ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q5ZUS2 | MKNDNRIIKNTIKQFKEKLCKDFSQKTNITSITRKLAVFIDTILIQLFIKNKLHFGDNFCLLALGSYGRRELQLHSDIDLLILHTEKVSNIQLQRAQKFIQDCWDVGLEVSHQITTVSSCANLASQDLSVISTIMDMFLLCGHGALMEELIYQTHTLHMWPSHQYFFAKLQEQQNRYAKYGETAYNLEPNIKNGPGGLRDLQILLSISKRHFKIKKLAEGIGYGFITDKEYEELKYCQNFLWRVRFALHMLAGKPEERLSFDYQVKLAQFFGYQDQSHILAIEQFMKDYFKVIKRNRELNEMLLQWFNETIVYHQKQKIIRLDDEFQLSNRFIEVRNNRVFKQNPQSILKLFYWLVKRPDIEGVRASTIRLIRESLFLMGKRFRQSKETANIFINIFRTGNDPYDALQRMNRYGVLAHYLDCFATVTGQMQYDLFHAYTVDQHTLFVIRNISRFKKNEYAKQFPLCAKIITALEKPEILYLGALFHDIAKGRGGDHSELGAIEAQQFTQRHYMEAEDSKLIVWLVRYHLLMSQTAQRKDIYDPKTIEQFCQLLPHARYLDYLYLLTVADICGTNPTLWNAWKDSLLKELYHAAKTRLHKQQELLDEAALISIRKQYAMDILISDGISFRVIQDLWGQFKGKYFLHESPEVIARHTKAILNSKQFPVVIIMPHHSQGGTEVFIYMPHKDERFTITTSVLSNHHVTIQEAAIITCDNQFDLDTYIILDENNQAFLNEQRARDIQKSLCDHLANTGRLPAVSRRRLSRALTHFNVKTQINFIDDNTNHQTQLFLVTNDRPGLLATISRVFLTLNIHLHNAKIATAGERVEDMFYISNQTGYSLNHEEKTILKEKLILEISKSKY | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Mass (Da): 100771
Sequence Length: 861
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
|
Q60BB2 | MDGPNSDRAHDRHAFDRVAACKARIQHNTAELAERFRTGTPVADLIRERTAFIDHLLSEAWDRRIGRGATDVALVAVGGYGRGELLLHSDVDLLILLDEAAPSSRKQDLSDFLRLLWDIGLKPGHSVRSPAECAEAARTDQTIITNLLEGRLLVGSAALWEAVRSETAPERMWSSAAFFEAKMAEQRIRYSKYHNTAYNLEPNVKEGPGGLRDIQLIGWIIRRHSDARGLQDLVAHGWLTDAEYRELKEAQAFLWRIRFALHALTGRCEDRLLFDYQRELAGLFGYRGETSNEVVEGFMQDYFRTVTGVERLNELLLQLFNEAVLHRDDAFSPTPVNDHFQAVNDYLEAVHPAVFREHPLALLEVFLILQKNSALEGVRAATIRLIRQHIHLIDDAFRNDPEACRLFMDILRQPGGVTHQLRRMNRYGVLAAYLPEFGRVVGRMQYDLFHVYTVDEHTLFVVRNLRRFALEEFQQENPLCYELFQLIEKPELLYIAALMHDIAKGSDGDHSEVGERIAEEFCRRHRIGPRETLLVKWLVRHHLVMSMTAQRKDLSDPEVIHEFAQIVRNQNTLNHLYLLTVADIRATNPSLWNSWKGALLQELYTSTSWTLRRGLDTPPDYAEQISAAKDEARTLLQRFGLAEDAITAVWENIGDDYFLRFLPEEIAWHTTAIAACRPEHLPLVLLRPESLRGSVEVFIYERNRDFLFAQTTAVLDQLGLTVLDAKIIASRQGFALLSFNVLERSGTAPEGLFRLVQICDRLKEALSGGGAPPPAVSRLATRQIRHFTVPTKVFFHDDPQNRFSILELIATDRPGLLSKVGQAFMRTGIRLHNAKISTVGSRAEDIFFITDREDRPLDGEADRAALRRVLIEFVGDQ | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Mass (Da): 99886
Sequence Length: 877
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
|
A5U6S3 | MEAESPCAASDLAVARRELLSGNHRELDPVGLRQTWLDLHESWLIDKADEIGIADASGFAIVGVGGLGRRELLPYSDLDVLLLHDGKPADILRPVADRLWYPLWDANIRLDHSVRTVSEALTIANSDLMAALGMLEARHIAGDQQLSFALIDGVRRQWRNGIRSRMGELVEMTYARWRRCGRIAQRAEPDLKLGRGGLRDVQLLDALALAQLIDRHGIGHTDLPAGSLDGAYRTLLDVRTELHRVSGRGRDHLLAQFADEISAALGFGDRFDLARTLSSAGRTIGYHAEAGLRTAANALPRRGISALVRRPKRRPLDEGVVEYAGEIVLARDAEPEHDPGLVLRVAAASADTGLPIGAATLSRLAASVPDLPTPWPQEALDDLLVVLSAGPTTVATIEALDRTGLWGRLLPEWEPIRDLPPRDVAHKWTVDRHVVETAVHAAPLATRVARPDLLALGALLHDIGKGRGTDHSVLGAELVIPVCTRLGLSPPDVRTLSKLVRHHLLLPITATRRDLNDPKTIEAVSEALGGDPQLLEVLHALSEADSKATGPGVWSDWKASLVDDLVRRCRMVMAGESLPQAEPTAPHYLSLAADHGVHVEISPRDGERIDAVIVAPDERGLVSKAAAVLALNSLRVHSASVNVHQGVAITEFVVSPLFGSPPAAELVRQQFVGALNGDVDVLGMLQKRDSDAASLVSARAGDVQAGVPVTRTAAPPRILWLDTAAPAKLILEVRAMDRAGLLALLAGALEGAGAGIVWAKVNTFGSTAADVFCVTVPAELDARAAVEQHLLEVLGASVDVVVDEPVGD | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Mass (Da): 86438
Sequence Length: 808
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
|
O34563 | MKKIFSLALISLFAVILLAACGSKGSNGEASKESKKDTLAAIKDNDKIVFGVKTDTRLFGLKNPSSGEIEGFDIDIAKQIAKDILGDEKKAQFKEVTSKTRIPMLQNGDIDAIVATMTITEERKKEVDFSDVYFEAGQSLLVKKGSKIKSVENLGKGSKVLAVKGSTSSQNIREKAPEASVLEFENYAEAFTALKSGQGDALTTDNAILYGMADENKNYQLTGKPFTDEPYGIAVKKGQSALAKEINASLKKMKSDGRYDEIYKKWIKEDPAE | Function: Part of the ABC transporter complex GlnHMPQ involved in glutamine transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 29756
Sequence Length: 273
Subcellular Location: Cell membrane
|
B8ZYW0 | MSETETGNDGIKLVMAIIRPDKLADVKTALAEVGAPSLTVTNVSGRGSQPAKKGQWRGEEYTVDLHQKVKIECVVADIPAGDVVDAIAEAAHTGEKGDGKIFILPVEGAVQVRTGKEGSPAV | Function: Involved in the regulation of nitrogen metabolism . Regulates the activity of its targets by protein-protein interaction in response to the nitrogen status of the cell . Increases the activity of the glutamine synthetase 3 in the presence of 2-oxoglutarate . May regulate the activity of the ammonia channel Amt1 via direct interaction .
PTM: Uridylylated on Tyr-61.
Sequence Mass (Da): 12705
Sequence Length: 122
Subcellular Location: Cytoplasm
|
Q7VM19 | MLKITAIPALQDNYIWAIQQGQEVMIVDPAQADPVFHFLAKNKLNLTTILITHYHQDHIGGIAGLQATYPDLTIYGSHEVAQYVNHIVQAGDHLHLLNSDVEVINSAGHTAQHISFLFAQQYLFCGDALFSAGCGRVFTGDYQAQFNTLQRFKTLPESTLVFPAHEYTLTNLKFAASVLPNNNDIREAQARAETLRAQQQPTLPSTIKQELRINPFLQADNLAEFITLRQQKDQY | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 26403
Sequence Length: 235
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
|
P71374 | MLFALPALNDNYIWLYQRENLPLIIVDLPETDKLFAWLEKQNATIEAVLLTHEHDDHTQGVSAFKKRYPTVPIYGPQECEKKGATQIVNEGKILTANYQIDVIPTGGHTKQHVSFLVDNHLFCGDALFSAGCGRVFTGNYALMFEGLQRLNTLPDETIVCPAHEYTLGNLAFAETVLVDKSAVEKSAVEKQRIFVETQRAENKPSLPTTLKLEREINPFLQAKTLEEFTALRKAKDIF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 26850
Sequence Length: 238
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
|
Q2SJ47 | MTEILPIPAFNDNYIWSIQSDQGDAWVVDPGDAQPVLRHLAENHLTLRGILITHHHHDHTGGVNELLANHPVPVYGFMRSAIKAITVPLQEGDRVDLGDFSLEVLETPGHTLDHISYFGDIAGAPRLFCGDTLFSAGCGRLFEGDPAMMRQSLDKLKRLPGDTYIYCAHEYTLSNLRFAQAVMPESDEVNKRKLQCESLRARGVPTLPAVLGEEIAYNPFLMAEHPVVRRMAQEVSGSPCATATDTFAAIRAWKDRF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28532
Sequence Length: 257
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
|
Q16775 | MVVGRGLLGRRSLAALGAACARRGLGPALLGVFCHTDLRKNLTVDEGTMKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREKDQFKMPRD | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 33806
Sequence Length: 308
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Subcellular Location: Mitochondrion matrix
EC: 3.1.2.6
|
Q31H51 | MKIVGLPTLSDNYTWVIQSENADDKRAWIVDPGESQKVIHYFEENQLQLDGILLTHHHYDHTDGIMGVMDALGEVAIVSNAQGPFKPVTHPVKEGDQVQVLNETFQVIETPGHTDEHICFYHPEALFSGDTLFTGGCGKIWQNPPEQMAESLLKLRALNDDCMVYCGHEYTYANLNFAKIAEPNTPAILDRLAEVKTNTQRNIPCVPARLGLEKQTNPFLRFDHPPLMQTLMERQAQPNESVSTLFATLRAWKDELDQTNILEAGLND | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 30195
Sequence Length: 268
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
|
Q0BWR4 | MSVLIEIHQFPCLNDNYGYLVHEPGSGRTIAIDTPDAAVYLAEAEKMSWTISEIWNTHWHPDHAGGNLKIKEATGCKIIGPAGEADKIPGIDRRVKGGDTVELGGATATVIDVPGHTLGHIAFHFPDQEAAFVGDAVFALGCGRVFEGTMEMMWESLKRIKKLPKKTQLYCAHEYTASNAKFAVTIEPENKALKEYVAWIEKRRAEDKPTVPALLERELETNPFLRADLPEMQLAMGHAGNAAATFGEIRGRKDRF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28240
Sequence Length: 256
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
|
Q5QZL0 | MRVHAIEAFDDNYIWAIETNDKDKVIIVDPGEAQPVQQWLEQNSKSIETILVTHHHYDHTGGIAELIEQSPCPVIGPENPEIKTLTKTVTEGDELTVGGIQWQVLTTPGHTLDHISFYTPGFLFCGDTLFSGGCGRMFEGTPEQFTQSLLKLRKLPGETRVFCAHEYTQANVNFALKVEPENAVLQSYAEKVRMLREQEQITLPSTLQLELAINPFLRFDQKSVIAAANKHAESVKNSPEDVFYTIRQWKDNA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28539
Sequence Length: 253
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
|
Q5ZVZ3 | MTILPISAFSDNYIWTFIDKIAGVLDCVDPGEAAPIIRFAQSNQLTLRTILLTHHHYDHIGGVDSLIKQWPSCKVYGPIDERINNVTHPIKQGQSVQVGSLHFHILFNPGHTSTHISYYEPQQGWLFCGDTLFSAGCGRVFDGTIEELHESLLLFKKLPRNTKVFCAHEYTFQNLKFAHTVEPCNSSVINYMQQILKQPSSCTLPSNIDLELSINPFLRTDKEQVKQYALSHGANSSDSLDVFKVLRNQKNSFK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Mass (Da): 28736
Sequence Length: 254
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
EC: 3.1.2.6
|
S3DB70 | MYKISFAGLLRGNDKDVEALAEAATTQGFLELELDCMEAKALQKDVKFLESFAESILDSPEDVKAAYHFHKTGRFRTTGFKPLGSEEGAKAGNPDGFEFFFLPQKEILLSEFREQLNCPPLAMSNIDTLTDCFKHYERTAQMLLQRLTEGLKLGNELLNAHNTSLPCVTNMGLIRYPPQPKESGNFGHIAHTDVGSLTILAATQRGLQTLDNITQKWIWVDPSDECLFVQLGDSLKFLSRGKILPSLHRVLPSDVAPEATKYTIAYFLRPNEEAEITSDDGKVWLYKDYHCRKFDAFARPLGYRPDGEESLISLRDYTGVE | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4 . The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain . The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide . L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain . The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively .
Sequence Mass (Da): 36124
Sequence Length: 321
Pathway: Mycotoxin biosynthesis.
EC: 1.14.-.-
|
S3E7P4 | MDQNPILIQRHHHRQNFAQKAPPAPLFLIHDGGGTVFSYFLLESLGRTVYGISNPNFETESTWENGIASMAEYYVNLIKATYPSGHILLGGWSLGGLIAIQAAHILSNDPELKVVGIVMIDSTFPVEGQFNKARRLAFMAETSTSPDMKEKTRKCMDEARIQSREWKAPSWRSSATETLDNHSQTINVQIHDHVTPTCPPTVLIRALDDGSNNSRDLNETSPTETSNDSETQALGFDRYQNFNLRYVVNTPGDHFSIFNKENVKELSKKVKEACDKLVMKS | Function: Probable thioesterase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4 . The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain . The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide . L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain . The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively .
Sequence Mass (Da): 31512
Sequence Length: 281
Pathway: Mycotoxin biosynthesis.
EC: 3.1.-.-
|
S3D775 | MIAALFTTNLQLGAVGVFIFALLAFAFNKLTTWEYSIPKEVQWVDRRTQPFSYLRAKARALARSKENTLEAYFRFNKLGKAAALAVPFGRPLLLLPQTFVRWIVDQPESIISLDPIHDDFHVFVGGDLTGDHTVQELLRRELTLNLDKLISVINDEIVCALDDVLGNSPEWKSTSLADDLKTIVARTSNRVFVGKDLCRNKHYISTVKGLALVIMPETVLQDLIPQFLKGPLSRITKAFNNIYGMKKFSSLLLGVVRQRYIDVKDVLEGSGDKTRLPDDLLTWMVQKSIRKGESSANIDKLLVARIAMANLAAIETTTAAMTRSVLDLVTQGSEGGFLKAVQEETLAVVEGCNYEPSKKDVLKLVLTENAIKEALRLQVAFPGLMRQVVAPNGVTLENGLHVPCGTRLGVSAAGIHVDESIYEDPTTYNPGRFLVRDLDPRGDPSPMWKGNENYLAFSLGRRSCPGRWYVTDQLKLTLAHIFSKYEIRFEKAAETASALRKILPGAPQDRVMIRRRSVGKR | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4 . The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain . The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide . L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain . The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively .
Sequence Mass (Da): 58099
Sequence Length: 521
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
|
S3DQN8 | MLSEVIARVELLIGEQTLSGGILTFLFIVVIAHFVLTRFTVHSRFWNSQAWTGVREEWFPKMRAKVRTIGNIRQMLSDGYEGFSKQNKAFALPVIAEKPWLVLPHSCIPELLAKSDSEIDMKIIHEEQLMHEYTTGSLGRHVVDVPIQYDILLRQVNRKLPLLISAFNEELDKSFCHYWGTDTSYSEVNLSETCEKIVTQALNRIFAGKEICRDEGFLEHSRLYSEGVGRNAIMVRMLPPLLRPLLAPFITYSNRKHRDICLRVCLPVIRERVQHTAAKRADAEHKWEPPLDVLQWIIEESFARNDPKELDPRMITQRLLALNFVAIDTTHMSMAHTILDLYRSPNSDDFLVGLREECERVLQANGGQWTKSGLDDLVCVDSTIRESMRYSDLGYISLTRMVVDPKGTQFNANGTNSSSPLSVPPGIRICVPAHAIHRDAALYPSPYEFQAFRFSKAREKYRGTQTELSEPKVSIVTTTDKFLPFGHGRHACPGRFFAAQQMKLMLAYLVQNYDVEKLSTKIQNKIMVGTTKPDASLKIKVKRRKV | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4 . The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain . The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide . L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain . The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62378
Sequence Length: 546
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
|
Q9FYG4 | MKKSTRLLWLLSIIVLVAAVSKAVAEVDNDDDDDNTSLEGMTTAKRETLEVEDHTSLEGMVKREALEVKPPKAGKGKGKGKGRGTVAAGPEMNWPGQWELFMKNSGVSAMHAILMPLINKVQFYDATIWRISQIKLPPGVPCHVFDAKKNKVDCWAHSVLVDINTGDIKPLALTTDTWCSSGGLTVNGTLVSTGGFQGGANTARYLSTCENCVWIEYPKALAARRWYSTQATLPDGTFIVVGGRDALNYEYILPEGQNNKKLYDSQLLRQTDDPEENNLYPFVWLNTDGNLFIFANNRSILLSPKTNKVLKEFPQLPGGARNYPGSASSALLPIRLYVQNPAIIPADVLVCGGAKQDAYFRAERLKIYDWALKDCARLNINSAKPVWKTETMPTSRVMSDTVILPNGEILIINGAKRGSSGWHLAKEPNFAPLLYKPNKPLGQRFKELAPSTIPRVYHSIAIALPDGKVLVGGSNTNNGYQFNVEYPTELRIEKFSPPYLDPALANMRPRIVNTATPKQIKYGQMFDVKIELKQQNVAKENVMVTMLAPSFTTHSVSMNMRLLMLGINNVKNVGGDNHQIQAVAPPSGKLAPPGYYLLFAVYNGVPSVGEWIQIV | Function: Catalyzes the oxidation of aldehydes to the corresponding carboxylate by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. Substrates include glyoxal and other aldehydes (By similarity). May be regulated by the transcription factor MYB80 during anther development and play a role in tapetum and pollen development .
Catalytic Activity: an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2
Sequence Mass (Da): 67775
Sequence Length: 615
Subcellular Location: Secreted
EC: 1.2.3.1
|
A0A2H4HHY6 | MASSIKTVILFLLPLLLAYSVLAAPDITDGGDKPGPEIDDGGGDKPVPGNNDGASDYAKPAFEPEFMGAWVIDNPNAGVAAMQLQLMPNDQIVWFDTTSLGASGYKLPEGTPCPINPDANNQPDCYAHGIAYDWKTSKYRPLTLQGDAWCSSGNLWPNGNLMATGGTFSGDKAIRVIANDDPKGDFTTKIGALADTRWYSSNQVLPDGSSVVLGGRDSYSYEIVPPQMEFKPKRFDLPFMQQTTEPPLGPGRPVENNLYPFLFLLPDGNIFLFANNRAITFEPATGKTVKEFPVLPGGSRNYPPSGSAALFPLKLTADNAPVIPEIVICGGNQPNAYELVDARHVTEKQFLPALQDCNRIQPMAADAAWIPEQNMPSPRTMGDLIHLANGDMLMLNGAKKGTSGWEDATEANLTPVLYTPYKPMGQRFKELTPTTIARMYHSCSALLPDTRVLVAGSNMHQFYTFDTEFPTELRVEKFSPPYLDPALETERTQIDPANTDAVLKYGKPFKITAALMEKQPLVLGEVKVTLLYPPFTTHGFSQNQRMIVPAITSVQNGVITAVAPPSGQIAPPGYYIMFVSHLGIPGAGIWVHID | Function: Catalyzes the oxidation of aldehydes to the corresponding carboxylate by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. Substrates include glyoxal and other aldehydes (Probable). Does not have enzymatic activity on D-galactose .
PTM: The N-terminus is blocked.
Catalytic Activity: an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2
Sequence Mass (Da): 64526
Sequence Length: 594
Subcellular Location: Cytoplasm
EC: 1.2.3.1
|
Q01772 | MLSLLAVVSLAAATLAAPAASDAPGWRFDLKPNLSGIVALEAIVVNSSLVVIFDRATGDQPLKINGESTWGALWDLDTSTVRPLSVLTDSFCASGALLSNGTMVSMGGTPGGTGGDVAAPPGNQAIRIFEPCASPSGDGCTLFEDPATVHLLEERWYPSSVRIFDGSLMIIGGSHVLTPFYNVDPANSFEFFPSKEQTPRPSAFLERSLPANLFPRAFALPDGTVFIVANNQSIIYDIEKNTETILPDIPNGVRVTNPIDGSAILLPLSPPDFIPEVLVCGGSTADTSLPSTSLSSQHPATSQCSRIKLTPEGIKAGWQVEHMLEARMMPELVHVPNGQILITNGAGTGFAALSAVADPVGNSNADHPVLTPSLYTPDAPLGKRISNAGMPTTTIPRMYHSTVTLTQQGNFFIGGNNPNMNFTPPGTPGIKFPSELRIETLDPPFMFRSRPALLTMPEKLKFGQKVTVPITIPSDLKASKVQVALMDLGFSSHAFHSSARLVFMESSISADRKSLTFTAPPNGRVFPPGPAVVFLTIDDVTSPGERVMMGSGNPPPTLE | Function: Catalyzes the oxidation of aldehydes to the corresponding carboxylic acids by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. Substrates include, methylglyoxal, glycolaldehyde, acetaldehyde, formaldehyde and glyoxal. May act as a source of extracellular hydrogen peroxide required for the oxidation reactions catalyzed by the lignin peroxidases (ligninases) and manganese peroxidases, both involved in lignin degradation.
Catalytic Activity: glyoxal + H2O + O2 = glyoxylate + H(+) + H2O2
Sequence Mass (Da): 59168
Sequence Length: 559
Subcellular Location: Secreted
EC: 1.2.3.15
|
Q3HRQ2 | MILDAAIVALADLPGTWELIVPNAGIASMHTAVTRYGTVVLLDRTNIGPSRKMLPKGHCRYDPKDEVLKRDCYAHSVILDLNTNKIRPLKILTDTWCSSGQFLPDGSLLQTGGDLDGVKKIRKFVPCGPHGFCDWEELKDVELETGRWYATNQILPDGSVIIVGGRAANSVEYYPPRKGGAVQLPFLSDVEDKQMDNLYPYVHLLPNGHLFIFANNKAVMYDYTSNKVMLEYPPLDGGPRNYPSAGSSVMLALEGDYSMAIIVVCGGAQFGAFIQKSTDTPAHGSCGRIVATSPHPVWEMEDMPFGRIMGDMVMLPTGDVLIINGAQAGSQGFELASSPCFFPLLYRPNQPLGLRFMTLTPGTVPRMYHSTANLLPDGRVLIAGSNPHYFYKFAAEFPTELRIEAFSPEYLFADKANIRPVIDESPEMVRFGEQFDVFVSVSLPVVGSMEVNLASAPFATHSFSQGQRLVKLTVSPTVPDADERYRIVCTAPPGGKIAPPGYYMMFAVNLGVPSVARWVQLVP | Function: Catalyzes the oxidation of aldehydes to the corresponding carboxylate by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. Substrates include glyoxal and other aldehydes (By similarity). Involved in disease resistance against the grapevine powdery mildew E.necator. Is sufficient to confer disease resistance to E.necator . Can produce hydrogen peroxide in response to E.necator infection, and this may directly play a role in the defense mechanism during plant-pathogen interactions .
Catalytic Activity: an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2
Sequence Mass (Da): 57319
Sequence Length: 523
Subcellular Location: Secreted
EC: 1.2.3.1
|
P43220 | MAGAPGPLRLALLLLGMVGRAGPRPQGATVSLWETVQKWREYRRQCQRSLTEDPPPATDLFCNRTFDEYACWPDGEPGSFVNVSCPWYLPWASSVPQGHVYRFCTAEGLWLQKDNSSLPWRDLSECEESKRGERSSPEEQLLFLYIIYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLSCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVLSEQWIFRLYVSIGWGVPLLFVVPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVNFLIFVRVICIVVSKLKANLMCKTDIKCRLAKSTLTLIPLLGTHEVIFAFVMDEHARGTLRFIKLFTELSFTSFQGLMVAILYCFVNNEVQLEFRKSWERWRLEHLHIQRDSSMKPLKCPTSSLSSGATAGSSMYTATCQASCS | Function: G-protein coupled receptor for glucagon-like peptide 1 (GLP-1) . Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels . Plays a role in regulating insulin secretion in response to GLP-1 (By similarity).
PTM: N-glycosylation enhances cell surface expression and lengthens receptor half-life by preventing degradation in the ER.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53026
Sequence Length: 463
Subcellular Location: Cell membrane
|
P32301 | MAVTPSLLRLALLLLGAVGRAGPRPQGATVSLSETVQKWREYRHQCQRFLTEAPLLATGLFCNRTFDDYACWPDGPPGSFVNVSCPWYLPWASSVLQGHVYRFCTAEGIWLHKDNSSLPWRDLSECEESKQGERNSPEEQLLSLYIIYTVGYALSFSALVIASAILVSFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLGCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVFSEQRIFKLYLSIGWGVPLLFVIPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVNFLVFIRVICIVIAKLKANLMCKTDIKCRLAKSTLTLIPLLGTHEVIFAFVMDEHARGTLRFVKLFTELSFTSFQGFMVAVLYCFVNNEVQMEFRKSWERWRLERLNIQRDSSMKPLKCPTSSVSSGATVGSSVYAATCQNSCS | Function: G-protein coupled receptor for glucagon-like peptide 1 (GLP-1) . Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels . Plays a role in regulating insulin secretion in response to GLP-1 (By similarity).
PTM: N-glycosylation enhances cell surface expression and lengthens receptor half-life by preventing degradation in the ER.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52877
Sequence Length: 463
Subcellular Location: Cell membrane
|
P84159 | TDPGHLQDVXVAINDPKXGVFVNRK | Function: May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved.
PTM: The three different mass spectrometry results appear to arise from different glycosylation variants.
Sequence Mass (Da): 2743
Sequence Length: 25
Subcellular Location: Secreted
|
Q87KM5 | MDQFQHIDVQGAQALLEQGEAKLVDIRDPQSFAVAHAESAYHLTNDTIVAFMEDVEFEQPILVMCYHGISSQGAAQYLVNQGFEQVYSVDGGFEAWQRAQLPIVRS | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 11845
Sequence Length: 106
Subcellular Location: Cytoplasm
EC: 2.8.1.1
|
Q8ZJI3 | MEQFEATSVEQAYLRWKEGKTALVDIRDPQSYEAGHAPGAFHLTNSSLHTFMQQTDFDQPVMVMCYHGNSSKGAAQYLLQQGFDVVYSIDGGFEAWARSYPQDITSESR | Function: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 12304
Sequence Length: 109
Subcellular Location: Cytoplasm
EC: 2.8.1.1
|
F9USY3 | MHGFLGEFLGTMVLIVFGVGSGAAMNLKGNYARHQNWTFICLAWGLAVTFGVYVAGQFGSDGHLNPAVTVGFALFGYLPMANVWPYLLGQFLGAFIGAVIVIIQYYPHFQAAKTAADGNQVGIFATGPAISNPVFNFLSETIATFFFIFVLLNLGNFTQGLKPLMVGLLIVVVGQTLGGTTGFAINPARDWAPRLAYTILPVPNKGLANWGYAWVPMFGPLLGGILAAGLETIIS | Function: Transporter that facilitates the transmembrane diffusion of water, dihydroxyacetone, glycerol and H(2)O(2). Is not permeable to urea and D/L-lactic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24998
Sequence Length: 235
Subcellular Location: Cell membrane
|
F9UTW9 | MMKDPLALQLLGEFLGTFILILLGDGVVAGVTLNKSKAQNAGWVAITLGWGFAVTMGVYASSFMSPAHLNPAVSLGMAVAGKFPWAYVIPYSAAQIAGGVIGGLVVWLHYYPHWQATKDAGAILGIFATGPGIRRYFWNFISEVIGTFVLVFGLLAFTKGQFTAGLNPIVVGILIIAIGLSLGGTTGYAINPARDLGPRIAHAVLPIANKGTSDWAYSWVPIAGPLVGGALGALLFNVLP | Function: Transporter that facilitates the transmembrane diffusion of water, dihydroxyacetone, glycerol and H(2)O(2). Is not permeable to urea and D/L-lactic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25054
Sequence Length: 240
Subcellular Location: Cell membrane
|
F9UUB3 | MTGSWEARYAAEFFGTLILVLLGNGAVANAFLKNTTGNDDPGLANGGWLLVASGYGLGVMLPAMMFGSISGNHLNPAITIGQAVIGIFPWAHVAPYLIWQFLGAIAGQCLILALYWPHYRQTTDNEAVLGTFATSDHANSQLNGFVTEMVGTAVLIFGAMGLYRGMFFHQNIDIANIGVGLLIAAMVISLGGPTGPALNPARDLGPRLVHALFPVPNKGSSHWEYSWVPVVAPIVGAVIGIWIYKIFFGL | Function: Probable transporter that facilitates the transmembrane diffusion of an unknown substrate. Is not permeable to water, dihydroxyacetone, glycerol, urea, H(2)O(2) and D/L-lactic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26557
Sequence Length: 250
Subcellular Location: Cell membrane
|
F9UUD2 | MRKYLAEFLGTFMLVFLGTATVVIAKGDVLAIGLAFGLAITVSAYAFGGISGGHFNPAVTTAMLINRRIDAADAIGYIIAQIIGAIVASAAVKSFVSALGLSATLLGQTDFPKIGSGMAFFVEALVTFLFLMVILNVTSNDHGNADFAGLTIGVTLAFLIIVALNLTGGSLNPARSIGPAIFAGGSALSHLWVYILAPEVGAILAAFCARVMGSED | Function: Probable transporter that facilitates the transmembrane diffusion of an unknown substrate. Is not permeable to water, dihydroxyacetone, glycerol, urea, H(2)O(2) and D/L-lactic acid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22133
Sequence Length: 216
Subcellular Location: Cell membrane
|
P18156 | MTAFWGEVIGTMLLIIFGAGVCAGVNLKKSLSFQSGWIVVVFGWGLGVAMAAYAVGGISGAHLNPALTIALAFVGDFPWKEVPVYIAAQMIGAIIGAVIIYLHYLPHWKSTDDPAAKLGVFSTGPSIPHTFANVLSEVIGTFVLVLGILAIGANQFTEGLNPLIVGFLIVAIGISLGGTTGYAINPARDLGPRIAHAFLPIPGKGSSNWKYAWVPVVGPILGGSFGGVFYNAAFKGHITSSFWIVSVILVVVLLGLYVYTKSHSAKTLSNSKYI | Function: Mediates glycerol diffusion across the cytoplasmic membrane via a pore-type mechanism.
Catalytic Activity: glycerol(in) = glycerol(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28735
Sequence Length: 274
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Cell membrane
|
P57392 | MNIYRKKNIIKKCFMEFFGTGLVMFFGIGCLAASKLTNANFTQFEISCIWGFGVSIAIYFSSSISGAHLNPAVTIFFWLSSKLNKRKVLPYIISQTLGSFFFTMLTYYLYNNLLISFERNNNVVRGTQESLNLASIFCVYPNYNNSFIYDFIIEIFSTALFILIVLEFNNRNSNYFLYNRSVAPILTGFLVCMINLVINPLNNISLNPARDLGPKILLSLTGWGLFSFTGGNDNILYCFIPIMGPILGANLGGWIHKTLINNS | Function: Mediates glycerol diffusion across the cytoplasmic membrane via a pore-type mechanism.
Catalytic Activity: glycerol(in) = glycerol(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29720
Sequence Length: 263
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Cell membrane
|
Q21944 | MVLLAAIDQGTSSSRFLVFEADTGELVTSHQIEVRQLFPHGGWVEMDPMELYDTVVSCISKTIEKLENLGISADEIKSVGVANQRETSIVWDKETGKPLYNAIVWLDTRTSSLADEAISRTASKSKDEFRAKTGLPIHPYFSALKLKWLFQNVPEVKKAYADGNLMFGTVDTWLIWKLTGAYVTDVSNASRTLLLDLHKRKWSTQLCEFFDLPIEILPEIRSSAEVYGHFDKGPLEGVPLSGCLGDQQAAMVGHQCLNAGQTKNTYGTGTFMLCNIGTRPIISKNGLLTTVGFQFGADSPVVYALEGSGSIGGNVVRFLRDNFKFISDAKEMEGLCRSVEDTSGAYFVPSFTGLYTPYWDSTARGTILGLTQVTQREHICLAALRAVAFQSAEMIAAVEQDLEGGTKVTTLKVDGGMIANKLFNEIQADIMGRDIVTPKITEISGWGAAVAGGIGAQQISLDEFLQQSSEDNRYTPQKDDNWRSAELARWKEAVKRSCGWAQ | Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 55165
Sequence Length: 502
Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
|
Q3AB25 | MTKKYVLALDQGTTSCRAILFDRDSNIVGVAQKEFTQHYPKPGWVEHDPEEIWSTQYGVIAELMARYNVNPEEIAAIGITNQRETTVVWDRNTGKPVYNAIVWQCRRTAGICDELKAKGLEEKVRYKTGLVIDAYFSGTKIKWILDNVEGAREKAERGELLFGTIDTWLVWKLTGGKVHVTDYSNASRTMIYNIRELKWDEELLAELGIPASMLPEVKPSSYVYGETDPNVFFGHAIPISGIAGDQQAALFGQTCFEPGMAKNTYGTGCFMLMNTGDKVYESKNGLLTTIAWGIDGKVEYALEGSIFIAGAVIQWLRDGLKLIESAADSEYFASKVPDTGGVYIVPAFAGLGAPYWDMRARGTIVGLTRGTNKYHLVRAALESMAYQTRDVLSAMEADSGIKLQALKVDGGAVANNLLMQFQADILGVPVERPVNIETTAMGAAYLAGLAVGFWADKQELVAKYKVSRRFEPTMDEQTREKLYKGWQRAVTRAREWEVEE | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 55606
Sequence Length: 500
Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
|
A9WJ21 | MAKYAAAIDQGTTSTRCMIFDHSGNVICYDQKEHEQIYPRPGWVEHSPDEIWERTQSVIRGALSKGGLSASDIVAVGITNQRETTVVWNRKTGRPVYNAIVWQDTRTDQICNELAADGGQDRFRPKVGLPLATYFSGPKIRWILDNVPGAREAAEAGDVVFGNIDTFLTWWLTGGPNGGVHVTDVTNASRTMLMNLETLDWDDEILGIMGIPRQMLPKIVPSSMVYGTATGELAGVPVAGILGDQQAAMVGQTCFDVGEAKNTYGTGSFMLLNTGTKLVPSKSGLLTTVCYKFGDQPAVYALEGSIAITGALVQWLRDNLGLITSSAEVEALANLVEDNGGIYFVPAFSGLFAPYWRSDARGVIVGLTRYVNKDHLARAVLEATAYQTREVLDAMEQDSGVKLTALKVDGGMVYNNTLMQFQADILGVPVIRPKVAETTSLGAAYAAGLAVGFWSNTDEMRANWGVDHTWTPQMDEATRERLYRGWKKAVTRTFDWVE | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 54383
Sequence Length: 498
Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
|
A5CS23 | MSEKYIVAIDQGTTSTRAIVFDHSGSIVSTGQLEHEQIFPRAGWVEHDPMEIWRNTREVIGQALSKADITRHDVEAVGITNQRETAVVWDRTTGKPVYNAIVWQDTRTQKIVDRLAADGGVERFKPTVGLPLATYFSGTKIVWILENVDGAREKAEAGELMFGTTDTWVLWNLTGGTDGGVHVTDVTNASRTLFMDLETLQWDDEILKAFDVPRSMLPEIKSSSEVYGQVESSSLLREVPIAGILGDQQAATFGQAAFDQGESKNTYGTGNFLIFNTGTDIIHSQNGLLTTLGYKLGDQEPHYALEGSIAVTGSLVQWMRDNLGLVSSAAEIETLAATVEDNGGVYFVPAFSGLFAPYWRSDARGALVGLTRYVNKGHIARAALEATAFQTREVLDAVNADSGVDLTELKVDGGMIANNLLMQFQADILGVPVVRPVVAETTALGAAYAAGLAVGFWKDLDDLRQNWQEDSRWTPDMDDAERERQLRLWKKAVTKTFDWVDDDVQ | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 55485
Sequence Length: 505
Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
|
Q01V13 | MSNYIGAIDQGTTSTRFIVFDHGGRIVSVAQKEHEQIFPQPGWVEHDANEIWRRTREVIAEALEKRALSASDLAAIGITNQRETTVVWDRLSGEPVYNALVWQDTRTAAAVAELARDGGADRFRAQTGLPLATYFSALKIGWILDNVPAVRARAEAGDILFGNIDTFLLWNLTGGLHLTDCTNASRTHLMNLQTLDWDDELLAAFRIPRAMLPRIVSSSEVYGNATLASVAGVPIAGILGDQQAALVGQTCFHAGEAKNTYGTGCFLLMNTGTKPTPSKHGMLTTVAYRFATQPAVYALEGSVAITGALVQWVRDNFGLIEKSSDIEVLARTVKDNGGVYFVPAFSGLYAPYWKDNARGVIAGLTRYTNKGHLARAVLEATAFQTREVVEAMEKDSAIALETLRTDGGMVSNDLLMQFQSDILDRPVVRPAVQETTALGAAYAAGLAVGFFQDTDDLRSRWSVDHTWKPQMEPERRQELYSFWKKAVTRSFDWL | Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 54310
Sequence Length: 494
Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
|
P17695 | METNFSFDSNLIVIIIITLFATRIIAKRFLSTPKMVSQETVAHVKDLIGQKEVFVAAKTYCPYCKATLSTLFQELNVPKSKALVLELDEMSNGSEIQDALEEISGQKTVPNVYINGKHIGGNSDLETLKKNGKLAEILKPVFQ | Function: Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity . The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX2 is more active as an oxidoreductase than GRX1 . Responsible for the S-glutathionylation of DHBP synthase .
Catalytic Activity: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Sequence Mass (Da): 15861
Sequence Length: 143
Subcellular Location: Cytoplasm
EC: 1.11.1.9
|
Q5XJ54 | MANFTDAASLQQFDELLKNNSKSLTVVHFHAPWAPQCSQMNDVMAELAKEHKHTMFVKLEAEAVPEVSEKYEITSVPTFLFFKGGEKIDRLDGAHAPELTNKVQRLGSGGGGAVGAGDVPKEDLNQRLKRLINAAPCMLFMKGSPQEPRCGFSRQIIQILKDHNVQYSSFDILSDEEVRQGLKTYSNWPTYPQVYVSGELIGGLDIVKELVESGELENTFPKTVSLENRLKSLINKSPVMLFMKGNKEAAKCGFSRQILEIMNNTGVEYDTFDILEDEEVRQGLKTYSNWPTFPQLYVKGDLIGGLDIVKELLEGGELVSVLKGEN | Function: Together with bola2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins (By similarity). Required for hemoglobin maturation . Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity (By similarity).
Sequence Mass (Da): 36335
Sequence Length: 326
Domain: The thioredoxin domain lacks the two redox-active cysteines. This strongly suggests that it lacks thioredoxin activity.
Subcellular Location: Cytoplasm
|
G3XCY6 | MSANGRSILLVDDDQEIRELLETYLSRAGFQVRSVSRGADFRQALCEEEASLAILDVMLPDEDGFSLCRWIRSHQRLACMPIIMLTASSDEADRVIGLELGADDYLGKPFSPRELLARIKALLRRAQFTQVRGGDVLAFEDWRLDTVSHRLFHEDGEEFFLSGADFALLKLFLDHPQQILDRDTIANATRGREVLPLERIVDMAVSRLRQRLRDTGKAPRLIQTVRGSGYLLAAQVRPHLQP | Function: Member of the two-component regulatory system GtrS/GltR involved in the regulation of glucose metabolism and transport, as well as regulation of the exotoxin A gene expression . GltR controls the transcription of genes involved in glucose metabolism (glk and edd/gap-1) and transport (oprB) as well as the expression of toxA that encodes exotoxin A, the primary virulence factor . Acts as a repressor that is released from its target operators upon phosphorylation .
PTM: Phosphorylated by GtrS.
Sequence Mass (Da): 27413
Sequence Length: 242
Subcellular Location: Cytoplasm
|
P0AER8 | MFHLDTLATLVAATLTLLLGRKLVHSVSFLKKYTIPEPVAGGLLVALALLVLKKSMGWEVNFDMSLRDPLMLAFFATIGLNANIASLRAGGRVVGIFLIVVVGLLVMQNAIGIGMASLLGLDPLMGLLAGSITLSGGHGTGAAWSKLFIERYGFTNATEVAMACATFGLVLGGLIGGPVARYLVKHSTTPNGIPDDQEVPTAFEKPDVGRMITSLVLIETIALIAICLTVGKIVAQLLAGTAFELPTFVCVLFVGVILSNGLSIMGFYRVFERAVSVLGNVSLSLFLAMALMGLKLWELASLALPMLAILVVQTIFMALYAIFVTWRMMGKNYDAAVLAAGHCGFGLGATPTAIANMQAITERFGPSHMAFLVVPMVGAFFIDIVNALVIKLYLMLPIFAG | Function: Catalyzes the sodium-dependent, binding-protein-independent transport of glutamate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42425
Sequence Length: 401
Subcellular Location: Cell inner membrane
|
O07605 | MKRIKFGLATQIFVGLILGVIVGVIWYGNPALPTYLQPIGDLFLRLIKMIVIPIVVSSLIIGVAGAGNGKQVGKLGFRTILYFEIITTFAIILGLALANIFHPGTGVNIHEAQKSDISQYVETEKEQSNKSVAETFLHIVPTNFFQSLVEGDLLAIICFTVLFALGISAIGERGKPVLAFFEGVSHAMFHVVNLVMKVAPFGVFALIGVTVSKFGLGSLISLGKLVGLVYVALAFFLIVIFGIVAKIAGISIFKFLAYMKDEILLAFSTSSSETVLPRIMEKMEKIGCPKGIVSFVIPIGYTFNLDGSVLYQSIAALFLAQVYGIDLTIWHQITLVLVLMVTSKGMAAVPGTSFVVLLATLGTIGVPAEGLAFIAGVDRIMDMARTVVNLTGNALAAVVMSKWEGMFNPAKAETVMSQSKTEQNATISG | Function: This carrier protein is part of the Na(+)-dependent, binding-protein-independent glutamate-aspartate transport system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45920
Sequence Length: 429
Subcellular Location: Cell membrane
|
O59010 | MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYADAVKTYVKPFGDLFVRLLKMLVMPIVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQFQPKQAPPLVKILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSAETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVKVVGELAKVTAAVYVGLTLQILLVYFVLLKIYGIDPISFIKKAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYSFTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGAIMLAMVLESVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGELEKGVIA | Function: Sodium-dependent, high-affinity amino acid transporter that mediates aspartate uptake (PubMed:17435767, PubMed:19380583, PubMed:17230192, Ref.11). Has only very low glutamate transport activity . Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions, resulting in electrogenic transport (PubMed:17435767, PubMed:19380583, Ref.11). Na(+) binding enhances the affinity for aspartate . Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport . In contrast to mammalian homologs, transport does not depend on pH or K(+) ions .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44807
Sequence Length: 425
Domain: Contains eight transmembrane regions plus two helical hairpins that dip into the membrane. These helical hairpin structures play an important role in the transport process. The first enters the membrane from the cytoplasmic side, the second one from the extracellular side. During the transport cycle, the regions involved in amino acid transport, and especially the helical hairpins, move vertically by about 15-18 Angstroms, alternating between exposure to the aqueous phase and reinsertion in the lipid bilayer. In contrast, regions involved in trimerization do not move.
Subcellular Location: Cell membrane
|
B9F676 | MDPPPRPRPHRVAVLLLLLLASSPAARAWKKDEFRNCNQTPFCKRARTRAPHSLDAPLSLDAASLAVATDGSLTASLSHPSRLRPLLLRLSALPPHALRLQIDEDYSSNTPPHRRFQVPDVLLPDVEARTLHLPQPKTSAAGVSTFALSSDVDVVVKHDPFELTVRRAGSGAPVLSFNSHGLFDFEPLQESKQEGETWEEQFRSHTDTRPRGPQSITFDVSFYGADFVYGLPEHGSTSLALRPTRGPGAEESEPYRLFNLDVFEYLHESPFGLYGSIPFMIAHGDGPSSGFFWLNAAEMQIDVLAPGWDGASSTENGRIDTLWMAEAGVVDAFFFVGSEPKDVIKQYISVTGTPSMPQQFAVAYHQCRWNYRDEEDVAGVDSGFDEHDIPYDVLWLDIEHTDGKRYFTWDHSAFPNPEVMQGKIADKGRKMVTIVDPHIKRDSSFHLHEEATAKGYYVKDATGKDFDGWCWPGASSYPDMLNPEIREWWADKFSYENYKGSTPTLYIWNDMNEPSVFNGPEVTMPRDAVHYGDVEHRELHNAYGYYFHMATADGLLKRGEGKDRPFVLSRAFFAGSQRYGAIWTGDNSADWDHLKSSIPMVLTLGLTGMTFSGADIGGFFGNPEPDLLVRWYQVGAFYPFFRGHAHHDTKRREPWLFGERRTALMREAIHMRYSLLPYYYTLFREASVTGVPVMRPLWLEFPDDKETYNNGEAFMVGPSLLAQGIYEEGQKSVSVYLPGEELWYDLRNGSPYKGGVSHKLEVSEDSIPSFQRAGAIVPRKDRFRRSSTQMVNDPYTLVIALNSSSAAEGELYVDDGKSYDYQQGAFIHRRFVFADNKLTSMNIAPKNLGNKKFSTECVIERIIILGVSSGSKKAIVEPGNHEVDIELGPISLRSGSSSVAPTVRKPNVRVVDDWTIRIA | Function: Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. May be required for defense response elicited by pathogen-associated molecular patterns (PAMPs).
Catalytic Activity: H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3)
Sequence Mass (Da): 103215
Sequence Length: 919
Pathway: Glycan metabolism; N-glycan metabolism.
Subcellular Location: Endoplasmic reticulum
EC: 3.2.1.207
|
Q9US55 | MRYHGICWFIFQAAIIFAIFGSCQGAFRHQFKTAEQDGFARRNRDLAKFQKENLNWNGLFQLNSISYNSGVVSGVFEQQSENGENQHLFPFSISFLKNDVVRFQMDEKSRLEGTVEYEKNILTKRRFDASTELGFNERAEVYGKDAHLLEQTSTSLTIRYGSHGRFTVIVTFSPFKVEFQRDGEPQVVLNERHLLNMEYYRPKSSRTPEQEANGMWDETFDNFHDSKPKGPESVGLDIKFVDYGNVYGVPEHTSSLSLKETNNSDAGYTEPYRLYNVDLFEYEVDSPMSQYGAIPFMQAHKPNSDVAVFWSNAAATWIDVEKESGPSPHSQSTSTHWYSESGTLDLFIFLGPKASDVYESYSALVGRPLLPPLFSIGYHQCRWNYVSEEDVLNVDAKFDEVDMPYDTIWLDIEYASKRRYFTWDKATFPNPKAMLEKLDSKSRKLIVILDPHIKNDPNYFVSKELIDYNYAVKDKSGVDNYNADCWPGNSVWVDFFNPEAQAWWGSLYEFDRFESDKNLWIWNDMNEPSVFRGPETSMHRDAIHYGGWEHRDIHNIYGHKCINGTYNGLIKRGEGAVRPFILTRSFFAGTSALAANWIGDTMTTWEHLRGSIPTVLTNGISGMAFSGADVAGFFGNPDAELFVRWYETAIFYPFFRAHAHIDTKRREPWLYGEPYTSLVRELLRIRYRLLPTWYTAFYNSHTHGFPILYPQFLMHPEDEEGFAIDDQFYVGDSGLLVKPVTHPSIDKITIYLADDEVYFDLHDHTEYAGKGHQVVPAPLGRVPVLLRGGNILITRERIRRAAELTRNDPFTLTIAVSKIGKNASGFLYLDDGVTFNYKKGEYLIRHFSYENGILTMKDSHSNPPVSPKYSSSQKHLKVERINIYGEQTRKSIKIRKIIDSEVTEWDVSVDDSGCIRNPQLFLV | Function: Catalytic subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins.
Catalytic Activity: H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3)
Sequence Mass (Da): 106282
Sequence Length: 923
Pathway: Glycan metabolism; N-glycan metabolism.
Subcellular Location: Endoplasmic reticulum
EC: 3.2.1.207
|
P38138 | MVLLKWLVCQLVFFTAFSHAFTDYLLKKCAQSGFCHRNRVYAENIAKSHHCYYKVDAESIAHDPLENVLHATIIKTIPRLEGDDIAVQFPFSLSFLQDHSVRFTINEKERMPTNSSGLLISSQRFNETWKYAFDKKFQEEANRTSIPQFHFLKQKQTVNSFWSKISSFLSLSNSTADTFHLRNGDVSVEIFAEPFQLKVYWQNALKLIVNEQNFLNIEHHRTKQENFAHVLPEETTFNMFKDNFLYSKHDSMPLGPESVALDFSFMGSTNVYGIPEHATSLRLMDTSGGKEPYRLFNVDVFEYNIGTSQPMYGSIPFMFSSSSTSIFWVNAADTWVDIKYDTSKNKTMTHWISENGVIDVVMSLGPDIPTIIDKFTDLTGRPFLPPISSIGYHQCRWNYNDEMDVLTVDSQMDAHMIPYDFIWLDLEYTNDKKYFTWKQHSFPNPKRLLSKLKKLGRNLVVLIDPHLKKDYEISDRVINENVAVKDHNGNDYVGHCWPGNSIWIDTISKYGQKIWKSFFERFMDLPADLTNLFIWNDMNEPSIFDGPETTAPKDLIHDNYIEERSVHNIYGLSVHEATYDAIKSIYSPSDKRPFLLTRAFFAGSQRTAATWTGDNVANWDYLKISIPMVLSNNIAGMPFIGADIAGFAEDPTPELIARWYQAGLWYPFFRAHAHIDTKRREPYLFNEPLKSIVRDIIQLRYFLLPTLYTMFHKSSVTGFPIMNPMFIEHPEFAELYHIDNQFYWSNSGLLVKPVTEPGQSETEMVFPPGIFYEFASLHSFINNGTDLIEKNISAPLDKIPLFIEGGHIITMKDKYRRSSMLMKNDPYVIVIAPDTEGRAVGDLYVDDGETFGYQRGEYVETQFIFENNTLKNVRSHIPENLTGIHHNTLRNTNIEKIIIAKNNLQHNITLKDSIKVKKNGEESSLPTRSSYENDNKITILNLSLDITEDWEVIF | Function: Catalytic subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins.
Catalytic Activity: H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3)
Sequence Mass (Da): 110266
Sequence Length: 954
Pathway: Glycan metabolism; N-glycan metabolism.
Subcellular Location: Endoplasmic reticulum
EC: 3.2.1.207
|
Q28034 | MLLLLLLLPMCWAVEVRRPRGVSLTNHHFYDESKPFTCLDGSASIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKALYISSRWVNDGVCDCCDGTDEYNSGIVCENTCKEKGRKERETLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEVLRTLKEEAEKPEEAAKDQHRRLWEEQQAISKEQRERELAASAFQELDDDMDGAVSVAELQTHPELDTDGDGALSEGEAQTLLGGDAQMDAAFFYDRVWAAIRDKYRSEVLPTEYPPSPPAPDVMEPKEEQPPMPSPPTEEEDEDEEDEETEEDEDEEDEDSQGEQPKDAPPPAPAPQTASPTEEDRMPPYDEQTQAFINAAQEARNKFEEAERSLKDMEESIRNLEQEISFDFGPNGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPKLGGSPTSLGTWGSWAGPDHDKFSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMTPAACPEPPPEYPVEGDHDEL | Function: Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (By similarity). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia (By similarity).
Sequence Mass (Da): 60151
Sequence Length: 533
Pathway: Glycan metabolism; N-glycan metabolism.
Subcellular Location: Endoplasmic reticulum
|
P14314 | MLLPLLLLLPMCWAVEVKRPRGVSLTNHHFYDESKPFTCLDGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVCDCCDGTDEYNSGVICENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLWEEQLAAAKAQQEQELAADAFKELDDDMDGTVSVTELQTHPELDTDGDGALSEAEAQALLSGDTQTDATSFYDRVWAAIRDKYRSEALPTDLPAPSAPDLTEPKEEQPPVPSSPTEEEEEEEEEEEEEAEEEEEEEDSEEAPPPLSPPQPASPAEEDKMPPYDEQTQAFIDAAQEARNKFEEAERSLKDMEESIRNLEQEISFDFGPNGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPKLGGSPTSLGTWGSWIGPDHDKFSAMKYEQGTGCWQGPNRSTTVRLLCGKETMVTSTTEPSRCEYLMELMTPAACPEPPPEAPTEDDHDEL | Function: Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins . Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia (By similarity).
Sequence Mass (Da): 59425
Sequence Length: 528
Pathway: Glycan metabolism; N-glycan metabolism.
Subcellular Location: Endoplasmic reticulum
|
Q88Q27 | MFSRDLTIAKYDAELFEAMQQEALRQEEHIELIASENYTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELFGADYANVQPHAGSQANAAVYLALLSAGDTILGMSLAHGGHLTHGASVSSSGKLYNAIQYGIDGNGLIDYDEVERLAVEHKPKMIVAGFSAYSQVLDFARFRAIADKVGAYLFVDMAHVAGLVAAGVYPNPVPFADVVTTTTHKTLRGPRGGLILARANADIEKKLNSAVFPGAQGGPLEHVIAAKAICFKEALQPEFKAYQQQVVKNAQAMASVFIERGFDVVSGGTQNHLFLLSLIKQEISGKDADAALGKAFITVNKNSVPNDPRSPFVTSGLRFGTPAVTTRGFKEAECKELAGWICDILADLNNEAVIDAVREKVKAICKKLPVYGN | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 44897
Sequence Length: 417
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
Q98A81 | MAEPGTYGRSSLVQVDCRVHELLLRQRRQERTMLKLIASENFASSAVLEATGSIFANKYAEGYPGARYYAGNEIVDELETLAIERLKALFGSEHANVQPYSGSPANQAVYRALLSPRDKVMGLPLPEGGHLTHGWSVNFSGTDYQRVPYGLHDKTQQIDYDRLRETARRERPKLIWVGGTSYPRVFDYAAMAEIALEANSYLVADIAHISGLIVAGAHPNPVVHCDVVTSTSHKSIRGPRGGFILSKNEDRYQALYHSTSKHNLAKRIDRAVFPQLQGGPHMNTIAALAVALQEAATPSFRTYGHQIVKNAKALAEALLGRGYYLVTGGTDNHMLILDLRDRPLSGKAYAERLARAGIITNFDMVPGDPRDPTVTSGIRLGSPAVTSMGMREAEMVQIAAFIDSVCRQPDDQEVHASVRRDVADFCTAFDVPGISDR | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 47991
Sequence Length: 437
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
Q9KMP4 | MNANLNKAYPNVSLENFFSTPLAATNDAVFAAIQAEYTRQNEQIELIASENIVSKAVMQAQGTCLTNKYAEGYPGRRYYGGCEHVDSVEQIAIERAKMLFQCQYANVQPHSGAQANGAVMLALLQPGDTIMGMSLDAGGHLTHGARPALSGKWFNAVQYGVDRQTLEINYDSVRALALEHKPKMIIAGGSAIPRTIDFAQFRSIVDEVGALLMVDMAHIAGLVATGAHPSPLPHAHVVTTTTHKTLRGPRGGMILTNSEEIHKKINSAVFPGLQGGPLMHVIAAKAVAFGEALGPEFRTYIDSVIDNAKVLAEVLQTRGCDIVTGGTDTHLMLVDLRPKGLKGNQVEQALERAGITCNKNGIPFDEEKPMITSGIRLGTPAGTSRGFGREEFKLIGEWIGDVLDGLVASPEGNPDVEQQVRKQVKALCQRFPLYQ | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 46911
Sequence Length: 435
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
Q7MEH7 | MNSHYQNHSLENFFSTNLSATDDAVFAGIQAEFTRQNEQIELIASENIVSKAVMQAQGTCLTNKYAEGYPGRRYYGGCEHVDTVEAIAIERAKKLFNCEYANVQPHSGAQANGAVKLALLQPGDTIMGMSLDAGGHLTHGARPALSGKWFNAVQYGVDKETLEINYDDVRALAVEHKPKMIIAGGSAIPRVIDFAKFREIADEVGAILMVDMAHIAGLIATGAHPSPLPHAHVVTTTTHKTLRGPRGGMILTNHEEIIKKINSAVFPGLQGGPLMHVIAAKAVAFGEALGPEFKTYIDSVINNAKVLAEVLQTRGCDIVTGGTDTHLMLVDLRPKGLKGNKAEEALERAGITCNKNGIPFDTEKPMITSGVRLGTPAGTSRGFGAEEFKLIGHWIGDVLDGLVENPEGNAEVEQRVRKEVKALCSRFPLYQ | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 46459
Sequence Length: 431
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
P50434 | IVAGWSAYPRQLDFVRFREIADKVGAYLFVDMAHFAGLVATGLHPSPVPHAHVVTSTTHKTLAGPRGGIILSNDAEIAKKLNSAVFPGQQGGPLEHVIAGKAVAFKIAASAEFKERQQRTLAGSRILAQRLTQADVAAKGISVLTGGTDVHLVLVDLRHSELDGQQAEDLLAKVEITVNRNSVPFDPRPPMTTSGLRIGTPALATRGFSEEAFAEVAEIIAQTLIAGAEGNTGVLPELKARILELAAAHPLYPNLKKIGE | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 27579
Sequence Length: 260
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
A7MGY5 | MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPHSGSQANFAVYTALLQPGDTVLGMNLAQGGHLTHGSPVNFSGKLYNIIPYGIDESGKIDYEDMAKQAKEHKPKMIIGGFSAYSGIVDWAKMREIADSIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKGGSEELYKKLNSAVFPSAQGGPLMHVIAAKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLNRGYKVVSGGTENHLFLLDLVDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRIGSPAVTRRGFKEAEVKELAGWMCDILDNINDEAVIERVKGKVLDICARFPVYA | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 45498
Sequence Length: 417
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
Q6AAU3 | MSDPRAVDPTARDIAEKLAPAYRTMLDAIAQVEPRIAEATRAELTDQRHSLKLIASENYASLPVLATMGTWFSDKYAEGTAGHRFYAGCQNVDTVETIAAEHACALFGAEHAYVQPHSGIDANLTAYWTILAHHIETPALSEFGARTVNDLTQVDWDTLRHRFNDQRAIGMSLDAGGHLTHGFRPNISGKMFDQRSYGTDPQTGLLDYDKVAELAREFKPLVIVAGYSAYPRRVNFAKMREIADEVGAVLMVDMAHFAGLVAGKVFTGDENPIPHAQVVTTTTHKSLRGPRGGMVLTTKDYADDVDRGCPMVLGGPLSHVMAAKAVALAEARTQTFRDYAQRVANNAKALAEGLMKRGVKLVTDGTDNHINLLDVTTSFGLTGRQAEAALLDAGVVTNRNSIPTDPNGAWYTSGIRIGTPALTSRGFGPDEFDQVAELIVTTLEATTPMTASTGKPGKAKYQIADGVAQKVHDAADELLGNFPLYPGLDLA | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 52936
Sequence Length: 491
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
Q6MS85 | MNTKISPLIKESLNKELKRQQSHIELIASENYVSKAVLELNGSVLTNKYAEGYPGKRYYGGCEFIDEIESLGIQTAKELFHAEHANIQPHSGSQANDAAYKALLEPKDRVVAMSLDAGGHLTHGYPINFSGYTYDFRFYGVNKDTEQLDYQEIEKIVLEHKPKLIVAGASAYSRIIDFKKFKEIADKVGAYLMVDMAHIAGLVAAGVHPNPLEYADIVTTTTHKTLRGARGGLILCKQEFAKKVDLAVFPGSQGGPLENLIAGKTQALLEASTDEFKEYGKQIVKNTKALANVLQENGLRLVAGGSDNHLINVDVKSTLRITGKKAEKILESIGIICNKNMIPFDTEKPFYTSGIRLGTPAMTTRGFKEEEFKQVGLIIVNALKDPSEENLEKLAKQVTSLCEKFPIYQNIKY | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 45688
Sequence Length: 413
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
A0R2V7 | MAADPSSNSSSVPAANGADYADTASAAYQAALQVIESVEPRVAAATRKELADQRDSLKLIASENYASPAVLLTMGTWFSDKYAEGTIGHRFYAGCQNVDTVESVAAEHARELFGAPYAYVQPHSGIDANLVAFWAILATRVEAPELANFGAKHINDLSEADWETLRNKLGNQRLLGMSLDAGGHLTHGFRPNISGKMFHQRSYGTNPETGFLDYDAVAAAAREFKPLVLVAGYSAYPRRVNFAKMREIADEVGATLMVDMAHFAGLVAGKVFTGDEDPVPHAHVTTTTTHKSLRGPRGGMVLATEEYAPAVDKGCPMVLGGPLSHVMAAKAVALAEARQPAFQQYAQQVADNAQALADGFVKRDAGLVTGGTDNHIVLLDVTSFGLTGRQAESALLDAGIVTNRNSIPADPNGAWYTSGVRLGTPALTSRGFGADDFDRVAELIVEVLANTQPEGTSKAKYKLADGTAERVHAASSELLSANPLYPGLTL | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 51904
Sequence Length: 490
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
Q3IRX5 | MNYEQVREADPAIAAALADERDRQEDTLAMIASENHVSEAVLQAQSSELTNKYAEGYPGERYYAGCGPADDVEELAIERAEELWGAEHINVQPHSGTQANMAVYLAMLEPGDRILSLELEHGGHLSHGHPANFTGQTYEVEQYEVDPETGYIDYDELHEQAEAFEPDIIVSGYSAYPREVEFERIQEAADAVDAYHLADIAHITGLVAAGVHQSPVGVADFVTGSTHKTIRAGRGGIVMCDEEYADDIDAAVFPGAQGGPLMHNVAGKAVGFKEALQPEFEQYAQQVIDNAEALGERLQEHGFSLVSGGTDNHLVLVDLRESHPDTSGTVAEEALEAAGIVLNKNTVPGETRSAFNPSGIRAGTPALTTRGFDEQACERVADIIANVIDNPDDEGTIDEAAAEVDALCEEYPLYQGESGITDFE | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 45731
Sequence Length: 424
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
Q5XC65 | MIFDKGNVEDFDKELWDAIHAEEERQEHHIELIASENMVSKAVMAAQGSVLTNKYAEGYPGNRYYGGTECVDIVETLAIERAKKLFGAAFANVQAHSGSQANAAAYMALIEAGDTVLGMDLAAGGHLTHGSPVNFSGKTYHFVGYSVDADTEMLNYEAILEQAKAVQPKLIVAGASAYSRSIDFEKFRAIADHVGAYLMVDMAHIAGLVAAGVHPSPVPYAHIVTSTTHKTLRGPRGGLILTNDEALAKKINSAVFPGLQGGPLEHVIAAKAVAFKEALDPAFKDYAQAIIDNTAAMAAVFAQDDRFRLISGGTDNHVFLVDVTKVIANGKLAQILLDEVNITLNKNAIPFETLSPFKTSGIRIGCAAITSRGMGVKESQTIAHLIIKALVNHNQTVILEEVRQEVRQLTDAFPLYKK | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 45015
Sequence Length: 418
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
Q97R16 | MIFDKDDFKAYDADLWNAIAKEEERQQNNIELIASENVVSKAVMAAQGSILTNKYAEGYPGRRYYGGTDVVDVVETLAIERAKEIFGAKFANVQPHSGSQANCAAYMSLIEPGDTVMGMDLASGGHLTHGAPVSFSGQTYNFVSYSVDPKTELLDFDAILKQAQEVKPKLIVAGASAYSQIIDFSKFREIADAVGAKLMVDMAHIAGLVAAGLHPSPVPYAHITTTTTHKTLRGPRGGLILTNDEELAKKINSAIFPGIQGGPLEHVVAAKAVSFKEVLDPAFKEYAANVIKNSKAMADVFLQDPDFRIISGGTENHLFLVDVTKVVENGKVAQNLLDEVNITLNKNSIPYESLSPFKTSGIRIGAAAITARGFGEEESRKVAELIIKTLKNSENEAVLEEVRSAVKELTDAFPLYED | Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 45243
Sequence Length: 418
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
Q8B121 | MGQVIGFFQSLPEIINEALNIALICVALLATIKGMVNIWKSGLIQLLFFLTLAGRSCSHSFTIGRFHEFQSVTVNFTQFMSYAPSSCSVNNTHHYFKGPQNTTWGLELTLTNESMINITNSMRVFTNIHHNVTNCVQNISEHEGVLKWLLETMHLSISKPGKHIAPVMCERQKGLLIEYNLTMTKDHHPNYWNQVLYGLAKLLGSSKRLWFGACNKADCQMQSDHQHIKCNYSNCKGYTSFKYLIIQNTTWENHCEYNHLNTIHLLMSPIGQSFITRRLQAFLTWTLSDALGNDLPGGYCLEQWAVVWFGIKCFDNTAMAKCNQNHDSEFCDMLRLFDYNRNAIQSLNDQSQARLNLLTNTINSLVSDNLLMKNKLRELMNVPYCNYTRFWFINDTKNGRHTLPQCWLVSDGSYLNETRFRTQWLSESNSLYTEMLTEEYEKRQGRTPLSLVDLCFWSTLFYISTLFAHLVGFPTHRHLIGEGCPKPHRLTGSGICSCGHYGIPGKPVRWTKMSR | Function: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.
PTM: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleavage by signal peptidase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 59232
Sequence Length: 515
Domain: The N-terminus is localized at the extracellular side of the GP-C, with a part embedded in the membrane probably.
Subcellular Location: Virion membrane
|
P09991 | MGQIVTMFEALPHIIDEVINIVIIVLIVITGIKAVYNFATCGIFALISFLLLAGRSCGMYGLKGPDIYKGVYQFKSVEFDMSHLNLTMPNACSANNSHHYISMGTSGLELTFTNDSIISHNFCNLTSAFNKKTFDHTLMSIVSSLHLSIRGNSNYKAVSCDFNNGITIQYNLTFSDAQSAQSQCRTFRGRVLDMFRTAFGGKYMRSGWGWTGSDGKTTWCSQTSYQYLIIQNRTWENHCTYAGPFGMSRILLSQEKTKFFTRRLAGTFTWTLSDSSGVENPGGYCLTKWMILAAELKCFGNTAVAKCNVNHDAEFCDMLRLIDYNKAALSKFKEDVESALHLFKTTVNSLISDQLLMRNHLRDLMGVPYCNYSKFWYLEHAKTGETSVPKCWLVTNGSYLNETHFSDQIEQEADNMITEMLRKDYIKRQGSTPLALMDLLMFSTSAYLVSIFLHLVKIPTHRHIKGGSCPKPHRLTNKGICSCGAFKVPGVKTVWKRR | Function: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion .
PTM: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleavage by signal peptidase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 56131
Sequence Length: 498
Domain: The N-terminus is localized at the extracellular side of the GP-C, with a part embedded in the membrane probably.
Subcellular Location: Virion membrane
|
P34898 | MSTYSLSETHKAMLEHSLVESDPQVAEIMKKEVQRQRESIILIASENVTSRAVFDALGSPMSNKYSEGLPGARYYGGNQHIDEIEVLCQNRALEAFHLDPKQWGVNVQCLSGSPANLQVYQAIMPVHGRLMGLDLPHGGHLSHGYQTPQRKISAVSTYFETMPYRVNIDTGLIDYDTLEKNAQLFRPKVLVAGTSAYCRLIDYERMRKIADSVGAYLVVDMAHISGLIASEVIPSPFLYADVVTTTTHKSLRGPRGAMIFFRRGVRSVDAKTGKETLYDLEDKINFSVFPGHQGGPHNHTITALAVALKQAASPEFKEYQQKVVANAKALEKKLKELGYKLVSDGTDSHMVLVDLRPIGVDGARVEFLLEQINITCNKNAVPGDKSALTPGGLRIGTPAMTSRGFGEADFEKVAVFVDEAVKLCKEIQASLPKEANKQKDFKAKIATSDIPRINELKQEIAAWSNTFPLPVEGWRYDAGL | Function: Interconversion of serine and glycine.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 52978
Sequence Length: 480
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
P03540 | MGQIVTLIQSIPEVLQEVFNVALIIVSVLCIVKGFVNLMRCGLFQLVTFLILSGRSCDSMMIDRRHNLTHVEFNLTRMFDNLPQSCSKNNTHHYYKGPSNTTWGIELTLTNTSIANETSGNFSNIGSLGYGNISNCDRTREAGHTLKWLLNELHFNVLHVTRHIGARCKTVEGAGVLIQYNLTVGDRGGEVGRHLIASLAQIIGDPKIAWVGKCFNNCSGDTCRLTNCEGGTHYNFLIIQNTTWENHCTYTPMATIRMALQRTAYSSVSRKLLGFFTWDLSDSSGQHVPGGYCLEQWAIIWAGIKCFDNTVMAKCNKDHNEEFCDTMRLFDFNQNAIKTLQLNVENSLNLFKKTINGLISDSLVIRNSLKQLAKIPYCNYTKFWYINDTITGRHSLPQCWLVHNGSYLNETHFKNDWLWESQNLYNEMLMKEYEERQGKTPLALTDICFWSLVFYTITVFLHIVGIPTHRHIIGDGCPKPHRITRNSLCSCGYYKYQRNLTNG | Function: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.
PTM: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleavage by signal peptidase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 57279
Sequence Length: 503
Domain: The N-terminus is localized at the extracellular side of the GP-C, with a part embedded in the membrane probably.
Subcellular Location: Virion membrane
|
P35623 | MAAPVNKAPRDADLWSLHEKMLAQPLKDNDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELEVLCQKRALQVYGLDPECWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQLEENARLFHPRLIIAGTSCYSRNLDYARLRKIADDNGAYLMADMAHISGLVAAGVVPSPFEHCHVVSTTTHKTLRGCRAGMIFYRKGVRSVDPKTGKETRYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTPEFRAYQRQVVANCRALAEALMGLGYRVVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDKSALRPSGLRLGTPALTSRGLLEEDFRKVAHFIHRGIELTLQIQDAVGVKATLKEFMEKLAGAEEHQRAVTALRAEVESFATLFPLPGLPGF | Function: Interconversion of serine and glycine.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Mass (Da): 53025
Sequence Length: 484
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.1
|
Q1I5A5 | MDMQSRIRRLFQASIDTKQQAMDILAPHIEQASLVMVNALLSDGKMLACGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTLTSIANDYSYNEVFSKQIRALGQPGDVLLAISTSGNSANVIQAIQAAHDREMIVVALTGRDGGGMASLLLPEDVEIRVPSTVTARIQEVHLLAIHCLCDLIDSQLFGSEE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
Catalytic Activity: 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
Sequence Mass (Da): 21208
Sequence Length: 197
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.1.28
|
Q4ZNX7 | MDMQSRIRRLFQASIETKQQAMEVLAPFIEQASQVMVNALLNEGKMLACGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTITSIANDYSYNEIFSKQIRALGQPGDVLLAISTSGNSANIIQAIQAAHDREMIVVALTGRDGGGMASLLLPEDVEIRVPANVTARIQEVHLLAIHCLCDLIDSQLFGSEE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
Catalytic Activity: 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
Sequence Mass (Da): 21313
Sequence Length: 197
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.1.28
|
A1SUJ5 | MNLSIIKAELLEAEKVLQAFLADEQNLKNIEKAASLLADSFKNDGKVLSCGNGGSHCDAMHFAEELTGRYREHRPAYPAIAISDPSHISCVGNDYGYDAIFARYLEGVGRKGDVLFCLSTSGNSKNILNAIEVAKAKGISVIALTGKDGGKMSGLADVEIRVPHFGFADRIQEVHIKIIHILIYLIEKKMA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
Catalytic Activity: 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
Sequence Mass (Da): 20761
Sequence Length: 191
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.3.1.28
|
Q85041 | MCGPRNAEAVSWRSWLIEVCGFALAALTLVLTLIFASLPEMGFPCFYATVADYDTLNDTSGGVWTRQPLVAPALFLETPTVTSFFGFTATVLLAHALYAVAGAVVLRREAGRLAFQPSVVLYAASTVAAPGTLMLGALCAWTLQAVVLLMAHKQAGLAAAAYITHFVFLALFGACHACKGTGDVRAALAASPPLRRVAVHARAVVTNVVLGAVGLGAAVVGLMLGVLLANSFHISLWKTAEAALAVFTLLALALMVFVEVVVSGYVQVLPTPAFCVLVASAAFGVSAHRYFAKFSEALGETHGVVIGTRAVLAVLSLIALAMIVVRLVRACIAHRARGSRFYANVDKARTTARRYLQKRLHGRGNDEYLLAPGSGDDEFDDGDEVVYENLGFE | Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41546
Sequence Length: 393
Subcellular Location: Virion membrane
|
P09298 | MGTQKKGPRSEKVSPYDTTTPEVEALDHQMDTLNWRIWIIQVMMFTLGAVMLLATLIAASSEYTGIPCFYAAVVDYELFNATLDGGVWSGNRGGYSAPVLFLEPHSVVAFTYYTALTAMAMAVYTLITAAIIHRETKNQRVRQSSGVAWLVVDPTTLFWGLLSLWLLNAVVLLLAYKQIGVAATLYLGHFATSVIFTTYFCGRGKLDETNIKAVANLRQQSVFLYRLAGPTRAVFVNLMAALMAICILFVSLMLELVVANHLHTGLWSSVSVAMSTFSTLSVVYLIVSELILAHYIHVLIGPSLGTLVACATLGTAAHSYMDRLYDPISVQSPRLIPTTRGTLACLAVFSVVMLLLRLMRAYVYHRQKRSRFYGAVRRVPERVRGYIRKVKPAHRNSRRTNYPSQGYGYVYENDSTYETDREDELLYERSNSGWE | Function: Envelope glycoprotein important for virion assembly and egress. Plays a role in the correct incorporation of gH-gL into virion membrane. Directs the glycoprotein N (gN) to the host trans-Golgi network.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48672
Sequence Length: 435
Subcellular Location: Virion membrane
|
P52206 | LLGTGESGKSTFIKQMRIIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEKVTTFEHRYVHAIKTLWDDPGIQECYDRRREYQLSDSAKYYLADVDRIATSGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDHVLVE | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (By similarity). Together with GNAQ, required for heart development (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 23133
Sequence Length: 198
Subcellular Location: Cell membrane
|
P29992 | MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEKVTTFEHQYVSAIKTLWEDPGIQECYDRRREYQLSDSAKYYLTDVDRIATLGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems . Acts as an activator of phospholipase C . Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) . Together with GNAQ, required for heart development (By similarity).
PTM: (Microbial infection) Deamidated at Gln-209 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA.
Location Topology: Lipid-anchor
Sequence Mass (Da): 42123
Sequence Length: 359
Subcellular Location: Cell membrane
|
P45645 | MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSEEDKKGFTKLVYQNIFTAMQSMIRAMETLKILYKYEQNKANAVLIREVDVEKVMTFEQPYVSAIKTLWNDPGIQECYDRRREYQLSDSAKYYLSDVDRIATPGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C.
Location Topology: Lipid-anchor
Sequence Mass (Da): 42058
Sequence Length: 359
Subcellular Location: Cell membrane
|
P27600 | MSGVVRTLSRCLLPAEAGARERRAGAARDAEREARRRSRDIDALLARERRAVRRLVKILLLGAGESGKSTFLKQMRIIHGREFDQKALLEFRDTIFDNILKGSRVLVDARDKLGIPWQHSENEKHGMFLMAFENKAGLPVEPATFQLYVPALSALWRDSGIREAFSRRSEFQLGESVKYFLDNLDRIGQLNYFPSKQDILLARKATKGIVEHDFVIKKIPFKMVDVGGQRSQRQKWFQCFDGITSILFMVSSSEYDQVLMEDRRTNRLVESMNIFETIVNNKLFFNVSIILFLNKMDLLVEKVKSVSIKKHFPDFKGDPHRLEDVQRYLVQCFDRKRRNRSKPLFHHFTTAIDTENIRFVFHAVKDTILQENLKDIMLQ | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems . Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF12/LARG) (By similarity). GNA12-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1) . GNA12-dependent Rho signaling also regulates protein phosphatese 2A activation causing dephosphorylation of its target proteins (By similarity). Promotes tumor cell invasion and metastasis by activating RhoA/ROCK signaling pathway and up-regulating pro-inflammatory cytokine production (By similarity). Inhibits CDH1-mediated cell adhesion in process independent from Rho activation (By similarity). Together with NAPA promotes CDH5 localization to plasma membrane (By similarity). May play a role in the control of cell migration through the TOR signaling cascade .
PTM: Myristoylation of mutated N-terminus in place of original palmitoylation restores the transformation activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 44095
Sequence Length: 379
Subcellular Location: Cell membrane
|
Q63210 | MSGVVRTLSRCLLPAEAGARERRAGAARDAEREARRRSRDIDALLARERRAVRRLVKILLLGAGESGKSTFLKQMRIIHGREFDQKALLEFRDTIFDNILKGSRVLVDARDKLGIPWQHSENEKHGMFLMAFENKAGLPVEPATFQLYVPALSALWRDSGIREAFSRRSEFQLGESVKYFLDNLDRIGQLNYFPSKQDILLARKATKGIVEHDFVIKKIPFKMVDVGGQRSQRQKWFQCFDGITSILFMVSSSEYDQVLMEDRRTNRLVESMNIFETIVNNKLFFNVSIILFLNKMDLLVEKVKSVSIKKHFPDFKGDPHRLEDVQRYLVQCFDRKRRNRGKPLFHHFTTAIDTENIRFVFHAVKDTILQENLKDIMLQ | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems . Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF12/LARG) (By similarity). GNA12-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1) . GNA12-dependent Rho signaling also regulates protein phosphatese 2A activation causing dephosphorylation of its target proteins (By similarity). Promotes tumor cell invasion and metastasis by activating RhoA/ROCK signaling pathway and up-regulating pro-inflammatory cytokine production. Inhibits CDH1-mediated cell adhesion in process independent from Rho activation (By similarity). Together with NAPA promotes CDH5 localization to plasma membrane (By similarity). May play a role in the control of cell migration through the TOR signaling cascade .
Location Topology: Lipid-anchor
Sequence Mass (Da): 44065
Sequence Length: 379
Subcellular Location: Cell membrane
|
Q14344 | MADFLPSRSVLSVCFPGCLLTSGEAEQQRKSKEIDKCLSREKTYVKRLVKILLLGAGESGKSTFLKQMRIIHGQDFDQRAREEFRPTIYSNVIKGMRVLVDAREKLHIPWGDNSNQQHGDKMMSFDTRAPMAAQGMVETRVFLQYLPAIRALWADSGIQNAYDRRREFQLGESVKYFLDNLDKLGEPDYIPSQQDILLARRPTKGIHEYDFEIKNVPFKMVDVGGQRSERKRWFECFDSVTSILFLVSSSEFDQVLMEDRLTNRLTESLNIFETIVNNRVFSNVSIILFLNKTDLLEEKVQIVSIKDYFLEFEGDPHCLRDVQKFLVECFRNKRRDQQQKPLYHHFTTAINTENIRLVFRDVKDTILHDNLKQLMLQ | Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems . Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG) . GNA13-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1) (By similarity). Promotes tumor cell invasion and metastasis by activating RhoA/ROCK signaling pathway . Inhibits CDH1-mediated cell adhesion in process independent from Rho activation .
PTM: Palmitoylation is critical for proper membrane localization and signaling.
Location Topology: Lipid-anchor
Sequence Mass (Da): 44050
Sequence Length: 377
Subcellular Location: Cell membrane
|
Q96P88 | MSAGNGTPWDATWNITVQWLAVDIACRTLMFLKLMATYSAAFLPVVIGLDRQAAVLNPLGSRSGVRKLLGAAWGLSFLLAFPQLFLFHTVHCAGPVPFTQCVTKGSFKAQWQETTYNLFTFCCLFLLPLTAMAICYSRIVLSVSRPQTRKGSHAPAGEFALPRSFDNCPRVRLRALRLALLILLTFILCWTPYYLLGMWYWFSPTMLTEVPPSLSHILFLLGLLNAPLDPLLYGAFTLGCRRGHQELSIDSSKEGSGRMLQEEIHAFRQLEVQKTVTSRRAGETKGISITSI | Function: Putative receptor for gonadotropin releasing hormone II (GnRH II) which is most probably non-functional.
PTM: Phosphorylated on the C-terminal cytoplasmic tail.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32537
Sequence Length: 292
Subcellular Location: Cell membrane
|
Q95JG1 | MSAGNGTPWGSAAGEESWAASGVAVEGSELPTFSAAAKVRVGVTIVLFVSSAGGNLAVLWSVTRPQPSQLRPSPVRTLFAHLAAADLLVTFVVMPLDATWNITVQWLAEDIACRTLMFLKLMAMYSAAFLPVVIGLDRQAAVLNPLGSRSGVRKLLGAAWGLSFLLALPQLFLFHTVHRAGPVPFTQCVTKGSFKARWQETTYNLFTFRCLFLLPLTAMAICYSHIVLSVSSPQTRKGSHAPAGEFALCRSFDNCPRVRLWALRLALLILLTFILCWTPYYLLGLWYWFSPTMLTEVPPSLSHILFLFGLLNAPLDPLLYGAFTLGCQRGHQELSIDSSNEGSGRMLQQEIHALRQQEVQKTVTSRSAGETKDISITSI | Function: Receptor for gonadotropin releasing hormone II (GnRH II). This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
PTM: Phosphorylated on the C-terminal cytoplasmic tail.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41459
Sequence Length: 379
Subcellular Location: Cell membrane
|
P15586 | MRLLPLAPGRLRRGSPRHLPSCSPALLLLVLGGCLGVFGVAAGTRRPNVVLLLTDDQDEVLGGMTPLKKTKALIGEMGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKSWQKIQEPNTFPAILRSMCGYQTFFAGKYLNEYGAPDAGGLEHVPLGWSYWYALEKNSKYYNYTLSINGKARKHGENYSVDYLTDVLANVSLDFLDYKSNFEPFFMMIATPAPHSPWTAAPQYQKAFQNVFAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIQFLDNAFRKRWQTLLSVDDLVEKLVKRLEFTGELNNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRGPGIKPNQTSKMLVANIDLGPTILDIAGYDLNKTQMDGMSLLPILRGASNLTWRSDVLVEYQGEGRNVTDPTCPSLSPGVSQCFPDCVCEDAYNNTYACVRTMSALWNLQYCEFDDQEVFVEVYNLTADPDQITNIAKTIDPELLGKMNYRLMMLQSCSGPTCRTPGVFDPGYRFDPRLMFSNRGSVRTRRFSKHLL | Cofactor: Binds 1 Ca(2+) ion per subunit.
PTM: The form A (78 kDa) is processed by internal peptidase cleavage to a 32 kDa N-terminal species (form B) and a 48 kDa C-terminal species.
Catalytic Activity: Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.
Sequence Mass (Da): 62082
Sequence Length: 552
Subcellular Location: Lysosome
EC: 3.1.6.14
|
Q9C7G6 | MGHLPQSLYSAAGPKFPYPGSSGLGVDQRKLTWSRFPVFLRCASTESLTSLTQNNAAEIELKYLVSQHGWDVRRLNRDDEDEIRRVSLVQAEAFHIPLALFDDFFFMFFQAEVLSALLYKLKNSPPDRYACLVAEQTSETETLSSSSVVGVVDVTAQTESSVLRYFPGVEEYLYVSGLAVSKSQRRKKMASTLLKACDVLCYLWGFKLLALRAYEDDAAARNLYSNAGYSVVETDPLWTSTWIGRKRRVLMSKRFS | Function: Protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA), with a preference for leucine, methionine, serine, valine and to a lower extent threonine and alanine as substrates (can also use glycine), and epsilon-lysine acetylation (KA) of several plastid proteins.
PTM: Autoacetylated.
Catalytic Activity: acetyl-CoA + an N-terminal L-alpha-aminoacyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alpha-aminoacyl-[protein]
Sequence Mass (Da): 28917
Sequence Length: 256
Subcellular Location: Plastid
EC: 2.3.1.255
|
Q555X4 | MSNFYNNNPRRNTFRLTERIKKKPYQTLIVFILIFLFLYVFGPFGEKKSNNNNNNHPVSKTSSFTESLYTKFQTETFAYRANGDLKKYDISIITQFTVDRFDRIAMMADKWRAPISAAVYITSFKDIDEVFKLVRNSFAVTEFVDLHFLFANKTRYPVNNLRNLALRNARTEWCLLLDVDFISPLGMYDYLHSTLEKLDTSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNENNDNDNGNNNNNNDNEKNFKKKQEDLKIDPNDFEGDLKAIEKLKRNGEKLYVKNLKKVLDGSENNLGKNINFNNNNNDNNNKDDGGGGGYYLNSDNSNINNNNKIAFVIPSFSSSISRFDFPDNKKDLLDFIKQDLIKEINSGVCPKCHGPTNYSRWYLSSEPYLVQYKWIYEPFLLYNRSQIHDYDERLKGYGFDKNSHTFGMAAAGFDFVVLPDAWIIHMNHVSKPWEGADTFNEQMFDCLSIVCESILPDAKSKNGYDPNAKLFNEPLKNNDNCLTREHW | Function: May have a role in modulating cell adhesion and glycosylation. Essential for development.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 59898
Sequence Length: 516
Subcellular Location: Membrane
|
Q9Y761 | MAFGSRRKIKAILVAASAMVFISLLGTFGSDSVYEKIKTFDVSWGSNVSGGLSSMLQKKKTVLYDPENIKQIPYSTIQKLYDHELESVTNIDWSQYAYVNYVADKNYVCSSMIHFNRLHESGTQAKLVMLVAKELTELPEDDSVTRMLAQFKEISDNCIVKPVENIVLSQGSAQWMTSMTKLRVFGMVEYKRIVYFDSDSIITRNMDELFFLPDYIQFAAPATYWFLNDNDLPQLIEDNKQIALANNQTAELTEIEDILQQKIDDSEDIYNFLPNLPKRLYPKSDNARIDSTDNTYFKYAATLMVIKPEQEMFERLEQEVLPKYLNTTNKYDMDLINIEFYDFNGTAEAQKKLYDQSPQSFKPSMLVLPFNQYTLLTKTIREKNRVKLLSNDMLGYETKKPTDFRDASYYHFSDSPIGKPWKYKGLEDIPCNPGDSEEICNAWHSIFSNFWDGRAKYCVA | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 53169
Sequence Length: 460
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q6CT96 | MLKRKVRYLLLIVVVFTGIILSVEAIMRFQLNKNVDYYLKFFDKHKDNIENMYDPLNIKQIPYSTIDQLYTKRQSEAEPIDWDKFAYVNYITDFEYLCNTLIQFRKLNDSGSKAKLLALVTDTLVNKSKENKEVEALLNKIKSVSDRVAVTEVGSVIQPNDHTPWSKSLTKLAIFNLTDYERIIYMDNDAIIHDKMDELFFLPSYVKFAAPISYWFVTADDLRTVSTDTKKLFKTNKLDPIEKKLASRVKNSLEIYNHLPNLPQHFYSKSMNFIIDIDGFQKSDNKVNFATHLMVIKPDVTMANDIRDNILPRYLKAKEEYDTDLINEELYNFKELIYYQFKIFRKIQYLFKPSVLILPYTKYGLLTKSIDDKRQKDLLKNAILGYERKEKDDLIQDAKFIHFSDYPLSKPWFYSNADDIQCSKKYSISDENCQLWKSLYKEYLESRAICQVN | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 53508
Sequence Length: 453
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q4WBL2 | MGNKKATLLPYRRDSASSEADFFDIPDEPCLAIAKRQLRRIRTWIFFAVFIILILWFRREAPSPAPVSHIDYNKVDWSRYAYSQYATSSAYLCNAVMVFEALERLGSRADRVLFYPEDWDLFVADDHDRDSQLLVLAKEKYKALLVPISAEMIKAGGGSGESWDKSIAKLLAFGETEYDRVIHIDSDVTVLQSMDELFFLPPAKVAMPRAYWALPDTKTLSSLLIVIEPSYREFKALMESAQPALHGQVEVDSNETQRYDMELLNNRYADSALVLPHRQYGLVTGEFRKKDHRSFFGNDYETWDPDKVLAEAKLVHFSDWPLPKPWVLSNQKLLAEILPKCDFKPGTMQERGCRDREVWKSLYEDFRRRRKVCPKIRTIHTEYG | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 44512
Sequence Length: 384
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q59ZI3 | MTSKSSSWKALLKNWEFKVAAFIGIYFLISHVVLETTDVVNEKGLKSHLKVLPEEVIDYYGKQPFSNVDKYAYMQYATNYDYLNLAIINFIHLRKANTKIPNLVIIYDEVLHYYASDKWSELYQVANQYKITLKAAPLIKASYQDDSNWAASFTKFHIFNQVEYDRIVFFDSDSMLVDIPNEIDFDNMESRFNHIDELFKIPQELSFASPQAYWLNNVVEGKSPRPRKNVEIPNKKRYSLRMKKLVNDLSIYQDFNLLPSLIYENHYFDNANHFFANHIMVITPSKNTFQELMRYIHNPWWWSITNRGSLRKPNDYDMEILNKYLNNELQRKRINVGILPHRVYGVLTGEFGEEWHERFVVEPQYLPFINKKSNKGWSPLEFFKKIKVVHFSDSPIPKPWEEENNEEHYNIKKIYCDKGDMEKFHKDYPVYKPRLTDDCDSVSIWNWFREQFYKERSGYWFA | Function: N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 55312
Sequence Length: 462
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
Q54CL4 | MFTDQQKIGAMLSAMGLFFGFLGVLLFLDRNLLALGNLLLVSGIVLILGLQKTTKFFAQKKKIKGTILFFFGIVVLLVTRWTFVGMVIEIFGFVNLFGDAFPIVISILRKLPIIGNILNHPLVNRLLQKADSGNELPF | Function: May be involved in fusion of ER-derived transport vesicles with the Golgi complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15343
Sequence Length: 138
Subcellular Location: Golgi apparatus membrane
|
Q9USJ2 | MWLSDLQKIGVGTTALGFLFMIMGIFMFFDGPLLSLGNLLLVFGFFMIAGFSKSVSFFLRKDRMLGSISFFSGLLLTLFHFPIIGFFVECLGFFNLFKVFYPLIISFLRTVPYIGPYIDRLTSYQQSPV | Function: Nonessential protein required for the fusion of ER-derived transport vesicles with the Golgi complex. Can be replaced by sft2 (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14707
Sequence Length: 129
Subcellular Location: Golgi apparatus membrane
|
Q03554 | MWLTEAQKFGVAFTFGGFLFFLFGIFTFFDRALLALGNILFLIGVFLIIGSQKTYIFFTRPNKRRGSLFFLVGAFLILLKWTFLGFIIESLGIIGLFGDFFGVIVQFLRSMPIIGPILSHPAIAPIVDKLAGVRVLPV | Function: Nonessential protein required for the fusion of ER-derived transport vesicles with the Golgi complex. Can be replaced by SFT2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15431
Sequence Length: 138
Subcellular Location: Golgi apparatus membrane
|
A0A3L6E0R4 | MGEITNVMEYQAIAKQKLPKMAYDYYASGAEDEWTLQENREAFSRILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAAAAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRKVVEQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPHLTLKNFEGLDLGKMDQAADSGLASYVAGQVDRTLSWKDVKWLQTITTLPILVKGVLTAEDTRLAVANGAAGIIVSNHGARQLDYVPATISALEEVVKAARGQLPVFVDGGVRRGTDVFKALALGAAGVFVGRPVVFSLAAAGEAGVSNVLRMLRDEFELTMALSGCTSLAEITRKHIITESDKLSAIPSRL | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2 . Is an essential enzyme in photorespiration in plants . Photorespiration plays a vital role in C4 photosynthesis in Z.mays and is essential for maize seedling development and maintaining low (non-toxic) levels of glycolate .
Catalytic Activity: glycolate + O2 = glyoxylate + H2O2
Sequence Mass (Da): 40095
Sequence Length: 369
Pathway: Photosynthesis; photorespiration; glycine from 2-phosphoglycolate: step 2/3.
Subcellular Location: Peroxisome
EC: 1.1.3.15
|
P13006 | MQTLLVSSLVVSLAAALPHYIRSNGIEASLLTDPKDVSGRTVDYIIAGGGLTGLTTAARLTENPNISVLVIESGSYESDRGPIIEDLNAYGDIFGSSVDHAYETVELATNNQTALIRSGNGLGGSTLVNGGTWTRPHKAQVDSWETVFGNEGWNWDNVAAYSLQAERARAPNAKQIAAGHYFNASCHGVNGTVHAGPRDTGDDYSPIVKALMSAVEDRGVPTKKDFGCGDPHGVSMFPNTLHEDQVRSDAAREWLLPNYQRPNLQVLTGQYVGKVLLSQNGTTPRAVGVEFGTHKGNTHNVYAKHEVLLAAGSAVSPTILEYSGIGMKSILEPLGIDTVVDLPVGLNLQDQTTATVRSRITSAGAGQGQAAWFATFNETFGDYSEKAHELLNTKLEQWAEEAVARGGFHNTTALLIQYENYRDWIVNHNVAYSELFLDTAGVASFDVWDLLPFTRGYVHILDKDPYLHHFAYDPQYFLNELDLLGQAAATQLARNISNSGAMQTYFAGETIPGDNLAYDADLSAWTEYIPYHFRPNYHGVGTCSMMPKEMGGVVDNAARVYGVQGLRVIDGSIPPTQMSSHVMTVFYAMALKISDAILEDYASMQ | Catalytic Activity: beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
Sequence Mass (Da): 65638
Sequence Length: 605
Subcellular Location: Secreted
EC: 1.1.3.4
|
P05414 | MEITNVNEYEAIAKQKLPKMVYDYYASGAEDQWTLAENRNAFSRILFRPRILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPFLTLKNFEGIDLGKMDKANDSGLSSYVAGQIDRSLSWKDVAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGARQLDYVPATIMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFIGRPVVFSLAAEGEAGVKKVLQMMRDEFELTMALSGCRSLKEISRSHIAADWDGPSSRAVARL | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2 . Is a key enzyme in photorespiration in green plants (Probable). To a lesser extent, is also able to use L-lactate and 2-hydroxbyutanoate as substrate in vitro, but shows almost no activity with L-mandelate .
Catalytic Activity: glycolate + O2 = glyoxylate + H2O2
Sequence Mass (Da): 40286
Sequence Length: 369
Pathway: Photosynthesis; photorespiration; glycine from 2-phosphoglycolate: step 2/3.
Subcellular Location: Peroxisome
EC: 1.1.3.15
|
F5HGP1 | MGKKEMIMVKGIPKIMLLISITFLLLSLINCNVLVNSRGTRRSWPYTVLSYRGKEILKKQKEDILKRLMSTSSDGYRFLMYPSQQKFHAIVISMDKFPQDYILAGPIRNDSITHMWFDFYSTQLRKPAKYVYSEYNHTAHKITLRPPPCGTVPSMNCLSEMLNVSKRNDTGEKGCGNFTTFNPMFFNVPRWNTKLYIGSNKVNVDSQTIYFLGLTALLLRYAQRNCTRSFYLVNAMSRNLFRVPKYINGTKLKNTMRKLKRKQALVKEQPQKKNKKSQSTTTPYLSYTTSTAFNVTTNVTYSATAAVTRVATSTTGYRPDSNFMKSIMATQLRDLATWVYTTLRYRNEPFCKPDRNRTAVSEFMKNTHVLIRNETPYTIYGTLDMSSLYYNETMSVENETASDNNETTPTSPSTRFQRTFIDPLWDYLDSLLFLDKIRNFSLQLPAYGNLTPPEHRRAANLSTLNSLWWWSQ | Function: Plays a role in viral entry into host cells. Forms a trimeric complex at the surface of the viral envelope together with gH and gL. This complex is required for entry in host fibroblasts . Mechanistically, engages host receptor(s) including PDGFRA to mediate infection .
PTM: N-glycosylated.
Sequence Mass (Da): 54701
Sequence Length: 472
Subcellular Location: Virion membrane
|
Q96P66 | MTSTCTNSTRESNSSHTCMPLSKMPISLAHGIIRSTVLVIFLAASFVGNIVLALVLQRKPQLLQVTNRFIFNLLVTDLLQISLVAPWVVATSVPLFWPLNSHFCTALVSLTHLFAFASVNTIVVVSVDRYLSIIHPLSYPSKMTQRRGYLLLYGTWIVAILQSTPPLYGWGQAAFDERNALCSMIWGASPSYTILSVVSFIVIPLIVMIACYSVVFCAARRQHALLYNVKRHSLEVRVKDCVENEDEEGAEKKEEFQDESEFRRQHEGEVKAKEGRMEAKDGSLKAKEGSTGTSESSVEARGSEEVRESSTVASDGSMEGKEGSTKVEENSMKADKGRTEVNQCSIDLGEDDMEFGEDDINFSEDDVEAVNIPESLPPSRRNSNSNPPLPRCYQCKAAKVIFIIIFSYVLSLGPYCFLAVLAVWVDVETQVPQWVITIIIWLFFLQCCIHPYVYGYMHKTIKKEIQDMLKKFFCKEKPPKEDSHPDLPGTEGGTEGKIVPSYDSATFP | Function: Orphan receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56716
Sequence Length: 508
Subcellular Location: Cell membrane
|
A0MD30 | MQWGHCGVKSASCSWMPSLSFLSVWLILSFSLPYCLGSPSQDGYWSFFSEWFAPRFSVRALPFTLPNYRRSYESLLPNCRPDVPQFAFKHPLGILWHMRVSHLIDEMVSRRIYQTMEHSGQAAWKYVVGEATLTKLSKLDIVTHFQHLAAVEADSCRFLSSRLVMLKNLAVGNVSLQYNTTLDRVELIFPTPGTRPKLTDFRQWLISVHASIFSSVASSVTLFIVLWLRIPALRYVFGFHWPTATHHSS | Function: Minor envelope protein. Along with GP4, serves as the viral attachment protein responsible for mediating interactions with CD163 thereby playing a role in virus entry into susceptible host cells.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 28561
Sequence Length: 249
Subcellular Location: Virion membrane
|
P28992 | MQRFSFSCYLHWLLLLCFFSGSLLPSAAAWWRGVHEVRVTDLFKDLQCDNLRAKDAFPSLGYALSIGQSRLSYMLQDWLLAAHRKEVMPSNIMPMPGLTPDCFDHLESSSYAPFINAYRQAILSQYPQELQLEAINCKLLAVVAPALYHNYHLANLTGPATWVVPTVGQLHYYASSSIFASSVEVLAAIILLFACIPLVTRVYISFTRLMSPSRRTSSGTLPRRKIL | Function: Minor envelope protein. Part of the glycoproteins heterotrimer GP2b-GP3-GP4 which is probably responsible for the attachment to target host cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25579
Sequence Length: 227
Subcellular Location: Virion membrane
|
P28968 | MGFIYARKLLLCMAVSIYAIGSTTTTETTTSSSSTSGSGQSTSSGTTNSSSSPTTSPPTTSSSPPTSTHTSSPSSTSTQSSSTAATSSSAPSTASSTTSIPTSTSTETTTTTPTASTTTPTTTTAAPTTAATTTAVTTAASTSAETTTATATATSTPTTTTPTSTTTTTATTTVPTTASTTTDTTTAATTTAATTTAATTTAATTTAATTTAATTTAATTTAATTSSATTAATTTAATTTAATTTAATTTAATTTAATTTGSPTSGSTSTTGASTSTPSASTATSATPTSTSTSAAATTSTPTPTSAATSAESTTEAPTSTPTTDTTTPSEATTATTSPESTTVSASTTSATTTAFTTESHTSPDSSTGSTSTAEPSSTFTLTPSTATPSTDQFTGSSASTESDSTDSSTVPTTGTESITESSSTTEASTNLGSSTYESTEALETPDGNTTSGNTTPSPSPRTPSFADTQQTPDNGVSTQHTTINDHTTANAQKHAGHHRGRAGGRRGSPQGGSHTTPHPDRLTPSPDDTYDDDTNHPNGRNNSIEIVPQLPPDRPIIELGVATLRKNFMEASCTVETNSGLAIFWKIGNASVDAFNRGTTHTRLMRNGVPVYALVSTLRVPWLNVIPLTKITCAACPTNLVAGDGVDLNSCTTKSTTIPCPGQQRTHIFFSAKGDRAVCITSELVSQPTITWSVGSDRLRNDGFSQTWYGIQPGVCGILRSEVRIHRTTWRFGSTSKDYLCEVSASDSKTSDYKVLPNAHSTSNFALVAATTLTVTILCLLCCLYCMLTRPRASVY | Function: Virulence factor.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 80343
Sequence Length: 797
Subcellular Location: Virion membrane
|
P25088 | RRGSPQGGSHTTPHPDRLTPSPDDTYDDDTNHPNGRNNSIEIVPQLPPDRPLIELGVATLRKNFMEASCTVETNSGLAIFWKIGKPSVDAFNRGTTHTRLMRNGVPVYALVSTLRVPWLNVIPLTKITCAACPTNLVAGDGEDLNSCTTKSTTIPCPGQQRTHIFFSAKGHRAVCITSELVSQPTITWSVGSDRLRNDGFSQTWYGIQPGVCGILRSRFAFTAPPGALDQHQRTISVRSAHRTQRRAITKCYPTPTQLPTSL | Function: Virulence factor.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28695
Sequence Length: 262
Subcellular Location: Virion membrane
|
O43292 | MGLLSDPVRRRALARLVLRLNAPLCVLSYVAGIAWFLALVFPPLTQRTYMSENAMGSTMVEEQFAGGDRARAFARDFAAHRKKSGALPVAWLERTMRSVGLEVYTQSFSRKLPFPDETHERYMVSGTNVYGILRAPRAASTESLVLTVPCGSDSTNSQAVGLLLALAAHFRGQIYWAKDIVFLVTEHDLLGTEAWLEAYHDVNVTGMQSSPLQGRAGAIQAAVALELSSDVVTSLDVAVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPEDWTSLDGPLQGLQTLLLMVLRQASGRPHGSHGLFLRYRVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFLYLLPGLSRFVSIGLYMPAVGFLLLVLGLKALELWMQLHEAGMGLEEPGGAPGPSVPLPPSQGVGLASLVAPLLISQAMGLALYVLPVLGQHVATQHFPVAEAEAVVLTLLAIYAAGLALPHNTHRVVSTQAPDRGWMALKLVALIYLALQLGCIALTNFSLGFLLATTMVPTAALAKPHGPRTLYAALLVLTSPAATLLGSLFLWRELQEAPLSLAEGWQLFLAALAQGVLEHHTYGALLFPLLSLGLYPCWLLFWNVLFWK | Function: Component of the GPI transamidase complex, necessary for transfer of GPI to proteins . Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67623
Sequence Length: 621
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
|
Q8G7C3 | MGKNITVLGAGAWGTAFGQVLADAGNTVTMWAKEQQIVEGIRDHHHNAVRLPSVEKLPDNMTATGDRAEAVKNADIVVVAIAAQFARVALVEFKGLIPDHAIVVSLMKGIERGTNKRMDEVVRESLDLPADRFAAISGPNLSKEIADRHPAATVVACTNLDNATKVAEACTTSYFKPFVTTDVIGLEMCGSLKNVTALAVGMARGAGYGENTAAMIETRGLAELTALGVAAGADPKTFFGLAGVGDLIATCGSSLSRNYTFGANLGKGLTVEEATKVSNGVAEGVPTTDAVVALGDQLDVPTPLAYQMSRVLNEGISCSEMLAGLFGHEVTGE | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 34616
Sequence Length: 333
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
Q7VS47 | MSQARPATLRVAVLGAGSWGTALAAAASRRHPTVLWARDGAQAQAMAARHENTRYLPGVALPHALQVSADLAQALAHLAHDPAHALIILGVPVAGMTPLCTELAARLPALGLQAVPLVWTCKGFEEQTARLPHETVQAALGAMPGLAAGVLSGPSFAREVAQGLPVALTVASGSSAVRDAVTTALHGAAVRIYASTDVVGVEVGGALKNVIAVACGICDGLALGTNARAALITRGLAEMARFGAALGAQQETFAGLTGLGDLVLTATGELSRNRRVGLEIGAGRKLADILASGMTAEGVRCARAARDRARALNIELPITEAVCAVLFEGLSPMTAVSALLAREARPESPTP | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 35664
Sequence Length: 351
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.