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Synthyra 7

G5EFT4

MAPPHPRDPSTAANYEQVTVSHYALKWKVDFEKKHIAGDVSITLDVKQDTERIVLDTRDLSVQSVALNLNGEPKKAGFTLEDNQALGQKLVITTESLKSGDRPVLEIKYESSNNAAALQFLTAEQTTDRVAPYLFSQCQAINARSIVPCMDTPSVKSTYEAEVCVPIGLTCLMSAIGQGSTPSECGKRTIFSFKQPVSIPSYLLAIVVGHLERKEISERCAVWAEPSQAEASFYEFAETEKILKVAEDVAGPYVWGRYDLVVLPATFPFGGMENPCLTFITPTLLAGDRSLVNVIAHEISHSWTGNLVTNFSWEHFWLNEGFTVFLERKIHGKMYGELERQFESESGYEEALVRTVNDVFGPDHEYTKLVQNLGNADPDDAFSSVPYEKGSALLFTIEQALGDNSRFEQFLRDYIQKYAYKTVSTEEWKEYLYDSFTDKKVILDNIDWNLWLHKAGLPPKPKYDSTPMQACKDLAAKWTTEGSEAPTDGEVFAKMSNSQKLAVLDAVRVNKTMFGDRMPALTATYKLDQAKNAELKFSWLMLGLETKWSPIVDASLAFALAVGRMKYCKPIYRSLFGWSATRDRAISQFKANIPNMHPITVKAIQSLLK

Cofactor: Binds 1 zinc ion per subunit. Function: Aminopeptidase which preferentially removes N-terminal Arg and Lys residues from peptides and proteins. Catalytic Activity: Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys. Sequence Mass (Da): 68249 Sequence Length: 609 Subcellular Location: Cytoplasm EC: 3.4.11.6

Q5HAP2

MINVSFLGLMSGISVLLKTTVIVVGIFEGSNHLEDNGALEGYNDKIMEIVNGYQSFDGKFAEVLPIIGLEKDFPVVVVIGLGKSEDFDENKALKVGGVIYSELNRMKIPDASIVINTDSNVSANIGYGALLRSFKFDKYFVEKKDKNSVYLNKLVLFSKSEPQEVTALFNDLKAEGESIFLARSFVSEPPNILYPETYAQMIYEELSKVGVTVEVFDEDYMKANQMMALLGVGQGSAKKSRLVVMKWNGGDESESPIAFVGKGVTFDTGGISLKPSKGMWDMKYDMAGSASVVGIMRTLAARKAKVNAVGVVGLVENSVDGNAQRPSDVVISMSGQTIEVLNTDAEGRLVLADALWYTQEMFTPKLMVDLATLTGAVVVALGNNQYAGLFSNDDAIANQLIVAGNESGEKLWRLPLDEAYDKLIDSSIADMQNISTKGYGADSITAAQFLQRFVNGVPWVHLDIAGMAWDYEGTEICPKGATGFGVRLLNRFVSKYYESH

Cofactor: Binds 2 manganese ions per subunit. Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Sequence Mass (Da): 54436 Sequence Length: 500 Subcellular Location: Cytoplasm EC: 3.4.11.1

Q8RHT8

MSFQCVKKYEDSYDKYVLAATSEKVVLPDYLDKESKKIAETIIKKNKFTAKASEKISMTLVNKKKVIEFIIIGLGEKKKLDAKNTRQYLFDGLKNIIGKVLFSFDNKDLDNIDILAEVVEHINYKFDKYFSKKKEEFLEVSYLTDKKVPKLIEGYELAKISNIVKDLVNEQAEVLNPKELADRATKLGKKFGFDVEILDEKKAQKLGMNAYLSVARAAHHRPYVIVMRYKGNAKSKYTFGLVGKGLTYDTGGLSLKPTDSMLTMRCDMGGAATMIGAMCSVAKMKLKKNVTCVVAACENSIGPNAYRPGDILTAMNGKTIEVTNTDAEGRLTLADALTYIVRKEKVNEVIDAATLTGAIMVALGEDVTGVFTNDEKMARKVIDASENWNEYFWQMPMFDLYKKNLKSSYADMQNTGVRWGGSTNAAKFLEEFIDDTKWVHLDIAGTAWASGANPYYSQKGATGQVFRTVYSYIKDNKN

Cofactor: Binds 2 manganese ions per subunit. Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Sequence Mass (Da): 53585 Sequence Length: 478 Subcellular Location: Cytoplasm EC: 3.4.11.1

Q74GB4

MVISVEAADYTAFPCAALLVGCREDNPLEDSLLARIDQLLQGAIASLVQSREITGELNRVTILHTLGRLPAERIVLVGLGNSGALTSDRLRQVGGSAVKALKGAGVTRAASVVHRAAGVPPTSVADIAQGLSLGDYSFDIYKTKPGTTVPVTELVNLFEPGTDTADAERLLAADATICEAVSFARDLVSQPGNVATPLFLAEKALEFSARLGIACTVLDRDEMERQGMEGILSVAKGSHQLPRFIVLEYRGGSADKRPTVLVGKGITFDSGGISLKPREGMERMKDDMAGAAAVMGAVMAVAGLRLPVNVIGLIPAAENLPGGGAYKPGDIVRTMSGQTVEIVNTDAEGRMILSDALFYAQRFKPAAVIDLATLTGACLVALGSAVSGVMGNDAALVKLLRRAGEATGERLWELPLWDEYGEIMKSDVADLKNAGGPHAGTITAAWFLQRFVGKSRWAHVDIAGTAWEEKGRPYQPKGATGVGVRLLVEYLKATVR

Cofactor: Binds 2 manganese ions per subunit. Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Sequence Mass (Da): 52228 Sequence Length: 496 Subcellular Location: Cytoplasm EC: 3.4.11.1

Q01433

MASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALITQAVQSEMLETIPEEAGITMSPGPQ

Cofactor: Binds 1 zinc ion per subunit. Function: AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle. Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+) Sequence Mass (Da): 94890 Sequence Length: 825 Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. EC: 3.5.4.6

Q9DBT5

MASYPGPGKSKAKYPFKKRAGLQASAAAPEARSGLGASPLQSARSLPGNAPCLKHFPLDLRTSMDGKCKEIAEELFSRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRGLWERDVVLEREFQRVIISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQSPDTPVSADAPVHPPALEQHPYEHCEPSAMPGDLGLGLRMVRGVVHVYTRRDPDEHCPEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNKISGKYFAHIIKEVMADLEESKYQNAELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALITQAVQSEMLETIPEEVGIVMSPGP

Cofactor: Binds 1 zinc ion per subunit. Function: AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle. Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+) Sequence Mass (Da): 94696 Sequence Length: 824 Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. EC: 3.5.4.6

Q01432

MPRQFPKLNISEVDEQVRLLAEKVFAKVLREEDSKDALSLFTVPEDCPIGQKEAKERELQKELAEQKSVETAKRKKSFKMIRSQSLSLQMPPQQDWKGPPAASPAMSPTTPVVTGATSLPTPAPYAMPEFQRVTISGDYCAGITLEDYEQAAKSLAKALMIREKYARLAYHRFPRITSQYLGHPRADTAPPEEGLPDFHPPPLPQEDPYCLDDAPPNLDYLVHMQGGILFVYDNKKMLEHQEPHSLPYPDLETYTVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEMLNEMSEFKELKSNPHRDFYNVRKVDTHIHAAACMNQKHLLRFIKHTYQTEPDRTVAEKRGRKITLRQVFDGLHMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGASELRDLYLKTENYLGGEYFARMVKEVARELEESKYQYSEPRLSIYGRSPEEWPNLAYWFIQHKVYSPNMRWIIQVPRIYDIFRSKKLLPNFGKMLENIFLPLFKATINPQDHRELHLFLKYVTGFDSVDDESKHSDHMFSDKSPNPDVWTSEQNPPYSYYLYYMYANIMVLNNLRRERGLSTFLFRPHCGEAGSITHLVSAFLTADNISHGLLLKKSPVLQYLYYLAQIPIAMSPLSNNSLFLEYSKNPLREFLHKGLHVSLSTDDPMQFHYTKEALMEEYAIAAQVWKLSTCDLCEIARNSVLQSGLSHQEKQKFLGQNYYKEGPEGNDIRKTNVAQIRMAFRYETLCNELSFLSDAMKSEEITALTN

Cofactor: Binds 1 zinc ion per subunit. Function: AMP deaminase plays a critical role in energy metabolism. Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+) Sequence Mass (Da): 88812 Sequence Length: 767 Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. EC: 3.5.4.6

O80452

MEPNIYQLALAALFGASFVAVSGFFMHFKALNLVLERGKERKENPDGDEPQNPTLVRRRSQVRRKVNDQYGRSPASLPDATPFTDGGGGGGGDTGRSNGHVYVDEIPPGLPRLHTPSEGRASVHGASSIRKTGSFVRPISPKSPVASASAFESVEESDDDDNLTNSEGLDASYLQANGDNEMPADANEEQISMAASSMIRSHSVSGDLHGVQPDPIAADILRKEPEQETFVRLNVPLEVPTSDEVEAYKCLQECLELRKRYVFQETVAPWEKEVISDPSTPKPNTEPFAHYPQGKSDHCFEMQDGVVHVFANKDAKEDLFPVADATAFFTDLHHVLKVIAAGNIRTLCHRRLVLLEQKFNLHLMLNADKEFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGTYLTLREVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLGEITKQVFSDLEASKYQMAEYRISIYGRKMSEWDQLASWIVNNDLYSENVVWLIQLPRLYNIYKDMGIVTSFQNILDNIFIPLFEATVDPDSHPQLHVFLKQVVGFDLVDDESKPERRPTKHMPTPAQWTNAFNPAFSYYVYYCYANLYVLNKLRESKGMTTITLRPHSGEAGDIDHLAATFLTCHSIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPVFFLRGLNVSLSTDDPLQIHLTKEPLVEEYSIAASVWKLSACDLCEIARNSVYQSGFSHALKSHWIGKDYYKRGPDGNDIHKTNVPHIRVEFRDTIWKEEMQQVYLGKAVISDEVVP

Cofactor: Binds 1 zinc ion per subunit. Function: AMP deaminase plays a critical role in energy metabolism. Essential for the transition from zygote to embryo. Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+) Location Topology: Single-pass membrane protein Sequence Mass (Da): 95130 Sequence Length: 839 Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. Subcellular Location: Membrane EC: 3.5.4.6

P82974

MLLDEGWLAEARRVPSPHYDCRPDDENPSLLVVHNISLPPGEFGGPWIDALFTGTIDPNAHPYFAGIAHLRVSAHCLIRRDGEIVQYVPFDKRAWHAGVSSYQGRERCNDFSIGIELEGTDTLAYTDAQYQQLAAVTNALITRYPAIANNMTGHCNIAPERKTDPGPSFDWARFRALVTPSSHKEMT

Cofactor: Zn(2+) is required for amidase activity. Function: Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also involved in beta-lactamase induction . Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Sequence Mass (Da): 20847 Sequence Length: 187 Subcellular Location: Cytoplasm EC: 3.5.1.28

Q54DD0

MSTPLRGSSPQVSFYESELDQEGGSDASHFTYRNYMEDDKINSFTFNMARKDQTQLFQRIILTNESESEIEEYAEVAEQLLDAINLREKYVFHPKIWKADAPVGEKPPYSPFESDESTNCATEHMFKEVNGVYFVYSNETDMKSNKALFSVPHTLASYYKDINNLMMLSSYGPAKTFTFKRLQLLESKFNMHTLLNDSLELFQQKTAPHRDFYNVRKVDTHVHHSSSMNQKHLLKFIKRKLKENPNEIVIFRDDKYLTLAEVFKSLNLDVDELSVDTLDVHADNNTFHRFDKFNLKYNPCGQSRLREIFLKTDNLIKGKYLAEISKEVFTDLESSKYQCAEYRLSIYGRKMSEWDTLASWIVDNDLFSTKVRWLIQVPRLYDVYRETSTTTFQDFLNNVFHPLFEVTKDPSSHPKLHLFLQQVVGIDCVDDESKFEKKFTEKFPVPGEWSSEHNPPYTYYLYYLYANLYTLNQFREEKGLNILTLRPHSGEAGEVDHMGAAFYLAHGINHGINLRKTPVLQYLYYLTQIGIAMSPLSNNSLFLTYNRNPFPAFFARGLNVSISTDDPLQFHYTKEPLMEEYSIATQVWRLSVCDICEIARNSVLQSGFEHNVKSHWLGPDYANSGGNDIKKTNISDIRVCFRNETLIEELHLILKSLQTLPNFKNLNINFLLDKLPSEITTGNDYKLKKAQLKLNGANKLRNSSVGSTPNNGTPSSSGTPSLSSPGAIVHLMKTKPYIPPPLSLNIKQENNNNNNNNNNNNNNNNNNNTNTNTNSNSTTTNQDDNSKSDK

Cofactor: Binds 1 zinc ion per subunit. Function: Catalyzes the conversion of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia (NH4(+)) . Participates in the regulation of the adenylated nucleotide pool and the interconversion to guanylated nucleotides during early morphodifferentiation . Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+) Sequence Mass (Da): 90954 Sequence Length: 790 Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. Subcellular Location: Cytoplasm EC: 3.5.4.6

P13016

MLLEQGWLVGARRVPSPHYDCRPDDETPTLLVVHNISLPPGEFGGPWIDALFTGTIDPQAHPFFAEIAHLRVSAHCLIRRDGEIVQYVPFDKRAWHAGVSQYQGRERCNDFSIGIELEGTDTLAYTDAQYQQLAAVTRALIDCYPDIAKNMTGHCDIAPDRKTDPGPAFDWARFRVLVSKETT

Cofactor: Zn(2+) is required for amidase activity. Function: Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also involved in beta-lactamase induction . Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Sequence Mass (Da): 20536 Sequence Length: 183 Subcellular Location: Cytoplasm EC: 3.5.1.28

P82973

MLLENGWLVDARHVPSPHHDCRPEDEKPTLLVVHNISLPPGEFGGPWIDALFTGTIDPDAHPFFAEIAHLALSADCLIRRDGEVVQYVPFDKRAWHAGVSMYQGRERCNDFSIGIELEGTDTTPYTDAQYEKLVAVTQTLIGRYPAIADNITGHSDIAPERKTDPGPAFDWSRFHAMLTTSSDKEIT

Cofactor: Zn(2+) is required for amidase activity. Function: Involved in cell wall peptidoglycan recycling. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety. Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Sequence Mass (Da): 20839 Sequence Length: 187 Subcellular Location: Cytoplasm EC: 3.5.1.28

Q84NP7

MDSTYALHLAVATLLGASFAAASAYYMHRKTLDQLLRFARSLDRDHRRRNRHLLDADDDDDDDPPRDHDRRTTLPIPPGLPPLHTGREGKPIISPASTKRVGPLVRPTTPRSPVPTVSAFETIEDSDDDDENIAPDAKNNAVSLLTNGTIGSDPLPGKASQNGDTKPVPSTNMIRSQSATGSLHGAQHNPVAADILRKEPEHETFSRINITAVETPSPDEIEAYKVLQKCLELREKYMFREEVAPWEKEIITDPSTPKPNPNPFYYEQQTKTEHHFEMVDGVIHVYPNKDAKERIYPVADATTFFTDMHYILRVLAAGDIRTVCYKRLNLLEQKFNLHLMVNADRELLAQKAAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGTYLTLKEVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKKSEWDQMASWIVNNELYSENVVWLIQIPRIYNVYREMGTINSFQNLLDNIFLPLFEVTVDPASHPQLHVFLQQVVGLDLVDDESKPERRPTKHMPTPEQWTNVFNPAYAYYVYYCYANLYTLNKLRESKGMTTIKLRPHCGEAGDIDHLAAAFLTSHNIAHGVNLKKSPVLQYLYYLAQIGLAMSPLSNNSLFIDYHRNPFPTFFLRGLNVSLSTDDPLQIHLTKEPLVEEYSIAASLWKLSSCDLCEIARNSVYQSGFSHRLKSHWIGRNYYKRGHDGNDIHQTNVPHIRIEFRHTIWKEEMELIHLRNVDIPEEIDR

Cofactor: Binds 1 zinc ion per subunit. Function: AMP deaminase plays a critical role in energy metabolism. Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+) Location Topology: Single-pass membrane protein Sequence Mass (Da): 93854 Sequence Length: 815 Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. Subcellular Location: Membrane EC: 3.5.4.6

P0CL03

MLPDKGWLVEARRVPSPHYDCRPDDEKPSLLVVHNISLPPGEFGGPWIDALFTGTIDPDAHPFFAEIAHLRVSAHCLIRRDGEIVQYVPFDKRAWHAGVSNYQGRERCNDFSIGIELEGTDTLAYTDAQYQQLAAVTRTLIASYPAIADNMTGHCNITPDRKTDPGPAFDWPRFRALVALSSHKEMT

Cofactor: Zn(2+) is required for amidase activity. Function: Involved in cell wall peptidoglycan recycling. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety. Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Sequence Mass (Da): 20943 Sequence Length: 187 Subcellular Location: Cytoplasm EC: 3.5.1.28

P50998

MNMEQEDDQVPAVAAETVPLKRYVTNPGANRDEEVAAAPSSQDTPYFDYAYERSLRHQDAKFLAMNGTQNGRDGLPSKSPRRPSVSASTVRNSDDVNHSKAGPGSGKLLNDTLQSKISSIHMPHVQQGDNAVVSSVGGPETDPGNMETTDPLFSDELAEIYLSIHKCMDMRHKYIRVSLQGELDNPIDDDSWIIYPDCKEGEDDTGLFNFADCKIPGIENEMEYHMDHQGIFQVYENDSAYIAGTPSFHIPTIRDYYIDLEFLLSASSDGPSKSFSFRRLQYLEGRWNMYMLLNEYQELADTKKVPHRDFYNVRKVDTHVHHSALANQKHLLRFIKAKLRKCPNEKVIWRDGKFLTLQEVFDSLKLTSYDLSIDTLDMHAHTDTFHRFDKFNLKYNPIGESRLRTIFLKTDNDINGRYLAELTKEVFTDLRTQKYQMAEYRISIYGRNREEWDKLAAWIIDNELFSPNVRWLIQVPRLYDVYKKSGIVETFEEVVRNVFEPLFEVTKDPRTHPKLHVFLQRVIGFDSVDDESKPERRTFRKFPYPKHWDINLNPPYSYWLYYMYANMTSLNSWRKIRGFNTFVLRPHCGEAGDTDHLASAFLLSHGINHGILLRKVPFLQYLWYLDQIPIAMSPLSNNALFLAYDKNPFLTYFKRGLNVSLSTDDPLQFAFTREPLIEEYAVAAQIYKLSAVDMCELARNSVLQSGFERQLKERWLGVDFQDIDRTNVPIIRLAYRALTLTQEIALVNKHVQPSKHPSNHDLEELIHKYDAMTGTSDPLSASPRTNDATISSRLSLHDGHDHGAFFPGLSVISERRRRKDSMASSSQDLKD

Cofactor: Binds 1 zinc ion per subunit. Function: AMP deaminase plays a critical role in energy metabolism. Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+) Sequence Mass (Da): 95887 Sequence Length: 831 Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. Subcellular Location: Cytoplasm EC: 3.5.4.6

P15274

MDNQATQRLNDLSLEPAPSHDEQDGSGLVIDIDQRKIGDEQAGVVVDDETPPLEQQDSHESLAADSRNANFSYHENQQLLENGTKQLALDEHDSHSAILEQPSHSTNCSSSNIAAMNKGHDSADHASQNSGGKPRTLSASAQHILPETLKSFAGAPVVNKQVRTSASYKMGMLADDASQQFLDDPSSELIDLYSKVAECRNLRAKYQTISVQNDDQNPKNKPGWVVYPPPPKPSYNSDTKTVVPVTNKPDAEVFDFTKCEIPGEDPDWEFTLNDDDSYVVHRSGKTDELIAQIPTLRDYYLDLEKMISISSDGPAKSFAYRRLQYLEARWNLYYLLNEYQETSVSKRNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKHKLRHSKDEKVIFRDGKLLTLDEVFRSLHLTGYDLSIDTLDMHAHKDTFHRFDKFNLKYNPIGESRLREIFLKTNNYIKGTYLADITKQVIFDLENSKYQNCEYRISVYGRSLDEWDKLASWVIDNKVISHNVRWLVQIPRLYDIYKKTGIVQSFQDICKNLFQPLFEVTKNPQSHPKLHVFLQRVIGFDSVDDESKVDRRFHRKYPKPSLWEAPQNPPYSYYLYYLYSNVASLNQWRAKRGFNTLVLRPHCGEAGDPEHLVSAYLLAHGISHGILLRKVPFVQYLYYLDQVGIAMSPLSNNALFLTYDKNPFPRYFKRGLNVSLSTDDPLQFSYTREPLIEEYSVAAQIYKLSNVDMCELARNSVLQSGWEAQIKKHWIGKDFDKSGVEGNDVVRTNVPDIRINYRYDTLSTELELVNHFANFKRTIEEK

Cofactor: Binds 1 zinc ion per subunit. Function: AMP deaminase plays a critical role in energy metabolism. Catalytic Activity: AMP + H(+) + H2O = IMP + NH4(+) Sequence Mass (Da): 93302 Sequence Length: 810 Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. EC: 3.5.4.6

O25681

MKGLERESHFTLNENAMFFECAYSCDNALFLQLDDRSFFITDSRYTQEAKESVQPKNGVLAEVVESSDLVQSAIDLIVKSSVKKLFFDPNQVNLQTYKRLNSALGDKVALEGVPSYHRQKRIIKNEHEIQLLKKSQALNVEAFENFAEYVKKIFDEKESLSERYLQHKVKDFLTREGVYDLSFEPILALNANASKPHALPSAKDFLKAEHSILLDMGIKYERYCSDRTRTAFFDPKDFVFKREQSFKDKERQKIYDIVKEAQEKAISGIRAGMTGKEADSLARGVISDYGYGQYFTHSTGHGIGLDIHELPYISSRSETILEEGMVFSVEPGIYIPGFFGVRIEDLVVIKNSRSELL

Cofactor: Binds 2 cobalt ions per subunit. Function: Hydrolyzes the N-terminal amino acid residue from a polypeptide chain, with a preference for substrates containing multiple alanine residues. Sequence Mass (Da): 40796 Sequence Length: 357 EC: 3.4.11.-

B6Q8T5

MTSTDGILAGKYPAKAHARRVVEYLRQNGFQGDGVLYLEAQKTRMIEDNDSEQPFRQRRFFFYLSGCLLPDAHLTYHISTDKLTLFIPPLDPESVIWSGLPLSPAQAKELYDVDEVLYTTDVNPTLAHLASKVGFVFAIDGQISDDVSLKSFPDTDKVALKTAIEECRAVKDAYEVAMIRKANDVTSQAHVAVLKAAKSATNERELEAAFIGTCIAQGCREMAYHPIVASGTSSATLHYVNNDEPLIDSSTNKKKLNLLLDAAGEYKAYCADVTRTFPLSGKFSPESREIYDIVLEMQTESLAMLKEGVLWEDVHITAHRVAIKGLLKLGILRGSEEELLEKRVSVAFFPHGLGHYLGMDTHDTGGHANYADKDKMFQYLRVRGKLPAGSVITVEPGVYFCRFIIEPYLKDSELSKYIDADVLEKYWEVGGVRIEDNIHITKEGHENLTTAPKTADQVELMINGS

Cofactor: Binds 2 manganese ions per subunit. Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Sequence Mass (Da): 51734 Sequence Length: 465 EC: 3.4.11.9

C9SEV5

MASGDNVDYEAVMVDEFDALNIEVRVSAGPSSSVPGAALSAPRCPGMRALPLKAPVMSTPVPAAAPLPTPPAVDDGPSAVGVGNVPPAVDDVPSAVDDVVIQKETTKYSAKLHAAKVADELKASAGLVFLPGEPSRTYEYSDMGPAFSSNAATSSTSPASTSLTPRKVLYNGRVPSIKDVLAASDVDEVRHMQDLPAFLHAYAHQHDKATVYLLDASQSHPALVDNARVHIDTAALRPAMDEARVTKTAHEIALIREANAVSSAAHRAVMRHIRRFASERQVAALFTAECTVRGAPTQAYAPIAGSGPNAATLHYGANDEPLAGRHVLVLDAGCEVNCYASDVTRTLPLGPTGHFTPEARHIYDLVERMQEACVAAVAPGLLYYSLHLKASAIALRGLLRLGILKGDEKAIWAAGTVAAFFPHGLGHHIGLETHDVTGRDRLLLAAGEREPRAKRDAVSAEMLVGLAAAVATGPPYRGKQMLRPGMVVTVEPGIYFNKDYIEGYFLREDKHRAFIDRDVLARYYPVGGVRIEDCILVTDDGYENLTKAPKGEDMLRIIRGEAQ

Cofactor: Binds 2 manganese ions per subunit. Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Catalytic Activity: Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide. Sequence Mass (Da): 60027 Sequence Length: 563 EC: 3.4.11.9

A2BJU0

MPVKGLKVEAASIDPGHDAVILNPRDAEHLGVVAGLRASVVCRGRGVGAVVIVDPRVPERVAQLTKGLVERLGDCDTVDVHPIDVPPSFDAFKKRLSGARLSAAEYKMLIADIVAGYYDDAQIASFLVSQLYSKLADEELEHLIRAMVETGEVVKFGEPVYDVHSIGGVPGNSKVALLVVPIVASRGLLIPKTSSRAITSPAGTADTMEVLAKVAFKPQELHDMALRARGLIVWGGALNLAPADDIFVRVERRIGVDPPTQMVASILAKKLAMSVSRLVIDLPTGRGAKVQDESEAELLASMFLAQAGRLNIAMRVAITFGGEPIGFSVGPALEAREALQTLMKGDGASSLVEKACSLAGLVFELGGVVPRGRGYSLACEILRSGAAYRKFREIIEVQEGDPDIKPEDIKLAPKQFTLEAPRDGIVTMIDNRAISLAARAAGAPEDKGAGIQLHVKTGYRVRKGDPLLTIYASSDTRLHEAVRLLDEYNAVLIEGVVVKVLP

Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. Catalytic Activity: AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate Sequence Mass (Da): 53499 Sequence Length: 502 EC: 2.4.2.57

Q12Z64

MQLKVQPIDVKVGKYKVILNTIDAKELGVHEGDRVRIKNHVTLTAIVDFTEDMISPGMIGLYHEVKEALSKEWTETVEVFPAEKPKSTYIIRKTMDGQKLTKEEIDILVKDIVEENLAEIEIAAFLTATYINDMTDDETEWLTRAMIDSGDKLEFDTHPIMDKHSIGGVPGNKISLLIVPIVAANGLLIPKTSSRAITGAGGTADLMEILAPVEFDAAEIKRMTEEVGGVLVWGGATNIAPADDKLIKVEYPLSIDPHCQMLASIMAKKGAIGADHVVMDIPTGPGTKIKNVQEGRKLARDLINLGDRLGMDVDCALTYGASPVGRTIGPALEVIEALKVLESFEGPNSLIEKSASLAGMLLEMGNVAGKDKGYDLAIETLKNGKALTKFKEIIKIQGGNPDVTHKDISVGEFTEDIIAPNNGYILEMDNKRLVQIARLAGAPNDKGAGILLHRKQGEPLKEGDPVMTIYAEKKSKLENAVKSAKERPPFIVEGMMLERIQSFKEI

Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. Catalytic Activity: AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate Sequence Mass (Da): 55123 Sequence Length: 506 EC: 2.4.2.57

Q2FTS5

MRLTVRLVDIAARGILLHHNDAKSLGVLAGDRIVISSPVTGKATVDYVETTGTLIDQGRIGVYHHTNEQLTLTENEVVEVRVADRPVSLDYIKKKMEGEKLTREDIRAIVADIVQDTLSPSEITAFVVSSYINQLDMDEIESLTRAMVETGDQLSFHAGPIVDKHSIGGVPGNKISLIVVPIIAASGLLIPKTSSRAITGAGGTADLMEVLAPVEFSASEVQEMTIKTGGVIVWGGATNIAPADDKIIIQEYPFKIDQIGQMIASVMAKKFAVGADVVAIDIPVGKYCKVHTIEEGKKLARQFIDLGERLNMRVECALTYGDAPVGRAIGPKLEIKEALSVLEGSDSPRSLIQKSCVIAGIALELAGKANRGEGANLALEILRSGKALKKFLDIIAVQGGTPDVSSEKITVGEHFYTVRADSTGYVIDLNNHSLITIARTAGAPADHGAGLYLHAKHGTSLSKGDPIFTIYADRKWRLEKAIEEARRLRPVMVEGMLIDRVPNVREWVPGRSRNLE

Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. Catalytic Activity: AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate Sequence Mass (Da): 55655 Sequence Length: 516 EC: 2.4.2.57

Q6M0E4

MLFLNAKFIDLDLGENAVIVNEDDLKGTSYYPQDRVLIESHAGSVIGNIYSTKTMVQKGEVGMLVSELAEISISEGEEVKLRHAEKPESIPFIKKKMDGQVLNPHEIRTIIDEIVSKKLSNIELSAFVSSTYINGMNMDEIGEMTKRIAETGDMISWEKNLVVDIHSIGGVPGNKYALLSIPILAAAGITIPKTSSRAITSPAGTADVMEVLTNVELKEDEIKRIVKTTNGCLVWGGGVNLAPADDIIINVERPVSIDPQPQLLASVMAKKIATGIKYSVIDIPVGKGVKIKNEAEGAKLARKFIELGELLNIKVECVLTYGGQPLGRAIGPALEAKEAIEALQDPKNAPKSLIEKALSLAGILLELGGAAQIGEGQNLAWEILESGRALEKFNQIIIEQGGTPKKPEEIELGDYIEEIIAPIDGYVTDINNTGITNVVKEAGAPRDKKAGLLLNSKIGNKVKKGDVLYTIYSGSEERLVSAVNLARRVYPVKVEGMLIERISKF

Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. Catalytic Activity: AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate Sequence Mass (Da): 54597 Sequence Length: 505 EC: 2.4.2.57

Q9BLG4

MVAGEIIKGVAAEITNGSSSSVVQKYLDCANQVAPDPGNTTWVLLSTILVLGMMPALAFFEAGLLRSKNTLSIITQIMSGIVVLTVMWQAFGYSLTFGPDQKGIIGNLDHAFLINVSYDDCSPNAPNIPAAAYAFFMMMFANITPLLMTGAFAERVKFKAFIALTVAWEIIVFYPVAHWIWGGGWLHKYFGVLDFAGGIVIHTSAGVSALVIALYVGRRKDFEKYGGEFPPSNLPLATIGAALLWMGWFGFNAGSALAAGNIATSAVASTQIGGSFSAIVWIILSAAKGKPNTVSVINGVIAGLAGITPASGYINSQYSIGLGICLGLASYYSVVLLKHKLHIDDALDVSSVHGLTGIIGSLAIGFCAELSVNPNGANGAFYGNPKLIGTQLLGVVSVAVWAAAWTWVLLKIIDATIGVKIDESEEELGLDLVEHGEFAYHNISLQGNENHYSSVINSHDFFK

Function: Ammonium transporter that mediates the excretion of ammonium. Controls ammonium homeostasis during growth and development. Ammonium has been shown to function as a morphogen at multiple steps during the development. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 49051 Sequence Length: 463 Subcellular Location: Cell membrane

I3R0S7

MIPLQVDPNVVAQGVNYVWILVVSFLIFFMQPGFALLEAGQVRAKNVGNVLMKNMTDWALGVLVYFVVGAGVATIVGGLTSPGGFDVAAAFSYIGDSGAWIDWLFGAVFAMTAATIVSGAVAERMDFRAYVVFAATITGFIYPVVQGLTWSGGLLSGSGYLGAALGVGYLDFAGATVVHMCGGVAGLVGAKMVGPRKGRFGASGESQPIPGHSMLLAVLGTLILAFGWYGFNVGTQATVLATTESGGLEFMGAALGRVALVTTLGMGAGAVAAMVVSTNYQGKPDPLWMANGLLAGLVAVTGAVPHVTWWGGLVLGALGGAIVLPAYRWTVDSLKIDDVCGVFAVHGVAGAVGTALIPVFAVGGFSATQLVMQVAGVGIIALWTIVASAVVFAAAGTVFGLRVSEEEELEGLDIGEHGVSVYPEFIGESGPDRGVGTRAATDGGNDVRTDGGNDVRTDGGNDVRTDGGNDVRTDGGNDVRTDGGNDVRTDGDVVGDNGVAVTEGNDSAAVDGGENQ

Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 52311 Sequence Length: 516 Subcellular Location: Cell membrane

Q60366

MFEVKHMDGIDVFFFMWAASLIFFMKAGFIALEIGQFRAKNVSYHCVLKLLDLAAVFIAYLFIGYGISYGFENIMPLITGTFDADLGAWWMKMVMFAAAAVTIITGGVAERIKILPYFIGALIVGGILYPIVEHLVWGGGFANLGINFHDYAGSGAVHLFGGLVGLMAAYVLGPRIDKYINGKPQAIPGHNIPIAVLGAFILAFGWYGFNIGSASGIANGVELASVAMATTMALAGGIIGGALSSRNDPLYTANGMCAGLVAVCSGVDLFTPIGAFIVGLLAGIQQPFTYKFIEEKLKIDDVCAIGPVHAMSGLIGVICAGIPFLLKADAVSKVSITGQIIGAIVIALIAIVGGLIIYKGLDLTIGLRVSEEAEKVGLDTAILQTTAYSEE

Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 41153 Sequence Length: 391 Subcellular Location: Cell membrane

Q9C0V1

MSSTTDATPTPSGVNGGDSMTVNLNQFYNNGDVAWILTSTALVFIMIPGVGFFYSGLARRRSAISMLFLSMMSVAIVAFQWFFWGYSLTFSHEGGPYIGSLANFGLRQTLGRPSSGASSVPDILFCVFQGMFAAITPALAIGAAADRGRMFPCMVFMFLWTSIVYDPIAFWTWNPNGWLNKLGSYDFAGGSPVHISSGMAALAYSIVIGKRCDHGTTKYRPHNVPHVVLGTVFLWFGWFGFNGGSSAAANMRGVMAVVVTHLAASVGGIVWCVIDFAKNRHWSVVGFCEGAVAGLVAITPGSGFVPPWAAVVIGALGAVFCYAATYLKKIIRVDDALDIFAEHGVGGMVGNILTALFAADYIEALDGSGTAYTGGWITHHYIQLGYQLADTVSCAAYSFAVSCALLFVMNYIPGLSLRVSREDEVLGLDKIELGESAYYYKDSTDEPPPITTSGVQYTSPTVSDSASNEKEQEHRAQNEAQKEEEYRAESEAQAPAI

Function: Transporter for ammonium to use as a nitrogen source. Under ammonium limitation acts as an ammonium sensor, generating a signal that leads to pseudohyphal growth. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 53387 Sequence Length: 497 Subcellular Location: Membrane

Q84KJ7

MAAAGAYSASLPAVPDWLNKGDNAWQLTASTLVGIQSMPGLVVLYGSIVKKKWAVNSAFMALYAYASSLLVWVLVGFRMAFGDQLLPFWGKAGVALTQSYLVGRATLPATAHGAIPRTEPFYPEATLVLFQFEFAAITLVLLAGSVLGRMNIKAWMAFTPLWLLLSYTVGAFSLWGGGFLYRWGVIDYSGGYVIHLSSGIAGFTAAYWVGPRLKSDRERFSPNNILLMIAGGGLLWMGWAGFNGGAPYAANIAASVAVLNTNVCAATSLLMWTCLDVIFFRKPSVIGAVQGMMTGLVCITPGAGLVQTWAAVVMGIFAGSVPWFTMMILHKKSALLMKVDDTLAVFHTHAVAGLLGGILTGLLATPELFSLESTVPGLRGAFYGGGIKQIGKQLGGAAFVIAWNLVVTTAILLGIGLFIPLRMPDEQLMIGDDAAHGEEAYALWGDGEKFDATRHDLSRGGGGGDRDGPAGERLSALGARGVTIQL

Function: Involved in ammonium transport. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 51411 Sequence Length: 486 Subcellular Location: Cell membrane

Q8S230

MHLRMASPPQPGPYMPDLPAVPAWLNKGDTAWQLVAATFVGIQSMPGLVVIYGSIVKKKWAVNSAFMALYAYASTLIVWVLVGFRMAFGDRLLPFWAKAGPALTQDFLVQRAVFPATAHYGSDGTLETPRTEPFYAEAALVLFEFEFAAITLVLLAGSLLGRMNIKAWMAFTPLWLLFSYTVGAFSLWGGGFLYQWGVIDYSGGYVIHLSSGVAGFTAAYWVGPRLKSDRERFSPNNILLMIAGGGLLWLGWAGFNGGAPYAPNVTATVAVLNTNVSAATSLLTWTCLDVIFFGKPSVIGAVQGMMTGLVCITPGAGLVHTWSAMLMGMFAGSVPWFTMMILHKKSTFLMKVDDTLAVFHTHAVAGILGGVLTGLLATPELCALDCPIPNMRGVFYGSGIGQLGKQLGGALFVTVWNLIVTSAILLCIGLFIPLRMSDDQLMIGDDAAHGEEAYALWGDGEKFDVTRPETTRTGGAGGAGREDTMEQRLTNMGARGVTIQL

Function: Involved in ammonium transport. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 53740 Sequence Length: 501 Subcellular Location: Membrane

G7LAA8

MNFNSSKYISHLPESLLPNDASPEWNNKADNAWQLTAATLVGLQTVPGLVILYGSMVKKKWAVNSAFMALYAFAAVLVCWVLWAHHMAFGTKLLPFVGKPNFALSQKFLLSKASTNYYLPMADFVFYQFAFAAITLVLLGGSLLGRMNFYAWMLFVPLWLTLSYTVGAFTIWGNGFLEGKIIDYAGGFVIHLSSGVAGFTAAYWVGPRTSNDRQNFPPNNIIHMLGGAGFLWMGWTGFNGGAPFQVGEITSLAIFNTHLCTATSILVWISLDMAVYKKGSLIGSVQGMMTGLVCITPGAGLVDPWAAILMGALSGSIPWYTMMVLHKKSPFFQSVDDTLGVFHTHAVAGILGGILSGVFAKPKLLRILYGPYGSGLLYSYFDDNIGQGIKQMWYQLLGAVFITIWNVVITSLICILLNRFVNLRMQEEDLEVGDDAAHGEEAYVLWGDGERMRLPLRRDISPIIPYISHQRHSFPINKIDE

Function: Involved in ammonium transport (By similarity). Required for arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme and G.intraradices) in low nitrogen conditions . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 53080 Sequence Length: 481 Subcellular Location: Cell membrane

G7L1W7

MELPSNLLPDEASPEWMNKGDNAWQLTAATMVGLQSIPGLVILYGSLVKKTWAINSAFMAFYAFASVLLCWVSWAYQMSFGEKMVFFLGKPNVALDEKFLLGKAFLGNFPNATMVFYQGVFAGLTLILIAGALLGRMNIRAWMLFVPLWVTFSYTVVAFSIWCPDGWLAKRGVIDFAGGYVIHLSAGVAGFTAAYWVGPRADKDRETFPAATNNMIMVLAGAGLLWMGWSGFNGGAPFVASTIASLAILNTHVCTAASITVWVMLDTFYFGKPTVFGAVQGMITGLVCITPAAGVVQGWAAILMGFISGSIPWYTMMVLHNKVNFLKKIDDPMAVFHTHAIAGALGGILTGFFAVPKLCRLFYMVPDWEKYIGLAYGLQNKGATQAGLKQMVIQIEAIVFVICYNVLMTSLICLIVRVIVPLRLNGDALQMGDKAIHGEDAFALHSEATKFVNIKRNQVYDTQDFSSIPESRSLGELQMV

Function: Involved in ammonium transport . May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 52393 Sequence Length: 480 Subcellular Location: Cell membrane

Q9M6N7

MAGAYDPSLPEVPEWLNKGDNAWQLTAATLVGLQSMPGLVILYASIVKKKWAVNSAFMALYAFAAVLLCWVLLCYKMAFGEELLPFWGKGGPAFDQGYLKGQAKIPNSNVAAPYFPMATLVYFQFTFAAITTILVAGSVLGRMNIKAWMAFVPLWLIFSYTVGAYSIWGGGFLYQWGVIDYSGGYVIHLSSGVAGFVAAYWVGPRPKADRERFPPNNVLLMLAGAGLLWMGWSGFNGGAPYAANLTSSIAVLNTNLSAATSLLVWTTLDVIFFGKPSVIGAIQGMVTGLAGVTPGAGLIQTWAAIIIGVVSGTAPWASMMIIHKKSALLQKVDDTLAVFYTHAVAGLLGGIMTGLFAHPDLCVLVLPLPATRGAFYGGNGGKQLLKQLAGAAFIAVWNVVSTTIILLAIRVFIPLRMAEEELGIGDDAAHGEEAYALWGDGEKFDATRHVQQFERDQEAAHPSYVHGARGVTIVL

Function: High affinity ammonium transporter that may play an important role in moving ammonium between the apoplast and symplast of cells throughout the plant. Does not transport methylammonium. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 50768 Sequence Length: 475 Subcellular Location: Cell membrane

O28528

MVGRMCVAVLIVLLLVATAGADPNGAETLKENPELPVDFVWALICGFLVMFMQAGFAMLEAGFSRAKNVANVMMKNLMDFAVGSLAFFAVGFALMMGADWQGIAGTTGWFLAGESYDVSTIELWFFMLVFAATAATIVSGSIAERPKFSVYLVYSAVVSAVIYPIYGHWLWGGGWLSSSEFMVKLGGGYGALDFAGSGVVHALGGYIALAAVMLLGPRLGKYDSDGNPRAIPGHNLAFAVIGTFILWFGWFGFNAGSTLSAHELRVSIIASNTNLAAAAGAVTAMAITWLRNGKPDVGMTCNGAVAGLVAITAPCAWVQPWSSVVIGTIAGFIATYGYWWLEKRGLDDVVGAIPVHGFSGTWGLIALGIFADGSYGLYATESPLVTGLLYGNWGFFIVQLISAIVNFAWAFGTGFALFWILKKVIGIRVSPEEEMLGLDIAEHAAVAYPNFVCTETELPLAMKQGGGR

Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)). Transport is electrogenic. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 49591 Sequence Length: 468 Subcellular Location: Cell membrane

Q20605

MNTLQNLTLKMDRQPTIRMKPDKQLDCSLSQDDGVWMMASSFIIFTMTAGFGLLESGRVSSKDEVNCMVKNVFDVIFGGLAYWMFGYGLTFGDSKHQLGRYVGFGDFFFDPERVSDDDSTDEKGISYSLFIFQMSFATTTSTIVSAGMSERIHLKSHCFISFFITLVHSVAGHWVWDQEGVFRMMGVVDSAGCSAVHLVGGVSGLVATLYLKPRRNRFAKNGIRTVSDPTKAILGFLMIWWGWLAFNTSSNYAVTHGQWTEGMRSAVGTILASAGGGVVTVIITRLSTKKIQMDMLIDGMLASLVASTGGCLYFTPWQATLVGAIGSSLALAAYPVTEWLKIDDPVGVFPVHVVGSIWGMIAPAIFVYRRPMNFGPPECDFQTSDEINGLLYGGGFYLLFLQSFVILVIGTYSAICAFIILFLIHHSPVGLRVDKYTEELGADLIEHGLAGFNVMTYTIEKKLDTKTLSAVLMIIVRWRAKAKLGAQRRKKIHDSGSVAPQQAESVEMNVIHRRH

Function: Involved in the uptake of ammonia (Probable). Implicated in aging. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 56840 Sequence Length: 515 Subcellular Location: Membrane

Q9BLG3

MEYLELNGTKEGLSAAVDDMWVLNATYLVFYMQAGFCMLEAGVVRAKNAKSIIMKSIIDTAIGSLLFWALGFGLAFGNADKASNPVIGTSHFFLINYQNLSFFAFQWAFCATSITIVSGSLAERVHVTSCLVYTIVMSAFIYPLSAHWVWSYNGWLRMIGFNGIIDFSGSIVVHIVGGCIGLVGTYLVGPRIGRFDSESGKPKPLPGHSITIYTLGAFIIWYGFYGFNTGSTLGISGGGIAIASRSAVTMTIIACASCATTLLAIKIKSGKYDVVKSVNSLLGGLVSSAAVCSLIDPWAAFIIGCVTSFVYLGCSHLLIKLRIDDPLDSSAIHLGCGIWGALSVGLFSTQENLSLVLKKSTNVYGLFFGGGFEQLGIQLLGIIIVMAWCFFCASILFTILKKFHLLRIEPTKELMGIDIDSAGGPAYQWDN

Function: Ammonium transporter that mediates the excretion of ammonium from the prestalk cells from the slug. Controls ammonium homeostasis during growth and development. Ammonium has been shown to function as a morphogen at multiple steps during the development. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 46368 Sequence Length: 431 Subcellular Location: Cell membrane

B8ZYW3

MLTALQADLASVVEGVNLVWVLTVTFLIFFMHAGFAMLEAGQVRAKNVANQLTKNLLTWSIGVIVFFLLGAAVSAIVAGLTGGPATTVADAFMGLYAPDASATTAWVDWLFGAVFAMTAATIVSGAVAGRARLRAYLTYTILIAGVIYPVVVGVTWAGGFLNGLGFHDFAGGMIVHGMGGIAGLTAAWIIGPRMNRFNADGSANVIPGHSITFAVLGTLILAFGWYGFNVGTAAAPLAYSDGGVTLGSFAYVGRVALVTTLGMAAGALGAGGVAFYKTGKVDTLYVANGVLAGLVGITAIADDIVWPGALVVGLLAGAQLPIVFEFVEKRLRIDDVCAVFPVHGSAGVLGTLLYPVFAVPVWHEGASIVSLAVPQVVGVGVIAVWTFVATTAIFGGFRAIGQVRVSADHERQGLDTAEHGVDTYPEFGSPDADTGIRADGSGIPYGHGFMTTQEDE

Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 46906 Sequence Length: 456 Subcellular Location: Cell membrane

Q58739

MWGENIATADLFANATDIHSIVQALTTLANASDVFFLVVMGVLVFMMQWGFAMLEGGQVRKKNVNNVMMKNMVDWLIGCVAWLFIGGILCSKGFDLSAFIDWWKQILGTNWPNNGLDLASWFFGLVFCATAATIVSGGVAERIKFSAYVLISLIITGLLYPLFVYLGPWGASIVPWHDYAGSLVVHGLGGFLALGAIAALGPRIGRFVDGRPVPILGHNIPMAVFGAFALAIGWYGFNVGSSLALGDISGLVCATTTMAMAGGGIGALIASRNDVLFTANGIVAGLVAICSGTDVVSPIGGLIIGLIAGLQVPIVYKLVEKAGLDDVCGVVPVHGTAGVIGAILTGILGLKIFGGAGGVSLIDQIIGAVFCIIYGTGLGYILAKIVGIALGGLRVSEEEEKMGLDMAEHKMPAYPEETVI

Function: Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) (By similarity). Transport is electrogenic (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 43786 Sequence Length: 420 Subcellular Location: Cell membrane

Q9US00

MSSVNSIPTATSTVYISVLPATATPSGGSGGNVLHEDLNKFYDYGNTSWILACTPLCLIMVPGVAFFYSGLARRKNTLALIMLSMLGLCVSFFQWYFWGYSLAFSQTGTSGYIGNLRHFAFIRTLADYSPGSNNIPELVFANFQGMFAAITVALFTGAAAERGRIGPMLIITFVWLTVVYCPIACWIWNPNGWAFKFGVYDFAGGGPVEVGSGFAALAYTVCLGRRSKFVEEQFRPHSVLNVVLGTSLLWFGWLGFNGGSAYGSNLRAAMAITNTNLAGAVAGLVWVIYDYIFRTRKWSTIGFCSGVVAGLVAATPCAGFVSPHASLAIGAITGLCCNWAIKLKSHMRIDDAMDIFAIHGVAGFVGTFLNGLFAVDYIAAMDGIYVGENKIRGGWFDHHWRQLGLQMAYICAVGAYDFVVTFIILFITDKIPYLQLRVSPDAEEIGVDADQIGEYAFDYIEERREYKHWKISPAGVPEEIIISNGVAQPTGNVAAPGKILESTNPLELGLTI

Function: Transporter for ammonium to use as a nitrogen source. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 55570 Sequence Length: 512 Subcellular Location: Membrane

Q84KJ6

MSGDAFNMSVAYQPSGMAVPEWLNKGDNAWQMISATLVGMQSVPGLVILYGSIVKKKWAVNSAFMALYAFAAVWLCWVTWGYNMSFGHKLLPFWGKARPALGQSFLLAQAVLPQTTQFYKGGGGADAVVETPWVNPLYPMATMVYFQCVFAAITLILLAGSLLGRMNIKAWMLFVPLWLTFSYTVGAFSLWGGGFLFHWGVMDYSGGYVIHLSSGVAGFTAAYWVGPRSTKDRERFPPNNVLLMLTGAGILWMGWAGFNGGDPYSANIDSSLAVLNTNICAATSLLVWTCLDVIFFKKPSVIGAVQGMITGLVCITPGAGLVQGWAAIVMGILSGSIPWFTMMVVHKRSRLLQQVDDTLGVFHTHAVAGFLGGATTGLFAEPVLCSLFLPVTNSRGAFYPGRGGGLQFVRQVAGALFIICWNVVVTSLVCLAVRAVVPLRMPEEELAIGDDAVHGEEAYALWGDGEKYDSTKHGWYSDNNDTHHNNNKAAPSGVTQNV

Function: Involved in ammonium transport. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 53794 Sequence Length: 498 Subcellular Location: Membrane

O76264

MFKLALTLTLCLAGSLSLAQHNPHWWGNRNTIVHLFEWKWSDIAQECENFLGPRGFAGVQVSPVNENIISAGRPWWERYQPISYKLTTRSGNEEEFGDMVRRCNDVGVRIYVDVLLNHMSGDFDGVAVGTAGTEAEPGKKSFPGVPYSAQDFHPTCEITDWNDRFQVQQCELVGLKDLDQSSDWVRSKPIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYSSLSNLNIDHGFPHNARPFIFQEVIDHGHETVSRDEYKDLGAVTEFRFSEEIGNAFRGNNALKWLQSWGTGWGFLPSGQALTFVDNHDNQRDAGAVLNYKSPKQYKMATAFHLAYPYGISRVMSSFAFDDHDTPPPQDAQERIISPEFDEDGACVNGWICEHRWRQIYAMVGFKNAVRDTEITGWWDNGDNQISFCRGNKGFLAINNNLYDLSQDLNTCLPQGTYCDVISGSLIDGSCTGKSVTVNEHGYGYIHIGSDDFDGVLALHVDAKV

Cofactor: Binds 1 Ca(2+) ion per subunit. Catalytic Activity: Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Sequence Mass (Da): 55420 Sequence Length: 493 Subcellular Location: Secreted EC: 3.2.1.1

Q9ZEU2

MLTPTQQVGLILQYLKTRILDIYTPEQRAGIEKSEDWRQFSRRMDTHFPKLMNELDSVYGNNEALLPMLEMLLAQAWQSYSQRNSSLKDIDIARENNPDWILSNKQVGGVCYVDLFAGDLKGLKDKIPYFQELGLTYLHLMPLFKCPEGKSDGGYAVSSYRDVNPALGTIGDLREVIAALHEAGISAVVDFIFNHTSNEHEWAQRCAAGDPLFDNFYYIFPDRRMPDQYDRTLREIFPDQHPGGFSQLEDGRWVWTTFNSFQWDLNYSNPWVFRAMAGEMLFLANLGVDILRMDAVAFIWKQMGTSCENLPQAHALIRAFNAVMRIAAPAVFFKSEAIVHPDQVVQYIGQDECQIGYNPLQMALLWNTLATREVNLLHQALTYRHNLPEHTAWVNYVRSHDDIGWTFADEDAAYLGISGYDHRQFLNRFFVNRFDGSFARGVPFQYNPSTGDCRVSGTAAALVGLAQDDPHAVDRIKLLYSIALSTGGLPLIYLGDEVGTLNDDDWSQDSNKSDDSRWAHRPRYNEALYAQRNDPSTAAGQIYQGLRHMIAVRQSNPRFDGGRLVTFNTNNKHIIGYIRNNALLAFGNFSEYPQTVTAHTLQAMPFKAHDLIGGKTVSLNQDLTLQPYQVMWLEIA

Function: Catalyzes the synthesis of alpha-glucan from sucrose. Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis, these two sucrose isomers being obtained by glucosyl transfer onto fructose. Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + sucrose = [(1->4)-alpha-D-glucosyl](n+1) + D-fructose Sequence Mass (Da): 72344 Sequence Length: 636 Subcellular Location: Secreted EC: 2.4.1.4

P16266

MPHHEFECSKVIPERKKHAVIKGKGETLADALPQGYLNTIPGSISERGCAYCGAKHVIGTPMKDVIHISHGPVGCTYDTWQTKRYISDNDNFQLKYTYATDVKEKHIVFGAEKLLKQNIIEAFKAFPQIKRMTIYQTCATALIGDDINAIAEEVMEEMPEVDIFVCNSPGFAGPSQSGGHHKINIAWINQKVGTVEPEITGDHVINYVGEYNIQGDQEVMVDYFKRMGIQVLSTFTGNGSYDGLRAMHRAHLNVLECARSAEYICNELRVRYGIPRLDIDGFGFKPLADSLRKIGMFFGIEDRAKAIIDEEVARWKPELDWYKERLMGKKVCLWPGGSKLWHWAHVIEEEMGLKVVSVYIKFGHQGDMEKGIARCGEGTLAIDDPNELEGLEALEMLKPDIILTGKRPGEVAKKVRVPYLNAHAYHNGPYKGFEGWVRFARDIYNAIYSPIHQLSGIDITKDNAPEWGNGFRTRQMLSDGNLSDAVRNSETLRQYTGGYDSVSKLREREYPAFERKVG

Cofactor: Binds 1 [8Fe-7S] cluster per heterodimer. Function: This iron-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Other nitrogenase complexes utilize a molybdenum-iron protein or a vanadium-iron protein. Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate Sequence Mass (Da): 58414 Sequence Length: 518 EC: 1.18.6.1

P16268

MSTASAAAVVKQKVEAPVHPMDARIDELTDYIMKNCLWQFHSRSWDRERQNAEILKKTKELLCGEPVDLSTSHDRCYWVDAVCLADDYREHYPWINSMSKEEIGSLMQGLKDRMDYLTITGSLNEELSDKHY

Function: The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-iron protein. Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate Sequence Mass (Da): 15343 Sequence Length: 132 EC: 1.18.6.1

Q46244

MEDPSKVQLNQLTDYIMKNCLWQFHSRKWDRERQNEGILTKTKQILLGEEVDLSTPADRCYYADALCLADAYKTEYPWINDMSKDELIQLMQQLKDRIDYVTITGSLNAELTDPRY

Function: The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-iron protein. Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate Sequence Mass (Da): 13714 Sequence Length: 116 EC: 1.18.6.1

Q46084

MTCEVKEKGRVGTINPIFTCQPAGAQFVSIGIKDCIGIVHGGQGCVMFVRLIFSQHYKESFELASSSLHEDGAVFGPCGRVEEAVDVLLSRYPDVKVVPIITTCSTEIIGDDVDGVIKKLNEGLLKEKFPDREVHLIAMHTPSFVGSMISGYDVAVRDVVRHFAKREAPNDKINLLTGWVNPGDVKELKHLLGEMDIEANVLFEIESFDSPHSADGSLVSHGNTHHRGSDRHRQCPTFPEPLRRHQGRRVSAEEIRRSRRSSARPRSHPQYRHLPAEPEEGDGKPIPQSLAHERGVAIDALADLTHMFLAEKRVAIYGAPDLVIGLAEF

Cofactor: Binds 1 [8Fe-7S] cluster per heterodimer. Function: This iron-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Other nitrogenase complexes utilize a molybdenum-iron protein or a vanadium-iron protein. Catalytic Activity: 16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate Sequence Mass (Da): 36373 Sequence Length: 329 EC: 1.18.6.1

Q8H0F2

MDQLHVFFFPFLANGHILPTIDMAKLFSSRGVKATLITTHNNSAIFLKAINRSKILGFDISVLTIKFPSAEFGLPEGYETADQARSIDMMDEFFRACILLQEPLEELLKEHRPQALVADLFFYWANDAAAKFGIPRLLFHGSSSFAMIAAESVRRNKPYKNLSSDSDPFVVPDIPDKIILTKSQVPTPDETEENNTHITEMWKNISESENDCYGVIVNSFYELEPDYVDYCKNVLGRRAWHIGPLSLCNNEGEDVAERGKKSDIDAHECLNWLDSKNPDSVVYVCFGSMANFNAAQLHELAMGLEESGQEFIWVVRTCVDEEDESKWFPDGFEKRVQENNKGLIIKGWAPQVLILEHEAVGAFVSHCGWNSTLEGICGGVAMVTWPLFAEQFYNEKLMTDILRTGVSVGSLQWSRVTTSAVVVKRESISKAVRRLMAEEEGVDIRNRAKALKEKAKKAVEGGGSSYSDLSALLVELSSYPHN

Function: Specifically glucosylates the 3'-hydroxy group of delphinidin 3,5-di-O-glucoside to produce gentiodelphin. Shows a strict specificity for UDP-glucose as donor. PTM: The N-terminus is blocked. Catalytic Activity: delphinidin 3,5-bis-O-beta-D-glucoside + UDP-alpha-D-glucose = delphinidin 3,3',5-tri-O-beta-D-glucoside + H(+) + UDP Sequence Mass (Da): 54041 Sequence Length: 482 EC: 2.4.1.238

P01016

DRVYIHPFHLLVYS

Function: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. PTM: In response to low blood pressure, the enzyme renin/REN cleaves angiotensinogen to produce angiotensin-1. Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2. Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3, angiotensin-4. Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2 and can be further processed by ACE to produce angiotensin 1-7, angiotensin 1-5 and angiotensin 1-4. Angiotensin 1-7 has also been proposed to be cleaved from angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin) (By similarity). Sequence Mass (Da): 1759 Sequence Length: 14 Subcellular Location: Secreted

P01019

MRKRAPQSEMAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVANPLSTA

Function: Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. PTM: Beta-decarboxylation of Asp-34 in angiotensin-2, by mononuclear leukocytes produces alanine . The resulting peptide form, angiotensin-A, has the same affinity for the AT1 receptor as angiotensin-2, but a higher affinity for the AT2 receptor . Sequence Mass (Da): 53154 Sequence Length: 485 Subcellular Location: Secreted

Q6W4T2

MSPLIKLAASSRLHDATHYVLCPFAGGGSGAFRHWRTLSLENEVISVMLYPGREFRIDDPTVINIGTLAEEMIQALKTCNQRIEDTIIVGHSMGAQVAYEASKKLVNQGLFLKGLIISGCQAPHIKGRRLLGECDDKTFIHNLVEIGGCDPSLAKSPEWWPIFLPALRADFTATEQYIFTSLPNDKEGLPIPTLLISGDQDREANFSEIEEWKLWCNKVVDHLVVEGGHFYITEQPQMMLECIRALSTETTA

Function: Probable thioesterase. Involved in anguibactin production, but is not essential for virulence or iron transport gene expression. Sequence Mass (Da): 28070 Sequence Length: 252 Pathway: Siderophore biosynthesis; anguibactin biosynthesis. EC: 3.1.2.-

P03880

MRILKSHPLLKIVNSYIIDSPQPANLSYLWNFGSLLALCLGIQIVTGVTLAMHYTPSVSEAFNSVEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGLYYGSYKTPRTLTWAIGTVILIVMMATAFLGYVLPYGQMSLWGATVITNLMSAIPWIGQDIVEFIWGGLYTDEPQCGDVLLKILLNAGKSPILGFAYDLFFIIVLLIGVKIAMTRGKSAGVRSLHTSEASQRLHAGDLTYAYLVGLFEGDGYFSITKKGKYLTYELGIELSIKDVQLIYKIKKILGIGIVSFRKINEIEMVALRIRDKNHLKSFILPIFEKYPMFSNKQYDYLRFRNALLSGIISLEDLPDYTRSDEPLNSIESIINTSYFSAWLVGFIEAEGCFSVYKLNKDDDYLIASFDIAQRDGDILISAIRKYLSFTTKVYLDKTNCSKLKVTSVRSVENIIKFLQNAPVKLLGNKKLQYLLWLKQLRKISRYSEKIKIPSNY

Function: Mitochondrial DNA endonuclease and mRNA maturase involved in intron homing and required for splicing of the cytochrome b (cobA) gene intron, containing its own coding sequence. The protein stimulates the intrinsic ribozyme activity of the intron through binding to and stabilizing specific secondary and tertiary structure elements in the RNA. As an endonuclease it introduces a specific double-strand break at the junction of the two exons the cobA gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with limited specificity and cleaves the sequence 5'-GAGGAGGTTTCTCTGTA-3'. The proteins RNA and DNA recognition and binding surfaces are independent. PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of cobA exon 1 plus intron, containing the I-AniI open reading frame. Cleavage may take place close to Met-213 resulting in an active endonuclease/maturase of about 30 kDa (By similarity). Sequence Mass (Da): 55395 Sequence Length: 488 Subcellular Location: Mitochondrion

Q02219

MKRQALAAMIASLFALAACGGEQAAQAPAETPAASAEAASSAAQATAETPAGELPVIDAVTTHAPEVPPAIDRDYPAKVRVKMETVEKTMKMDDGVEYRYWTFDGDVPGRMIRVREGDTVEVEFSNNPSSTVPHNVDFHAATGQGGGAAATFTAPGRTSTFSFKALQPGLYIYHCAVAPVGMHIANGMYGLILVEPKEGLPKVDKEFYIVQGDFYTKGKKGAQGLQPFDMDKAVAEQPEYVVFNGHVGSIAGDNALKAKAGETVRMYVGNGGPNLVSSFHVIGEIFDKVYVEGGKLINENVQSTIVPAGGSAIVEFKVDIPGSYTLVDHSIFRAFNKGALGQLKVEGAENPEIMTQKLSDTAYAGSGAASAPAASAPAASAPAASASEKSVY

Cofactor: Binds 1 Cu(+) ion. Function: Catalyzes the reduction of nitrite to nitric oxide (NO), probably with azurin as electron donor. Essential for growth and survival in oxygen-depleted environments. Can also provide protection against killing by normal human sera. Catalytic Activity: Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H(+) + nitrite PTM: Palmitoylated. Location Topology: Lipid-anchor Sequence Mass (Da): 40954 Sequence Length: 392 Subcellular Location: Cell outer membrane EC: 1.7.2.1

Q9U6Y9

MNYYVCLHQEGVNSIPKLIEKAFANNYNVVSTSINANMLPFEPHESDPTYPATILSGSDWNSKVIFTMSDVNVDSPNDKLREHAKEVFMRDVAWAEHLQNVGNLMVRLRGPENENLASIVLAKTKDDFPSGNWFIQVPITNPELATFEHRKDATAEEVAEAESNDPWNWWNNLRMVTKHSTKVKVVIELNDADRPSKETVRRWLGEPIEAIIIPSSLFVRNRSNYCVLKKEWQLIVGHFISVRANIIISTNPNDKALCQYADYVNKLINDNCDKHMLNSYENMLEIPLQPLCDNLDTYTYEVFETDPVKYKLYQDAVQAALLDRVSAAEAKTKLTVVMLLGGGRGPLARAVFNAAELTKRKVRLYIIEKNPNAIRTLSNMVKTLWADKDVHIFSKDMRDFSPPELADIMVSELLGSFGDNELSPECLDGALKLLKPDGISIPYKSTSYINPLMSAVLHQNVCQLLPTYPAFDYGYVSLLKNIYHIDEPQALFEFVHPNRAENIDNTRCKTVSFKVNKDCVLHGIGGYFDTHLYKDICLSINPLTHTPGMFSWFPMFFATRPRTLREGQTISIQFWRCVDATKVWYEWQVVNSPDDWEHHNTRGTGYNMRL

Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA) (By similarity). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins SmD1 and SmD3. Required for arginine symmetrical dimethylation of piwi family proteins, piwi, aub and AGO3, during germline development. Required during oogenesis for pole cell formation in the pathway controlled by oskar (osk) and for abdominal segments during early embryogenesis. Involved in nanos (nos) and germ cell mRNAs localization. Sequence Mass (Da): 69741 Sequence Length: 610 Subcellular Location: Cytoplasm EC: 2.1.1.-

O14744

MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL

Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA . Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles . Methylates SUPT5H and may regulate its transcriptional elongation properties . May methylate the N-terminal region of MBD2 . Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development (By similarity). Methylates histone H3 'Arg-8', which may repress transcription (By similarity). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation . Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity . Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9 . Methylates and regulates SRGAP2 which is involved in cell migration and differentiation . Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation . Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner . Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination . Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression . Symmetrically methylates NCL . Methylates p53/TP53; methylation might possibly affect p53/TP53 target gene specificity . Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 (By similarity). Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Sequence Mass (Da): 72684 Sequence Length: 637 Subcellular Location: Cytoplasm EC: 2.1.1.320

Q4R5M3

MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKRESIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLGRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL

Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties (By similarity). May methylate the N-terminal region of MBD2 (By similarity). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development (By similarity). Methylates histone H3 'Arg-8', which may repress transcription (By similarity). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (By similarity). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner. Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression. Symmetrically methylates NCL. Methylates p53/TP53; methylation might possibly affect p53/TP53 target gene specificity (By similarity). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 (By similarity). Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Sequence Mass (Da): 72566 Sequence Length: 637 Subcellular Location: Cytoplasm EC: 2.1.1.320

Q8CIG8

MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIHPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDVIANAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKVQQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKETNVQVLMVLGAGRGPLVNASLRAAKQAERRIRLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPKPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYRDITLSIRPETHSPGMFSWFPIFFPIKQPITVHEGQNICVRFWRCSNSKKVWYEWAVTAPVCSSIHNPTGRSYTIGL

Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA . Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties (By similarity). May methylate the N-terminal region of MBD2 (By similarity). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation (By similarity). Methylates histone H2A and H4 'Arg-3' during germ cell development . Methylates histone H3 'Arg-8', which may repress transcription . Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage . Methylates RPS10 (By similarity). Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity . Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (By similarity). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter . Methylates GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner. Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression. Symmetrically methylates NCL. Methylates p53/TP53; methylation might possibly affect p53/TP53 target gene specificity (By similarity). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 . Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Sequence Mass (Da): 72680 Sequence Length: 637 Subcellular Location: Cytoplasm EC: 2.1.1.320

Q6YXZ7

MPLGQRAGDKSESRYCGVEVLDFPAGEELPAVLSHSLSSSFDFLLAPLVDPDYRPTPGSVLPVAASDLVLGPAQWSSHIVGKISEWIDLDAEDEQLRLDSEITLKQEIAWASHLSLQACVLPPPKRSSCANYARVVNHILQGLTNLQLWLRIPLEKSEPMDEDHDGAKDNSDMSDTVDSWEWWNSFRLLCEHSSQLCVALDVLSTLPSMNSLGRWFGEPVRAAILQTNAFLTNARGYPCLSKRHQKLLTGFFNHSVQVIISGRSNHNVSQGGVLSGDENHTEDTAVRHALSPYLDYIAYIYQRMDPLPEQERFEINYRDFLQSPLQPLMDNLEAQTYETFEKDTVKYTQYQRAIAKALVDRVSDDDVSTTKTVLMVVGAGRGPLVRASLQAAEETGRKLKVYAVEKNPNAVITLHSLIKLEGWESLVTIISSDMRCWEAPEKADILVSELLGSFGDNELSPECLDGAQRFLKPDGISIPSSYTSFIEPITASKLHNDIKAHKDIAHFETAYVVKLHRIARLAPTQSVFTFDHPNPSPNASNQRYTKLKFEIPQETGSCLVHGFAGYFDAVLYKDVHLGIEPNTATPNMFSWFPIFFPLRKPIYVPSKTPIEVHFWRCCGATKVWYEWAVTAPSPSPIHNSNGRSYWVGL

Function: Methylates arginine residues in proteins such as histone H4. Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Sequence Mass (Da): 72673 Sequence Length: 649 Subcellular Location: Cytoplasm EC: 2.1.1.320

Q6NWG4

MSQHATKKRKLDRSTEDYMYFDSYSDVTIHEEMIADTVRTNTYRMGIFKNSKSIEGKVVLDVGAGTGVLSLFCAQAGARKVYAVEASSIADQAVKIVKLNQMEDRIEVIKSTLETIELAEKVDVIVSEWMGYALLHESMLNSVIFARDKWLKPGGLILPSRADLYIAPINDVVVEGRLDFWSTVKGQYGVDMSCMTDFARKCIMNKDITVNPVTVEDVLSHPCKFAELDLNTVTLEQLRDVNGSFSCVCFGSSSIHAFCVWFTVTFPAEEKALVLSTSPFKAETHWKQAVLYLDDAVDVMQDTKVEGEISLYPSEENSRHICIRVDYVIGEQKKHSKSFSIPDQYLEVK

Function: Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53. Repression of TP53 blocks cellular senescence. Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Sequence Mass (Da): 39251 Sequence Length: 349 Subcellular Location: Nucleus EC: 2.1.1.319

Q96LA8

MSQPKKRKLESGGGGEGGEGTEEEDGAEREAALERPRRTKRERDQLYYECYSDVSVHEEMIADRVRTDAYRLGILRNWAALRGKTVLDVGAGTGILSIFCAQAGARRVYAVEASAIWQQAREVVRFNGLEDRVHVLPGPVETVELPEQVDAIVSEWMGYGLLHESMLSSVLHARTKWLKEGGLLLPASAELFIAPISDQMLEWRLGFWSQVKQHYGVDMSCLEGFATRCLMGHSEIVVQGLSGEDVLARPQRFAQLELSRAGLEQELEAGVGGRFRCSCYGSAPMHGFAIWFQVTFPGGESEKPLVLSTSPFHPATHWKQALLYLNEPVQVEQDTDVSGEITLLPSRDNPRRLRVLLRYKVGDQEEKTKDFAMED

Function: Arginine methyltransferase that can catalyze the formation of both omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA . Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates . Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a . H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3) . Acts as a transcriptional repressor of various genes such as HOXA2, THBS1 and TP53 . Repression of TP53 blocks cellular senescence (By similarity). Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to the stimulation of its polymerase activity by enhancing DNA binding and processivity . Methylates HMGA1 . Regulates alternative splicing events. Acts as a transcriptional coactivator of a number of steroid hormone receptors including ESR1, ESR2, PGR and NR3C1. Promotes fasting-induced transcriptional activation of the gluconeogenic program through methylation of the CRTC2 transcription coactivator (By similarity). May play a role in innate immunity against HIV-1 in case of infection by methylating and impairing the function of various HIV-1 proteins such as Tat, Rev and Nucleocapsid protein p7 (NC) . Methylates GPS2, protecting GPS2 from ubiquitination and degradation (By similarity). Methylates SIRT7, inhibiting SIRT7 histone deacetylase activity and promoting mitochondria biogenesis . PTM: Automethylation enhances its stability and antiretroviral activity. Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Sequence Mass (Da): 41938 Sequence Length: 375 Subcellular Location: Nucleus EC: 2.1.1.319

Q2RZV7

MDALLALHRRSRRTVVGLMSGTSLDGVDAALVQLDGSGPDLTMNPEAFVHIPYPTALRDLIRTNTDPASSSVQDVTRLDARLAETYAAAVDRVAAEADVDRGTVDLVGAHGQTVCHLPEPADCAGKDVRATLQLGNPSTLATRLGVPVVGNFRAADLALGGQGAPLVPYFDRVAFTAPDEARGLLNLGGIANLTVLPAGAAPDDVRAFDTGPANMVIDALAARLFDAPHDPDGRHANAGTPDHDLLADLLEGEYFRREPPKSTGRNDFGPDYVDRLLGAAQSRTLSPEDTMATATLLTAASVYQAYAQYVRPEQAIDELIVSGGGVHNDTLLRMLEEAFTPIPVRPTSDYGVAPDAKEALCFAVLAHEAVNGTPTNLPSVTGASARTPLGSLSVPGP

Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Sequence Mass (Da): 41533 Sequence Length: 397 Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. EC: 2.7.1.170

Q07YV2

MSKPEYFIGLMSGTSMDGVDAVLVDFSAEHPVLIASHTEAIPAHLLKGLQRLCQPETDEINRLGRLDRSVGKLFAQAVNHLLAKTTVTAAEVIAIGSHGQTVRHMPNLEMGFTLQIGDPNTIAIETNIDVIADFRRKDIALGGQGAPLVPAFHQQVFAQPGHSRVILNIGGIANITYLPGNSEQVLGFDTGPGNNLIDAFIQQNLNQPFDEDGAWADSGTTHPDLLKQLLSHSYFSLAYPKSTGRELFNRAWLEQQLADYSHLDQQDIQSTLLDLTCHSIANDINKLSPNGELFVCGGGALNKALMQRLATLVPGYKVDTTSALGVDAKWVEGIAFAWLAMRYHHDLPANLPAVTGASRTAILGGRFKAR

Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Sequence Mass (Da): 40075 Sequence Length: 370 Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. EC: 2.7.1.170

Q8EHB5

MNKAYYIGLMSGTSMDGVDAVLVDFAGEQPQLIGTHTETIPTHLLKGLQRLCLPGTDEINRLGRLDRSVGKLFALAVNNLLAKTKIAKDEIIAIGSHGQTVRHMPNLEVGFTLQIGDPNTIATETGIDVIADFRRKDIALGGQGAPLVPAFHQQTFAQVGKKRVILNIGGIANITYLPGNSEEVLGFDTGPGNTLIDAWVQQVKNESYDKNGAWAASGKTDPQLLAQLLSHPYFSLAYPKSTGRELFNQAWLEQQLSAFNQLNEEDIQSTLLDLTCHSIAQDILKLAQEGELFVCGGGAFNAELMQRLAALLPGYRIDTTSALGVDPKWAEGIAFAWLAMRYQLGLPANLPAVTGASREAILGGRFSAK

Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. Catalytic Activity: 1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) + N-acetyl-D-muramate 6-phosphate Sequence Mass (Da): 39810 Sequence Length: 369 Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation. EC: 2.7.1.170

Q7XJR2

MATVGSLKPLHHSSCSSSFPRNPIVNRKALLGFVFDSARKNQIRCENLRYSSESDGKRRNAAAKKRNQSPERCAAEGVLTGGGGSEAIAEVRTMMPERIKVVILTACMMCLCNADRVVMSVAVVPLADKLGWSSSFLGVVQSSFLWGYIFSSVIGGALVDRYGGKRVLAWGVALWSLATLLTPWAAAHSTLALLCVRAFFGLAEGVAMPSMTTLLSRWFPMDERASAVGISMAGFHMGNVVGLLLTPLMLSSIGISGPFILFASLGLLWVSTWSSGVTNNPQDSPFITRSELRLIQAGKPVQPSTISPKPNPSLRLLLSKLPTWAIIFANVTNNWGYFVLLSWMPVYFQTVFNVNLKQAAWFSALPWATMAISGYYAGAASDFLIRTGHSVTSVRKIMQSIGFMGPGLSLLCLNFAKSPSCAAVFMTIALSLSSFSQAGFLLNMQDIAPQYAGFLHGISNCAGTLAAIVSTIGTGYFVQWLGSFQAFLTVTAFLYFATTVFWLLFATGERVF

Function: Inorganic phosphate and probable anion transporter. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 55307 Sequence Length: 512 Subcellular Location: Plastid

Q66GI9

MCYSLSIQSSIDFHNRNALKIHGDRAILTSNLPTLRRIPFLPERDRRRKLVLCTGRVVNSLKFTGNTSVDLCGIPRHRLRVSCSDARRTPEETAAELTAQPNFSEFITSERVKVVAMLALALALCNADRVVMSVAIVPLSLSRGWSKSFSGIVQSSFLWGYLISPIAGGTLVDRYGGKVVMAWGVALWSLATFLTPWAADSSLWALLAARAMVGVAEGVALPCMNNMVARWFPPTERSRAVGIAMAGFQLGNVVGLMLSPILMSQGGIYGPFVIFGLSGFLWLLVWLSATSSAPDRHPQITKSELEYIKQKKQISTMENKRISTSGIPPFGRLLSKMPTWAVIVANSMHSWGFFVILSWMPIYFNSVYHVNLKQAAWFSAVPWSMMAFTGYIAGFWSDLLIRRGTSITLTRKIMQSIGFIGPGIALIGLTTAKQPLVASAWLSLAVGLKSFSHLGFLINLQEIAPEYSGVLHGMCLTAGTLAAIVGTVGAGFFVELLGSFQGFILLTAILYLLSALFYNIYATGERVDFDTTA

Function: Inorganic phosphate and probable anion transporter. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 58243 Sequence Length: 533 Subcellular Location: Plastid

Q9FKV1

MKLSNIPQRYVIVFLTFLSTCVCYIERVGFSIAYTVAADAAGINQSSKGTILSTFFVGYACSQVPGGWAAQKIGGRKVLLLSFVLWSSTCFLVPLDPNRVGLLVVARLLVGVAQGFIFPSIHTVLAQWVPPHERSRLVSITTSGMYLGAALGMWLLPALVELRGPESVFLAEALAGVIWSLLWIRYATDPPRSEHPKAAAAGFGGALLPTNVNHHKVTHIPWKKIMLSLPVWAIVVNNFTFHYALYVLMNWLPTYFELGLQISLQGMDSSKMVPYLNMFVFSIVGGFIADYLITKRILSVTRTRKFLNTVGFLIASAALMVLPMFRTENGVILCSSVALGFLALGRAGFAVNHMDIAPRYAGIVMGVSNTAGTLAGIIGVDLTGKLLEASKLVYSDLSHPESWRVVFFIPGLLCIFSSVVFLLFSTGERIFD

Function: Inorganic phosphate and probable anion transporter. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 47166 Sequence Length: 432 Subcellular Location: Golgi apparatus membrane

Q3E9A0

MARLTLRPHNHFFSSPIYAHKQPFLSVYTIFPHHHQNPLIKSRVKCSASGTERVRESKKLPPKDPIEDPKPQLPIPEVLSTETGFEQNWPPWKNIPQRYKLIGATSLAFVICNMDKVNLSIAIIPMSHQFGWSSSVAGLVQSSFFWGYALSQLPGGWLSKIFGGRKVLEIGVFTWSFATALVPLLAGFMPGLIFSRILVGIGEGVSPSAATDLIARTIPVKERSRAVGFVFGGLSLGSVMGLLLAPPIIETFNWESVFYLFGLLGVGWFVGFQFLNEEEVSYKGNEISTSHKSENATKEELGSSLKEIPWKSFFQSPAVWAMIYTHFCGSWGHYTCLSWLPTYFSEALSLNLTEAAWVSILPPLASIVVTSLASQFADYLITNGVDTTTVRKICQTIAFVAPAICMTLSSVDIGLPPWEIVGILTAGLALSSFALSGLYCTHQDISPEYASILLGITNTVGAVPGIVGVALTGFLLDSTHSWTMSLFVPSIFFYLTGTVVWLAFASSEPQTFRKEDS

Function: Inorganic phosphate and probable anion transporter. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 56683 Sequence Length: 517 Subcellular Location: Plastid

D4GSY7

MTTERPDAGDSGSEKPDETAAPDPAANGARRSKTRLAARSLGHGFGDGAVLEDISLAVEPGEILAVVGPSGTGKTTLFRLLAMFERPDEGTVEVGGDDVWDLPEARRLAVRRRVGMAFQTRSLFSTTVEENVSYGLRVRRSWSARVRDAVEGLFGRDEPSETVRDALRTVGMFDKVGRDAGSLSAGEAQRVAIARALAPDPDVLLLDEPTSNLDPRNTAAIESAMRAARDRGIAVALATHDMQQARRVSDRTAVILGGTCIESGPTDAVFESPDDDRVRQFVEGKLVY

Function: Part of an ABC transporter complex involved in anions import (Probable). Responsible for energy coupling to the transport system (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 30906 Sequence Length: 288 Subcellular Location: Cell membrane EC: 7.3.2.-

D4GSY8

MFALGDLNLTYLVSITAVSLYVSTAAVALSAALGLPISLAVGFRDFYGKSVVTSVISTGMGFPSVVVGLVVLLVLSRSGPLGTFELLFTPEAMILSQTILALPVLVSVSLSAVQSVPQDLRDAAFAAGGTSTDIALLVVREARYGIVTALLAAYGRAISEVGSVLIVGGNIVFSDSTSFTRTLTTAITVEARKGNIETGIALGAILLALVLGVNALGARFRDRTPGRNGRGR

Function: Part of an ABC transporter complex involved in anions import (Probable). Responsible for the translocation of the substrate across the membrane (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 23860 Sequence Length: 232 Subcellular Location: Cell membrane

W6QY25

MSAPKGPITKFPAEGLRHARRFITTHNKEGKGVFAVDDDGDHHRIMVDGLAVANIIYSTSGNPVDMNDDNDLVYARDNEVRRFAGQINLFV

Function: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of annullatin D, an alkylated aromatic polyketide with a fused dihydrobenzofuran lactone ring system that exhibits potent agonistic activities toward the cannabinoid receptors . The annullatin backbone 2-hydroxymethyl-3-pentylphenol is assembled from one acetyl-CoA starter unit and 5 malonyl-CoA elongation units by cooperation of the highly reducing polyketide synthase anuA, the short-chain dehydrogenase anuB and the oxidoreductase anuC, before being hydroxylated at the C-5 alkyl chain by the cytochrome P450 monooxygenase anuE to form (8S)-annullatin E. The prenyltransferase anuH subsequently installs one isoprenyl group at the benzene ring to form (8S)-annullatin J. Enzymatic or nonenzymatic dihydro-benzofuran ring formation between the prenyl and the phenolic hydroxyl groups in (8S)-annullatin J results in two diastereomers (2S,9S)-annullatin H and compound 12. The intermediate (2S,9S)-annullatin H is then converted to (2S,9S)-annullatin D by the FAD-linked oxidoreductase anuG-catalyzed five-member lactone ring formation. The isomer 12 acts as a substrate for the short-chain dehydrogenase anuF and is oxidized to (2R)-annullatin F, which is subsequently acetylated by an acetyltransferase leading to (2R)-annullatin G formation. The remaining enzymes identified within the cluster, anuD, anuI and anuJ, seem not to be involved in annullatin biosynthesis (Probable). Sequence Mass (Da): 10097 Sequence Length: 91 Pathway: Secondary metabolite biosynthesis. EC: 1.-.-.-

Q16853

MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLVYEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQAPKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFHPSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVWAEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSADSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN

Cofactor: Binds 1 copper ion per subunit. Function: Cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has semicarbazide-sensitive (SSAO) monoamine oxidase activity. May play a role in adipogenesis. Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+) PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 84622 Sequence Length: 763 Subcellular Location: Cell membrane EC: 1.4.3.21

O08590

MTQKTTLVLLALAVITIFALVCVLLAGRSGDGGRLSQPLHCPSVLPSVQPQTHPGQSQPFADLSPEELTAVMSFLIKHLGPGLVDAAQARPSDNCVFSVELQLPAKAAALAHLDRGGPPPVREALAIIFFGGQPKPNVSELVVGPLPHPSYMRDVTVERHGGPLPYYRRPVLTREYQDIQEMIFHRELPQASGLLHHCCFYKRQGHNLLKMTTAPRGLQSGDRATWFGIYYNLSGAGFYPHPIGLELLVDHKALDPALWTIQKVFYQGRYYESLTQLEDMFEAGLVNVVLVPDNGTGGSWSLKSSVPPGRAPPLQFHPEGPRFSVQGSQVRSSLWAFSFGLGAFSGPRIFDIRFQGERVAYEISVQEAIALYGGNSPASMSTCYMDGSFGIGKYSTPLTRGVDCPYLATYVDWHFLLESQTPKTLRDAFCVFEQNQGLPLRRHHSDFYSHYFGGVVETVLVVRSVATLLNYDYVWDMVFHSNGAIEVKFHATGYITSAFFFGAGEKFGNRVAEHTLGTVHTHNAHFKVDLDVAGLKNWAWAEDLAFVPMNVPWQPEFQMQRLQVTRKLLETEEEAAFPLGNATPRYLYLASNHSNKWGHRRGYRIQILSFAGKPLPQESPIEKAFTWGRYHLAVTQRKEEEPSSSSIYNQNDPWTPTVDFTDFISNETIAGEDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSPDSIYFRKDQDVTDCEVNSLACLSQTANCVPDLPAFSHGGFTYK

Cofactor: Binds 1 copper ion per subunit. Function: Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis (By similarity). Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+) PTM: N- and O-glycosylated. Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 84981 Sequence Length: 763 Subcellular Location: Membrane EC: 1.4.3.21

Q93ZC5

MIMASSAAASISMITLRNLSRNHQSHQSTFLGFSRSFHNQRISSNSPGLSTRARSTTSSTGGFFRTICSSSSNDYSRPTKIQELNVYEFNEGDRNSPAVLKLGKKPDQLCLGDLVPFTNKLYTGDLTKRIGITAGLCVLIQHVPEKKGDRFEASYSFYFGDYGHISVQGPYLTYEDTFLAITGGSGVFEGAYGQVKLRQLVYPTKLFYTFYLKGVAADLPVELTGKHVEPSKEVKPAAEAQATQPGATIANFTN

Function: Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid. Catalytic Activity: (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate = (9S,13S,15Z)-12-oxophyto-10-15-dienoate Sequence Mass (Da): 27809 Sequence Length: 254 Subcellular Location: Plastid EC: 5.3.99.6

Q29437

MFIFIFLSLWTLLVMGREEGGVGSEEGVGKQCHPSLPPRCPSRSPSDQPWTHPDQSQLFADLSREELTTVMSFLTQQLGPDLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGGQPQPNVTELVVGPLPQPSYMRDVTVERHGGPLPYYRRPVLLREYLDIDQMIFNRELPQAAGVLHHCCSYKQGGQKLLTMNSAPRGVQSGDRSTWFGIYYNITKGGPYLHPVGLELLVDHKALDPADWTVQKVFFQGRYYENLAQLEEQFEAGQVNVVVIPDDGTGGFWSLKSQVPPGPTPPLQFHPQGPRFSVQGNRVASSLWTFSFGLGAFSGPRVFDVRFQGERLAYEISLQEAGAVYGGNTPAAMLTRYMDSGFGMGYFATPLIRGVDCPYLATYMDWHFVVESQTPKTLHDAFCVFEQNKGLPLRRHHSDFLSHYFGGVAQTVLVFRSVSTMLNYDYVWDMVFYPNGAIEVKLHATGYISSAFLFGAARRYGNQVGEHTLGPVHTHSAHYKVDLDVGGLENWVWAEDMAFVPTAIPWSPEHQIQRLQVTRKQLETEEQAAFPLGGASPRYLYLASKQSNKWGHPRGYRIQTVSFAGGPMPQNSPMERAFSWGRYQLAITQRKETEPSSSSVFNQNDPWTPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDQEPSMDSADSIYFREGQDAGSCEINPLACLPQAATCAPDLPVFSHGGYPEY

Cofactor: Binds 1 copper ion per subunit. PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+) Sequence Mass (Da): 84757 Sequence Length: 762 Subcellular Location: Secreted EC: 1.4.3.21

A2XID3

MAAAAPSRVSVRAAAPGQTGGFAKIRPQVVVAAAARSAGVSGRRARSVRASLFSPKPATPKDARPAKVQEMFVYEINERDRESPAYLRLSAKQTENALGDLVPFTNKLYSGSLDKRLGISAGICILIQHVPERNGDRYEAIYSFYFGDYGHISVQGPYLTYEESYLAVTGGSGVFEGAYGQVKLNQIVFPFKIFYTFYLKGIPDLPRELLCTPVPPSPTVEPTPAAKATEPHACLNNFTN

Function: Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid (JA). Required for the production of JA in response to wounding. Necessary for flower and coleoptile development regulation by light, including blue (BL), red (RL) and far red (FR) lights. Involved in the auxin-mediated signaling pathway leading to growth stimulation. Essential for photodestruction of phyA upon activation by RL and FR. Implicated in responses to salt stress (NaCl). Catalytic Activity: (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate = (9S,13S,15Z)-12-oxophyto-10-15-dienoate Sequence Mass (Da): 26051 Sequence Length: 240 Pathway: Lipid metabolism; polyunsaturated fatty acid biosynthesis. Subcellular Location: Plastid EC: 5.3.99.6

P58027

MASREKTSIEGHMFDVVVIGGGISGLSAAKLLAEHEVDVLVLEARDRVGGRTYTVRNEHVDYVDVGGAYVGPTQNRILRLSKELGLETYKVNVNERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTMDNMGKEIPADAPWEAPHAEEWDKMTMKDLIDKICWTKTARRFASLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMERLGDRVKLKRPVTYVDQSDDNIIIETLNHELYECKYVISAIPPTLTAKIHFRPELPSERNQLIQRLPMGAIIKCMMYYKEAFWKKKDYCGCMIIEDEEAPISITLDDTKPDGSLPAIMGFILARKADRLAKLHKEIRKRKICELYAKVLGSQEALQPVHYEEKNWCEEQYSGGCYTAYFPPGIMTHYGRVIRQPFGRIYFAGTETATHWSGYMEGAVEAGERTAREVLNALGRVAEKDLKTQEPESKDVPAMEITHTFWERNLPSVTGLLKLIGFTTSVTALWIVAYKFRLLRRS

Function: Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially oxidizes serotonin. Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline. Catalytic Activity: a secondary aliphatic amine + H2O + O2 = a primary amine + an aldehyde + H2O2 Location Topology: Single-pass type IV membrane protein Sequence Mass (Da): 60088 Sequence Length: 527 Subcellular Location: Mitochondrion outer membrane EC: 1.4.3.21

P21397

MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKDVPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS

Function: Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues . Preferentially oxidizes serotonin . Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline (By similarity). Catalytic Activity: a secondary aliphatic amine + H2O + O2 = a primary amine + an aldehyde + H2O2 Location Topology: Single-pass type IV membrane protein Sequence Mass (Da): 59682 Sequence Length: 527 Subcellular Location: Mitochondrion outer membrane EC: 1.4.3.21

P21396

MTDLEKPNLAGHMFDVGLIGGGISGLAAAKLLSEYKINVLVLEARDRVGGRTYTVRNEHVKWVDVGGAYVGPTQNRILRLSKELGIETYKVNVNERLVQYVKGKTYPFRGAFPPVWNPLAYLDYNNLWRTMDEMGKEIPVDAPWQARHAQEWDKMTMKDLIDKICWTKTAREFAYLFVNINVTSEPHEVSALWFLWYVRQCGGTARIFSVTNGGQERKFVGGSGQVSEQIMGLLGDKVKLSSPVTYIDQTDDNIIVETLNHEHYECKYVISAIPPILTAKIHFKPELPPERNQLIQRLPMGAVIKCMVYYKEAFWKKKDYCGCMIIEDEEAPIAITLDDTKPDGSLPAIMGFILARKADRQAKLHKDIRKRKICELYAKVLGSQEALYPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIYFAGTETATQWSGYMEGAVEAGERAAREVLNALGKVAKKDIWVEEPESKDVPAIEITHTFLERNLPSVPGLLKITGVSTSVALLCFVLYKIKKLPC

Function: Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues . Preferentially oxidizes serotonin . Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline . Catalytic Activity: a secondary aliphatic amine + H2O + O2 = a primary amine + an aldehyde + H2O2 Location Topology: Single-pass type IV membrane protein Sequence Mass (Da): 59508 Sequence Length: 526 Subcellular Location: Mitochondrion outer membrane EC: 1.4.3.21

Q8LPL6

MTGMRGLSVFISDVRNCQNKEAERLRVDKELGNIRTCFKNEKVLTPYKKKKYVWKMLYIHMLGYDVDFGHMEAVSLISAPKYPEKQVGYIVTSCLLNENHDFLKLAINTVRNDIIGRNETFQCLALTLVGNIGGRDFAESLAPDVQKLLISSSCRPLVRKKAALCLLRLFRKNPDAVNVDGWADRMAQLLDERDLGVLTSSTSLLVALVSNNHEAYSSCLPKCVKILERLARNQDVPQEYTYYGIPSPWLQVKAMRALQYFPTIEDPSTRKALFEVLQRILMGTDVVKNVNKNNASHAVLFEALSLVMHLDAEKEMMSQCVALLGKFISVREPNIRYLGLENMTRMLMVTDVQDIIKKHQSQIITSLKDPDISIRRRALDLLYGMCDVSNAKDIVEELLQYLSTAEFSMREELSLKAAILAEKFAPDLSWYVDVILQLIDKAGDFVSDDIWFRVVQFVTNNEDLQPYAASKAREYLDKIAIHETMVKVSAYILGEYGHLLARQPGCSASELFSILHEKLPTISTPTIPILLSTYAKLLMHAQPPDPELQKKVWAVFKKYESCIDVEIQQRAVEYFELSKKGPAFMDVLAEMPKFPERQSSLIKKAENVEDTADQSAIKLRAQQQPSNAMVLADQQPVNGAPPPLKVPILSGSTDPESVARSLSHPNGTLSNIDPQTPSPDLLSDLLGPLAIEAPPGAVSNEQHGPVGAEGVPDEVDGSAIVPVEEQTNTVELIGNIAERFHALCLKDSGVLYEDPHIQIGIKAEWRGHHGRLVLFMGNKNTSPLTSVQALILPPAHLRLDLSPVPDTIPPRAQVQSPLEVMNIRPSRDVAVLDFSYKFGANVVSAKLRIPATLNKFLQPLQLTSEEFFPQWRAISGPPLKLQEVVRGVRPLALPEMANLFNSFHVTICPGLDPNPNNLVASTTFYSESTGAILCLARIETDPADRTQLRMTVGTGDPTLTFELKEFIKEQLITVPMGSRALVPAAGPAPPVAQPPSPAALADDPGAMLAGLL

Function: Subunit of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The complex binds polyphosphoinositides (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 112150 Sequence Length: 1012 Subcellular Location: Membrane

O95782

MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCVSLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHYDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIDTVINALKTERDVSVRQRAADLLYAMCDRSNAKQIVSEMLRYLETADYAIREEIVLKVAILAEKYAVDYSWYVDTILNLIRIAGDYVSEEVWYRVLQIVTNRDDVQGYAAKTVFEALQAPACHENMVKVGGYILGEFGNLIAGDPRSSPPVQFSLLHSKFHLCSVATRALLLSTYIKFINLFPETKATIQGVLRAGSQLRNADVELQQRAVEYLTLSSVASTDVLATVLEEMPPFPERESSILAKLKRKKGPGAGSALDDGRRDPSSNDINGGMEPTPSTVSTPSPSADLLGLRAAPPPAAPPASAGAGNLLVDVFDGPAAQPSLGPTPEEAFLSELEPPAPESPMALLADPAPAADPGPEDIGPPIPEADELLNKFVCKNNGVLFENQLLQIGVKSEFRQNLGRMYLFYGNKTSVQFQNFSPTVVHPGDLQTQLAVQTKRVAAQVDGGAQVQQVLNIECLRDFLTPPLLSVRFRYGGAPQALTLKLPVTINKFFQPTEMAAQDFFQRWKQLSLPQQEAQKIFKANHPMDAEVTKAKLLGFGSALLDNVDPNPENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEPVSRHLCELLAQQF

Function: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 . The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 107546 Sequence Length: 977 Subcellular Location: Cell membrane

P17426

MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCISLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHYDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIDTVINALKTERDVSVRQRAADLLYAMCDRSNAKQIVSEMLRYLETADYAIREEIVLKVAILAEKYAVDYSWYVDTILNLIRIAGDYVSEEVWYRVLQIVTNRDDVQGYAAKTVFEALQAPACHENMVKVGGYILGEFGNLIAGDPRSSPPVQFSLLHSKFHLCSVATRALLLSTYIKFINLFPETKATIQGVLRAGSQLRNADVELQQRAVEYLTLSSVASTDVLATVLEEMPPFPERESSILAKLKRKKGPGAASALDDSRRDTSSNDINGGVEPTPSTVSTPSPSADLLGLRAAPPPAAPPAPVGGNLLVDVFSDGPTAQPSLGPTPEEAFLSELEPPAPESPMALLADPAPAADPGPEDIGPPIPEADELLNKFVCKNSGVLFENQLLQIGVKSEFRQNLGRMYLFYGNKTSVQFQNFLPTVVHPGDLQTQLAVQTKRVAAQVDGGAQVQQVLNIECLRDFLTPPLLSVRFRYGGTAQSLTLKLPVTINKFFQPTEMAAQDFFQRWKQLSLPLQEAQKIFKANHPMDAEVTKAKLLGFGSALLDNVDPNPENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEPVSRHLCELLAQQF

Function: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 . The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 107664 Sequence Length: 977 Subcellular Location: Cell membrane

Q8LPK4

MTGMRGLSVFISDVRNCQNKEAERLRVDKELGNIRTCFKNEKVLTPYKKKKYVWKMLYIHMLGYDVDFGHMEAVSLISAPKYPEKQVGYIVTSCLLNENHDFLKLAINTVRNDIIGRNETFQCLALTLVGNIGGRDFAESLAPDVQKLLISSSCRPLVRKKAALCLLRLFRKNPDAVNVDGWADRMAQLLDERDLGVLTSSTSLLVALVSNNHEAYSSCLPKCVKILERLARNQDVPQEYTYYGIPSPWLQVKAMRALQYFPTIEDPSTRKALFEVLQRILMGTDVVKNVNKNNASHAVLFEALSLVMHLDAEKEMMSQCVALLGKFISVREPNIRYLGLENMTRMLMVTDVQDIIKKHQSQIITSLKDPDISIRRRALDLLYGMCDVSNAKDIVEELLQYLSTAEFSMREELSLKAAILAEKFAPDLSWYVDVILQLIDKAGDFVSDDIWFRVVQFVTNNEDLQPYAASKAREYMDKIAIHETMVKVSAYILGEYGHLLARQPGCSASELFSILHEKLPTVSTPTIPILLSTYAKLLMHAQPPDPELQKKVWAVFKKYESCIDVEIQQRAVEYFELSKKGPAFMDVLAEMPKFPERQSSLIKKAENVEDTADQSAIKLRAQQQPSNAIVLADPQPVNGAPPPLKVPILSGSTDPESVARSLSHPNGTLSNIDPQTPSPDLLSDLLGPLAIEAPPGAVSYEQHGPVGAEGVPDEIDGSAIVPVEEQTNTVELIGNIAERFHALCLKDSGVLYEDPHIQIGIKAEWRGHHGRLVLFMGNKNTSPLTSVQALILPPAHLRLDLSPVPDTIPPRAQVQSPLEVMNIRPSRDVAVLDFSYKFGTNVVSAKLRIPATLNKFLQPLQLTSEEFFPQWRAISGPPLKLQEVVRGVRPLALPEMANLFNSFHVTICPGLDPNPNNLVASTTFYSETTGAMLCLARIETDPADRTQLRLTVGSGDPTLTFELKEFIKEQLITIPMGSRALVPAAGPAPSPAVQPPSPAALADDPGAMLAGLL

Function: Subunit of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The complex binds polyphosphoinositides. Location Topology: Peripheral membrane protein Sequence Mass (Da): 112299 Sequence Length: 1013 Subcellular Location: Membrane

Q0VCK5

MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLHRASPDLVPVGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLEAILNKAQEPPKSKKVQHSNAKNAVLFEAISLVTHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSIREEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAAKTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLTQFHLLHSKFHLCSVPTRALLLSTYIKFVNLFPEVKGTIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLEEMPPFPERESSILAKLKKKKGPSTVTDLEEAKRERSADVNGGPEPALASTSAVSTPSPSADLLGLGAAPPVPAGPPPSSGGLLVDVFSDSPSAAAPLAPGSEDNFARFVCKNNGVLFENQLLQIGLKSEFRQNLGRMFIFYGNKTSTQFLNFTPTLICSDDLQANLSLQTKPVDPTVDGGAQVQQAVNIECVSDFTEAPVLNIQFRYGGTFQNVSVKLPITLNKFFQPTEMASQDFFQRWKQLSNPQQEVQSIFKAKHPMDTEVTKAKIIGFGSALLEEVDPNPANFVGAGIIHTRTAQIGCLLRLEPNLQAQMYRLTLRTSRETVSQRLCELLSEQF

Function: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (By similarity). The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 103769 Sequence Length: 938 Subcellular Location: Cell membrane

Q86KI1

MSMNVTNPNIAKTSMRGLTNFISDLRNSPSKENEEKRVTKEMAHIRKEFKENKNIDGYQRRKYVCKLVYMYMLGYELDFGHMEAVTLLSSTKFSEKQIGYIALGILLNEQHEMLPLIINSFKEDLLARSDYFQSLALAAICNIGGKEVAEFLSPLIQKLLIANTSSPMVKKRCALAILRMNRKHIGLVTPDSWVERLVSVLDEPDFGVLTSLMSLLIELASENPIGWEPAIPKVIHLLKKIIINKEFPKEYVYYHVTCPWLQVKLLKFLRYFPAPDDSQGGKVLGEILTAVFAQSESAKAGTVNHKNSLNAVLFEAINLIIHLDNDPVLLKQTSLLLGRFITVKETNIRYLGLEAMSHFASLSNETSIMIKKYQDTVLLSLKDSDISIRRRALDLLYGMCDKNTCKHIVAELLSYLQTADYAIREELVIKIANLAEKFASNYSWYVDVILQLITTAGDFVSDDIWFRVVKIVTNHEDIQAYAASTVFNALQSRNCHETLIKVGGYILGEFGHLIADNPQSSPLVQFNILHSKFNTCGAPTKALLLSTYAKFVNLFPELTQQTQEVFKQHQSYIDAEIQQRACEYLNLTSLNEDLMQTVLDVIPAFIDAKDNSNTTSNTANNSNMINSQDSKISSGGFNQSPQPSQQQQQQQPPQQQQAQLQQNVSSNGLDLLDPFGLGLGNQQQQQQQPVQQAQPVYQQQQQAESFSPVQSDTVSSFGQQQQQQQGGFSSPTIQASSSPISSGGSDPMQIKILASYKRLCLVSEGVLYEDSMLQVGLKSEYQSGQGRLMLYYGNSSAFPLTNFNVTLNSIAGLTLQPQSIAPVIQPKAQLQQPVTFSCTSEFTESPVITINFLTPGKPITITLRLPIVISKFFEPLRLSSGDFFARWKTISGKPLEIQEIFKSTKPIDIQSYNRVIQEGLNITVLKQVDPNPNNIVASCLFPFGSNGQPINSYIRIETNPQANMCRLTIRSQSATLTNTIKNLLISHLQ

Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 110700 Sequence Length: 989 Subcellular Location: Cell membrane

P17427

MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSPDLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPDPAVRGRLTECLETILNKAQEPPKSKKVQHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSIREEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAAKTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRALLLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLEEMPPFPERESSILAKLKKKKGPSTVTDLEETKRERSIDVNGGPEPVPASTSAASTPSPSADLLGLGAVPPAPTGPPPSSGGGLLVDVFSDSASAVAPLAPGSEDNFARFVCKNNGVLFENQLLQIGLKSEFRQNLGRMFIFYGNKTSTQFLNFTPTLICADDLQTNLNLQTKPVDPTVDGGAQVQQVVNIECISDFTEAPVLNIQFRYGGTFQNVSVKLPITLNKFFQPTEMASQDFFQRWKQLSNPQQEVQNIFKAKHPMDTEITKAKIIGFGSALLEEVDPNPANFVGAGIIHTKTTQIGCLLRLEPNLQAQMYRLTLRTSKDTVSQRLCELLSEQF

Function: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 . The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. Location Topology: Peripheral membrane protein Sequence Mass (Da): 104017 Sequence Length: 938 Subcellular Location: Cell membrane

P91926

MAPVRGDGMRGLAVFISDIRNCKSKEAEVKRINKELANIRSKFKGDKTLDGYQKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYSEKQIGYLFISVLVNTNSDLIRLIIQSIKNDLQSRNPVHVNLALQCIANIGSRDMAESFSNEIPKLLVSGDTMDVVKQSAALCLLRLFRSSPDIIPGGEWTSRIIHLLNDQHMGVVTAATSLIDALVKRNPDEYKGCVNLAVSRLSRIVTASYTDLQDYTYYFVPAPWLSVKLLRLLQNYNPVTEEAGVRARLNETLETILNKAQEPPKSKKVQHSNAKNAVLFEAINLIIHSDSEPNLLVRACNQLGQFLSNRETNLRYLALESMCHLATSEFSHEEVKKHQEVVILSMKMEKDVSVRQMAVDLLYAMCDRGNAEEIVQEMLNYLETADYSIREEMVLKVAILAEKYATDYTWYVDVILNLIRIAGDYVSEEVWYRVIQIVINREEVQGYAAKTVFEALQAPACHENMVKVGGYILGEFGNLIAGDSRSAPLVQFKLLHSKYHLCSPMTRALLLSTYIKFINLFPEIRTNIQDVFRQHSNLRSADAELQQRASEYLQLSIVASTDVLATVLEEMPSFPERESSILAVLKKKKPGRVPENEIRESKSPAPLTSAAQNNALVNNSHSKLNNSNANTDLLGLSTPPSNNIGSGSNSNSTLIDVLGDMYGSNSNNNSSAVYNTKKFLFKNNGVLFENEMLQIGVKSEFRQNLGRLGLFYGNKTQVPLTNFNPVLQWSAEDALKLNVQMKVVEPTLEAGAQIQQLLTAECIEDYADAPTIEISFRYNGTQQKFSIKLPLSVNKFFEPTEMNAESFFARWKNLSGEQQRSQKVFKAAQPLDLPGARNKLMGFGMQLLDQVDPNPDNMVCAGIIHTQSQQVGCLMRLEPNKQAQMFRLTVRASKETVTREICDLLTDQF

Function: Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. AP-2alpha is a subunit of the plasma membrane adapter. Location Topology: Peripheral membrane protein Sequence Mass (Da): 105620 Sequence Length: 940 Subcellular Location: Cell membrane

Q8D3I0

MSHYLIGDIHGCYSEFKSMLDLINFNLKNDIIWIAGDFIGRGPDSLKVLRLIYKLKRNIFVVLGNHEINLLLLYAKIKKIKEEDKLTEILNAPDLKILISWLRKQPLLKIDKQKKIIMIHAGIIPKWDMSDLITNSKKVECELKSKNYKKFLKFMYIKNNEHKNIWKNNLPEIIKMRLTLNIITRIRYCISETEIDLLHKEHPEKSPNHLIPWFKFKNNITKNYSIVFGHWSSIKDYKTPKNIYGLDTGCCWKGELTALKWDNKLFFKIKSK

Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Sequence Mass (Da): 32246 Sequence Length: 272 EC: 3.6.1.41

Q3BX84

MSVWAIGDLQGCYDITQRLLEKINFDPAQDTLWFCGDLVNRGGQSLETLRLVHSLRAHSVVVLGNHDLSLLAIGARSEEEQRKVNPDLLRIVMAEDRDALLDWLRMQKLAHVDRTLGWMMIHAGLAPKWTTQMAEKHAREVEQQLQGGGYRKLLRNMYGDQPGWSPGLSGYDRSRAIINLFTRMRYCTPRGRIATDDKGTPGTQAQGLYPWFEVPGRVERDLKIVCGHWSALGLTITQGVHAIDTGAVWGGKLTALQLDSEELRVVQVPGREVTGPAPVARAPRRPRERQGRQRSRGNRGNAGNAAAGPKPSVDTPQD

Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Sequence Mass (Da): 35377 Sequence Length: 318 EC: 3.6.1.41

Q8PCE5

MSVWAIGDLQGCYDITQQLLEKIRFDPAQDTLWFCGDLVNRGGQSLETLRLVHSLRAHSVVVLGNHDLSLLAIGARSEEEQRKVNPDLQRIVLAEDRDVLLDWLRMQKLAHVDRELGWMMIHAGLAPKWTTQMAEKHAREVEQQLQGGGYRKLLRNMYGDQPGWSPGLSGYDRSRAIINLFTRMRYCTPRGRIATDDKGTPGTQAQGLYPWFEVPGRVERDLKIVCGHWSALGLTITQGVHAIDTGAVWGGKLTALQLDTDELRVVQVPGREVTAPATAPRAPRRPRERQGRQRARGGRGGGNGNGNGGNAAAPAAAPGDAPQE

Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+) Sequence Mass (Da): 35713 Sequence Length: 324 EC: 3.6.1.41

Q66KI8

MGIPCFYSSLISCLFSIITLVDVGQSSALTLSDSRLHPQSLEKSPWREFQCQHMLKHLHNGARVTVQMPPNIEGHWVSMGCEVRSGPEFITRSYRFYNNNTFKAYQHYYGNNHCTIPTYTLVIRGKIRLRQASWIIRGGTEADYQLHNVQIIPHSETVAEKLTWLVNHTCAGFVPGDMPWEPGISYDLWREEGGFKCTKALNFAMHELQLIRVEKQYMHHNLDHLVEELFLGDIHTDPSQRMYYRPSSYQPPLQNAKNHNQNCVACRIILRSDEHHPPILPAKADLPVGLNGEWVSQRCEVRPEVLFLTRHFIFNDNNHTWEGFYYHYSDPICKHPSFTIYAKGRYSRGVYSSKVMGGTEFVFKVNHMKVTPMDFATASLLNVFNGDECGAEGSWKVGVEQDVTHTNGCVALGIKLPHTEYELFRMEQDNRGRYLLYNGQRPSDGSSPARPEKRATSYQVPLVQCTSVSLNPEGAHDGQHKSQSRNSAAGHIFLYLFSNLFLLFICTLLHLEILS

Function: Negative regulator of the Wnt signaling pathway. Inhibits Wnt signaling in a cell-autonomous manner and functions upstream of beta-catenin. Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 58943 Sequence Length: 515 Subcellular Location: Cell membrane

Q5P5G5

MAIPTLEQKLTWLKPAPASSRELDLAAQIDPAQFEIGFQRTNDILDEGMDVFVRSCRCAMGVAGDSLVAIMTADGDIVNGSCGTYLHAVIPPLIIKYILETYGDEIRDGDLWFANDAVYGGVHNPDQMVCMPVYYEGKLVAWTAALVHTTETGAIEPGGMPVSATTRFEEGMNLPPMRIGENFKLREDVVSMFVAFGLRAPSMIAVDLKARCTTADRVRTRIIELCEREGADYVTGLFRKMLQVAEAGARELIEQWPDGKYRCVTFSDAVGLKQGLVRSCYMTLEKKGDRMLVDLSETGPETPSPYNAHPQAAIAHFSNYIYEYLFHSLPISNGTFANIDFKFGKNTCLSPDPRAATSCSVMISTGVMSAVHNACAKAMFSTSLWKQSGASMGNGGNALVLAGQNQWGSSFADMLAYSINTEGQGARPTEDGMDAFGFPWCVFGRAPNTESVENEFPLLVPLSNHWKDSCGHGKYRGGVGTAQVWVAHHVPELYMMAIADNTKLQTPQPLFGGYAPCTVPGIGIRNANIKELMAEGSDKIKLDVETLLAERTIDGKYEIEFQGRSVRPYSNGEVVTFAFSCGGTGYGDPLDRDPKSVEVDLLKGVLTEQTAQNIYKVKWDANLRRVDLDETSRLRAAEHDARRKRGVPYEQFEREWLKQRPDDEILKYYGTWPDAKVAQPLLRA

Cofactor: Divalent metal cations. Magnesium or manganese are required for activity. Function: Catalyzes the carboxylation of acetophenone to form 3-oxo-3-phenylpropanoate (benzoylacetate) in the anaerobic catabolism of ethylbenzene. Also carboxylates propiophenone at the same rate and 4-acetyl-pyridine at lower rates. Catalytic Activity: acetophenone + 2 ATP + H2O + hydrogencarbonate = 3-oxo-3-phenylpropanoate + 2 ADP + 2 H(+) + 2 phosphate Sequence Mass (Da): 75405 Sequence Length: 684 Subcellular Location: Cytoplasm EC: 6.4.1.8

P11389

TVVSQVILKADDELRYPSSGELKSITEFLQTGEQRVRIAQ

Function: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers. PTM: Contains one covalently linked bilin chromophore. Location Topology: Peripheral membrane protein Sequence Mass (Da): 4506 Sequence Length: 40 Subcellular Location: Cellular thylakoid membrane

P11390

MTIVSQVILKADDELRYPSGGELKNITDFFKTGEQRLRIAQVLSDSEKKIVDQASRKLWQRRPDFIAPGGNAYGQRQRAQCLRDYGWYLRLITYGVLAGDKEPIESIGLLGAREMYNSLGVPLPGMAEAIRTLKEASLALLSSADATVAAPYFDFLIQGMETI

Function: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers. PTM: Contains one covalently linked bilin chromophore. Location Topology: Peripheral membrane protein Sequence Mass (Da): 18130 Sequence Length: 163 Subcellular Location: Cellular thylakoid membrane

Q5P5G6

MEAAGALWRRRMQELARGAGKPHAPLFVPLIMGCAAQIEAIPAIDMVRDGTRLRKNLSELRRMLKLDALTCAVPSCMEAEAVGVEVSQDQWPPRIGTTAQVDVTAEIDADRLAASPRIAAALDAVRQIAVDPGEPVIAAALTGPAALVAQLRAAGVEAGDEAIYDFAGRILATLARLYAEAGVNLLSWHEAARPAEEQDDFWKGALGTAGNVARFHRVPPVLVLPASLAAGPWPAQAVPCPALNHPPLPPVRTHARAWAADPAGWPCLPVEGVAERLILTDAEVPPETEIATLKAQVERVRGE

Cofactor: Divalent metal cations. Magnesium or manganese are required for activity. Function: Catalyzes the carboxylation of acetophenone to form 3-oxo-3-phenylpropanoate (benzoylacetate) in the anaerobic catabolism of ethylbenzene. Also carboxylates propiophenone at the same rate and 4-acetyl-pyridine at lower rates. Catalytic Activity: acetophenone + 2 ATP + H2O + hydrogencarbonate = 3-oxo-3-phenylpropanoate + 2 ADP + 2 H(+) + 2 phosphate Sequence Mass (Da): 32124 Sequence Length: 303 Subcellular Location: Cytoplasm EC: 6.4.1.8

Q9ULZ1

MNLRLCVQALLLLWLSLTAVCGGSLMPLPDGNGLEDGNVRHLVQPRGSRNGPGPWQGGRRKFRRQRPRLSHKGPMPF

Function: Endogenous ligand for the apelin receptor (APLNR) . Drives internalization of the apelin receptor (By similarity). Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR (By similarity). Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis (By similarity). Has an inhibitory effect on cytokine production in response to T-cell receptor/CD3 cross-linking; the oral intake of apelin in the colostrum and the milk might therefore modulate immune responses in neonates (By similarity). Plays a role in early coronary blood vessels formation (By similarity). Mediates myocardial contractility in an ERK1/2-dependent manner (By similarity). May also have a role in the central control of body fluid homeostasis by influencing vasopressin release and drinking behavior (By similarity). PTM: Several active peptides may be produced by proteolytic processing of the peptide precursor. Sequence Mass (Da): 8569 Sequence Length: 77 Subcellular Location: Secreted

Q9R0R4

MNLRLCVQALLLLWLSLTAVCGVPLMLPPDGTGLEEGSMRYLVKPRTSRTGPGAWQGGRRKFRRQRPRLSHKGPMPF

Function: Endogenous ligand for the apelin receptor (APLNR). Drives internalization of APLNR (By similarity). Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR (By similarity). Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis (By similarity). Has an inhibitory effect on cytokine production in response to T-cell receptor/CD3 cross-linking; the oral intake of apelin in the colostrum and the milk might therefore modulate immune responses in neonates . Plays a role in early coronary blood vessels formation . Mediates myocardial contractility in an ERK1/2-dependent manner (By similarity). May also have a role in the central control of body fluid homeostasis by influencing vasopressin release and drinking behavior . PTM: Several active peptides may be produced by proteolytic processing of the peptide precursor. Sequence Mass (Da): 8658 Sequence Length: 77 Subcellular Location: Secreted

Q9R0R3

MNLSFCVQALLLLWLSLTAVCGVPLMLPPDGKGLEEGNMRYLVKPRTSRTGPGAWQGGRRKFRRQRPRLSHKGPMPF

Function: Endogenous ligand for the apelin receptor (APLNR) . Drives internalization of the apelin receptor . Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR . Hormone involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis (By similarity). Has an inhibitory effect on cytokine production in response to T-cell receptor/CD3 cross-linking; the oral intake of apelin in the colostrum and the milk might therefore modulate immune responses in neonates (By similarity). Plays a role in early coronary blood vessels formation (By similarity). Mediates myocardial contractility in an ERK1/2-dependent manner . May also have a role in the central control of body fluid homeostasis by influencing vasopressin release and drinking behavior . PTM: Several active peptides may be produced by proteolytic processing of the peptide precursor. Sequence Mass (Da): 8677 Sequence Length: 77 Subcellular Location: Secreted

Q8W4B2

MEATDIWGEIERSESYLVCSMYEEAESLSSSILKRIFGNIDVLSDEASQGDHQFHDMLESAGMVLVQSLHGIGRTVEIVNELRDVFGEVAAIPVQVLLTGVCLQISNGSYLGVRDILEEFFRIWVYKDNHYILNDAGVSTKGFHAKNCLDIDEYMEVVELYTFGVLAKFSNDMGLAISWVEKAALPEERRQGILRRLHSLLSLKTASSFEENSKDSSYAVVNNKKSLGNEKNDEIDSFLKLSKQHEPWSLWSSHPLSLKVGNTQFSMSRGKVAVSLVGLIICYALKRKRAALIRIIRRQMESTRKAIVDFWKLAFSYQVNPLAAIQSIPSTTT

Function: Involved in peroxisome biogenesis and matrix protein import . Required for pollen maturation and in vivo germination via its role in peroxisomal function, which partially involves jasmonic acid biosynthesis . Transported to peroxisomes via the interaction with PEX19-1 . Required for peroxisomal protein import by acting as an anchoring protein for the AAA ATPase complex, which consists of PEX1 and PEX6 . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 37467 Sequence Length: 333 Subcellular Location: Peroxisome membrane

A9UGV5

MAGQLKSKIVAVAVAAVVVVASSLVGTASAADAPAPAPTSGATATAAAAPAFAAVSVAAAALGGYLFC

Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline residues are glycosylated with arabinogalactan. Location Topology: Lipid-anchor Sequence Mass (Da): 6144 Sequence Length: 68 Subcellular Location: Vacuole

A9UGV6

MARFSAAAVIAFAVVAAAALATVASAADAPAPAPTSGAVAAVSAPLSVCCVAGLLLALLRH

Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline residues are glycosylated with arabinogalactan. Location Topology: Lipid-anchor Sequence Mass (Da): 5688 Sequence Length: 61 Subcellular Location: Vacuole

A9UGV7

MASRILYAAAVVAAVAVSSLAGVAYAADAPAPSPTSGAAAVSSSLVAAVLCPAVALLLGNLRQ

Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline residues are glycosylated with arabinogalactan. Location Topology: Lipid-anchor Sequence Mass (Da): 5938 Sequence Length: 63 Subcellular Location: Vacuole

P23196

MPKRGKKGAVVEDAEEPKTEPEAKKSKAGAKKNEKEAVGEGAVLYEDPPDQKTSPSGKSATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPVELQELSGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEYDAFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLTDSFRHLYPNTAYAYTFWTYMMNARSKNVGWRLDYFLLSQSVLPALCDSKIRSKALGSDHCPITLYLAL

Function: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA (By similarity). PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 in response to MPP(+)/MPTP (1-methyl-4-phenylpyridinium) reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death (By similarity). Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. Sequence Mass (Da): 35570 Sequence Length: 318 Domain: The N-terminus contains the redox activity while the C-terminus exerts the DNA AP-endodeoxyribonuclease activity; both function are independent in their actions. An unconventional mitochondrial targeting sequence (MTS) is harbored within the C-terminus, that appears to be masked by the N-terminal sequence containing the nuclear localization signal (NLS), that probably blocks the interaction between the MTS and Tom proteins (By similarity). Subcellular Location: Nucleus EC: 3.1.11.2