPEGLFWLLVTGEAPSQEQVNWISKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARGYAEGVNKTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSSIGAIDSNLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFSAAMNGLAGPLHGLANQEVLVWLTSLQKDLGGEVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMKEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLMQLVGSKSG | Catalytic Activity: acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+)
Sequence Mass (Da): 51834
Sequence Length: 468
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
Subcellular Location: Mitochondrion matrix
EC: 2.3.3.1
|
P07661 | MTQQPSRAGTFGAILRVTSGNFLEQFDFFLFGFYATYIAKTFFPAESEFAALMLTFAVFGSGFLMRPIGAVVLGAYIDRIGRRKGLMITLAIMGCGTLLIALVPGYQTIGLLAPVLVLVGRLLQGFSAGVELGGVSVYLSEIATPGNKGFYTSWQSASQQVAIVVAALIGYGLNVTLGHDEISEWGWRIPFFIGCMIIPLIFVLRRSLQETEAFLQRKHRPDTREIFTTIAKNWRIITAGTLLVAMTTTTFYFITVYTPTYGRTVLNLSARDSLVVTMLVGISNFIWLPIGGAISDRIGRRPVLMGITLLALVTTLPVMNWLTAAPDFTRMTLVLLWFSFFFGMYNGAMVAALTEVMPVYVRTVGFSLAFSLATAIFGGLTPAISTALVQLTGDKSSPGWWLMCAALCGLAATTMLFARLSSGYQTVENKL | Function: Uptake of citrate across the boundary membrane with the concomitant transport of protons into the cell (symport system).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46980
Sequence Length: 431
Subcellular Location: Cell inner membrane
|
P52687 | MSIYPMYTRKITHWFARRSFQNRIFLLILFTSTIVMLAMSWYLTDITEERLHYQVGQRALIQAMQISAMPELVEAVQKRDLARIKALIDPMRSFSDATYITVGDASGQRLYHVNPDEIGKSMEGGDSDEALINAKSYVSVRKGSLGSSLRGKSPIQDATGKVIGIVSVGYTIEQLENWLSLQISSLLIPMAIMLLLLLFCARRFSLHIKKQMLNMEPQQLSQLLIQQSVLFESVFEGLIAIDSDYKITAINQTARRLLNLSQPEPTLIGKRISSVISQEVFFYDAPQTNKKDEIVTFNQIKVIASRMAVILNNEPQGWVISFRSKDDINTLSLQLSQVQQYADNLRAVQHEHRNLISTIAGLLFLKRYNQALELIQQQSESHQKVIDFIARNFQDNHLAGLLIGKYYRAKELGLELIFDPACFVDRLPTALSHNEWISIVGNLLDNAYNASLRQPQGSKQIECLINSDGQEVIIEIADQGCGIDEALRDRIFERGVTSSASKDHGIGLWLVRSYVEQAGGSIVVENNIPFGTIFTLYIPLTRDEHHG | Function: Member of the two-component regulatory system CitA/CitB. Probably activates CitB by phosphorylation. The periplasmic domain binds H-citrate(2-), which is essential for induction of the citrate-fermentation genes.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 61780
Sequence Length: 547
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
|
Q1ERH9 | MKGQTGLRSLALLYISPLYILERLPLKLSAPDTLVVRGSFIVPTEPLYPSITMVQTNLEVVDDTLHLPRILCLHGGGSNAAIFQAQCRRLIAQLRSEFRFVFAQAPFLSDAEPNVMSVYSQWGPFRRWLRWCPDHPEIRPEDAIRAIDDCLEDVKRQDDAKGATGAWVGLLGFSQGAKMCASLLYRQQIRQELRGRSFAGSDYRFGVLLAGRAPLVSLDPDLDLNSSLPDVSQITDAKYHGPSQDVLRIPTVHVHGMRDPHVDLHRQLFEEFCAPESRRLVEWDGDHRVPLKYNDVSLVAYQIRELATQTGAP | Function: Esterase; 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): 35226
Sequence Length: 313
Pathway: Mycotoxin biosynthesis.
EC: 3.1.2.-
|
P52688 | MDSITTLIVEDEPMLAEILVDNIKQFPQFDVIGIADKLESARKQLRLYQPQLILLDNFLPDGKGIDLIRHAVSTHYKGRIIFITADNHMETISEALRLGVFDYLIKPVHYQRLQHTLERFARYRSSLRSSEQASQLHVDALFNIQAREQTEPASAPLRGIDESTFQRVLQLFADPTVVHTADSLARILGSSKTTARRYLEQGVKNDFLEAEISYGKVGRPERIYHGKQTYPEQR | Function: Member of the two-component regulatory system CitA/CitB essential for expression of citrate-specific fermentation genes. Phosphorylated CitB binds to two sites in the citS-citC intergenic region where it probably activates transcription of both genes.
PTM: Phosphorylated by CitA.
Sequence Mass (Da): 26821
Sequence Length: 234
Subcellular Location: Cytoplasm
|
Q1ERI0 | MPISTKSSFYLPAVDISPYLQDPNSDAARKVIDDVRAACTSTGFFQLLGHGISPALQQSVFAAAAKFFALPSDVKSRCRNVGFRGYDPMASQSYELGVLPDLKEGFIAGKDIPLDDPRVASQRFFMGQNAWPPSELLPEANFRRPIEEYYQAMLKLCWVVLDLVAATLPYGPHVFDEFKENDPACPLRLLHYPPAPAPDVAKGRQLGSSAHTDFGAITLLLQDDHSGLEVQDCETGEWIGVPPNKDAYVVNLGDMMSRITRGHYKSSIHRVINQNLTDRYSVVFFFDGNLDYRLRPLDRVGQNWDEEDTLTVEEHMLERTTTTYNLKVK | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; 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): 36894
Sequence Length: 329
Pathway: Mycotoxin biosynthesis.
EC: 1.14.-.-
|
P77390 | MFGNDIFTRVKRSENKKMAEIAQFLHENDLSVDTTVEVFITVTRDEKLIACGGIAGNIIKCVAISESVRGEGLALTLATELINLAYERHSTHLFIYTKTEYEALFRQCGFSTLTSVPGVMVLMENSATRLKRYAESLKKFRHPGNKIGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFIKEQSVINHCYTEIDLKIFRQYLAPALGVTHRFVGTEPFCRVTAQYNQDMRYWLETPTISAPPIELVEIERLRYQEMPISASRVRQLLAKNDLTAIAPLVPAVTLHYLQNLLEHSRQDAAARQKTPA | 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): 40077
Sequence Length: 352
EC: 6.2.1.22
|
P44462 | MQFERISTEQKKLSLIQTFLHQNALKLDEQIEYFVVGYNDNEQIVVCGGLAGNIIKCVAIDESLRGSGVALQLITELVDLAYTLKRPHLFIYTKPEYATLFKSCGFYIISDANPYVVLLENSATRLQKQCSLWEKMRVDGNRIGSIVMNANPFTLGHRYLIEQALQQCDHLHLFIVGEDASQFSYTERFEMIQQGIFDLSNITLHSGSDYIISRATFPNYFLKDQLITDESYFEIDLKLFRLHIAQALGITHRFVGTELNCPVTAEYNRQMHYWLMDAEMNAPKINVIEIPRKTASNHIISASTVRKHLAEKNWAQLAEFVPMTTLNYLQKCGRF | 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): 38495
Sequence Length: 335
EC: 6.2.1.22
|
P58161 | MSMPATLTKTTKLATSLIDEYALLGWRAMLTEVNLSPKPGLVDRINCGAHKDMALEDFHRSALAIQGWLPRFIEFGACSAEMAPEAVLHGLRPIGMACEGDMFRATAGVNTHKGSIFSLGLLCAAIGRLLQLNQLLTPTTVCSTAASFCRGLTDRELRTNNSQLTAGQRLYQQLGLTGARGEAEAGYPLVINHALPHYLTLLDQGLDPELALLDTLLLLMAINGDTNVASRGGEGGLRWLQREAQTLLQKGGIRTPADLDYLRQFDRECIERNLSPGGSADLLILTWFLAQI | Function: Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP and dephospho-CoA.
Catalytic Activity: 3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + adenine
Sequence Mass (Da): 31701
Sequence Length: 292
EC: 2.4.2.52
|
Q9H0W9 | MACAEFSFHVPSLEELAGVMQKGLKDNFADVQVSVVDCPDLTKEPFTFPVKGICGKTRIAEVGGVPYLLPLVNQKKVYDLNKIAKEIKLPGAFILGAGAGPFQTLGFNSEFMPVIQTESEHKPPVNGSYFAHVNPADGGCLLEKYSEKCHDFQCALLANLFASEGQPGKVIEVKAKRRTGPLNFVTCMRETLEKHYGNKPIGMGGTFIIQKGKVKSHIMPAEFSSCPLNSDEEVNKWLHFYEMKAPLVCLPVFVSRDPGFDLRLEHTHFFSRHGEGGHYHYDTTPDIVEYLGYFLPAEFLYRIDQPKETHSIGRD | Function: Exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate.
Sequence Mass (Da): 35117
Sequence Length: 315
Subcellular Location: Nucleus
EC: 3.1.-.-
|
A2XVN3 | MELKAMYLYAAVLAVLLCSSVNFIQSPTDVLGPVALLEPTPSSARDFGAVVSDAPFAVMRPESPDDIALLLGALSSTAPSPRATVAAVGAGHSLHGQAQARDGIVVETRALPRDVHVVSARAHGGDDDATVRAYADVGAGALWVEVLEECLKLGLAPPSWTDYLYLTVGGTLSNGGISGQTFKHGPQISNVLQLEVVTGKGEVVTCSPTEIPELFFAVLGGLGQFGIITRARIPLQLAPPKVRWVRAFYDSFETFTGDQELLVSMPEQVDYVEGFMVLNEQSLHSSSVAFPAQLNFSPDFGSKGRKKVYYCIEFAVHDFQQDSSRADHVVKLVSAKLSYLRPHVYSVEVSYFDFLNRVRMEEESLRSRGLWDVPHPWLNVFVPKHGITQFKGLLMDTVSADDFEGPILVYPLLTDKWDGNTSAVVPAAPDGVMYIFGVLRSTDPARCGRACVDSIMARHRRVADEACRDGGGGGRGIGAKQYLARQPSPARWRDHFGAGWGRFAARKARFDPLHVLGPGQGIFPRTDSAGSM | Function: Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group.
Catalytic Activity: A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal + adenine + AH2
Sequence Mass (Da): 57619
Sequence Length: 532
Subcellular Location: Secreted
EC: 1.5.99.12
|
Q75K78 | MRPSLLQYLKLLLLLALGGVTTMHVPKQDVPSSLEELTLDGHFSFHDVSAAAQDFGNLSSFPPVAVLHPGSVADIATTIRHVFLMGEHSTLTVAARGHGHSLYGQSQAAEGIIISMESLQSNTMRVNPGVSPYVDASGGELWINVLHETLKYGLAPKSWTDYLHLTVGGTLSNAGVSGQTFRHGPQISNVNELEIVTGRGDVITCSPEQNSDLFHAALGGLGQFGVITRARIPLEPAPKMVRWLRVLYLDFTSFTEDQEMLISAEKTFDYIEGFVIINRTGILNNWRSSFNPQDPVRSSQFESDGKVLFCLEMTKNFNPDEADVMEQEVNTLLSQLRYMPSSLFHTDVTYIEFLDRVHSSEMKLRAKGMWEVPHPWLNIIIPRSMIHKFAKEVFGKILKDSNNGPILLYPVNKSRWDNRTSVVIPDEEVFYLVAFLSSALGPHNIKHTLDLNYRIIEFSDKAGIGVKQYLPNYTTEQEWQSHFGARWDTFQQRKKAYDPLAILAPGQRIFQKASASLPLPS | Function: Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group (Probable). Possesses cytokinin oxidase activity toward trans-zeatin (tZ) and N6-(2-isopentenyl)adenine (2iP) in vitro . Functions as a primary strigolactone-responsive gene to regulate rice tillering, plant height, and panicle size, likely via a secondary response gene, RR5, which encodes a cytokinin-inducible rice type-A response regulator that seems to act as negative regulator of the cytokinin signaling .
Catalytic Activity: A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal + adenine + AH2
Sequence Mass (Da): 58269
Sequence Length: 521
Subcellular Location: Secreted
EC: 1.5.99.12
|
P58763 | FLPKSLFTLVTDKSL | Function: Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group. Substrate preference is 2-(2-hydroxyethylamino)-9-methyl-N(6)-isopentenyladenine >> isopentenyladenine > cis-zeatin = isopentenyladenosine = zeatin >> zeatin riboside.
Catalytic Activity: A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal + adenine + AH2
Sequence Mass (Da): 1709
Sequence Length: 15
Subcellular Location: Membrane
EC: 1.5.99.12
|
Q9LEX1 | MGLISGILFGIIFGVALMAGWSRMMTHRSSKRVAKAVDMKLLGSLSRDDLKKICGDNFPQWISFPAFEQVKWLNKLLSKMWPYIAEAATMVIRDSVEPLLEDYRPPGITSLKFSKLTLGNVAPKIEGIRVQSFKEGQVTMDVDLRWGGDPNIVLGVTALVASIPIQLKDLQVFTVARVIFQLADEIPCISAVVVALLAEPKPRIDYTLKAVGGSLTAIPGLSDMIDDTVDTIVKDMLQWPHRIVVPIGGIPVDLSDLELKPQGKLIVTVVKATNLKNKELIGKSDPYATIYIRPVFKYKTKAIENNLNPVWDQTFELIAEDKETQSLTVEVFDKDVGQDERLGLVKLPLSSLEAGVTKELELNLLSSLDTLKVKDKKDRGSITLKVHYHEFNKEEQMAALEDEKKIMEERKRLKEAGVIGSTMDAVGMVGSGLGAGVGMVGTGIGTGVGLVGSGVSSGVGMVGSGFGAVGSGLSKAGRFMGRTITGQSSKRSGSSTPVNTVPENDGAKQQ | Function: May be involved in membrane trafficking (By similarity). Acts as a repressor of abiotic stress (e.g. drought and salt) responses by binding specifically to the promoter of THAS1 to regulate its transcription . Binds to membrane lipid ceramides .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55095
Sequence Length: 510
Domain: The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Subcellular Location: Nucleus membrane
|
Q8IUN9 | MTRTYENFQYLENKVKVQGFKNGPLPLQSLLQRLCSGPCHLLLSLGLGLLLLVIICVVGFQNSKFQRDLVTLRTDFSNFTSNTVAEIQALTSQGSSLEETIASLKAEVEGFKQERQAGVSELQEHTTQKAHLGHCPHCPSVCVPVHSEMLLRVQQLVQDLKKLTCQVATLNNNASTEGTCCPVNWVEHQDSCYWFSHSGMSWAEAEKYCQLKNAHLVVINSREEQNFVQKYLGSAYTWMGLSDPEGAWKWVDGTDYATGFQNWKPGQPDDWQGHGLGGGEDCAHFHPDGRWNDDVCQRPYHWVCEAGLGQTSQESH | Function: Probable role in regulating adaptive and innate immune responses. Binds in a calcium-dependent manner to terminal galactose and N-acetylgalactosamine units, linked to serine or threonine. These sugar moieties are known as Tn-Ag and are expressed in a variety of carcinoma cells.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35446
Sequence Length: 316
Subcellular Location: Membrane
|
Q9Y240 | MQAAWLLGALVVPQLLGFGHGARGAEREWEGGWGGAQEEEREREALMLKHLQEALGLPAGRGDENPAGTVEGKEDWEMEEDQGEEEEEEATPTPSSGPSPSPTPEDIVTYILGRLAGLDAGLHQLHVRLHALDTRVVELTQGLRQLRNAAGDTRDAVQALQEAQGRAEREHGRLEGCLKGLRLGHKCFLLSRDFEAQAAAQARCTARGGSLAQPADRQQMEALTRYLRAALAPYNWPVWLGVHDRRAEGLYLFENGQRVSFFAWHRSPRPELGAQPSASPHPLSPDQPNGGTLENCVAQASDDGSWWDHDCQRRLYYVCEFPF | Function: Promotes osteogenesis by stimulating the differentiation of mesenchymal progenitors into mature osteoblasts . Important for repair and maintenance of adult bone (By similarity).
PTM: O-glycosylated. Probably sulfated on the O-glycans.
Sequence Mass (Da): 35695
Sequence Length: 323
Subcellular Location: Cytoplasm
|
Q9P126 | MQDEDGYITLNIKTRKPALISVGSASSSWWRVMALILLILCVGMVVGLVALGIWSVMQRNYLQGENENRTGTLQQLAKRFCQYVVKQSELKGTFKGHKCSPCDTNWRYYGDSCYGFFRHNLTWEESKQYCTDMNATLLKIDNRNIVEYIKARTHLIRWVGLSRQKSNEVWKWEDGSVISENMFEFLEDGKGNMNCAYFHNGKMHPTFCENKHYLMCERKAGMTKVDQLP | Function: C-type lectin-like receptor that functions as a platelet receptor for the lymphatic endothelial marker, PDPN . After ligand activation, signals via sequential activation of SRC and SYK tyrosine kinases leading to activation of PLCG2 .
PTM: Glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 26596
Sequence Length: 229
Subcellular Location: Membrane
|
Q9SKU1 | MATFDDGDFPAQTHSPSEHEDFGGYDNFSEAQQPPTQHQSGGFSSFNGDPASPNGYGFGASSPNHDFSSPFESSVNDANGNGGGSGGDAIFASDGPILPDPNEMREEGFQRREWRRLNTIHLEEKEKKEKEMRNQIITEAEDFKKAFYEKRDKTIETNKTDNREKEKLYWANQEKFHKEVDKHYWKAIAELIPREVPNIEKKRGKKDPDKKPSVNVIQGPKPGKPTDLGRMRQIFLKLKTNPPPHMMPPPPPAKDAKDGKDAKDGKDAKTGKDGKDAKGGKDAKDLKDGKPADPKVTEEKRPSPAKDASVETAKPDAAASGEGEKPVAVTEAEGTKAE | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37225
Sequence Length: 338
Subcellular Location: Cytoplasmic vesicle membrane
|
Q7XKE9 | MASFFADDGADELPRTASHPFDADDDAAPDASGGAAADDTGYGGYASFVDGGVEDVEEEEEEIAVESEGVPIGHVSGGFSPSPFSPDPELDGGDGPILPPPAQMGAEEGILLREWRRQNAIVLEEKERKEKELRAQILAEAEEFKKAFYEKRIQNCETNKVHNREREKIFVAGQEKFHAEADKQYWKSISELIPHEIATIEKRGKKDKDKKPSITVIQGPKPGKPTDLSRMRQILVKLKHAPPPHMMQPPPASAAKDGAKDGAKDGTPAPANGTKKPAESKEKPANGSPAEAEKEQPAASE | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32536
Sequence Length: 301
Subcellular Location: Cytoplasmic vesicle membrane
|
Q9USP6 | MSQFPALEDFDDGLVTAPVDDSKNNTDFLEREKLALGEDAGQFETPEDKDALLNFENDSEAEQTRFEQNFPPIDAEMQASGTFSAPKAPYMGQAEVHPPEDESGDPEPVRKWKEDQMKRIQERDESSKKLRESNIEKARKAIDDFYENFNDKRDKVIAKSRKEQEKLLEENESKSTGTTSWERILKLIDLSDKPEAHGRSTERFRELLISLAKDSNAPGAAGTTVSSSS | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25863
Sequence Length: 229
Subcellular Location: Cytoplasmic vesicle membrane
|
P17891 | MSEKFPPLEDQNIDFTPNDKKDDDTDFLKREAEILGDEFKTEQDDILETEASPAKDDDEIRDFEEQFPDINSANGAVSSDQNGSATVSSGNDNGEADDDFSTFEGANQSTESVKEDRSEVVDQWKQRRAVEIHEKDLKDEELKKELQDEAIKHIDDFYDSYNKKKEQQLEDAAKEAEAFLKKRDEFFGQDNTTWDRALQLINQDDADIIGGRDRSKLKEILLRLKGNAKAPGA | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi. The yeast light chain is important for cell growth. The light chain may help to properly orient the assembly/ disassembly of the clathrin coats.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26532
Sequence Length: 233
Subcellular Location: Cytoplasmic vesicle membrane
|
Q6UVW9 | MINPELRDGRADGFIHRIVPKLIQNWKIGLMCFLSIIITTVCIIMIATWSKHAKPVACSGDWLGVRDKCFYFSDDTRNWTASKIFCSLQKAELAQIDTQEDMEFLKRYAGTDMHWIGLSRKQGDSWKWTNGTTFNGWFEIIGNGSFAFLSADGVHSSRGFIDIKWICSKPKYFL | Function: Plays a role in modulating the extent of T-cell expansion. Enhances the expansion of TCR-stimulated T-cells by increasing their survival through enhanced expression of anti-apoptotic proteins. May modulate the capacity of T-cells to home to lymph nodes through SELL. Facilitates dedicated immune recognition of keratinocytes via interaction with its receptor KLRF2 by stimulating natural killer cell mediated cytotoxicity.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 19972
Sequence Length: 174
Subcellular Location: Cell membrane
|
P51791 | MESEQLFHRGYYRNSYNSITSASSDEELLDGAGAIMDFQTSEDDNLLDGDTAAGTHYTMTNGGSINSSTHLLDLLDEPIPGVGTYDDFHTIDWVREKCKDRERHRRINSKKKESAWEMTKSLYDAWSGWLVVTLTGLASGALAGLIDIAADWMTDLKEGICLSALWYNHEQCCWGSNETTFEERDKCPQWKTWAELIIGQAEGPGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDCGPLESSSLCDYRNDMNASKIVDDIPDRPAGVGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDWFIFKEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNGYPFLDAKEEFTHTTLAADVMRPRRSDPPLAVLTQDNMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESARKKQEGIVGSSRVCFAQHTPSLPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKDILRHMAQTANQDPASIMFN | Function: May influence large dense-core vesicle exocytosis in adrenal chromaffin cells.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90812
Sequence Length: 818
Subcellular Location: Cytoplasmic vesicle
|
P51793 | MVNAGAMSGSGNLMDFLDEPFPDVGTYEDFHTIDWLREKSRDTDRHRKITSKSKESIWEFIKSLLDAWSGWVVMLLIGLLAGTLAGVIDLAVDWMTDLKEGVCLSAFWYSHEQCCWTSNETTFEDRDKCPLWQKWSELLVNQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCNIAWCRRRKTTRLGKYPVLEVIVVTAITAIIAYPNPYTRQSTSELISELFNDCGALESSQLCDYINDPNMTRPVDDIPDRPAGVGVYTAMWQLALALIFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHHHDWIIFRNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAHIHLNGYPFLDVKDEFTHRTLATDVMRPRRGEPPLSVLTQDSMTVEDVETLIKETDYNGFPVVVSRDSERLIGFAQRRELILAIKNARQRQEGIVSNSIMYFTEEPPELPANSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQMANQDPESIMFN | Function: Strongly outwardly rectifying, electrogenic H(+)/Cl(-)exchanger which mediates the exchange of chloride ions against protons . The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons . The presence of conserved gating glutamate residues is typical for family members that function as antiporters .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84917
Sequence Length: 760
Subcellular Location: Early endosome membrane
|
P51795 | MAMWQGAMDNRGFQQGSFSSFQNSSSDEDLMDIPATAMDFSMRDDVPPLDREVGEDKSYNGGGIGSSNRIMDFLEEPIPGVGTYDDFNTIDWVREKSRDRDRHREITNKSKESTWALIHSVSDAFSGWLLMLLIGLLSGSLAGLIDISAHWMTDLKEGICTGGFWFNHEHCCWNSEHVTFEERDKCPEWNSWSQLIISTDEGAFAYIVNYFMYVLWALLFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILCHCFNKYRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLVLFYVEFHTPWHLFELVPFILLGIFGGLWGALFIRTNIAWCRKRKTTQLGKYPVIEVLVVTAITAILAFPNEYTRMSTSELISELFNDCGLLDSSKLCDYENRFNTSKGGELPDRPAGVGVYSAMWQLALTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLLGVGMEQLAYYHQEWTVFNSWCSQGADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVADALGREGIYDAHIRLNGYPFLEAKEEFAHKTLAMDVMKPRRNDPLLTVLTQDSMTVEDVETIISETTYSGFPVVVSRESQRLVGFVLRRDLIISIENARKKQDGVVSTSIIYFTEHSPPLPPYTPPTLKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLKHIAQMANQDPDSILFN | Function: Proton-coupled chloride transporter. Functions as antiport system and exchanges chloride ions against protons . Important for normal acidification of the endosome lumen. May play an important role in renal tubular function. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The absence of conserved gating glutamate residues is typical for family members that function as channels (Probable).
PTM: Ubiquitinated by NEDD4L in the presence of albumin; which promotes endocytosis and proteasomal degradation.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in)
Sequence Mass (Da): 90785
Sequence Length: 816
Subcellular Location: Golgi apparatus membrane
|
P51797 | MAGCRGSLCCCCRWCCCCGERETRTPEELTILGETQEEEDEILPRKDYESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFFVRLFTQLKFGVVQTSVEECSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPEVKCYLNGVKVPGIVRLRTLLCKVLGVLFSVAGGLFVEKEGPMIHSGSVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCSDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHPKPKLVRVLESLLVSLVTTVVVFVASMVLGECRQMSSSSQIGNDSFQLQVTEDVNSSIKTFFCPNDTYNDMATLFFNPQESAILQLFHQDGTFSPVTLALFFVLYFLLACWTYGISVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHIYSGTFALIGAAAFLGGVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDFFNKGIYDIHVGLRGVPLLEWETEVEMDKLRASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNEKEFMKGNQLISNNIKFKKSSILTRAGEQRKRSQSMKSYPSSELRNMCDEHIASEEPAEKEDLLQQMLERRYTPYPNLYPDQSPSEDWTMEERFRPLTFHGLILRSQLVTLLVRGVCYSESQSSASQPRLSYAEMAEDYPRYPDIHDLDLTLLNPRMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTYEFLQARLRQHYQTI | Function: Voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the late endosome lumen. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters.
PTM: N-glycosylated on several asparagine residues.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in)
Sequence Mass (Da): 97289
Sequence Length: 869
Subcellular Location: Late endosome membrane
|
Q9TT16 | MAGCRGSLCCCCRWCCCCGERETRTPEELTILGETQEEEDEILPRKDYESLDYDRCINDPYLEVLETMDHKKGRWYEVVKWTVVFAIGVCTGLVGLFVDFFVQLFTQLKFGVVEASVEECSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPEIKCYLNGVKVPGIVRLRTLLCKVFGVLFSVAGGLFVGKEGPMIHSGAVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGIAAAFGAPIGATLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCSDSDKKCHLWTAMDMGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHPKPKLVRVLESLLVSLVTTLVVFVASMVLGECRQMSSSSQISNGSLKLQVTSDVNSSIKAFFCPNDTYNDMATLFFNPQESAILQLFHQDGTFSPITLALFFVLYFLLACWTYGISVPSGLFVPSLLCGAAFGRLVANVLKSYIGLSHIYSGTFSLIGAAALLGGVVRMTISLTVILIESTNEITYGLPIMITLMVAKWTGDFFNKGIYDIHVGLRGVPLLEWETEVEMDKLRASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNEKEFMKGNQLISNNIKFKKSSILTRAGEQRRRSQSMKSYPSSELRNVCDEHVASEEPAEKEDLLQQMLERRYTPYPNLYPDQSPSEDWTMEERFRPLTFHGLILRSQLVTLLVRGVCYSESQSSASQPRLSYAEMAEDYPRFPDIHDLDLTLLNPRMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIVTRHNLTYEFLQARLRQHYQTI | Function: Voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the late endosome lumen. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters.
PTM: N-glycosylated on several asparagine residues.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in)
Sequence Mass (Da): 97161
Sequence Length: 869
Subcellular Location: Late endosome membrane
|
Q9UBY8 | MNPASDGGTSESIFDLDYASWGIRSTLMVAGFVFYLGVFVVCHQLSSSLNATYRSLVAREKVFWDLAATRAVFGVQSTAAGLWALLGDPVLHADKARGQQNWCWFHITTATGFFCFENVAVHLSNLIFRTFDLFLVIHHLFAFLGFLGCLVNLQAGHYLAMTTLLLEMSTPFTCVSWMLLKAGWSESLFWKLNQWLMIHMFHCRMVLTYHMWWVCFWHWDGLVSSLYLPHLTLFLVGLALLTLIINPYWTHKKTQQLLNPVDWNFAQPEAKSRPEGNGQLLRKKRP | Function: Could play a role in cell proliferation during neuronal differentiation and in protection against cell death.
PTM: Does not seem to be N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32787
Sequence Length: 286
Subcellular Location: Endoplasmic reticulum membrane
|
Q7Z7G1 | MNRQGNRKTTKEGSNDLKFQNFSLPKNRSWPRINSATGQYQRMNKPLLDWERNFAAVLDGAKGHSDDDYDDPELRMEETWQSIKILPARPIKESEYADTHYFKVAMDTPLPLDTRTSISIGQPTWNTQTRLERVDKPISKDVRSQNIKGDASVRKNKIPLPPPRPLITLPKKYQPLPPEPESSRPPLSQRHTFPEVQRMPSQISLRDLSEVLEAEKVPHNQRKPESTHLLENQNTQEIPLAISSSSFTTSNHSVQNRDHRGGMQPCSPQRCQPPASCSPHENILPYKYTSWRPPFPKRSDRKDVQHNEWYIGEYSRQAVEEAFMKENKDGSFLVRDCSTKSKEEPYVLAVFYENKVYNVKIRFLERNQQFALGTGLRGDEKFDSVEDIIEHYKNFPIILIDGKDKTGVHRKQCHLTQPLPLTRHLLPL | Function: An adapter protein which plays a role in the regulation of immunoreceptor signaling, including PLC-gamma-mediated B-cell antigen receptor (BCR) signaling and FC-epsilon R1-mediated mast cell degranulation (By similarity). Together with FGR, it acts as a negative regulator of natural killer cell-activating receptors and inhibits interferon-gamma production (By similarity). Acts as a positive regulator of both T-cell receptor and natural killer T (NKT) cell receptor signaling in CD4-positive NKT cells (By similarity). Together with MAP4K1, it enhances CD3-triggered activation of T-cells and subsequent IL2 production (By similarity). May be involved in tumor necrosis factor induced cell death by promoting reactive oxidative species generation, and MLKL oligomerization, ultimately leading to necrosis (By similarity). Involved in phosphorylation of LAT (By similarity). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity).
PTM: Tyrosine-phosphorylated upon BCR cross-linking. Tyrosine phosphorylation at both Tyr-69 and Tyr-96 are required for BCR-induced calcium response and are essential to restore PLCG2-mediated signaling in BLNK-deficient DT40 cells, but this phosphorylation is dispensable in cells expressing LAT. Interacts with the SH2 domain of PLCG1 via phosphorylated Tyr-96 (By similarity). Tyrosine phosphorylation is increased when complexed with SKAP1 and FYB1 (By similarity).
Sequence Mass (Da): 49554
Sequence Length: 428
Domain: The N-terminal proline-rich region interacts with the SH3 domain of PLCG1.
Subcellular Location: Cytoplasm
|
Q9QZE2 | MTSQGNKRTTKEGFGDLRFQNVSLLKNRSWPSLSSAKGRCRAVLEPLPDHRRNLAGVPGGEKCNSNNDYEDPEFQLLKAWPSMKILPARPIQESEYADTRYFQDTMEAPLLLPPKASVSTERQTRDVRMTHLEEVDKPTFKDVRSQRFKGFKYTKINKTPLPPPRPAITLPKKYQPLPPAPPEESSAYFAPKPTFPEVQRGPRQRSAKDFSRVLGAEEESHHQTKPESSCPSSNQNTQKSPPAIASSSYMPGKHSIQARDHTGSMQHCPAQRCQAAASHSPRMLPYENTNSEKPDPTKPDEKDVWQNEWYIGEYSRQAVEDVLMKENKDGTFLVRDCSTKSKAEPYVLVVFYGNKVYNVKIRFLESNQQFALGTGLRGNEMFDSVEDIIEHYTYFPILLIDGKDKAARRKQCYLTQPLPLARLLLTQYSSQALHE | Function: An adapter protein which plays a role in the regulation of immunoreceptor signaling, including PLC-gamma-mediated B-cell antigen receptor (BCR) signaling and FC-epsilon R1-mediated mast cell degranulation . Together with FGR, it acts as a negative regulator of natural killer cell-activating receptors and inhibits interferon-gamma production . Acts as a positive regulator of both T-cell receptor and natural killer T (NKT) cell receptor signaling in CD4-positive NKT cells . Together with MAP4K1, it enhances CD3-triggered activation of T-cells and subsequent IL2 production . May be involved in tumor necrosis factor induced cell death by promoting reactive oxidative species generation, and MLKL oligomerization, ultimately leading to necrosis . Involved in phosphorylation of LAT . May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells .
PTM: Tyrosine-phosphorylated upon BCR cross-linking . Tyrosine phosphorylation at both Tyr-69 and Tyr-96 are required for BCR-induced calcium response and are essential to restore PLCG2-mediated signaling in BLNK-deficient DT40 cells, but this phosphorylation is dispensable in cells expressing LAT . Interacts with the SH2 domain of PLCG1 via phosphorylated Tyr-96 . Tyrosine phosphorylation is increased when complexed with SKAP1 and FYB1 .
Sequence Mass (Da): 49492
Sequence Length: 435
Domain: The N-terminal proline-rich region interacts with the SH3 domain of PLCG1.
Subcellular Location: Cytoplasm
|
M1WEN7 | MSLQWLQQTRHELSWTWILLTTCIALISPLVLKGIYNVYFHPLRNIPGPKLAALTDFYAFYWNWIRDEGYSKQFSRLHEQYNSPIIRIGPNNVHTTQVEFYDVIFKSGSKWLKDKSFYKYFNGLDAMIEPYQYRTYRTHLAPLYAQRAIDGLAPKLRSDLTNSASGMMRQTKNGQTVNMAKVLRTLSTSMILHNLFSLDISLNDGDEYHPFLEAFEQLMTQSWLFVTYPMVPMVLSLIPGTSFARFNSSYTTFSNYCTAWNDEDMRKQRESEEQSTRDSHTKRYLSLKDDDARKKTAIPYPLDDVFNFVAGGSDTTAYTTACAFYHILSSPTVRENLVVELDEHSSIIRDEFDYNKIQNLPYLNAVIKETLRISVPVPGSLPRIVPQGGITIGSFSLPAGTGVSITQQAISFNEKIFPLPHSFLPERWIGPKSVGLDKWNIAFSRGPRQCIGTTLAYLELRCVIAYFFSRFDMALTGNCGDQLRWVDRFVAVNLDDVELQILADRWT | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid . DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan . The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde . Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione . The presence of easA is not required to complete this reaction . Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA . Paspalic acid is then further converted to D-lysergic acid . Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit . LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone . LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines . LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea . D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams . Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent dioxygenase easH which introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58238
Sequence Length: 507
Pathway: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
|
Q8QGQ6 | MFFTISTHKMSSIADRNDGSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGNIIYVSESVTPLLEHLPSDLVDQSVFNFIPEGEHSEIYKILSSHLLESDSLTPEYLKSKNQLEFCCHMLRGTIDPKEQPTYEYVKFIGNFKCLNNVPNSAHNGFEGTIQRSHRPSYEDKVCFIATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLDNLAKCHEHLMQYGKGKSCYYRFLTKGQQWIWLQTHYYITYHQWNSRPEFIVCTHTVVSYAEVRAERRRELGIEESLPEIKADKSQDSGSDNHINTVSLKEALERFDTSPTPSASSRSSRKSSHTAVSDHSSTPTKMTVDTSTPPRQSLSAHEKSTQRRSSLSSQSLSSQSLGQPVTQPTMSQPATLQLQSSMSQPVFQFSAQLGAMQHLKDQLEQRTRMIEANIHRQQEELRKIQEQLQIVHGQGLQLSSGPCVPKIHRTDVTVPEMFLQQSTSGLNFSSVQLTSGNSSSVQQLAPGNMQGQVVQTNQTQSGMNTGHTSTPHMIQQQPLQSSASQHNQQNVLSGHGQQSSLAGQSQNTVSTPLYNTMVISQPTAGNVVQVPSSLPQNNNQNAAAVTTFTQDRQIRFSQGQQLVTKLVTAPVACGAVMVPSTMFMGQVVTAYPTFAAQQQQPQTLPVTQQQQQQQQQSQQDQQQQQQQLTAVQQPAQPQLTQHPQQFLQTSRLLHGNQSAQLILSAAFPLQQSTFTQSHHQQHQPQQQQLSRHRTDKMTDPSKAQPQ | Function: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. CLOCK regulates the circadian expression of AANAT in the retinal photoreceptor cells. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (By similarity). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (By similarity).
PTM: Ubiquitinated, leading to its proteasomal degradation.
Sequence Mass (Da): 98659
Sequence Length: 875
Subcellular Location: Cytoplasm
|
O08785 | MVFTVSCSKMSSIVDRDDSSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKETTAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGSIIYVSESVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPEYLKSKNQLEFCCHMLRGTIDPKEPSTYEYVRFIGNFKSLTSVSTSTHNGFEGTIQRTHRPSYEDRVCFVATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLENLAKCHEHLMQYGKGKSCYYRFLTKGQQWIWLQTHYYITYHQWNSRPEFIVCTHTVVSYAEVRAERRRELGIEESLPETAADKSQDSGSDNRINTVSLKEALERFDHSPTPSASSRSSRKSSHTAVSDPSSTPTKIPTDTSTPPRQHLPAHEKMTQRRSSFSSQSINSQSVGPSLTQPAMSQAANLPIPQGMSQFQFSAQLGAMQHLKDQLEQRTRMIEANIHRQQEELRKIQEQLQMVHGQGLQMFLQQSNPGLNFGSVQLSSGNSNIQQLTPVNMQGQVVPANQVQSGHISTGQHMIQQQTLQSTSTQQSQQSVMSGHSQQTSLPSQTPSTLTAPLYNTMVISQPAAGSMVQIPSSMPQNSTQSATVTTFTQDRQIRFSQGQQLVTKLVTAPVACGAVMVPSTMLMGQVVTAYPTFATQQQQAQTLSVTQQQQQQQQQPPQQQQQQQQSSQEQQLPSVQQPAQAQLGQPPQQFLQTSRLLHGNPSTQLILSAAFPLQQSTFPPSHHQQHQPQQQQQLPRHRTDSLTDPSKVQPQ | Function: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. May play a role in spermatogenesis; contributes to the chromatoid body assembly and physiology. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (By similarity). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (By similarity). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3'. CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region. The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner (By similarity). Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis . Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 .
PTM: Ubiquitinated, leading to its proteasomal degradation.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 96393
Sequence Length: 855
Domain: Contains a Gln-rich C-terminal domain which could correspond to the transactivation domain.
Subcellular Location: Nucleus
EC: 2.3.1.48
|
Subsets and Splits