ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P33274 | MSQLSLSWLGLGPEVAFPWQTLLLFGASWILAQILTQIYAAYRNFRRLRGFPQPPKRNWLMGHVGMVTPTEQGLKELTRLVGTYPQGFLMWIGPMVPVITLCHSDIVRSILNASAAVALKDVIFYTILKPWLGDGLLVSAGDKWSRHRRMLTPAFHFNILKPYVKIFNDSTNIMHAKWKRLISEGSSRLDMFEHVSLMTLDSLQKCVFSFDSNCQEKSSEYIAAILELSALVAKRHQQPLLFMDLLYNLTPDGMRFHKACNLVHEFTDAVIRERRRTLPDQGLDEFLKSKAKSKTLDFIDVLLLTKDEDGKELSDEDIRA... | Function: A cytochrome P450 monooxygenase involved in the metabolism of arachidonic acid and its oxygenated derivatives . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (... |
P78329 | MSQLSLSWLGLWPVAASPWLLLLLVGASWLLAHVLAWTYAFYDNCRRLRCFPQPPRRNWFWGHQGMVNPTEEGMRVLTQLVATYPQGFKVWMGPISPLLSLCHPDIIRSVINASAAIAPKDKFFYSFLEPWLGDGLLLSAGDKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQLLASEGSACLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVSKRHHEILLHIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFIDVLLLSKDEDGKKLSDEDIRA... | Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, eicosanoids and vitamins . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH ... |
Q08477 | MPQLSLSSLGLWPMAASPWLLLLLVGASWLLARILAWTYTFYDNCCRLRCFPQPPKRNWFLGHLGLIHSSEEGLLYTQSLACTFGDMCCWWVGPWHAIVRIFHPTYIKPVLFAPAAIVPKDKVFYSFLKPWLGDGLLLSAGEKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQLLASEGSARLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVTKRHQQILLYIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFIDVLLLSKDEDGKKLSDEDIRA... | Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and their oxygenated derivatives (oxylipins) . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons... |
Q99N16 | MSQLSMSWMGLGHTAASPWLLLLLAGASCLLAYILTPIYGVFENSLRLRCFPQPPKRNWILGHLGLIQSSEEGLLYIQSLVRTFRDACCWWVGPLHPVIRIFHPAFIKPVVLAPALVAPKDTVFYRFLKPWLGDGLLMSTGDKWSRHRRMLTPAFHFNILKPYVKVFNDSTNIMHAKWQRLASKGSAYLNMFEHISLMTLDSLQKCVFSFDSNCQEKPSEYITAILELSTLVARRHQRLLLHVDLFYYLTHDGMRFRKACRLVHDFTDAVIRERRRTLLDQGGVDVLKAKAKAKTLDFIDVLLLSKDEHGKALSDEDIRA... | Function: A cytochrome P450 monooxygenase involved in the metabolism of the pro-inflammatory lipid mediator leukotriene B4 (LTB4) . Hydroxylates at the omega-1 and omega-2 positions LTB4. This oxidation step leads to LTB4 inactivation, which is postulated to be a crucial part of the resolution of inflammation . Mechani... |
P51869 | MPQLDLSWLGLRLETSLPWLLLLLIGASWLLVRVLTQTYIFYRTYQHLCDFPQPPKWNWFLGHLGMITPTEQGLKQVTKLVATYPQGFMTWLGPILPIITLCHPDVIRSVLSASASVALKEVIFYSFLKPWLGDGLLLSDGDKWSCHRRMLTPAFHFNILKPYVKIFNDSTNIMHAKWQDLASGGSARLDMFKNISLMTLDSLQKCVFSFDSNCQEKPSEYISAILELSALVAKRYQQLLLHTDSLYQLTHNGRRFHKACKLVHNFTDAVIQGRRRALPSQHEDDILKAKARSKTLDFIDVLLLTKDEDGKELSDEDIRA... | Function: A cytochrome P450 monooxygenase involved in the metabolism of arachidonic acid and its oxygenated derivatives . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (... |
Q9CFB4 | MDKKKGILLVALGTPRSCEADDVRDYLKEFLGDPLVIQKPRWLWLPILNGIILKVRPQKSAEMYKKIWTDEGSPLMIYTVAQAKQLQDMREDFDVRFAMTYGEPRIDKVIAEMKESGVEEITVLPLYPQYSLTTVEPVIQQVKKIDDKIKVIRDFHKVESYSDLLAESIREKWQANDYDKLVLSYHGIPLSYVTKKKDAYEEQCKETTRLVVSKLGLREEEYEHTYQSKFGPEKWLEPATIDRVAELPKENAKKVLICSPAFVADCLETLFELEIENKEVFVENGGETFDFVHPFNDSLDFTRVLSEVVDQNRL | Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Sequence Mass (Da): 36436
Sequence Length: 314
Pathway: Porphyrin-containing... |
Q88XC3 | MHPGLLLVNLGSPASPRTKDVKAYLQEFLSDPSVIEMPAALWQPLLRGIILPTRSWRSATFYQDSWLPQGSPLIVYSQAICQQVQAALPDWNVRLAMTYGQPDIGATLKAMVADGCEKPIILPLFPQYTQSTHGGIHRQVEATGLPHTFIDSFYDQPTYIHLLATKVWQSYQAHHYDAVIFSYHSIPTAMVRHGDPYQRECEATTKAVLAERPELPADKVITAYQSKFGPMPWLKPYLKNELMQLVELGKRNVLVVTPSFVVDCLETLEEDYVQNYQTFRASGGDRFDLVPPMNKDTGFSQFLADLAIQKQEASNHAITS... | Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Sequence Mass (Da): 36370
Sequence Length: 324
Pathway: Porphyrin-containing... |
Q6AHF2 | MLGATPAAAGVAEHVTEPVAYDAILLAGFGGPEGQDDVIPFLRNVTRGRGILDERLEEVAQHYRHFGGVSPINDQNRALKAALEAELASRGIDLPVLWGNRNWDPYLADALTEADQRGFTKLIAVATSAYSSYSSCRQYREDFARALRETGLEGRIQIDKVRQFFDHPGFVEPFIEGVKNAVEELRERAPEIHPATGVRILFSTHSIPSTDAGKSGPSGRPDSGEPWGEGGAYAAQHLAVAEIVSHEATGGTIGWDLVYQSRSGPPSMPWLEPDINDRIAELPELGVKAIIIVPLGFVSDHMEVLWDLDTEAMESSEENG... | Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Sequence Mass (Da): 42217
Sequence Length: 389
Pathway: Porphyrin-containing... |
Q03Z41 | MNKKGLLLVNLGTPDSPHPDDVKAYLKEFLSDTNVIQMPRLLWQPILRGKILPKRSFKSAELYQKIWRKDGSPLMVYAKKQVEQVQQLQPNWIVRCAMTYRKPNIAETLKEMRLAGADDIVVLPLFPQYSVTSTQSVIDQVRKADKNINIVKSFYNDEAYLDLLARDIREAWAKNDYDRLIISYHGVPESYVRRGDPYVDHCTATTQGVLERVGPLTPDNTHQVFQSRFGPTEWVKPYLSDTLRSLPSQGIKRVLVATPAFVADCLETIEEIHVENHDIFKQAGGEVFDVVQPFNEHIDFSKYIASLANRHFAQN | Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Sequence Mass (Da): 36114
Sequence Length: 315
Pathway: Porphyrin-containing... |
P0A577 | MQFDAVLLLSFGGPEGPEQVRPFLENVTRGRGVPAERLDAVAEHYLHFGGVSPINGINRTLIAELEAQQELPVYFGNRNWEPYVEDAVTAMRDNGVRRAAVFATSAWSGYSSCTQYVEDIARARRAAGRDAPELVKLRPYFDHPLFVEMFADAITAAAATVRGDARLVFTAHSIPTAADRRCGPNLYSRQVAYATRLVAAAAGYCDFDLAWQSRSGPPQVPWLEPDVTDQLTGLAGAGINAVIVCPIGFVADHIEVVWDLDHELRLQAEAAGIAYARASTPNADPRFARLARGLIDELRYGRIPARVSGPDPVPGCLSSI... | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Sequence Mass (Da): 37144
Sequence Lengt... |
Q5APU2 | MTTPLSSYSTTVTNHHPTFSFESLNSISSNNSTRNNQSNSVNSLLYFNSSGSSMVSSSSDAAPTSISTTTTSTTSMTGASANADNQQVYTITEEDSINDINRKEQNSFSIQPNQTPTMLPTSSYTLQRPPGLHEYTSSISSISSTSSNSTSAPVSPALINYSPKHSRKPNSLNLNRNMKNLSLNLHDSTNGYTSPLPKSTNSNQPRSNFIMDSPSKKSTPVNRIGNNNGNDYINATLLQTPSITQTPTMPPPLSLAQGPPSSVGSESVYKFPPISNACLNYSAGDSDSEVESMSMKQAAKNTIIPPMAPPFALQSKSSPL... | Function: Protein tyrosine phosphatase that acts as a repressor of the yeast-hyphal switch. Plays an important role in virulence. Negatively regulates CST20-HST7-CEK1-CPH1 filamentous growth pathway. Represses hyphal genes such as SAP4, SA5, SAP6, and HYR1, by acting through a CEK1-independent mechanism.
Catalytic Acti... |
Q01958 | MFAFICLLAIASAIDFNTWASKNNKHFTAIEKLRRRAIFNMNAKFVDSFNKIGSFKLSVDGPFAAMTNEEYRTLLKSKRTTEENGQVKYLNIQAPESVDWRKEGKVTPIRDQAQCGSCYTFGSLAALEGRLLIEKGGDANTLDLSEEHMVQCTRDNGNNGCNGGLGSNVYDYIIEHGVAKESDYPYTGSDSTCKTNVKSFAKITGYTKVPRNNEAELKAALSQGLVDVSIDASSAKFQLYKSGAYTDTKCKNNYFALNHEVCAVGYGVVDGKECWIVRNSWGTGWGDKGYINMVIEGNTCGVATDPLYPTGVQYL | Function: Cysteine protease which degrades matrix proteins such as collagen, laminin and fibronectin and thus is involved in the destruction of human tissue . Can abolish adhesion . May play an important role in pathogenicity .
Catalytic Activity: Hydrolysis of proteins, including basement membrane collagen and azocase... |
P36184 | MFALILFVSLACANEVAFKQWAATHNKVFANRAEYLYRFAVFLDNKKFVEANANTELNVFADMTHEEFIQTHLGMTYEVPETTSNVKAAVKAAPESVDWRSIMNPAKDQGQCGSCWTFCTTAVLEGRVNKDLGKLYSFSEQQLVDCDASDNGCEGGHPSNSLKFIQENNGLGLESDYPYKAVAGTCKKVKNVATVTGSRRVTDGSETGLQTIIAENGPVAVGMDASRPSFQLYKKGTIYSDTKCRSRMMNHCVTAVGYGSNSNGKYWIIRNSWGTSWGDAGYFLLARDSNNMCGIGRDSNYPTGVKLI | Function: Cysteine protease which may be involved in pathogenicity.
Catalytic Activity: Hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-|-Xaa in small molecule substrates including Z-Arg-Arg-|-NHMec.
Sequence Mass (Da): 33851
Sequence Length: 308
Subcellular Lo... |
Q58DC0 | MSTAEAGGVFHRARGRTLDAFSSEKEREWKGPFYFIQGADPQFGLMKAWATGDCDNGGDEWEQEIRLAEQAVQAINKLNPKPKFFVLCGDLVHAMPGRPWRKEQTEDLQRVLRTVDSDIPLVLVSGNHDVGNVPTPETIAEFQRTWGDDYFSFWVGGVLFLVLNSQFLYDASRCPALKQEHDHWLDQQLRIAGQRACRHAVVFQHIPLFLQSIGEDDDYFNLTKSVRKEMADKFVEAGVKAVFSGHYHRNAGGTYRNLDMVVSSAIGCQLGTDTHGLRVVVVTAEKITHRYYSLDELSEKGIEDDLMDLLKEN | Cofactor: Binds 2 divalent metal cations.
Function: Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes (By similarity).
Catalytic Activity: H2O + O-phospho-L-sery... |
Q9BRF8 | MSAAEAGGVFHRARGRTLAAFPAEKESEWKGPFYFILGADPQFGLIKAWSTGDCDNGGDEWEQEIRLTEQAVQAINKLNPKPKFFVLCGDLIHAMPGKPWRTEQTEDLKRVLRAVDRAIPLVLVSGNHDIGNTPTAETVEEFCRTWGDDYFSFWVGGVLFLVLNSQFYENPSKCPSLKQAQDQWLDEQLSIARQRHCQHAIVFQHIPLFLESIDEDDDYYFNLSKSTRKKLADKFIHAGVKVVFSGHYHRNAGGTYQNLDMVVSSAIGCQLGRDPHGLRVVVVTAEKIVHRYYSLDELSEKGIEDDLMDLIKKK | Cofactor: Binds 2 divalent metal cations.
Function: Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-... |
Q8BFS6 | MSAMEAADVFHRARGRTLDAFSSEKEREWKGPFYFVQGADTQFGLMKAWSTGNCDAGGDEWGQEIRLTEQAVEAINKLNPKPKFFVLCGDLVHAMPGTPWRQEQTRDLQRVLKAVDQDIPLVMVSGNHDLGNAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFLYDASRCPALKQAQDHWLDQQLNIAEQKQCQHAIVFQHIPLFLQSIDEDDDYFNLTKTVRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQLGKDTHGLRVVAITAEKIVHRYYSLDELSQGGVEEDLKELLKE | Cofactor: Binds 2 divalent metal cations.
Function: Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes (By similarity).
Catalytic Activity: H2O + O-phospho-L-sery... |
O49290 | MSMLMAVKTTSLCCSSLNLTASPTFRRNPRAARLVNPTARIQTRFHRLIEEQGIVLMPGCYDALSAAIVQQTGFSAGFISGYALSASLLGKPDFGLLTPPEMAATARSVCASAPNIPIIADADTGGGNALNIQRTVKDLIAAGAAGCFLEDQAWPKKCGHMRGKQVIPAEEHAAKIASARDAIGDSDFFLVARTDVRATSAKSGLEDAIARVNLYMEAGADASFVEAPRDDDELKEIGKRTKGYRVCNMIEGGVTPLHTPDELKEMGFHLIVHPLTALYASTRALVDVLKTLKENGSTRDHLQKMATFEEFNSLVDLDSW... | Catalytic Activity: 1-carboxyvinyl carboxyphosphonate + H(+) = 3-(hydrohydroxyphosphoryl)pyruvate + CO2
Sequence Mass (Da): 36566
Sequence Length: 339
Subcellular Location: Plastid
EC: 2.7.8.23
|
P11435 | MAVTKARTFRELMNAPEILVVPSAYDALSAKVIQQAGFPAVHMTGSGTSASMLGLPDLGFTSVSEQAINLKNIVLTVDVPVIMDADAGYGNAMSVWRATREFERVGIVGYHLEDQVNPKRCGHLEGKRLISTEEMTGKIEAAVEAREDEDFTIIARTDARESFGLDEAIRRSREYVAAGADCIFLEAMLDVEEMKRVRDEIDAPLLANMVEGGKTPWLTTKELESIGYNLAIYPLSGWMAAASVLRKLFTELREAGTTQKFWDDMGLKMSFAELFEVFEYSKISELEARFVRDQD | Function: Catalyzes the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos (BA). Catalyzes the rearrangement of the carboxyphosphono group of CPEP to form the C-P bond of phosphinopyruvate.
Catalytic Activity: 1-carboxyvinyl carboxyphosphonate + H(+) = 3-(hydrohydroxyphosp... |
Q9SU30 | MATIPMDIVNDIFLRLPAKTLVRCRALSKPCYHLINDPDFIESHLHRVLQTGDHLMILLRGALRLYSVDLDSLDSVSDVEHPMKRGGPTEVFGSSNGLIGLSNSPTDLAVFNPSTRQIHRLPPSSIDLPDGSSTRGYVFYGLGYDSVSDDYKVVRMVQFKIDSEDELGCSFPYEVKVFSLKKNSWKRIESVASSIQLLFYFYYHLLYRRGYGVLAGNSLHWVLPRRPGLIAFNLIVRFDLALEEFEIVRFPEAVANGNVDIQMDIGVLDGCLCLMCNYDQSYVDVWMMKEYNVRDSWTKVFTVQKPKSVKSFSYMRPLVY... | Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Regulates negatively both salicylic acid (SA)-dependent and SA-independent defense signaling.
Sequence Mass (Da): 47259
Sequence Len... |
P32198 | MAEAHQAVAFQFTVTPDGIDLRLSHEALKQICLSGLHSWKKKFIRFKNGIITGVFPANPSSWLIVVVGVISSMHAKVDPSLGMIAKISRTLDTTGRMSSQTKNIVSGVLFGTGLWVAVIMTMRYSLKVLLSYHGWMFAEHGKMSRSTKIWMAMVKVLSGRKPMLYSFQTSLPRLPVPAVKDTVSRYLESVRPLMKEEDFQRMTALAQDFAVNLGPKLQWYLKLKSWWATNYVSDWWEEYIYLRGRGPLMVNSNYYAMEMLYITPTHIQAARAGNTIHAILLYRRTLDREELKPIRLLGSTIPLCSAQWERLFNTSRIPGE... | Function: Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion . Plays an important role in hepatic triglyceride metabolism .
Catalytic Activity: ... |
Q58DK1 | MAEAHQAVAFQFTVTPEGVDFQLSREVLKHIYLSVIRSWKKRLIRIKNGILRGVYPGSPTSWLVVVMATAGSSYYNVDISMGLVYYIQRWLPEGRPYRTPYTRTLFSMAIFSTGVWMMGIFFFRQTLKLLLSYHGWMFELHGQTSHLTRVWAVCVRLLSGRRPMLYSFQTSLPKLPVPSVPATVHRYLESVEHLLDDEQYYRMETLAKEFEEKTAPRLQKYLVLKSWWATNYVSDWWEEYVYLRGRNPIVVNSNYYVMDLVLVKNTDVQAARLGNAVHAMITYRRKLDREEIKPVMALGLVPMCSYQMERMFNTTRIPGK... | Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88512
Sequence Length: 771
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.1.21
|
Q92523 | MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPTSWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTGIFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPRVSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEEYIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALGIVPMCSYQMERMFNTTRIPG... | Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87801
Sequence Length: 772
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.1.21
|
Q63704 | MAEAHQAVAFQFTVTPDGVDFRLSREALRHIYLSGINSWKKRLIRIKNGILRGVYPGSPTSWLVVVMATVGSNYCKVDISMGLVHCIQRCLPTRYGSYGTPQTETLLSMVIFSTGVWATGIFLFRQTLKLLLSYHGWMFEMHSKTSHATKIWAICVRLLSSRRPMLYSFQTSLPKLPVPSVPATIHRYLDSVRPLLDDEAYFRMESLAKEFQDKIAPRLQKYLVLKSWWATNYVSDWWEEYVYLRGRSPIMVNSNYYAMDFVLIKNTSQQAARLGNTVHAMIMYRRKLDREEIKPVMALGMVPMCSYQMERMFNTTRIPG... | Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88217
Sequence Length: 772
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.1.21
|
Q8TCG5 | MAEAHQAVGFRPSLTSDGAEVELSAPVLQEIYLSGLRSWKRHLSRFWNDFLTGVFPASPLSWLFLFSAIQLAWFLQLDPSLGLMEKIKELLPDWGGQHHGLRGVLAAALFASCLWGALIFTLHVALRLLLSYHGWLLEPHGAMSSPTKTWLALVRIFSGRHPMLFSYQRSLPRQPVPSVQDTVRKYLESVRPILSDEDFDWTAVLAQEFLRLQASLLQWYLRLKSWWASNYVSDWWEEFVYLRSRNPLMVNSNYYMMDFLYVTPTPLQAARAGNAVHALLLYRHRLNRQEIPPTLLMGMRPLCSAQYEKIFNTTRIPGVQ... | Function: May play a role in lipid metabolic process.
Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90989
Sequence Length: 803
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitoch... |
C1K5M2 | MSSLVLQCWKLSSPSLILQQNTSISMGAFKGIHKLQIPNSPLTVSARGLNKISCSLNLQTEKLCYEDNDNDLDEELMPKHIALIMDGNRRWAKDKGLEVYEGHKHIIPKLKEICDISSKLGIQIITAFAFSTENWKRSKEEVDFLLQMFEEIYDEFSRSGVRVSIIGCKSDLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFDQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEEDLKEAIMNFQQRHRRFGGHTY | Function: Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 10 carbon product neryl diphosphate.
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate
Sequence Mass (Da): 34601
Sequence Length: 303
S... |
P23786 | MVPRLLLRAWPRGPAVGPGAPSRPLSAGSGPGQYLQRSIVPTMHYQDSLPRLPIPKLEDTIRRYLSAQKPLLNDGQFRKTEQFCKSFENGIGKELHEQLVALDKQNKHTSYISGPWFDMYLSARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNMTVSAIRFLKTLRAGLLEPEVFHLNPAKSDTITFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPKPSRDELFTDDKARHLLVLRKGNFYIFDVLDQDGNIVSPSEIQAHLKYILSDSSPAPEFPLAYLTSENRDIWAELRQKLMSSGNEESLRKVDS... | Function: Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites . Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxi... |
P18886 | MMPRLLFRAWPRCPSLVLGAPSRPLSAVSGPDDYLQHSIVPTMHYQDSLPRLPIPKLEDTMKRYLNAQKPLLDDSQFRRTEALCKNFETGVGKELHAHLLAQDKQNKHTSYISGPWFDMYLTARDSIVLNFNPFMAFNPDPKSEYNDQLTRATNLTVSAVRFLKTLQAGLLEPEVFHLNPSKSDTDAFKRLIRFVPPSLSWYGAYLVNAYPLDMSQYFRLFNSTRIPRPNRDELFTDTKARHLLVLRKGHFYVFDVLDQDGNIVNPLEIQAHLKYILSDSSPVPEFPVAYLTSENRDVWAELRQKLIFDGNEETLKKVDS... | Function: Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites. Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxid... |
K7WQ45 | MNSSIVSQHFFISLKSSLDLQCWKSSSPSSISMGEFKGIHDKLQILKLPLTMSDRGLSKISCSLSLQTEKLRYDNDDNDDLELHEELIPKHIALIMDGNRRWAKAKGLEVYEGHKLIIPKLKEICDISSKLGIQVITAFAFSTENWKRSKEEVDFLMQLFEEFFNEFLRFGVRVSVIGCKSNLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFEQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEKDLKKAILNFQQRHRRFGGHTY | Function: Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 20 carbon product nerylneryl diphosphate.
Catalytic Activity: dimethylallyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + nerylneryl diphosphate
Sequence Mass (Da): 36020
Sequence... |
P53674 | MSQAAKASASATVAVNPGPDTKGKGAPPAGTSPSPGTTLAPTTVPITSAKAAELPPGNYRLVVFELENFQGRRAEFSGECSNLADRGFDRVRSIIVSAGPWVAFEQSNFRGEMFILEKGEYPRWNTWSSSYRSDRLMSFRPIKMDAQEHKISLFEGANFKGNTIEIQGDDAPSLWVYGFSDRVGSVKVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQSLRRLRDKQWHLEGSFPVLATEPPK | Function: Crystallins are the dominant structural components of the vertebrate eye lens.
PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization.
Sequence Mass (Da): 28023
Sequence Length: 252
Domain: H... |
P02523 | MSQVAKAAATTAVNPGPDGKGKGTPSTGTAPAPGPTPVPASVPRPAAKVGELPPGSYRLVVFEQENFQGRRVEFSGECLNLGDRGFDRVRSLIVLSGPWVAFEQSAFRGEMFVLEKGEYPRWDTWTSSYRSDRLMSFRPIRMDSQEHKICLFEGANFKGNTMEIQEDDVPSLWVYGFCDRVGSITVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQAVRRLRDRQWHQEGCFPVLTAEPPK | Function: Crystallins are the dominant structural components of the vertebrate eye lens.
PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization. The protease responsible for this partial degradation co... |
Q91318 | MASDHQSPATKQQQPSSKIVLFEQENFQGRCHELSGPCTSLKEAGMEKIGSILVHSGPWVGYEQQNCKGEQFVFEKGEYPRWDSWTNSRKSESISSLRPIKVDSQEHKIVLYENPNFTGKKIEIIDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGYQYLFEKGDYKDSSDFGAQHPQIQSVRRIRDMQWHQRGTFHPTN | Function: Crystallins are the dominant structural components of the vertebrate eye lens.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 23649
Sequence Length: 205
Domain: Has a two-domain beta-structure, folded into four very similar Greek key motifs.
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A0A0K2JL91 | MTVPENAQHTAPDQTQHTAPDRTRQAQQAAPDTAGRRLIELMAGFWKTQAIYLAAESGLVDAIAAAGRAPAVELANRTGTDPDALGRLLLFLESLDVVSGEDPAGYALTPVGELLRTGTQDSMRDHVRIYGSHFYRAWGALDHSLRTGRSAFTEVYGSDLFRYLNQHPDLSLTYERAMVAGTPFFAQVPEVHDFSGARLIVDVAGGHGALLHEILKSCPEPRAVLFDAPHVIAETADRPIASEHGDRVTLVPGDFFEGVPQGGDVYLLSRILHCFDDEACLRILAHCRSAMAPGGRLVVVERLLTRGTGSSLAQGYNMHM... | Function: Part of a gene cluster involved in the biosynthesis of cremeomycin, a light-sensitive o-diazoquinone with antibacterial and antiproliferative effects . Catalyzes the methylation of the C4 hydroxyl group of 3-amino-2,4-dihydroxybenzoate (3,2,4-ADHBA) to form 3-amino-2-hydroxy-4-methoxybenzoate (3,2,4-AHMBA) . ... |
Q9VC61 | MTENQLYPMSSEFFDTGSNSSSNTLKYDLYSLGSTVVGAALPTLTINTGYGSSSSNNNNTNNNNNNSSSHSSSSNCSTSTTNTCNVMLSTTAITIPRSSNHNQIHHHPYQQSDLQTPRHHPSPLHTLPSMTHQQNQLQQQQQQQHHNQQQQLQQSHLALGELSDFGLDALDAASLSPTLLQDVSLSAVSPLSTTLYNGNTSGAGSSNGIGSGSGGYFTPDMSHSLSLNVVSEQVLLQEATTPNELLYEMTPNSNAMWSDISSAIIHTKHEPFSLDDDYIFPNDKAEIQAADLSDLNGGDFLDVIGNIEDFLPQTAVTQSV... | Function: Transcriptional regulator that acts in the TORC1 signaling pathway to regulate energy homeostasis and promote survival during nutrient deprivation. Interacts with REPTOR to form a transcriptional activator complex that functions downstream of TORC1 to up-regulate the expression of most target genes induced by... |
Q8IUR6 | MPQPSVSGMDPPFGDAFRSHTFSEQTLMSTDLLANSSDPDFMYELDREMNYQQNPRDNFLSLEDCKDIENLESFTDVLDNEGALTSNWEQWDTYCEDLTKYTKLTSCDIWGTKEVDYLGLDDFSSPYQDEEVISKTPTLAQLNSEDSQSVSDSLYYPDSLFSVKQNPLPSSFPGKKITSRAAAPVCSSKTLQAEVPLSDCVQKASKPTSSTQIMVKTNMYHNEKVNFHVECKDYVKKAKVKINPVQQSRPLLSQIHTDAAKENTCYCGAVAKRQEKKGMEPLQGHATPALPFKETQELLLSPLPQEGPGSLAAGESSSLS... | Function: Acts as a negative regulator of the endoplasmic reticulum stress response or unfolded protein response (UPR). Represses the transcriptional activity of CREB3 during the UPR. Recruits CREB3 into nuclear foci.
PTM: Probably degraded by the proteasome.
Sequence Mass (Da): 72149
Sequence Length: 639
Subcellular L... |
Q8CDG5 | MPQPSVSGMDPPFGDAFRSHTFSEQTLMSTDLLANSSDPDFMYELDREMNYQQNPRDNFLSLEDCKDIENLETFTDVLDNEDALTSNWEQWDTYCEDLTKYTKLTSCDIWGTKEVDYLGLDDFSSPYQDEEVISKTPTLAQLNSEDSQSVSDSLYYPDSLFSVKQNPLPPSSFPSKKITNRAAAPVCSSKTLQAEVPSSDCVQKASKPTSSTQIMVKTNMYHNEKVNFHVECKDYVKKAKVKINPVQQGRPLLSQVHIDAAKENTCYCGAVAKRQERRGVEPHQGRGTPALPFKETQELLLSPLTQDSPGLVATAESGSL... | Function: Acts as a negative regulator of the endoplasmic reticulum stress response or unfolded protein response (UPR). Represses the transcriptional activity of CREB3 during the UPR. Recruits CREB3 into nuclear foci (By similarity).
PTM: Probably degraded by the proteasome.
Sequence Mass (Da): 72598
Sequence Length: 6... |
O75177 | MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILEYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALTQSGSSQGLHSQGSLSDAISTGLPPSSLLQGQIGNGPSHVSMQQTAPNTLPTTSMSISGPGYSHAGPASQGVPMQGQGTIGNYVSRTNINMQSNPVSMMQQQAATSHYSSAQGGSQHYQGQSSIAMMGQGSQGSSMMGQRPMAPYRPSQQGSSQQYLGQEEYYGEQYSHSQGAAEPMGQQYYPDGHGDYAYQQSSYTEQSYDRSFEESTQHYYEGGNSQYSQQQAGYQQG... | Function: Transcriptional activator which is required for calcium-dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent re... |
Q8BW22 | MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILDYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALSQSGSSQGLHPQGSLSDTVSTGLPPASLMQGQIGNGPNHVSMQQTAQSTLPTTSMSLSGSGHGTGPGYSHSGPTSQSVPMQGQGAISNYVSRTNINMQSNPVSMMHQQAATSHYNSAQGGSQHYQGQAPIAMMGQGGQGGSMMGQRPMAPYRPSQQGSSQQYLGQEEYYSEQYSHSQGSAEPMSQQYYPDGHGDYAYQQSSYTEQSYDRSFEDPTQHYYEGGNSQYSQQQ... | Function: Transcriptional activator which is required for calcium-dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent re... |
Q8J0P4 | MYFKYTAAALAAVLPLCSAQTWSKCNPLEKTCPPNKGLAASTYTADFTSASALDQWEVTAGKVPVGPQGAEFTVAKQGDAPTIDTDFYFFFGKAEVVMKAAPGTGVVSSIVLESDDLDEVDWEVLGGDTTQVQTNYFGKGDTTTYDRGTYVPVATPQETFHTYTIDWTKDAVTWSIDGAVVRTLTYNDAKGGTRFPQTPMRLRLGSWAGGDPSNPKGTIEWAGGLTDYSAGPYTMYVKSVRIENANPAESYTYSDNSGSWQSIKFDGSVDISSSSSVTSSTTSTASSASSTSSKTPSTSTLATSTKATPTPSGTSSGSNS... | PTM: The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Location Topology: Lipid-anchor
Sequence Mass (Da): 40284
Sequence Length: 395
Subcellular Location: Cell membrane
EC: 3.2.-.-
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P0DQH7 | RIKKPIFAFPRF | Function: Conorfamide As1a: this amidated form is active on both ASIC channels and nicotinic acetylcholine receptors (nAChRs) . Shows a weak inhibition of peak current of rat ASIC1a and rat ASIC3 . Inhibits desensitization of ASIC1a and to a lesser degree ASIC3 currents, resulting in a sustained opening of channels in ... |
Q04930 | MLLSAPVNSTVRRKPHSPNKKKPKETGTAASFSSSSSTVVLSSNNDGSFDALWDPSISKASDFESSYISAKRLKPESSNRQKKKNSYKYSREENTNEVEEKTSLGSSSKTEADNIFNDQLTSAGNTTYVSNKRDVNFGANSAVVLLGLPTSKSESHRQYHSPSASTTNEDEEDIGVDILVDNHIDSCETVSINNNRGITHQYPETESDVDFDEAVILTPMDGTDKGVKNPRPLEKKYSSSCFEDRTPLNLDDGHFSECNHFSTLDVSSFFHLNEHVHKIDEVELDGPDRTFSLDNVAINTRKKDIDCLYNSSREDLSNLT... | Function: Transcription factor, corepressor with FHL1 of ribosomal protein genes. May be involved in the blocking of the spread of silencing.
PTM: Phosphorylated by CDC28 and YAK1.
Sequence Mass (Da): 51697
Sequence Length: 467
Subcellular Location: Cytoplasm
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Q4WI46 | MVRIGSSLLLATLAATTVSAASDPPKCSQDSHCPEEWPCCSLYGQCGTGAYCLGGCDPLMSFSLDSCTPEPICQGKTYKDWSNLDNLASNTKYLGDASKSDWVYSGYPKVEDGNLLLTMPKNSVGTLIANNHYIWYGKITAKIKSSRGAGVVTGFILLSDTKDEIDYEFVGADLTNVQTNYYFQGVLDYNHGGNASVSGGNTFGDWHEYTIDWKPDAITWSVDGEVKRTLKKESTYNETSKQYMYPQTPSRMQLSLWPAGQASNAPGTIAWAGGEIDWDSEDIKDPGYYYATFGEITVECYDPPSGADIKGTKAYIFKDK... | PTM: The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Location Topology: Lipid-anchor
Sequence Mass (Da): 46710
Sequence Length: 443
Subcellular Location: Cell membrane
EC: 3.2.-.-
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Q8GYA4 | MRRNTDQESPIMSYYSSFFFLFLFSFLTSFRVSAQDPTYVYHTCQNTANYTSNSTYNNNLKTLLASLSSRNASYSTGFQNATVGQAPDRVTGLFNCRGDVSTEVCRRCVSFAVNDTLTRCPNQKEATLYYDECVLRYSNQNILSTLITTGGVILVNTRNVTSNQLDLLSDLVLPTLNQAATVALNSSKKFGTRKNNFTALQSFYGLVQCTPDLTRQDCSRCLQLVINQIPTDRIGARIINPSCTSRYEIYAFYTESAVPPPPPPPSISTPPVSAPPRSGKDGNSKVLVIAIVVPIIVAVLLFIAGYCFLTRRARKSYYTP... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74283
Sequence Length: 669
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9ZP16 | MKQRSLFSVLCFFFISFGVASVSAQTCTTDKGTFRPNGTYDVNRRLILSSLPSNVTDQDGLYYNGSIGQQPNRVYAIGMCIPGSTSEDCSDCIKKESEFFLKNCPNQTEAYSWPGEPTLCYVRYSNTSFSGSADLNPRNWLTNTGDLDSNLTEFTKIWEGLMGRMISAASTAKSTPSSSDNHYSADSAVLTPLLNIYALMQCTPDLSSGDCENCLRQSAIDYQSCCSQKRGGVVMRPSCFLRWDLYTYSNAFDNLTVASPPPEPPVTVPQPAGDQDNPTNNDSKGISAGVVVAITVPTVIAILILLVLGFVLFRRRKSYQ... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74139
Sequence Length: 667
Subcellular Location: Membrane
EC: 2.7.11.-
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O65472 | MPLLFLWFFLTSTSLVSALQTLPCINTTYFIPNSTYDTNRRVILSLLPSNVTSHFGFFNGSIGQAPNRVYAVGMCLPGTEEESCIGCLLSASNTLLETCLTEENALIWIANRTICMIRYSDTSFVGSFELEPHREFLSIHGYKTNETEFNTVWSRLTQRMVQEASSSTDATWSGAKYYTADVAALPDSQTLYAMMQCTPDLSPAECNLCLTESVVNYQSCCLGRQGGSIVRLSCAFRAELYPFGGAFTVMTARPLSQPPPSLIKKDSGKFSTETIAAIVVPIIVVAIIFLVLLVLSRLFARRRKSYQEIDLDQSGITTLH... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73720
Sequence Length: 659
Subcellular Location: Membrane
EC: 2.7.11.-
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Q0PW40 | MKQRSLLSILCFILLASGVASVSAQTCIENRKYFTPNGTYDSNRRLILSSLPNNTASRDGFYYGSIGEEQDRVYALGMCIPKSTPSDCSNCIKGAAGWLIQDCVNQTDAYYWALDPTLCLVRYSNISFSGSAAFWEIEPQYLVLNTATIASNLTEFKTIWEDLTSRTITAASAARSTPSSSDNHYRVDFANLTKFQNIYALMQCTPDISSDECNNCLQRGVLEYQSCCGNNTGGYVMRPICFFRWQLFTFSKAFHNITLATTPPLSPPPLQRPVVASQPPSADNRDKKRDNSSGKISMKTILAIVVVGIVILIIISGILA... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75295
Sequence Length: 673
Subcellular Location: Membrane
EC: 2.7.11.-
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Q8W4G6 | MSSGASFIFLFFFLTSFTASVENVFYIKHICPNTTTYSRNSPYLTNLRTLLSSLSAPNASYSTGFQSARAGQAPDRVTGLFLCRGDVSPAVCRNCVAFSINDTLVQCPSERKSVFYYDECMLRYSDQNILSTLAYDGAWIRMNGNISIDQNQMNRFKDFVSSTMNQAAVKAASSPRKFYTVKATWTALQTLYGLVQCTPDLTRQDCFSCLESSIKLMPLYKTGGRTLYSSCNSRYELFAFYNETTVRTQQAPPPLPPSSTPLVTSPSLPGKSWNSNVLVVAIVLTILVAALLLIAGYCFAKRVKNSSDNAPAFDGDDITT... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 69705
Sequence Length: 627
Subcellular Location: Membrane
EC: 2.7.11.-
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Q8L710 | MAKTSCEIILCFFFFILSFRVISVSAQQTCDNTAGSFKPNSTYDNNRRLLLSTFASNVTAQNGYFNGSFGLGTDRVYAMGMCAPGAEPDVCSNCIKNTAEGLLQICLNQTDGFSWSGEETLCLVRYSNKSFSGLLGLEPSNDFFNVNEIRKEDQKEFDSVFDELMFRTIQGASSSVRNNSNSLSLSGKYYAKDVAPEPVYGNISVVMQCTPDVSSKDCNLCLERSLDFYKKWYNGKRGTIILRPSCFFRWELYTFFGAFDSINARHPPPPPRPLSPPPLKTPSVTNQTNITKKNDSRISGGTIAAIVVVVVVTIILIVVG... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 76354
Sequence Length: 686
Subcellular Location: Membrane
EC: 2.7.11.-
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Q8RX80 | MATKSCELVLCFFVFFVISFSAISVSAQTCDNTTGTFIPNSPYDKNRRLILSTLASNVTAQEGYFIGSIGIAPDQVFATGMCAPGSERDVCSLCIRSTSESLLQSCLDQADAFFWSGEETLCLVRYANRPFSGLLVMDPLGAIFNTGELNTNQTVFDIEWNNLTSSMIAGITSSSSGGNNSSKYYSDDIALVPDFKNISALMQCTPDVSSEDCNTCLRQNVVDYDNCCRGHQGGVMSRPNCFFRWEVYPFSGAIDQINLPKSPPPSVTSPSPIANITKNDSRISGGKIAAIVVVTVVTIILVVLGFVISNRRKQKQEMDL... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 72799
Sequence Length: 659
Subcellular Location: Membrane
EC: 2.7.11.-
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Q8GWJ7 | MSSLISFIFLFLFSSITASAQNTFYLYHNCSVTTTFSSNSTYSTNLKTLLSSLSSLNASSYSTGFQTATAGQAPDRVTGLFLCRVDVSSEVCRSCVTFAVNETLTRCPKDKEGVFYYEQCLLRYSNRNIVATLNTDGGMFMQSARNPLSVKQDQFRDLVLTPMNLAAVEAARSFKKWAVRKIDLNASQSLYGMVRCTPDLREQDCLDCLKIGINQVTYDKIGGRILLPSCASRYDNYAFYNESNVGTPQDSSPRPGKGGNSSVIIIAVVVPITVLFLLLVAVFSVRAKNKRTLNEKEPVAEDGNDITTAGSLQFDFKAIE... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 71620
Sequence Length: 645
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9LMB9 | MQICASIAQFLAWVSFLVLLATVGSSSSSESLLNCQPLDHHLVNPSRLLGFLRAMSSVNDFITNDKLWVVSSITDVSPPIYVFLQCREDLSVSDCRHCFNESRLELERKCSGSGGRIHSDRCFLRFDDRDFSEEFVDPTFDKANCEETGTGFGEFWRFLDEALVNVTLKAVKNGGFGAASVIKTEAVYALAQCWQTLDENTCRECLVNARSSLRACDGHEARAFFTGCYLKYSTHKFFDDAAEHKPDADQRNFIRSSFFPHLSDRDVTRLAIAAISLSILTSLGAFISYRRVSRKRKAQVPSCVNFKYEMLEKATESFHD... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 69176
Sequence Length: 615
Subcellular Location: Membrane
EC: 2.7.11.1
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Q12126 | MDIEKSDKWTYVKERKVGEGTYAVVFLGRQKETNRRVAIKKIKVGQFKDGIDISALREIKFLRESRHDNVIELVDVFSTKSNLNIILEFLDSDLEMLIKDKFIVFQPAHIKSWMVMLLRGLHHIHSRFILHRDLKPNNLLISSDGVLKLADFGLSRDFGTPSHMSHQVITRWYRPPELFMGCRSYGTGVDMWSVGCIFAELMLRTPYLPGESDLDQLNVIFRALGTPEPEVIKSMQQLPNYVEMKHIPPPNGGMEALFSAAGHEEIDLLKMMLDYNPYRRPTAQQALEHHYFSALPKPTHPSLLPRKGGEEGIKHVSSDL... | Function: Protein kinase essential for cell proliferation, where it is required for completion of cytokinesis. Phosphorylates the C-terminal repeat domain (CTD) of RNA polymerase II.
Catalytic Activity: [DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]
Sequence Mass (Da): 38538
Se... |
Q3E9X6 | MQKNKMVDLRAIFWFVVISSCAVAAPTCIQRSDFFKANGPYDINLRAMLSSLPSRVKDNEGFYKTPFKPGPNIAHGLGMCSRGTTTQDCSDCITSVSHTLLHTCPNQAEAIDWSSGDSLCLVRYSNHLINGSLDEDIIWAEYIEYKYNTSFGQTNLTEFKSTWQALMDRVINKVDGSLYANSIQELGSFPFRSIYAIAQCNKDLTKLNCEKCLQHLRIDNRSCCRGIQVGYIARTSCFMRWDLQPFLGLFINGMLPTPPSELDNGHSNTTKKDGKNISTGSIVAIAVVSVVVSTVLLALGYAVSRRRKAYQSFASENGYF... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 76859
Sequence Length: 690
Subcellular Location: Membrane
EC: 2.7.11.-
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O65482 | MSSWASFIFLFIFSFLTSFRVFAQDPTYRYHSCPNTTIFSRDSAYFSNLQTLLSFLSSPDASSSYSSGFRNDAVGTFPDRVTGLFDCRGDLPPEVCHNCVAFAVKDTLIRCPNERDVTLFYDECTLRYSNLVVTSALDPTYVYHVCPSWATFPRSSTYMTNLITLLSTLSSPSASYSTGFQNATAGKHPDRVTGLFNCRGDVSPEVCRRCVSFAVNETSTRCPIEKEVTLYYDQCTLRYSNRNILSTSNTNGGIILANSQNMTSNEQARFKDLVLTTMNQATIAAANSSKRFDARSANFTTLHSLYTLVQCTHDLTRQDC... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 92316
Sequence Length: 830
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9N623 | MKFASKKNNQKNSSKNDERYRELDNLVQEGNGSRLGGGSCLGKCAHVFKLIFKEIKDNIFIYILSIIYLSVCVMNKIFAKRTLNKIGNYSFVTSETHNFICMIMFFIVYSLFGNKKGNSKERHRSFNLQFFAISMLDACSVILAFIGLTRTTGNIQSFVLQLSIPINMFFCFLILRYRYHLYNYLGAVIIVVTIALVEMKLSFETQEENSIIFNLVLISALIPVCFSNMTREIVFKKYKIDILRLNAMVSFFQLFTSCLILPVYTLPFLKQLHLPYNEIWTNIKNGFACLFLGRNTVVENCGLGMAKLCDDCDGAWKTFA... | Function: May regulate endogenous transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48675
Sequence Length: 424
Subcellular Location: Vacuole membrane
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Q4UDS9 | MLKEGSSLDLSASSSSGTLRSDNSFGNSPLDRITSLLILIYKSIRACFKWIYSKSFGIICILFVILDVLTTVFFKRFIDHTKNYVMFTIQVIIFTFWIIVCCIAILCFLFNREYMKRHFNVRPLVFLGFLDMLSTGLSANGSAHTSGLMLVLLGQISVPLTMVSCKLILSKKYHHYQYISSAIILTFAVLKPILNRTDTTDNRFYNNMLYLLASVPDSIASALREKQYTSKFFHVVKYQFFGFLFHFFYNILYTLLFTLPFNSVKGYFDSLYKLCVNGYKCIFFGVNTITENCGPTLIPTCDNCLEAFKIYCLYILFSSA... | Function: May regulate endogenous transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48721
Sequence Length: 430
Subcellular Location: Vacuole membrane
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P15455 | MARVSSLLSFCLTLLILFHGYAAQQGQQGQQFPNECQLDQLNALEPSHVLKSEAGRIEVWDHHAPQLRCSGVSFARYIIESKGLYLPSFFNTAKLSFVAKGRGLMGKVIPGCAETFQDSSEFQPRFEGQGQSQRFRDMHQKVEHIRSGDTIATTPGVAQWFYNDGQEPLVIVSVFDLASHQNQLDRNPRPFYLAGNNPQGQVWLQGREQQPQKNIFNGFGPEVIAQALKIDLQTAQQLQNQDDNRGNIVRVQGPFGVIRPPLRGQRPQEEEEEEGRHGRHGNGLEETICSARCTDNLDDPSRADVYKPQLGYISTLNSYD... | Function: Seed storage protein.
PTM: Phosphorylated in seeds on some Tyr residues in response to abscisic acid (ABA).
Sequence Mass (Da): 52595
Sequence Length: 472
Subcellular Location: Protein storage vacuole
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Q96318 | MVKLSNLLVATFGVLLVLNGCLARQSLGVPPQLQNECNLDNLDVLQATETIKSEAGQIEYWDHNHPQLRCVGVSVARYVIEQGGLYLPTFFTSPKISYVVQGTGISGRVVPGCAETFMDSQPMQGQQQGQPWQGRQGQQGQPWEGQGQQGQQGRQGQPWEGQGQQGQQGRQGQQGQPWEGQGQQGQQGFRDMHQKVEHVRRGDVFANTPGSAHWIYNSGEQPLVIIALLDIANYQNQLDRNPRVFHLAGNNQQGGFGGSQQQQEQKNLWSGFDAQVIAQALKIDVQLAQQLQNQQDSRGNIVRVKGPFQVVRPPLRQPYE... | Function: Seed storage protein.
PTM: Proteolytically processed during seed maturation at a conserved Asn-Gly peptide bond by an asparaginyl endopeptidase to produce two mature polypeptides referred to as alpha and beta subunits that are joined together by a disulfide bond.
Sequence Mass (Da): 58235
Sequence Length: 524... |
Q9ZWA9 | MHKLLFSLLSVVSLSFLLFFHGAEARQREAPFPNACHFSQINSLAPAQATKFEAGQMEVWDHMSPELRCAGVTVARITLQPNSIFLPAFFSPPALAYVVQGEGVMGTIASGCPETFAEVEGSSGRGGGGDPGRRFEDMHQKLENFRRGDVFASLAGVSQWWYNRGDSDAVIVIVLDVTNRENQLDQVPRMFQLAGSRTQEEEQPLTWPSGNNAFSGFDPNIIAEAFKINIETAKQLQNQKDNRGNIIRANGPLHFVIPPPREWQQDGIANGIEETYCTAKIHENIDDPERSDHFSTRAGRISTLNSLNLPVLRLVRLNAL... | Function: Seed storage protein.
PTM: Ubiquitinated.
Sequence Mass (Da): 49675
Sequence Length: 451
Subcellular Location: Protein storage vacuole
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A0A0A1GNF2 | MGSGKDRTLAGWTLPETKTDATAQFDRFVTENRFTIAVVFPLVGAVTLLASAEGLLPDPLAFNPYFVLFGTFVMRLPLVAGIFPLVDRRAGLALVALTLYSYGIELVGVRTGWPYGEFTYGVDLGPMLLGDVPFGLPVFFFPLVLNAYLLVLLLLGNRAASTTVRLLSTLATVMLVDLVLDPGAVAIGFWIYEMPQFYGVPWQNYAGWLLSGSVAVLLFDFGFDRAGLRRRLRDCPFMLDDLVSFVLLWGGINLFYTNWVPFGLAALLGAGLLWTDRFDFDLSETRLGRAVWR | Function: Involved in the biosynthesis of the acyclic C50 carotenoid bacterioruberin (BR). Catalyzes the reaction that introduces hydroxyl groups to C3'' and C3''' of bisanhydrobacterioruberin (BABR) to generate BR.
Catalytic Activity: bacterioruberin = bisanhydrobacterioruberin + 2 H2O
Location Topology: Multi-pass me... |
Q5XEZ5 | MATLQDIGVSAGINILSAFVFFIIFAVLRLQPFNDRVYFSKWYLKGLRSSPARGGAFAQRFVNLDFRSYMKFLNWMPEALKMPEPELIDHAGLDSVVYLRIYWLGLKIFTPIAVLAWAVLVPVNWTNNTLEMAKQLRNVTSSDIDKLSVSNIPEYSMRFWTHIVMAYAFTIWTCYVLMKEYETIANMRLQFVASEARRPDQFTVLVRNVPPDADESVSELVEHFFLVNHPDHYLTHQVVCNANKLADLVKKKKKLQNWLDYYQLKYARNNSQRIMVKLGFLGLWGQKVDAIEHYIAEIDKISKEISKEREEVVNDPKAIM... | Function: Acts as an osmosensitive calcium-permeable cation channel . Specifically conducts cations including Ca(2+), K(+) and Na(+) in vitro. Inactivation or closure of the channel is calcium-dependent . Mechanosensitive ion channel that converts mechanical stimuli into a flow of ions .
Location Topology: Multi-pass m... |
X1WEM4 | MAFESWPAGGVRPVEELDVRSFLMEENSTAERCYRSHSRSSVLQGLPFGGVPTVLAINVVLWLILLLIFSCLRKAAWDYGRLALLMKNDSLTSLFYGEQSEKEKTPSDSSPSDSETKDMGFCSWLTSLYHMKDEEIRSKCGIDAVTYLSFQRHIILLMMVVCLLSLTIILPVNLSGNLLGDNPENFGRTTVVNVPAQNIFLWLHSIFALLYFVITVLCMAHHSSRLEYREDEKVARTLMITSIPREISDPGLITKHLHEAYPSCTVTDIHFCFNVQKLMKLDSERRKAMKGRLYFTTKAQKNGRIMIKTHPCAQIFCCDI... | Function: Acts as an osmosensitive calcium-permeable cation channel (By similarity). Required for the functional integrity of the kidney glomerular filtration barrier .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 94430
Sequence Length: 825
Subcellular Location: Cell membrane
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Q9P1W3 | MSASPDDLSTGGRLQNMTVDECFQSRNTVLQGQPFGGVPTVLCLNIALWVLVLVVYSFLRKAAWDYGRLALLIHNDSLTSLIYGEQSEKTSPSETSLEMERRDKGFCSWFFNSITMKDEDLINKCGDDARIYIVFQYHLIIFVLIICIPSLGIILPINYTGSVLDWSSHFARTTIVNVSTESKLLWLHSLLSFFYFITNFMFMAHHCLGFAPRNSQKVTRTLMITYVPKDIEDPELIIKHFHEAYPGSVVTRVHFCYDVRNLIDLDDQRRHAMRGRLFYTAKAKKTGKVMIRIHPCARLCFCKCWTCFKEVDAEQYYSEL... | Function: Acts as an osmosensitive calcium-permeable cation channel . Required for the functional integrity of the kidney glomerular filtration barrier (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93317
Sequence Length: 806
Subcellular Location: Cell membrane
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Q09809 | MAFNGYGIFDSDPRKNPSSDLRTQFWLAFLLGASACVFFCFFRKRWKVLYAPRTTIEGLNLPTLSSSYYKWLMDLVNIPDDVVQNCAGLDGYVFLLFFKMGIKFLSFASLLGVLIIMPVNKHFRGDAFGNITLSMPAKSEYFFSSPLVKKSIVQSPIIANGSELNVGVLGPSLFNPIGNLSDIPGLPQPGDGFLYLYVLFTYFISIFLLYVLFSSTKSIADIRQSYLARQNRLTDRTVFISGLPNELCSTENLKAYFDKLDVGSIDSLSICRNYSYMDILLSKKSKYVKKLEKYWSIYLSNCKKLGISTLPPSNYLSPNR... | Function: Acts as an osmosensitive calcium-permeable cation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90573
Sequence Length: 793
Subcellular Location: Vacuole membrane
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Q06538 | MTSYIERLKSAASYLDTVPDEHHDFRKPTAKVVTTQLTIATSLGIFALLSFSILLKKWPRLYASRRYKDDGNLRLPSWNQSSLFGWLTVLYKIRDEQILEYAGLDAYVFLSFFKMCIKLLSIFCFFSVCVISPVRYHFTGKIDDGNDDDDSESSLIHLVKRIVEGSGDGDNHSAPERTNVYLWMYVLFTYFFTFIAIKMAVAETKHVVSTRQAYLGKQNTITDRTIRLSGIPIELRDSEALKTRIEQLKIGTVSSITICREWGPLNKLFHCRKKILKNLELKYSECPRELRTRQPYSENYHLLGNEQSGAVTHGENVPSS... | Function: Acts as an osmosensitive calcium-permeable cation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89344
Sequence Length: 782
Subcellular Location: Membrane
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Q49Z29 | MQNFKELGISDKMAETLQSMGFNEATPIQKESIPLALEGKDVLGQAQTGTGKTGAFGIPLIEKVADQEGVQSLILAPTRELAMQVAESLKAFAKGQNIQVVTVFGGMPIDRQIKALKKGPQIVVGTPGRVIDHLNRRTLKTNDIHTLILDEADEMMNMGFIDDMKFIMDKIPAEQRQTMLFSATMPKAIQTLVQQFMKSPVIVKTMNNEMSDPQIEEYYTIVKELEKFDTFTSFLDVHQPELAIVFGRTKRRVDELTSALISKGYKAEGLHGDITQAKRLEVLKKFKNDQLDILVATDVAARGLDISGVSHVYNFDIPQD... | Function: DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 56734
Sequence Length: 506
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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P54475 | MKETKFELYELKPFIIDAVHRLGFYEPTDIQKRLIPAVLKKESVIGQSQTGTGKTHAYLLPLLNKIDPAKDVVQVVITAPTRELANQIYQEALKITQGEEGSQIRSKCFIGGTDKQKSIDKLKIQPHLVVGTPGRIADLIKEQALSVHKAESLVIDEADLMLDMGFLADVDYIGSRMPEDLQMLVFSATIPEKLKPFLKKYMENPKYAHVEPKQVTAAKIEHILIPSKHRDKDKLLFDIMSHLNPYLGIVFANTKNTADHIAQYLTGKGMKIGLLHGGLTPRERKKVMKQINDLEFTYIIATDLAARGIDIKGVSHVINY... | Function: DEAD-box RNA helicase that plays a role in 70S ribosome assembly. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 50027
Sequence Length: 438
Subcellular... |
Q8Y755 | MTKKSRFDQFGFQPFIGLAIDKLGFYEPTEVQQKLIPGILKGESIIGQSQTGTGKTHTFILPIINNVNPEKDAVQAVITAPSRELATQIYNEIRKVTKYSEKEIAVQLVIGGTDKQRAIDKLKKQPQIIVGTPGRINDLIREQALFVHTAKTLVIDEADMTLDMGFLNDVDHIAGKMPANLQMLVFSATIPQKLKPFLSKYMENPRYEHIQPKVAASKTVEHRIMATRSRNKLDLLKNVLVGSQPYLAIVFTNTKTTADEVANGLIERGLKVAKIHGDVNPRERKRTMKQIENLDYQYVVATDLAARGIDIQGISHVVNY... | Function: DEAD-box RNA helicase involved in cold tolerance, motility, and tolerance to heat, alkali and oxidative stress.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 49651
Sequence Length: 435
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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Q2FY15 | MAKHPFEQFNLESSLIDAVKDLNFEKPTEIQNRIIPRILKRTNLIGQSQTGTGKSHAFLLPLMQLIDSEIKEPQAIVVAPTRELAQQLYDAANHLSQFKAGVSVKVFIGGTDIEKDRQRCNAQPQLIIGTPTRINDLAKTGHLHVHLASYLVIDEADLMIDLGLIEDVDYIAARLEDNANIAVFSATIPQQLQPFLNKYLSHPEYVAVDSKKQNKKNIEFYLIPTKGAAKVEKTLNLIDILNPYLCIIFCNSRDNANDLARSLNEAGIKVGMIHGGLTPRERKQQMKRIRNLEFQYVIASDLASRGIDIEGVSHVINFDV... | Function: Probable DEAD-box RNA helicase. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 51081
Sequence Length: 448
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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Q81E85 | MIKDMQPFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLVRVTRAESKSLVEHTYIICERREKNDYVRRIMHMGDVKAVAFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIH... | Function: DEAD-box RNA helicase. Probably has an RNA-dependent ATPase activity and a 3' to 5' RNA helicase activity that uses the energy of ATP hydrolysis to destabilize and unwind short RNA duplexes.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 44067
Sequence Length: 389
EC: 3.6.4.13
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Q7XHV0 | MALSPAAAGRTGRNNNNDAGLADPLLPAGGGGGGGKDKYWVPADEEEEICRGEDGGRPPAPPLLYRTFKVSGVLLHPYRLLTLVRLIAVVLFLAWRLKHRDSDAMWLWWISIAGDFWFGVTWLLNQASKLNPVKRVPDLSLLRRRFDDGGLPGIDVFINTVDPVDEPMLYTMNSILSILATDYPADRHAAYLSDDGASLAHYEGLIETARFAALWVPFCRKHRVEPRAPESYFAAKAAPYAGPALPEEFFGDRRLVRREYEEFKARLDALFTDIPQRSEASVGNANTKGAKATLMADGTPWPGTWTEPAENHKKGQHAGI... | Function: May catalyze both beta-1,3 and beta-1,4 glycosidic linkage on beta-D-glucan. Essential for (1,3;1,4)-beta-D-glucans synthesis in grasses and cereals (Poaceae). The mixed-linked glucans (which are not present in walls of dicotyledons or most other monocotyledonous plants) are particularly important constituent... |
Q8VYR4 | MEPQRKHSTALHTCHPCRRTIPYRIYAVFHTCGIIALMYHHVHSIVNANNTLITCLLLLSDIVLAFMWATTTSLRLNPIHRTEYPEKYAAKPEDFPKLDVFICTADPYKEPPMMVVNTALSVMAYEYPSHKISVYVSDDGGSSLTLFALMEAAKFSKHWLPFCKNNNVQDRSPEVYFSSKSHSSSDEAENLKMMYEDMKSRVEHVVESGKVETAFIACDQFSCVFDLWTDKFTRHDHPTIIMVLQHNETEMMPNLIYVSREKSKVSPHHFKAGALNTLLRVSAVMTNSPIILTLDCDMYSNNPTTPLHALCYLSDPKINF... | Function: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82120
Sequence Length: 722
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q339N5 | MEAAARGNKKLQERVPIRRTAWRLADLAILFLLLALLLHRVLHDSGAPWRRAALACEAWFTFMWLLNVNAKWSPVRFDTFPENLAERIDELPAVDMFVTTADPVLEPPLVTVNTVLSLLALDYPAAGEKLACYVSDDGCSPLTCYALREAARFARTWVPFCRRHGVAVRAPFRYFSSTPEFGPADGKFLEDWTFMKSEYEKLVHRIEDADEPSLLRHGGGEFAEFLDVERGNHPTIIKVLWDNNRSRTGDGFPRLIYVSREKSPNLHHHYKAGAMNALTRVSALMTNAPFMLNLDCDMFVNNPRVVLHAMCLLLGFDDEI... | Function: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83833
Sequence Length: 750
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q9UBW8 | MSAEVKVTGQNQEQFLLLAKSAKGAALATLIHQVLEAPGVYVFGELLDMPNVRELAESDFASTFRLLTVFAYGTYADYLAEARNLPPLTEAQKNKLRHLSVVTLAAKVKCIPYAVLLEALALRNVRQLEDLVIEAVYADVLRGSLDQRNQRLEVDYSIGRDIQRQDLSAIARTLQEWCVGCEVVLSGIEEQVSRANQHKEQQLGLKQQIESEVANLKKTIKVTTAAAAAATSQDPEQHLTELREPAPGTNQRQPSKKASKGKGLRGSAKIWSKSN | Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease t... |
Q9CZ04 | MSAEVKVTGQNQEQFLLLAKSAKGAALATLIHQVLEAPGVYVFGELLDMPNVRELAESDFASTFRLLTVFAYGTYADYLAEARNLPPLTDAQKNKLRHLSVVTLAAKVKCIPYAVLLEALALRNVRQLEDLVIEAVYADVLRGSLDQRNQRLEVDYSIGRDIQRQDLSAIAQTLQEWCVGCEVVLSGIEEQVSRANQHKEQQLGLKQQIESEVANLKKTIKVTTAAAAAATSQDPEQHLTELREPASGTNQRQPSKKASKGKGLRGSAKIWSKSN | Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease t... |
Q94JU3 | MDIEQKQAEIIDQLVKRASTCKSEALGPLIIEATSHPSLFAFSEILALPNVAQLEGTTDSVYLDLLRLFAHGTWGDYKCNATRLPHLSPDQILKLKQLTVLTLAESNKVLPYDTLMVELDVSNVRELEDFLINECMYAGIVRGKLDQLKRCFEVPFAAGRDLRPGQLGNMLHTLSNWLNTSENLLISIQDKIKWADNMSEMDKKHRKEAEEGVEEVKKSLSMKGDVDIRGNKEMFGEPSGVMDYEEDGIRPKRRRHPVTR | Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin su... |
Q9C5H6 | MKNGIAECPACHSKLVSPGSKTISRAYDDHKIRVSSKQRVLNVLLVVGDCMLVGLQPVLVYMSKVDGKFNFSPISVNFLTEIAKVIFAIVMLLIQARHQKVGEKPLLSVSTFVQAARNNVLLAVPALLYAINNYLKFTMQLYFNPATVKMLSNLKVLVIAVLLKMVMKRRFSIIQWEALALLLIGISVNQLRSLPEGATAIGIPLATGAYVCTVIFVTVPSMASVFNEYALKSQYDTSIYLQNLFLYGYGAIFNFLGILGTVIYKGPGSFDILQGHSRATMFLILNNAAQGILSSFFFKYADTILKKYSSTVATIFTGIA... | Function: Sugar transporter involved in the transport of CMP-sialic acid from the cytoplasm into the Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44541
Sequence Length: 405
Subcellular Location: Golgi apparatus membrane
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F4JN00 | MEYRKIKDEDDHDVASDIESVKGKSHTVASSNIAMATLGVGSSERINWKRKGVVTCALTILTSSQAILIVWSKRAGKYEYSVTTANFLVGTLKCALSLLALTRIWKNEGVTDDNRLSTTFDEVKVFPIPAALYLFKNLLQYYIFAYVDAPGYQILKNLNIISTGVLYRIILKRKLSEIQWAGFILLCCGCTTAQLNSNSDRVLQTSLPGWTMAIVMALLSGFAGVYTEAIIKKRPSRNINVQNFWLYVFGMAFNAVAIVIQDFDAVANKGFFHGYSFITLLMILNHALSGIAVSMVMKYADNIVKVYSTSVAMLLTAVVS... | Function: Sugar transporter involved in the transport of CMP-sialic acid from the cytoplasm into the Golgi (By similarity). Essential protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38979
Sequence Length: 352
Subcellular Location: Golgi apparatus membrane
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Q6K8S7 | MQRNGVVECSVCRSRLVVPSPRSVSRAYDKHRSKISSKFRALNVLLVVGDCILVGLQPILVFMSKVDGKFQFSPISVNFLTEVTKVVFAIVMLIIQSRKQKVGEKPLLARSTFIQAARNNALLAVPALLYAINNYLKFIMQLYFNPSTVKMLSNLKVLVIAVLLKFIMKRRFSVIQWEALALLLIGISINQLRTVPAGNTAFGLPVTAIAYIYTLIFVTVPSLASVYNEYALKSQYDTSIYLQNLFLYGYGAIFNFLGILGTALFQGPESFNILRGHSRATMFLICNNAAQGILSSFFFKYADTILKKYSSTVATIFTGL... | Function: Sugar transporter involved in the transport of CMP-sialic acid from the cytoplasm into the Golgi. May transport important nucleotide sugars such as CMP-Kdo (2-keto-3-deoxy-D-manno-octulosonic acid) in physiological conditions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44888
Sequence L... |
P27450 | MGACISFFSSSSPSKTGLHSHATTNNHSNGTEFSSTTGATTNSSVGQQSQFSDISTGIISDSGKLLESPNLKVYNFLDLKTATKNFKPDSMLGQGGFGKVYRGWVDATTLAPSRVGSGMIVAIKRLNSESVQGFAEWRSEVNFLGMLSHRNLVKLLGYCREDKELLLVYEFMPKGSLESHLFRRNDPFPWDLRIKIVIGAARGLAFLHSLQREVIYRDFKASNILLDSNYDAKLSDFGLAKLGPADEKSHVTTRIMGTYGYAAPEYMATGHLYVKSDVFAFGVVLLEIMTGLTAHNTKRPRGQESLVDWLRPELSNKHRV... | Function: Acts as a spatial inhibitor of signaling that modulates abscission zone cell adhesion and expansion. Acts both directly and indirectly by physically interacting with RLK5/HAE and SOBIR1/EVR at the cell surface.
PTM: Autophosphorylated on serine, threonine and tyrosine residues.
Location Topology: Lipid-anchor... |
Q9SY88 | MPQRHSKNNNDLAYFTYDEKKKLGYGTQRERLGRDSIKPFDACSLCLKPFIDPMCCHKGHVFCRECILECFLAQKKDIQRRLAAHSSQKKQDKDEEEERLMLQKARELDEFDQQNHSAMPRNSDKNHNEDKNGFHGANSVKTTSFEEEALRTMKAFWLPSATPAASVRVDAPETHTVCPEGKEKLKLKNLFAIRFTEDNSEEEETKTKSASSSSYDKSYICPSCKVTLTNTMSLVALSSCGHVFCKKCAEKFMPVDKVCLVCDKPCKDRNLVGLKKGGTGFAEHDDHLEAKEYKHLGSGSGLGLVRPVKT | Function: RING-finger E3 ubiquitin-protein ligase that plays an major role in maintaining COP1 homeostasis in darkness. Negatively regulates COP1 protein accumulation by targeting COP1 for ubiquitination and subsequent proteasomal degradation in dark-grown seedlings. Negatively regulates the accumulation of SPA1 protei... |
Q9V3A4 | MAKQVADYQCSKLQLYQKLALVVILGAVLFSLPALCAGQGNPSFKYSREANENFDPQKAPRAEHHHHHDHDHDHGHHHHGHDHDHDHDHGHDHGHHHHGHDHDHDHDHGHHHHGHDERHTKAKPDLDMSTIWLHSIGSTLLISAAPFVLLYIIPLDNSEAMKPRLKVLLAFASGGLLGDAFLHLIPHATHPHSHGEHGHDHGHDHHHHHDGEEHEHGHSHDMSIGLWVLGGIIAFLSVEKLVRILKGGHGGHGHSHGAPKPKPVPAKKKSSDKEDSGDGDKPAKPAKIKSKKPEAEPEGEVEISGYLNLAADFAHNFTDG... | Function: Negatively regulates tyrosine hydroxylase activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48658
Sequence Length: 449
Subcellular Location: Membrane
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P29349 | MSSRRWFHPTISGIEAEKLLQEQGFDGSFLARLSSSNPGAFTLSVRRGNEVTHIKIQNNGDFFDLYGGEKFATLPELVQYYMENGELKEKNGQAIELKQPLICAEPTTERWFHGNLSGKEAEKLILERGKNGSFLVRESQSKPGDFVLSVRTDDKVTHVMIRWQDKKYDVGGGESFGTLSELIDHYKRNPMVETCGTVVHLRQPFNATRITAAGINARVEQLVKGGFWEEFESLQQDSRDTFSRNEGYKQENRLKNRYRNILPYDHTRVKLLDVEHSVAGAEYINANYIRLPTDGDLYNMSSSSESLNSSVPSCPACTAA... | Function: Required in all receptor tyrosine kinase signaling pathways. Functions downstream of the receptor tyrosine kinase torso, acting in concert with D-Raf via tailless. Also functions downstream of Egfr (epidermal growth factor receptor) and btl (fibroblast growth factor receptor). The SH2 domain suggests that csw... |
Q24708 | WFHGNLSGKEAEKLILERGKNGSFLVRESQSKPGDFVLSVRTDDKVTHVMIRWQDKKYDVGGGESFATLSELIEHYKRHPMVETCGTVVHLRQPFNATRITAAGINARVEQLVKGGFWEEFESLQQDSRDTFSRHEGYKDENRLKNRYHDHTRVKLQDVERSAPGAEYINANYIRLPTDGDLYNMSSSSESLNSTVAACPACTAAQTQRNCPNCHLLNKTCVKCAVKSATLPTNCATCNRKSDSLSKHKRSESMSASANASAAGTGPGTPTAAGNTSAAAALNGCLAVLLKKHCGDASPPPSTTSSCSGPLTGSLLNGEG... | Function: Required in all receptor tyrosine kinase signaling pathways. Functions downstream of the receptor tyrosine kinase torso, acting in concert with D-Raf via tailless. Also functions downstream of Egfr (epidermal growth factor receptor) and btl (fibroblast growth factor receptor). The SH2 domain suggests that csw... |
P0CI23 | RCCGYKMCHPC | Function: Chi-conotoxins inhibit the neuronal noradrenaline transporter (NET/SLC6A2).
Sequence Mass (Da): 1301
Sequence Length: 11
Domain: The cysteine framework is X (CC-CX[hydroxyPro]C).
Subcellular Location: Secreted
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P58808 | MRCLPVLIILLLLTASAPGVVVLPKTEDDVPMSSVYGNGKSILRGILRNGVCCGYKLCHPC | Function: Chi-conotoxins inhibit the neuronal noradrenaline transporter (NET/SLC6A2).
Sequence Mass (Da): 6499
Sequence Length: 61
Domain: The cysteine framework is X (CC-CX[hydroxyPro]C).
Subcellular Location: Secreted
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P58810 | VGVCCGYKLCHPC | Function: Chi-conotoxins inhibit the neuronal noradrenaline transporter (NET/SLC6A2).
Sequence Mass (Da): 1382
Sequence Length: 13
Domain: The cysteine framework is X (CC-CX[hydroxyPro]C).
Subcellular Location: Secreted
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P94286 | MVRFMYALRKRRLSLLLAMSLLVMCVASVVSPPPQALASGSGGIERVFTDKARYNPGDAVSIRVQAKNGTGSSWSGAARLEIFHLENSVYTSSQSLSLTNGQSTTLTFTWTAPSTDFRGYFVRIDAGTLGQGATAIDVSSDFTKYPRYGYISEFESGETALESKAKVDQLAQDYHINAWQFYDWMWRHDKMIKRTGGSIDSTWLDLFNREISWSTLQNQIDAVHDVNGKAMAYAMIYASRENYSPLGISPTWGIYEDSSHTNQFDVDFGDGSTYLYMSDPQNPNWQNYIHAEYIDSINTAGFDGIHVDQMGQRSNVYDYN... | Function: Produces cycloisomaltooligosaccharide from dextran containing 7, 8 or 9 glucose units. The enzyme is specific for (1->6)-alpha-D-glucans (dextrans) and, without activity toward (1->4)-alpha-D-glucans, such as amylose. It also has no activity on oligosaccharides, such as amylopectin and pullulan, containing (1... |
A5FXV3 | MSGAAARGDRLVGTWLLVICFMIFGMVVGGGHARTIGAGFVIQTWQPFTGIVPPLTHAAWERAFGLYKATAQYQAMQPKMTLAQFQSLYLPMFLDRDWGRLMAVVFLVPLAVFRLRGRISNRLTAWLLFLFGLGAGEATMGWYMTYEGMTSRILQPSPLYLGPHFVLAMLIFTAMLWTALTLRNPEPAILPGLARLRGLLSVSIGLIIATIGLGALVAASGALKVYNTFPLMDGHALPPHALAMHPLWLNFLANKATVQFEHRVAATVTAIVVVIAAAMGLRAPVGAKARDLFLLLAGLVSLQYILGMSTLVSGMAELGY... | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A... |
A5FXV4 | MASQSVAGIGGRTAAGEARAASPESRRMVAIWLFVSFALIVEMFGIGAYVQNMNAGLSIMAWQPVSGVIPPLTHAAWERMFALYKTIPQYKELNRGMDLAGFKAIFWPEWIHRMWGRLLGFDFGVPLVWFLWTGRIERRLRPWLVTLFVLGGVQGLIGWWMVASGFQPGLTEVSVFRLSVHYCFATLLAIAVFATALTVLKPAETRLPPEEAARYAGARRMAMGSIVLISIAIVAGTFLSGTHAYTIDNTFPLMQGRWVPPDYAALHPFWKNFFLNKAATQFDHRLLGTVAAVGVLAAVVAAIRADLPARARDAFLVMGA... | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A... |
Q7CZN9 | MANGSVDMVVEAALQKQEKDRRLLRIWLRVVLFTLFCLVLVGGATRLTESGLSITEWKPIHGAIPPLSVAEWEEEFQLYKRIPQYQEINKGMSLDEFKTIFWWEWAHRLLARTIGLVFALPLAFFWLTGRVEKRLRLPLVGLLALGGFQGFVGWWMVSSGLVNRTDVSQYRLATHLTIACLIFAGCMWILRGLSHHSPDAADERTGRGFAALLTVLCLFQIYLGALVAGLNAGLSYNTWPLMDGSLVPGDLFLQQPWWINLFENPKTVQFVHRLGAYTLFAATLWHMVSMARALPGTPHARRAVLFFVLISVQAGLGITT... | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A... |
Q04443 | MHKRLKIYSVITSIGVLIVLLQGALVTKTGSGEGCGATWPLCFGEVIPTNPAIETIIEYSHRIVSGLVGAMIIILAIWAWKQLKHMREAKALSFAAVILIIFQGLLGAGAVVFGQSKAILALHFGISAMSLAAVVLLTILAFEDGREHTMAPKVSRGFKYYVFFVITYCYAVIYSGAYVKHSEATLACAGFPLCNGQIFPGLYGPVGAHYFHRVVGTILLLFLLILMIWTLSRYRHYRVLTWTAVLSFLLVVGQFISGISIVFTQNALSVGLIHALIISILFSALSYMTMIITRPSH | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A... |
Q5PBP7 | MKAHFGVTVWLGVCCSMTLLMVVIGGITRLTHSGLSITEWQPIVGVVPPIGDEAWLREKEKYAQTPEYRHRAADISLDDFKRIYIIEYIHRLFGRALGAVFCLPIPYFAITKRIDRAMVAKLLIVALLGGMQGAMGWFMVKSGLVDTPRVSHYRLAGHLFLTILLFSILWHSFLRCAGVRSTTTTTNARFFTAAAVVGLTVLQMVLGALVAGLDAGLTYNTFPLMDGAIIPQSLFSAKLWHGGFLHDVTAVQFLHRLVAVLIVVCAAPLPFWLKTRGAWLFLACVALQFLLGVATLVSVVHIFLAAMHQVFGFVTLAAGV... | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A... |
Q13363 | MGSSHLLNKGLPLGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYS... | Cofactor: NAD is required for efficient interaction with E1A. Cofactor binding induces a conformation change.
Function: Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi co... |
Q9Z2F5 | MSGVRPPIMNGPMHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEA... | Cofactor: Cofactor binding induces a conformational change.
Function: Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) dif... |
O23702 | MSKIRSSATMPHRDQPSPASPHVVTLNCIEDCALEQDSLAGVAGVEYVPLSRIADGKIESATAVLLHSLAYLPRAAQRRLRPHQLILCLGSADRAVDSTLAADLGLRLVHVDTSRAEEIADTVMALILGLLRRTHLLSRHALSASGWLGSLQPLCRGMRRCRGMVLGIVGRSVSARYLASRSLAFKMSVLYFDVPEGDEERIRPSRFPRAARRMDTLNDLLAASDVISLHCALTNDTVQILNAECLQHIKPGAFLVNTGSCQLLDDCAVKQLLIDGTIAGCALDGAEGPQWMEAWVKEMPNVLILPRSADYSEEVWMEIR... | Cofactor: Cofactor binding induces a conformational change.
Function: Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex (By similarity). Required for cortical microtubules (MTs) arrangement that confers cell shape. Cooperatively with IPGA1, regulates negatively cortical... |
P00766 | CGVPAIQPVLSGLSRIVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN | Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 25666
Sequence Length: 245
Subcellular Location: Secreted
EC: 3.4.21.1
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B2S753 | MRVLLIEDDSAIAQSIELMLKSESFNVYTTDLGEEGIDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLSKVKTPILILSGMAGIEDKVRGLGFGADDYMTKPFHKDELIARIHAIVRRSKGHAQSVITTGDLVVNLDAKTVEVAGQRVHLTGKEYQMLELLSLRKGTTLTKEMFLNHLYGGMDEPELKIIDVFICKLRKKLDAVSGNQSYIETVWGRGYVLREPDAEMRESA | Function: Component of a regulatory phosphorelay system that controls B.abortus cell growth, division, and intracellular survival inside mammalian host cells. This signaling pathway is composed of CckA, ChpT, CtrA and CpdR. CtrA is a response regulator substrate of ChpT. When phosphorylated, directly regulates the expr... |
P47796 | MGHEVDSVLPGLFRRTYGCGRPAISPVITGYSRIVNGEEAVPHSWSWQVSLQDQTGFHFCGGSLINENWVVTAAHCNVKNYHRVVLGEHDRSSNSEGVQVMTVGQVFKHPRYNGFTINNDILLVKLATPATLNMRVSPVCLAETDDVFEGGMKCVTSGWGLTRYNAADTPALLQQAALPLLTNEQCKKFWGNKISDLMICAGAAGASSCMGDSGGPLVCQKAGSWTLVGIVSWGSGTCTPTMPGVYARVTELRAWVDQTIAAN | Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 28294
Sequence Length: 263
Subcellular Location: Secreted
EC: 3.4.21.1
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P0A0V8 | MFKVKFYIRHAVLLLCGSLIVGCSAIPSSGPSAKKIVSLGQQSEVQIPEVELIDVNHTVAQLLYKAQINQSFTQFGDGYASAGTLNIGDVLDIMIWEAPPAVLFGGGLSSMGSGSAHQTKLPEQLVTARGTVSVPFVGDISVVGKTPGQVQEIIKGRLKKMANQPQVMVRLVQNNAANVSVIRAGNSVRMPLTAAGERVLDAVAAVGGSTANVQDTNVQLTRGNVVRTVALEDLVANPRQNILLRRGDVVTMITNPYTFTSMGAVGRTQEIGFSARGLSLSEAIGRMGGLQDRRSDARGVFVFRYTPLVELPAERQDKWI... | Function: Involved in transport of capsular polysaccharides to the cell surface. May function as a membrane anchor for capsular polysaccharides. Possible porin properties.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41949
Sequence Length: 391
Subcellular Location: Cell outer membrane
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P17538 | MASLWLLSCFSLVGAAFGCGVPAIHPVLSGLSRIVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHCGVRTSDVVVAGEFDQGSDEENIQVLKIAKVFKNPKFSILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKYNANKTPDKLQQAALPLLSNAECKKSWGRRITDVMICAGASGVSSCMGDSGGPLVCQKDGAWTLVGIVSWGSDTCSTSSPGVYARVTKLIPWVQKILAAN | Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 27713
Sequence Length: 263
Subcellular Location: Secreted
EC: 3.4.21.1
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