entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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F4HXL0
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PLIP2_ARATH
|
Phospholipase A1 PLIP2, chloroplastic (EC 3.1.1.32) (Galactolipase PLIP2) (EC 3.1.1.26) (Protein PLASTID LIPASE 2)
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MDSLCLNSGLHGVIPAITAVGNGGCGGVVEVRATASAPSQKRGPFGFSFKYPLTPFWSRGGGGGIASRRRSGLCLDDAVLVDSGDSRKPIAEETAVEMDTERRNGSWVLKILDVQSTWKHEEEEDDDEVEDEDGDEDEEVELDDAVVSEDDGGCDVCSVLEDDGNEANKFQLDRESFSKLLRRVTLPESKLYAQLSYLGNLAYSISKIKPANLSKYYGLRFVTSSAEKTESALKAENGEVSGETKPIVEAEEEVEEEEKNKSRKISASAAYEIVASAASYLHSRTNNILPFNSSSKAENSDKHDVNLTNAESSSDVAYSVTSVVAAEEDVKQAVADDLKSTISSPCDWFICDDDQSHTRFVVIQGSESLASWQANLLFEPIEFEGLGAIVHRGIYEAAKGMYEQMLPEVKAHIKTHGTSAKFRFTGHSLGGSLSLLLNLMLLVRGEVPASSLLPVITYGAPFVLCGGDRLLKKLGLPKSHVQAIVMHRDIVPRAFSCNYPYHVAELLKAVNGNFRSHPCLNKQSMLYSPMGELLILQPDETFSPGHELLPSGNGLYLLTSDFESPDIEDSDEERLRAAQTVFLNTPHPLDILSDRSAYGSSGTIQRDHDMNSYLKAVRSVIRKEVNQIRRAKREHRRSLWWPILVARESGSSGIAVSNGQINGQDFSGMMQTGRKSLQRFSRLVASQHMPLIVVMLFPVKLLFLGAFNVFSFR
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Sn-1-specific phospholipase A1 that catalyzes the initial step of oxylipins and jasmonate (JA) biosynthesis. Hydrolyzes polyunsaturated acyl groups preferentially from chloroplastic monogalactosyldiacylglycerol (MGDG). May function downstream of abscisic acid (ABA) and provide a link between ABA-mediated abiotic stress responses and oxylipin and JA signalings. In vitro, possesses broad substrate specificity. Can hydrolyze the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), the sulfolipid sulfoquinovosyldiacylglycerol (SQDG), and the phoshpolipids phosphatidylcholine (PC), and phosphatidylglycerol (PG).
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F4HXP9
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MYO9_ARATH
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Myosin-9 (Myosin XI C) (AtXIC)
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MVRECFTFLNIFVLHSIGSHVWFEDPEVAWIDGEVEKINGQEVVIQATTGKKVTAKLSKIYPKDVEAPAGGVDDMTKLSYLHEPGVLQNLKIRYELNEIYTYTGNILIAINPFQRLPHIYDAHMMQQYKGAPLGELSPHVFAVADVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRAVTEGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKQGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPQEEIEKYKLGHPKTFHYLNQSKCFELVGISDAHDYLATRRAMDIVGISEKEQEAIFRVVAAILHIGNIDFTKGKEVDSSVPKDEKSKFHLKTAAELLMCDLKALEDALCKRVMITPEEVIKRSLDPQSAVTSRDGLAKTVYSRLFDWLVDKINKSIGQDANSRSLIGVLDIYGFESFKTNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEAIDWSYIEFVDNQDVLDLIEKKPGGIVALLDEACMFPKSTHETFANKLYQTFKTHKRFIKPKLSRTDFAVAHYAGEVLYQSELFLDKNKDYVIPEHQDLLGASKCPFVVGLFPPLPEETSKSSKFSSIGSRFKLQLQQLMETLNCTEPHYIRCVKPNNLLKPAIFENVNIMQQLRCGGVLEAIRISCAGYPTRKPFFEFINRFGLLSPAALEGNFDEKVACQKILDNMGLKGYQIGKTKVFLRAGQMAELDARRAEVLSSAAKKIQRRIRTHQAQKRFIVLRKATISLQAICRGRLSCKHYDNLRREAAAVKIQKNGRRHYSRKSYKKLHVASLVVQTGLRAMAARKQFRFRKQTKAATIVQAQWRCHRAISYYKKLKNGVVLSQTRWRGRLAKRELRKLKMAARETGALKEAKDMLEKKVEELTYRVQLEKRSRGDLEEAKTQEILKLKSSFEEMRKKVDETNALLLKEREAAKKAAEEAPPVIKETQILVEDTKKIELMTEELESVKVTLENEKQRADDAVRKFEEAQESLEDKKKKLEETEKKGQQLQESLTRMEEKCSNLESENKVLRQQAVSMAPNKFLSGRSRSILQRGSESGHLAVDARSNLDLHSHSINHRDPSEVEDKPQKSLNEKQQENQDLLIRSIVQHLGFQGNRPITACIIYKCLLQWRSFEVERTSVFDRIIQTIGHAIETQDNNNTLAYWLSNTSTLLLLLQRTLKASGAAGMAPQRRRSSSATLFGRMSQSFRGAPPGVNLAMINGAAGGGADTFRQVEAKYPALLFKQQLTAYVEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGASRSVGNTAAQQALIAHWQGIVKSLTNFLNTLKSNNVPSFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEYVKAGLSELEHWCFKATNEYAGSSWDELKHIRQAIGFLVVHQKPKKTLDEISHDLCPVLSIQQLYRISTMYWDDKYGTHSVSPDVIANMRVLMTEDSNNAVSNSFLLDDDSSIPFSVDDLSKSMEKFEIADIEPPPLIRENSGFSFLLPVSE
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Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in trafficking of Golgi stacks and mitochondria.
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F4HXU3
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KNATM_ARATH
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Protein KNATM (KNOX Arabidopsis thaliana MEINOX protein)
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MDVKKDENSILENMKQEINHSLKEEAQEEEEILKKRISSHPLYGLLLHSHLNCLKVCSGDFDSPEIMNTADDLALSKLSLHPDSSSEATSSELDQFMVLFFFSPCQNIFTQQKTTFHVLLFFPLQINLTFKYSKFILPRKKQ
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[Isoform KNATM-B]: Transcriptional regulator involved in leaf proximal/distal patterning. May act by sequestering BELL transcription factors.
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F4HXY7
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PSS1_ARATH
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CDP-diacylglycerol--serine O-phosphatidyltransferase 1 (EC 2.7.8.8) (Phosphatidylserine synthase 1)
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MEPNGYRKERRKEQHLGRMNGGGGDVETDLDPWTAWAYKPRTISLLLIGACFLIWASGALDPDSTTSDDLVTSVKRGVWAMIAVFLAYSLLQAPSTVLIRPHPAIWRLVHGMAVIYLVALTFLLFQRRDDARQFMKFLHPDLGIELPEKSYGADCRIYVPDHPTNRFKNLYDTVFDEFFLAHIFGWWGKAILIRNQPLLWVLSIGFELLEVTFRHMLPNFNECWWDSIVLDILICNWFGIWAGMYTVRYFDGKTYEWVGISRQPNIIGKVKRTLGQFTPAHWDKDEWHPLQGPWRFIQVLTLCIIFLTVELNTFFLKFSLWIPPRNPVILYRLILWWLIAIPTTREYNSYLQDRKPVKKVGAFCWLSLGICIVELLICIKFGSGLYPTEMPLWVVTLWGSVGLGLVAFLLSWTWKIQKILAQKRR
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Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Is essential for phosphatidylserine (PS) biosynthesis and PE seems to be the most plausible substrate. Plays an important role in microspore maturation.
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F4HXZ1
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BRO1_ARATH
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Vacuolar-sorting protein BRO1 (BRO domain-containing protein 1) (AtBRO1)
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MASSSLSNLMLAIHEKKTSSVDLYRPLRNYVTFTYSEREAQLIDDDLETLKQLRSDIERVSDPSPAARRDLLISYYKVLCLVETRFPISPDKDHVNAVSFVWYDAFKQKHKATQQNIHLEKAAVLFNLGASYSQIGLGHDRTTVDGRRQASHAFMAAAGAFAHLRDNESIKATIGPSTTVDVSVECVGMLERLMVAQAQECVFENTIAKGSTPGVSAKIARQVGIFYEEALSALIISPLKDHFDKGWISHVQLKAALFYGEACFRYGKELHEKEEIAEEIARLRSGASRLAEAKKSSRGAPAQLIEAMNTLESSINGNLDRAVKENDRVYLMRVPSPSSLSPLPAFSMVKPMNMTDILDASKEKMFSILVPDSSAKALSRYTEMVDDVIRTQAERLQQASELTRVRLKEMDLPDSILAVDGNSALPVDLKEDVEAVQISGGPAGLEAELQQLRDLKRVNQELLVHTEELLQKEATEDSQFRSQFGTRWTRPQSSTLTKNLQDRLNRFAANLKQAGESDVKIERSVRDNSALMSILDRRPIESAVPTLARPIMSLDATEDAIVGTLKQSLRQLENLGAQRAGLEDMLKEMKRKDDILPKLMTITGSYEDMFRKEISKYDHICEDISQNIEVQEQLLMQIQAQNEEFSTIFNLEDYKASKEKCYKQIQAAIMKYREIKENINEGLKFYVTLQDAITNVKQQCSDFVMTRSIQCRDMIEDVQRQMSGLSFQDHRSSGPYPSVHQPTASSPPPPPETQNPSHPHPHAPYYRPPEQMSRPGYSIPPYGPPPPYHTPHGQAPQPYPPQAQQQPHPSWQQGSYYDPQGQQPRPPYPGQSPYQPPHQGGGYYRQ
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Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen (Probable). Associates with FREE1 and ELC to perform function in the ESCRT-I complex. Binds ubiquitin in vitro. Plays a role in the biogenesis of vacuole and multivesicular bodies (MVBs). Required for the endosomal location of AMSH3. Mediates high-affinity phosphate transporter trafficking to maintain phosphate homeostasis. Regulates vacuolar degradation of PHT1-1.
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F4HY56
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RLT1_ARATH
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Homeobox-DDT domain protein RLT1 (Protein HOMEOBOX-1) (Protein RINGLET 1)
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MEMGSDGEDQKIRSVVGDANLNNKKKKIDNNSSSKDGRVKPKRQMKTPFQLETLEKVYSEEKYPSEATRAELSEKLDLSDRQLQMWFCHRRLKDKKDGQSNKPVKSSVAAVQSASVNELPAAAGSVPEQDSRSDSGSESGCSPYSNSRRNFASGSSSSRAELDEYETMGKPSYESRLSTMVHRAIVCIEAQLGEPLRDDGPILGMEFDPLPPGAFGTPIAMQKHLLHPYESDLYERHDPRPRRSHAAARSFHEQQSLDDPSSFTPNMYERYSENHARGMDYEVARSRISSFMHANGPVPRSYVTPGHASRNCSTSQQDMPSPIESAHHGDRFLLEKDSSVLGTEDPYLLPDGVRKSSDVHRKGKINDGRLGRGSETRENHGPKDLEKLEIQRKKNEERMRKEMERNERERRKEEERLMRERIKEEERLQREQRREVERREKFLQRENERAEKKKQKDEIRREKDAIRRKLAIEKATARRIAKESMDLIEDEQLELMELAAISKGLPSVLQLDHDTLQNLEVYRDSLSTFPPKSLQLKMPFAISPWKDSDETVGNLLMVWRFLISFSDVLDLWPFTLDEFIQAFHDYDSRLLGEIHVTLLRSIIRDVEDVARTPFSGIGNNQYTTANPEGGHPQIVEGAYAWGFDIRSWKKHLNPLTWPEILRQLALSAGFGPKLKKKHSRLTNTGDKDEAKGCEDVISTIRNGTAAESAFASMREKGLLAPRKSRHRLTPGTVKFAAFHVLSLEGSKGLTVLELADKIQKSGLRDLTTSKTPEASISVALTRDVKLFERIAPSTYCVRAPYVKDPKDGEAILADARKKIRAFENGFTGPEDVNDLERDEDFEIDIDEDPEVDDLATLASASKSAVLGEANVLSGKGVDTMFCDVKADVKSELEKEFSSPPPSTMKSIVPQHSERHKNTVVGGVDAVIDESNQGQSWIQGLTEGDYCHLSVEERLNALVALVGIANEGNSIRTGLEDRMEAANALKKQMWAEAQLDNSCMRDVLKLDLQNLASSKTESTIGLPIIQSSTRERDSFDRDPSQLLDETKPLEDLSNDLHKSSAERALINQDANISQENYASKRSRSQLKSYIGHKAEEVYPYRSLPLGQDRRHNRYWHFAVSVSKSDPCSRLLFVELHDGKWLLIDSEEAFDILVASLDMRGIRESHLRIMLQKIEGSFKENACKDIKLARNPFLTEKSVVNHSPTDSVSPSSSAISGSNSDSMETSTSIRVDLGRNDTENKNLSKRFHDFQRWMWTETYSSLPSCARKYGKKRSELLATCDACVASYLSEYTFCSSCHQRLDVVDSSEILDSGLAVSPLPFGVRLLKPLLVFLEASVPDEALESFWTEDQRKKWGFRLNTSSSPGELLQVLTSLESAIKKESLSSNFMSAKELLGAANAEADDQGSVDVLPWIPKTVSAVALRLSELDASIIYVKPEKPEVIPEDENEQISLFPRDSPFKGKGPREQEDQDEVAPNPGNRNKKRARVSLGSGSNRKVKRKKAQSGLNKFVVGRRNVAVNSNLMAVELNHQVPGKGKRTVRKRPERIDEDNSHLVNRMANIVRPKSEEVEEDEEEEEQTFRDINEDWAAGETPREMEEDWANETPNRMMTPMQVDDESDNSVGVESEDEDGGGQFVDYSQRNKWGLDWNSNLNVAIEEDEEEEVVGVGRVEGEDDAEMSESSEDDDVPANNAANNYDRESEGYSSSDS
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Transcriptional regulator required for the maintenance of the plant vegetative phase. In association with CHR11 or CHR17 may prevent the early activation of the vegetative-to-reproductive transition by regulating key genes that contribute to flower timing, such as FT, SEP1, SEP3, AGL8/FUL, SOC1 and FLC.
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F4HYF3
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DCYD1_ARATH
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Bifunctional D-cysteine desulfhydrase/1-aminocyclopropane-1-carboxylate deaminase, mitochondrial (EC 3.5.99.7) (EC 4.4.1.15) (1-aminocyclopropane-1-carboxylic acid deaminase 1) (AtACD1) (AtD-CDes1) (D-CDes1) (D-CDES)
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MRGRSLTLSRVKLELARRSMSATSVPSMADFLTKKPYSPPSWASHLRPLPSHTFSLAHLPTPIHRWNLPGLPNGTELWIKRDDFTGMELSGNKVRKLEFLMAEAVDQHADTVITIGGIQSNHCRATATASNYLNLNSHLILRTSKLLADEDPGLVGNLLVERLVGANVHLISKEEYSSIGSEALTNALKEKLEKEGKKPYVIPVGGSNSLGTWGYIEAAREIEEQLNYRPDDLKFDDIVVACGSGGTIAGISLGSWLGALKAKVHAFSVCDDPDYFYDFVQGLLDGLHAGVNSRDIVNIHNAKGKGYAMNTSEELEFVKKVASSTGVILDPVYSGKAAYGLINEITKDPKCWEGRKILFIHTGGLLGLYDKVDQMASLMGNWSRMDVSESVPRKDGVGKMF
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Catalyzes the production of hydrogen sulfide (H2S) from cysteine. Is mainly responsible for the degradation of cysteine to generate H2S, a regulator of stomatal movement and closure. Has high affinity for D-cysteine. Possesses 1-aminocyclopropane-1-carboxylic acid (ACC) deaminase activity. Acts as a regulator of ACC levels and causes changes in ethylene levels.
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F4HZB2
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BCHA1_ARATH
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Protein SPIRRIG (BEACH domain-containing protein A1) (BEACH-domain homolog A1)
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MKWATLLKDIKEKVGLAQSSDSDPFPVDLTAPPSSSSSSSSPSFTYPSSSSLHHFNFSPSSRDNHELELDFKRLWEEFRSSSSEKEKEAALNLTVDIFCRLVKRHANVDQLVTMLVETHIFSFVIGRAFVTDIEKLKIGSKTRSLNVEKVLRFFSDVTKEGFSPGANLLTAVEVLVSGPIDKQSLLDSGIFCCLIHVLIALLAYDELSKSKITGDLEVVSAEKDAGYIVLQTRRLEVEGSVVHIMKALASNPSAAQSLIEDDSLESLFNMVANGSITVFSQYKEGLVPLHNIQLHRHAMQILGLLLVNDNGSTARYIRKHHLIKVLLMAVKEFDPSCGDSAYTMGIVDLLLECVELSYRPEAGGVRLREDIRNAHGYHFLVQFALVLSSLPKNPIFVSSNHDSGSDDPEVFHDGENTNSTENADFSSQNFAPSLSRLLDVLVTLAQTGPAEPSVGRASRSSQTKPTGHSRSRTSSVDSIYDETWEQGSGKVKDLEAVQMLQDIFLKAENKDLQAEVLNRMFKIFSSHVENYRLCQELRTVPLLVLNMAGFPSSLQDIILKILEYAVTVVNCVPEQELLSLCCLLQQPITSQLKHTILSFFVKLISFDQQYKKVLREVGVLEVLQDDLKQHKLLIGPDQYSGVSSHSDRKPSSGSFRKNLDTKDAIISSPKLMESGSGKLPVFEVDNTITVGWDCLISLLKKAEANQSSFRAANGVAIILPFLISDAHRSGVLRILSCLITEDTKQVHHDELGAVVDLLKSGMVTGISGHQYKLHDDAKCDTMGALWRIVGVNGSAQRVFGEATGFSLLLTTLHTFQGKREHMDESDLTVYIKLFKYLFRLMTAAVCENAVNRMKLHAVITSQTFFELLAESGLLCVELERQVIQLLLELALEVVVPPFLTSESTALATIPENENTTFVVTTPSGQFNPDKERIYNAGAVRVLIRSLLLFSPKMQLEFLRLLESLARASPFNQENLTSIGCVELLLEIIYPFLAGSSPFLSYALKIVEILGAYRLSPSELRMLFRYVLQMRIMNSGHAIVGMMEKLILMEDTALEHLSLAPFVELDMSKTGHASVQVSLGERSWPPAAGYSFVCWFQFRNFLTTQGKESEASKAGGSSKTRMTSAQQHEQNIFRMFSVGAVSNESPFYAELYFQEDGILTLATSNSHSLSFSGLEIEEGRWHHLAVVHSKPNALAGLFQASVAYVYLDGKLRHTGKLGYSPSPVGKSLQVTVGTPATCARVSDLTWKTRSCYLFEEVLTSGCIGFMYILGRGYKGLFQDADLLRFVPNQACGGGSMAILDSLDTDMTSSSNGQKFDGSNRQGDSKADGSGIVWDLERLGNLAFQLPGKKLIFAFDGTCSEFIRASGNFSLLNLVDPLSAAASPIGGIPRFGRLVGNVSICRQSVIGDTIRPVGGMTVVLALVEAAESRNMLHMALSLLACALHQNPQNVKDMQTIRGYHLLALFLRPKMTLFDMQSLEIFFQIAACEALFSEPKKLESVQSNITMPPTETIFENSYEDLSLSRFRYDSSSVGSHGDMDDFSVPKDSFSHLSELETDIPVETSNCIVLSNADMVEHVLLDWTLWVTSPVSIQIALLGFLENLVSMHWYRNHNLTILRRINLVEHLLVTLQRGDVEVPVLEKLVVLLGCILEDGFLTSELENVVRFVIMTFNPPEVKSRSSLLRESMGKHVIVRNMLLEMLIDLQVTIKAEDLLELWHKIVSSKLITYFLDEAVHPTSMRWIMTLLGVCLASSPNFSLKFRTSGGYQGLLRVLQNFYDSPDIYYILFCLIFGKPVYPRLPEVRMLDFHALVPNDGSYVELKFIELLDSVVAMAKSTYDRLIMQSMLAHQSGNLSQVSASLVAELIEGAEMTGELQGEALMHKTYAARLMGGEASAPAAATSVLRFMVDLAKMCPQFSTACRRAEFVENCADLYFSCVRAAYAVKMAKQLSVKAEEKHINDADDSGSQGSLPHDQDQSTKTSISVGSFPQGQVSLGSEDMSLPANYVVNDKMENILPPPTQDTSKSLQGVEDVKKQDDHHVGPSASSERDFQDFTGNPVQVQATDSQSSASFPMIESPLLSEKSSLKVSFTPSPSPVVALASWLGSNYNESKSSTLGSPSLESYVSVNEVDASSERKSGSQGSSAANAFFTVSPKLLLETDETGYGGGPCSAGASAVLDFMAEALADLVTEQIKAVPVLESILEMVPFYVDPESVLVFQGLCLSRVMNYLERRLLRDDEEDEKKLDKAKWSVNLDAFCWMIVDRVYMGAFSQPAGVLRALEFLLSMLQLANKDGRVEEVTPSGKGLLSLGRATRQLDAYVHSILKNTNRMVLYCFLPSFLITIGEEDLLSQLGLLVESKKRPSPNPATDESGIDISTVLQLLVANRRIIFCPSNLDTDLNCCLCVNLISLLLDQRKSVQNMSLDIVKYLLVHRRSALEDLLVTKPNQGQNFDVLHGGFDKLLTGNLPEFFKWLESSDKIINKVLEQCAAIMWVQYIAGSAKFPGVRIKGMEGRRKREMGRKSRDMSKLDLKHWDQLNERRYALEVLRDAMSTELRVVRQNKYGWILHAESEWQTHLQQLVHERGIFPMRKSKGTEDPEWQLCPIEGPYRMRKKLERCKLKIDSIQNVLDGKLELGEIELPKVKNEDGPVISDTDSEPPFLLSELYDESFLKESDDFKDVASARNGWNDDRASSTNEASLHSALDFGGKSSIASVPITDTTHVKSETGSPRHSSSAKMDETNGREEKSEKELNDDGEYLIRPYLEHLEKIRFRYNCERVVDLDKHDGIFLIGEFCLYVIENFYIDEDGCICEKECEDELSVIDQALGVKKDVSGSSDFHSKSSTSWTTTVKTGAVGGRAWAYGGGAWGKEKMCMTGNLPHPWRMWKLNNVHEILKRDYQLRPVAIEIFSMDGCNDLLVFHKKEREEVFKNLVAMNLPRNSMLDTTISGSAKQESNEGGRLFKLMAKSFSKRWQNGEISNFQYLMHLNTLAGRGYSDLTQYPVFPWVLADYDSESLDFSDPKTFRKLHKPMGCQTPEGEEEFRKRYESWDDPEVPKFHYGSHYSSAGIVLFYLIRLPPFSSENQKLQGGQFDHADRLFNSIKDTWLSAAGKGNTSDVKELIPEFFYMPEFLENRFSLDLGEKQSGEKVGDVFLPPWARGSVREFILKHREALESDYVSENLHHWIDLIFGYKQRGKAAEEAVNVFYHYTYEGNVDIDAVTDPAMKASILAQINHFGQTPKQLFPKAHVKRRTDRKIPLHPLKHSMHLVPHEIRKCSSSISQIITFHDKVLVAGANCFLKPRGYTKYITWGFPDRSLRFMSYDQDKLLSTHENLHESNQIQCAGVSHDGRIVVTGAEDGLVCVWRVSKDGPRGSRRLRLEKALCAHTAKVTCLRVSQPYMMIASGSDDCTVIIWDLSSLSFVRQLPDFPVPISAIYINDLTGEIVTAAGTVLAVWSINGDCLAVANTSQLPSDSVLSVTGSTSSDWLETSWYVTGHQSGAVKVWRMIHCTDPVSAESKTSSSNRTGGLNLGDQVPEYKLILHKVLKFHKQPVTALHLTSDLKQLLSGDSAGQLLSWTVPDETLRASMKQASLKQASLKQASLKQASSV
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Involved in cell morphogenesis. May have a function in membrane fusion or membrane composition. Required for salt stress tolerance. Regulates the salt stress-dependent post-transcriptional stabilization, cytoplasmic agglomeration, and localization to P-bodies of a subset of salt stress-regulated mRNAs.
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F4HZD1
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JMJ24_ARATH
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E3 ubiquitin-protein ligase JMJ24 (EC 2.3.2.27) (Inactive histone demethylase JMJ24) (Jumonji domain-containing protein 24) (AtJMJ24) (Protein JUMONJI 24)
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MQVNFDETCDSVIRMNANEQTRSANGIGNGNGESIPGIPDDLRCKRSDGKQWRCTAMSMADKTVCEKHYIQAKKRAANSAFRANQKKAKRRSSLGETDTYSEGKMDDFELPVTSIDHYNNGLASASKSNGRLEKRHNKSLMRYSPETPMMRSFSPRVAVDLNDDLGRDVVMFEEGYRSYRTPPSVAVMDPTRNRSHQSTSPMEYSAASTDVSAESLGEICHQCQRKDRERIISCLKCNQRAFCHNCLSARYSEISLEEVEKVCPACRGLCDCKSCLRSDNTIKVRIREIPVLDKLQYLYRLLSAVLPVIKQIHLEQCMEVELEKRLREVEIDLVRARLKADEQMCCNVCRIPVVDYYRHCPNCSYDLCLRCCQDLREESSVTISGTNQNVQDRKGAPKLKLNFSYKFPEWEANGDGSIPCPPKEYGGCGSHSLNLARIFKMNWVAKLVKNAEEIVSGCKLSDLLNPDMCDSRFCKFAEREESGDNYVYSPSLETIKTDGVAKFEQQWAEGRLVTVKMVLDDSSCSRWDPETIWRDIDELSDEKLREHDPFLKAINCLDGLEVDVRLGEFTRAYKDGKNQETGLPLLWKLKDWPSPSASEEFIFYQRPEFIRSFPFLEYIHPRLGLLNVAAKLPHYSLQNDSGPKIYVSCGTYQEISAGDSLTGIHYNMRDMVYLLVHTSEETTFERVRKTKPVPEEPDQKMSENESLLSPEQKLRDGELHDLSLGEASMEKNEPELALTVNPENLTENGDNMESSCTSSCAGGAQWDVFRRQDVPKLSGYLQRTFQKPDNIQTDFVSRPLYEGLFLNEHHKRQLRDEFGVEPWTFEQHRGEAIFIPAGCPFQITNLQSNIQVALDFLCPESVGESARLAEEIRCLPNDHEAKLQILEIGKISLYAASSAIKEVQKLVLDPKFGAELGFEDSNLTKAVSHNLDEATKRPQQNSCT
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Binds histone H3 but seems to have lost demethylase activity probably due to its inability to bind iron Fe(2+). Possesses E3 ubiquitin ligase activity and targets directly CMT3 for proteasomal degradation to initiate destabilization of the heterochromatic state (e.g. CHG cytosine methylation and H3K9me2) of endogenous silenced loci. Required for the removal of repressive H3K9me2 histone marks to facilitate the transcription of AtSN1, AtMu1c, solo LTR and SDC, thus counteracting their transcriptional silencing. Mainly required to promote the basal level transcription of silenced loci such as TE and repeats targeted by RNA-dependent DNA methylation (RdDM) for silencing, a specialized branch of the RNA interference (RNAi) pathway. Cooperates also with RNAi pathways for gene silencing both by contributing to the production of 24-nt siRNA to initiate RdDM and by recruiting RDR2 to enable local transcripts to make dsRNA. Antagonizes histone H3K9 demethylase IBM1/JMJ25 function.
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F4HZG9
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ICP55_ARATH
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Intermediate cleaving peptidase 55, mitochondrial (EC 3.4.11.-) (AtICP55) (Protein INTERMEDIATE CLEAVAGE PEPTIDASE 55)
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MQFLARNLVRRVSRTQVVSRNAYSTQTVRDIGQPTPASHPHLMAEGEVTPGIRIEEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVLSDERGLCMFMPESTPKDIAWEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHNVQSASQRYTNLDDFQNSASLGKVKTLSSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLCDGLMKMGILKSRRLYHQLNPTSIGHYLGMDVHDSSAVGYDRPLQPGFVITIEPGVYIPSSFDCPERFQGIGIRIEDDVLITETGYEVLTGSMPKEIKHIETLLNNHCHDNSARTSPVSLCKVKGLHTNRNPRRLF
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Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome.
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F4I096
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MED13_ARATH
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Mediator of RNA polymerase II transcription subunit 13 (Protein GRAND CENTRAL) (Protein MACCHI-BOU 2)
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MWTNVFRIGGLHNVSWFQFLPSETELNPGFDRSSRAEQNEVATYLVLSSHLRLQKEGFLTTWTNSFVGPWDPSQGLYNPDEKIKLWLFLPGRHSSISDKAQAAVSKLRVVASGIWVAPGDSEEISVAFSQSLRNCIERALSGISYMRFGDVFSKFSPQSEEYLRRGQPTVEFIFAATEEAVFVHVIISAKNVRTLSSGDAERMLRSSLKNSSYRLPAFRKCLGLAKSEDNRLCYINTSHRPMLFPPVIVSPHGMRGSLTGFCPNDLVKQVYFSSGNLKTSTGYVGLPSHIGRGSRLINGNHCYVEVTLGCCQNRNDNTSQANSTFAVNLPHNQCPEPSVGSKDHRKGQSDLSSVCEKKFIYPAEAVLVPILQSAFAKFSLKRAGDFDCLGASENKSDGFYEKNGYNSSGSSRNSSISSTSSASSGSGWRMTSRTGDLDADADSLTCRQSGLTCNDDRLKMGSKRPRTGMAESFGQVGIENDQIGWDWDADDDDDDREVGMDIKALLSEFGDFGDFFENDALPFGEPPGTAESHVLVFPPDSADVGSSPVDMMDVSDQIVLPVGFSSFESFNPVPPIIDECLIKSQEVLHSSITSVPSNQMSISSTGEFDHLLKAEAMMTFAPEYGAVEAPMSEISSTFFKSPYLPKSHKVESSNSRTSNYVYGATPPTTDSDGAGDMILFGSKSCIGNNAGRTLYHSREHYTQVEGRKGRHDKLPTVISDNSSTKEGVSQSIHSKHSAANAVKVVQGKKTDGISAVVSTLLSSKTLLATDVGSVMFQAFMCRMRHIITSSKHSSPVSLTRLSGNFFLNQLSNEPSTLTDNISARNEIYKKDIPTRIAGDFDGGMLDSHMSAPVGVWRTVSVPKTAKPASSPNIEAGSSLPHSSFSEDSLLSYGQRQPLQDLLDGIALLVQQATSFVDLALDSDCGDGPYGWLALEELWRRELSCGPSAGHAGCGGTLASCHSLDIAGVKLVDPLSAEVFPSSVITLLQSDIKTALKSAFGQSDGPLSVTDWCKGRNQSGDGGSISEGFTAESALSEVNGVNISDDFIIDKYFGKQAVSNAIDGGKGDETAQSQDIYSSELLRPTLFVLPSPAILVGYQDDWLKISTNSLTHWEKAPFEPYALPKSINYAVVCPDIDPLTCAATDFFQQLGTGESTSLSFVKEVMLKHDRNWLGTHLPQSLGNQMEKDVGRLSSSGFVLLDCPQSMKIESNNTSLLGSLSDYFLSLSNGWNVNSYLKSLSKALKGLKLGSGLYTNQKEGSGSPCVVVYIVCPFPDPSAVLRTIVESSIALGSVIQSDRDRRSILNSQVARAFSSSTAVDEASISHIPVLSGFSVPKLVLQVVSVDSIFRITSPSFNELVILKDTAFSVYNKARRISRGMPNDAFFSSSLPSRSSSALTPMNSISGIWKDCGGSRMTGSTHPRDGEIDVSLRTSGWDTSTSWQIPRSGGLSCDPNRNGDFYLNDEIFYLFEPLFILSEPGSVERGVSPTFTSLGSESSKPIPEDGGRGSGPGMNSMEGITSGSSSQGDVSQLEGKAIPSLHCCYGWTEDWRWLVSIWTDARVLQQGCQILQACSSPDNGSFKPRDFVITRIGNFFELEYQEWQKAIYSAGGPEIKKWPIQLRRSAPSGIATNSNGSSLQQQDLSLIQERASSTSTLYSSHSKQSTFVKGSMGQSAGRKQIMGGQTISGTPRGLFQWVHSISFASISLDHSLHFVLPAELVSAGGGQSSTGMSSVNYIEGFTPVKSLGSTAFSYMMIPSPNMRFLHPSPLQLPTCLTAESPPLAHLLHSKGYAIPLSTGFVVSKAVPSMRKDSRINVKEEWPSVLSVSLIDYYGGYDNAHDKILQGIVKQGGGTKETRDFEVESHLILESIAAELHALSWMTVSPAYLDRRTALPFHCDMVLRLRRLLHFADKEVSRIPDKTGV
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Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Acts closely together with MAB12. Involved in the regulation of embryo patterning and cotyledon organogenesis. May act through transient repression of specific genes such as the ones responsive to auxin.
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F4I0K2
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SCKL2_ARATH
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Fructokinase-like 2, chloroplastic (pfkB-type carbohydrate kinase family protein 1)
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MASLSFTQFLSFPRCNADVPCLLQSHGFVKFRGERWNGKQSFSMAAGRRKLSESAPLEEEGNDGNGAVVGKKPSKSVKRTTKKKVVVKDEPLEEISEFLVDNDDVLDKESIVSALKPKKTRTRKKAAAASSDVEEVKTEKKVRRKRTVKKDKDVEDDLATIMDAEVSDVEEALAVESTDTESEEEEIDLSKHEGEDISHTYGWPPLVCCFGSAQHAFVPSGRPANRLLDYELHERMRDAKWAPEKYIRAPGGCAGGVAIALASLGGKVAFMGKLGADDYGQAMLYYLNVCKVQTRSVKIDGKRVTACSTMKISKRGRLKSTCIKPCAEDSLSKSEINVDVLKEAKMFYFSTHSLLDKKMMSTTIQAIKISKQLGNVIFYDLNLPLPLWHSSEETKSFIQEVWNLADVIEITKQELEFLCGIEPTEEFDTENNDISKFVHYPPETVEQLWHENLKVLFVTNGTSKIHYYTKEHNGAVSGMEDVPITPFTRDMSASGDGIVAGLIRMLTVQPDLMNNKGYLERTARYAIECGIIDQWLLAQTRGYPPKDDMEEEEDDEEEDEVESDPNGIRSITEKEYRTSKPYDEPDGPYVMKPVEEREYKKLELVGSMFEDGSL
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Required for proper chloroplast development, most likely through regulating plastid-encoded polymerase (PEP) dependent chloroplast transcription. Acts as a component of the transcriptionally active plastid chromosome that is required for plastid gene expression.
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F4I171
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MD15A_ARATH
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Mediator of RNA polymerase II transcription subunit 15a
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MDNNNWRPSLPNGEPAMDTGDWRTQLPPDSRQKIVNKIMETLKKHLPFSGPEGINELRRIAARFEEKIFSGALNQTDYLRKISMKMLTMETKSQNAAGSSAAIPAANNGTSIDSIPTNQGQLLPGSLSTNQSQAPQPLLSQTMQNNTASGMTGSTALPSSMPPVSSITNNNTTSVVNQNANMQNVAGMLQDSSGQHGLSSNMFSGPQRQMLGRPHAMSSQQQQQPYLYQQQLQQQLLKQNFQSGNVPNPNSLLPSHIQQQQQNVLQPNQLHSSQQPGVPTSATQPSTVNSAPLQGLHTNQQSSPQLSSQQTTQSMLRQHQSSMLRQHPQSQQASGIHQQQSSLPQQSISPLQQQPTQLMRQQAANSSGIQQKQMMGQHVVGDMQQQHQQRLLNQQNNVMNIQQQQSQQQPLQQPQQQQKQQPPAQQQLMSQQNSLQATHQNPLGTQSNVAGLQQPQQQMLNSQVGNSSLQNNQHSVHMLSQPTVGLQRTHQAGHGLYSSQGQQSQNQPSQQQMMPQLQSHHQQLGLQQQPNLLQQDVQQRLQASGQVTGSLLPPQNVVDQQRQLYQSQRTLPEMPSSSLDSTAQTESANGGDWQEEVYQKIKSMKETYLPDLNEIYQRVAAKLQQDSMPQQQRSDQLEKLRQFKTMLERMIQFLSVSKSNIMPALKDKVAYYEKQIIGFLNMHRPRKPVQQGQLPQSQMQPMQQPQSQTVQDQSHDNQTNPQMQSMSMQGAGPRAQQSSMTNMQSNVLSSRPGVSAPQQNIPSSIPASSLESGQGNTLNNGQQVAMGSMQQNTSQLVNNSSASAQSGLSTLQSNVNQPQLSSSLLQHQHLKQQQDQQMQLKQQFQQRQMQQQQLQARQQQQQQQLQARQQAAQLQQMNDMNDLTSRQGMNVSRGMFQQHSMQGQRANYPLQQLKPGAVSSPQLLQGASPQMSQHLSPQVDQKNTVNKMGTPLQPANSPFVVPSPSSTPLAPSPMQVDSEKPGSSSLSMGNIARQQATGMQGVVQSLAIGTPGISASPLLQEFTSPDGNILNSSTITSGKPSATELPIERLIRAVKSISPQALSSAVSDIGSVVSMVDRIAGSAPGNGSRASVGEDLVAMTKCRLQARNFMTQEGMMATKKMKRHTTAMPLSVASLGGSVGDNYKQFAGSETSDLESTATSDGKKARTETEHALLEEIKEINQRLIDTVVEISDDEDAADPSEVAISSIGCEGTTVRFSFIAVSLSPALKAHLSSTQMSPIQPLRLLVPCSYPNGSPSLLDKLPVETSKENEDLSSKAMARFNILLRSLSQPMSLKDIAKTWDACARAVICEYAQQFGGGTFSSKYGTWEKYVAAS
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Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
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F4I1S7
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ELP2_ARATH
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Elongator complex protein 2 (AtELP2) (Elongator component 2) (Protein GREEN NPR1 SEEDLING ON SA MEDIUM 1)
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MSENTKVEAKRVFIGAGCNRVVNNVSWGASGLVSFGAQNAVAVFCPKTAQILTTLPGHKASVNCTHWLPTSKFAFKAKKLDRQYLLSGDSDGIIILWELSTLNNDWRHVLQLPLSHKKGVTCITAYMVSETDAMFASASSDGVVNVWDVSFPSQPSEECKVVCLDSICVDTKAIVTLSLAELPQNPGRFALALGGLDNKIKLYSGERTGKFTSVCELKGHTDWIRSLDFSLPLHTTEEIPNSIMLVSSSQDKVIRIWKLVLVGDVGSWRREITLASYIEGPVFVSGTFTYQISVESVLIGHEDWVYSVEWQPPVIDFIDGRLVNHQPLSILSASMDKTMMIWRPEKKTGVWVNVVCVGELSHCALGFYGGHWSPNSLSILAHGYGGAFHLWRNVSSSKESENWQMQKVPSGHFAAVTDVTWARTGEYLLSVSQDQTTRVFSAWKNDEGNEAEDEHWHELARPQVHGHDINCVAMVQGKGNHRFVSGAEEKVVRVFEAPLSFLKTLNHTCAGGEGSFPEDLQADVQVLGANMSALGLSQKPIYLHSSSEPLERNGGGEGLDTFETVPEAAPAELKEPPIEDQLAFHTLWPESHKLYGHGNELFSLCSDHKGNLVASSCKAQSASMAEIWLWEVGTWKAVGRLQSHSLTVTHLEFSYDDTLLLSVSRDRHFSVFSIQRTDNGEVSHKLMAKVEAHKRIIWACSWNPFGHQFATSSRDKTVKIWSVENDARIKQILVLPPFGSSVTAVAWTGLDRNEKSGCVAVGMESGLIELSNVKIIETEEGTTATAALALRLEPFMCHVSAVNRLAWRPTEKCESNQSLRWLTSCGDDNCVRVFNFKF
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Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). Promotes organ development by modulating cell division rate. Prevents abscisic acid (ABA) signaling leading to stomatal closure and seedling growth inhibition. Involved in oxidative stress signaling. Prevents anthocyanin accumulation. Accelerator of defense gene induction required for rapid defense gene induction, and for the establishment of both basal and effector-triggered immunity (ETI), in a NPR1-independent manner, but is not required for systemic acquired resistance (SAR) establishment.
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F4I1T7
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NP214_ARATH
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Nuclear pore complex protein NUP214 (Nucleoporin 214) (Protein EMBRYO DEFECTIVE 1011) (Protein LNO1) (Protein LONO1)
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MSRVEIEEDTEGDRISTNDYYFERIGEPISIKEDDAQYDLENPPSQPLAISERHAVLFVAHSSGFFVGRTNDVISASKNSNGNGDKVFIQDLSLVDVPVGDVRILSLSADDSILAVTVAADIHFFSVDSLLKKDAKPSFSYSPDESGFVKDFRWRRNDKHSYLVLSNTGKLFHGIDNAPPRHVMDAVDAVEWSSKGSYIAVAQDNSLRIFSSKFNEKRCIALSFDSWIGDSDEDCFVKVDSIRWVRNNCILLGCFQLIEGREENYLVQVIRSPDGKISDGSTNLVALSFSDLFPCSMDDLVPVGVGPHLLFSYIDQCKLAVTANRKSIDEHIVLLDWSSGDDKSAVSVVDIDRETFLPRIGLQENNDDNTVMGLCIDRVSIEGTVNVRSGDDELKELQPYFVLVCLTLEGKLVMFNVASVAGRPASSDTDLASSSDIEDAYTPLIEDDLSKQSSEKHQQLNIAVQNDQKHLNTEKFSTEQRLPNENIFSKEFESVKSSVSGDNNKKQEPYAEKPLQVEDAQQSMIPRLSGTSFGQLPMSLGYDTNKFAGFGPALPVSEKLQKDIFAQSNSMHLQANVESKSTAAFFGSPGLQNAILQSPQNTSSQPWSSGKSVSPPDFVSGPFPSMRDTQHKQSVQSGTGYVNPPMSIKDKSVQVIETGRVSALSNLSPLLGQNQDTNEGVEKIEPIPSIRASQLSQQVKSSFEKSASHQQHKTPLSTGPLRLEHNMSNQPSNINEMAREMDTLLQSIEGPGGFKDSCAFILKSNVEELEQGLESLAGKCQTWKSTIHEQQAEIQHLLDKTIQVLAKKTYMEGMYKQTADNQYWQLWNRQKLNPELEAKRQHIMKLNKDLTHQLIELERYFNRLELDRYNEDGGHPVARRGVPNRSAPSRRVQSLHSLHNTMSSQLAAAEQLSECLSKQMTYLKIDSPVKKNVKQELFETIGIPYDASFSSPDAVKAKNASSAKNLLLSSIPASINQQSRQRQSSAMKNSDPETARRRRESLDRVIFNWAAFEPPKTTVKRMLLQEQQKTGMNQQTVLSERLRSANNTQDRSLLHVKDHASPVVSSNKGIMESFQQDTSEAQSTPFKTRPPMPQSNSPFTISPISASKPSFNWSGNKSSNTTSYAEESAPSQIKDTRTVSQPGGSSFLPKRPVASTVLEQTEKKAGEFKFSEAKANAFVETAAGSVQRLSTTSSGSDFESSKGFGAQFSTMSSGAPASSFSSKSLFGFNSSSSIPGDKFTFPAVTAPLSGTPLDSTSTLFTASSAPVSSSSQDPVPASIPISSAPVPQTFSVTSTSTVSATGFNVPFGKPLTSVKVDLNQAAPSTPSPSPGPTAGFTFNLPALSPSSPEMVSSSTGQSSLFPPSAPTSQVSSDQASATSSLTDSSRLFSSTSLSSTPPITPPDAFQSPQVSTPSSAVPITEPVSEPKKPEAQSSSILSTQSTVDSVANATKTQNEPLPVKSEISNPGTTVTPVSSSGFLSGFSSGTQSSLASMAAPSFSWPGSSQPQQLSSTPAPFPASSPTSASPFGEKKDIVDTQEDEMDEEAPEASQTTELSMGSFGGFGLGSTPNPGAPKTNPFGGPFGNATTTTSNPFNMTVPSGELFKPASFNFQNPQPSQPAGFGSFSVTPSQTPAQSGFGQPSQIGGGQQALGSVLGSFGQSRQIGAGLPGATFGSPTGFGGSNPGSGLPNAPASGGFAAAGSSATGGFAAMASAGRGFAGASSTPTGGFAALASGSGGFAGAAPGGGGGGFGGLGSGTGGFGGFAPQGSSGGFAGAAGGGGFGGFGGQAQGQAGGGGFSAFGGNSGATGKPSELFTQMRK
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Required for normal embryogenesis and seed viability. Involved in the first asymmetrical cell division of the zygote. Regulates the number and planes of cell divisions required for generating the normal embryo proper and suspensor, apical-basal axis, cotyledons and meristem.
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F4I240
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JMJ17_ARATH
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Lysine-specific demethylase JMJ17 (EC 1.14.11.67) (Jumonji domain-containing protein 17) (AtJMJ17) (Protein JUMONJI 17) (Lysine-specific histone demethylase JMJ17) ([histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ17)
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MLLCDSCNKGWHIYCLSPPLKHIPLGNWYCLECLNTDEETFGFVPGKCLLLEDFKRIADRAKRKWFGSGTVSRTQIEKKFWEIVEGSGGEVEVMYGNDLDTSVYGSGFPRIGDQRPESVEADIWDEYCGSPWNLNNMPKLKGSMLQAIRHNINGVTVPWLYLGMLFSSFCWHFEDHCFYSVNYLHWGEAKCWYGIPGSAASAFEKVMRKTLPDLFDAQPDLLFQLVTMLSPTVLQENKVPVYTVLQEPGNFVITFPKSFHAGFNFGLNCAEAVNFATADWLPYGGSGAELYRLYRKPSVISHEELLCVVAKGNCCNNEGSIHLKKELLRIYSKEKTWREQLWKSGILRSSPMFVPECADSVGIEEDPTCIICQQFLHLSAIVCNCRPSVFACLEHWKHLCECEPTKLRLEYRYTLAELDMMVQEVEKFGGCKTQETKISQRPSSGTKRSIALNKKEGMQVSQARPADKWLLRASKVLDAAFSSVEYATLLKESEQFLWAGSEMDRVRDVTKSLNKAKIWAEAVSDCLSKVEGEVNDDSMKVHLEFIDELLRVNPVPCFNSGYLKLKDYAEEARKLSEKIDSALSSSPTITQLELLHSEVSRSPISLKKHEILSKKISSAKMLAKRAKRYLTDAKPPGIEMDALFKLNSEMLELHVQLPETEGILDLVKKSESARDKSNKVLTGSLSLENVEELLHEFDSFSINVPELNILRQYHVDTLSWISRFNDVMVDVREGKDQRKLISDLSSLLRDGASLGIQVEGLPLVEVELKKASCREKARTVYTARKSLDFIEQLLSEAVILHIEEEEIFVEISGILSTARCWEERASTILENETQMYELKDLVRMSVNIDAVLPTLQGIENTISSAETWLQKSEPFLSATSSMASSPCSMLELPVLKDLVTQAKLLNVQLQEPRILETLLLNCERWQCDNHQLLQETEDLLDNAKIDDGTHSNILPKIMDLITRVDSARRSGLALGLNFDELPKLRTASLKLGWCCKTITLSSSSPTSELLEDVGKPSLQHIQQHLKEGQTLEILPEEYYLGKRLMELKDTGLEWAKRARKVVTDSGALALEDVFELISEGENLPVHAEQELQSLRARSMLHCICLKPYNSRSMVSCSQCGEWYHTYCLKLHWRPKAYVCSACCPLAETTPQIDPARATEPERPSLNQRRTRMVATDAAVNDLKWKTRKHIKRTTKRSPQVHILPWFFT
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Functions as histone H3 'Lys-4' (H3K4me) demethylase involved in the regulation of gene expression. Active on H3K4me1, H3K4me2 and H3K4me3. Repressor of the abscisic acid (ABA) signaling pathway, especially during stomatal closure regulation. Negative regulator of responses to dehydration stress by binding directly to the chromatin of SRK2E/OST1 and demethylating H3K4me3 to regulates its expression. Together with JMJ14 and JMJ16, required for plant growth and development.
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F4I2H7
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TPX2_ARATH
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Protein TPX2 (AtTPX2) (Targeting protein for XKLP2)
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MEATAEESVSTLVTTMVDETYEFLAPRWFDFVNGETEDESRRAELWFQSALSCAPSPSVPRIKARRSFKVEAMCNFNEAEEETLKDKEPLEPVVPIVSLQSQPSQAKKAEVAPSKASTVKPSRISSKDAEVNNKTVDASDPTTEPIEDKENIAPACTPKPPMQFSLGAKSVDLKKQQTARKIASLLKNPSTLRPKNQSQAKGSHQKSVKGETNLNNIASTTNLIQENQAIKRQKLDDGKSRQILNPKPATLLHKTRNGLVNTGFNLCPSVTKHTPKENRKVYVREQIAPFVSTAELMKKFQTSTRDLFVQNRPKLTLTRPKEPEFVTSQRARPLRVKSSAELEEEMLAKIPKFKARPVNKKILAAPALPAPQRSTPHLPEFQEFHLQTMARANQHAETSSIASTEVSKQHNDQKHHLTEPKSPVLQTMLRARPTIAKTTAELEQEELEKAPKFKAKPLNKKIFESKGEMGIFCNTKKHITIPQEFHFATDERISRPESVLDIFDKLSLNSESCHEKPLPRNTAPNPFNLKTEERGAEKEKKFYMELMYKKLGDVKARVPKANPYPYTTDYPVVPPKPEPKQCTQPEPFQLESLVRHEEEMRREREERRRMETEEAQKRLFKAQPVIKEDPIPVPEKVRMPLTEIQEFNLHVEHRAVERADFDHKIKEKENQYKRYREESEAAKMVEEERALKQMRKTMVPHARPVPNFNKPFLPQKSNKGTTKAKSPNLRVIKRTERRTMMARPTISAATSASAVHCLMYPGSSFNKLKKKTVLTNIVHCLMYPDSSLLN
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Regulates prospindle assembly during late prophase and at the onset of mitosis, before nuclear envelope breakdown (NEB). Is exported from the nucleus shortly before NEB and organized into two polar crescents. After NEB, is progressively associated with the forming spindle. Probably mediates AUR1 activation and localization to spindle microtubules. Has a microtubule binding capability and is able to trigger microtubule assembly induced by RanGTP in a heterologous system. Not involved in phragmoplast assembly, nuclear envelope reformation, and cortical microtubule assembly at the onset of G1. Involved in the formation of specific nuclear and perinuclear microtubular arrays in the nuclei of acentrosomal plant cells. Fungi and plants have acentrosomal microtubule arrays because they lack centrosomes. They use other microtubule organizing center (MTOC) structures to organize their microtubules. May function through interaction with importin.
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F4I2J8
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CATIN_ARATH
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Splicing factor Cactin
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MGSHGKGKRDRSGRQKKRRDESESGSESESYTSDSDGSDDLSPPRSSRRKKGSSSRRTRRRSSSDDSSDSDGGRKSKKRSSSKDYSEEKVTEYMSKKAQKKALRAAKKLKTQSVSGYSNDSNPFGDSNLTETFVWRKKIEKDVHRGVPLEEFSVKAEKRRHRERMTEVEKVKKRREERAVEKARHEEEMALLARERARAEFHDWEKKEEEFHFDQSKVRSEIRLREGRLKPIDVLCKHLDGSDDLDIELSEPYMVFKKKKVRIGIWLNFQLSITNVYVEAEYKNDSACLLLRSRVDILLNKGLTVKDMEELRDDIKMYLDLDRATPTRVQYWEALIVVCDWELAEARKRDALDRARVRGEEPPAELLAQERGLHAGVEADVRKLLDGKTHAELVELQLDIESQLRSGSAKVVEYWEAVLKRLEIYKAKACLKEIHAEMLRRHLHRLEQLSEGEDDVEVNPGLTRVVEENEEEINDTNLSDAEEAFSPEPVAEEEEADEAAEAAGSFSPELMHGDDREEAIDPEEDKKLLQMKRMIVLEKQKKRLKEAMDSKPAPVEDNLELKAMKAMGAMEEGDAIFGSNAEVNLDSEVYWWHDKYRPRKPKYFNRVHTGYEWNKYNQTHYDHDNPPPKIVQGYKFNIFYPDLVDKIKAPIYTIEKDGTSAETCMIRFHAGPPYEDIAFRIVNKEWEYSHKKGFKCTFERGILHLYFNFKRHRYRR
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Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (By similarity). Required for embryogenesis.
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F4I2N7
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RLK7_ARATH
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Receptor-like protein kinase 7 (EC 2.7.11.1)
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MAPSLRNFNFFHRFSTFLVFSLFSVVSSDDLQVLLKLKSSFADSNLAVFDSWKLNSGIGPCSFIGVTCNSRGNVTEIDLSRRGLSGNFPFDSVCEIQSLEKLSLGFNSLSGIIPSDLKNCTSLKYLDLGNNLFSGAFPEFSSLNQLQFLYLNNSAFSGVFPWKSLRNATSLVVLSLGDNPFDATADFPVEVVSLKKLSWLYLSNCSIAGKIPPAIGDLTELRNLEISDSGLTGEIPSEISKLTNLWQLELYNNSLTGKLPTGFGNLKNLTYLDASTNLLQGDLSELRSLTNLVSLQMFENEFSGEIPLEFGEFKDLVNLSLYTNKLTGSLPQGLGSLADFDFIDASENLLTGPIPPDMCKNGKMKALLLLQNNLTGSIPESYANCLTLQRFRVSENNLNGTVPAGLWGLPKLEIIDIEMNNFEGPITADIKNGKMLGALYLGFNKLSDELPEEIGDTESLTKVELNNNRFTGKIPSSIGKLKGLSSLKMQSNGFSGEIPDSIGSCSMLSDVNMAQNSISGEIPHTLGSLPTLNALNLSDNKLSGRIPESLSSLRLSLLDLSNNRLSGRIPLSLSSYNGSFNGNPGLCSTTIKSFNRCINPSRSHGDTRVFVLCIVFGLLILLASLVFFLYLKKTEKKEGRSLKHESWSIKSFRKMSFTEDDIIDSIKEENLIGRGGCGDVYRVVLGDGKEVAVKHIRCSSTQKNFSSAMPILTEREGRSKEFETEVQTLSSIRHLNVVKLYCSITSDDSSLLVYEYLPNGSLWDMLHSCKKSNLGWETRYDIALGAAKGLEYLHHGYERPVIHRDVKSSNILLDEFLKPRIADFGLAKILQASNGGPESTHVVAGTYGYIAPAEYGYASKVTEKCDVYSFGVVLMELVTGKKPIEAEFGESKDIVNWVSNNLKSKESVMEIVDKKIGEMYREDAVKMLRIAIICTARLPGLRPTMRSVVQMIEDAEPCRLMGIVISKESDVKVKEIS
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Plays a role in pattern-triggered immunity (PTI) signaling induced by pathogen-associated molecular patterns (PAMPs). Acts as a receptor for PIP1 defense peptide. PIP1 is an endogenous secreted peptide that acts as elicitor of immune response and positive regulator of defense response. Involved in the control of seed germination speed, in tolerance to oxidative stress and in maintaining seed longevity.
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F4I313
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SCY2A_ARATH
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SCY1-like protein 2 A (Inactive protein kinase SCYL2A)
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MSINMRTLTQALAKTAAVIEKTVQTTVQEVTGPKPLQDYELLDQIGSGGPGLAWKLYSAKARDSTRPQQYPTVCVWVLDKRALSEARARAGLSKAAEDAFLDLIRADSGKLVRLRHPGVVHVVQALDENKNAMAMVTEPLFASVANALGNVENVDNVPKDLKSMEMSLLEVKHGLLQIAETLNFLHNNAHLIHRAVSPENVFITSAGSWKLAGFGFAISQAQDGNLDNLQSFHYSEYDVEDSILPLQPSLNYTAPELVRSKTSSAGVSSDIFSFGCLTYHLVARKPLFDCHNNVKMYMNTLNYLTNETFSSIPSDLVSDLQRMLSMNESYRPTALDFTGSSFFRSDTRLRALRFLDHMLERDNMQKSEFLKALSDMWKDFDSRVLRYKVLPPLCAELRNLVMQPVILPMVLTIAESQDKNDFELTTLPALVPVLSTATGDTLLLLIKRAELIINKTNAEHLVSHVLPLLLRAYNDNDVRIQEEVLKRSTSVAKQLDGQVVRQAILPRVHGLALKTTVAAVRVNALLCLAELVQTLDKLAVTEILQTIQRCTAVDRSAPTLMCTLAIANAILKQYGVEFTSEHVLPLIIPLLTAQQLNVQQFAKYILFVKDILRKIEEKRGVTVNDSGVPEVKPGCVADGLQFQTPTKKTEKVASAAKNSPAWDEDWALPTKISAPRDPGPANSPQFNNSTVQSQSSNRTSVPTTCPAVDLEWPPRQSFNATAQPANDETRINAAGTPTTPSFDELDPFANWPPRPNSASTASGGFHNSTTTQPPINNSGSGLRNNLTDGRQFQTTNNDFWAFGNASLSSMKSQQETSGIRASNADPLTSFGIQNQNQGMPSFGSSSYGNQKPQADISSIFSSSRTEQSAMKLAPPPSIAVGRGRGRGRSGTSISKPNGSKQQQTEQPSLLDLL
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Probably inactive kinase. Component of the AP2-containing clathrin coat that regulates clathrin-dependent trafficking at plasma membrane, TGN and endosomal system. Together with SCYL2B, required for cell growth, plant growth and development.
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F4I316
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SUN3_ARATH
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SUN domain-containing protein 3 (AtSUN3)
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MQRSCRTRRRVSVNKFNGRNSFYKVSLSLVFLLWVLLFFSTLLISHGDGAKDEPLNDSMGMADPDDGQSDEKVVPFDGPLSLASASVDVTSDLSRNDDVNLSEESEDKEQEAEISSTVSGNDIESKDTYLLKQSEINKKDTGIDAGSKYDDFPKKSEINNTGTWNDTEGKDDNNFLKQSQLNKTGTGNDTESSDNEFLEQNQMNKTVLGNGTEINVSKVDQPSRAVPLGLDEFKSRASNSRNKSLSDQVSGVIHRMEPGGKEYNYASASKGAKVLSSNKEAKGAASILSRDNDKYLRNPCSTEGKFVVVELSEETLVNTIKIANFEHYSSNLKEFELQGTLVYPTDTWVHMGNFTASNVKHEQNFTLLEPKWVRYLKLNFISHYGSEFYCTLSLIEVYGVDAVERMLEDLISVQDNKNAYKPREGDSEHKEKPMQQIESLEGDDGADKSTHREKEKEAPPENMLAKTEASMAKSSNKLSEPVEEMRHHQPGSRMPGDTVLKILMQKLRSLDLNLSILERYLEELNLRYGNIFKEMDREAGVREKAIVALRLDLEGMKERQEGMVSEAEEMKEWRKRVEAEMEKAEKEKENIRQSLEQVSKRLEWMEKKCLTVFTVCLGFGIIAVIAVVIGMGTGLAEKTGSGAWLLLLISSTFIMFVLSL
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Encodes a member of the mid-SUN subfamily of SUN-domain proteins that is localized to both the nuclear envelope and the ER. It is involved in early seed development and nuclear morphology. [TAIR].
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F4I3P9
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MURE_ARATH
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE homolog, chloroplastic (AtMurE) (Protein ALBINO OR PALE-GREEN 13) (Protein PIGMENT DEFECTIVE EMBRYO 316)
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MAFTFLSPHPVFLSLTGTTSSFSYKPVLLPFSRNSRTLTVAAGPARRNSYPNPADDDPPEAPEDSMHGVSKFQQIQRQAARARKLEEEDFEKNRNTYLSAIADVEDAAETGRDDEESGGDLFSDIDRAISMKRSEFVKQGLLKPNPPKTASLKKIGEEGNEEEGDVTDDVDELDEEEVVDLDEIDKLTGLTEISDEEDWVDEEGNTRINKKKEFGSDHQFEFDLDDFGESKARIVEPKFKMCLAELLDESKVVPISVYGDLDVEITGIQHDSRGVSAGDLFVCCLGSENFLSEADKRGAVAVVASKEIDIEDTLGCRALVIVEDTNAVLAALASSFYRHPSKNMSVIGVTGTDGKTTTTYLIKSLYEAMGVRTGMFSTVSCYIHGDNKLDTPNATMNPDAVLVQSLMAKMLHNGTESLVMEASPQELALGKCDEVDFDIAVFTNLTRENTDFRGTDEEYRDAEAKLFSRMVDPERHRKVVNIDDPNAAFFVQQGNPNVPVVTFAMENTKADVHPLKFELSLFETQVLVNTPQGILEISSGLLGRHNIYNILAAVAVGIAVGAPLEDIVRGVEEVDAVPGRCELIDEEQAFGVIVDHANTPDGLSRLLDSIRELKPRRIITVIGCEGENERGKRPLMTKIATEKSDVTMLTSDNPRNEDPLDILDDMLSGIGWTMQEYLKHGEHDYYPPLANGHRLFLHDIRRVAVRCAVAMGEEGDMVVVAGKGHEAYQLEGEKKEFYDDREECREALQYVDELHQAGIDTSEFPWRLPESH
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Involved in chloroplast biogenesis. Required for thylakoid membrane development. Seems to be required for plastid-encoded plastid RNA polymerase (PEP)-dependent gene expression.
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F4I3V6
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SHW1_ARATH
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Protein SHORT HYPOCOTYL IN WHITE LIGHT 1
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MAAATTTLSSSSSSPSLTLINASHRFVSVTPFSSNSIFLRRRFRRLNRSLASSSSHSRRRYESDDRFFGGGDNYDVVPDDDGFSDDDDEEDERESSVDLLIRFLRSMFKKVSKRTKKASRRILPAAMSPRLVSFAVDGILLLGSLSITRAFLEVICNLGGTVFTVILLIRLFWAAASFFQTYGNSFGPNPVN
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Negative regulator of photomorphogenesis modulating both light and abscisic acid (ABA) signaling pathways. Regulates negatively the light-mediated inhibition of hypocotyl elongation, probably in a PHYB-mediated signaling pathway, but promotes flowering time (especially in long days) and lateral root formation. Enhances light-regulated gene expression. Promotes COP1-mediated degradation of HY5 during seedling development (e.g. hypocotyl growth) through enhanced ubiquitination in the darkness. Also involved in root gravitropism.
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F4I443
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BARD1_ARATH
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BRCA1-associated RING domain protein 1 (AtBARD1) (Protein REPRESSOR OF WUSCHEL 1)
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MAEFTNMLMNPWVLHLQKLELELKCPLCLKLLNRPVLLPCDHVFCDSCVHKSSQVESGCPVCKSKHPKKARRDLRFMESVISIYKSLNAAVSVHLPQLQIPNDCNYKNDALNNSNSPKHGESEDSEMTDKDVSKRSGGTDSSSRDGSPLPTSEESDPRPKHQDWTEKQLSDHLLLYEFESEYDAANHTPESYTEQAAKNVRDITASEQPSNAARKRICGDSFIQESSPNPKTQDPTLLRLMESLRSDDPTDYVKAQNHQQLPKSHTEQDSKRKRDITASDAMENHLKVPKRENNLMQKSADIDCNGKCSANSDDQLSEKISKALEQTSSNITICGFCQSARVSEATGEMLHYSRGRPVDGDDIFRSNVIHVHSACIEWAPQVYYEGDTVKNLKAELARGMKIKCTKCSLKGAALGCFVKSCRRSYHVPCAREISRCRWDYEDFLLLCPAHSSVKFPNEKSGHRVSRAEPLPKINPAELCSLEQTPAFTKELVLCGSALSKSDKKLMESLAVRFNATISRYWNPSVTHVIASTDEKGACTRTLKVLMGILNGKWIINAAWMKASLKASQPVDEEPFEIQIDTQGCQDGPKTARLRAETNKPKLFEGLKFYFFGDFYKGYKEDLQNLVKVAGGTILNTEDELGAESSNNVNDQRSSSIVVYNIDPPHGCALGEEVTIIWQRANDAEALASQTGSRLVGHTWVLESIAGYKLHPVIG
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Binds specifically to H3K4me3 regions of target genes (e.g. WUS and WOX5) promoters to repress their transcription via chromatin remodeling. Required for the shoot apical meristem (SAM) organization and maintenance, by confining WUS expression to the organizing center, and for the quiescent center (QC) development in the root apical meristem (RAM), by repressing WOX5 expression in the root proximal meristem. Plays a role in DNA repair and in cell-cycle control. Required for the repair of DNA double-strand breaks (DSBs), both natural and induced by genotoxic stress, by homologous recombination (HR).
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F4I460
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MYO8_ARATH
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Myosin-8 (Myosin XI B) (AtXIB)
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MVATFNPAVGSHVWVEDPDEAWLDGEVVEINGDQIKVLCASGKQVVVKDSNIYPKDVEAPASGVEDMTRLAYLHEPGVLQNLQSRYDINEIYTYTGSILIAVNPFRRLPHLYSSHMMTQYKGASLGELSPHPFAVADAAYRQMVNEGVSQSILVSGESGAGKTESTKLLMRYLAFMGGRGAATEGRTVEQKVLESNPVLEAFGNAKTVKNNNSSRFGKFVEIQFDQSGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEEDAKKFKLGDPKIYHYLNQSKCIQLDAMNDAEEYHATKKAMDVVGISSEEQDAIFRVVASILHLGNIEFAKGTEIDSSIPRDEKSWFHLKTAAELLMCNEKSLEDSLCKRIMATRDETITKTLDPEAALLSRDALAKVMYSRLFDWLVEKINTSIGQDPDSKYLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYKKEEINWSYIEFVDNQDILDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTYKNHKRFTKPKLARSDFTICHYAGDVTYQTELFLDKNKDYVIAEHQALLNASTCSFVANLFPPVSDDSKQSKFSSIGTRFKQQLVSLLEILNTTEPHYIRCIKPNNLLKPGIFENQNVLQQLRCGGVMEAIRISCAGYPTRKHFDEFLNRFGIIAPQVLDKNSNEPAACKKLLDKAGLEGYQIGKSKVFLRAGQMADLDTRRTEILGRSASIIQRKVRSYLAQKTFIQLRISATQIQAVCRGYLARSIYEGMRREAAALKIQRDLRKFLARKAYTELFSATILIQAGMRGMVSRKELCLRRQTKAATIIQTRCRVYLARLHYRKLKKAAITTQCAWRGKVARKELKNLKMAARETGALQEAKNKLEKQVEELTWRLQLEKRMRTDLEEAKKQENAKYESSLEEIQNKFKETEALLIKEREAAKTVSEVLPIIKEVPVVDQELMEKLTNENEKLKGMVSSLEIKIDETAKELHETARISQDRLKQALAAESKVAKLKTAMQRLEEKISDMETEKQIMLQQTILNTPVKSVAGHPPTATIKNLENGHRTNLENQFNEVEVNGNAGKSAAERQLENVDTLIDCVKENIGFSNGKPIAAFTIYKCLLHWKCFESEKTSAFDRLIEMIGSAIENEDDNGHLAYWLTNTSALLFLLQKSLKPAGAGATASKKPPITTSLFGRMALSFRSSPNLAAAAEAAALAVIRPVEAKYPALLFKQQLAAYVEKIFGMIRDNLKKELSALISMCIQAPRISKGGIQRSARSLGKDSPAIHWQSIIDGLNSLLAILKDNYVPLVLIQKIHTQTFSFVNVQLFNSLLLRKECCTFSNGEFVKSGLAELELWCGQVNEYAGPSWDELKHIRQAVGFLVIHQKYRVSYDDIVHDLCPILSVQQLYRICTLYWDDCYNTRSVSQEVISSMRALMTEESNDADSNSFLLDDNSSIPFSIDEISNSMHEKDFASVKPAKELLENPEFVFLH
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Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables.
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F4I4F2
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RHS3_ARATH
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Serine/threonine-protein kinase RHS3 (EC 2.7.11.1) (AGC serine/threonine-protein kinase subfamily 1 member 6) (Protein ROOT HAIR SPECIFIC 3)
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MLLKPGNKLVSPETSHHRDSASNSSNHKCQQQKPRKDKQKQVEQNTKKIEEHQIKSESTLLISNHNVNMSSQSNNSESTSTNNSSKPHTGGDIRWDAVNSLKSRGIKLGISDFRVLKRLGYGDIGSVYLVELKGANPTTYFAMKVMDKASLVSRNKLLRAQTEREILSQLDHPFLPTLYSHFETDKFYCLVMEFCSGGNLYSLRQKQPNKCFTEDAARFFASEVLLALEYLHMLGIVYRDLKPENVLVRDDGHIMLSDFDLSLRCSVNPTLVKSFNGGGTTGIIDDNAAVQGCYQPSAFFPRMLQSSKKNRKSKSDFDGSLPELMAEPTNVKSMSFVGTHEYLAPEIIKNEGHGSAVDWWTFGIFIYELLHGATPFKGQGNKATLYNVIGQPLRFPEYSQVSSTAKDLIKGLLVKEPQNRIAYKRGATEIKQHPFFEGVNWALIRGETPPHLPEPVDFSCYVKKEKESLPPAATEKKSKMFDEANKSGSDPDYIVFEYF
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Involved in root hair growth and morphogenesis.
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F4I4K5
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LPR1_ARATH
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Multicopper oxidase LPR1 (EC 1.-.-.-) (Protein LOW PHOSPHATE ROOT 1)
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MESLLCRRRIKRVMVLIIALTWLRSTCGELEDQLFEVGKLKMFVDDLPDMPRLYGFNSVHGIIKPASLQIGMFSTKWKFHRDLPATPVFAYGTSRSKATVPGPTIETVYGVDTYVTWRNHLPKSHILPWDPTISPATPKHGGIPTVVHLHGGIHEPTSDGNADAWFTAGFRETGPKWTKTTLHYENKQQPGNMWYHDHAMGLTRVNLLAGLVGAYILRHHAVESPFQLPTGDEFDRPLIIFDRSFRKDGSIYMNATGNNPSIHPQWQPEYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSNGLDFIVVGSDSAYLSKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANDAPYPYPSGDPVNEENGKVMKFIINNESEDDTCTIPKKLINYPNADVSNAVLTRYISMYEYVSNSDEPTHLLVNGLPYEAPVTETPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEQTALLAAGLEEFKECMTKQNDAVKCQISKYARGKKTAVTAHERGWKNVFKMMPGHVTRILVRFSYIHTNASYPFDPTQEPGYVYHCHILDHEDNMMMRPLKVII
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Multicopper oxidase that may be involved in copper homeostasis and oxidative stress response, and that is necessary for root growth inhibition by low phosphate conditions. Functions together with LPR2 and PDR2 in a common pathway that adjusts root meristem activity to phosphate availability. Oxidizes the substrate 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulphonate) in vitro.
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F4I562
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AP3M_ARATH
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AP-3 complex subunit mu (Adaptor protein complex AP-3 subunit mu) (Adaptor protein-3 mu-adaptin) (Adaptor-related protein complex 3 subunit mu) (At-muD-Ad) (Mu3-adaptin) (Protein ZIG SUPPRESSOR 4)
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MLQCIFLISDSGEVMLEKQLTGHRVDRSICAWFWDQYISQGDSFKALPVIASPTHYLFQIVRDGITFLACSQVEMPPLMAIEFLCRVADVLSEYLGGLNEDLIKDNFIIVYELLDEMIDNGFPLTTEPSILKEMIAPPNLVSKMLSVVTGNASNVSDTLPSGAGSCVPWRPTDPKYSSNEVYVDLVEEMDAIVNRDGELVKCEIYGEVQMNSQLTGFPDLTLSFANPSILEDMRFHPCVRYRPWESHQVLSFVPPDGEFKLMSYRVKKLKNTPVYVKPQITSDSGTCRISVLVGIRSDPGKTIESITLSFQLPHCVSSADLSSNHGTVTILSNKTCTWTIGRIPKDKTPCLSGTLALEPGLERLHVFPTFKLGFKIMGIALSGLRIEKLDLQTIPPRLYKGFRAQTRAGEFDVRL
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Part of the AP-3 complex, an adaptor-related complex which seems to be clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. It also functions in maintaining the identity of lytic vacuoles and in regulating the transition between storage and lytic vacuoles.
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F4I5N6
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RIC3_ARATH
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CRIB domain-containing protein RIC3 (ROP-interactive CRIB motif-containing protein 3) (Target of ROP protein RIC3)
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MATVKGLLKGLRYITQIFDEEKDKDMQIGFPTDVKHVAHIGSDGPATNVPSWMGDFKPQENENGQVVSRADANNNQIGEGVGLQELLPPTDKPKHKKTRRKSETVSQNGSPPRRNSSASASDMQPKNTRRHHRSRHGSIDSSNDPSVRRRRVVSVTTNDMEGSYPLSDSSTHSRKSTSRHRKPKGSGGGELSMKKTKGKTENPIVESVDTCNDNNISDKE
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Functions as downstream effector of Rho-related GTP binding proteins of the 'Rho of Plants' (ROPs) family. Participates in the propagation of ROP GTPase signals in specific cellular responses. Functions as downstream effector of ARAC11/ROP1 to activate calcium signaling that leads to F-actin disassembly associated with exocytosis in the tip of the growing pollen tube. Counteracts the ARAC11/ROP1-RIC4 pathway, which promotes apical F-actin assembly associated with vesicle accumulation, to control actin dynamics and pollen tube apical growth.
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F4I6G4
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JMJ18_ARATH
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Lysine-specific demethylase JMJ18 (EC 1.14.11.-) (Jumonji domain-containing protein 18) (AtJMJ18) (Protein JUMONJI 18) (Lysine-specific histone demethylase JMJ18) ([histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ18)
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MENPPLESEIKEDMSLKNHPPDKDKDKDTIMEQPSSPRHRKVVARWLPDEAQRPIINDAPVFTPSLEEFVDPLAYIEKIRPLAEPYGICRIIPPSTWKPPCRLKEKSIWEQTKFPTRIQTVDLLQNREPMKKKPKSRKRKRRRNSRMGSSKRRSGSSPAESTSSPEAEEKFGFNSGSDFTLDEFEKYALHFKDSYFEKKDSGGDIVKWTPSVDDIEGEYWRIVEQPTDEVEVYYGADLENGVLGSGFYKRAEKFTGSDMEQYTLSGWNLNNLPRLPGSVLSFEDCDISGVLVPWLYVGMCFSSFCWHVEDHHLYSLNYHHFGEPKVWYGVPGSNATALEKAMRKHLPDLFEEQPDLLHGLVTQFSPSILKDEGVQAYRVVQNSGEYVLTFPRAYHAGFNCGFNCAEAVNVAPVDWLAHGQNAVELYSKETRKTSLSHDKLLLGAAYEAVKALWELSASEGKENTTNLRWKSFCGKNGTLTNAIQARLQMEEGRITALGRDSSSLKKMEKDFDSNCERECFSCFYDLHLSASGCKCSPEEYACLKHADDLCSCDVKDGFILLRYTMDELSSLVRALEGESDDLKIWASKVLGIEHSDEDQTKTSSVISEEKKLKEGSFDLNIDLEMDYQEDVKEEASTSGGELTASENLGVSVEPINLGFLIFGKLWCNKYAIFPKGFRSRVKFYNVLDPTRMSNYISEVLDAGLMGPLFRVTLEESPDESFFNVSAQQCWEMVMRRVKDTSTSLGLPILPQFESINGLQMFGFLSPSIVQAIEALDPNHRLVEYWNHKNQTSSDSKDHFISSNCSASLTKGKLFGVDLM
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Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3 and H3K4me2. No activity on H3K9me3/2, H3K27me3/2 and H3K36me3/2. Involved in the control of flowering time by demethylating H3K4me3 at the FLC locus and repressing its expression. The repression of FLC level and reduction in H3K4me3 at the FLC locus results in induction of the flowering activator FT, which is a downstream target of FLC.
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F4I6M1
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POLIA_ARATH
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DNA polymerase I A, chloroplastic/mitochondrial (EC 2.7.7.7) (DNA polymerase PolI-like B) (AtPolI-like A) (Polymerase gamma 2) (POLGAMMA2)
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MAMGVSLTSHNNPLLRHLSPSSSWVSRSSSRLSSSPLPSFLFPCRRTLLQRKLASTDGNVGYCTTTVCQGFQHSVHQRSSSVVFNGEWELRSESNKVRMVPKIIKVGNQTEVAETHQVPGTVSAWREEANKLRERNGQIARNLDDNGYFNGSVPIISSAPSYETSQKIDYEFKPRGTTRSTTATLNKELIGITQSEPVVSLPRKGLDVGDNMDVNPKGEGIQRPLISDKSSGTANGNKNTVAISKVERSTEPSNVRENLGKIYDKVLIVDNVQAAKDTVAKLVNQFRNHVHSCDTEVSGIEVKEETPVDHGELICFSIYCGPEADFGNGKSCIWVDVLGENGREVLAEFKPYFEDSFIRKVWHNYSFDSHIIRNHGIEISGFHADTMHMARLWDSARRIKGGYSLEALTSDPKVLGGTQTKEEAEFLGKISMKTIFGKRKLKKDGSEGKIVVIPPVEELQREDREAWISYSALDAISTLKLYESMTKKLQLMDWHLDGKPVLGRTMLDFYHEFWRPFGELLVKMEAEGILVDREYLAEIEKVAKAEQQVAGSRFRNWASKYCPDAKYMNIGSDTQLRQLFFGGISNSHDEVLPVEKLFKVPNIDKVIEEGKKTPTKFRNIKLHRISDSPLSTENFTASGWPSVGGDVLKELAGKVSAEYDFMDDVSDISLEEVVEDDDVETSETQKSKTDDETDTSAYGTAYVAFGGGERGKEACHAIASLCEVCSIDSLISNFILPLQGSNVSGKDGRVHCSLNINTETGRLSARRPNLQNQPALEKDRYKIRKAFVASPGNTLVVADYGQLELRILAHLTGCKSMMEAFKAGGDFHSRTAMNMYPHVREAVENGQVILEWHPEPGEDKPPVPLLKDAFGSERRKAKMLNFSIAYGKTAVGLSRDWKVSTKEAQETVDLWYNDRQEVRKWQEMRKKEAIEDGYVLTLLGRSRRFPASKSRAQRNHIQRAAINTPVQGSAADVAMCAMLEISINQQLKKLGWRLLLQIHDEVILEGPIESAEIAKDIVVDCMSKPFNGRNILSVDLSVDAKCAQNWYAAK
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In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity (By similarity). Required for DNA replication and accumulation in plastids and mitochondria. May be required for DNA repair in both organelles. {ECO:0000250, ECO:0000269|PubMed:21427281, ECO:0000269|PubMed:23167278}.
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F4I718
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CSI3_ARATH
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Protein CELLULOSE SYNTHASE INTERACTIVE 3
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MLKAFLPGTQEEETLSSLQSGKVDAKMEMDDPEKAMATVAQLIEQLHAKTSSPQDKELTTARLLGIAKGKREARRLIGSYGQAMPLFISMLRNGTTLAKVNVASILCVLCKDKDLRLKVLLGGCIPPLLSVLKSGTMETRKAAAEAIYEVSSAGISNDHIGMKIFITEGVVPTLWDQLSLKGNQDKVVEGYVTGALRNLCGVDDGYWRLTLEGSGVDIVVSLLSSDNPNSQANAASLLARLVLSFCDSIQKILNSGVVKSLIQLLEQKNDINVRASAADALEALSANSDEAKKCVKDAGGVHALIEAIVAPSKECMQGKHGQSLQEHATGALANVFGGMRHLIIYLGQVSQSPRLTEPIGDVIGALAYALMIFKQPESSENIFDPSVIESILVKLLKPRDTKLIQERILEAMASLYGNSSLSCYLDDAEAKRVLIALITMASADVRERLIICLSGLCHDKVGIWEAIGKREGIQLFISFLGLSSEQHQEYAVEMLKILTAQVDDSKWAVTAAGGIPPLVQLLETGSQKAKEDAACILWNLCCHSEEIRDCVERAGGIPAFLWLLKTGGPNSQETSAKTLVKLVHTADPATINQLLALLLGDDPTSKIQVIEVLGHVLSKASQEDLVHRGCAANKGLRSLVESLTSSREETKEHTASVLADLFSSRQDICGHLATDDIINPWIKLLTNNTQNVAKQVARALDALSRPVKNNNNKKKSYIAEGDIKSLIKLAKNSSIESAENAVSALANLLSDPDIAAEALAEDVVSAFTRILADGSPEGKRNASRALHQLLKNFPVCDVLKGSAQCRFAILSLVDSLKSIDVDSADAFNILEVVALLAKTKSGVNFSYPPWIALAEVPSSLETLVQCLAEGHTLVQDKAIEVLSRLCSDQQFLLSELIVSRPKSMLVLADRIVNASSLEVRVGSTALLLCAAKEKKQLITETLDQSGFLKLLLHALVDMIKHNSTSFSLETEVQTPKGFLEKNVFQDTGSFYFPDPAKILGGTVALWLLCILTSVDAKSKVIVMEAGGLEVLVGKLARYTSSAQAEFEDTEGIWISALLLAIMFQDDNVSFSSTTMRIIPTLAVLLGSDELIDRYFAAHAMASLVCTRNRGINLTIANSGAVSGIINLLGYVESEILNLVALANEFSLVKEPDQVILQHLFEIEDVRLGSTARKSIPLLVDLLRPIPDRPGAPQFAVQILIRIADGSDTNKLLMAEAGAVEALTKYLSLSPQDSTEYAISELLRVLFSNHELRQNEMALSSLNQLIAVLRLGSRSARYSAAGALNELFDAENIRNSEIACQAVQPLMDILGSVSESEQEVALSALIKLSSGNTSNTALLIDVEGSLLENVIKILSSATASEELKINAARLCSVVFSNKNIRTSASASGCMKPLITLMQSERSAAVEAAVFAIKILLDDEQHLELAAAHNIQELLVGLVSGKNYVIIEASLSALIKLGKDRVPRKLDMVEAGIIERCLELLPGASSSLCSAVVELFRILTNSGVIARRPDVAKTVEPLFAVLLRSDLTLWGQHSALQALVNILEKQQTLEAFSFTPSEAIVPLISFLESSSQAIQQLGAELLSHFLTMEDFQQDITTQSAVVPLVRLAGIGILSLQETAIKALEKISASWPKAVLDAEGIFELSKVILQEDPQPPLDLWESAAFVLSNILQYDAECFFRVELPVLVKLLFSTIESTVLLALKALMLHEKNDASSTVQMAELGAIDALLDLLRSHQCEEESGSLLEVIFNNPRVRELKLCKYAIAPLSQYLLDPHTRSEPGRLLAALALGDLSQHEGLSRSSGSVSACRALISVLEEQPTEEMKVVAICALQNFVMNSRTNRRAVAEAGGVLLIQELLLSCNPEVSGQAALMVKFLFSNHTLQEYVSNELIRSLTAALERGLWSTATINIEVLRTLNVIFSNFPKLRASEAATFCIPHLVGALKSGVEDVQGLVLDILYLLRHSWTNMSIDVAKSQAMIAAEAIPVLQMLMKTCPPRFHDKADSLLHCLPGCLTVNVMRANNLKQSMATTNAFCQLTIGNCPPRQTKVVSNSTTPEWKEGFTWAFDVPPKGQKLHIICKSKSTFGKTTLGRVTIQIDKVVTEGEYSGSLSLNHENSKDASSRSLDIEIAWSNRTTDETH
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Regulator of the microtubular cytoskeleton (By similarity). Microtubule-associated protein involved in the association of cellulase synthase (CESA) complexes (CSCs) and cortical microtubules. Promotes dynamics of CSCs in the plasma membrane in both microtubules-dependent and microtubules-independent manners. Regulates primary cell wall biosynthesis and cellulose microfibrils organization.
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F4I735
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PDS5B_ARATH
|
Sister chromatid cohesion protein PDS5 homolog B (Precocious dissociation of sisters protein 5-B) (AtPDS5B)
|
MEKTPTQIVSELCSRLLQLSRPNKDSLVKLLREVANTLSKIDQPSATNKEKGLKLIEAELRPLKKSIIKHALLKNRDNDVSLLVTVCVSELFRILAPHLPFEDEYLRDIFTLFIAEFSELSDTVSPYFSKRAKILETVSRLKFCLLMLDEDCQDLVHEMFNMFFSLVREHHQQSLINQKSMKTQQRKANTQQTQHSLFNNILAIMSDVLEEEANSSFVVVILENLVKEGEDTTSGADKLASSLIERCADRLEPLICSFLTSCFMEKDSIQTNLKDSYHEIIFKISLIAPQMLLAVIPKLTQELLTDQVDVRIKALNLAGRIFAQPKHCLSSYVETYQDLYAEFLRRFSDKSAEVRMAALKCGKQCYFANPSGNKASGVLTAIQERLLDFDDRVRTQALIVACDIMKFNMKYVPLNLISEASERLRDKKISVRKKALQKLTEVYQDYCDKCSEGDMTITDNFEQIPCKILLLCCEKNCEEFRSQNLELVLSDDLFPRLLPVEERMRHWVQCFAIMNHIHLKSLNSILSQKRRLQNELRHCLTLWRKAKVDNIEEAQRKKKSYFVKLSACFPDASEAEDLFEKLDRMRDASIFDVLTLLLEELSSTNAQIIKEKFLKMIGVKHSLFEFLRILSTKCSPSIFSSEHVQCLLNQLCGSTSANTQLKAPSIKLLLVILNMFPSYLRGSEKQFLKLLEENDSAADELIVVLSKAAPYISVNFGDYYPVLEKVCLEGTRSQTKCAVSAISSLAGSSEKSVFSELCEMLMDSLLCGRNIPTTLQSLACVGQYSVLEYDNIYEDITSYIYRVFQAEPSDNQLPCDQSSGCCNSCKLKIYGLKTLVKSFLPRHGQVVRKIDDLLNILKKTLKSQGHDGIKSCEDTGANVRLAAAKAVLLLSRKWDLHISPEVFRLTILMAKDSNAFITKTFLTKLYKLLTEHMIPSRYACAFSFSLSSPCRDLHDDSFRYINGFINKATRESRTCRDLDQGESLTDSPVYMTVFLIHVLAHDPEFPSEDCRDEHIYARFCGPLFSVLQVLLSINNNGFTIKETAPFLFCIFRAIKRAEDAVDSRKTPRLHILADIGYSAVNILNSIVVTSPQAPRSILLPSSLYSLTSITDNQNKAKSRTRNALEQSFIERIVHIFQSQISMHDQRCQKDSLAVGSEDKVLPPLLGNQIETSITGSTEASQNNTRCSRKRTHLGEHISCNSLSLRTVESEIPIKKLERHTTCAKESVKASVSNKITSSKHSGVVSALKDISNHGEAIIGQRIKLLSPTDGCFYPGTVEKFNSKSNSHKIIFDNGDVELVCLDSESWETLSHESMGQQERLGKETESYGSRNCVPEISHTLAKVTAQKQTTTTKQQNKKVPAKLNPPAVPCFMMSAKSKKGNSDSGEGSVSEVTDTSDNIGPRRSRRQRIS
|
Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex. Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication (By similarity). Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for proximal-distal cell cycle-driven leaf growth in both lamina and petiole.
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F4I7C7
|
WAPL1_ARATH
|
Wings apart-like protein 1 (AtWAPL1)
|
MIIVKLTANRICCSLLQLRRSYEHFYIFVFLPEIPLFRFSHLKLFPKNLQIQRLVSAMMERTYGRRKPGIPRTLSDSLNDSVSQTEYLSSSSSPDIEPIDYSLLPFSSQESSSLWHSSSRSNFREDYPQNGGVVRRAKRVRNGAEAAAFTSTLLEAQEFGELMEHEDEVNFALDGLRKGHQLRIRRASLSSLLSICASQHQRRSLRAQGISQSIIDAILVLSLDDIPSNLAAATLFFALTADGQDEHFMESPKCIKFLIKLLKPVIVTSTEGKPRNIGFKLLSLLKDVDAARDPVKMDDPSSSDILSRVQELLVNCKEMRLNDSYITETTRPELSTKWVALLAMERACVSKISFDDTSGSVKKTGGNFKEKLRELGGLDAVLEVVMDCHAVMERWVEYDALSVQEKKDNLHKQSLMLLLKCLKIMENATFLSTDNQNHLLGFKKCLGSHDSRMSFTELTISVIKMLSGLHLRGGFSSPNTNNVNSHYSNGGNHDSVLEANRKVTNEVVTISSDTYSTVGSISTRNGSVSQRSQSIIHLDFSPTSMSGSQSSVSGNEPTTSKTRVGSTISGSFAGRLASLGSDIARTTLRTTQAGEPICKKFGEFAPPEESEDPFAFDLEDYKPSKWAVVSVNQKKSRAQKKKGCYKQSKDESLYQLFSSQEESSNHRLNSQEESSNRDCSTSLQPSHCTNDIDEECLCLLFDCLLTAVKVLMNLTNDNVVGCRQVGGCRGLESMAELIARHFPSFTRSQLFSEMEKTGSSHQKKDKYLTDQELDFLVAILGLLVNLVERDGVNRSRLASASVPITKPEELQESEQEMIPLLCSIFLTNQGSAETKEETTTFTLDDEEAVLEGEKEAEKMIVEAYSALLLAFLSTESRSIRNSIKDYLPKRNLAILVPVLERFVAFHMTLNMIPPETHKAVMGVIESCKSP
|
Regulator of sister chromatid cohesion in meiosis which negatively regulates cohesin association with chromatin, acting as an antagonist of CTF7. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair (By similarity). Essential for the prophase removal of cohesin during meiosis thus determining the timely release of meiotic cohesion. Important for proper spindle attachment and assembly during meiosis. Helps to prevent abnormal centromere association during prophase I in meiocytes. Required for early embryonic patterning. Also involved in chromosome segregation during mitosis.
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F4I7I0
|
ALAT1_ARATH
|
Alanine aminotransferase 1, mitochondrial (AtAlaAT1) (AtAlaATc) (EC 2.6.1.2) (Alanine-2-oxoglutarate aminotransferase 4) (EC 2.6.1.-)
|
MRRFVIGQAKNLIDQSRRRQLHHHKNLSFVSLIPPFSAPSDSSSRHLSSSSSSDMSASDSSSSLPVTLDTINPKVIKCEYAVRGEIVNIAQKLQEDLKTNKDAYPFDEIIYCNIGNPQSLGQQPITFFREVLALCSYTALLDESATHGLFSSDSIERAWKILDQIPGRATGAYSHSQGIKGLRDAIADGIEARDGFPADPNDIFMTDGASPGVHMMMQLLITSEKDGILCPIPQYPLYSASIALHGGTLVPYYLDEASGWGLEISELKKQLEDARSKGITVRALAVINPGNPTGQVLSEENQRDVVKFCKQEGLVLLADEVYQENVYVPDKKFHSFKKVARSMGYGEKDLALVSFQSVSKGYYGECGKRGGYMEVTGFTSDVREQIYKMASVNLCSNISGQILASLIMSPPKPGDDSYESYIAEKDGILSSLARRAKTLEEALNKLEGVTCNRAEGAMYLFPCLHLPQKAIAAAEAEKTAPDNFYCKRLLKATGIVVVPGSGFRQVPGTWHFRCTILPQEDKIPAIVDRLTAFHQSFMDEFRD
|
Is the major alanine aminotransferase in roots that catalyzes the conversion of alanine to pyruvate. Involved in the rapid conversion of alanine to pyruvate during recovery from low-oxygen stress.
|
F4I7Y4
|
BSK11_ARATH
|
Serine/threonine-protein kinase BSK11 (EC 2.7.11.1) (Brassinosteroid-signaling kinase 11)
|
MGCCQSSFLKPSSLHDKKITSDDLSGRRGKGAKRGNRHRHANINEGRGWHFSDVPDFSEFSASVLRDATNNFNKNAVVSVCSDQEPNLVYQGCIRSDKDKRLIAVKKFSKTTWPDPKQFATEARAIGSLRHVRLVNLIGYCCEGDERLLVSEYMPNESLTKHLFHWEKQTMEWAMRLRVALYVAEALEYCRQSGLKLYHDLNTCRVLFDENGSPRLSCFGWMKNSKDGKNFSTNLAYTPPEYLRSGTLIPESVVFSFGTFLLDLLSGKHIPPSHAVGTIQKQNLNVLMDSHLEGNYPEEDAAMVFDLASKCLHNNPNERPEIGDIISVITTLQQKLDVPSYTMLGISKLEKLEMEHPKSLIYDACHQMDLAALHQILEAMEYKEDEVTCELSFQQWAQQIKDVCNTRQQGDSAFRNKHFESAIDKYTQFIEIGIMISPTVYARRSMCYLFCDQPDAALRDAMQAQCVYSDWPTAFYLQAVALSKLNMVEDSATMLKEALILEDKRGS
|
Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1.
|
F4I893
|
ILA_ARATH
|
Protein ILITYHIA
|
MSYSMVNASSAVSSPETAKNSDEPPPISSEAVNVLFPSVDPNSKLFRNSLNITISREAPPLTTSRIDFLSLFIFCKLTHWLSLNPSSHRDEEEEEASPFYPFTIVLTYQPGPGQSPWKEMASPLESLLSISGSVSTSSTLIRLRIFRHDIPEILQNSDMTSDIAPVIVDMIFQTLAIYDDRASRKAVDDLIVKGLGNVTFMKTFAAMLVQVMEKQLKFCFDTVCYRLLIWSCLLLEKSQFATVSKNAFVRVASTQASLLRIIMESSFRMRRACKRFMFHLFSQSQAIYSLYMDEVKGSRIPYKDSPELLGLLLEFSCSSPALFEQSKAIFVDIYVKDVLNSREKQKPNLSNCFKPLLQRLSHEEFQTVILPAAVKMLKRNPEIVLESVGFLLANVNIDLSKYALELLPVILPQARHTDEDRRLGALSMVMCLSEKSSNPDTIEAMFASVKAIIGGSEGRLQSPHQRIGMLNAVQELASAPEGKYIGSLSRTICSFLIACYKDEGNEDVKLSILSAVASWASRSSVAIQPNLVSFIAAGLKEKEALRRGHLRCVRIICRNPDTISQISDLLSPLIQLVKTGFTKAVQRLDGIYALLIVSKIAACDIKAEDTMVKEKLWTLISQNEPSLVQITLASKLSSDDCVVCVDLLEVLLVEHSSRVLEAFSLKSLSQLLLFLLCHPSWNVRKTAYNSVTKIFLATSQLATTLLDEFSDFLSITGDQIVSSRTSDADNPADHQAPFVPSVEVLVKALIVISSAAVAGPPSSWIVRAIFCSHHPSIVGTGKRDAVWKRLQKCLKTCGFDVATFLSTNGESVCKSLLGPMGLTSAKTPEQQAAVYSLSTMMSLAPEDTFTVFKMHLQDLPDRLSHDMLSETDIKIFHTPEGMLLSEQGVYVAQTIGAKYTKQEPSSNHSLKKGLASRETANSGRRDTAKLTKKADKGKTAKEEARELMLKEEASTRENVHRIQKSLSLVLHALGEMGLANPVFCHSQLPFLATFLDPLLRSPIVSAAAFENLVKLARCTVQPLCNWALEISTALRLIAIDEVDTSFDFRPSVDKAGKTYEGLFERIVNGLSISCKSGPLPVDTFTFIFPVLYHVLGVVPAYQASVGPALNELCLGLQADDVANALYGVYSKDVHVRLACLNAVKCIPAVSKCSLPQNVKIATNIWIALHDPEKSVAESADDLWARYGHDLGTDYSGIFKALSHINLNVRLAAAEALADALHESPSSIQLSLSTLFSLYIRDATSGEDVFDAGWIGRQGIALALQSAADVLTTKDLPAVMTFLISRALADPNTDVRGKMINAGIMIIDKHGKENVSLLFPIFENYLNKEASDEEEYDLVREGVVIFTGALAKHLARDDPKVHNVVEKLLEVLNTPSESVQRAVSTCLSPLVLSKQEEAPALFLRLLDKLMKSDKYGERRGAAFGLAGVVMGFGISSLKKYGLIVTLQEALIDRNSAKRREGALLAFECLCEKLGKLFEPYVIKMLPLLLVSFSDQVGAVREAAECAARAMMSQLSAYGVKLVLPSLLKGLEDKAWRTKQSSVQLLGAMAFCAPQQLSQCLPRVVPKLTEVFKTIQVLTDTHPKVQSAGQLALQQVGSVIKNPEISSLVPTLLLALTDPNEYTRHALDTLLQTTFVNSVDAPSLALLVPIVHRGLRERSSETKKKASQIVGNMCSLVTEPKDMIPYIGLLLPEVKKVLVDPIPEVRSVAARAVGSLIRGMGEDNFPDLVPWLFETLKSDTSNVERYGAAQGLSEVIAALGTDYFENILPDLIRHCSHQKASVRDGYLTLFKFLPRSLGAQFQKYLQLVLPAILDGLADENESVRDAALGAGHVLVEHHATTSLPLLLPAVEDGIFNDNWRIRQSSVELLGDLLFKVAGTSGKALLEGGSDDEGASTEAQGRAIIDILGMDKRNEVLAALYMVRTDVSLSVRQAALHVWKTIVANTPKTLKEIMPILMSTLISSLASPSSERRQVAGRSLGELVRKLGERVLPLIIPILSKGLKDPDVDKRQGVCIGLNEVMASAGRSQLLSFMDQLIPTIRTALCDSALEVRESAGLAFSTLYKSAGLQAMDEIIPTLLEALEDDEMSTTALDGLKQIISVRTAAVLPHILPKLVHLPLSALNAHALGALAEVAGAGFNTHLGTILPALLSAMGGENKEVQELAQEAAERVVLVIDEEGVETLLSELLKGVSDSQASIRRSSAYLIGYFFKSSKLYLIDEAPNMISTLIVMLSDSDSTTVAVSWEALARVIGSVPKEVLPSYIKLVRDAVSTARDKERRKRKGGYVVIPGLCLPKSLKPLLPVFLQGLISGSAELREQAAIGLGELIEVTSEQALKEFVIPITGPLIRIIGDRFPWQVKSAILATLIILIQRGGMALKPFLPQLQTTFVKCLQDSTRTIRSSAAVALGKLSALSTRIDPLVGDLMTSFQAADSGVREAILSAMRGVIKHAGKSIGPAVRVRIFDLLKDLMHHEDDQVRISATSMLGVLSQYLEAAQLSVLLQEVNDLSASQNWGARHGSVLCISSLLKHNPSTIMTSSLFSSMLNSLKSSLKDEKFPLRESSTKALGRLLLKQLATDPSNTKVVIDVLSSIVSALHDDSSEVRRRALSSLKAFAKDNPSATMANISVIGPPLAECLKDGNTPVRLAAERCALHVFQLTKGAENVQAAQKYITGLDARRLSKFPEQSDDSESDDDNVSG
|
Involved in immunity against bacterial infection and in non-host resistance. Required for embryo development. Required for systemic acquired resistance, but functions in an salicylic acid-independent manner. Required for bacterium-triggered stomatal closure response.
|
F4I8I0
|
SUN4_ARATH
|
SUN domain-containing protein 4 (AtSUN4)
|
MQRSRRALLVRRRVSETTSNGRNRFYKVSLSLVFLIWGLVFLSTLWISHVDGDKGRSLVDSVEKGEPDDERADETAESVDATSLESTSVHSNPGLSSDVDIAAAGESKGSETILKQLEVDNTIVIVGNVTESKDNVPMKQSEINNNTVPGNDTETTGSKLDQLSRAVPLGLDEFKSRASNSRDKSLSGQVTGVIHRMEPGGKEYNYAAASKGAKVLSSNKEAKGASSIICRDKDKYLRNPCSTEGKFVVIELSEETLVNTIKIANFEHYSSNLKDFEILGTLVYPTDTWVHLGNFTALNMKHEQNFTFADPKWVRYLKLNLLSHYGSEFYCTLSLLEVYGVDAVERMLEDLISIQDKNILKLQEGDTEQKEKKTMQAKESFESDEDKSKQKEKEQEASPENAVVKDEVSLEKRKLPDPVEEIKHQPGSRMPGDTVLKILMQKIRSLDVSLSVLESYLEERSLKYGMIFKEMDLEASKREKEVETMRLEVEGMKEREENTKKEAMEMRKWRMRVETELEKAENEKEKVKERLEQVLERLEWMEKKGVVVFTICVGFGTIAVVAVVFGMGIVRAEKQGGLAWLLLLISSTFVMFILSL
|
Encodes a member of the mid-SUN subfamily of SUN-domain proteins that is localized to both the nuclear envelope and the ER. It is involved in early seed development and nuclear morphology. [TAIR].
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F4I902
|
CHS1_ARATH
|
Disease resistance protein CHS1 (EC 3.2.2.6) (Protein CHILLING SENSITIVE 1)
|
MSTSYSFLLAGRELDVFLSFSGKIALDVDFGYDLSRNGIKAFKSESWKESSFKPIDLRTLEALTESKVAVVMTSDEEVSSVGFLEELIVIIEFQEKRSLTVIPVFLTKHPLDVEKVSQIFPERAKIWRTAIAKLDNIAAQYSFSRNLAVMHGTHRIKQIADDIRLMFLSSASSDFKGLAGMDRHMKALYALLALESDEKVRTIGIWGSSGVGKTTLARYTYAEISVKFQAHVFLENVENMKEMLLPSENFEGEDLRSVNHEMNEMAEAKQKHRKVLLIADGVNNIEQGKWIAENANWFAPGSRVILITQEKSLLVQSGVNHVYEVGSLRYDEALQLFSRFAFKQPYPSPDFERLSVRAVQLAGFLPVTIRLFGSFLTGRDKEEWEATLLKLNAKQGKDIKEVWKIMEALEDKDIVEASQR
|
Confers resistance to low temperatures by limiting chloroplast damage and cell death, thus maintaining growth homeostasis. Regulates steryl-esters and sterols accumulation. Limits leaf necrosis associated with virulent bacterial infection (e.g. Pseudomonas syringae pv. tomato DC3000).
|
F4I907
|
GLYR2_ARATH
|
Glyoxylate/succinic semialdehyde reductase 2, chloroplastic (AtGLYR2) (AtGR2) (SSA reductase 2) (EC 1.1.1.79) (EC 1.1.1.n11)
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MPLVSLSFASSSSKAMALCSICPRIPLRFRPKPISPFLSKPQICLAYRVYSSLQSTTPSTRDELGTVSIGFLGMGIMGSPMAQNLIKAGCDVTVWNRTKSKCDPLVGLGAKYKSSPEEVTATCDLTFAMLADPESAIDVACGKNGAIFGISSGKGYVDVSTVDVASSILISKQIKDTGALFLEAPVSGSKKPAEDGQLIFLTAGDKPLYEKAAPFLDIMGKSKFYLGEVGNGAAMKLVVNMIMGSMMASFAEGILLSQKVGLDPNVLVEVVSQGAINAPMYSLKGPSMIKSVYPTAFPLKHQQKDMRLALGLAESVSQSTPIAAAANELYKVAKSYGLSDEDFSAVIEALKAAKSREA
|
Catalyzes the NADPH-dependent reduction of glyoxylate to glycolate as well as succinic semialdehyde (SSA) to gamma-hydroxybutyrate in vitro. May function in redox homeostasis and play a role in oxidative stress tolerance by detoxifying glyoxylate and SSA generated in glycolate metabolism and GABA metabolism, respectively.
|
F4I9A2
|
TNO1_ARATH
|
Trans-Golgi network-localized SYP41-interacting protein 1 (TGN-localized SYP41-interacting protein 1)
|
MHEKDDLPQDSIADGIENDDESNGQEEEELDPDQGTAFVDSKEDMFVDAPEELNFDTPSKEALTTDDDDNDDLGTHFNIEKGDWEKELAGLQEQFKLLTGENDLTGEDGNTTVDIVSRFSKFLKTAKEERIQHEVALKELHGVISGRDDEIADLTTKISELSSSQPVSEMGDQAQNLEHLEAATDRIMVSLSNVFGEGELQYGSSISEKLAHLENRVSFLGAKYTEFYYGADQLRKCLASDVLDLSFQEDFGSALGAACSELFELKQKEAAFFERLSHLEDENRNFVEQVNREKEMCESMRTEFEKLKAELELEKTKCTNTKEKLSMAVTKGKALVQNRDALKHQLSEKTTELANRLTELQEKEIALESSEVMKGQLEQSLTEKTDELEKCYAELNDRSVSLEAYELTKKELEQSLAEKTKELEECLTKLQEMSTALDQSELDKGELAKSDAMVASYQEMLSVRNSIIENIETILSNIYTPEEGHSFDIVEKVRSLAEERKELTNVSQEYNRLKDLIVSIDLPEEMSQSSLESRLAWLRESFLQGKDEVNALQNRIESVSMSLSAEMEEKSNIRKELDDLSFSLKKMEETAERGSLEREEIVRRLVETSGLMTEGVEDHTSSDINLLVDRSFDKIEKQIRDSSDSSYGNEEIFEAFQSLLYVRDLEFSLCKEMLGEGELISFQVSNLSDELKIASQELAFVKEEKIALEKDLERSEEKSALLRDKLSMAIKKGKGLVQDREKFKTQLDEKKSEIEKLMLELQQLGGTVDGYKNQIDMLSRDLERTKELETELVATKEERDQLQQSLSLIDTLLQKVMKSVEIIALPVDLASEDPSEKIDRLAGYIQEVQLARVEEQEEIEKVKSEVDALTSKLAETQTALKLVEDALSTAEDNISRLTEENRNVQAAKENAELELQKAVADASSVASELDEVLATKSTLEAALMQAERNISDIISEKEEAQGRTATAEMEQEMLQKEASIQKNKLTEAHSTINSLEETLAQTESNMDSLSKQIEDDKVLTTSLKNELEKLKIEAEFERNKMAEASLTIVSHEEALMKAENSLSALQGEMVKAEGEISTLSSKLNVCMEELAGSSGNSQSKSLEIITHLDNLQMLLKDGGLISKVNEFLQRKFKSLRDVDVIARDITRNIGENGLLAGEMGNAEDDSTEAKSLLSDLDNSVNTEPENSQGSAADEDEISSSLRKMAEGVRLRNKTLENNFEGFSTSIDTLIATLMQNMTAARADVLNIVGHNSSLEEQVRSVENIVREQENTISALQKDLSSLISACGAAARELQLEVKNNLLELVQFQENENGGEMESTEDPQELHVSECAQRIKELSSAAEKACATLKLFETTNNAAATVIRDMENRLTEASVALEKAVLERDLNQTKVSSSEAKVESLEELCQDLKLQLENLRVKEEKWHEKEVELSTLYDKLLVQEQEAKENLIPASDMRTLFDKINGIEVPSVDLVNGLDPQSPYDVKKLFAIVDSVTEMQHQIDILSYGQKELNSTLAEKDLEIQGLKKATEAESTTELELVKAKNELSKLISGLEKLLGILASNNPVVDPNFSESWTLVQALEKKITSLLLESESSKSRAQELGLKLAGSEKLVDKLSLRVKEFEEKLQTKAIQPDIVQERSIFETPRAPSTSEISEIEDKGALGIKSISPVPTAAQVRTVRKGSTDHLSINIDSESEHLMNNNETDEDKGHVFKSLNMSGLIPTQGKIIADRVDGIWVSGGRVLMSRPQARLGVMVYSLLLHLWLLASIL
|
Tethering factor involved in vesicle fusion at the trans-Golgi network (TGN) thus being required for efficient protein trafficking to the vacuole. Implicated in resistance to salt and osmotic stresses. Modulates the cell morphology (e.g. epidermal cell file rotation (CFR) and cell expansion) in mature regions of roots and the base of hypocotyls as well as root skewing, a process leading to root movement within the soil in order to maximize anchorage and nutrient acquisition, probably by regulating microtubule stabilization independently of their orientation.
|
F4I9G2
|
ESV1_ARATH
|
Protein EARLY STARVATION 1, chloroplastic (AtESV1) (Protein REDUCED GRAVITROPIC 1)
|
MSEMAASSAISLLDIKLRRFGVGASNHELRLTKWFKGDQAGAPTRRFTCFADMLAPIRRSEKSEERRFDQKMSAHGAGIKTSSSAVPFASPKSRFLSKQEKFYPRCTPRLTGPQSRDTPPKRDTGIANEKDWGIDLLNENVNEAGTNEDGSSWFRESGHDLGDNGYRCRWSRMGGRSHDGSSEWTETWWEKSDWTGYKELGVEKSGKNSEGDSWWETWQEVLHQDEWSNLARIERSAQKQAKSGTENAGWYEKWWEKYDAKGWTEKGAHKYGRLNEQSWWEKWGEHYDGRGSVLKWTDKWAETELGTKWGDKWEEKFFSGIGSRQGETWHVSPNSDRWSRTWGEEHFGNGKVHKYGKSTTGESWDIVVDEETYYEAEPHYGWADVVGDSTQLLSIQPRERPPGVYPNLEFGPSPPPEPDLPPDQPQ
|
Binds preferentially to highly ordered alpha-glucans, such as starch and crystalline maltodextrins. Involved in the organization of the starch granule matrix, thus influencing starch turnover by modulating the accessibility of starch polymers to modifying and degrading enzymes involved in phosphorylation, hydrolyzes and synthesis, including starch synthases (SSI and SSIII), starch phosphorylases (PHS1), isoamylase, beta-amylase, glucan water dikinase (GWD) and phosphoglucan water dikinase (PWD). Prevents GWD- and PWD-mediated starch phosphorylation, and subsequent degradation. Required for the control of starch degradation in leaves and starch distribution in nonphotosynthetic parts (e.g. cells immediately adjacent to veins, columella cells of root caps, stems, flowers and siliques) by limiting the hasty depletion of starch reserves during the night. Promotes gravitropic responses, negative in shoots but positive in roots, by maintaining starch granules (statoliths) accumulation in hypocotyls and roots columella, especially in dark conditions and in the endodermis, where starch is formed from transported glucose-6-phosphates.
|
F4I9J7
|
Y14_ARATH
|
RNA-binding protein Y14 (AtY14) (RNA-binding protein 8A)
|
MANIESEAVDFEPEEDDLMDEEGTAIDGADVSPRAGHPRLKSAIAGANGESAKKTKGRGFREEKDSDRQRRLSSRDFESLGSDGRPGPQRSVEGWIILVSGVHEETQEEDITNAFGDFGEIKNLNLNLDRRSGYVKGYALIEYEKKEEAQSAISAMNGAELLTQNVSVDWAFSSGPSGGESYRRKNSRYGRSQRSRSPRRRY
|
Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGO-Y14 heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGO-Y14 heterodimer interacts with the EJC key regulator PYM leading to EJC disassembly in the cytoplasm (By similarity). Can increase in vitro the expression from reporter constructs that contain leader introns required for the expression of different genes. In association with MAGO and PYM, participates in intron-mediated enhancement of gene expression. The MAGO-Y14 heterodimer works synergistically with the NMD pathway to regulate male gametophyte development.
|
F4IAG2
|
SSY3_ARATH
|
Starch synthase 3, chloroplastic/amyloplastic (AtSS3) (EC 2.4.1.21) (Soluble starch synthase III)
|
MISYFLNQDFSRKKQGRMAASGPKSSGPRGFGRRTTVGSAQKRTQKKNGEKDSNATSTATNEVSGISKLPAAKVDVQKQSSVVLNERNVLDRSDIEDGSDRLDKKTTDDDDLLEQKLKLERENLRRKEIETLAAENLARGDRMFVYPVIVKPDEDIEVFLNRNLSTLNNEPDVLIMGAFNEWRWKSFTRRLEKTWIHEDWLSCLLHIPKEAYKMDFVFFNGQSVYDNNDSKDFCVEIKGGMDKVDFENFLLEEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAENVWYIEPSDFKAEDTVKLYYNKRSGPLTNSKELWLHGGFNNWVDGLSIVVKLVNAELKDVDPKSGNWWFAEVVVPGGALVIDWVFADGPPKGAFLYDNNGYQDFHALVPQKLPEELYWLEEENMIFRKLQEDRRLKEEVMRAKMEKTARLKAETKERTLKKFLLSQKDVVYTEPLEIQAGNPVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMEATDDESSHVKTTAKVPLDAYMMDFVFSEKEDGGIFDNKNGLDYHLPVVGGISKEPPLHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRSYHWGGTEIKVWHGKVEGLSVYFLDPQNGLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKTRIVFTIHNLEFGANAIGKAMTFADKATTVSPTYAKEVAGNSVISAHLYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEELQNRLGLKSADFPVVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSSHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGLFDTVFDVDHDKERAQAQVLEPNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPALEYLELYHSARK
|
Involved in the synthesis of glycan chains within amylopectin in leaves. May play a regulatory role in the control of starch accumulation in plastids.
|
F4IAT2
|
THOC2_ARATH
|
THO complex subunit 2 (AtTHO2) (Protein EMBRYO DEFECTIVE 2793)
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MSLPLLECKYVTEEFVREGKNGNYGTKLPSSVPMLRFLYELSWILVRGELPIQSCKAVLEGVEFLDKPSREELASCFADVVTQIAQDLTMSGDQRSRLIKLAKWLVESQTVPQRLFQERCEEEFLWEADMVKIKAQDLKGKEVRLNTRLLYQQTKFNLLREESEGYAKLATLLCRGSASSSHNASAATMGIIKSLIGHFDLDPNRVFDIVLDCFELEQDYDTFLNLIPIFPKSHASQILGFKFQYYQRLEVNSPVPVGLYKLTALLVKEEFINLESIYAHLLPKDEEVFEDYNVSSAKRFEEANKIGKINLAATGKDLMEDEKQGDVTVDLFAALDMESEAVTERLPELENNQTLGLLNGFLSVDDWYHANILFERLAPLNPVAHDQICSGLFRLIEKSITHSYRIARQTRFQSSSSASTVKLTPTANTTANRTYLDLPKEVFQMLVTVGPYLYRNTQLLQKICRVLRAYYLSALDLVRDGSNQEGSAYEVSRGHLKEVRLRVEEALGTCLLPSLQLVPANPAVGHEIWEVMSLLPYEARYRLYGEWEKDDEQNPLLLAARQVAKLDTRRILKRLAKENLKQLGRMVAKLAHANPMTVLRTIVNQIEAYRDMIAPVVDAFKYLTQLEYDILEYVVIERLAQSGRDKLKDDGINLSDWLQSLASFWGHLCKKYPSMELRGLFQYLVNQLKRGQGIELVLLQELVQQMANVQYTENLTEDQLDAMAGSETLRYHATSFGMMRNNKALIKSSNRLRDSLLPNDEPKLAIPLLLLIAQHRSLVVVNADAPYIKMVTEQFDRCHGILLQYVDFLSSAVSPTTAYARLVPSLDELVHTYHLEAEVAFLVFRPVMRLFKCRRNGDVSWPLDSGESMDADSEISESESSMILDVGTSEKAVTWSDVLDTVRTMLPSKAWNSLSPDLYATFWGLTLYDLHVPRNRYESEISKQHTALKTLEEVADNSSSAITKRKKEKERIQESLDRLTGELKKHEEHVASVRRRLSREKDTWLSSCPDTLKINMEFLQRCIFPRCTFSMADSVYCAMFVNMLHSLGTPFFNTVNHIDVLICKTLQPMICCCTEYEVGRLGRFLFETLKIAYHWKSKESVYEHECGNMPGFAVYYRYPNSQRVTFGQFVKVHWKWSGRITRLLIQCLESNEYMEIRNALIMLTKISGVFPVTRKTGINLEKRATKIKNDEREDLKVLATGVGAALSARKPHWVTDEEFSMGFLELKAPPVHTPKHASSQNGLLVGVSQGEPTGERATVNQQPESGGLGKDQMLKTKPLDGRTESIPSKSDQGHLKSKGGNPLDSQPSISKKSMEQKETDETPRISDENPVKPASKYSEAELKASSKRGASVNKSAKQDFGKDDGKSGKAIGRTSTADKDLNYLESRQSGLTKALSSTAANGSIATGSSKVKDDGAEALDAQKQSSRTVHSPRHEIVTSVRSSDRLQKRANAVEDSERISKRRKGDAEHKEHDSEPRSSDRDRSVEARLDLNKTVTDDQSTHRDQDRSKDKGYERQDRDHRERVDRSDKPRGDDVEKARDKSLERHGRERSVEKGLDKGTTRSYDRNKDERNKDDRSKLRHSEASLEKSHPDDHFHSQGLPPPPPLPPNIIPHSMAAKEDLERRAGGARHSQRLSPRHEEREKRRSEENLSVSVDDAKRRRDDDIRDRKRDDRETITVKGEEREREREREREREKSLPLKEDFEASKRRKLKREQQVPSAEPGEYSPMPHHSSLSTSMGPSSYEGRERKSSSMIQHGGYLEEPSIRLLGKEASSKMARRDPDPIAKSKSKNSNFLDIALESMTVNGKTTRGEQSGSGEIGSRE
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Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export.
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F4IAX0
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CAOA2_ARATH
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Amine oxidase [copper-containing] alpha 2, peroxisomal (AtCuAO8) (AtCuAOalpha2) (EC 1.4.3.21)
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MAQVHLTIFIFSSIFVISSSSFIPPPHPFDPLTETELKLVRNIINKSYPIGHNHKFTFQYVGLNEPEKSLVLSWHSSPDRNVKPPPRQAFVIARDKGMSREIVIDFSTRAIVSNKIHVGNGNPMLTIDEQQAATAVVQKYKPFCDSIIKRGLNLSEVVVTSSTMGWFGETKTKRFIRTIPFYLNGSVNTYLRPIEGMTIIVNLDQMKVTGFKDRFTGPMPKANGREYRISKLKPPFGPSLRSAVVFQPDGPGFKIDGHVVRWANWEFHMSFDVRAGLVISLASIFDMDMNRYRQVLYKGHLSEMFVPYMDPNDDWYFISYLDCGEFGCGQTAVSLEPYTDCPPNAAFMDGIFPGQDGTPTKISNVMCIFEKYAGDIMWRHTEAEVPGLKITEVRPDVSLVARMVTTVGNYDYIIEYEFKPSGSIKMGVGLTGVLEVKPVEYVHTSEIKEDDIYGTIVADNTVGVNHDHFVTFRLDLDIDGTENSFVRTELVTKRTPKSVNTPRKSYWTTKRNTAKTEADARVKLGLRAEELVVVNPTKKTKHGNEVGYRLLPGPASSPLLVQDDYPQIRAAFTNYNVWITPYNKSEVWASGLYADRSQGDDTLAVWSQRDREIENKDIVMWYTVGFHHVPCQEDFPTMPTMFGGFELRPTNFFEQNPVLKAKPFNLTTIPKCTTKNE
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Copper amine oxidase that can use putrescine and spermidine as substrates. Involved in putrescine catabolism in peroxisomes in response to salt stress. Regulates arginine-dependent nitric oxide (NO) production, a key signaling molecule regulating a wide range of physiological processes including responses to salt stress, by influencing arginine bioavailability. Modulates primary root growth.
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F4IAX1
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CAOA3_ARATH
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Amine oxidase [copper-containing] alpha 3, peroxisomal (AtCuAO2) (AtCuAOalpha3) (Copper amine oxidase 2) (EC 1.4.3.21)
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MAPLHFTILILFSFVIVVSSSSFTPPRHPFDPLTETELKLVRTIINKSYPVGPNHKFTFQYVGLNEPNKSLVLSWYSSPNHTIKPPPRQAFVIARDNGKTREIVLDFSSRAIVSDKIHVGNGYPMLSNDEQEASTELVVKFKPFIDSVAKRGLNVSEIVFTTSTIGWYGETKAEAERVIRLMPFYLDGTVNMYLRPIEGMTIIVNLDEMKVSEFKDRSVVTMPIANGTEYRISKLNPPFGPTLHNAVLLQPDGPGFKVDGHIVRWANWEFHISFDVRAGIVISLASLFDTDVNKYRQVLYKGHLSEMFIPYMDPSDDWYFITYLDCGDFGCGQCAVSLQPYTDCPAGAVFMDGIFAGQDGTPAKIPKVMCIFEKYAGDIMWRHTEAEIPNLEITEVRPDVSLVARIVTTVGNYDYIVDYEFKPSGSIKMGVGLTGVLEVKPVEYIHTSEIKLGEDIHGTIVADNTVGVNHDHFVTFRLHLDIDGTENSFVRNELVTTRSPKSVNTPRKTYWTTKPKTAKTEAEARVKLGLKAEELVVVNPNRKTKHGNEVGYRLLHGSAAGPLLAQDDFPQIRAAFTNYNVWITPYNRSEVWAGGLYADRSQGDDTLAVWSQRNRKIEKEDIVMWYTVGFHHVPSQEDYPTMPTLSGGFELRPTNFFERNPVLKTKPVKVTTARKCTPKND
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Copper amine oxidase that can use putrescine and spermidine as substrates. Involved in putrescine catabolism in peroxisomes.
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F4IB81
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LYK3_ARATH
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LysM domain receptor-like kinase 3 (LysM-containing receptor-like kinase 3) (EC 2.7.11.-)
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MNLTFYIFFLSLLPSFSSSKPMNCSDTTRLCSSFLAFKPNQNQSFSVIQSMFDVLPQDITADISGGYFFIKKNCSCLTTTHQYTTNTTFTIRQNVGYVYNVTVSAYSGLAFPPNTTRAARAGAVVSVQLLCGCSSGLWNYLMSYVAMAGDSVQSLSSRFGVSMDRIEDVNGILNLDNITAGDLLYIPLDSVPGEPYETSKINPPAPSPAPASSLANGNISDDQVNHTAKSGSHVPYIWIVGGLGVVLALLVLCILVCICLRSSSCSSSEEDGNGHNFQILRKSGFFCGSGRYNCCRSGDFRQTNGETQVVAIPKALGDGMFEIEKPMVFTYEEIRAATDEFSDSNLLGHGNYGSVYFGLLREQEVAVKRMTATKTKEFAAEMKVLCKVHHSNLVELIGYAATVDELFVVYEYVRKGMLKSHLHDPQSKGNTPLSWIMRNQIALDAARGLEYIHEHTKTHYVHRDIKTSNILLDEAFRAKISDFGLAKLVEKTGEGEISVTKVVGTYGYLAPEYLSDGLATSKSDIYAFGVVLFEIISGREAVIRTEAIGTKNPERRPLASIMLAVLKNSPDSMNMSSLKEFVDPNMMDLYPHDCLFKIATLAKQCVDDDPILRPNMKQVVISLSQILLSSIEWEATLAGNSQVFSGLVQGR
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Putative Lysin motif (LysM) receptor kinase that may recognize microbe-derived N-acetylglucosamine (NAG)-containing ligands.
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F4ICB6
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IBS1_ARATH
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Protein IMPAIRED IN BABA-INDUCED STERILITY 1 (EC 2.7.11.-)
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MGCVNSKQTVSVTPAIDHSGVFRDNVCSGSGRIVVEDLPPVTETKLLSWWSKSGKKSSSKKSGSELGSDFGELSESGRASSNCRSESVSFRLGNLSKYLEAEQVAAGWPAWLSNVAGEAIHGWVPFRSDAFEKLEKIGQGTYSSVFRARETETGRIVALKKVRFDNFEPESVRFMAREILILRKLNHPNIIKLEGIVTSKLSCSIHLVFEYMEHDLTGLLSSPDIDFTTPQIKCYMKQLLSGLDHCHARGVMHRDIKGSNLLVNNEGILKVADFGLANFCNASGNKQPLTSRVVTLWYRPPELLLGATEYGASVDLWSVGCVFAELLIGKPVLQGRTEVEQLHKIFKLCGSPPEDYWKKSKLPHAMLFKPQQHYDGCLRETLKLKGLSDADINLIETLLSIQPHKRGTASTALVSQYFTSKPFACDPSSLPVYSPSKEIDAKHREDTTRKKISGNGRRGTESRKPTRKPPAFAKLAPAEDVRHHSQKFQKRNGHSVHNSIDSDSTLFEKMQKPSNHEKDEASHVKNASQGDVPFSGPLQVSVSSGFAWAKRRKDDICVRSHNRSLSRGHIPNLLGPSPAFSENTDVDSKNNEKEKEEKHGERTDSQDREAYEMLKLSMLKKWRQLERPDSFGGSDEYHSQELSLELYQREEKAAKLGHLGYEDNDEKIEFSGPLLSKSYGVDELLERHERQIRQLVRKSWFQKGKKQGK
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Required for beta-aminobutyric acid (BABA)-induced resistance (BABA-IR) against bacteria (e.g. P.syringae) and oomycetes (e.g. H.parasitica) via priming for salicylate (SA)-dependent defense responses such as pathogenesis-related PR-1 gene expression and trailing necrosis. Involved in BABA-mediated sterility. Necessary for the inheritance of BABA-priming to next generation, especially for the primed to be primed phenotype which consists in an enhanced second BABA-priming in transgenerationally primed plants.
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F4ICF4
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RBL10_ARATH
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RHOMBOID-like protein 10, chloroplastic (AtRBL10) (EC 3.4.21.-)
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MVSVSLSHHNLWPPESGSTAFRGFATAASVHACHHVSRHLRLDFHLRSSLKKLQHFSDDARMKFARYQRVFVFNGANFLKSRVDIRLSQSSPFVCFFNGGESRLNPRGGEEGSSNPETSKRNTVNGRRWTNVLLAINVIMYIAQIASDGKVLTWGAKINSLIERGQLWRLATASVLHANPMHLMINCYSLNSIGPTAESLGGPKRFLAVYLTSAVAKPILRVLGSAMSYWFNKAPSVGASGAIFGLVGSVAVFVIRHKQMVRGGNEDLMQIAQIIALNMAMGLMSRRIDNWGHIGGLLGGTAMTWLLGPQWKYEYTTRDGRRVFMDSAPIPLLLRWRNEQRRL
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Rhomboid-type serine protease that catalyzes intramembrane proteolysis. Required for correct root growth, floral development, fertility and photoprotection. May be involved in TIC22 processing during its import and in AOS accumulation in the chloroplast membrane.
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F4ICK8
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IWS1_ARATH
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Protein IWS1 homolog 1 (AtIWS1) (Interacts with SPT6 protein 1) (Protein HIGH NITROGEN INSENSITIVE 9) (Protein SUPPRESSOR OF BES-1-D 1)
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MGFEDDPYRDVDGEPIVDFDDFGNDREPSTEPLQDFDEDLADDIGDWDGEGSQTPVYDNDKVAKPRKRLVKKSSSERVTIDVPELIDEDVDDAEFDEFMGGRGGGSTDYDDKVGRKRKKEKERSSSGSGKEKRHKFPNRGERKSEEIDEMWKSIAHNPENDEEGVRTMDDDNFIDDTGLDPSERYGGDAGDRSPTHYPQAEEGEDEDEVNNLFKMGKKKKKTERNPAEIALLVENVMAELEVTAEEDAELNRQGKPAINKLKKLSLLTDVLGKKQLQTEFLDHGVLTLLKNWLEPLPDGSLPNINIRAAILRVLTDFPIDLDQYDRREQLKKSGLGKVIMFLSKSDEETNSNRRLAKDLVDKWSRPIFNKSTRFEDMRNLDEDRVPYRRPPVKKPSNKATMESRDGDFDLEIRERKTGLTSGQSSRGDRQMTMRPEATPLDFLIRPQSKIDPDEIIARAKQVSQDQRRVKMNKKLQQLKGTKKKRLQATKVSVEGRGMIKYL
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Transcription factor involved in RNA polymerase II (RNAPII) transcription regulation. Involved in transcription elongation. May function at post-recruitment and elongation steps of transcription. May be recruited by BZR2/BES1 to target genes and promote their expression during transcription elongation process. Required for brassinosteroid (BR)-induced gene expression. Required the for regulation of numerous nitrogen-responsive genes in roots. Acts in roots to repress NRT2.1 transcription in response to high nitrogen supply. This repression is associated with an IWS1-dependent increase of trimethylation on 'Lys-27' H3K27me3 at the NRT2.1 locus.
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F4ICX9
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TSA1_ARATH
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TSK-associating protein 1
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MEIYTMKTNFLVLALSLCILLSSFHEVSCQDDGSGLSNLDLIERDYQDSVNALQGKDDEDQSAKIQSENQNNTTVTDKNTISLSLSDESEVGSVSDESVGRSSLLDQIKLEFEAHHNSINQAGSDGVKAESKDDDEELSAHRQKMLEEIEHEFEAASDSLKQLKTDDVNEGNDEEHSAKRQSLLEEIEREFEAATKELEQLKVNDFTGDKDDEEHSAKRKSMLEAIEREFEAAMEGIEALKVSDSTGSGDDEEQSAKRLSMLEEIEREFEAASKGLEQLRASDSTADNNEEEHAAKGQSLLEEIEREFEAATESLKQLQVDDSTEDKEHFTAAKRQSLLEEIEREFEAATKDLKQLNDFTEGSADDEQSAKRNKMLEDIEREFEAATIGLEQLKANDFSEGNNNEEQSAKRKSMLEEIEREFEAAIGGLKQIKVDDSRNLEEESAKRKIILEEMEREFEEAHSGINAKADKEESAKKQSGSAIPEVLGLGQSGGCSCSKQDEDSSIVIPTKYSIEDILSEESAVQGTETSSLTASLTQLVENHRKEKESLLGHRVLTSPSIASSTSESSATSETVETLRAKLNELRGLTARELVTRKDFGQILITAASFEELSSAPISYISRLAKYRNVIKEGLEASERVHIAQVRAKMLKEVATEKQTAVDTHFATAKKLAQEGDALFVKIFAIKKLLAKLEAEKESVDGKFKETVKELSHLLADASEAYEEYHGAVRKAKDEQAAEEFAKEATQSAEIIWVKFLSSL
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Involved in seedling development in the dark. May be involved, when interacting with TSK, in the organization of spindle microtubules and may participate, when interacting with GIP1, in structural links between the nuclear envelope and the cytoskeleton.
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F4IDB2
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PHL_ARATH
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Protein PHYTOCHROME-DEPENDENT LATE-FLOWERING
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MGVSFKISKVGRKFRPKISTELATPDSPKAIVLSGKPKATDDSNIGDVSGFSKPSLPDISPDHEVSFILSLYPNGYSIGKTSEAMQQISFRDVPKVLHPYDRAAEGLLSAIEAGRLPGDILEDIPCKFVDGVVICEVHDYRKHTSSQVSPVINKLRLKMSLENVVKDIPSMSDNSWTYGDLMEVESRILKALQPELCLDPLPRLDRLSKNPLTAKLDLSLSTLRRKRLRQMAEVTVMSQNKIQGKKVCIDRLPESSERGNLPGHLIMQQTNNNQAIQNLGTNMLAGLRSQPLQDAPNSSLALVPPQQQRYMGIGSTRNTQDQGSNSVSVSGASPGGLDAMLPYGSDSMNPGTSFHRKRESQEGQMSSMPGLNKRTRVSHMGPDGVPQQQLGQRMDGLHGSDTNWKNTLLQHQDMLGRSIQYPNTSIQRFSPHQMEGVMNQEGGPMQFPASQQGGMKYTSKEEPFETGKIDGGTRNNIPGVGSDANDLDPRIQSRMPHNAFIRSNFPQTSWNVNPGQQIEKEPKKEEQFSRRISAQSPRLSAGGPPQSPLSSKSGEFSGGSMGTHYGAVAAAQKDKAVTSIPAIGATQSVGSSANEAMQQRQHQAQMAAKRRTNSLPKTQVISTVGSPVSVNTISVPVNARSPSVGPQTLGDHAILDRFSKIERVAARYQLNCKKHKVDEYSRRPRVYAKQPLTVCLSNLSNEEVFKDEDEALSKSIFGGSMNTYKTRVIHFGQMERVMQGSVPSFIPRNRTRLVMSEKAVDGTVAWYQGDVDEGDVFQAEDFLLALPNTHIADLLATQFKSLMAREGYMIEEHIMAKPNRGDTGPISSHPNSAGGYPRGYSANDMQQYGDAVAGQASGEASKHGNTGNTPNNSTQNILANARMVPPTNSQALQMSQGLLSGVSMPMQPQQLDPQQSALLSSHSQQKNQQSMFTQQQHPQMQRPSMILPTNPLSAINSMSQSSGMQPGGQMANKYSPLQLQMLQQQQQAAVQKKIMMGLGSGVGMGMGMGMGMGMGSMGNSIAGLGALGNQLNMAGRGMGGTGISSSMSVPGIGNMGQNPMNLNPASNLNAISQQLRSGALTPQQNALFTQIRMGMANRGGVMGAPQTGISGVSGTRQMHPSSAGLSMLDQNRANLQRAAAMGNMGPPKLMPGMMNLYMNQQQQQQQLQQQPQQQQLQHQQQLQQPMSQPSQQLAQSPQQQQQLQQHEQPQQAQQQQQATASPLQSVLSPPQVGSPSAGITQQQLQQSSPQQMSQRTPMSPQQVNQRTPMSPQISSGAMHPMSTSNLEGCPASPQLSSQTMGSVGSITNSPMELQGPKNNSAGNNS
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Triggers photoperiod-monitored flowering by repressing PHYB-dependent flowering negative regulation, probably through physical interactions with PHYB and CO.
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F4IDC2
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SWA2_ARATH
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Protein SLOW WALKER 2 (Protein EMBRYO SAC DEVELOPMENT ARREST 25)
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MSKIKPLSKSSQDLSLLTSDIASFASSIGLASALPSSGFNDTDFRKPAKSKTQKRKKPKKDQQHKDEDEEGEPKSNIGNEKGKDFGARKQNKDAPVKQTLQPKPKPGFLSIDDESTGYKKKRFDEFKSLPKLPLVKASLLSSEWYNDAAEFEEKVFGGRKVAVANKEDFKGVVEKKRELGERLMWQYAEDFATSKGKGGDMKMVISAQKSGTVADKITAFEIMVGENPIANMRSLDALLGMVTSKVGKRFAFKGLKALSEILIRLLPDRKLKSLLQRPLNIIPENKDGYSLLLFWYWEDCLKQRYERFVTALDESSKDMLPELKDKALKTIYFMLTSKSEQERKLLVSLVNKLGDPQNKSASNADYHLTNLLADHPNMKAVVIDEVDSFLFRPHLGLRAKYHAVNFLSQIRLSHKGEDPKVAKRLIDVYFALFKVLTTEANRKQGADDKGAADKKKSNPKDTKQEVSTDSPIELDSRILSALLTGVNRAFPYVSTDEADDIIESQTPVLFKLVHSANFNVGVQSLMLLDKISSKNKIVSDRFYRALYSKLLLPSAMNSSKAEMFIGLLLRAMKNDINIKRVAAFSKRVLQVALQQPPQYACGCLFLLSEVLKSRPPLWKMVVQRESVEEEEDIEHFEDVIEGDDVDPNKKAENDENVVEVDHDGVEKSSRDGDSSSDDEEALAIRLSDEEDDNASDDSEELIRNETPQLEEVMEVSNDMEKRSQPPMRPSSLPGGYDPRHREPSYCNADRASWWELGVLSKHAHPSVATMAGTLLSGTNIVYNGNPLNDLSLTAFLDKFMEKKPKQNTWHGGSQIEPSKKLDMSNRVIGAEILSLAEGDVAPEDLVFHKFYVNKMTSTKQSKKKKKKKLPEEEAAEELYDVNDGDGGENYDSDVEFEAGDESDNEEIENMLDDVDDNAVEEEGGEYDYDDLDGVAGEDDEELVADVSDAEMDTDMDMDLIDDEDDNNVDDDGTGDGGDDDSDGDDGRSKKKKKEKRKRKSPFASLEEYKHLIDQDEKEDSKTKRKATSEPTKKKKKKKSKASE
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Together with NOC2, probably involved in pre-ribosome export from the nucleus to the cytoplasm. Required for coordinated cell cycle progression during female gametophyte and pollen development.
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F4IDI6
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BRG2_ARATH
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Probable BOI-related E3 ubiquitin-protein ligase 2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRG2)
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MAVDAHHLFLSPPQLFSNRELTMNNNTMEPTSGGFCNNNQTGYGVVSPFSVPNHTSTTTTATPPLLHVYGGSDTIPTTAGYYADGATNLDCEFFPLPTRKRSRDSSRSNYHHLLLQNPRSSSCVNAATTTTTTTLFSFLGQDIDISSHMNQQQHEIDRFVSLHLYQMERVKYEIEEKRKRQARTIMEAIEQGLVKRLRVKEEERERIGKVNHALEERVKSLSIENQIWRDLAQTNEATANHLRTNLEHVLAQVKDVSRGAGLEKNMNEEDDAESCCGSSCGGGGEETVRRRVGLEREAQDKAERRRRRMCRNCGEEESCVLLLPCRHLCLCGVCGSSVHTCPICTSPKNASVHVNMSS
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Probable E3 ubiquitin-protein ligase. Has no effect on the stability of the DELLA proteins.
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F4IDQ6
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NIH_ARATH
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DExH-box ATP-dependent RNA helicase DExH2 (EC 3.6.4.13) (DEIH-box RNA/DNA helicase) (EC 3.6.4.12)
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MAKKKKDTKHTRLCEATGAWATKVLEDFRASGNDSYVFEQQLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFKGDGISKSDKRRMYEARNQKEKEGDGISKSYSKHRYETRFQKAGGIRKTRISPKKLKCVSFPPEAKAVLHDLFTRYPPCDGDTTGTSLGIYTTGNVNSNWKDDFFKKPHMTKHDIENNVVSLSSRLKKERHFREIFEARSKLPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKEACKIICTQPRRISAISVSDRISWERGETIGRTVGYKVRLQSEGGRESSVVFCTNGILLRVLIGKGVNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILMSATLDAERFSEYFGGCPVVRVPGFTYPVRTFFLDDALSVLNSDKNSHLLSAVKRDFKDEDKVSLDEAIDLAWTNDEFDCLVDLVSSEGSHEAYNYQNSTTGLTPLMVFAGKGRVSDVCKLLSVGADCTLKSKEGITALELAEKENQFETAQIIREHAGNIQSNSQQAQDLLDKYMATIKPEEVDVGLIVKLMKKICSDSKDGAILVFLPGWEEISKTKEKLLDDRFFAHSAKFIILCLHSRVPAEEQKKVFNRPPRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKANAKQRAGRAGRCQAGICYHLYSKLRAASLPEYRVPEVMRMPVDELCLQVKMLDPNCNVNDFLQKLMDPPVAQSIENALIILKDIGALTPEEELTELGQKFGQLPVHPRISKMIYFAILVNCLDPALILACAADEKDPFTMPLSPGDRKKAAAAKHELASLYGDHSDHLATVAAFQCWKNAKASGQAKEFCSKYFISQVVMKRLDDLCRKLQGELNRHGVIPSSSSNCSLNAHDPGILRAVIAVGLYPMLGRMCPLSKNRTRSVIETIAGAKVRVPSLSNNVDMSSTKFDEALIVFDEITRGDWGVVIRSCTVLPTIPVLLFSREIAVSTTESYDAVKSDDEEDHKVGNVGDAMDIDKEVGRPGEKIMLGPENSVKVVVDRWLPFKVTAFEIAQMYILRERLMASILFKVKHPKENLPPHLGASMYAIASVLSYDSLAQSSVQTVAVQPITSVVDATSPRDDIPSTNPNELREHDPNTTPMGSKLELANKLGLGNMEESLPSNFADGNEQPDPNTSPVEDVSAATKQKKMQSESKRCKSLNNVDLGNIEENFGNMEENPPSDLAIGNEQTLPKLASNLDMGNMEENTPSDLANGNEKTEPNSANSMDLGNMEENTPSDLANGNKKKEPKSVSKLDLGSEKVSIPSNLVNGNEQHDLNIAPGEDASAAKQPEKKRSRSKKRKSGNNLDLGKMEKSKPSDLANENEQTEPKSANNLDLGNMKENTPSDLANENEQTELRLPNNSDYGNMEESLPLNLANGDEQPDPTTAPMEAAKQPKKKRSRSKKCKSVNNLDLGNMEENKPSDLANGNEQKDPESVNRLDPGKEKESIPSNLVSGNEQPDSNTAPAKKPKKKKRKLANNFDSVNNMEEKMPSTNVLSQGNKSGLIEEKPSIPSDQ
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May function as an ATP-dependent RNA/DNA helicase. Binds DNA in vitro in a non-specific manner.
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F4IDS7
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VPS18_ARATH
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Vacuolar sorting protein 18
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MDQGRQVFSVDLLERYATKNRGMITCMAAGNDVIVLGTSKGWIIRYDFGVGSSNDIDLAVGRTGEQSIHKVFVDPGGSHCIATVTGVGGAETFYTHAKWLKPRVLSRLKGLLVNAVAWNRQQITEVSTKEIILGTQDGQLFEMAVDEKDKREKYIKFLFELEELPEAFKALQMETANISSGMRYYVMAVTPTRLYSFTGIGTLESVFASYKERAVHFMELPGEIPNSELHFFIKQRRAVHFAWLSGTGIYHGGLNFGAQHSYPNGDENFVENKALLDYSKLSDGTEAVKPGSMALSEYHFLLLIGNKVKVVNRISEQIIEELQFDITSDSVSRGIIGLCSDASANVFYAYDQNSIFQVSVIDEGRDMWKVYLDLKVYAAALANCRDPLQRDQVYLVQAESAFTDKEYLRAASFYAKINYVISFEEVTLKFISINEPEALRTFLLHKLDNLSKDDKCQITMISTWATELYLDKINRLLLEDDTAIENRDSEYHSVIQEFRAFMSDCKDELDEATTVKILESYGRVEELVYFANLKEQYEIVVLHYIQQGEAKKALEVLQKSSVSVELQYQFAPELIMLDAYETVESWMANKNLNPRRLITAMMRYSSGPHAKNETHEVIKYLEFCVHRLHNEDPGIHSLLLSLYAKQEDDGALLRFLQCKFGKGRENGPEFFYDPKYALRLCLKERRTRACVHIYSMMSMHEEAVALALQIDPELAMAEADKVEDDEDLRKKLWLMVAKHVVKQEKGAKRENIRKAIAFLKETDGLLKIEDILPFFPDFALIDDFKEAICSSLEDYNKQIEQLKEEMNDATRGADNIRNDISALTQRYAVIDRDEECGVCKRKILMMSGDFRMAQGYSSAGPLAPFYVFPCGHSFHAQCLITHVTSCAHEEQAEHILDLQKQLTLLGSETRRDINGNRSDEPITSTTTADKLRSELDDAIASECPFCGELMINEITLPFIKPEDSQYSTSWDLRSETNLANQRTISLPV
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Essential protein required during embryogenesis. Believed to act as a core component of the putative HOPS endosomal tethering complex and of the class C core vacuole/endosome tethering (CORVET) complex. CORVET is required for vacuolar transport of SYP22. HOPS is required for the central vacuole formation. Involved in root development. Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport pathways (By similarity).
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F4IDU4
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MBOA1_ARATH
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Lysophospholipid acyltransferase 1 (AtLPLAT1) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Lysophosphatidylcholine acyltransferase 1) (LPCAT1) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lysophosphatidylglycerol acyltransferase) (LPGAT) (Lysophosphatidylserine acyltransferase) (LPSAT)
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MDMSSMAGSIGVSVAVLRFLLCFVATIPVSFACRIVPSRLGKHLYAAASGAFLSYLSFGFSSNLHFLVPMTIGYASMAIYRPKCGIITFFLGFAYLIGCHVFYMSGDAWKEGGIDSTGALMVLTLKVISCSMNYNDGMLKEEGLREAQKKNRLIQMPSLIEYFGYCLCCGSHFAGPVYEMKDYLEWTEGKGIWDTTEKRKKPSPYGATIRAILQAAICMALYLYLVPQYPLTRFTEPVYQEWGFLRKFSYQYMAGFTARWKYYFIWSISEASIIISGLGFSGWTDDASPKPKWDRAKNVDILGVELAKSAVQIPLVWNIQVSTWLRHYVYERLVQNGKKAGFFQLLATQTVSAVWHGLYPGYMMFFVQSALMIAGSRVIYRWQQAISPKMAMLRNIMVFINFLYTVLVLNYSAVGFMVLSLHETLTAYGSVYYIGTIIPVGLILLSYVVPAKPSRPKPRKEE
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Lysophospholipid acyltransferase with broad specificity. Mediates the conversion of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Catalyzes the acylation of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Can convert lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). Exhibits preference for C18-unsaturated acyl-CoA when transferring an acyl group to lysophosphatidylcholine. Can also utilize lysophosphatidylglycerol (LPG) as substrate in vitro. Has neither activity towards lysophosphatidic acid (LPA) nor lysophosphatidylinositol (LPI). Lysophospholipid acyltransferases catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle (Probable). The primary function of the Lands cycle is to provide a route for acyl remodeling to modify fatty acid (FA) composition of phospholipids derived from the Kennedy pathway. Is involved in PC acyl editing and phosphocholine headgroup exchange between PC and diacylglycerols. This processes control the majority of acyl fluxes through PC to provide polyunsaturated fatty acids for triacylglycerols synthesis in seeds. Involved with LPCAT2 in the direct incorporation of newly synthesized fatty acids exported form the chloroplast into PC through acyl editing.
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F4IDW9
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PTD_ARATH
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Protein PARTING DANCERS (AtPTD) (EC 3.1.-.-)
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MATAGSSYSVSTDHQVSSPLVNLGNVAGVCIMSNAWKVEQEPSLINFISAFLSANSFRLNFVSIPPDLIFNCGGVSIAFVFVTKWDFSNVASIFSRVKRLKGQFAQLYVVATLSTKEQSDSFMRSYFQYEMEFGKPAFVQVTDAEMGFEKIVKIAHSRGVCKQQKVASKLKVERKRTVQDTNIFIRFVTSIPNINKHDANTLYQAIGSIEAIAKASKEDILANTDLSSKKADTLTRFFQDPEFYLSPKFN
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Required for chromosome segregation during meiosis. During diakinesis and prometaphase I, essential for the formation of class I meiotic crossovers and homologous recombination.
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F4IDY5
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BTSL1_ARATH
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Zinc finger protein BRUTUS-like At1g18910
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MGVGDPLPLPPEKNRREVNKPPDIASTSSSSASAVNNARLSDAPILLFVYFHKAFRAQLAELQFLAGDTVRSGSDLAVELRSKFEFLKLVYKYHSAAEDEVIFSALDTRVKNIVFNYSLEHDATDDLFTSVFHWLNVLEEEQGNRADVLREVVLCIGTIQSSICQHMLKEERQVFPLMIENFSFEEQASLVWQFICSVPVMVLEEIFPWMTSLLSPKEKSEVETCFKEVVPNELSLQLVINSWLIDDSQSSLTALTKIMKGVQSVEVSENMTNSQTNSSSSGVFQRFWQWSKKMSFSSPNTGHILVHGIHLWHNAIRKDLVDIQKGLCQLTFPSLSLDLNVLVVRLNFLADVLIFYSNAFKTFFYPVFEDMVDQQHSSSSKQFTIDGHVENFKKSLDLETRAGSDNFVITLQEKLESLILTVAKQFSIEETEVFPIISKNCNIEMQRQLLYRSIHFLPLGLLKCVIMWFSAQLPEDECQSIIHYLSSEDSFPNKPFAHLLLQWFRFGYSGKTPVESFWNELSFMFKPRCSFEEELTEEASGSFFQQSPQKLFKVSDPYSMDPPAGYMNETPYSSAMNQQILIPGKLRPLLHLPDLFGDKTIGEHLTMDLKPIDLIFYFHKAMKKDLDYLVRGSARLATDYSFLGEFQQRFHLIKFLYQIHSDAEDEIAFPALEAKGKLQNISQSYSIDHELEVEHLNKVSFLLNELAELNMLVLDHKNVKYEKLCMSLQDICKSIHKLLSEHLHREETELWCLFRDCFTIEEQEKIIACMLGRISGEILQDMIPWLMESLIPDEQHAVMSLWRQATRKTMFGEWLTEWYNSHAVEEETEEANKDPSENSDPLDVVWSYLFEGAADEYKGSICSKPLEETELKGIMNKPLGKAAPNNKVEFGNKEENHLEISGSKKVCTGADETKYKEQTDSNAQAFQMSHNTSQSGQDSRYECLLSMSQEDVEATIRRISRDSSLDPQKKSYIIQNLLMSRWIATQRIYNLEPSILSSNREAVPGQNPSYRDPHKLIFGCKHYKRSCKLLAPCCNKLYTCIRCHDEEVDHLLDRKQITKMMCMKCMIIQPVGASCSNISCSSSMGKYYCKICKLFDDDREIYHCPYCNLCRLGKGLSIDYFHCMKCNACMSRLIVEHVCREKCLEDNCPICHEYIFTSNSPVKALPCGHVMHSTCFQEYTCSHYTCPICSKSLGDMQVYFRMLDALLAEQKMPDEYLNQTQVILCNDCGRKGNAPYHWLYHKCSSCASYNTRLF
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Probable E3 ubiquitin-protein ligase that may regulate the response to iron deficiency and thus contributes to iron homeostasis.
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F4IE66
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PRP22_ARATH
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Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH10 (EC 3.6.4.13) (DEAH RNA helicase homolog PRP22) (Protein ROOT INITIATION DEFECTIVE 1)
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MPSMAQGELKSFVQNSRPNPKSPTVSPFSMRQKIAEHRRSLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKMIGITQPRRIAAVTVAKRVAEECEVQLGQKVGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQPVSEKTEFGNVASQVQTTTRDANGPQQNGVLKGYQGRKLSPLKLIIMSASLDARVFSEYFGGAKAVHVQGRQFPVDILYTVHPESDYVDATLVTIFQIHFEEKPGDILVFLTGQDEIESVERLVQERLQNIPEDKRKLLPLAIFSALPSEQQMKVFAPAPTGFRKVILATNIAETSITIPGIRYVIDPGFVKARSYDPSKGMESLDVVPASKAQTLQRSGRAGREGPGKSFRLYPEREFEKLEDSTKPEIKRCNLSNIILQLKALGIDDIVGFDFIDKPSRGAIIKALAELHSLGALADDGKLENPVGYQMSRLPLEPVYSKALILANQFNCLEEMLITVAVLSVESIFYDPREKREEARTSKNHFASVEGDHLTYLSVYRESDEFLEKRKAAGSGNNIDKIMKKWCKENYVNSRSLKHARDIYRQIREHVEQIGFNVSSCGNDMLAFRRCLAASFFLKAAQRQLDGTYRALESGEVVHIHPTSVLFRAKPECVIFNELMQTSKKYIKNLTIIDSLWLSELAPHHFQTAE
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Involved in pre-mRNA splicing. Plays a role during development in processes such as meristem maintenance, leaf morphogenesis and root morphogenesis.
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F4IED2
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NAC13_ARATH
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NAC domain-containing protein 13 (ANAC013) (Protein NTM1-like 1)
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MDLSVENGGLAPGFRFHPTDEELVVYYLKRKIRRKKLRVEAIGETDVYKFDPEELPEKALYKTRDRQWFFFSLRDRKHGSRSSRATERGYWKATGKDRVIHCDSRPVGEKKTLVFHRGRAPNGERTNWVMHEYTLHKEELKRCGGEDVKDAYVLYKIYKKSGSGPKNGEQYGAPFIEEEWAEDDDDDVDEPANQLVVSASVDNSLWGKGLNQSELDDNDIEELMSQVRDQSGPTLQQNGVSGLNSHVDTYNLENLEEDMYLEINDLMEPEPEPTSVEVMENNWNEDGSGLLNDDDFVGADSYFLDLGVTNPQLDFVSGDLKNGFAQSLQVNTSLMTYQANNNQFQQQSGKNQASNWPLRNSYTRQINNGSSWVQELNNDGLTVTRFGEAPGTGDSSEFLNPVPSGISTTNEDDPSKDESSKFASSVWTFLESIPAKPAYASENPFVKLNLVRMSTSGGRFRFTSKSTGNNVVVMDSDSAVKRNKSGGNNDKKKKKNKGFFCLSIIGALCALFWVIIGTMGGSGRPLLW
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Transcriptional activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP). Involved in oxidative stress tolerance by mediating regulation of mitochondrial retrograde signaling during mitochondrial dysfunction. Interacts directly with the mitochondrial dysfunction DNA consensus motif 5'-CTTGNNNNNCA[AC]G-3', a cis-regulatory elements of several mitochondrial retrograde regulation-induced genes, and triggers increased oxidative stress tolerance.
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F4IEM5
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GCR2_ARATH
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LanC-like protein GCR2 (G-protein coupled receptor 2)
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MGERFFRNEMPEFVPEDLSGEEETVTECKDSLTKLLSLPYKSFSEKLHRYALSIKDKVVWETWERSGKRVRDYNLYTGVLGTAYLLFKSYQVTRNEDDLKLCLENVEACDVASRDSERVTFICGYAGVCALGAVAAKCLGDDQLYDRYLARFRGIRLPSDLPYELLYGRAGYLWACLFLNKHIGQESISSERMRSVVEEIFRAGRQLGNKGTCPLMYEWHGKRYWGAAHGLAGIMNVLMHTELEPDEIKDVKGTLSYMIQNRFPSGNYLSSEGSKSDRLVHWCHGAPGVALTLVKAAQVYNTKEFVEAAMEAGEVVWSRGLLKRVGICHGISGNTYVFLSLYRLTRNPKYLYRAKAFASFLLDKSEKLISEGQMHGGDRPFSLFEGIGGMAYMLLDMNDPTQALFPGYEL
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May play a role in abscisic acid (ABA) signaling.
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F4IF36
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FGT1_ARATH
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Protein FORGETTER 1 (Protein EMBRYO DEFECTIVE 1135)
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MTQSPVQPPPPLPAQPHSAAGGVIRGDVQVRCAGCRVILRVKTGVVEFSCPTCQLPQMLPPELLSRARPQFPQSPQQPPQPIQTLPPPIQQQLKPLNLPRPPVPAHGIDPTKMQLPCANCQAILNVPHGLTRFSCPQCHVELAVDVSKLNRSLTASQSHSNPPTPAAPTVPPPPPPEEVNEEAIEVEREEDEGGTAGETFMDYRPPKLSIGPPHPDPIVETSSLSAVQPPEPTYDLKIKEELERSKALSCLQIETLVYACQRHLQHLADGTRAGFFVGDGAGVGKGRTIAGLIWENWKHGRRKALWISIGSDLKYDARRDLDDVGATCVGVNPLNKLPYSKLDSKNVGIKEGVVFLTYNSLIASSEKGRSRLQQLVQWCGPEFDGLLIFDECHKAKNLVPEAGSQPTRIGQAVVDIQDKIPQARVIYCSATGASEPRNMGYMVRLGLWGAGTSFSDFNKFLGALDKGGTGALELVAMDMKARGMYVCRTLSYKGAEFEIVEARLEAGMEAMYNKSAEFWAELRIELLSASAFLPNEKPNSSQLWRLYWSSHQRFFRHLCMSAKVPVTVRLAKKALSTNKCVVIGLQSTGEARTEEAVNKYGLELDDFVSGPRELLLKFVEENYPLPEQPEPLSEDDSVKELQRKRHSASPGVSIRGRVRKMAKWKPDSDNESDLESEADSADDSNDSDDEFQICQICSGEDERKKLLHCSECDKLFHPDCVVPPVIDLPSEAWICFSCKEKTEEYIQARRLYIAELQKRYEAALERKSKIIEIIRSLNLPNNPLDDIVDQLGGPEKVAEMTGRRGMLVRASNGKGVTYQARNTKDITMEMVNMHEKQLFMDGKKLVAIISEAGSAGVSLQADRRAVNQKRRVHLTLELPWSADRAIQQFGRTHRSNQTSAPEYRLLFTNLGGERRFASIVAKRLETLGALTQGDRRAGPSGPSLSAYNYDSNFGKKSLMVMYRGIMEQEKLPVLPPGCSIDEPETVKEFLTKARAALVAVGIVRDSVLANGKDVGRFSGRIIDSDMHDVGRFLNRLLGLPPDIQNRLFELFTSILDVLVHNARIEGSFDSGIVDMKANSVELLSTPKTVHVDQMSGASTMLFTFTLDRGVTWESASSMLEGKRRDGLGSANDGFFESKREWLGRRHFILAFESAASGLFKIVRPAVGESIREMSLSELKTKYRKLSSLEKARTGWEDEYEVSSKQCMHGPKCKLGEYCTVGRRIQEVNVVGGLILPIWGTIEKALSKQARHSHKRIRVIRIETTTDNQRIVGLSIPNAAVETVLQDLAWVQEIDD
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Required for normal embryo development. Necessary to acquire heat stress (HS) memory, by modulating nucleosome occupancy and regulating heat-induced gene expression. Associates globally with the nucleosome-poor regions flanking the transcription units of expressed genes. Binds to the promoter regions, primarily to the proximal promoter just upstream of the transcriptional start sites (TSS) and somewhat more weakly to the region downstream of the transcription termination site (TTS), of actively expressed genes (e.g. HSA32, HSP18.2 and HSP22.0) in a heat-dependent fashion.
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F4IFN6
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DPOE2_ARATH
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DNA polymerase epsilon catalytic subunit B (EC 2.7.7.7) (DNA polymerase 2 b) (AtPOL2b) (DNA polymerase II subunit b) (Protein TILTED 2)
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MSGRRCDRRLNVQKVSAADELETKLGFGLFSQGETRLGWLLTFASSSWEDADTGKTFSCVDLFFVTQDGSSFKTKYKFRPYLYAATKDNMELEVEAYLRRRYERQVADIQIVHKEDLYLKNHLSGLQKKYLKVSFDTVQQLVEVKRDLLHIVERNLAKFNALEAYESILSGKREQRPQDCLDSVVDLREYDVPYHVRFAIDNDVRSGQWYNVSISSTDVILEKRTDLLQRAEVRVCAFDIETVKLPLKFPDAEYDQIMMISYMVDGQGFLITNRECVGKDIEDLEYTPKPEFEGYFKVTNVTNEVELLRKWFSHMQELKPGIYVTYNGDFFDWPFIERRASHHGIKMNEELGFRCDQNQGECRAKFVCHLDCFSWVKRDSYLPQGSQGLKAVTKVKLGYDPLEVNPEDMVRFAMEKPQTMASYSVSDAVATYYLYMTYVHPFVFSLATIIPMVPDEVLRKGSGTLCEMLLMVEAYKANVVCPNKNQADPEKFYQGKLLESETYIGGHVECLQSGVFRSDIPTSFKLDASAYQQLIDNLGRDLEYAITVEGKMRMDSVSNFDEVKEVIREKLEKLRDDPIREEGPLIYHLDVAAMYPNIILTNRLQPPSIVTDEVCTACDFNGPEKTCLRKLEWVWRGVTFKGNKSEYYHLKKQIESESVDAGANMQSSKPFLDLPKVEQQSKLKERLKKYCQKAYSRVLDKPITEVREAGICMRENPFYVDTVRSFRDRRYEYKTLNKVWKGKLSEAKASGNLIKIQEAHDMVVVYDSLQLAHKCILNSFYGYVMRKGARWYSMEMAGVVTYTGAKIIQNARLLIERIGKPLELDTDGIWCALPGSFPENFTFKTIDMKKFTISYPCVILNVDVAKNNSNDQYQTLVDPVRKTYNSRSECSIEFEVDGPYKAMIIPASKEEGILIKKRYAVFNHDGTIAELKGFEMKRRGELKLIKVFQAELFDKFLHGSTLEECYSAVAAVANRWLDLLEGQGKDIADSELLDYISESSTMSKSLADYGQQKSCAVTTAKRLADFLGDTMVKDKGLRCQYIVAREPEGTPVSERAVPVAIFQTDDPEKKFYLQKWCKISSYTGIRSIIDWMYYKQRLHSAIQKVITIPAAMQKVANPVLRVRHPYWLEKKVCDKFRQGKIVDMFSSANKDHSTTQDNVVADIEEFCKENRPSVKGPKPVARSFEVDRNHSEGKQQESWDPEFHDISLQNVDKNVDYQGWLELEKRKWKMTLTNKKKRRYSSSLFGFDLEQNINKKVCKGRVGVGSYFRRPEEALTSSYLQIIQLVQSPQSGQFFAWVVVEGLMLKIPLTIPRVFYINSKASIAGNFTGKCINKILPHGKPCYNLMEVNIQEDQFIKESKKLAALLADPEIEGIYETKMPLEFSAICQIGCVCKIEDTAKHRNTQDGWKLGELHRITTTECRYLENSIPLVYLYHSTSTGRAVYVLYCHASKLMSVVVVNPYGDKELLSSALERQFRDRCQELSPEPFSWDGILFQVEYVDHPEAATKFLQKALCEYREENCGATVAVIECPDFNTTKEGVKALEDFPCVRIPFNDDDNSYQPVSWQRPAAKIAVLRCASAIQWLDRRIAQSRYAHVPLGNFGRDWLTFTVDIFLSRALRDQQQVLWVSDNGVPDLGDINNEETFLADETSLLFPGAYRKVSVELKVHRLAVNALLKSDLVSEMEGGGFLGVNSRGSSLNDNGSFDENNGCAQAFRVLKQLIKRLLHDACNSGNIYADSILQHLSWWLRSPSSKLHDPALHLMLHKVMQKVFALLLTDLRRLGAIIIYADFSKVIIDTGKFDLSAAKTYCESLLTVMGSRDIFKLILLEPVHYWHSLLFMDQHNYAGIRATGDEISGNEVTIEPKWSVARHLPEYIQKDFIIIVATFIFGPWKFALEKKRGSAESLEAEMVEYLKEQIGTRFISMIVEKIGNIRSHIKDINVSDASWASGQAPKGDYTFEFIQIITAVLALDQNVQQDVLVMRKILLKYIKVKECAAEAEFIDPGPSFILPNVACSNCGAYRDLDFCRDSALLTEKEWSCADPQCVKIYDKEQIESSIIQMVRQRERMYQLQDLVCNRCNQVKAAHLTEQCECSGSFRCKESGSDFHKRIEIFLDIAKRQKFRLLEECISWILFATSC
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DNA polymerase II, which participates in chromosomal DNA replication (By similarity). Involved in the determination of cell fate during plant embryogenesis. Contributes to the flowering time repression. {ECO:0000250, ECO:0000269|PubMed:16212602, ECO:0000269|PubMed:16278345, ECO:0000269|PubMed:19947980}.
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F4IGZ2
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SMXL8_ARATH
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Protein SMAX1-LIKE 8 (AtSMXL8) (Protein D53-like 3) (AtD53-like 3) (Protein D53-like SMXL 8)
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MPTAVNVAKQCLTAEASYALEEAVNVARRRGHSQTTSLHAISALLSLPTSVLRDACARVRNSAYSPRLQFKALDLCLSVSLDRIQSGHQLGSDDSPPVSNSLMAAIKRSQAHQRRLPENFRIYQEMSQSQNQNSLSCVKVELRQLILSILDDPVVSRVFGEAGFRSSELKLSIIRPVPHLLRYSSQQPLFLCNLTGNPEPNPVRWGFTVPSLNFNGDLDYRRISAVFTKDKGRNPLLVGVSAYGVLTSYLNSLEKNQTDGMILPTKLHGLTAVNIGSEISDQISVKFDKTYTDTRFHDLGKLAEQGSGPGLLLHYGDLRVFTNGEGNVPAANYIVNRISELLRRHGRRVWLIGATTSNEVYEKMMRRFPNVEKDWDLQLLTITSLKPCLPHNKSSLIGSFVPFGGFFSTTPSELKLPFSGFKTEITGPVSSISDQTQSTLPPWLQMTTRTDLNQKSSAKVVQTKEGLESVCGNKFTSSASASTCSAKSVTTDLNLRVSSVTTGSGLKKHLDSKDFSQPQSVSSYSFDNPRDLNAESFKIIYRRLTDMVSGQDEAARVISCALSQPPKSVTRRDVWLNLVGPDTVGKRRMSLVLAEIVYQSEHRFMAVDLGAAEQGMGGCDDPMRLRGKTMVDHIFEVMCRNPFCVVFLENIEKADEKLQMSLSKAIETGKFMDSHGREVGIGNTIFVMTSSSQGSATTTSYSEEKLLRVKGRQVEIRIETVSSLPMVRSVYGPTSVNKRKLMGLGNLQETKDTVESVKRLNRTTNGVLDLNLPAQETEIEEKYHCEENSNVWLMNLKNHKRLIEVPFKPFDFEGLAEKIKKSVKENFDKCVRSDCLLEVDPKIIERLLAAVYFSDSRKDIKELLENIMSPVFLRIKERYEITTSCVVKLVGRDLDIFLEDQMDLFFVKSQ
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Probable component of a transcriptional corepressor complex involved in branching control. Regulates cotyledon expansion and lateral root growth, but not germination or hypocotyl elongation. Promotes auxin transport and PIN1 accumulation in the stem and represses BRC1/TCP18 expression in axillary buds.
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F4IH25
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BOP1_ARATH
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Ribosome biogenesis protein BOP1 homolog (Pescadillo-interacting protein 1) (AtPEIP1) (Protein BLOCK OF CELL PROLIFERATION 1)
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MTKRSKGANEDKLIETKSKNVSGKSQKQKKPVEAESLKEEDLLQASGTDSDYDGDSLPGSLNSDDFDSDFSDSEDDGTHEGTEDGDVEFSDDDDVLEHDGSIDNEDDDGSEHVGSDNNEEHGSDEDSERGEAVEESDSSEDEVPSRNTVGNVPLKWYEDEKHIGYDLTGKKITKKEKQDKLDSFLATIDDSKTWRKIYDEYNDEDVELTKEESKIVQRILKGEAPHADFDPYAPYVEWFKHDDAIHPLSSAPEPKRRFIPSKWEAKKVVKIVRAIRKGWIKFDKPEEEPNVYLLWGDDSTSDQKSKHLTYIPPPKLKLPGHDESYNPSLEYIPTEEEKASYELMFEEDRPKFIPTRFTSLRSIPAYENALKESFERCLDLYLCPRVRKKRINIDPESLKPKLPSRKDLRPYPNSCYLEYKGHTGAVTSISTDSSGEWIASGSTDGSVRMWEVETGRCLKVWQFDEAIMCVAWNPLSRLPVLAVAMGRDLFFLNTELGTDEEQEITKERLHSGNIPEPDASVAAIVTWLPDELYGGIKIRHFKSISSIDWHRKGDYLSTVMASGETRGVVLHQLSKQKTQRLPFKIRGLPVCTLFHPSLSYFFVATRKDVRVYNLLKPGEATKKLETGLREISSMAIHPGGDNLIVGSKEGKMCWFDMDLSSKPYKTLKNHPKDITNVAVHRSYPLFASCSEDSTAYVFHGMVYNDLNQNPLIVPLEILRGHSSKGGVLDCKFHPRQPWLFTAGADSIIKLYCH
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Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit (By similarity). Plays an essential role in cell growth and survival through its regulation of ribosome biogenesis and mitotic progression. {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000269|PubMed:26940494}.
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F4IH31
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CAN2_ARATH
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Staphylococcal-like nuclease CAN2 (EC 3.1.31.-) (Calcium-dependent nuclease 2) (AtCAN2) (Ca(2+)-dependent nuclease 2)
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MGNALTFLYGKCCKPTTTDDSLGPHGVSAATVGVSALAHDLFNFEITSQVPEGLGRYVQSSRKAQANWYRKILEAWKQAKPPPQTAEEASRLVTDILKRNQKADVEGLLSFYGLPLSHTLVEVTVEAPVSLPEGILFEFQTLPVDPKAVADGDTITVYVSTSEPVVSSSVPREVNLAAVQRAKAREKRNYPKADELHQKIIDSGYRVLNIENEEVLARKFRIRLRGIDAPESQMPFGKEAQEGLLKIVGRKSLKVLVYGEDQYGRCVGDLYCNGIFVQEAMLKKGLAWHYLAYDKRPVLAKWEKEARQKRIGLWASSNPEKPWDWRKNNRRE
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Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond. Possesses activity toward the single-stranded DNA, double-stranded DNA and RNA. May be involved in genomic DNA degradation during programmed cell death.
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F4IHS2
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SYD_ARATH
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Chromatin structure-remodeling complex protein SYD (EC 3.6.4.-) (ATP-dependent helicase SYD) (Protein CHROMATIN REMODELING 3) (Protein SPLAYED)
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MTSSSHNIELEAAKFLHKLIQDSKDEPAKLATKLYVILQHMKTSGKENTMPYQVISRAMDTVVNQHGLDIEALKSSCLPHPGGTQTEDSGSAHLAGSSQAVGVSNEGKATLVENEMTKYDAFTSGRQLGGSNSASQTFYQGSGTQSNRSFDRESPSNLDSTSGISQPHNRSETMNQRDVKSSGKRKRGESSLSWDQNMDNSQIFDSHKIDDQTGEVSKIEMPGNSGDIRNLHVGLSSDAFTTPQCGWQSSEATAIRPAIHKEPGNNVAGEGFLPSGSPFREQQLKQLRAQCLVFLALRNGLVPKKLHVEIALRNTFREEDGFRGELFDPKGRTHTSSDLGGIPDVSALLSRTDNPTGRLDEMDFSSKETERSRLGEKSFANTVFSDGQKLLASRIPSSQAQTQVAVSHSQLTFSPGLTKNTPSEMVGWTGVIKTNDLSTSAVQLDEFHSSDEEEGNLQPSPKYTMSQKWIMGRQNKRLLVDRSWSLKQQKADQAIGSRFNELKESVSLSDDISAKTKSVIELKKLQLLNLQRRLRSEFVYNFFKPIATDVEHLKSYKKHKHGRRIKQLEKYEQKMKEERQRRIRERQKEFFGGLEVHKEKLEDLFKVRRERLKGFNRYAKEFHKRKERLHREKIDKIQREKINLLKINDVEGYLRMVQDAKSDRVKQLLKETEKYLQKLGSKLKEAKLLTSRFENEADETRTSNATDDETLIENEDESDQAKHYLESNEKYYLMAHSIKENINEQPSSLVGGKLREYQMNGLRWLVSLYNNHLNGILADEMGLGKTVQVISLICYLMETKNDRGPFLVVVPSSVLPGWQSEINFWAPSIHKIVYCGTPDERRKLFKEQIVHQKFNVLLTTYEYLMNKHDRPKLSKIHWHYIIIDEGHRIKNASCKLNADLKHYVSSHRLLLTGTPLQNNLEELWALLNFLLPNIFNSSEDFSQWFNKPFQSNGESSAEEALLSEEENLLIINRLHQVLRPFVLRRLKHKVENELPEKIERLIRCEASAYQKLLMKRVEDNLGSIGNAKSRAVHNSVMELRNICNHPYLSQLHSEEVNNIIPKHFLPPIVRLCGKLEMLDRMLPKLKATDHRVLFFSTMTRLLDVMEDYLTLKGYKYLRLDGQTSGGDRGALIDGFNKSGSPFFIFLLSIRAGGVGVNLQAADTVILFDTDWNPQVDLQAQARAHRIGQKKDVLVLRFETVNSVEEQVRASAEHKLGVANQSITAGFFDNNTSAEDRKEYLESLLRESKKEEDAPVLDDDALNDLIARRESEIDIFESIDKQRKENEMETWNTLVHGPGSDSFAHIPSIPSRLVTEDDLKLLYETMKLNDVPMVAKESTVGMKRKDGSMGGLDTHQYGRGKRAREVRSYEEKLTEEEFEKLCQTESPDSPQGKGEGSERSLANDTSNIPVENSSDTLLPTSPTQAITVQPMEPVRPQSHTLKEETQPIKRGRGRPKRTDKALTPVSLSAVSRTQATGNAISSAATGLDFVSSDKRLEAASHPTSSLALTSPDLSGPPGFQSLPASPAPTPIRGRGRGRSRGRGAGRGRRVEGVLHGSNSSITQRTETATSLASDAEATKFALPRSASEIVSRVPKANEGSTSNPDQVSPVHSATTALRSDKAADKDLDAPPGFDSGSHVQTLNVLENSSERKAFAVKKRPLIQGVSSQHPGPNKQPLDLPVSTSSTLLGGGPVQNQNAVSSVCDGSKSPSEGRTYTALQGVTTAPSDATLPMSSQPSDATLPMSSQPVGSTVEAQEANVPSLPAALPAKRRVRNLPSRGETPKRQGKRRGQPLPATDASSARSTGLTPQIEVKVGNLSGTKAKFDAVAKEQPHFSQSVAPDIHSSGSLSQEIRRDTSGTGGSARKQTADVTDVARVMKEIFSETSLLKHKVGEPSATTRTNVPDAQSPGEMNLHTVETHKAEDSSGLKNQEALYNLSKADKLVSDIPHPVPGDLTTSGSVANKDVDIGSSKVAAENELVKIPGGDVDSSVIQLSLGNTLTAKSSLEKCTADQLLGEKLSQEGETTPASDGETCHLAEETASSLSYVRSEPTASASTTAEPLPTDKLEKNISFQDEVKTLNGDKREAILLSSEEQTNVNSKIETNSEELQASRTDEVPHVDGKSVDVANQTVKEDEAKHSVEIQSSMLEPDELPNAGQKGHSSIDLQPLVLVTSNENAMSLDDKDYDPISKSADIEQDPEESVFVQGVGRPKVGTADTQMEDTNDAKLLVGCSVESEEKEKTLQSLIPGDDADTEQDPEESVSDQRPKVGSAYTQMEDTDEAKLLMGCSVESEEKEKTLQSHIPGDDADTEKNPEESVSVQGVDRPKVGTTDTQMEDTNDAKLLVGCSVASEEKEKTLQSHIPGDDADTEQNPEESVSVQGVNRPKVGNANTQMEDTDEAKVLVGCSVESEEKEKTLQSHIPGDDADTEQNPEESVSNFDRPKDGTADTHMEDIDDAKLLVGCSVESEEKEKSLQSHMPSDDAVLHAPFENTKDSKGDDLHGESLVSCPTMEVMEQKGFESETHARTDSGGIDRGNEVSENMSDGVKMNISSVQVPDASHDLNVSQDQTDIPLVGGIDPEHVQENVDVPASPHGAAPNIVIFQSEGHLSPSILPDDVAGQLESMSNDEKTNISSEQVPDVSHDLKVSQDQTDIPPVGGIVPENLQEIVDVPASPHGVVPDVVVSQSEEIQSPSILPDDVPGQPDDGNCEKMDTMQNNTSIDIGITSGKTCQPSSSTQPEDENRNSLSHCEPSEVVEQRDSRDQVCIGSVESQVEISSAILENRSADIQPPQSILVDQKDIEESKEPGIESADVSLHQLADIQAEPSNLVDQMDIEESKEPGTESADVSLHQLADIQPGPSILVDQMDTEKSKEPGTESADVSLHQLADIQPGPSILVDQMDTEKSKEPGTESADVSLHQLADIQPGPSILVDQMDTEEFKNPDVSLHQLADIEPSLSISAVQKNIEDKDQSHVETAGSELVDVSAECSTEPQVQLPPSSEPVGDMHVHLGASKSEIVAEGTDFSSSLPKTEEENAKSQLADTEPSSSLTAVQKNIEDQVETAGCEFVVVSTGCSTEPQVQLPPSAEPVVAEGTEFPSSLLMTGVDNSSHLMTGVDNAKTHLADVVPSSSPTTMEKNIEAQDQDQVTTGGCGLVDVLTECSSEPQLQLPPSAEPVISEGTELATLPLTEEENADSQLANIEPSSSPSVVEKNIEAQDQDQVKTAGCELVSTGCSSEPQVHLPPSAEPDGDIHVHLKETEKSESMVVVGEGTAFPSSLPVTEEGNAESQLADTEPFTSPTVVEKNIKDQEQVETTGCGLVDDSTGCSSEPQVQLPPSAEPMEGTHMHLEETKKSETVVTEIQLADIDPSFSLIVVQTNIEDQDQIETGGCDLINVPSGCSTEPQIQLSSSAEPEEGMHIHLEAAMNSETVVTEGSELPSSLPMTEDENADGQLAEVEPSVSLTVEQTNIEEKDHIETAECELVDVSPGCSSQPEVKFPPSPDAVGGMDVHLETVVTEDTDSNSSLPKTEEKDAENPSDRLDGESDGTTVATVEGTCVESNSLVAEESNIEVPKDNEDV
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Catalytic component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls stem cell fate via the transcription regulation of WUS in the shoot apical meristem, by modulating its promoter. LFY-dependent repressor of the meristem identity switch from vegetative to reproductive development probably by modulating chromatin state. Involved in the regulation of floral homeotic gene expression in response to environmental stimuli. Required for carpel and ovule development, and for cotyledon separation via the regulation of CUC2 transcription. Regulates the promoters of several genes downstream of the jasmonate (JA) and ethylene (ET) signaling pathways. Required for resistance against the necrotrophic pathogen B.cinerea but not the biotrophic pathogen P.syringae.
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F4IHS9
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UXT1_ARATH
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UDP-xylose transporter 1
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MGEMKSMQMGVIGALFLSVASSVSIVICNKALMTNLGFPFATTLTSWHLMVTYCTLHVAYKLNFFENKPIDMRTVVLFGLLNGISIGLLNLSLGFNSIGFYQMTKLAIIPFTVLLETLFLNKKFSQKIKFSLFLLLVGVGIASITDLQLNFVGSVLSLLAIATTCVGQILTNTIQKRLNVTSTQLLYQSAPFQAAILFVSGPFVDKYLTSLNVFSFHYSPIVVGFITLSCLIAVSVNFSTFLVIGKTSPVTYQVLGHLKTCLVLAFGYTLLHDPFTPRNIAGILIAVLGMLLYSYFCSVASKSKQASSDSTFLGKDRDTTPLLGQENENHHEAKKLDKHSPV
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Nucleotide-sugar transporter that transports UDP-xylose and UMP in a strict counter-exchange mode.
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F4IHY7
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PTA12_ARATH
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Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic (pTAC12) (Plastid-encoded RNA polymerase-associated protein 5) (PEP-associated protein 5) (Protein HEMERA)
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MASISTTTWLYRGQVCTDSGKSSNCIVQRRVKCGFPLKTLHAGITSRDRSLRHCIKCKKEDGDGDVSEGSKKSEEGFEYVTVERHPYHSYMDSTSGKLEPASGARASIPGEDYWPEGTSSRVRAARAPQPAGESSSFPSYGKNPGSRRKKNRKATEENVTVETNDEVSDSEDSSEEEENDSSDGFVTYKNEFEREEEETGFELDKKLGRPHPFIDPTKKKQIEKTLTSDESWWNWRKPEKEQWSRWQRRRPDVETVFLKAMAETGQVKLYGEEPTLTETSLYRARRHLFKEERLQAERERLAKEGPMAFYSEWVKAWKRDTSREAVQKHFEETGEDENTQLIEMFSHQTDREYRIMMGTDIRIKRDPLAMRMREDQIKQIWGGDPVYPTINYIQDPNAVMDFRGPDFHEPTPNMLSYLKENGKVISREMHEALLTKEKTEQLEVPDMDDAMAQAVDIGENDDDEDDADVEKDDEKVPRNWSVLKETPELRTAKPKPKKEGRMSLDEAVDDAENLTDFLMDFEEETDP
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Involved in plastid gene expression. Required in the nucleus for the initiation of photomorphogenesis mediated by phytochromes (PHYs) (e.g. PHYA and PHYB) by mediating PHYs localization to photobodies, especially in response to red and far-red light, and implicating phytochrome nuclear bodies as sites of proteolysis for PHYs and PIFs proteins (e.g. PIF1 and PIF3). Acts downstream of PHYs and upstream of DET1.
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F4IIM1
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CSI1_ARATH
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Protein CELLULOSE SYNTHASE INTERACTIVE 1 (Protein POM-POM 2)
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MTSALGWRFPSTNGNGLAPSDTERNGDMKMHDSEPPTPHSTTKMSLRDRTTSMEDPDGTLASVAQCIEQLRQGSSSAQEREYCLKQLLDLIEMRENAFSAVGSHSQAVPVLVSLLRSGSVGVKIQAATVLGSLCKENELRVKVLLGGCIPPLLGLLKSSSVEGQIAAAKTIYAVSEGGVKDHVGSKIFSTEGVVPVLWDQLRSGNKKGEVDGLLTGALKNLSSTTEGFWSETIRAGGVDVLVKLLTSGQSSTLSNVCFLLACMMMEDASVCSSVLTADITKQLLKLLGSGNEAPVRAEAAAALKSLSAQSKEAKREIANSNGIPVLINATIAPSKEFMQGEYAQALQENAMCALANISGGLSYVISSLGQSLESCSSPAQTADTLGALASALMIYDGKAETTRASDPLVVEQTLLKQFKPRLPFLVQERTIEALASLYGNSILSVKLSNSDAKRLLVGLITMAVNEVQDELVKALLMLCNHEGSLWQALQGREGIQLLISLLGLSSEQQQECAVALLCLLSNENDESKWAITAAGGIPPLVQILETGSAKAREDSATILRNLCNHSEDIRACVESADAVPALLWLLKNGSPNGKEIAAKTLNHLIHKSDTATISQLTALLTSDLPESKIYVLDALKSMLSVVPFNDMLREGSASNDAIETMIKLMSSGKEETQANSASALAAIFQSRKDLRESALALKTLLSAIKLLNVDSERILVESCRCLAAILLSIKENRDVAISAREALPTIVSLANSSVLEVAEQGMCALANLILDSEVSEKVIVEDIILSATRILREGTVSGKTLAAAAIARLLSRRRIDSALTDSVNRAGTVLTLVSLLESADGRSDAISEALDALAIFSRSGANGNVKPAWAVLAESPNSMAPIVSSIVSVANPSLQDKAIEVLSRLCRDQPIVLGNMVNNARDCVSSIAKRVINTRDPKIKIGGAAIIICAAKVDDQKMIENLNETQLCAKFVQALVGILDSVQDQEKDEKDKICICIHPKEKEEDEEEEATENREGSTGATVISGDNLAIWLLSVLSCHDEKSRAVILESEGIELITDRIGNRFLQADNGEDANIWVCALLLAILFQDREITRAHATMKAVPVLSNLVKSEEYADRYFAAQALASLVCNGSRGTLLSVANSGAAAGFISLLGCSDDDIKELLQLSQEFTLVRYPDQVALERLFRVEDIRVGATSRKAIPLLVELLKPIPDRPGAPLLSLNLLTQLAGDCPQNMIVMVESGALEGLSKYLSLGPQDEQEEAATGLLGILFSSAEIRRHESAFGAVSQLVAVLRLGGRGARYSAAKALDSLFTADHIRNAESSRQAVQPLVEILNTGSEREQHAAIAALVRLLSDNPSRALAVADVEMNAVDVLCRILSSNYTMELKGDAAELCYVLFANTRIRSTVAAARCVEPLVSLLVTEFSPAQHSVVRALDKLVDDEQLAELVAAHGAVVPLVGLLYGKNYVLHEAISRALVKLGKDRPACKLEMVKAGVIDCVLDILHEAPDFLCAAFSELLRILTNNATIAKGQSAAKVVEPLFHLLTRLEFGADGQHSALQVLVNILEHPQCRADYTLTPHQVIEPLIPLLESPSPAVQQLAAELLSHLLYEEHLQKDPLTQLAIGPLIHVLGSGIHLLQQRAVKALVSIALTWPNEIAKEGGVSELSKVILQADPSLSNVLWESAASILVIILQFSSEFYLEVPVAVLVRLLRSASENTVVGALNALLVLESDDGTSAESMAESGAIEALLDLLRSHQCEDTAARLLEVLLNNVKIRDSKATKTAILPLSQYLLDPQTQAQQARLLATLALGDLFQNEALARSTDAASACRALVNVLEEQPTEEMKVVAICALQNLVMYSRSNKRAVAEAGGVQVVLDLISSSDPETSVQAAMFVKLLFSNHTVQEYASSETVRAITAAIEKDLWATGTVNDEYLKALNSLFNNFPRLRATEPATLSIPHLVTSLKTGSEATQEAALDALFLLRQAWSACPAEVSRAQSVAAADAIPLLQYLIQSGPPRFQEKAEFLLQCLPGTLVVTIKRGNNMKQSVGNPSVFCKITLGNNPPRQTKVISTGPNPEWDESFSWSFESPPKGQKLHISCKNKSKMGKSSFGKVTIQIDRVVMLGAVAGEYSLLPESKSGPRNLEIEFQWSNK
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Regulator of the microtubular cytoskeleton. Microtubule-associated protein essential for the functional association of cellulase synthase (CESA) complexes (CSCs) and cortical microtubules. Promotes dynamics of CSCs in the plasma membrane. Regulates primary cell wall biosynthesis and cellulose microfibrils organization. Required for the regulation of root cell elongation/expansion. Necessary for the formation of ovules, pollen cell wall morphogenesis and pollen tube development. Involved in anther dehiscence, via dehydration-induced microtubule depolymerization and reorganization. May play a role in early gynoecial development. Target of the cellulase synthase (CESA) complexes (CSCs) trafficking inhibitor CESTRIN, which reduces cellulose content and alters anisotropic growth of hypocotyls CESTRIN treatment inhibits the dynamics of CSCs.
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F4IIS5
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KN5A_ARATH
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Kinesin-like protein KIN-5A (AtKRP125c) (Protein LOOPHOLE) (Protein RADIALLY SWOLLEN 7)
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MDSNNSKKGSSVKSPCQTPRSTEKSNRDFRVDSNSNSNPVSKNEKEKGVNIQVIVRCRPFNSEETRLQTPAVLTCNDRKKEVAVAQNIAGKQIDKTFLFDKVFGPTSQQKDLYHQAVSPIVFEVLDGYNCTIFAYGQTGTGKTYTMEGGARKKNGEIPSDAGVIPRAVKQIFDILEAQSAAEYSLKVSFLELYNEELTDLLAPEETKFADDKSKKPLALMEDGKGGVFVRGLEEEIVSTADEIYKVLEKGSAKRRTAETLLNKQSSRSHSIFSVTIHIKECTPEGEEIVKSGKLNLVDLAGSENISRSGAREGRAREAGEINKSLLTLGRVINALVEHSGHIPYRESKLTRLLRDSLGGKTKTCVIATVSPSVHCLEETLSTLDYAHRAKHIKNKPEVNQKMMKSAIMKDLYSEIERLKQEVYAAREKNGIYIPKERYTQEEAEKKAMADKIEQMEVEGEAKDKQIIDLQELYNSEQLVTAGLREKLDKTEKKLYETEQALLDLEEKHRQAVATIKEKEYLISNLLKSEKTLVDRAVELQAELANAASDVSNLFAKIGRKDKIEDSNRSLIQDFQSQLLRQLELLNNSVAGSVSQQEKQLQDMENVMVSFVSAKTKATETLRGSLAQLKEKYNTGIKSLDDIAGNLDKDSQSTLNDLNSEVTKHSCALEDMFKGFTSEAYTLLEGLQGSLHNQEEKLSAFTQQQRDLHSRSMDSAKSVSTVMLDFFKTLDTHANKLTKLAEDAQNVNEQKLSAFTKKFEESIANEEKQMLEKVAELLASSNARKKELVQIAVQDIRQGSSSQTGALQQEMSAMQDSASSIKVQWNSHIVQAESHHLDNISAVEVAKEDMQKMHLKCLENSKTGTQQWKTAQESLVDLEKRNVATADSIIRGAIENNEKLRTQFSSAVSTTLSDVDSSNREIISSIDNSLQLDKDASTDVNSTIVPCSENLKELRTHHDDNVVEIKQNTGKCLGHEYKVDEATSSTPRKREYNIPTVGSIEELKTPSFEELLKAFHDCKSPKQMQNGEAKHVSNGRPPLTAIN
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Responsible for microtubule translocation. May be important for the organization of phragmoplast-specific arrays of microtubules (By similarity). Plays an essential role in stabilizing the mitotic spindle. Required during mitotic cytokinesis.
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F4IIU4
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AIR9_ARATH
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187-kDa microtubule-associated protein AIR9 (Auxin-induced in root cultures protein 9)
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MEEVAAKVEEETVETNVDAVKEDNATIANESRSPESVSAVSVVSNRAASTKKKPVISSNLIKPTASSSLRVSGTTPVTIRRNSTGGVTENLAGTSKVLPKQVSTTASRTDPVRRSLPELRKSSVSSLSAKTVSKPSLSESKKSVPVSPGSRSLTKSTGFSLSKPESSARPAMSVSVSSKRAPSSSVDSSGSRTSSGRLHSTLTSGRTVSKVSSPSAGSSPSVSSSIRSKSFSSPLDRTSNFSGRKKTSTPESRDSRLIILPKVEVKAGDDMRLDLRGHRIRSLTSGGLHLSPNLEFVYLRDNLLSTLEGIEILNRVKVLDLSFNDFKGPGFEPLENCKMLQQLYLAGNQITSLASLPQLPNLEFLSVAQNKLKSLAMASQPRLQVLAASKNKITTLKDFPYLPVLEHLRVEENPLLKISHLEAASILLVGPTLKKFNDRDLSREEVAIAKRYPPQTALCLREGWEFCKSDLAAESTFRFLVERWKDTLPSGYLIKEAHVDRPSEEAPCQCHFGLFQESPTATDQELALKFQWSVADRSLSNFVPILNATKEVYWPKREDIGKILKIECTPVMAETEYPSIFAISSPVQRGKGIPKVVSLELNGELVEGNIIKGQAVVAWCGGTPGKCITSWLRRKWNGSPVVIDGAEDEEYMLSLDDVGSSMVFMYTPVTEGGARGEPQYKYTEFVKAAPPSVSNVRITGDAVEGCVLKGVGDYFGGKEGPSKFEWLRKNKETGELSLISAGTSEYTLTQEDVGTHVTFVYIPANFEGLEGEPVSTSSSVVKPAPPKVTDAKIVGDLRENSKVTVTGTVTGGTEGSSRVQWFKSSCSILEGDNSLEELSTSKVAKSFRIPLGAVGYYIVAKYTPMTPDGECGEPVYVLSERAVETLPPSLNFLSITGDNIEGGILTASYGYIGGHEGKSKYEWHYHKAENDLPGALIPEASGLLQYTITKEAIGKFISFQCIPVRDDGIVGEPRSCMSQERVRPGNPSTVSLHVVGALVEGTMLSAEKEYWGGEEGASVFRWFRTNSDGTPCEIKGATTSSYLLSVGDIGYFISVSYEPVRNDRARGPTAISEIAGPIVAGHPNCQSLEFLGSMIEGQRLSFVASYTGGMKGNCYLEWVRVKNNGVKEILSSDEFLDLSLDDVGESIELIYTPVREDGIEGSPRSIRTDGIAPANPMGLELLIPDCCEKQEVVPHKTYFGGHEGVGEYIWYRTKVKLHGSALTEISYAGEEVVVCCRTLKYTPSLEDVGAYLVLYWIPTRVDGRSGKPVVVITNSPVAPADPEVSNVRVKKLFSDAYSGEGEYFGGHEGPSLFSWYRENDGTIDLIDGANSKTYEVTESDYNCRILFGYTPVRSDSVVGELKMSEPTEIILPEVPKVDMLAFTGKAVQGDVLTAVQVIPKTEIQQLVWSKYKGDIQYQWFRSPESGDKISYEALSSEISCSYKVRFEDIGRCLKCECVVHDVFGRSSELAYAETDPISPGFPRIEKLEIEGQGFHTNLYAVRGNYFGGKEGKSKIQWLRSMVGSPDLISIPGETGRMYEANVDDVGYRLVVVYTPIREDGVQGHPVSASTEPVAVEPDILKEVRQKLETGLVKFEVLCDKDPYPKKIVGEGNLERRMLEMNRKRIKVVKPGSKTSFATTEVRGSYGPPFHVETFRNDQRRLRIVVDSENEVDIVVQSRHLRDVIVLVIRGFAQRFNSTSLNSLLKIDT
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Microtubule-associated protein that may be involved in the maturation of cell plates and proper insertion of cross-walls after cytokinesis.
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F4IMH3
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NOC4_ARATH
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Protein NUCLEOLAR COMPLEX ASSOCIATED 4 (AtNoc4) (Protein EMBRYO DEFECTIVE 2762)
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MASILSKKQKKNEKYTLKELKSLGHDLLTSRSHINNLPLLLTFVSPESPPQFVVESLLSLQSFFTPLLSQLPPTSSSPSSTKTEDPEVVFKAWLRSKFDEFVKLLLDVLVSQQSEDSLRGIVLGTLMEFVKLLNAGRFHSSIYHRLLDAIIHSEVDIEIFLDILTSKYFKYIDVRYFTYISMEKFVKTLEASVSADRTVIENNEAESDSKESLELSVRKIYQVLSQIPPPEKQAEKSQHEMWSGSDESISEKPTDKKKKTEKGDSTLLSPATISKRMKLKFTKAWISFLRLPLPIDVYKEVLASIHLTVIPHLSNPTMLCDFLTKSYDIGGVVSVMALSSLFILMTQHGLEYPFFYEKLYALLVPSVFVAKHRAKFLQLLDACLKSSMLPAYLAASFTKKLSRLSLSIPPAGSLVITALIYNLLRRNPTINHLVQEIVENADEANTEAGEHNESQPKTIKKRKLGIDYFNNQESDPKKSGALKSSLWEIDTLRHHYCPPVSRFISSLETNLTIRSKTTEMKIEDFCSGSYATIFGDEIRRRVKQVPLAFYKTVPTSLFADSDFPGWTFTIPQEEGTC
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Essential protein required during embryogenesis. Involved in nucleolar processing of ribosomal RNA (rRNA) 40S and 90S ribosomal subunits and ribosome assembly early in ribosome biogenesis, especially required during the maturation of 5.8S rRNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity).
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F4IN23
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BZP34_ARATH
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Basic leucine zipper 34 (AtbZIP34) (bZIP protein 34)
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MAQLPPKIPNMTQHWPDFSSQKLSPFSTPTATAVATATTTVQNPSWVDEFLDFSASRRGNHRRSISDSIAFLEAPTVSIEDHQFDRFDDEQFMSMFTDDDNLHSNPSHINNKNNNVGPTGSSSNTSTPSNSFNDDNKELPPSDHNMNNNINNNYNDEVQSQCKMEPEDGTASNNNSGDSSGNRILDPKRVKRILANRQSAQRSRVRKLQYISELERSVTSLQAEVSVLSPRVAFLDHQRLLLNVDNSALKQRIAALSQDKLFKDAHQEALKREIERLRQVYNQQSLTNVENANHLSATGAGATPAVDIKSSVETEQLLNVS
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Transcriptional activator involved in the sporophytic control of cell wall patterning and gametophytic control of pollen development. May play a role in the control of metabolic pathways regulating cellular transport and lipid metabolism.
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F4IN69
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MD33B_ARATH
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Mediator of RNA polymerase II transcription subunit 33B (Protein REDUCED EPIDERMAL FLUORESCENCE 4) (AtREF4)
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MAPSEFQPSLWESVTSLIRSAQEKNVDPLHWALQLRLTLASAGISLPSPDLAQFLVTHIFWENHSPLSWKLLEKAISVNIVPPLLVLALLSPRVIPNRKLHPAAYRLYMELLKRHAFSFMPLIRAPGYHKTMNSIDDILHLSETFGVQDQEPGSILLAFVFSIVWELLDASLDEEGLLELTSNKRSKWPSSPHDMDLDGLENSVKRNENHDALEKANTEMAIELIQEFLQNKVTSRILHLASQNMESKTIPRGEFHAIVSSGSKLALTSDSALWLPIDLFFEDIMDGTQAAAASAVENLTGLVKALQAANSTSWHDAFLALWLAALRLVQRENLCLRYCFFMHMLEILSEERDPIEGPVPRTDTFLCVLLSVTPLAVANIIEEEESQWIDQTSSSPSNQWKEKKGKCRQGLINSLQQLGDYESLLTPPRSVQSVANQAAAKAIMFISGITNSNGSYENTSMSESASGCCKVRFSLFTLKMFVVMGVYLLCNISCWSLVMKGSPLTPSLTNSLITTPASSLAEIEKMYEVATTGSEDEKIAVASILCGASLFRGWSIQEHVIIFIVTLLSPPAPADLSGSYSHLINSAPFLNVLLVGISPIDCVHIFSLHGVVPLLAGALMPICEAFGSGVPNITWTLPTGELISSHAVFSTAFTLLLRLWRFDHPPLDYVLGDVPPVGPQPSPEYLLLVRNCRLECFGKSPKDRMARRRFSKVIDISVDPIFMDSFPRLKQWYRQHQECMASILSELKTGSPVHHIVDSLLSMMFKKANKGGSQSLTPSSGSSSLSTSGGDDSSDQLKLPAWDILEAAPFVLDAALTACAHGSLSPRELATGLKILADFLPATLGTMVSYFSSEVTRGLWKPVSMNGTDWPSPAANLASVEQQIEKILAATGVDVPRLPADGISAATLPLPLAALVSLTITYKLDKATERFLVLVGPALDSLAAACPWPCMPIVTSLWTQKVKRWSDFLIFSASRTVFHHNRDAVIQLLRSCFTCTLGLTPTSQLCSYGGVGALLGHGFGSRYSGGISTAAPGILYIKVHRSIRDVMFLTEEILSLLMFSVKSIATRELPAGQAEKLKKTKDGSRYGIGQVSLSLAMRRVKLAASLGASLVWISGGLNLVQALIKETLPSWFISVHGEEDELGGMVPMLRGYALAYFAILSSAFAWGVDSSYPASKRRPRVLWLHLEFMVSALEGKISLGCDWATWQAYVTGFVSLMVQCTPAWVLEVDVEVIKRLSKSLRQWNEQDLALALLCAGGLGTMGAATELIVETCHQH
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Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Involved in the repression of phenylpropanoid biosynthesis. May compete with MED33B for common binding partners or for occupancy in Mediator.
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F4IPE3
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IDD15_ARATH
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Zinc finger protein SHOOT GRAVITROPISM 5 (Protein indeterminate-domain 15) (AtIDD15)
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MRTDQVMLSNKNTNTCCVVSSSSSDPFLSSSENGVTTTNTSTQKRKRRPAGTPDPDAEVVSLSPRTLLESDRYICEICNQGFQRDQNLQMHRRRHKVPWKLLKRDNNIEVKKRVYVCPEPTCLHHNPCHALGDLVGIKKHFRRKHSNHKQWVCERCSKGYAVQSDYKAHLKTCGTRGHSCDCGRVFSRVESFIEHQDNCSARRVHREPPRPPQTAVTVPACSSRTASTVSTPSSETNYGGTVAVTTPQPLEGRPIHQRISSSILTNSSNNLNLELQLLPLSSNQNPNQENQQQKVKEPSHHHNHNHDTTNLNLSIAPSSSYQHYNNFDRIKEIMASEQIMKIAMKEKAYAEEAKREAKRQREIAENEFANAKKIRQKAQAELERAKFLKEQSMKKISSTIMQVTCQTCKGQFQAVAVPAATADETSLVVSYMSSANTDGELENGF
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Transcription factor involved in inflorescence stems gravitropism, probably by regulating starch accumulation in amyloplasts of graviperceptive cells. Required for stem circumnutation movements. Regulates lateral organ morphogenesis and gravitropic responses. Acts cooperatively with IDD16 to control silique and branche orientation. Involved in the establishment of auxin gradients through the regulation of auxin biosynthesis and transport.
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F4IPK2
|
TAF14_ARATH
|
Transcription initiation factor TFIID subunit 14 (Protein AF-9 homolog b) (TBP-associated factor 14) (AtTAF14)
|
MESDIEILSEADASMRKLRIFGIDDREDENGRRRIKDVEVYVPIVCGSIAFYLGKKATEYRTHKWTVYVRGATNEDLGVVIKRVIFHLHPSFNNPTRVVDAPPFALSECGWGEFKIDITVFFHTDVCEKKLELSHVLKLNPENAYGPIPKSIKIPVVAESYNEVVFPDPFESFVARVHNHPAIQISNIPDGLNLPPPGVADTYYLMEKGDTKEHPLSPWFLKFSEVEELFKLTAARQKVQADIAKLKRQLIMVDGQPEGLESSSGYEC
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Negative regulator of flowering controlling the H4K5 acetylation levels in the FLC and FT chromatin. Positively regulates FLC expression. Component of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of a NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A.
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F4IPY2
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SYCM_ARATH
|
Cysteine--tRNA ligase, chloroplastic/mitochondrial (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (CysRS)
|
MASSVLNLFKSCRPFTPIRFSSLPKSQFRIQFPLRPGKETQLRRCFTTLSSLTDGGAPISGGKELWLHNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLLRYLKHLGYEVSYVRNFTDVDDKIIARAKELEEDPISLSRRFCEEFNRDMEQLQCLDPSVQPRVSDHIPQIIDLIKQILDNGYAYKVDGDIYFSVDKFPTYGKLSGRKLEDNRAGERVAVDTRKKHPADFALWKAAKEGEPFWESPWGRGRPGWHIECSAMSAAYLGYSFDIHGGGMDLVFPHHENEIAQSCAACDSSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLMGTHYRSPINYSDFLLESASERIFYIYQTLHDCESALGEKDSTFENGSVPSDTLTSINTFRTEFVASMSDDLLTPVTLAAMSEPLKTINDLIHTRKGKKQARREESLKALETTIRDVLTILGLMPTSYSEVLEQLKEKALKRAGLKEEDVLQRVQERTDARKNKEYERSDAIRKDLAKVGIALMDSPEGTTWRPAIPLALQEPVTTTP
|
Required for female gametophyte development. Is necessary for the fusion of central cell nuclei and programmed cell death (PCD) of the antipodals.
|
F4IQV7
|
SCY2_ARATH
|
Preprotein translocase subunit SCY2, chloroplastic (Protein EMBRYO DEFECTIVE 2289)
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MNSSQACFFHFSLRPISLSHPSYAFLSKRDPFLCSQPRKCLTTNLNMSRTRQGHSIQMNRRHLLMKERKSFSINYSDKFRDDSMSSEEMHTDALDVEIIPPDSQDIRNSQNSAVSNTLQDDRPKSFRNRFLDFVRISSVLNTAAERFFKSEIRRRLFVTAVLLVLSRVGYFIPLPGFDRRLIPQDYLSFVSGSVEELGEFGAEIKLSLFQLGLSPQIIASIIMQVLCHVLPSLVKLRKEGLDGHEKIKSYIWWLSFFFAIVEALVVAYTSLQYSVFAATAQVKHVMMTSSLLVCGAMTMTWLCDTISESGFGHGSSLIICVGILTGYTETLHKMLNQISGSFSNWLPYLLGLLGIFTVVTMFAVVVTEGCRKIKLQYYGFKLASASREGSPITEVEPYIPFNINPAGMQPVLTTTYLLAFPSILASILGSPFLLNMKEILNPESTVGAPPWVYYSIYAFFVFLFNIFDIANLPKEIADYLNKMGARIPNIKPGKATIEYLTKIQASTRFWGGLLLSFLATASTVLDHYLRSINQGFSIGFTSVLIIVGSIIELRRSYHAYNVMPSLSKALKRYGV
|
Involved in protein export. Probably interacts with other proteins to allow the postimport or conservative sorting pathway for inner membrane proteins in plastids. Central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity). {ECO:0000250, ECO:0000269|PubMed:21051552}.
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F4IRB4
|
MYB88_ARATH
|
Transcription factor MYB88 (Myb-related protein 88) (AtMYB88)
|
MEETTKQNNMKKKKKILLHSDDSKKKERHIVTWSPEEDDILRKQISLQGTENWAIIASKFNDKSTRQCRRRWYTYLNSDFKRGGWSPEEDTLLCEAQRLFGNRWTEIAKVVSGRTDNAVKNRFTTLCKKRAKHEAMAKENRIACCVNSDNKRLLFPDGISTPLKAESESPLTKKMRRSHIPNLTEIKSYGDRSHIKVESTMNQQRRHPFSVVAHNATSSDGTEEQKQIGNVKESDGEDKSNQEVFLKKDDSKVTALMQQAELLSSLAQKVNADNTDQSMENAWKVLQDFLNKSKENDLFRYGIPDIDFQLDEFKDLVEDLRSSNEDSQSSWRQPDLHDSPASSEYSSGSGSGSTIMTHPSGDKTQQLMSDTQTTSHQQNGGELLQDNGIVSDATVEQVGLLSTGHDVLKNSNETVPIPGEEEFNSPVQVTPLFRSLAAGIPSPQFSESERNFLLKTLGVESPSPYPSANPSQPPPCKRVLLDSL
|
Transcription factor that binds to DNA in promoters cis-regulatory element 5'-GGCGCGC-3' of cell cycle genes, including cyclins, cyclin-dependent kinases (CDKs), and components of the pre-replication complex. Binds to DNA in promoters cis-regulatory element 5'-AGCCG-3' of auxin regulated genes (e.g. PIN3 and PIN7). Together with FAMA and MYB124, ensures that stomata contain just two guard cells (GCs) by enforcing a single symmetric precursor cell division before stomatal maturity. Represses the expression of the mitosis-inducing factors CDKB1-1 and CDKA-1, specifically required for the last guard mother cells (GMC) symmetric divisions in the stomatal pathway. Represses CYCA2-3 in newly formed guard cells. Together with MYB88, regulates stomata spacing by restricting divisions late in the stomatal cell lineage thus limiting the number of GMC divisions. In collaboration with CDKB1-1 and CDKB1-2, restrict the G1/S transition and chloroplast and nuclear number during stomatal formation, and normally maintain fate and developmental progression throughout the stomatal cell lineage. Involved in sensing and/or transducing abiotic stress (e.g. drought and salt), probably via the positive regulation of NAC019. Regulates female reproduction being required for entry into megasporogenesis, probably via the regulation of cell cycle genes. Plays a minor role in lateral roots (LRs) initiation. Involved complementarily in establishing the gravitropic set-point angles of lateral roots by regulating the transcription of PIN3 and PIN7 in gravity-sensing cells of primary and lateral roots.
|
F4IRR2
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SAD2_ARATH
|
Importin beta-like SAD2 (Protein ENHANCED MIRNA ACTIVITY 1) (Protein SUPER SENSITIVE TO ABA AND DROUGHT 2) (Protein UNARMED 9)
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MDLHSLALILRTAALSPIPDERKVSEQQLNQLEHTPQHLVRLLQIAVDGNCDMAVRQIASIQFKNLIAKNWSPEDCGPAVRQQQIFESDKELVRDNILVYVTQVPTLLRSQLGESLKTIIYADYPEQWPRLLDWVKYNLQNQQIYGALFVLRILSRKYEFKSDEERTPVSRIVEETFPQLLTIFNGLIQIPNPSLEIAELMKLICKIFWSSIYLELPRQLFDLNVFNAWMVLFLSVSERPVPVEGQPMDPELRKSWGWWKVKKWTVHILNRLYSRFGDPKLQSPENKPFAQMFQKNYAGRILEGHLNFLNTIRVGGYLPDRVINLLLQYLSNSISKNSMYKLLLPRLDVLLFEIVFPLMCFNDNDQKLWEEDPHEYVRKGYNIIEDLYSPRTASMDFVNELVRKRGKENLPKFVKFVVEIFLSYEKATVEEKPYRQKDGAMLAVGALCDKLKQTDPYKSQLELMLVQHIFPDFNSPVGHLRAKAAWVAGQYAHINFSDQNNFRKALHSVVSGLRDPDLPVRVDSVFALRSFVEACKDLNEIRPILPQLLDEFFKLMNEVENEDLVFTLETIVDKFGEEMAPFAFGLCQNLAAAFWRCLNTSEANDDSDDMGALAAVGCLRAISTILESVSSLPQLFVEIEPTILPIMQKMLTTDGQEVFEEVLEIASYMTFYSPSISLDIWSLWPLMVEALVDWGIDFFPNILVPMDNFISRGTAHFLTCKEPDYQQSLYNVLSTLMTDRNIEDSEIESAPKLIEVVFQNCKGQVDQWVEPYLRLTVDRLQRAETSYVKSLLIQVVANMLYYNPGLTLGVLHNTGLASKVFDLWFQMLQQKRKSGLPANFKREHDKKVCCLGLTSLLALPGGQFPDEALQRVFRATLDLLVAYKNQLAEAAKETEVDYEEEMNGLQSSDDDYDDDGSDGEMDDTEEGDEAQSVKLQKLAAQAKAFHYDDDDDDDSDDDFSDEDEFQSPIDEVDAFVFFVDAIRVMQASDAQRFQNLNQSLDFTYQAIANGIAQHAELRRVEIEKEKQKKLAAASTPVTAL
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Functions probably in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with other importin subunits (Probable). Involved in the regulation of the abscisic acid (ABA)-mediated pathway in response to cold or salt stress. Involved in UV-B responses by regulating accumulation of UV-absorbing pigments through mediation of MYB4 nuclear transport. Involved in trichome initiation by controlling GL1, GL2, GL3 and TTG1 transcription and may affect an upstream regulator of GL3 and disrupt complex function. Acts as negative regulator miRNA activity by regulating miRNA loading into AGO1 complexes.
|
F4IS56
|
ILK1_ARATH
|
Integrin-linked protein kinase 1 (EC 2.7.11.1) (Ankyrin protein kinase 1)
|
MENITAQLKRGISRQFSTGSIRRTLSRQFTRQSSLDPRRTNMRFSFGRQSSLDPIRRSPDSSKSDDEPHMSVPENLDSTMQLLFMASKGDVRGIEELLDEGIDVNSIDLDGRTALHIAACEGHLGVVKALLSRRANIDARDRWGSTAAADAKYYGNLDVYNLLKARGAKVPKTRKTPMTVSNPREVPEYELNPLEVQVRKSDGISKGAYQVAKWNGTRVSVKILDKDSYSDPERINAFRHELTLLEKVRHPNVIQFVGAVTQNIPMMIVVEYNPKGDLSVYLQKKGRLSPSKALRFALDIARGMNYLHECKPDPIIHCDLKPKNILLDRGGQLKISGFGMIRLSKISQDKAKVANHKAHIDLSNYYIAPEVYKDEIFDLRVDAHSFGVILYEITEGVPVFHPRPPEEVARMMCLEGKRPVFKTKSRSYPPDIKELIEKCWHPEAGIRPTFSEIIIRLDKIVANCSKQGWWKDTFKFPWK
|
Functions as a link between plant defense pathways, stress responses and potassium homeostasis. Promotes osmotic stress sensitivity, responses to the bacterial-derived pathogen-associated molecular pattern (PAMP) flg22, and resistance to bacterial pathogens. Promotes the accumulation of POT5/HAK5, a potassium transporter that mediates high-affinity uptake during potassium deficiency.
|
F4IS91
|
RSA1_ARATH
|
Protein SHORT ROOT IN SALT MEDIUM 1 (AtRSA1) (Protein EMBRYO DEFECTIVE 1579)
|
MHRDMYSSRGTGYGQQQYGSQSGYSQNLGSGYPGSSVSGGAEGGSQISLSSRHPSITGAPQETDIGGGYRSHLSTAASHYGTQYGSVYGSTSLSSSQPLSTNGLGSSVLDNRSGYVPTLPDSPKFASGSYLSPSSHGYGQKTDDLYSDKLSGYIPVDRRQYGEQSSSYLGRELQNEPTRRYADPSNFARQTDLYDRIDQASLLRGEQLLKMQSLHTSSVDAGVNRQTDYLTERSSTVRHSDQEAMHYGGRLESDPHGLSVRNTSSYASQHTPSLLGAVPRRNLDDYIYPESSSNPGYGVSLPPGRDYGTGKGIHSAASLDLDYPGGMLARGTGAAPRVDDLRKGDRASYLREFDLREEERRREDQRARDKEREREREREHDRERERQRERERQRARDRERERILERREKERQGERERERKRALEIKRDRTPTARATSKDTKERTPVPKSISRDARSSSLRRDAHHREASIRRSSPIKPIRRDYVCKVLSSRLVDMERDYVTLDKRYPRLFVPSEFSKVVVNWPKQKLTLSMHTAVSFEHDYIEDGGADVKSTSTKPLALKTGGKSVWNAKMVLMSGLSRTALEDLASDKFFEDRIPHICNILKFAVLKKDHSFMAIGGSWDPTDGMDPSVDQSSLIQTMLRHSKDKLHLDLSNCRHWNPFLEIHYDRVGTDGVFSYKEITVLFVPDLSECLPSFDVWRTQWLAHRKALTERDRLLSQEVKKDTVEVTKDAEKKSPGDTSGTPTTGTKKTVKKIIKRVVKRPVNDGKATGMKGEKSDVPEHVAIPETTVPKEESTGTSSNKKIVKKVAETGDTSDPSAKANEQTPAKTIVKKKIIKRVAKRKVAEIDNKMDGDSKKDGDSDEKKVMEVGKKSSDSGSVEMKPTAESLEDVKDENASKTVDVKQETGSPDTKKKEGASSSSKKDTKTGEDKKAEKKNNSETMSEGKKIDRNNTDEKEVKEKVTEKEIKERGGKDESRIQVKDRKKCEEPPRAGFILQTKRNKDSKLRSLSASLDSLLDYTDKDLDESSFEISLFAESLYEMLQYQMGSRIFEFLKKLRVKIVRQRNQRKRHQEELSVKQNEAKSQDKRQKTAEHEDKEASVISESAPGKDDKETSGKETVDGSREIADKEAVAKTKETLGSKEVTVGEAVNMEVENQDEEDDDGDDDPEEDPEEDPEEDPEEDPEEDPEECEEMDVANTEQEEPAEEPQKKEENLEKTSGTVADPITEAETDNRKEERGPNDSKTEIKPKSETEKHGKQDGGTSDAAKREETVDKELLQAFRFFDRNQAGYVRVEDMRVTIHSLGKFLSHREVKELVQSALLESNTGRDDRILYNKLVRLSL
|
Required for salt tolerance and sodium (Na) homeostasis after salt stress. Together with BHLH148/RITF1, regulates the transcription of several genes involved in the detoxification of reactive oxygen species (ROS) generated by salt (NaCl) stress. Binds calcium.
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F4ISL7
|
TI236_ARATH
|
Protein TIC236, chloroplastic (236 kDa translocon at the inner-envelope-membrane of chloroplasts) (Protein EMBRYO DEFECTIVE 2410)
|
MSLRLQNPFLSTPLLHGSFNRREKRINVARRAFRSKRIYSEKKQNDWLAKVAKFSQFCGKNVQLLRKSLDSRSRMEVKCLKEPFVRSKDLVRSLAPVWEEGLFFLRCSVFFAVISGVCLLVWYGQNKARVFVETKLLPSVCSVLSETIQREVDFGKVRRVSPLCITLEASSIGPHGEEFSCGEVPTMKVCVRPFASLRRGKIVVDAILSNPTVLVAQKKDFTWLGIPLSDTTLPSHLSSEEGIDFRTKTRRVSREEAGIRWDEERDNDARKAAEIGYIVPCKNYSQAKDNAVKHDRRFTEIANPNSFICMDEKMHSAEQHCMDPGVEYDVKHAELEKSFGIKIPGSGLKFLSKMLKVPRKYKFKWNSKSHKNSMSNISAKKRILERSASAALSYFHSLSQQKLDEPSVLSTNYDGLSLDMLLVKGDREISNQYDRHVPYGEQSLANDLDGKGYRVRGKRLLGVKKASTLDKFTVSCDPFLMTVDRLCALLQTKRSPSVEDIVNSSESETLSSQRGDISMNVVNQNTDDVPHGNRSGNQPRDFTFKKHEHQPVANHWRPSWPRNKKLKEAVFNILTGSSKKLTGRADPNAPHLSDELEKLPAVYVEKTLPVMLDSVQFKGGTLLLLAYGDTEPREMRNVHGHVKFQNHYGRVYVQLGGNCNMWRSDVTSEDGGLLSVDVFVDTVEQNWHANLNVANFFVPIFERILEIPIEWSKGRATGEVHLCMSRGESFPNLHGQLDVTGLGFHINDAPSSFSDVSASLSFRGQRIFLHNANGWFGKVPLEASGDFGIHPDEGEFHLMCQVPYVEINALMKTFKMKPLFFPLAGSVTAVFNCQGPLDAPVFVGSCMVSRKIAYLSPDLPTSLAYEAMLKNKEAGAVAAFDRVPFSYLSANFTFNTDNCVADLYGIRATLVDGGEIRGAGNAWICPEGEVDDTALDVNFSGNISFDKVLHRYMPEYFNIGMLKLGDLTGETKLSGALLKPRFDIKWAAPKADGSLTDARGDIVISHDNIIVNSSSVAFDLFTKLDTSYHDPCLSHQDFTQGEAMPFVVEGLDLDLRMRGFEFFSLVSSYPFDSPRPTHLKATGRIKFLGKIKRHSTTKDGDVGSDKCEDAAAISSLDGDISISSLKLNQLILAPQLSGRLSVSRDHVKLDAAGRPDESLTLDFIGPLQPNSDENVQSGKLLSFSLQKGQLRANACFQPQQSATLEIRNFPLDELELASLRGLIQKAEIQLNLQKRRGHGLLSVIRPKFSGVLGEALDVAVRWSGDVCFMLSGRLEVMITVEKTILEQSNSRYELQGEYVLPGSRDRDLGQKEAGSFLMRAMTGHLGSVISSMGRWRMRLEVPKAEVAEMLPLARLLSRSTDPAVHSRSKDLFIQSVQNLCLQAENLRDLLEEIRGYYTPPSEVVLEDLSLPGLAELKGHWHGSLDASGGGNGDTLAEFDFHGDDWEWGTYKTQRVLATGSYNNDDGLRLKEMLIQKGNATLHADGTLLGPKTNLHFAVLNFPVSLIPTLVEVVESSATDIVHSLRKLLSPIKGILHMEGDLRGSLEKPECDVQVRLLDGAVGGIDLGRAEVFASLTSNSRFLFNSNFEPFVQNGHVHIQGSVPVSFSQKNMSEGEVSETDRGGAVKIPSWAKEKEDDEKRTSRDRSEERWDSQLAESLKGLYWNILDAGEVRLEADIKDGGMTLLTAISPYANWLQGNADIRLQVGGTVDHPVLDGSASFHRASISSPVLRKPLTNFGGTLHVKSNRLCITSLESRVSRKGKLVVKGNLPLRSNEASAGDGIELKCEVLEVRAKNFLSCQVDTQLQITGSMLQPTISGNIKLSQGEAYLPHDKGGGAAPLNRLAANQYSIPGAAINQAVSSRYFARFFGTERASSGMKFSQSTGKSNSVEKEIEEVKMKPNMDIRLSDMKLVLGPELRIMYPLILNFAVSGELELDGMAHPKFIKPKGVLTFENGDVNLVATQVRLKREHLNVAKFEPEHGLDPLLDLALVGSEWQFRVQSRASNWQDKLVVTSTRSVEQDALSPSEAAKVFESQLAESILEGDGQLAFKKLATATLGTIMPRIEGKGEFGQARWRLVYAPQIPSLLSVDPTVDPLKSLASNISFGTEVEVQLGKRLQASVVRQMKDSEMAMQWTLIYQLTSRLRVLLQSAPSKRLLFEYSATSQD
|
Part of the inner chloroplast membrane translocon complex (TIC) which associates with the outer chloroplast membrane translocon complex (TOC) and forms a supercomplex involved in protein precursor import into the chloroplast stroma. Required for the import of HSP93, TIC40 and RBCS protein precursors in the chloroplast stroma. Links the outer and inner membrane translocons of the chloroplast envelope.
|
F4ISV9
|
APD4_ARATH
|
E3 ubiquitin-protein ligase APD4 (EC 2.3.2.27) (Protein ABERRANT POLLEN DEVELOPMENT 4)
|
MGSIRGDLQPLFVMPPPPLDEDCDDIFNSDESSWGLLSLSCFGIIMGLWFFASVCLIFGVYGSETVWLGPNSSILVKPSSIFVKSINAKELDFSKPGLQLYGFNGQSTPSGYFVNWTESRVLSVSQNSYKGWPYYLNRGTHMNISYNILPKGSAVRLVITEGMPFFYRSSLKDIAFRDTAWSWNLIQGSGMIQLDISKSKGYYLTVANLKRKDVEVELDIDVKVVLYDTKQSSYNCSFSNGECSFKMNERSPVENYAVVTSPALGQGVSIDDEWYIELSYQPRLIAYGSFTGVLLSFMLVAIHFCNKLKCCGGEGFLSEDDSVRTCLLADKGDNDCCNDVEASNKSLCAICFDAPRDCCFLPCGHCVSCYQCGTKIKRTKGRCPICRKKIMHVKRIYTA
|
Involved in pollen mitosis II (PMII) regulation during male gametogenesis.
|
F4ITL6
|
RTE1_ARATH
|
Protein REVERSION-TO-ETHYLENE SENSITIVITY1
|
MSRGRGVPMMDLKRSYDVEDRVVSVSIPSIIEADEADLWPLPEIDTKKSKFPCCIVWTPLPVVSWLAPFIGHIGLCREDGVILDFAGSNFINVDDFAFGPPARYLQLDRTKCCLPPNMGGHTCKYGFKHTDFGTARTWDNALSSSTRSFEHKTYNIFTCNCHSFVANCLNRLCYGGSMEWNMVNVAILLMIKGKWINGSSVVRSFLPCAVVTSLGVVLVGWPFLIGLSSFSLLLFAWFIIATYCFKNIIT
|
Acts at an early step in the ethylene signaling pathway. Positively regulates ETR1, leading to the negative regulation of ethylene responses.
|
F4ITM1
|
RGSL1_ARATH
|
E3 ubiquitin-protein ligase RSL1 (EC 2.3.2.31) (Protein RING FINGER OF SEED LONGEVITY 1) (RING-type E3 ubiquitin transferase RSL1)
|
MEEDDLNPAGKPLYRLYFKGLVTEEKEMLLAGFGVAICGDKDDLLFDLKVSIHDPTITLLEVELIALKSGLNQAVSLGINHISICCDHEYIFELVMGISTPKQESIALLLRDVQGIRKYLTSSIPVMLTQNQSNLAYDFAIEAISSEIIIDIPAQKETCNICLNDDINADQMFSVDKSGHMCCSECVKRHIEVRLLEGSLITCPHYRCNSLLTSVRCGNLLTPKLNKMWEQKTKDELIPVMDRVYCPNPRCSTLMSETELSGLNIGVRRCCVKCGEPFCVKCKVSWHNNLSCDEYKTLHPNPTENDGRLRDLANEKSWRQCSKCKHMIELSSGCISVVCRCGHTFCYQCGADAGDCFHGLGRDDLDLTQCCGSCCCFVFFLVIIAIVVTIILLVRRFS
|
Acts as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. Negative regulator of the abscisic acid (ABA) signaling pathway which targets PYL4 and PYR1 ABA receptors in plasma membrane to promote their FREE1/FYVE1-dependent trafficking and degradation upon ubiquitynation this process involves clathrin-mediated endocytosis and trafficking through the ESCRT pathway. Involved in the maintenance of seed longevity. May enhance gibberellins responses.
|
F4IUX6
|
RENT2_ARATH
|
Regulator of nonsense transcripts UPF2 (Nonsense mRNA reducing factor UPF2) (Up-frameshift suppressor 2 homolog) (AtUpf2)
|
MDHPEDESHSEKQDDEEALARLEEIKKSIEAKLTLRQNNLNPERPDSAYLRTLDSSIKRNTAVIKKLKQINEEQREGLMDDLRGVNLSKFVSEAVTAICEAKLKSSDIQAAVQICSLLHQRYKEFSASLTQGLLKVFFPGKSAEDLEADKNSKAMKKRSTLKLLLELYYVGVIEDSNIFINIIKDLTSVEQLKDRDTTQTNLTLLTSFARQGRIFLGLPISGQDEDFFKGLDVTADQKKSFKKAFNTYYDALADLLQSEHKLLLQMEKENAKLVNAKGELSEDSASSYEKLRKSYDHLYRNISSLAEALDMQPPVMPEDGTTRLTAGDEASPSGTVKDTSVPEPIWDDEDTKTFYECLPDLRAFVPAVLLGEAEPKSNEQSAKAKEKLSESSSEVVENQQTTEDTTEVSADSASMDDRSNAEQPKEKEEVEKEKAKDTKKEKGKEKDSEKKMEHEKEKGKSLDVANFERLLQRLPGCVSRDLIDQLTVEYCYLNSKTNRKKLVKALFNVPRTSLELLAYYSRMVATLASCMKDIPSMLVQMLEDEFNSLVHKKDQMNIETKIRNIRFIGELCKFKIVPAGLVFSCLKACLDEFTHHNIDVACNLLETCGRFLYRSPETTLRMTNMLDILMRLKNVKNLDPRQSTLVENAYYLCKPPERSARISKVRPPLHQYVRKLLFSDLDKDSIANVLKQLRKLPWSECEQYILKCFMKVHKGKYGQIHLIASLTSGLSRHHDEFVVAVVDEVLEEIRVGLELNEYGAQQKRLAHMRFLGELYNYEHVDSSVIFETLYLTLLYGHDTSEQEVLDPPEDFFRVRMVIILLETCGHYFDRGSSKKRLDQFLIHFQRYILSKGHLPLDIEFDLQDLFANLRPNMTRYSTIDEVNAAILQLEEREHASSGDKVSIERHSDTKPSNKSSSDVISSNGKSTAKDIRENGEAHGEESDSDSGSGSVVRDGQNEELDDGNHERGSESGDGDDYDDGDGPGSDDDKFRVRQKVVTVDLEEQADFDQELKALLQESMEQRKLELRGRPALNMTIPMSVFEGSGKDHHHFGRVVGENGEEVLDEENGEQREVQVKVLVKRGNKQQTRQMLIPSDCALVQSTKQKEAAELEEKQDIKRLVLEYNERDEEEANGLGTQILNWTSGGSRGSTRTGEGSGKSGGSRHRFYYHQGGGGSYHARRK
|
Recruited by UPF3 associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3 stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA (By similarity). Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Required for plant development and adaptation to environmental stresses, including plant defense and response to wounding. {ECO:0000250, ECO:0000269|PubMed:22353561}.
|
F4IV16
|
TPK2_ARATH
|
Thiamine pyrophosphokinase 2 (AtTPK2) (EC 2.7.6.2) (Thiamine kinase 2)
|
MLSAMDVMIHSSSFLLPCDETCGTRYALVVLNQNLPRFTPLLWEHAKLRLCADGGANRIYDELPLFFPHEDPFVIRNRYKPDVIKGDMDSIRRDVLDFYVYWGTKVIDESHDQDTTDLDKCISYIRHSTLNQESSRLQILATGALGGRFDHEAGNLNVLYRYPDTRIVLLSDDCLIQLLPKTHRHEIHIHSSLQGPHCGLIPIGTPSANTTTSGLKWDLSNTEMRFGGLISTSNLVKEEIITVESDSDLLWTISIKKTGLPVQDHKP
|
Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate (TPP). TPP is an active cofactor for enzymes involved in glycolysis and energy production. Plant leaves require high levels of TPP for photosynthesis and carbohydrate metabolism.
|
F4IV66
|
RNE_ARATH
|
Ribonuclease E/G-like protein, chloroplastic (RNase E/G-like protein) (EC 3.1.26.-) (RNase E)
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MDVTEVPWRRLPQFSVSSRASWLVSSGFPLSSYMFSHVERGKTFRLTLCFGVSRLRPRSAIPLRFLLSVFSEQPPSRLKGLCEVVWIVEADLAANEHLYVTGDPSTLGSWEPDCAISMYPTENDNEWEAKVKIASGVNFRYNYLLKAGYGSSSDVIWRPGPQFSLSVPSSVNQDRKIIIRDSWMSMSISSKSQESYGWGSWIDDAYLFPNCVTPAQSEDECTSADSAIEVPRTHLNDKQVGAESFLCDELAAFSSENSNLSALFSDNYQPIEEPWLIQESITLQHERNMQTDSEQDVESCDDNENNLNTDEQNHQLTETLLPDGGFFQSESIATTILINSSICTVQRIAVLEGGKLVELLLEPVKTNVQCDSVYLGVITKFVPHMGGAFVNIGSARHSFMDIKSNREPFIFPPFCDGSKKQAADGSPILSMNDIPAPHEIEHASYDFEASSLLDIDSNDPGESFHDDDDEHENDEYHVSDHLAGLVNGTVVNHGAVEVGSENGHIPMERGHSADSLDSNASVAKASKVMSSKDNKWIQVRKGTKIIVQVVKEGLGTKGPTLTAYPKLRSRFWVLLTRCKRIGVSKKISGVERTRLKVIAKTLQPQGFGLTVRTVAAGHSLEELQKDLDGLLLTWKNITDEAKSAALAADEGVEGAIPALLHRAMGQTLSVVQDYFNDKVEKMVVDSPRTYHEVTHYLQDMAPDLCNRVELHDKGIPLFDLYEIEEEIEGILSKRVPLSNGGSLVIEQTEALVSIDVNGGHGMFGQGNSQEKAILEVNLAAARQIAREIRLRDIGGIIVVDFIDMADESNKRLVYEEVKKAVERDRSLVKVSELSRHGLMEITRKRVRPSVTFMISEPCSCCHATGRVEALETTFSKIEQEICRQLAKMEKRGDLENPKSWPRFILRVDSHMSSFLTTGKRTRLAILSSSLKVWILLKVARHFTRGTFEVKPFMDEKTVNERQHQVAISLLKKADAIADSSGKKKLTLIPIKKEKTSGKQRR
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Involved in intercistronic processing of primary transcripts from chloroplast operons. The endonucleolytic activity of the enzyme depends on the number of phosphates at the 5' end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences.
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F4IVI0
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BUB1_ARATH
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Mitotic checkpoint serine/threonine-protein kinase BUB1 (AtBUB1) (EC 2.7.11.1) (Protein BUDDING UNINHIBITED BY BENZYMIDAZOL 1)
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MTIGYRDAAGDPLFPWLMEIKNSMEDLYAGKNSGYDLDKLLFDCISTYKKDSRYRNDLRFLKIWFLYLEGREDFERVYREIEETEICKGHSLLYEWYAIFLEVKGLWRRANSVYQTGLSRKAEPFDRLKEAHSLFLQRISKRTKASSLEKVGDDAQATDLETGFVNPWETSTVNGLIHKIKPQLVKYDGYHVSNKVFPGKANLSSLQNYSRNKIIEIGGRKYQMKGCAGQGGFAQVFKAFIDSNPDEVVALKVQKPPFPWEFHMYRQLDCRIPDSQRSSFGLAQRVHVYSDYSILVCDYLSHGTLQDVINSYVVVGKSMEEVLCMYYTIEMLNMLETLHSVGIIHGDFKPDNLLIRYPPENLTETGFHEKTGSWSKKGLCLVDWGRGIDLSLFPRTTEFTGDCRTSGFRCVEMKEDKPWKFQVDTYGLCVIVHMMLHNVYMEIEKKQSLDGGYINMPRTSFKRYWKVDLWKELFTKLLNRETCEDDTETLRNLRKSMEEYICSDPKLMKKLNELLAKQRISLCSS
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Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore. Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C). Necessary for ensuring proper chromosome segregation. Can regulate chromosome segregation in a kinetochore-independent manner. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity (By similarity).
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F4IVL6
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GRV2_ARATH
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DnaJ homolog subfamily C GRV2 (Protein GRAVITROPISM DEFECTIVE 2) (Protein GREEN FLUORESCENT SEED 2) (Protein KATAMARI2)
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MDSVSRGAVASTTGGAVEEPEYLARYLVVKHSWRGRYKRILCISSGGIVTLDPNTLAVTNSYDTGSNFDGASPLVGRDENTESVGGEFTVNVRTDGKGKFKAMKFSSRCRASILTELYRLRWNQIRPVAEFQVLHLRRRNAEWVPYKLKITFVGLELVDSKSGNSRWILDFRDMGSPAIILLSDAYRTKSADSAGFVLCPMYGRKSKAFRAAPGTTNSSIVASLAKTAKSMVGVFLSVDDSQLLTVSEYMTRRAKEAVGAEETPNGWWSVTRLRSAAHGTLNMPGLSLAIGPKGGLGEHGDAVALQLILTKASLVERRIDNYEVVIVRPLSSVSSLVRFAEEPQMFAIEFSDGCPVLVYASISRDNLLAAILDTLQTEGHCPIPVLPRLTMPGHRIDPPCGRVSLISGPQHLVADLETCSLHLKHLAAAAKDAVAEGGSVPGCRARLWRRIREFNACIPYTGVPANSEVPEVTLMALITMLPSTPNLPVDAPPLPPPSPKAAATVIGFVTCLRRLLSSRSAASHIMSFPAAVNRIMGLLRNGSEGVAAEAAGLIASLIGGWSADLSTAPDSRGEKHATIMHTKSVLFAQQGYVTILVNRLKPMSVSPLFSMAIVEVFEAMVCDPHGETTQYTVFVELLRQIAALRRRLFALFAHPAESVRETIAVIMRTIAEEDAIAAESMRDAALRDGALLRHLLNAFSLPASERREVSRQLVALWADSYQPALDLLSRVLPPGLVAYLHTRPDDVVDDTDQEGSSTNRRQKRLLQQRRGRIAKGMGAQDIPLPPGNNVEAGDAAKHMSANASVPDNFQRRAADSSSEASNPQASAFPGVDSTIAGVSQNGYPAFASVTTNANGHEQPETNASDVVGSDPNLYGIQNSVLPAPAQVIVESTAVGSGKLLLNWREFWRAFGLDHNRADLIWNERTRQELIEALKAEVHNLDVEKERTEDISPGDVEATTGQEIIPRISWNYSEFSVSYRSLSKEVCVGQYYLRLLLESGNAGKAQDFPLRDPVAFFRALYHRFQCDADMGLTIDGAVPDELGSSGDWCDMSRLDGFGGGGGASVRELCARAMAIVYEQHYNTIGPFEGTAHITALIDRTNDRALRHRLLLLLKALVKVLLNVEGCVVVGGCVLAVDLLTVVHENSERTPIPLQSNLIAATAFMEPPKEWMYIDKGGAEVGPVEKDVIRSLWSKKDIDWTTKCRALGMSDWKKLRDIRELRWAVAVRVPVLTPSQVGDAALSILHSMVSAHSDLDDAGEIVTPTPRVKRILSSTRCLPHIAQALLSGEPVIVEAGAALLKDVVTRNSKAMIRLYSTGAFYFALAYPGSNLYSIAQLFSVTHVHQAFHGGEEATVSSSLPLAKRSVLGGLLPESLLYVLERSGPAAFAAGMVSDSDTPEIIWTHKMRAENLICQVLQHLGDYPQKLSQHCHSLYDYAPMPPVTYPELRDEMWCHRYYLRNLCDEIQFPNWPIVEHVEFLQSLLVMWREELTRKPMDLSEGEACKILEISLNNVSSDDLNRTASVELNEEISNISKQIQNLDEEKLKRQYRKLAMRYHPDKNPEGREKFLAVQKAYECLQATMQGLQGPQPWRLLLLLKAQCILYRRYGHVLRPFKYAGYPMLLDAVTVDKDDNNFLSNDRSPLLVAASELVSLTCAASSLNGEELVRDGGVQLLSTLLSRCMCVVQPTTSQHEPAAIIVTNVMRTLSVISQFESARAGFLELPSLIEDIVHCTELERVPAAVDAALQSIAKVSVFPELQHGLLKAGALWYILPLLLQYDSTAEESNSVESHGVGVSIQIAKNEHALQASQALSRLTGLCADESLTPYNATAADVLKALLTPKLASLLKDEVAKDLLSKLNTNLETPEIIWNSATRSELLNFVDEQRACQCPDGSYDLKNAQSFSYDALSKEVFVGNVYLKVYNDQPDSEISEPESFCNALIDFISSLVHTELPSVSEDQNLIEDRNSSNDTPELQSSVAEPSLIEEHSDHQPSSEGMKNEECFLIDHLQLGLTALQNLLTKYPDLASVFSSKERLLPLFECFSVAIASKTDIPKLCLNVLSRLTAYAPCLETMVSDGSSLLLLLQMLHSAPSFREGALHVLYALASTPELAWAAAKHGGVVYILELLLPLQKEIPLQQRAAAASLLGKLVAQPMHGPRVAITLVRFLPDGLVSIIRDGPGEAVVHALERTTETPELVWTPAMAASLSAQIATMASDIYREQQKGSVIEWDVPEQSAGQQEMRDEPQVGGIYVRRFLKDPKFPLRNPKRFLEGLLDQYLSAMAATHYEQHPVDPELPLLLSAALVSLLRVHPALADHIGHLGYVPKLVAAVAYEGRRETMSSGEVKAEEIGSDGVNESTDPSSLPGQTPQERVRLSCLRVLHQLAASTTCAEAMAATSAGNAQVVPLLMKAIGWLGGSILALETLKRVVVAGNRARDALVAQGLKVGLIEVLLGLLDWRTGGRYGLSSHMKWNESEASIGRVLAVEVLHGFATEGAHCSKVREILDASEVWSAYKDQKHDLFLPSNTQSAAGVAGFIENSSNSLTYALTAPPPPSHP
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Required for endosome formation, vacuolar protein sorting and determination of the embryo growth axis. Necessary for the transport of proteins into protein storage vacuoles (PSVs). Participates in vesicle trafficking from the endosome to the central vacuole. Involved in the regulation of shoot phototropism and gravitropism, probably through the positioning of specialized amyloplasts (statoliths) in endodermal cells.
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F4IVV0
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RIC1_ARATH
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CRIB domain-containing protein RIC1 (ROP-interactive CRIB motif-containing protein 1) (Target of ROP protein RIC1)
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MATTMKGLLKGLRYITQIFDEEKEQEMQIGFPTDVKHVAHIGSDGPTNTTPSWMNDFKTQEHEKGQVVSRGNSNKYNPQGTNQRGAGLKELLPSNTNEKPKQKTRRKPGGAASPNHNGSPPRKSSGNAASSDEPSKHSRHNRSAHGSTDSSNDQEPSVRRRRGGIPAPDTEVPNQIPDGSAPPRKATSRPRKLKGSSAGGEGSIKKSSKGKPENSVDTTCNDII
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Functions as downstream effector of Rho-related GTP binding proteins of the 'Rho of Plants' (ROPs) family. Participates in the propagation of ROP GTPase signals in specific cellular responses. Required for cortical microtubule organization. Promotes microtubule bundling and formation of well-ordered microtubule arrays in the neck region of pavement cells. This restricts cell lateral expansion to generate the narrow neck morphology of pavement cells. Its function is inhibited when it interacts with activated ARAC4/ROP2. Represses ARAC4/ROP2 activation and antagonizes the RIC4-actin pathway that promotes the assembly of cortical actin microfilaments. Acts as downstream effector of ARAC3/ROP6 which functions in a signaling pathway that negatively regulates clathrin-mediated endocytosis and internalization of PIN1 and PIN2. Required for the asymmetric auxin distribution during root gravitropism and vascular patterning. Positively regulates auxin responses, but negatively regulates ABA responses during lateral root development and primary root elongation.
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F4IW47
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TKTC2_ARATH
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Transketolase-2, chloroplastic (TK) (EC 2.2.1.1)
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MASTSSLALSQALLTRAISHNGSENCVSIPAFSALKSTSPRTSGTISSRRRNASTISHSLRPLVRAAAVEAIVTSSDSSLVDKSVNTIRFLAIDAVEKAKSGHPGLPMGCAPMSHILYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDSVREEDLKSFRQWGSKTPGHPENFETPGVEATTGPLGQGIANAVGLALAEKHLAARFNKPDNEIVDHYTYSILGDGCQMEGISNEVCSLAGHWGLGKLIAFYDDNHISIDGDTDIAFTESVDKRFEALGWHVIWVKNGNNGYDEIRAAIREAKAVTDKPTLIKVTTTIGYGSPNKANSYSVHGAALGEKEVEATRNNLGWPYEPFHVPEDVKSHWSRHTPEGAALEADWNAKFAAYEKKYPEEAAELKSIISGELPVGWEKALPTYTPDSPGDATRNLSQQCLNALAKAVPGFLGGSADLASSNMTMLKAFGNFQKATPEERNLRFGVREHGMGAICNGIALHSPGFIPYCATFFVFTDYMRAAMRISALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLSSFRAMPNIMMFRPADGNETAGAYKIAVTKRKTPSVLALSRQKLPQLPGTSIESVEKGGYTISDNSTGNKPDVILIGTGSELEIAAQAAEKLREQGKSVRVVSFVCWELFDEQSDAYKESVLPSDVSARVSIEAGSTFGWGKIVGGKGKSIGIDTFGASAPAGKLYKEFGITIEAMVEAAKSLI
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Catalyzes the reversible transfer of a two-carbon ketol group from fructose-6-phosphate or sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-4-phosphate or ribose-5-phosphate, respectively (By similarity). Could act as a stress sensor involved in adaptation process. {ECO:0000250, ECO:0000269|PubMed:22214485}.
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F4IXE7
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IDM1_ARATH
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Increased DNA methylation 1 (Histone H3 acetyltransferase IDM1) (EC 2.3.1.-) (Protein ROS4) (Repressor of silencing 4)
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MLPGAEIEMLGGDCFEGSYEDHQIFREVFFGSDPGNTTKRCLVTGAINFECDSSKNVNSSLSSNSVVTSGYACPQGFEASASRDGSDFNTKAKRVKLSGNKHLDARDEKGSALHGFPTSDIARETIPLHLVESSNKGVSTSSYLLKHSIVKGREVYLGGIVSGKCKSLNLDKCDGKEFKAIASPVSQESFATRMISVGASTPHSEKACFPLQLNNGSKVSPNELIMSKTCLKIDPKEDPRPLLYKYVCKVLTAARWKIEKRERSAGRKHVDTFYISPEGRKFREFGSAWKALGGILLADRKLMDTGTKKWTGINDFWSDLSLTLLDIEENMKNLNLANTRALWWSALEPFVVVVFISKQVGSLRKGNKVEVARNSNPDKLKKEDTICLNLISGCPESVLTVSEGSHLVHDVDANQEIHSDLEVQTKISSQKVSSRLERQSIIGKEISGTHEQEASKGIVASKLIAEDMHESVMRKNLHRRSKKISDIKPASLDQHDSLDSNSLNSFEFQDKEMGNIHLVSKGSRDERLRNEKMNNSCCNSKKGRKKARKHYTQDDDLMGSTITRNKGKFSRSSQKKKTQKPKARTKKRNNRGGCRLLPRSSSNVENHFFQGNWSILGPRTVLSWLIATKVISRDEVIQLRDPDDDTVVKTGLVTKDGVVCTCCNKTVSLSEFKNHAGFNQNCPCLNLFMGSGKPFASCQLEAWSAEYKARRNGWRLEKASDDDPNDDSCGVCGDGGELICCDNCPSTFHQACLSMQVLPEGSWYCSSCTCWICSELVSDNAERSQDFKCSQCAHKYHGTCLQGISKRRKLFPETYFCGKNCEKVYNGLSSRVGIINPNADGLSWSILKCFQEDGMVHSARRLALKAECNSKLAVALSIMEESFLSMVDPRTGIDMIPHVLYNWGSTFARLDFDGFYTVVVEKDDVMISVASIRVHGVTIAEMPLVATCSKYRRQGMCRILVAAIEEMLMSLKVEKLVVAALPSLVETWTEGFGFKPMDDEERDALKRINLMVFPGTTLLKKTLYESTKPSTMKGVCLSKERNNPSNKEADLEPGLDKAGSPMSTQVESCDQMVPAGSDDEPSPGFPVPLGADQTEPTSETENPSRDSNANDRPNKTTVVSIGEEEEEECLQKDVSKLSEEGKETTRASSSSAALEEVSGLGLGVVNNVSDEMLLCVDEQLDSDSSQDSE
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Histone H3 acetyltransferase that binds methylated DNA at chromatin sites lacking histone H3K4 di- or trimethylation and catalyzes H3K18 and H3K23 acetylation. Prevents the transcriptional silencing of transgenes and of some endogenous genes. Requires the presence of IDM2 for efficient H3K18 acetylation, but not for H3K23 acetylation.
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F4IXW2
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BIG5_ARATH
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Brefeldin A-inhibited guanine nucleotide-exchange protein 5 (BIG5) (ARF guanine-nucleotide exchange factor BIG5) (Protein BFA-VISUALIZED ENDOCYTIC TRAFFICKING DEFECTIVE 1) (Protein BEN1) (Protein HOPM INTERACTOR 7) (AtMIN7)
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MAAGGFLTRAFDTMLKESGGKKFPDLQKAIQAYQDGSKVVTQAAPSSIVESSQAEGGGEKTGVEADEPQKVTSAEVAQQASQSKSETINVSLANAGHTLGGAEVELVLKPLRLAFETKNLKIFDAALDCLHKLIAYDHLEGDPGLDGGKNSAPFTDILNMVCSCVDNSSPDSTVLQVLKVLLTAVASGKFKVHGEPLLGVIRVCYNIALNSKSPINQATSKAMLTQMISIVFRRMETDIVSASSTVSQEEHVSGDTSSPKNEEITAADENEKEMTLGDALTQAKDTTLASVEELHTLVGGADIKGLEAALDKAVHLEDGKKIKRGIELESMSIGQRDALLVFRTLCKMGMKEDSDEVTTKTRILSLELLQGMLEGVSHSFTKNFHFIDSVKAYLSYALLRASVSQSSVIFQYASGIFSVLLLRFRDSLKGEIGIFFPIIVLRSLDNSECPNDQKMGVLRMLEKVCKDPQMLVDVYVNYDCDLEAPNLFERMVTTLSKIAQGSQSADPNPAMASQTASVKGSSLQCLVNVLKSLVDWEKIRREAENSTRNANEDSASTGEPIETKSREDVPSNFEKAKAHKSTMEAAISEFNRNSVKGVEYLIANKLVERNPASVAQFLRSTSSLSKVMIGDYLGQHEEFPLAVMHAYVDSMKFSEMKFHSAIREFLKGFRLPGEAQKIDRIMEKFAERYCADNPGLFKNADTAYVLAYAVIMLNTDAHNPMVWPKMSKSDFTRMNATNDPEDCAPTELLEEIYDSIVQEEIKLKDDDTMKKLSSQRPGGEERGGLVSILNLGLPKRISAADAKSETEDIVRKTQEIFRKHGVKRGVFHTVEQVDIIRPMVEAVGWPLLAAFSVTMEVGDNKPRILLCMEGFKAGIHIAYVLGMDTMRYAFLTSLVRFTFLHAPKEMRSKNVEALRILLGLCDSEPDTLQDTWNAVLECVSRLEFIISTPGIAATVMHGSNQISRDGVVQSLKELAGRPAEQVFVNSVKLPSESVVEFFTALCGVSAEELKQSPARVFSLQKLVEISYYNIARIRMVWARIWSVLAEHFVSAGSHHDEKIAMYAIDSLRQLGMKYLERAELTNFTFQNDILKPFVIIMRNTQSQTIRSLIVDCIVQMIKSKVGSIKSGWRSVFMIFTAAADDEVESIVEKSFENVEQVILEHFDQVIGDCFMDCVNCLIRFANNKASDRISLKAIALLRICEDRLAEGLIPGGVLKPVDGNEDETFDVTEHYWFPMLAGLSDLTSDYRPEVRNCALEVLFDLLNERGNKFSTPFWESIFHRILFPIFDHVSHAGKESLISSGDVKFRETSIHSLQLLCNLFNTFYKEVCFMLPPLLSLLLDCAKKSDQTVVSISLGALVHLIEVGGHQFSEGDWDMLLKSIRDASYTTQPLELLNALSFDNPKKNLVLAGDIEADASDSPRVDRNPDDIKDNGKVSAQASPRIGTHGTSLESGIPPKADGSEGRPSSSGRAQKDVDDVNLQRSQTFGQRFMDNLFLRNLTSQPKSSVAEVTVPSSPYKHEDPTEPDSREEESPALGAIRGKCITQLLLLGAINSIQQKYWSNLKTPQKIAIMDILFSFIEFASSYNSYSNLRTRMNHIPTERPPLNLLRQELEGTTIYLDVLQKTTSGLADDASNSEDRLEGAAEEKLVSFCEQVLKETSDLQSTLGETTNMDVHRVLELRSPVIVKVLEGMCFMNNTIFRKHMREFYPLLTRLVCCEQMEIRGALANLFKAQLKPLLQQ
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Activates the ARF proteins by exchanging bound GDP for free GTP. Plays a role in vesicular protein sorting. Acts as the major regulator of early endosomal vesicle trafficking, particularly at the trans-Golgi-network/early endosome (TGN/EE), but is also involved in the endocytosis process. Together with VPS45/BEN2 required for polar PIN-FORMED (PIN) proteins localization, for their dynamic repolarization, and consequently for auxin activity gradient formation and auxin-related developmental processes (e.g. embryonic patterning, organogenesis and vasculature venation patterning). Target of hopM1, a conserved Pseudomonas syringae virulence protein that directs the protein to its own proteasome-mediated degradation. Plays a broad role in PAMP-triggered immunity (PTI), effector-triggered immunity (ETI), and salicylic acid (SA)-regulated immunity.
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F4IY62
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UGPA3_ARATH
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UTP--glucose-1-phosphate uridylyltransferase 3, chloroplastic (EC 2.7.7.9) (UDP-glucose pyrophosphorylase 3)
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MANPQASPILHHPQNHLSLFHFRTTTSPRSFSSLHFRKPLLFLSSSSSFSSKLQQSEQQCNNHQVRHVSTVPVEYSTPTPPESDDFLSEIDRLKSLLSKLDVSKDLRRKDAVIDADSRVRRFFSENRGGLSKVFGYLGLNSNEMFLVKCVIAAGQEHALCMNYEEAFGEEEEEYTVRSSVKNALYALVEMIERFDVNSSGYKGRREMGTVLDSEEIAHFRKFLTFLEEIEQFYDCIGGIIGYQVMVLELLHQSSKRRNTNRSQLVEESLGCQYLEMHTPSVLDLTQEEDYASQAALWGIEGLPDLGEIYPLGGAADRLGLIDSETGECLPAAMLAHCGRTLLEGLIRDLQAREFLYFKLYGKQCVTPVAIMTSAAKNNHEHVSSLCERLKWFGRGQSNFRLFEQPLVPAVSAEDGQWIVSKPFVPVSKPGGHGVIWKLAYDKGVFNWFYDHGRKGATVRQVSNVVAATDVTLLALAGIGLRYNKKLGFASCKRNAGATEGINVLMEKKNFDGKWEYGISCIEYTEFDKFDISNRSPSSNGLQADFPANTNILYVDLHSAELIGSSSNAKSLPNMVLNTKKRIEYLDQYGDYHSVMGGRLECTMQNIADNFFNKFPSRCHGSLEDKLDTYIVYNERRKVTSSAKKKKPHASAALHQTPDGALLDILRNGYDLLTECDIKLPMIEANDKYVDSPPPYLILLHPALGPLWEVSRQKFKGGSISSCSELQLEIAEFSWNNVQVDGSLIVTAENAMGSTTPNDNGEPILQYGLRCGKCKLHNVNVVNRGIDWNSKSNVYWRNDVNRLETCKIILHGNAEFEASNVTIEGHHVFEVPDGHKLKITSGNAGLSINLEALKEEVMETGSWYWNYQLNGSHIHLQQVEVSQS
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Involved in the biosynthesis of sulfolipids in the chloroplast. Catalyzes the first committed step in sulfolipid biosynthesis. Converts glucose 1-phosphate to UDP-glucose, the precursor of the polar head of sulfolipid. In addition to glucose 1-phosphate, can use galactose 1-phosphate, but with much lower activity. No uridyltransferase activity with other hexose monophosphates. Specific for UTP and cannot use ATP, CTP, and GTP.
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F4IYH6
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AIPP2_ARATH
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ASI1-immunoprecipitated protein 2 (PHD finger-containing protein 3)
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MADRRVGNRPMGRRGRLEIQSGTCNVCSAPCSSCMHHNAEFSGSKSDESSDENSHGVLASQCSFNGDNLLRSSGVNAPGSSHNTSSEASHLVNSNHDTSSENAESKEIIRSSDISHGPLLDRPHKDQDSMKVDSCNDHQARSTLGQGKVKEKSGAKNNEEKKNTLTGSSKHSGPRVGKSGENVLLNKADESNTSAMSDSESENDPEMLELDVKVCDTCGDAGREDLLAICSRCSDGAEHTYCMRVMLKKVPKGYWLCEECKFAEKAEKHKLETKRKRESEVNVNTQISSKRHIDKFEAVPDSKRLAVGAQIGSPKRSVLPRMSTLSRETSFKGLEKPTRKLAHYSSFNSHSSDDTESTRSTDSQLQSPKGSFLKSNSFNSLSSRSKVRPVDDDMLPRQKTGNENSSLEVKEGFSKNVGKSMSSRCIDVGSSNCNDSKVKGSKQLKDWSTEANPSASISRGNSSIPYAKSPRDLKDLQSDGKQGSLSKQARHLSRNRLEDIVASVGDSSKNEKCSSSEQISSEAKCKDELAQVDGVPRSREFREAGEKTKDAVGNHQKRNIGEDNNKGNRLRAAVDAALRKKPSFSKNRGLEQSDLPPVSNVDSGCNKALKCLSSKVPVIRDWPVGFQGLPGGHPNLRTDKQTNTVNEKQFTLAGTDATTASQSVEPEVNDPSVQSVMRDLPVAAPNVLSTTSAIPKPEYIWQGDLEVQKSRNLSAMHSGIQAYLSTLASPKVVEVVKQFPEKVTLNEVPRLSSWPAQFQDTGAKEQHVALFFFAKDIESYEKNYKPLVDNMIQKDLALKGNLEGVELLIFASNQLPQDCQRWNMLFFLWGVFRGKKESCSNPPKNTPLPASCVSPNRDTFRHENPSNKKSLTDRTLSRMQSCMKEEDAKEGKACSGTEKENAFSVSYGEGEVDVETEEGEIGVSPQLKYEKTAGPGTVKSADMNQRVNVDDLNKEGLCEGPANKKLKTVTGVETGCSIVRRDTSVHKFASRKFV
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Together with AIPP3/BDT1 and PAIPP2, cooperates to form a BAH-PHD bivalent histone reader complex able to read histone H3 lysine 27 trimethylation (H3K27me3) and low-methylated H3K4 histone marks in order to regulate transcription, especially to prevent early flowering promotes AIPP3/BDT1 binding to H3K27me3. CPL2 is subsequently recruited to form a BAH-PHD-CPL2 complex (BPC) in order to silence several H3K27me3 and low-methylated H3K4 enriched loci, including AGO5, via the phosphorylation state-dependent inhibition of Pol II release from the transcriptional start site (e.g. Ser5P-Pol II dephosphorylation). The BPC complex represses flowering by inhibiting the expression of several genes, including AGL6, FT, FUL and SOC1. Prevents the accumulation of intronic heterochromatin-containing genes (e.g. IBM1, At3g05410 and RPP7).
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