UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
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Q6CWK2 | MSEGEVQVIELINNFFLKSALLLEQSKVAHNFDTEEALRDGNHLFNIETRGDPLLEAQIQPWITFDGVKTMPPLVIETYLDLRALQPNHMVYLHDADGNPWMVCKGGKKTEIVLERWLVELDKQTIDDSIDSNDPENLHKQLVLLFRYLYTLTQLLPANDIITKPHNSQQPALINVQTRLLDGSKPILSKGRVGLSKPIIASYSNTMNETNIASHLEQRKITPIKTTFGSLRITVSYRKDVDFYVIDSDDLQKRYMTPSLSNETTTVPDRRASSNCSRSMSVSPKTNTINATLFPLEGSSARRQSISSKLQPFKVGSVGSGSFVQSGSAQSTTSLVPSLSRNVSSSSVVAALKVQRGSAGSTIVNGDVPPELSSVGSGSKYSSSFGRIRRHSSIRRSESFDRTAKPRKSTENPPEDLLEFVKLLEDKKELNMKPNTILPQQDISNSLMRFQSMKSNNDALSDNLSMSMSIDQPNVRFGSNSHSPIPSFSPNYGSIPSRLSQGSRNNSNAELITSRKSSLDRHKHNLLSRTGSNVDINRRGSVGTMETTNEDSKEDEQSHMKGMHFSNEATINKDDDEDEMLMKRSFNAGTSTTEQVMGSPRSIRSISVSSYPRNQLPLKHLNLSHPTTSATTTHAKFHKSEMSPDPLHTEGAQPHTSSQHHNSSQKNDEDDDLLFVMSDMNLTN | Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Interacts with ATG1 to form the ATG1-ATG13 kinase complex. Belongs to the ATG13 family. Fungi subfamily. |
W0TA43 | MSDSDREIIGLINNFFLKAALLLEQCKVVARGGGFDGEEPLRDGNHLFNIETRGDPTLEAQIQPWTTFDGEKSMPPLVLETFLDLRGLHSNQTVYLHDSDGNPWMVCKGGKKSEIVLERWLIELDRQFSSTTGSTDAAEDDEYNEFNDPENLHKQLVLLFRYLYTLTQLLPANDIITKLQASQQGTAQATTTTGTLKPLHIHTRLLDGSKPILSKGRVGLSKPIIASYSNTMNETNIASHLEQRKITPIKTKFGSLRITVSYRKDVDFYVIDQEDPYKRTTNVSALQDTVTATDRRISSNSNISISVSPKTTNMLNANHIPVDSSGGGFARRQSISSKLQPFKVGSVGSGSFVQSGSLQSVTNPNPSLSRNVSSSSVAAALKVQRGSAGSTVLNSDLPPELSSVGSGSKYSSSFGRIRRHSSVRRSESIDRTAKPRKSNETPPEDLLEFVKLLEDKKELNMKPSTILPQQDISSSLIKFQSMKPNNDTLSDNLSMSMSIDQPNMRMGSNSHSPIPSFSPNYGSIPSRLSQGSRNNSNVELITSRKSSLDRHRLSLLNRTGSNVDIRRGSVGTMETTNEDSKEDEDSHVHGLRFNSGTVNDKTEDNNEDDDEEEILIKRSSNAVASSTEHFSVSPRSARSISVSSYTRSQLPLKHPNFSYPTTSATTAHAKFHKSEVIPDQLHREGSHHHNSSHKNDEDDDLLFVMSDMNLTN | Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy (PubMed:26442587, PubMed:24793651). Involved in ATG9 and ATG23 cycling through the pre-autophagosomal structure (By similarity). Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation (PubMed:24793651). Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy (By similarity). Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Hypophosphorylated form interacts with ATG1 to form the ATG1-ATG13 kinase complex (PubMed:24793651). The ATG1-ATG13 complex interacts with the ATG17-ATG29-ATG31 complex through direct interaction with ATG17 (PubMed:24793651). Interacts with VAC8 (By similarity). The minimum ATG1-binding domain (residues 441 to 500) comprises two alpha-helices and a linker connecting them (PubMed:24793651). Hyperphosphorylated under nutrient-rich conditions (PubMed:24793651). Starvation and TOR inactivation results in ATG13 partial dephosphorylation leading to ATG1-binding (PubMed:24793651). Dephosphorylation induces ATG17-binding (PubMed:24793651). Impairs ATG17 localization to the preautophagosomal structure (PubMed:24793651). Still forms preautophagosomal structures (PAS) in proximity to the vacuolar membrane (PubMed:26442587). Kluyveromyces marxianus proteins are shorter in length and have a more ordered secondary structure than their S.cerevisiae counterparts, which might contribute to the superior thermotolerance and solubility (PubMed:26442587). K.marxianus could be therefore useful as a new model organism for further elucidation of the molecular details of autophagy (PubMed:26442587). Belongs to the ATG13 family. Fungi subfamily. |
Q80TU9 | METELSSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALSGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLNGLGEGFQTVRVGTVGTPVGTLTLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAEDAGVAYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAVLGLGSADLAYPVVFTAGLNTTHAHQLMVPGKEGGVTLAPSHPTHGAQADPERLVMHMPSDGTHCAATPSSSEDTETVSNSSEGRASPHDILETIFVRKVGAFVNKPINQVTVTSLDIPFAMFAPKNLELEDADPMVNPPESPETTSPLHGSLHSDGSSGGSGGSTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDFGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ | Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. Part of a complex consisting of ATG13, ULK1 and RB1CC1 (PubMed:19258318, PubMed:19211835). Interacts with ATG101 (By similarity). Interacts with ULK1 (via C-terminus); this interaction is increased in the absence of TMEM39A (By similarity). Interacts with ULK2 (via C-terminus) (By similarity). Interacts (via the LIR motif) with GABARAP, GABARAPL and GABARAPL2 (By similarity). Interacts (via the LIR motif) with MAP1LC3A, MAP1LC3B and MAP1LC3C (By similarity). Interacts with TAB2 and TAB3 (By similarity). Interacts with C9orf72 (By similarity). Interacts with RB1CC1; this interaction is increased in the absence of TMEM39A (By similarity). Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family proteins GABARAP, GABARAPL, GABARAPL2, and MAP1LC3A. Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. ULK1-mediated phosphorylation of ATG13 at Ser-354 is required for efficient clearance of depolarized mitochondria. Belongs to the ATG13 family. Metazoan subfamily. The sequence differs from that shown because it seems to be derived from a pre-mRNA. |
W1QCN1 | MSSVRRPSKLLSEKQSDKLAQIIQNFFLKAAHVIFHFRVAFPSVVLQPDDSYGAMGDSFAQSKYNNRWFNLDLGNYEIPRTELSLWRNKDILSLPPLVLETFLDLRGLSSNQTLMLDDVIVKTSKKSEIVLERWLIEFDLSTFDNEVMEFPSIYKKIIILFRSLYLLAGLLPSYKLRDKLVKSKSKNSAIHVSCRILDGSKPITSKGRIGLSKKLLSEDEHTSSKKLQPILTPIGALRVSVSYRTNCNFQVSDNEEALSSQFMLDHLPSVRTNYDSDGNSLTSPMDYLQNRVSSASIHLSDQSPRRRSSTRSVQLFKVGSINSSSSPPPGATQSNQSVSSFSTSKPIPVTLNKTNSSASLVPILRQNRDSLPKSIGSMVQNQMQETGHQVSSNSRRFSSSFGSRFRTVSSRNNSLDGQLVVANQPFSTPNNPILHNFRSRNKSPSVSSTELGPSSSIYMDDDLDSFMKMLDSKPDLRFPSNSPSVYEDPLANFKTFQKSNDFLTLEQQQHGSPSSNQIMIHSQSQTSQSQVFKRTVSSDRSRRGSVSSNYSPSSQALRPGVSAPMVTPSVTYGKFHASSGSPSNSSLAQYLRHNSSPPASATAVATVHNSLRRLTSSSQRTNTNSTNSSTRPVNPELLKLKSFNEDVFESDDDEHDEHSPRSTDTKSRNTGPSSGHAEDDEDDLLFAMSDMTLAKNNQEF | Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy (By similarity). Involved in ATG9 and ATG23 cycling through the pre-autophagosomal structure (By similarity). Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation (By similarity). Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy (By similarity). Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Acts as a negative regulator of xylose alcoholic fermentation, a role that is not related to autophagy (PubMed:29438555). Hypophosphorylated form interacts with ATG1 to form the ATG1-ATG13 kinase complex (By similarity). The ATG1-ATG13 complex interacts with the ATG17-ATG29-ATG31 complex through direct interaction with ATG17. Interacts with VAC8 (By similarity). Leads to derepression of several genes involved in xylose catabolism including PDC1, DAS1 and AOX1, and subsequent increased ethanol production from xylose (PubMed:29438555). Belongs to the ATG13 family. Fungi subfamily. |
A5A6N3 | METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEITHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLMVPGKEGGVPLAPNQPVHGTHADQERLATCTPSDGTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKNVREFDAFVETLQ | Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. Part of a complex consisting of ATG13, ULK1 and RB1CC1. Interacts with ATG101. Interacts with ULK1 (via C-terminus). Interacts with ULK2 (via C-terminus). Interacts (via the LIR motif) with GABARAP, GABARAPL, GABARAPL2. Interacts (via the LIR motif) with MAP1LC3A, MAP1LC3B and MAP1LC3C. Interacts with TAB2 and TAB3. Interacts with C9orf72. Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane; the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome formation. The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family proteins GABARAP, GABARAPL, GABARAPL2, and MAP1LC3A. Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. ULK1-mediated phosphorylation of ATG13 at Ser-318 is required for efficient clearance of depolarized mitochondria. Belongs to the ATG13 family. Metazoan subfamily. |
B6GWT6 | MHQHPRSSVPSPAPNFPPRPTARDDRREQEAAPSSPTVDMGSNSARGLGIEPGPQPSEQGRNAALGREALTRLNQIISNYHTKAALIILHSRVALPPSFNKGSESPRVNRWFNVELDDTDVLREPLRPWRTCDATDNRPPPLVIETYLDTKGLTNNQSLVILDENGKRWDVRESLAALQGARAKPYQSENDEIILERWRIELGESSSRLPADLGSILPTVYKKSIVLFRSLFTYSKFLPAWRFSKRNKKLRQSPALQIKYRVVDGSVARDDLSLDHLTAPLSEGSEKVVDTYSFGVTESPAGPFSVQVTYRTNCDFRVDDSEALLSSRFMGADDEIFRPSLPSDDVNRPNPEIGSVPVERKAVENPDCTRAYGSLSTFHQVGPTTGASPISTLRAMRDSGAGSPSPTDSPKRLLPPAKVVPSGRAGQIAGEGGSSNFQRRPSVSFQPFKAPPLSASPALADSPLGMSPRNMSSRIPTGTSADSRVMPPPSSAASARRPTTIASEQAISSSNSASPKPAPISRYSSSFSHRRGRLSAGANRLEDDNSSGRASATSSNAQPGSGLLTEATGTSAESIQADDENISEFLKMLDSKKDLMNSSTSASIQPGPSTTAAALARFRGMRDSNAALSDSMSQSMHMHRSSISSSKQLSGVPPMVAGTSISTASSPGKPMSPHTPHTPHTPAIRSRLSSNSVADDIETDHHSRLPRIHHDPPLEEHSSAENTRAPSSTAGAIDIPTSPRIFNPAYRRSSSAAVRRPIVTSDDDEIFPFGIRSLSLGADESANATLGATQQQNESQKDQQSPAEDRSGPSVSTTGPYRDSASLRGQMSGPTSASASSNPHVYQPRFASSRGRGYSGGHSLSSASSSLARGANLTPHLAERDQDRDGNASGSNSGNSTLEIRRGSGQRPSTGRTLSGQAPEDDEPLLFAMSDFGASRRSLDEGRHGNHGGTESAAGSRRGSGRRGAGLPGFHVWS | Activates the atg1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, atg13 is also required for glycogen storage during stationary phase (By similarity). Interacts with atg1 to form the atg1-atg13 kinase complex. Belongs to the ATG13 family. Fungi subfamily. |
Q0UPX4 | MNPYQRASPRTASPASNLQTNPTRTNNPRHSADRNSYFDNPPYNDRGSEDGEDDMASRGDHMAETDQRQYQKINQVIQNFFTKSALSIVSSRVILPTSFNKNGDIRQNKWFNVILDDSDELQLRLTEWKTMDAMAGQHPPLYIEVYLDISGLGHKQSLVVHDEDGKRWDVAAALNAAQPTSRASSRPARPTQIVIERWKIYVGDIDSVHPSDLTEPLPNVYKKAVVLFRGLYANLRLLPAFKYNKSMAKQPANHTSLKLNYRILNGASERPQLDTLSLPLCPSTDPITETAHIGSTNSPIGPLCISVEYRDACEFSVEDSESLLSDQFMGLDDTYLEQKPRAAAPVPGSLPVDKLNTQETPDVGQAYGSLSTFHQVGPPTGTSPISALRAARDMPSSSPIETPPQKLPPNHRTAQGSKSSLRSNDTSSFQRRTSVSFQPFKAGSLSSSPAPGPAGPASPSSSLGRPTSAFGRNINIVPNSLNQPRNRTSLNALPQAALRAPSLPNDNAIASSASSSPKPAPITRYSSSFGHRRGKFSTGGSKTEEDALSSGKGSATSSLQRGSDTLNDGEGGSSGEMRSEDDNISDFLKLLEAKKDLKSFNRSDSSTRDATMRKTTAQLGKYQRMRDSHAQLSDSVSSSTMLHRSSSSSSRQLSSVPAMIHGTSISTASSPGKPISPHTPHTPAIPSRLSANSIIEYDQPHRSRNHRSRSRSGRTARGQGPENLEEQSEVEDDAAGIDIPLSPRPWNYQRRSSSVAQQNRNLPEDEPDMFGVRAASLPVEEGDRARDLHRITSTDLTSSGLFAQTESLASASRDNQAPDDGDSRDDLPRASSTSNTPAKRGTYSSNLRGRGGFFSQGSSTTGSTGGTSSTERQSRYNFNSRAANLDDDEPLLFQMSEIGAGGSRRSLEEARGGSSTGSARGRNSPWGGR | Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Interacts with ATG1 to form the ATG1-ATG13 kinase complex. Belongs to the ATG13 family. Fungi subfamily. |
A7KAJ8 | MSSARRPSKLLSEKQSDKLAQIIQNFFLKAAHVIFHFRVAFPSVVLQPDDSYGAMGDTFSQSKYNNRWFNLDLGNYEIPRTELSLWRNKDILSLPPLVLETFLDLRGLSSNQTLMLDDVIVKTSKKSEIVLERWLIEFDLSTFDNEVMEFPSIYKKIIILFRSLYLLAGLLPSYRLRDKLVKSKSKNSAIHVSCRILDGSKPITSKGRIGLSKKLLSEEEHTSSKKLQPVLTPIGALRVSVSYRTNCNFQVSDTEEALSSQFMLDHLPSVRTNYDSDGNSLTSPMDYLQNRVSSASIHWSDQSPRRRSSTRSVQLFKVGSINSSSSPPPGATQSNQSVSSFSTSKPIPVTLNKTNSSASLVPILRQNKDSLPKSIGSMVQNQMQETGHQVSSNSRRFSSSFGSRFRTVSSRNNSLDGQLVVANQPFSTPSNNPILHNFRSRNKSPSVSSTELGPSSSIYMDDDLDSFMKMLDSKPDLRFPSNSPSVYEDPLANFKTFQKSNDFLALEQQQHGSPTSNQIMIHSQSQTSQSQVFKRTVFSDRSRRGSVSSNYSPSSQALRPGASAPMVTPSVTYGKFHASSGSPSNSSLAQYLRHNSSPPASATAVATVHNSLRRLTSSSQRTNTNSTNSSTRPVNPELLKLKSFNEDVFESDDDEHDEHSPRSTDTKSRNTGPSSGHAEDDEDDLLFAMSDMTLAKNNQEF | Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Interacts with ATG1 to form the ATG1-ATG13 kinase complex. Belongs to the ATG13 family. Fungi subfamily. |
A5DQA8 | MEKPKQKLTQVTVNFFLKTSQMILQARSLDEHGKGKLNKWFNLHTFNSDDLRSELRLWRSTIDLTAVPPMIVETYLDLGNLPQGHTLALKDEHGNLWPVTKGGSKKTEVVLERWLVEFDPNEFGTIEELPYIYKQAIILCRSIYTIIRIMPAASLRNQSPHYVLANKIVDGSKPISSKGRIGLSKTIIPHQMLTDTHVRHRTFSPIETSLGTLKVSVAYRSHCEFTELAEWDHRELGREKEPREDLRQVESKGEEDHSIESIPYEEKAYKTDEEKSDKTPEHVQYKPFKPEFKQLEAVKLEGSDFKSELHEGTSPLSLSGSPSSPPRDDKKRPSIQPFRVGSIGNSPPPASSSLERRISITSNKSTSNASLAAVLRNPRSSFSIPIAGSIGTGAPVTGGFPRSVSSSHGYGYEDSDSAANTPRFSSSFGSRASRRFSNTSVRHGSLHDTTSPLGTSAGSATSIPLSGLYIDDDISDFVRMIDSKQDLRFGHDSGGSGSQSGSQYEVLNRFHQLKSQHQQLGDSVNASVMMHRKSSSPPGSYESHVPSIHSRLRESSEPHPAPATAPAPGPLIKPASKMMSSPVISTTSAHAMSQTASATTRDEIVGLATTPSTYRKHLHYENVFDDDDEDEDHHGYFKAKARSKSLSRSHFDDDDDLLFTMSDTNLAKH | Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Interacts with ATG1 to form the ATG1-ATG13 kinase complex. Belongs to the ATG13 family. Fungi subfamily. |
A3LQY1 | MASQDISYQYKSQQEHYPNEKISDSYVQKQNSKLTQVIQQCFSKAVKIIIQSRTVPPAAASPLLNPALHDDSASGNKINRWFNLHIQNSQDLPKDDLKLWKSNHLQSMPPMIIETYLDLRQLTSSQTIVLNDDNGNPWAVAKSGGKKQEVVLERWLIEFDHTDASGSIVDELPLIYKQAIILFRSIYGFARLMPAFKLKKRLLINKSSTKLNKLTIGNKILDGKQPISSKGRIGLSKTIIPRQMLTTDSHMSQKHFQPIQTSLGTLKISIAYRNHCDFCIHDNEEVLSTHFISMDSTPLTESGHGHTKANNTSMSVSPCSSGHPALREGSPTKRGTPPTAIQPFKVGSISNSPPPASHTPNSGYGGSLERRISITSNRSTSNASLFAMLRNPRSSTSSTHTTSNIPIAPSSSSNSTNATNMNNMSYPRSISSSHGSNMQHDDSMFSNPDSTTNTPRFSSSFGSRASRRYSNTSVRQSTPVAASTLTGGSPLSGLYIDDDISEFVRSIDSKADLRFSNSYTAHNSGEPKNNMGSPSGGDALNKFQMMKSHHQQLGDSVNASLILQHNNAVSGSGSGFGVSNSRHSSTSRKSSHSIRSPSPSMSGLYDVVPGSYGRSERRSSSGAGVPGQLSLPSGGGLAAHSPSATEPTSAATITPRETNFNFSNASFLRSASKLSATPVTSTTTAHATIHSVTGMATSPSLYQRTKVGSSIHYENVFEDDDDDEMVMKKPVVTSSGRDEEQLQHKQMKVVSIEKDAGANNFDDDDLLFTMSDMNLTKSS | Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Interacts with ATG1 to form the ATG1-ATG13 kinase complex. Belongs to the ATG13 family. Fungi subfamily. |
Q9USM8 | MAQDDSYEEKPEVISSDSGGSGYSTEIQIVGTVTSSDGSYVEYEIVHQKRSVWRRYSDFESLVKLMRRQYPAAIVPPIPGKQSLLSYAKHPRKAKSDAEFLNFRSRMLELFLRQCLLHPCIRSNPIFDKFIHSTVSWHVTLSSLDLPKDSNTDPLRLPPIATEHDPFAHLRSSMPLVMANSLSPPSSRALKPIHSLSNPSTASSLEPSSPLGSEDECHPPTSDMQPTHELNESPSTPTAPDFPHYNSSPSELSPTQRRSSISNGKDAPSPVLKDLTSYTQEVIVCRKFLHHSLSPSIHSTLSSISKMESCLSKLGSAFHSLTALNEIQLANHLQVIANAFEFSGMYAKEFEQEFNSSVYEKMVQSMQLAKCAADALKYKQLKIQQRDFLQDQLIHSNTMSATDSMVAASPTIHPATRLNTIQRAVVSQAKKGYTIFGRLQNVLHDFVEGETSISKESLQQHKNTIENQLAAANWDCQKIDEFMDAELKFYKECQTSQWEEIIKSVHECIYKWAQTNLQRWLRTREELENLSKDI | Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway (By similarity). The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization of ATG20 to the perivacuolar punctate structures. Belongs to the sorting nexin family. |
A7TIP6 | MKQKKNRFGSGKRITDQSSVDGDLIAPGNSSMDKRRNSSSSRSSSTQESKELTESLASVHTSDMHQSNIHERIDGDDNPFLDQDDESFKSTRANTSATKLTDVVNPNAEYKDNDSDNDEEILTATAPDTSITEGIVSTEADGGNDVVTASVEDKEGTVTDTAVGLDNANNTVDQKVKESIIPDIKLINDRVQILEANKVSEGQGRAYVAYTIKWGDQSVRRRYSDFESLRSVLMKLFPTSLLPPIPEKQTLKNYSKSIAGSKSNYLLPSEGTGSVDLVLSVINGTVTNNDEKLIRHRIRMLTSFLNKLLQDEEILKTPIIYDFLDPNNINWNDFINSSATFSMLPKSVLQCNPLDPTNTTRIHACLPVPSTSHILPSKEKVSDTKTIERKDGFDIIEQEHKQYESLLKSGFYKHNTQITKSLYGMQHDMKDLSDTFAHFASAQACEAELAEQLTYMSNAYDDAASNLEALVGLLYYNINEPLGESVRMAGSAKELIKYRKLKGVQLEILINSLESKRQQLHKLELQRGVQPRNGNTASGASGNDESSVKKPQASKSQSSSYGGKFLNRFNKIAAMVKETINYQEQDPQTTMANLIKEIEQLNESEQVARHDLEDISKIIKEDRLTKFSEEREKELNEILRNYSKYLKDYAKKNLELWKEIKTRQEQL | Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway (By similarity). The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization of ATG20 to the perivacuolar punctate structures. Belongs to the sorting nexin family. |
A6ZXL6 | MSDLNDVQENAKLNSETRNTGKAEPPHGTTEYVAEAEISKNGVGSPKKSPKKGKVGKGDNNKVETELVHTALLEKDNPFMEEGPTGFTKSALLEIPGMRSHKLKNPNEDYEDDSEGLLPLNQESNAETCRTSLSGSINSMNGETSASEEPSVSNRKKSARIHILEAKRVSEGQGRAYIAYVIQFENSTVQRRYSDFESLRSILIRLFPMTLIPPIPEKQSIKNYGKSITGSSSKYLLPSEGSGSVDLSLSVIHASVNNSDEKLIRHRIRMLTEFLNKLLTNEEITKTSIITDFLDPNNHNWHEFVNSSSTFSSLPKSILQCNPLDPTNTTRIHAMLPIPGSSSQLLLNKESSDKKMDKERSKSFTNIEQDYKQYENLLDNGIYKYNRRTTKTYHDLKSDYNEIGEVFAQFAHEQAQVGELAEQLSYLSNAFSGSSISLEKLVGRLYYNINEPLNESVHMATSARELIKYRKLKYLQNEMIKKSLNSKRAQLEKLEAQNNEYKDVDKIIDNEMSKSHTINLERPNNNTGSGGKSYGGKLFNGFNKLASMVKDSVKYQETDPHTASINLKKEIEQLSESLEVTENDLEVISKVIKNDQLPKFSKEREVDLSEILKHYSRYMRNYARQNLEIWKEVKRHQDFA | Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway. Required for proper sorting of the v-SNARE protein SNC1 (By similarity). Forms a complex with SNX4 and ATG17. The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization of ATG20 to the perivacuolar punctate structures. Belongs to the sorting nexin family. |
D6VRN7 | MSDLNDVQENAKLNSETRNTGKAEPPHGTTEYVAEAEISKNGVGSPKKSPKKGKVGKGDNNKVETELVHTALLEKDNPFMEEGPTGFTKSALLEIPGMRSHNLKNPNEDYEDDSEGLLPLNQESNAETCRTSLSGSINSMNGETSASEEPSVSNRKKSARIHILEAKRVSEGQGRAYIAYVIQFENSTVQRRYSDFESLRSILIRLFPMTLIPPIPEKQSIKNYGKSITGSSSKYLLPSEGSGSVDLSLSVIHASVNNSDEKLIRHRIRMLTEFLNKLLTNEEITKTSIITDFLDPNNHNWHEFVNSSSTFSSLPKSILQCNPLDPTNTTRIHAMLPIPGSSSQLLLNKESNDKKMDKERSKSFTNIEQDYKQYENLLDNGIYKYNRRTTKTYHDLKSDYNEIGEVFAQFAHEQAQVGELAEQLSYLSNAFSGSSISLEKLVGRLYYNINEPLNESVHMATSARELIKYRKLKYLQNEMIKKSLNSKRAQLEKLEAQNNEYKDVDKIIDNEMSKSHTINLERPNNNTGSGGKSYGGKLFNGFNKLASMVKDSVKYQETDPHTASINLKKEIEQLSESLEVTENDLEVISKVIKNDQLPKFSKEREVDLSEILKHYSRYMRNYARQNLEIWKEVKRHQDFA | Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway. Required for proper sorting of the v-SNARE protein SNC1. Forms a complex with SNX4 and ATG17. The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization of ATG20 to the perivacuolar punctate structures. Present with 358 molecules/cell in log phase SD medium. Belongs to the sorting nexin family. |
Q75D34 | MKVLRFNQDASCFSAVSRPHSMTIYNCDPFGKCFELENSVVTSESCDTECLTKAQGDQCSNFVTEMLFATSLIAVVNRDQGLQKARKLRIVNTKRKTTICELTFPHEVVDIVMNRKRMCVLLSSDQIFIYDISCMKLLQTISVLEDKLKMAVSDQGHVSTSVVGRQLQGETSMVRIALCSDDKSILCYTAYCRTNKNSYILNDLVVYDALNMTPLNYLNTVHKGNVACLCISNDGKMVATASDKGTIVRIFSTGDENTLQSGNTLLHEFRRGTRPCSIYEMKIDPTRRYLACVGHTDTIHIFDLERQGQQNKSLSDSQSTALLREGKLSKESTLQFASFLSKKVISKIPNQNMERHFAHIKVDDSVRHCLGFPDEFSDRVYVASNNGEFQVWNIPQSGGECILVKKSKF | Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity). Vacuolar and perivacuolar punctate structures. Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2). The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions. Belongs to the WD repeat PROPPIN family. |
A0A1D8PCZ9 | MVTINDLSFNPDYSSISVSTSDGFKIFNCEPFGEFYSSQESPLRKSISNSLEDSAGCQNPTHSKTDSQDTPARFPTAFLKMLFSTSLTIVVPQTQDNLGNRLLKIYNLKQNLKICELNFPSSIIDIKLNRKRLLVVLDTGQLYIYDLSCVRLLKILQLSFNEHDGDQKFIGDLSADDSSWLIIPVQSTNNQTDLLNAETGSQPSTPKLTPSDSVINTGSYSQYLEFTRNSSLSNLKKKNKLITLEDIKNDSEGWVVVYDTINLAPVVIFEAHHSTIARICISHRDNKVATASIKGTIIRIFDLKEFEGKVKVHKVKNLRRGHNLVKVNSLSFHNDNHILGCGSESNTIHLFKIHEEESDICTNENSEDRTNHNSDYEDSDGDTSKSSEDLNENLANLLISKPLDPVPMETEDKLSSSWFVKTKKLINNQYTSSIIKKLPYKDYFENLIWEPPQRSFAYIKLPEYAPHNEKDPRSNKVEIGFNNDLVFIASYHTGNFYQYQIPKQRGPVSSINEDDKREECSLISQFNLI | Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity). Vacuolar and perivacuolar punctate structures. Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2). The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions. Belongs to the WD repeat PROPPIN family. |
Q6FRU4 | MKVLRFNQDASCCVVNSGANELTVYNCDPFGKCFEFNISNVNGDSNDNGIGYDSLEAGSSSIESQVIAEMLFSTSLLAVVDKGQGINTGKKLKIVNIKKRSLICEIAFPSLIVDVVMNRKRICVLLDNDQIFIYDISCMKLMETLDLWESNNEGNLNDHIKVGERASNMINENLKNGNELDRIRSKSNNNNDQTNSDNGRSRTYSINGSHKIKPQLTLSGNDNSILCYSKYSSSKQNPARILNDIVVYDALNLKPINYLNSVHKGCVLKTSVSIDGKLLATASEKGTIIRIHKTGVDSDFASGPLLYKEFRRGSRPSHIHQLLFNKDSTLLVCVGDSDTIHIFRTDDDGLALDGIDGDIGSDSGGSLELIKNRIPHEQVKKFFSRKIKSHIPNQNLHRDFAHINMDRIVHTVVGFPEEFDNKIYVASDDGSFKTYTIPSKHGQCVLNKTSHFI | Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity). Vacuolar and perivacuolar punctate structures. Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2). The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions. Belongs to the WD repeat PROPPIN family. |
Q6BIA1 | MVIINNLTFNQDYSCVSVSTTKYHKIFNCDPFGEFYSSYQGSSGTKGDKPNDNDKEIIIDKGNGNEYNKIGEDSPTSYLKMLFSTSLTIIIPQNESVGNRLLKIYNLKQNMKICELTFPSHIIDVKLNRKRLCVILESGQIYIYDLSCVRLIKVLEISSFSSKDSEEETHQKLFVGDLGAEDKSLLVLPISNITDQTDLFNTENGVNVTRASDSNILTSLKPLIEFTENKIDKDIITLEDLQKDSNGWVLIYDTIKLKPRLIYKAHDSSLAKITISNDNKKIATASSKGTIIRVCHLESSDDEDVSKPFNISQIINLRRGHNIAKVNCLSFSLDNSILGCGSESNTIHFFRLSKQPHESFEYEEDPANESDPDDEDRSSEDLNQNLANLLISKTPDASAPDQKDSAKSSYFGVLKKKVEGSSRFMNNPYTQTIVRNLPYKNYFENLIWEPPRRAFAYVKLPEYTPPQLFNLHQSKNKVAIGFANTNNNGHLIMLASYQTGQFYHYQLPKPSDQPEPSDSRHECNLIAQYSLL | Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity). Vacuolar and perivacuolar punctate structures. Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2). The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions. Belongs to the WD repeat PROPPIN family. |
Q6CLZ2 | MALKLLGFNQDATCFSVISSNKGVTIYNCDPFGKCFELEKSTSNDEELDFLVEMLFSTSLIAVVDKTIGASKRKKLKIVNTKRKATICELTFPHEIMDVIMNRKIICVVLKSDQIFVYDISCMKLLRTIDVRGEKLKSTSKFRNSEAVGDIGVRVSLSTDNNSILCYSSYSKSDKENAPLNDIVVFDALKCIQINVLPAVHQSNIVCIACSPDGMLMATASEKGTIIRVFKTIDTENDEPILVNEFRRGSRPSRISEMKFNHDNTLLACVGESDTIHIFALPVTTTEADANEDDTLQQSSHSLSSSINGLQYISKGLANRFGKIIVSKIPTQSQQRHVAYIKIPENAKYRIGFPKDTTNTIHICGEDGNYLVYSIPRNEVGPCTLVKSNTFD | Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity). Vacuolar and perivacuolar punctate structures. Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2). The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions. Belongs to the WD repeat PROPPIN family. |
Q5QJC0 | MALRSISFNQDYTCLAAGFDAAYKVYNCDPFGECFQKADDGGANLVEMLFSTSLIAVVGIGDKPANTMRKLKIINTKRKAVICELTFPTAILYVKMNRKRLVVVLVDQIFVYDVSCMKLLHSIEASAGLDDRIICDLCADDESVLVFQQSGSSDELAANAGTVVVFDALQIQPINVIECHRSPLQRIAVSKDGRLLATASVKGTIVRVFRVADGRKVHEFRRGSYTAQISCLSFNVDATVLCCSSNTGTVHFFRLDDVDRRRSTGSIDANIDGSETLPRESSITEEESSEINRLINSQLGGHNGFAKKKSAESLKNFIWSKSKTYLPSQINSILEPKRDYAFIKLTTEVESVVGLVDNNCYVATRAGDFFVYSVQPGQCVLLKHYKIE | Involved in peroxisome sequestration to the vacuole during macropexophagy. Also required for microautophagy. Vacuolar and other perivacuolar punctate structures. Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2). The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions. Belongs to the WD repeat PROPPIN family. |
A7TTC8 | MGLSRFNQDATCFVTSSEGNSVTIYNCDPFGKCFEMVDEDTQNIGDDDARGDDNSGGDDDLLVEMLFSTNLVAIVHRKQGILKSKKLKIVNIKRKTIICELSFPHPIQDVVMNRKRVCVLLNSDQIHIYDISCMKHLHTIDIWDSQVKSITGQGVDSLSNSGTSNMTSLRERSSTFSKSISPKICLSNDDRSILAFNCYSTSSKSVILNDVVIFDALNISPLNYINSVHKGNVASLAISPDGKFIATASEKGTLVRIFNTGAETESELLTPLLYEFRRGNRPCNINQLTFNSDSTLLGCVGDSDTIHIFKLDSTSRLLSMSVNSEDNSHITSEDIKALRKDPNSKQFTKLISKTIKKSIPSQALRRDFAHITIKNTKTKHILGFPKEFMNQVYVLSNDGSFFIYSLPSTSGSCVLSKQNDFK | Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity). Vacuolar and perivacuolar punctate structures. Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2). The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions. Belongs to the WD repeat PROPPIN family. |
A6ZWF0 | MKVLQFNQDATCCVVAASSHQISIFNCDPFGKCFEIDTKNSKKKTSNNNGTASNSESRNNEESILITNGSRDRTDAEEEEDNEDNALVTGNILKEGEFVIEMLFSTSLIAIADRGQGLNKGKKLKIVNTKRKSTICEIVFPHEIVDVVMNRKRMCVLLESDQIFIYDISCMKPLETIDLWEDHYKRSQANSFSNASNTGTLEGDSANLNRVATNLLANATQKSVNGSNPSVRTRRNSLRSKIRPRMVLSNDDRSILCFTAYSSPKKNKPNSEALYDVVIYDTLNVTPVNYLNSVHKGNVACLAVSHDGKLLATASDKGTIIRVFHTGVDSDYMSSRSLFKEFRRGTRLCNLYQLAFDKSMTMIGCVGDTDTIHLFKLDDASNSLPGDNSSNGHWNEEEDILASNSNPSMGTPKEIPLSKPRIANYFSKKIKSSIPNQNLSRNFAYITVNESNRSCLGFPDEFPNQVYIASDDGTFSIYSIPSKPGECVLTKNNKFT | Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage. Essential for maturation of proaminopeptidase I (By similarity). And perivacuolar punctate structures. Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2). The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions. Belongs to the WD repeat PROPPIN family. |
D6W3R6 | MKVLQFNQDATCCVVAASSHQISIFNCDPFGKCFEIDTKNSKKKTSNNNGSASNSESRNNEESILITNGSRDRTDAEEEEDNEDNALVTGNILKEGEFVIEMLFSTSLIAIADRGQGLNKGKKLKIVNTKRKCTICEIVFPHEIVDVVMNRKRMCVLLESDQIFIYDISCMKPLETIDLWEDHYKRSQANSFSNASNTGTLEGDSANLNRVATNLLANATQKSVNGSNPSVRTRRNSLRSKIRPRMVLSNDDRSILCFTAYSSPKKNKPNSEALYDVVIYDTLNVTPVNYLNSVHKGNVACLAVSHDGKLLATASDKGTIIRVFHTGVDSDYMSSRSLFKEFRRGTRLCNLYQLAFDKSMTMIGCVGDTDTIHLFKLDDASNSLPGDNSSNGHWNEEEYILASNSNPSMGTPKEIPLSKPRIANYFSKKIKSSIPNQNLSRNFAYITVNESNRSCLGFPDEFPNQVYIASDDGTFSIYSIPSKPGECVLTKNNKFT | Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage. Essential for maturation of proaminopeptidase I. And perivacuolar punctate structures. Contains a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2). The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium and in both its recruitment to and dissociation from the PAS under starvation conditions. Present with 6020 molecules/cell in log phase SD medium. Belongs to the WD repeat PROPPIN family. |
Q751W1 | MSYETIPTSDENFDRDVSATNRNVFGWYLYAFSSEPFIVSAMSTYFPLLLEEFARNNGVQVDDHTVACGAEDKHCVLPLFGRRVFVDTSSFALYTFALGVLLQTVLVISVSGVVDVCKTVRFKRNVLLSFGMVGGLATCSTVLLRGNQYYILALLTVISNCCYGVINVVGNSLLPDVVSDLKRVLYLYRVIDSDQLTTVISGRGSGIGYIAAFVVQLCSVWLLRQPEYRDDIRVAVLLVGGWWMLFQLPLIWMLDDVVVRENSTQFKWSRSRQYLKAGWQSLGHAAMHANLLKDVLIFLVGWFIISDSITTINSAAILFSKTELHMSTVNLVVISILTMINAVIGAYFVPQLLSERLELPPHQSLIYLICWAGVIPFYGTLGFVFQSIGLKHPFEMYILAVWYGISMGGLAAVSRSVFSLLIPRGKESTFFSLFSITDKGSSVVGPLLIGLITDKTHNIRYSFYFLFLFVVASIPVFNALNVQRGKVEAEELAGINESRLETNDGFA | Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation (By similarity). Vacuole and punctate structures. Belongs to the ATG22 family. |
A0A1D8PSS7 | MKVNHNHISNTGVNDSEDILEAQDEISIDNNKNQENIWNKKSIFHTWLLLCYSTGPVASMSRTYIPASIQSIAKNVGKTKMNQPCGTQGNDCYVKFGFMTVHHTSYVLYLRAVSTAIEGVVAIFLMGIADYSNYRKSFLIFSILVYGFLALPFIGLTNNDYQTLVLASILYSLLIIDDSIYQILEGSYIPLFMRADKKNPMQRGSVVAVLGLFLGNLGGITALVIGIIISYLSGTPESKGYHNFLLAITIAGCLTIGLSLFSALYIPNVQGKQRIDNFLVLPFKRFFNLLKDIQKYPMAFLYCISWVIWNVSFNNFMSMFLLLFRSTLGLGNSDAEYTVYTFMSYICSSWGSLVWMFLYQKWNSNIKYWGYSFLSVSLLANFWGCLGIHKLTPLGYQNRWEFWVFEVFYSATSSAMRSLNRCVYSSLLPEGNEAQYFGLEVTLGIASGWIGGLVNAVIQDRTNDDRFPFLPNMFLVVVSLIVYYYVDLQKGKNDVNNGNS | May be required for lysis of autophagic vesicles after delivery to the vacuole. Vacuole and punctate structures. Belongs to the ATG22 family. |
Q6FX92 | MAYESLASEPNDGVTDHNDDALYVGIDTLKAARDNIKGWYLYSFSSEPFVVSAVATYVPLLLEQFARINGVQLDDHNAPCSTSSSDKCVLGLFNNRVFVDSSSFALYVFSLSVLFQTVVVISVSGMVDRWKTISFRKNVLVTFGMVGAFATVLISLLNETQYYSLVVYYIVANSCYGVINVVGNSLLPLFVDDLVRLQPDHTVPAAEELSLDTDDKDGLTTVISGRGASIGYSAALVVQLMSILLVRLSPSKQDIQYAVFFVGLWWAVWQFPMYWLLSDSIIPDQQSNQAIANGRYYDIDGSIFTFVNLSSLKYGWKLLGEALKHATLLRDVVIFLIGWFILSDSLTTINSTAIIFAKTELHMSTINLISLSIITMISAMVGAFAIPQIVSTSLHVPPQRTILLIICWASIIPLYGMLGFIFQSFGLKHQFEMFILGVWYGISMGSVAAVSRSLFTIIIPKGRESTFFSLFSITDKGSSIVGPFIIGIVTDKTHNIRYSFFILFILLVFSLPIFKMLNVERGKREAEEISKLHVNIDPIQD | Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation (By similarity). Vacuole and punctate structures. Belongs to the ATG22 family. |
Q2HFE0 | MVPRNDPEAGRPPLAPRLFSRFSQLSKHSFLSYSSSFEADDERSSTGSLENFGIMSPGRSRSNSGSGSSSFGALPPRYPGDDTRPTSPKELAGWYAYAFAAEVYVICGSFIPILLESLARENGVLLSDRKTPCGSSSDKNGDNGGQCIVYVLGMEINTASFAMYTFSISVLIQALLVVSISCAADHGNYRKKLLLAFGWIGSIAVMLYIFVSKNLYIFGALLAIVSNTSFGASFVLLNSFLPLLVRHHPEIIDKEANIVPNGQDAQDHEDLDGETAMADSTAALLPRGSLEDGNALSRVQTREELTSHELNLSTQVSAKGIGIGYIAGLFLQCVAIFILIQMKNTTWSQRVVLFVIGAWWAIFTVPAAMWLRPRPGPPLPASSRHTGIRAFIAYTFYAWKSLFRTVQLARRLVDIMLFLGGWFLLSDAIATTSSTAILFAKTQLHMEPWALGMINVISTAAGITGAFSWSYISRRLHLQAHQTILACIALFEIIPLYGLLGYLPFVKNWGVFGLQQPWEMYPLAAVYGFVLGGLSGYCRSLYGELIPPGSEAAFYALYAITDKGSSVFGPAIVGAIIDASGEIRPAFWFLAAIVGLPAPLIWCINVERGRSEGEKLAEVIEGFKVTRSPERESDEESRAILDVYDEETDR | Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation (By similarity). Vacuole and punctate structures. Belongs to the ATG22 family. |
J3KIA5 | MTSSPPSTWRNLDENEALLRHPILNKYPGEDTRPTSKKELAGWYSYGWAAEVFAVCAMGSFLPITLEQMTRDQGVLLSDKKTPCSASWPTAPTAYAAADATASPRVGPPQCVIYVLGIEINTASFAMYTFSISVLIQSVLIISMSAAADHGVYRKKFLLAFALMGALSMILFLFLLPRFYLLAAVLAIIANTGFGASFVLLNSFLPVLVRNDPSIQATRYAAASDEQTYYTQNPSGSNTISPVDEPERLDVSSNDSALVSAELRLSTKLSSNGIGIGYIAAVLVQIGCILLVVATHSTTFSLRLVLFIIGLWWLVFTIPAALWLRPRPGPPVPDSAYGKGRWAWVSYIVFAWVSLGRTIVRARQLKDVLLFLAAWFLLSDGIATVSGTAVLFAKTQLGMNIAALGLINVIAMISGVLGAFSWSYISHHFNLRPSRTIVACICLFEVIPLYGLLGFLPFIKRLGVIGLQQPWEMYVLGAIYGLVLGGLSSYCRSFFGELIPPGFEASFYALYAITDKGSSMFGPAIVGAITDRYGEIRPAFGFLALLILLPLPLMLLVDVDRGKRDAKELAEALEGVKDMGTNGTGYATVATHEVEVGYEGDRE | Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation (By similarity). Vacuole and punctate structures. Belongs to the ATG22 family. |
Q5KFW2 | MPPPHVRAWYSYAFAAEVFSSYPSGNIPANHFGTCDGKALQSSDPRGMDRYSFVQSSSMYVKSIAVACQAICIISIGPLADIAYWRKRLLLTFAYSGSLSGILFLLFPPLPYAWTPIMAAILNIVGNATYSTSIVCSNAFLPGLAKEDVDVQKAWEEATSEGLQDGLRDVHEDTDEENTGSVSREDEATHLLPDRLIPAVCAISTQDLALSDPLAKLIEPSNAKKHYESRLSLTTSRLSSTGTAIGFFSGVSVLTLLLIPVTALGGSTFSMRLAIGLSGVWWALFTVPTCIGLPGGAPGHGSDFSASQVKKAWVKIGKMVAPKQIHQLPNLYIFLLAWIFLSDGFHTTTYAAILYASSVLSMSAPKIILVGILVQLAAVVSSVLVPRVQRRLSTTSSKPVTNYKVLLAGVVAAAFIPVYTCAGLVLPFGGLRSEGEMYVLAVWFGLVFGPFLSYSRAVYAELIPPGHESTFFSLFAFTDKSASFIGPAAVGLISDLTGNIRYGFLFLLVMLVVPIPVLGRVAVERGRREAVEWAERSRKEMSDERV | Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation (By similarity). Vacuole and punctate structures. Belongs to the ATG22 family. |
I1RMK9 | MADSVDRVFVHALNTVKKIPKTGASRPPPTDRLRLYGLYKQAMEGDVDGVMERPTAASGLASDELQREKDKWDAWNLQKGLSRTESKRRYIEALIDTMHRYATTPDAEELVSELEFVWNQIKDNSPSSSLSSPRPNQSTGAGAQQPQQEPEQASDGEGPLKELRPMSEYDEAELRSQRQVDLEDDEVDVPTSDRSSGRWQRKVERALTTMSAEVAALREQIMTGREWRTKKERSVPAWVKWFAWLLVKHIFADLVILSVVLLWLRKRKDQRLEDIVRAGVRLMREYVRNVLPSRG | Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy (By similarity). Required for both micropexophagy and macropexophagy, but not for the cytoplasm to vacuole transport (Cvt) or autophagy pathways (By similarity). Required for functional micropexophagic apparatus (MIPA) and relocation of ATG11 to the peroxisome-sequestering arms of the vacuole (By similarity). Binds palmytoyl-CoA but not oleyl-CoA (By similarity). Does not significantly decrease the growth rate under nutrient-rich conditions (PubMed:28894236). Belongs to the ATG37 family. |
C4R8D7 | MSESIDRVFVKAIGTIRTLSSRTGYGGLPRPPIENRVKLYGLYKQATEGDVAGVMERPLGDSPEAEAAKRKWDAWRSEQGTSKTEAKRQYISYLIDTMKQFASDTTEARELLSELEYLWNQISDVSPNDSSDSESNAGPAQLLQNHAQLLSRDISVVDDPITSSGMDPMYNPSFQRHNSSRFINASTAERLNSLSNYYSNLNPTPPLSSRRYQGSVTPRNVDFIKWQNDINNSINKLNHDLQLLANRRLQSSASDPLYSKRGSDLTHDDFVNDISSSSSNRRFRARRNQPLVSKVLLGTISLLLKLIKTVIKHVAIDAVIIAVLVAVIKRSIIIPNLISNEISLQKIHHSELESNSSIKGDSNGGRLTIVLPFINGKDFFQENSLLGKLLKVFHDYVDHVSRIRLIKRN | Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy. Required for both micropexophagy and macropexophagy, but not for the cytoplasm to vacuole transport (Cvt) or autophagy pathways. Required for functional micropexophagic apparatus (MIPA) and relocation of ATG11 to the peroxisome-sequestering arms of the vacuole. Binds palmytoyl-CoA but not oleyl-CoA. Interacts with ATG30 and PEX3. Localization to the peroxisome is ATG30-dependent. Repressed in glucose and ethanol media, but induced under peroxisome proliferation conditions in methanol and oleate media. Phosphorylated. Belongs to the ATG37 family. |
D6VYL2 | MSTLAEVYTIIEDAEQECRKGDFTNAKAKYQEAIEVLGPQNENLSQNKLSSDVTQAIDLLKQDITAKIQELELLIEKQSSEENNIGMVNNNMLIGSVILNNKSPINGISNARNWDNPAYQDTLSPINDPLLMSILNRLQFNLNNDIQLKTEGGKNSKNSEMKINLRLEQFKKELVLYEQKKFKEYGMKIDEITKENKKLANEIGRLRERWDSLVESAKQRRDKQKN | Autophagy-related protein required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. ATG38 is required for the integrity of the active PI3-kinase complex I by maintaining an association between VPS15-VPS34 and ATG1P-VPS30 subcomplexes. Homodimer. Component of the autophagy-specific VPS34 PI3-kinase complex I composed of VPS15, VPS30, VPS34, ATG14 and ATG38. Interacts directly with ATG14 and VPS34. Localization to the preautophagosomal structure requires ATG14. |
D6VYV5 | MSEEDDHWNLVRLRRLRKGREGEEQSSKSEISLDSLHESSFAGEDDEDFDADVLSNTSSEESAQMNRIYDFRTSNEFSNAGVNIDQTGVPTISESFDTLSGSNVGGTVLPSMEGSKLKDSTIRNSSTLSDHIIDKSEGKSAKLKMWHVIMLSSLLSMTFSYLALEYSLTGDVLAGFKSQQSLRNNERKLLYGNIDFVDKKSYDSSSDSLSQWAPSGKYYVDFDNHIAYPLKDDDLMGWRRYKTDLVILWYTTKARMKDGWHKRINKINGGRIKLHLFLKNSFKSAQESLRVLHKEQKRRWKRLFVLLHNKYRQFSPHIKRYFDHSCQKAKQCWSGSRLQLRKLRFKSMKPFRVFQFKVRKDTNWFVKQLKRFGLKLQHSRMYKAMSECRKKNYFKCKH | Acts as a receptor for reticulophagy and nucleophagy. Directs autophagic sequestration of double-membrane vesicles derived from the nuclear envelope and perinuclear endoplasmic reticulum (pnER) into autophagosomes. Is not required for the cytoplasm-to-vacuole targeting pathway, mitophagy, pexophagy, and non-selective autophagy. Interacts with ATG8 and ATG11. Expression is increased by rapamycin, which mimics nitrogen starvation by inactivating the TORC1 complex. Partially blocks reticulophagy, and the double ATG39/ATG40 knockout almost completely blocks this pathway. Leads to abnormal morphology in the nucleus/pnER, when exposed to prolonged nitrogen starvation. |
Q9FKG9 | MVLSQKLHEAFKGTVERITGPRTISAFKEKGVLSVSEFVLAGDNLVSKCPTWSWESGDASKRKPYLPSDKQFLITRNVPCLRRAASVAEDYEAAGGEVLVDDEDNDGWLATHGKPKDKGKEEDNLPSMDALDINEKNTIQSIPTYFGGEEDDDIPDMEEFDEADNVVENDPATLQSTYLVAHEPDDDNILRTRTYDLSITYDKYYQTPRVWLTGYDESRMLLQPELVMEDVSQDHARKTVTIEDHPHLPGKHASVHPCRHGAVMKKIIDVLMSRGVEPEVDKYLFLFLKFMASVIPTIEYDYTMDFDLGSSST | E2 conjugating enzyme responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Interacts with ATG8 through an intermediate thioester bond between Cys-258 and the C-terminal Gly of ATG8. Also interacts with the C-terminal region of the E1-like ATG7 enzyme (By similarity). Belongs to the ATG3 family. |
Q755K1 | MLRSTLSNWREYLTPVTHQSTFENTGQITPEEFIKAGDYLCHMFPTWRWNQQQGGMVYRDFLPQDRQFLVTRKVPSNMRAADSVNVGGEEETSAGEYWVLQPQQESADGGEEIDIDEMLQEMDIEDQSGEQDIIQLRPSHTRFYDLYITYSTSYRVPKMYLVGFNNDGTPLTPQQMFQDIAPDYRTKTATIEKLPFFKSAVVAVSIHPCRHANVMRVLMEKVRAAKQKPVEEEQPDGPREDWEDLQDEVDSSLRVDQYLVVFLKFITSVTPGIEHDYTMEGW | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Monomer. Interacts with ATG8 through an intermediate thioester bond through the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5 conjugate. The N-terminal region is involved in phosphatidylethanolamine-binding and is required for ATG8-PE conjugation. The flexible region (FR) is required for ATG7-binding. The handle region (HR) contains the ATG8 interaction motif (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Belongs to the ATG3 family. |
A1CAN8 | MNILHSTLSTWRDRLAPVSRTSTFRTTGQITPEEFVLAGDYLVYKFPSWSWADASSPAKRVSYLPPGKQFLVTRGVPCHRRLNENFAGDAGHEDEIVRDMLAGDDGDGWLRTGGGRDLAEGHADRTGDVRTVDEAGNIGEREEGDDEEEEEIPDMEDEDDDEEAIIREPAGTSSTTQPIRTYNLYITYSNFYRTPRLYLSGYLSPSEPLPPHLMMEDIVGDYKDKTVTLEDFPWFDGGVKMATVHPCRHASVMKTLLDRADAALKIRRDKLKQAHSPAEASRISAERGLEGLVDETRGLSLGEQQQQGGGGSGGDEWEVLQHDEEDQVAIRVDQYLVVFLKFIASVTPGIEHDFTMGV | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of atg8. The atg12-atg5 conjugate plays a role of an E3 and promotes the transfer of atg8 from atg3 to phosphatidylethanolamine (PE). This step is required for the membrane association of atg8. The formation of the atg8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Monomer. Interacts with atg8 through an intermediate thioester bond through the C-terminal Gly of atg8. Also interacts with the 40 amino acid C-terminal region of the E1-like atg7 enzyme. Interacts also with the atg12-atg5 conjugate. The N-terminal region is involved in phosphatidylethanolamine-binding and is required for atg8-PE conjugation. The flexible region (FR) is required for atg7-binding. The handle region (HR) contains the atg8 interaction motif (AIM) and mediates binding to atg8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Belongs to the ATG3 family. |
Q4WUE5 | MNILHSTLSTWRDRLAPVSRTSTFRTTGQITPEEFVLAGDYLVYKFPTWSWADASSPAKRVSYLPPGKQFLVTRGVPCHRRLNENFAGDAGHEDEIVRDMLSGADADDDDGWLRTGGGRDLAEKQAERIKDVRTVDESGNMGEQEDDEEDIPDMEDDDDDEEAIIREPAGKSTTQPTRTYNLYITYSNFYRTPRLYLSGYLSPSEPLPPHLMMEDIVGDYKDKTVTLEDFPWFDGGVKMASVHPCRHASVMKTLLDRADAALKIRRDKLKQAHSADQANRINSERGLEGLVDETRGLSLNEQQGHAAGGDEWEVLQHDEEDQVAIRVDQYLVVFLKFIASVTPGIEHDFTMGV | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of atg8. The atg12-atg5 conjugate plays a role of an E3 and promotes the transfer of atg8 from atg3 to phosphatidylethanolamine (PE). This step is required for the membrane association of atg8. The formation of the atg8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Monomer. Interacts with atg8 through an intermediate thioester bond through the C-terminal Gly of atg8. Also interacts with the 40 amino acid C-terminal region of the E1-like atg7 enzyme. Interacts also with the atg12-atg5 conjugate. The flexible region (FR) is required for atg7-binding. The handle region (HR) contains the atg8 interaction motif (AIM) and mediates binding to atg8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Belongs to the ATG3 family. |
Q2U7R4 | MNILHSTLSTWRDRLAPVSRTSTFRNTGQITPEEFVLAGDYLVYKFPSWSWADASNPAKRVSYLPPGKQFLVTRGVPCHRRLNDNFAGDAGHDDELVRDMLSGGTGGVDDDGWLRTGGGQDSADRQENRIKDVRTVDESGNMGEREEEEDEIPDMEDEDDDEEAIIRDPASGTTQPTRTYNLYITYSNFYRTPRLYMSGYLSPSEPLPPHLMMEDVVGDYKDKTVTLEDFPWYDGNVKMASVHPCRHASVMKTLLDRADAALKLRREKLKQAQSDPSKAPSVGESGLEGLVDDIKALSLSDQQQHGSDKSGGDEWEVLQHDEEEQVAIRVDQYLVVFLKFIASVTPGIEHDFTMGV | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of atg8. The atg12-atg5 conjugate plays a role of an E3 and promotes the transfer of atg8 from atg3 to phosphatidylethanolamine (PE). This step is required for the membrane association of atg8. The formation of the atg8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Monomer. Interacts with atg8 through an intermediate thioester bond through the C-terminal Gly of atg8. Also interacts with the 40 amino acid C-terminal region of the E1-like atg7 enzyme. Interacts also with the atg12-atg5 conjugate. The N-terminal region is involved in phosphatidylethanolamine-binding and is required for atg8-PE conjugation. The flexible region (FR) is required for atg7-binding. The handle region (HR) contains the atg8 interaction motif (AIM) and mediates binding to atg8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Belongs to the ATG3 family. |
M7UQV4 | MNFLHSTLDRLREFTPVSNTSTFRTNGQITPEEFVAAGDYLVFKFPTWSWADASPTSKRANYLPAGKQFLVTRGVPCHRRLDDDFAGDAGHDETVVRDGEDFRGDGPHSPGDDEDGWLRTGGLAASQEARVRDVRTVDESGEMGEREDDEDDIPDMEDDDDDDEAIIRDPKADNASSSRRTYTIYIAYTPYYRTPRLYLSGYLSSSQPLPPHLMMEDIVGDYKDKTVTLEDFPYFSNNIKMASIHPCKHASVMKTLLDRADAALKLRREKQRQGKAVPGSKDTGMEGLVDDFEKTKIGDKKAVLEGLKAGGNGNDEWEVLQHDQDFANEEEEVAIRVDQYLVVFLKFMASVTPGIEHDFTMGV | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy (PubMed:29417220). Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (By similarity). Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of atg8. The atg12-atg5 conjugate plays a role of an E3 and promotes the transfer of atg8 from atg3 to phosphatidylethanolamine (PE) (By similarity). This step is required for the membrane association of atg8. The formation of the atg8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt) (By similarity). The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Required for normal mycelial growth and conidiogenesis, and regulates sclerotial formation (PubMed:29417220). Plays an essential role in pathogenesis (PubMed:29417220). Monomer (By similarity). Interacts with atg8 through an intermediate thioester bond through the C-terminal Gly of atg8 (By similarity). Interacts with the C-terminal region of the E1-like atg7 enzyme (PubMed:29417220). Interacts also with the atg12-atg5 conjugate (By similarity). The N-terminal region is involved in phosphatidylethanolamine-binding and is required for atg8-PE conjugation (By similarity). The flexible region (FR) is required for atg7-binding (By similarity). The handle region (HR) contains the atg8 interaction motif (AIM) and mediates binding to atg8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Blocks the autophagic process (PubMed:29417220). Leads to fewer aerial hyphae and slower mycelial growth rate and fails to produce any conidia (PubMed:29417220). Reduces also the production of sclerotia in cold environment (PubMed:29417220). Fails to infect wounded cucumber leaves and shows only slight virulence on wounded tomato and grape fruits (PubMed:29417220). Belongs to the ATG3 family. |
G2XNY3 | MNFLHSTLDRLREFTPVSNTSTFRTNGQITPEEFVAAGDYLVFKFPTWSWADASPTSKRANYLPAGKQFLVTRGVPCHRRLDDDFAGDAGHDETVVRDGEDFRGDGPHSPGDDEDGWLRTGGLAASQEARVRDVRTVDESGEMGEREDDEDDIPDMEDDDDDDEAIIRDPKADNASSSRRTYTIYIAYTPYYRTPRLYLSGYLSSSQPLPPHLMMEDIVGDYKDKTVTLEDFPYFSNNIKMASIHPCKHASVMKTLLDRADAALKLRREKQRQGKAVPGSKDTGMEGLVDDFEKTKIGDKKAVLEGLKAGGNGNDEWEVLQHDQDFANEEEEVAIRVDQYLVVFLKFMASVTPGIEHDFTMGV | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy (PubMed:29417220). Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (By similarity). Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of atg8. The atg12-atg5 conjugate plays a role of an E3 and promotes the transfer of atg8 from atg3 to phosphatidylethanolamine (PE) (By similarity). This step is required for the membrane association of atg8. The formation of the atg8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt) (By similarity). The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Required for normal mycelial growth and conidiogenesis, and regulates sclerotial formation (PubMed:29417220). Plays an essential role in pathogenesis (PubMed:29417220). Monomer (By similarity). Interacts with atg8 through an intermediate thioester bond through the C-terminal Gly of atg8 (By similarity). Interacts with the C-terminal region of the E1-like atg7 enzyme (PubMed:29417220). Interacts also with the atg12-atg5 conjugate (By similarity). The N-terminal region is involved in phosphatidylethanolamine-binding and is required for atg8-PE conjugation (By similarity). The flexible region (FR) is required for atg7-binding (By similarity). The handle region (HR) contains the atg8 interaction motif (AIM) and mediates binding to atg8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Blocks the autophagic process (PubMed:29417220). Leads to fewer aerial hyphae and slower mycelial growth rate and fails to produce any conidia (PubMed:29417220). Reduces also the production of sclerotia in cold environment (PubMed:29417220). Fails to infect wounded cucumber leaves and shows only slight virulence on wounded tomato and grape fruits (PubMed:29417220). Belongs to the ATG3 family. |
A6S8P6 | MNFLHSTLDRLREFTPVSNTSTFRTNGQITPEEFVAAGDYLVFKFPTWSWADASPTSKRANYLPAGKQFLVTRGVPCHRRLDDDFAGDAGHDETVVRDGEDFRGDGPHSPGDDEDGWLRTGGLAASQEARVRDVRTVDESGEMGEREDDEDDIPDMEDDDDDDEAIIRDPKADNASSTPRLYLSGYLSSSQPLPPHLMMEDIVGDYKDKTVTLEDFPYFSNNIKMASIHPCKHASVMKTLLDRADAALKLRREKQRQGKAVPGSKDTGMEGLVDDFEKTKIGDKKAVLEGLKAGGNGNDEWEVLQHDQDFANEEEEVAIRVDQYLVVFLKFMASVTPGIEHDFTMGV | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of atg8. The atg12-atg5 conjugate plays a role of an E3 and promotes the transfer of atg8 from atg3 to phosphatidylethanolamine (PE). This step is required for the membrane association of atg8. The formation of the atg8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Monomer. Interacts with atg8 through an intermediate thioester bond through the C-terminal Gly of atg8. Also interacts with the 40 amino acid C-terminal region of the E1-like atg7 enzyme. Interacts also with the atg12-atg5 conjugate. The N-terminal region is involved in phosphatidylethanolamine-binding and is required for atg8-PE conjugation. The flexible region (FR) is required for atg7-binding. The handle region (HR) contains the atg8 interaction motif (AIM) and mediates binding to atg8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Belongs to the ATG3 family. |
Q0VCL3 | MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPSGKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGIAGITEAVKEITLESKDSIKLQDCSALCEEEEEEDEGEAADMEEYEESGLLETDEATLDTRKIVEACKAKTDAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM | E2-like enzyme involved in autophagy and mitochondrial homeostasis. Catalyzes the conjugation of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to phosphatidylethanolamine (PE). PE-conjugation to ATG8-like proteins is essential for autophagy. Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway (By similarity). Interacts with ATG7 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5. Interacts with FNBP1L (By similarity). Conjugated to ATG12 at Lys-243. ATG12-conjugation plays a role in regulation of mitochondrial homeostasis and cell death, while it is not involved in PE-conjugation to ATG8-like proteins and autophagy (By similarity). Belongs to the ATG3 family. |
Q5ABF0 | MSLRSKLSSLREYLTPINHNSNFVTTGEISPEEFVKAGDYLVYKFPTWQWGNDCPKNLQKSFLPPDKQYLVTRHVPSYQRASNYLTGEDKKGANPEEDDEEEEEEDEEGWVKSKKIHKVIDDTHDSQINKGEEINDIDDFIDENAEEQEHDQIGDHELDDDEFDDLDIINDSKNNKLRRFDLYITYSTSYRVPKLYLVGFDSNGIPLLPQQMFEDINSDYKDKTATIENLPVAHNTTSVSIHPCKHSSVMKVLMKHSKLNKKNLQQKDESLSDDLSKLSVNEKKTQDEHSQINNDDKEEEEEGIRVDHYLIIFLKFIASVTPGIEYDYTMDAL | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Monomer. Interacts with ATG8 through an intermediate thioester bond through the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5 conjugate. The N-terminal region is involved in phosphatidylethanolamine-binding and is required for ATG8-PE conjugation. The flexible region (FR) is required for ATG7-binding. The handle region (HR) contains the ATG8 interaction motif (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Belongs to the ATG3 family. |
Q6FQJ2 | MIRSALSNWREYLTPVSHKSTFLTTGQITPEEFVQAGDYLCHMFPTWKWNDMADDNKYRDFLPKDKQFLVIRKVPCSERAQAVVTMDEIENGTSTDAFSAADDEDNDDDSIEIIPVSKSSSGADNDVNDIDELMEEMELEEDDDIVANKTNEMLRYYDLFITYSTSYRVPKMYIVGFNGNGTPLTPKEMFEDITPDYRKKTATIEKLPFYKRNVPSVSIHPCKHANVMKVLLDKISVVKERQREEEMQKNAEVGAPKSAGSDDGDNENWEDLQQDIDDSLRVDLYLVVFLKFITSVTPTIQHDYTMEGW | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Monomer. Interacts with ATG8 through an intermediate thioester bond through the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5 conjugate. The N-terminal region is involved in phosphatidylethanolamine-binding and is required for ATG8-PE conjugation. The flexible region (FR) is required for ATG7-binding. The handle region (HR) contains the ATG8 interaction motif (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Belongs to the ATG3 family. |
Q2H427 | MNIIYSTVNSLRDRYTPASHTSTFRNTGEITPEEFVAAGDYLVFKFPSWTWSDAETPAKRVAHLPPEKQYLVTRNVPCHRRLNDDFAGDAGHEEAVVEGGKNSGDDGWLRTGGLASSQPLKARDVRTVDDAGNVADRGAIDDEDDIPDMEEEEDDEAIIQDGSHGKHSGSRTYSLYITYSPWYKTPRMYMLGYQPNGQALIPHLMMEDIVGDYKDKTVTLEDFPFFATSVKTASIHPCKHAPVMKTLLDRADAALKLRKERQKAGLEVGSNQGLEGLEAQVVKLAVSGTGTDVANDANDEWEEVQHDAADQDVAIRVDQYLFIASVTPGIEHDFTMGV | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Monomer. Interacts with ATG8 through an intermediate thioester bond through the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5 conjugate. The N-terminal region is involved in phosphatidylethanolamine-binding and is required for ATG8-PE conjugation. The flexible region (FR) is required for ATG7-binding. The handle region (HR) contains the ATG8 interaction motif (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Belongs to the ATG3 family. |
Q5K9X6 | MNNPLLAIQSQYWAVRDYLSPVLRESKFKEHGRITPEEFVAAGDFLTFKFPVWQWEKGESSRARDFLPPDKQYLVTRNVPCLRRATAVDYTNADEDAEKLLSFLDDAEEAPGPDDDWVATHINRSPPHRPTDMDEIPDIPDSPTTAPTREMAGLNVSSGGKLEEDEIPDIDDIPDMDEEGLEDLEDDAAVRIVHPSEAEVNSTAGKNLLQVRTYDCIISYDKHYQTPRFWLFGYDEHKNPLTPAQVFQDVPADHAFKTMTMESFPHSGAQLASVHPCKHASVMKKFIDRMEAAQGPAPTAEPETISSTSGTSGSAGGKEEKEKKKKWGLGSMVRKVTGGSVPKVEKDKDEVVTGVPVDFYLVIFLKFIASIVPTIEVDSTTSTAL | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Monomer. Interacts with ATG8 through an intermediate thioester bond through the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5 conjugate. The N-terminal region is involved in phosphatidylethanolamine-binding and is required for ATG8-PE conjugation. The flexible region (FR) is required for ATG7-binding. The handle region (HR) contains the ATG8 interaction motif (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Belongs to the ATG3 family. |
Q6PFS7 | MQNVINSVKGTALGVAEFLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWKWASGEEAKVKPYLPNDKQFLLTRNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTFHNSGVTGVTEAVREISLDNKDNMNMNVKTGACGNSGDDDDDEEGEAADMEEYEESGLLETDDATLDTSKMADLSKTKAEAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEDRQPLTVDQMYEDISQDHVKKTVTIENHPNLPPPAMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of atg8-like proteins (gabarap, gabarapl1, gabarapl2 or map1lc3a). The atg12-atg5 conjugate plays a role of an E3 and promotes the transfer of atg8-like proteins from atg3 to phosphatidylethanolamine (PE). This step is required for the membrane association of atg8-like proteins. The formation of the atg8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of atg12 to itself, atg12 conjugation to atg3 playing a role in mitochondrial homeostasis but not in autophagy. atg7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with atg3 (By similarity). Interacts with atg7 and atg12. The complex composed of atg3 and atg7 plays a role in the conjugation of atg12 to atg5. Conjugated to atg12 at Lys-246. ATG12-conjugation plays a role in regulation of mitochondrial homeostasis and cell death, while it is not involved in PE-conjugation to ATG8-like proteins and autophagy (By similarity). Belongs to the ATG3 family. |
Q6BSC4 | MLRSKLSSLREYLTPIRHTSDFTTTGEISPEEFVEAGDYLVYKFPTWQWSSAPDKLKKDFLPPDKQYLITKHVSSYQRAVTYLGIKSDLDEDEEELEDGWVKSHKINNDPSRLKTDASGENSGGNTNDNDDTNEINDIDELIDENAEEQSSEDENDFEELVETNANSNLRKYDLYITYSTSYRVPKMYLVGFNSNGIPLLPKQMFEDISGDYRDKTATIETLPVSYNTMSVSIHPCKHSSVMKVLMAHAAASKKRENPADLTDLAEQTGSLNLKDKVPGRDFGEDVDIEENVPGIRVDQYLIIFLKFIASVTPGIEYDYTMDAL | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Monomer. Interacts with ATG8 through an intermediate thioester bond through the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5 conjugate. The N-terminal region is involved in phosphatidylethanolamine-binding and is required for ATG8-PE conjugation. The flexible region (FR) is required for ATG7-binding. The handle region (HR) contains the ATG8 interaction motif (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-vacuole targeting pathway (By similarity). Belongs to the ATG3 family. |
G4NCJ6 | MRSKFKDEHPFEKRKAEAERIRQKYTDRIPVICEKVEKSDIATIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFVQDTLPPTAALMSSIYELHKDEDGFLYITYSGENTFGDLFEEVE | Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Interacts with ATG4, (PubMed:19923912). Interacts with acetylated ATG3 (PubMed:30776962). The C-terminal 7 residues are removed by ATG4 to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
A1D3N4 | MRSKFKDEHPFEKRKAEAERIRQKYADRIPVICEKVEKSDIATIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFVDEVLPPTAALMSSIYEEHKDEDGFLYITYSGENTFGDC | Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. The C-terminal 2 residues are removed by atg4 to expose Gly-116 at the C-terminus. The c-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
Q1K4Y7 | MRSKFKDEHPFEKRKAEAERIRQKYSDRIPVICEKVEKSDIATIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFVDEVLPPTAALMSSIYEEHKDEDGFLYITYSGENTFGDFETA | Ubiquitin-like modifier involved in autophagosomes formation. With cpr-1/atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The apg-6/atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. The C-terminal 5 residues are removed to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
B6GZ65 | MRSKFKDEHPFEKRKAEAERIRQKYADRIPVICEKVEKSDIATIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFVDEVLPPTAALMSSIYEEHKDEDGFLYITYSGENTFGDL | Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. The C-terminal 2 residues are removed by atg4 to expose Gly-116 at the C-terminus. The c-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
Q0V3Y9 | MRSKFKDEHPFEKRKAEAERIRQKYNDRIPVICEKVEKSDIATIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFVDEVLPPTAALMSSIYEEHKDEDGFLYITYSGENTFGEAI | Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. The C-terminal 3 residues are removed by ATG4 to expose Gly-116 at the C-terminus. The c-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
Q8H715 | MSSFKKEHPFEKRQAEAQRIRSKYPDRIPVICEKADRSDIPDIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFINNVLPPTAALMSNIYEEQKDVDGFLYITYSGENTFGQ | Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. The C-terminal Gln residue is removed to expose Gly-115 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
Q5QFG1 | MRSQFKDEHPFERRKAEASRIRGKFLDRIPVICEKVEESDIPEIDKRKYLVPSDLTVGQFVYVIRKRIQLPSEKAIFIFVNDILPPTASLMSTIYEQYKDEDGFLYILYSGENTFGQLEGVEETL | Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Expression is increased after the shift of cells from glucose to methanol. The last C-terminal 9 residues are removed to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitine. Belongs to the ATG8 family. |
Q8NJJ4 | MRSQFKDEHPFEKRKAEAMRIRYKFADRIPVICEKVEKSDIPEVDKRKYLVPCDLTVGQFVYVIRKRIKIPSEKAIFIFIDDILPPTAALMSKVYEEHKDEDGFLYVLYSGENTFGDIPGVEEIE | Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Interacts with ATG4 (By similarity). Interacts with ATG30 and ATG32 (PubMed:23559066). The last C-terminal 9 residues are removed to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitine. Belongs to the ATG8 family. |
A3GFU8 | MRSQFKDEHPFEKRQAEATRIAQRFKDRVPVICEKVENSDIPEIDKRKYLVPVDLSVGQFVYVIRKRIKLPSEKAIFIFVNDILPPTAALISTIYEEHKDEDGFLYVLYSGENTFGQKKPLDLSTIDWSDLSDLDLAQK | Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. The C-terminal 23 residues are removed by ATG4 to expose Gly-116 at the C-terminus. The c-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
Q8J282 | MRSKFKDEHPFEKRKAEAERIRQKYADRIPVICEKVEKSDIATIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFVDEVLPPTAALMSSIYEEHKDEDGFLYITYSGENTFGGFETA | Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Punctate structures under nutrient-rich conditions and large punctate perivacuolar structures and vacuolar lumen under nitrogen starvation conditions or heterokaryon incompatibility conditions. Expression is positively regulated by idi-4. The C-terminal 5 residues may be removed to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Increases the rate of incompatibility cell death. Belongs to the ATG8 family. |
O94272 | MRSQFKDDFSFEKRKTESQRIREKYPDRIPVICEKVDKSDIAAIDKKKYLVPSDLTVGQFVYVIRKRIKLSPEKAIFIFIDEILPPTAALMSTIYEEHKSEDGFLYITYSGENTFGTVFPF | Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Contributes to the maintenance of cell viability under conditions of nitrogen-depletion. Plays a role in meiosis and sporulation and contributes to oxidative stress resistance (PubMed:17295836, PubMed:19778961, PubMed:20070859). Interacts with atg43 (via N-terminal atg8 interacting motif); the interaction is direct. The C-terminal 5 residues are removed to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
A7E8H4 | MRSKFKDEHPFEKRKAEAERIRQKYSDRIPVICEKVEKSDIATIDKKKYLVPSDLTVGQFVYVIRKRIKLSPEKAIFIFVDEVLPPTAALMSSIYEEHKDEDGFLYISYSGENTFGEALEEAN | Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. The C-terminal 7 residues are removed by atg4 to expose Gly-116 at the C-terminus. The c-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
A0A0D1DQB5 | MRSAFKNEHSFEKRKAEAERIRQKYPDRIPVICEKADRTDIPTIDKKKYLVPSDLTVGQFVYVIRKRIKLAPEKAIFIFVDEVLPATAALMSAIYEEHKDEDGFLYVSYSGENTFGQL | Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Required for selective autophagic degradation of the mitochondria (mitophagy) which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Required for wild-type budding of haploid sporidia and for complete symptom development during pathogenic growth such as gall formation and teliospore production in ears of mature maize (PubMed:20618705, PubMed:22843561). Conjugation to phosphatidylethanolamine (PE) leads to homodimerization. Interacts with ATG1, ATG3, ATG4, ATG7, ATG12, ATG32, ATG34 and the C-terminal 10 residues domain of ATG19. Interacts also with the endoplasmic reticulum to Golgi v-SNARE protein BET1 and the vacuolar v-SNARE protein NYV1. Interacts with the UBX domain-containing protein SHP1. Transcripts accumulate during carbon stress conditions. The C-terminal 2 residues are removed by ATG4 to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Prevents vacuolar accumulation of autophagosomes and affects survival during carbon starvation. Belongs to the ATG8 family. |
A7TDU7 | MKSSFKSEYPFEKRKTESERITEKFQNRIPVICEKAEKSDIPEIDKRKYLVPSDLTVGQFVYVIRKRIMLPPEKAIFIFVNDTLPPTAALMSAVYQEHKDKDGFLYVTYSGENTFGSL | Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. The C-terminal 2 residues are removed by ATG4 to expose Gly-116 at the C-terminus. The c-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
Q6C794 | MRSKFKDEHPFEKRRAEAERIRKKYDDRVPVICEKVEKSDIPVIDKKKYLVPADLTVGQFVYVIRKRIKLSSERAIFIFVDDVLPPTAALMSSIYEEHKDEDGFLYVTYSGENTFGDLEQYRLE | Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. The C-terminal 8 residues are removed to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. Belongs to the ATG8 family. |
A6ZKM4 | MKSTFKSEYPFEKRKAESERIADRFKNRIPVICEKAEKSDIPEIDKRKYLVPADLTVGQFVYVIRKRIMLPPEKAIFIFVNDTLPPTAALMSAIYQEHKDKDGFLYVTYSGENTFGR | Ubiquitin-like modifier involved in cytoplasm to vacuole transport (Cvt) vesicles and autophagosomes formation. With ATG4, mediates the delivery of the vesicles and autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Moreover not only conjugation, but also subsequent ATG8-PE deconjugation is an important step required to facilitate multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. Also plays a role in regulation of filamentous growth. Conjugation to phosphatidylethanolamine (PE) leads to homodimerization. Interacts with ATG1, ATG3, ATG4, ATG7, ATG12, ATG32, ATG34 and the C-terminal 10 residues domain of ATG19. Interacts also with the endoplasmic reticulum to Golgi v-SNARE protein BET1 and the vacuolar v-SNARE protein NYV1. Interacts with the UBX domain-containing protein SHP1. Membrane-associated through a lipid anchor. This association needs the 2 ubiquitin-like systems required for cytoplasm to vacuole transport and autophagy. ATG18 and ATG21 facilitate the recruitment of ATG8-PE to the site of autophagosome formation and protect it from premature cleavage by ATG4. Localizes to both the isolation membrane (IM) and the vacuole-isolation membrane contact site (VICS) during IM expansion. The IM is a membrane sac generated from the pre-autophagosomal structure that ultimately expands to become a mature autophagosome. Upon starvation, is also recruited to into unique membrane structures near SEC13-containing ER exit sites which lack components of the Golgi apparatus and the endosomes, and which were called a compartments for unconventional protein secretion (CUPS). The C-terminal Arg-117 residue of ATG8 is removed by ATG4 to expose Gly-116 at the C-terminus. This Gly-116 forms then a thioester bond with the 'Cys-507' of ATG7 (E1-like activating enzyme) before being transferred to the 'Cys-234' of ATG3 (the specific E2 conjugating enzyme), in order to be finally amidated with phosphatidylethanolamine. This lipid modification anchors ATG8 to membranes and can be reversed by ATG4, releasing soluble ATG8. Belongs to the ATG8 family. |
D6VPS5 | MKSTFKSEYPFEKRKAESERIADRFKNRIPVICEKAEKSDIPEIDKRKYLVPADLTVGQFVYVIRKRIMLPPEKAIFIFVNDTLPPTAALMSAIYQEHKDKDGFLYVTYSGENTFGR | Ubiquitin-like modifier involved in cytoplasm to vacuole transport (Cvt) vesicles and autophagosomes formation. With ATG4, mediates the delivery of the vesicles and autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Moreover not only conjugation, but also subsequent ATG8-PE deconjugation is an important step required to facilitate multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. Also plays a role in regulation of filamentous growth. Conjugation to phosphatidylethanolamine (PE) leads to homodimerization. Interacts with ATG1, ATG3, ATG4, ATG7, ATG12, ATG32, ATG34 and the C-terminal 10 residues domain of ATG19. Interacts also with the endoplasmic reticulum to Golgi v-SNARE protein BET1 and the vacuolar v-SNARE protein NYV1. Interacts with the UBX domain-containing protein SHP1. Membrane-associated through a lipid anchor. This association needs the 2 ubiquitin-like systems required for cytoplasm to vacuole transport and autophagy. ATG18 and ATG21 facilitate the recruitment of ATG8-PE to the site of autophagosome formation and protect it from premature cleavage by ATG4. Localizes to both the isolation membrane (IM) and the vacuole-isolation membrane contact site (VICS) during IM expansion. The IM is a membrane sac generated from the pre-autophagosomal structure that ultimately expands to become a mature autophagosome. Upon starvation, is also recruited to into unique membrane structures near SEC13-containing ER exit sites which lack components of the Golgi apparatus and the endosomes, and which were called a compartments for unconventional protein secretion (CUPS). Up-regulated upon starvation conditions. Expression is under the control of UME6 which acts along with a histone deacetylase complex including SIN3 and RPD3 to regulate negatively ATG8 levels and subsequent autophagic activity. The C-terminal Arg-117 residue of ATG8 is removed by ATG4 to expose Gly-116 at the C-terminus (PubMed:11038174, PubMed:11149920, PubMed:16680092). This Gly-116 forms then a thioester bond with the 'Cys-507' of ATG7 (E1-like activating enzyme) before being transferred to the 'Cys-234' of ATG3 (the specific E2 conjugating enzyme), in order to be finally amidated with phosphatidylethanolamine (PubMed:11100732, PubMed:15277523, PubMed:20615880, PubMed:17632063, PubMed:17699586, PubMed:18725539, PubMed:19285500, PubMed:23064152, PubMed:22539722, PubMed:28330855, PubMed:20428927). This lipid modification anchors ATG8 to membranes and can be reversed by ATG4, releasing soluble ATG8 (PubMed:22240591, PubMed:22622160, PubMed:22652539, PubMed:28330855). Present with 2010 molecules/cell in log phase SD medium. Belongs to the ATG8 family. |
A5D7D0 | MAQFDTEYQRLEASYSDSPPGEEDLLVHVPEGSKSPWHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFANKMVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWVHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEVVFFTRGLKYNFELILFWGPGSLFLNEWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNRGYKPASKYMNCFLSPLLTLLAKNCAFFAGSILAVLIALTIYDEDVLAVEHVLTTVTLLGVTVTVCRSFIPDQHMVFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQHGHPQWLSGGQTEASVYQQAEDGKTELSLMHFAITNPGWQPPRESTAFLGFLKEQVQRDGAAAGLAQGGLLPENALFTSIQSLQSESEPLSLIANVVAGSSCRGPPLPRDLQGSRHRAEVASALRSFSPLQPGQAPTGRAPSTMTGSGVDARTASSGSSVWEGQLQSLVLSEYASTEMSLHALYMHQLHKQQAQAEPERHVWHRRESDESGESAPEEGGEGARATQPIPRSASYPCAAPRPGAPETTALQGGFQRRYGGITDPGTVPRAPSHFSRLPLGGWAEDGQSASRHPEPVPEEGSEDELPPQVHKV | Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 (By similarity). In addition to autophagy, also plays a role in necrotic cell death (By similarity). a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) Homotrimer; forms a homotrimer with a central pore that forms a path between the two membrane leaflets. Interacts (via cytoplasmic its C-terminus) with ATG2A. Interacts with SUPT20H. Interacts (via the tyrosine-based sorting signal motif) with AP4M1; promoting association with the AP-4 complex. Interacts with ARFIP1 and ARFIP2. Interacts with PI4K2A and PI4KB. Interacts with ATG4A; the interaction is direct and promotes ATG9A trafficking. Mainly localizes to the trans-Golgi network (TGN) and the endosomal system; cycles between them though vesicle trafficking. Export from the TGN to promote formation of autophagosomes is mediated by the AP-4 complex. Under amino acid starvation or rapamycin treatment, redistributes to preautophagosomal structure/phagophore assembly site (PAS). The starvation-induced redistribution depends on ULK1, ATG13, as well as SH3GLB1. Upon autophagy induction, a small portion transiently localizes to the autophagic membranes. Recruited to damaged mitochondria during mitophagy in a RIMOC1-dependent manner. Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9A-containing vesicles, thereby enabling growth into autophagosomes. The tyrosine-based sorting signal motif, also named YXX-psi motif, promotes interaction with the AP-4 complex. Belongs to the ATG9 family. |
Q9HAG7 | MAQFDTEYQRLEASYSDSPPGEEDLLVHVAEGSKSPWHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFANKMVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEAVFFTRGLKYNFELILFWGPGSLFLNEWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNRGYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVLAVEHVLTTVTLLGVTVTVCRSFIPDQHMVFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQHGHPQWLSAGQTEASVYQQAEDGKTELSLMHFAITNPGWQPPRESTAFLGFLKEQVQRDGAAASLAQGGLLPENALFTSIQSLQSESEPLSLIANVVAGSSCRGPPLPRDLQGSRHRAEVASALRSFSPLQPGQAPTGRAHSTMTGSGVDARTASSGSSVWEGQLQSLVLSEYASTEMSLHALYMHQLHKQQAQAEPERHVWHRRESDESGESAPDEGGEGARAPQSIPRSASYPCAAPRPGAPETTALHGGFQRRYGGITDPGTVPRVPSHFSRLPLGGWAEDGQSASRHPEPVPEEGSEDELPPQVHKV | Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion (PubMed:22456507, PubMed:27510922, PubMed:29437695, PubMed:32513819, PubMed:33468622, PubMed:33850023, PubMed:32610138, PubMed:33106659). Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (PubMed:16940348, PubMed:22456507, PubMed:33106659). Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (PubMed:33106659). Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 (PubMed:30917996). In addition to autophagy, also plays a role in necrotic cell death (By similarity). a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) Homotrimer; forms a homotrimer with a central pore that forms a path between the two membrane leaflets (PubMed:32610138, PubMed:33106659). Interacts (via cytoplasmic its C-terminus) with ATG2A (PubMed:32610138, PubMed:33106659). Interacts with SUPT20H (PubMed:19893488). Interacts (via the tyrosine-based sorting signal motif) with AP4M1; promoting association with the AP-4 complex (PubMed:29180427). Interacts with ARFIP1 and ARFIP2 (PubMed:30917996). Interacts with PI4K2A and PI4KB (PubMed:30917996). Interacts with ATG4A; the interaction is direct and promotes ATG9A trafficking (PubMed:33773106). Mainly localizes to the trans-Golgi network (TGN) and the endosomal system; cycles between them though vesicle trafficking (PubMed:27316455, PubMed:27663665). Export from the TGN to promote formation of autophagosomes is mediated by the AP-4 complex (PubMed:29180427, PubMed:30262884). Under amino acid starvation or rapamycin treatment, redistributes to preautophagosomal structure/phagophore assembly site (PAS) (PubMed:16940348). The starvation-induced redistribution depends on ULK1, ATG13, as well as SH3GLB1 (PubMed:16940348). Upon autophagy induction, a small portion transiently localizes to the autophagic membranes (PubMed:22456507). Recruited to damaged mitochondria during mitophagy in a RIMOC1-dependent manner (PubMed:34432599). Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer (PubMed:32610138, PubMed:33106659). Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9A-containing vesicles, thereby enabling growth into autophagosomes (PubMed:33106659). The tyrosine-based sorting signal motif, also named YXX-psi motif, promotes interaction with the AP-4 complex. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the ATG9 family. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. |
Q3ZAQ4 | MAQFDTEYQRLEASYSDSPPGEEDLLVHVAEGSKSPWHHIENLDLFFSRVYNLHQKNGFTCMLIGEMFELMQFLFVVAFTTFLVSCVDYDILFANKMVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEVVFFTRGLKYNFELILFWGPGSLFLNEWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNRGYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVLAVEHVLTTVTLLGVTVTVCRSFIPDQHMVFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQHGHPQWLSGGQTEASVYQQAEDGKTELSLMHFAITNPGWQPPRESTAFLGFLKEQVQRDGAAAGLAQGGLLPENALFTSIQSLQSESEPLSLIANVVAGSSCRGPSLSRDLQGSRHRADVASALRSFSPLQPGAAPQGRVPSTMTGSGVDARTASSGSSVWEGQLQSLVLSEYASTEMSLHALYMHQLHKQQTQAEPERHVWHRRESDESGESAPEEGGEGARAPQPIPRSASYPCATPRPGAPETTALHGGFQRRYGGITDPGTVPRGPSHFSRLPLGGWAEDGQPASRHPEPVPEEGSEDELPPQVHKV | Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion (PubMed:23402761, PubMed:27587839). Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (By similarity). Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (By similarity). Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 (By similarity). In addition to autophagy, also plays a role in necrotic cell death (PubMed:27811852). a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) Homotrimer; forms a homotrimer with a central pore that forms a path between the two membrane leaflets (By similarity). Interacts (via cytoplasmic its C-terminus) with ATG2A (By similarity). Interacts with SUPT20H (By similarity). Interacts (via the tyrosine-based sorting signal motif) with AP4M1; promoting association with the AP-4 complex (By similarity). Interacts with ARFIP1 and ARFIP2 (By similarity). Interacts with ATG4A; the interaction is direct and promotes ATG9A trafficking (By similarity). Mainly localizes to the trans-Golgi network (TGN) and the endosomal system; cycles between them though vesicle trafficking (PubMed:27587839). Export from the TGN to promote formation of autophagosomes is mediated by the AP-4 complex. Under amino acid starvation or rapamycin treatment, redistributes to preautophagosomal structure/phagophore assembly site (PAS). The starvation-induced redistribution depends on ULK1, ATG13, as well as SH3GLB1. Upon autophagy induction, a portion of transiently localizes to the autophagic membranes (By similarity). Recruited to damaged mitochondria during mitophagy in a RIMOC1-dependent manner (By similarity). Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9A-containing vesicles, thereby enabling growth into autophagosomes. The tyrosine-based sorting signal motif, also named YXX-psi motif, promotes interaction with the AP-4 complex. Lethality; mice die within one day after birth caused by impaired autophagy (PubMed:19926846). Mice also show aberrant activation of the innate immune response (PubMed:19926846). Fetal mice display significantly retarded growth (PubMed:26370455). Conditional deletion in brain causes axon-specific degeneration: mice were born normally, but half of them die within one week, and none live beyond 4 weeks of age (PubMed:28513333). Defects are caused by impaired autophagy in neurons, leading to progressive degeneration in the axons and their terminals, but not in neuronal cell bodies (PubMed:28513333). In addition to defects in autophagy, mice also display impaired necrotic cell death during bone morphogenesis: the bone surface is rougher and bones are more porous due to defects in necrotic cell death in bone surface formation (PubMed:27811852). Belongs to the ATG9 family. |
Q2G506 | MPPETATNPKDARHDGWQTLKRFLPYLWPADNAVLRRRVVGAILMVLLGKATTLALPFAYKKAVDAMTLGGGAQPALTVALAFVLAYALGRFSGVLFDNLRNIVFERVGQDATRHLAENVFARLHKLSLRFHLARRTGEVTKVIERGTKSIDTMLYFLLFNIAPTVIELTAVIVIFWLNFGLGLVTATILAVIAYVWTTRTITEWRTHLREKMNRLDGQALARAVDSLLNYETVKYFGAESREEARYASAARAYADAAVKSENSLGLLNIAQALIVNLLMAGAMAWTVYGWSQGKLTVGDLVFVNTYLTQLFRPLDMLGMVYRTIRQGLIDMAEMFRLIDTHIEVADVPNAPALVVNRPSVTFDNVVFGYDRDREILHGLSFEVAAGSRVAIVGPSGAGKSTIARLLFRFYDPWEGRILIDGQDIAHVTQTSLRAALGIVPQDSVLFNDTIGYNIAYGRDGASRAEVDAAAKGAAIADFIARLPQGYDTEVGERGLKLSGGEKQRVAIARTLVKNPPILLFDEATSALDTRTEQDILSTMRAVASHRTTISIAHRLSTIADSDTILVLDQGRLAEQGSHLDLLRRDGLYAEMWARQAAESAEVSEAAE | Mediates the ATP-dependent export of glutathione-conjugated substrates, such as heavy metal-glutathione conjugates. ATP hydrolysis is stimulated by glutathione binding. Protects cells against toxic heavy metal ions, such as silver and mercury ions. May also mediate the transport of glutathione-conjugated aromatic hydrocarbons, such as dinitrobenzene. Homodimer. Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily. |
O13721 | MLERCPWKLISSPRNIPARSFLNSRGTYLVLRKSNILPLQHILRFSNFASKQCFPLRNGNNSASKALWNNKSKEKEPLNTSVKLASDVPDDKNVTGQMIVKDMLQYIWPKGKTNLKVRVVSALALLVAAKILNVQVPFYFKSIIDTMNTTLVQEVGALWSTVGAVVLGYGFARIFSTVFQELRNSVFAIVSQSAIRSVSSNVYQHLLNLDMNFHLSKQTGSITRAMDRGTKGISFILSSMVLHIIPITLEIAMVSGILTYKYGPSFSAIAATTVALYALFTVRTTSWRTVFRRQANAADSKASAAAIESLINYEAVKTFNNESYEMSRYEKHLSAYEKANVKVASSLAFLNSGQAIIFSTALTLMMYMGCRGIVTSNLTVGDLVMINQLVFQLSIPLNFLGSVYREMRQAFTDMEQLFSLKRINIQVKEAPDARDLVLKGGSIQFDNVHFSYNPNRPILNGCSFNIPAGAKVAFVGASGCGKSTILRLLFRFYDTDSGKILIDNQRLDQITLNSLRKAIGVVPQDTPLFNDTILYNIGYGNPKASNDEIVEAAKKAKIHDIIESFPEGYQTKVGERGLMISGGEKQRLAVSRLLLKNPEILFFDEATSALDTNTERALLRNINDLIKGSHKTSVFIAHRLRTIKDCDIIFVLEKGRVVEQGSHEQLMAKNSVYTSMWHSQESPFGESNKSGDA | Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by nfs1 and other mitochondrial proteins (PubMed:16306692). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity). Homodimer. Abnormal mitochondrial function; decreases growth on glycerol (non-fermentable carbon source) (PubMed:16306692). Abnormal endocytosis and vacuole fusion (PubMed:16306692). Sensitive to copper, and dithiothreitol (PubMed:16306692). Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily. |
A0A0D1E8N7 | MRVAIRRLPWQATDARHRTIGLVSTNRLPSRIQPRSISSTSIAALVYHSRNSLRTNIFDIAATPSSRYGSSQRFYQHMAADRDGDHVPKHQAKMLPGSASDKIIAAASPASKSASSPAQKKQPDGDDPLNLNSREKTVKEQRLVDWAIIKKLIQYVWPKGDFGTKQRVVLALALLIGGKLLNVQVPFFFKTIVDRLNDVVNAPLDMSNPNTVWVVAGSAVLGYGLARVGAAAFSELRNAVFANVAQRSIRRVAKSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHIVPTALEISMVCGILSYKCGPSFAAVTAITMAAYAWFTIRTTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMTVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDMETMFNLENVNVAVKEDKNAPPLKVSGGEIRFENVTFGYHPDRPIFRNISFTVPAGYKTAFVGPSGCGKSTIFRLLFRFYEPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDEDVEKAARAAKVDQIVLNLPEGYSTKVGERGLMISGGEKQRLAVARLLLKNPSVLFFDEATSALDSYTETELMRNIHATLLADKKTAIFVAHRLRTISDSDFIIVLQGGGVKEQGTHDQLMDSKGLYWDLWQAQSTVGVGHGAGANEHLQDLERDQNSSTTPM | Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (By similarity). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity). Homodimer. Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily. Truncated N-terminus. |
Q6C6N0 | MWLSLPRSGYGSVATLTSKRVLACLTPLRQFSTSPAVSNANHKNVDNINKSPANDAANNAVEKGDKPTTSPEKLATKAEKSSANSVKAAANALGESNLSNSEQRRLDWIIMKDMLKYIWPKGKTSVKFRVLVAVALLVGAKLLNVQVPFFFKEIIDDMNIEWNSATALGVGITALIFSYGAARFGAVLFGELRNAIFASVAQKAIKEVATNVFRHLLKLDMAFHLSRQTGGITRAIDRGTKGISFVLSSMVFHIIPIALEISLVCGILSYNFGWKYALVTGATMVSYAIFTITTTSWRTKFRRNANRADNEASNVCLDSLINIEAVKSFGNEGYMVDKYQSALTKYEKASIKIATSLAFLNSGQNLIFSSALTAMMYMTCCGVADGSLTVGDLVLVNQLVFQLSVPLNFLGSVYRDLRQSLLDMGSLFSLQKVAGQIQESPNAKPLQLTNGEIRFENVTYGYHPDRPILKNASFVIPGGLKTAIVGPSGSGKSTILKLAFRFYDTQEGRILIDGQDVREVTLASLRSAIGVVPQDTPLFNDSIMNNIRFGRLEADDKEVENAACAAKLDALVRQLPDGWNTNVGERGMMISGGEKQRLAVARVLLKNSPVVFLDEATSALDTNTERQLLANMDQVLGDKTCVAIAHRLRTVADSDKIICLNQGGVEEEGTQAELLLKDGLYKSMWDAQEQVELGEEGIKEAEEKAAKKDV | Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (By similarity). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity). Homodimer. Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily. |
D6W0C8 | MLLLPRCPVIGRIVRSKFRSGLIRNHSPVIFTVSKLSTQRPLLFNSAVNLWNQAQKDITHKKSVEQFSSAPKVKTQVKKTSKAPTLSELKILKDLFRYIWPKGNNKVRIRVLIALGLLISAKILNVQVPFFFKQTIDSMNIAWDDPTVALPAAIGLTILCYGVARFGSVLFGELRNAVFAKVAQNAIRTVSLQTFQHLMKLDLGWHLSRQTGGLTRAMDRGTKGISQVLTAMVFHIIPISFEISVVCGILTYQFGASFAAITFSTMLLYSIFTIKTTAWRTHFRRDANKADNKAASVALDSLINFEAVKYFNNEKYLADKYNGSLMNYRDSQIKVSQSLAFLNSGQNLIFTTALTAMMYMGCTGVIGGNLTVGDLVLINQLVFQLSVPLNFLGSVYRDLKQSLIDMETLFKLRKNEVKIKNAERPLMLPENVPYDITFENVTFGYHPDRKILKNASFTIPAGWKTAIVGSSGSGKSTILKLVFRFYDPESGRILINGRDIKEYDIDALRKVIGVVPQDTPLFNDTIWENVKFGRIDATDEEVITVVEKAQLAPLIKKLPQGFDTIVGERGLMISGGEKQRLAIARVLLKNARIMFFDEATSALDTHTEQALLRTIRDNFTSGSRTSVYIAHRLRTIADADKIIVLDNGRVREEGKHLELLAMPGSLYRELWTIQEDLDHLENELKDQQEL | Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (PubMed:10406803, PubMed:31040179, PubMed:25006243). Hydrolyzes ATP (PubMed:25006243, PubMed:24604199). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (PubMed:24604199, PubMed:25006243, PubMed:31040179). Homodimer. Impairs cytosolic iron-sulfur (Fe-S) cluster assembly and decreases cytosolic tRNA thiolation. Present with 3250 molecules/cell in log phase SD medium. Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily. |
A9JPE4 | MDSVLRYVFLLLAMTSFYMMYISLFNNGFFNLLSHQLATRALPGESDIALLSEYTGLKAFDGILESIVIFFWPISQGHHVGLSLTGLSFSGGMVGIWMIVVVHICRIRSFTRGMVITLIVGIAQQAVGPGIVIPCYFALTSRARPPNKNLHLTGTYSTSNHGLVVSMIMSYIFPLVIMSLPAPAMISPHSKQQVIAAWQGWPVYFVIIMTTHHLFINRGHRKEASARRQVLSVYHFGFACSCLCHMAWLSAFVASKIQSLSQSSNFWYLCPYGVAFPLLNQPAQRLGALEAGLFTFLQWDYCVAAAATMVWSTDRYIQECHRAELEIDKFRLILRLLGWILIDGPSATAVRLIWESEGPSYLQNPN | Aflatrem synethesis protein A; part of the ATM2 gene cluster that mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin with acute neurotoxic effects (PubMed:19801473, PubMed:2867895). Synthesis of geranylgeranyl diphosphate (GGPP) by AtmG (a GGPP synthase) precedes condensation of GGPP with indole 3-glycerol phosphate, followed by epoxidation and cyclization by AtmM (a FAD-dependent monooxygenase) and AtmC (a prenyltransferase) to produce paspaline (PubMed:19801473). AtmB is also essential for paspaline production, but its exact role has not been identified yet (PubMed:19801473). AtmP, a cytochrome P450 monooxygenase, subsequently converts paspaline to 13-desoxypaxilline via PC-M6 by removal of the C-30 methyl group and oxidation at C-10 (PubMed:19801473). AtmQ, a cytochrome P450 monooxygenase, then catalyzes the oxidation of 13-desoxypaxilline, first at C-7 to produce paspalicine and then at C-13 to form paspalinine (PubMed:19801473). Finally, AtmD prenylates paspalinine to form aflatrem (PubMed:19801473). The role of atmA in the aflatrem biosynthesis is still unknown (PubMed:19801473). The onset of expression occurs at 48 h old stationary cultures and the steady-state levels correlates with the onset of aflatrem biosynthesis at 108 h (PubMed:19801473). Belongs to the membrane-bound ascI terpene cyclase family. |
P39168 | MFKEIFTRLIRHLPSRLVHRDPLPGAQQTVNTVVPPSLSAHCLKMAVMPEEELWKTFDTHPEGLNQAEVESAREQHGENKLPAQQPSPWWVHLWVCYRNPFNILLTILGAISYATEDLFAAGVIALMVAISTLLNFIQEARSTKAADALKAMVSNTATVLRVINDKGENGWLEIPIDQLVPGDIIKLAAGDMIPADLRILQARDLFVAQASLTGESLPVEKAATTRQPEHSNPLECDTLCFMGTTVVSGTAQAMVIATGANTWFGQLAGRVSEQESEPNAFQQGISRVSMLLIRFMLVMAPVVLLINGYTKGDWWEAALFALSVAVGLTPEMLPMIVTSTLARGAVKLSKQKVIVKHLDAIQNFGAMDILCTDKTGTLTQDKIVLENHTDISGKTSERVLHSAWLNSHYQTGLKNLLDTAVLEGTDEESARSLASRWQKIDEIPFDFERRRMSVVVAENTEHHQLVCKGALQEILNVCSQVRHNGEIVPLDDIMLRKIKRVTDTLNRQGLRVVAVATKYLPAREGDYQRADESDLILEGYIAFLDPPKETTAPALKALKASGITVKILTGDSELVAAKVCHEVGLDAGEVVIGSDIETLSDDELANLAQRTTLFARLTPMHKERIVTLLKREGHVVGFMGDGINDAPALRAADIGISVDGAVDIAREAADIILLEKSLMVLEEGVIEGRRTFANMLKYIKMTASSNFGNVFSVLVASAFLPFLPMLPLHLLIQNLLYDVSQVAIPFDNVDDEQIQKPQRWNPADLGRFMIFFGPISSIFDILTFCLMWWVFHANTPETQTLFQSGWFVVGLLSQTLIVHMIRTRRVPFIQSCASWPLMIMTVIVMIVGIALPFSPLASYLQLQALPLSYFPWLVAILAGYMTLTQLVKGFYSRRYGWQ | Mediates magnesium influx to the cytosol. ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate By low extracellular levels of Mg(2+), proline and by osmotic shock. The leader of mgtA mRNA functions as a riboswitch, favoring transcription under low Mg(2+). Under limiting proline levels the MgtL peptide encoded within the mgtA leader is unable to be translated, also favoring transcription of full mgtA mRNA. Osmotic shock induction also depends on MgtL translation (Probable). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIB subfamily. |
Q2M665 | MFKEIFTRLIRHLPSRLVHRDPLPGAQQTVNTVVPPSLSAHCLKMAVMPEEELWKTFDTHPEGLNQAEVESAREQHGENKLPAQQPSPWWVHLWVCYRNPFNILLTILGAISYATEDLFAAGVIALMVAISTLLNFIQEARSTKAADALKAMVSNTATVLRVINDKGENGWLEIPIDQLVPGDIIKLAAGDMIPADLRILQARDLFVAQASLTGESLPVEKAATTRQPEHSNPLECDTLCFMGTTVVSGTAQAMVIATGANTWFGQLAGRVSEQESEPNAFQQGISRVSMLLIRFMLVMAPVVLLINGYTKGDWWEAALFALSVAVGLTPEMLPMIVTSTLARGAVKLSKQKVIVKHLDAIQNFGAMDILCTDKTGTLTQDKIVLENHTDISGKTSERVLHSAWLNSHYQTGLKNLLDTAVLEGTDEESARSLASRWQKIDEIPFDFERRRMSVVVAENTEHHQLVCKGALQEILNVCSQVRHNGEIVPLDDIMLRKIKRVTDTLNRQGLRVVAVATKYLPAREGDYQRADESDLILEGYIAFLDPPKETTAPALKALKASGITVKILTGDSELVAAKVCHEVGLDAGEVVIGSDIETLSDDELANLAQRTTLFARLTPMHKERIVTLLKREGHVVGFMGDGINDAPALRAADIGISVDGAVDIAREAADIILLEKSLMVLEEGVIEGRRTFANMLKYIKMTASSNFGNVFSVLVASAFLPFLPMLPLHLLIQNLLYDVSQVAIPFDNVDDEQIQKPQRWNPADLGRFMIFFGPISSIFDILTFCLMWWVFHANTPETQTLFQSGWFVVGLLSQTLIVHMIRTRRVPFIQSCASWPLMIMTVIVMIVGIALPFSPLASYLQLQALPLSYFPWLVAILAGYMTLTQLVKGFYSRRYGWQ | Mediates magnesium influx to the cytosol. ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate Upon Mg(2+) depletion, MgtA is stabilized by interaction with MgtS. Interacts with MgtS. Induced by low levels of proline and by osmotic shock. The leader of mgtA mRNA functions as a riboswitch, favoring transcription under low Mg(2+) conditions. Under limiting proline levels the MgtL peptide encoded within the mgtA leader cannot be translated, thereby favoring the transcription of the mgtA ORF. Induction by osmotic shock also depends on translational regulation by MgtL (Probable). Induced by low extracellular levels of Mg(2+) via the PhoQ/PhoP two-component regulatory system. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIB subfamily. |
D0ZTB2 | MLKIITRQLFARLNRHLPYRLVHRDPLPGAQTAVNATIPPSLSERCLKVAAMEQETLWRVFDTHPEGLNAAEVTRAREKHGENRLPAQKPSPWWVHLWVCYRNPFNILLTILGGISYATEDLFAAGVIALMVGISTLLNFVQEARSTKAADALKAMVSNTATVLRVINENGENAWLELPIDQLVPGDIIKLAAGDMIPADLRIIQARDLFVAQASLTGESLPVEKVAATREPRQNNPLECDTLCFMGTNVVSGTAQAVVMATGAGTWFGQLAGRVSEQDNEQNAFQKGISRVSMLLIRFMLVMAPVVLIINGYTKGDWWEAALFALSVAVGLTPEMLPMIVTSTLARGAVKLSKQKVIVKHLDAIQNFGAMDILCTDKTGTLTQDKIVLENHTDISGKPSEHVLHCAWLNSHYQTGLKNLLDTAVLEGVDETAARQLSGRWQKIDEIPFDFERRRMSVVVAEDSNVHQLVCKGALQEILNVCTQVRHNGDIVPLDDNMLRRVKRVTDTLNRQGLRVVAVATKYLPAREGDYQRIDESDLILEGYIAFLDPPKETTAPALKALKASGITVKILTGDSELVAAKVCHEVGLDAGDVIIGSDIEGLSDDALAALAARTTLFARLTPMHKERIVTLLKREGHVVGFMGDGINDAPALRAADIGISVDGAVDIAREAADIILLEKSLMVLEEGVIEGRRTFSNMLKYIKMTASSNFGNVFSVLVASAFLPFLPMLPLHLLIQNLLYDVSQVAIPFDNVDEEQIQKPQRWNPADLGRFMVFFGPISSIFDILTFCLMWWVFHANTPETQTLFQSGWFVVGLLSQTLIVHMIRTRRLPFIQSRAAWPLMAMTLLVMVVGVSLPFSPLASYLQLQALPLSYFPWLIAILVGYMTLTQLVKGFYSRRYGWQ | Mediates magnesium influx to the cytosol. ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate By low extracellular levels of Mg(2+) and by low levels of proline; induction is higher in the absence of both. Also by osmotic shock (0.3 M NaCl). The leader of mgtA mRNA functions as a riboswitch; at low Mg(2+) stem loop 'C' forms which favors transcription of the full-length mgtA mRNA. Under limiting proline levels the 17 residue, proline-rich MgtL peptide encoded within the mgtA leader is unable to be fully translated, and the same stem loop 'C' is able to fold, again favoring transcription of the full mgtA mRNA. Osmotic shock induction also depends on MgtL translation. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIB subfamily. |
P36640 | MLKIITRQLFARLNRHLPYRLVHRDPLPGAQTAVNATIPPSLSERCLKVAAMEQETLWRVFDTHPEGLNAAEVTRAREKHGENRLPAQKPSPWWVHLWVCYRNPFNILLTILGGISYATEDLFAAGVIALMVGISTLLNFVQEARSTKAADALKAMVSNTATVLRVINENGENAWLELPIDQLVPGDIIKLAAGDMIPADLRIIQARDLFVAQASLTGESLPVEKVAATREPRQNNPLECDTLCFMGTNVVSGTAQAVVMATGAGTWFGQLAGRVSEQDNEQNAFQKGISRVSMLLIRFMLVMAPVVLIINGYTKGDWWEAALFALSVAVGLTPEMLPMIVTSTLARGAVKLSKQKVIVKHLDAIQNFGAMDILCTDKTGTLTQDKIVLENHTDISGKPSEHVLHCAWLNSHYQTGLKNLLDTAVLEGVDETAARQLSGRWQKIDEIPFDFERRRMSVVVAEDSNVHQLVCKGALQEILNVCTQVRHNGDIVPLDDNMLRRVKRVTDTLNRQGLRVVAVATKYLPAREGDYQRIDESDLILEGYIAFLDPPKETTAPALKALKASGITVKILTGDSELVAAKVCHEVGLDAGDVIIGSDIEGLSDDALAALAARTTLFARLTPMHKERIVTLLKREGHVVGFMGDGINDAPALRAADIGISVDGAVDIAREAADIILLEKSLMVLEEGVIEGRRTFSNMLKYIKMTASSNFGNVFSVLVASAFLPFLPMLPLHLLIQNLLYDVSQVAIPFDNVDEEQIQKPQRWNPADLGRFMVFFGPISSIFDILTFCLMWWVFHANTPETQTLFQSGWFVVGLLSQTLIVHMIRTRRLPFIQSRAAWPLMAMTLLVMVVGVSLPFSPLASYLQLQALPLSYFPWLIAILVGYMTLTQLVKGFYSRRYGWQ | Mediates magnesium influx to the cytosol. ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate Induced by low levels of proline and by osmotic shock. The leader of mgtA mRNA functions as a riboswitch, favoring transcription under low Mg(2+) conditions. Under limiting proline levels the MgtL peptide encoded within the mgtA leader cannot be translated, thereby favoring the transcription of the mgtA ORF. Induction by osmotic shock also depends on translational regulation by MgtL (Probable). Induced by low extracellular levels of Mg(2+). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIB subfamily. |
A9JPE3 | MDGFGSSQAPAAYREVEWIADVFVIGMGIGWIINYVGMVYGSLKGRTYGMAIMPLCCNIAWEIVYGLIYPSKTLYEQGVFLSGLTINLGVIYTAIKFGPKEWTHAPLVMHNLPLIFMLGILGFLTGHLALAAEIGPALAYNWGAAFCQLLLSVGGLCQLISRGSTRGASYTLWLSRFLGSFSVVISAWLRYKYWPQAFSWLGKPLILWCLFAWLVVDGSYGVCFYYVKRYERRIGHDSDRKTV | Terpene cyclase; part of the ATM2 gene cluster that mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin with acute neurotoxic effects (PubMed:19801473, PubMed:2867895). Synthesis of geranylgeranyl diphosphate (GGPP) by AtmG (a GGPP synthase) precedes condensation of GGPP with indole 3-glycerol phosphate, followed by epoxidation and cyclization by AtmM (a FAD-dependent monooxygenase) and AtmC (a prenyltransferase) to produce paspaline (PubMed:19801473). AtmB is also essential for paspaline production, but its exact role has not been identified yet (PubMed:19801473). AtmP, a cytochrome P450 monooxygenase, subsequently converts paspaline to 13-desoxypaxilline via PC-M6 by removal of the C-30 methyl group and oxidation at C-10 (PubMed:19801473). AtmQ, a cytochrome P450 monooxygenase, then catalyzes the oxidation of 13-desoxypaxilline, first at C-7 to produce paspalicine and then at C-13 to form paspalinine (PubMed:19801473). Finally, AtmD prenylates paspalinine to form aflatrem (PubMed:19801473). The onset of expression occurs at 48 h old stationary cultures and the steady-state levels correlates with the onset of aflatrem biosynthesis at 108 h (PubMed:19801473). Expression is regulated by nsdC (PubMed:26686623). Belongs to the paxB family. |
P22036 | MTDMNIENRKLNRPASENDKQHKKVFPIEAEAFHSPEETLARLNSHRQGLTIEEASERLKVYGRNEVAHEQVPPALIQLLQAFNNPFIYVLMALAGVSFITDYWLPLRRGEETDLTGVLIILTMVSLSGLLRFWQEFRTNRAAQALKKMVRTTATVLRRGPGNIGAVQEEIPIEELVPGDVVFLAAGDLVPADVRLLASRDLFISQSILSGESLPVEKYDVMADVAGKDSEQLPDKDKSLLDLGNICLMGTNVTSGRAQAVVVATGSRTWFGSLAKSIVGTRTQTAFDRGVNSVSWLLIRFMLIMVPVVLLINGFSKGDWVEASLFALAVAVGLTPEMLPMIVSSNLAKGAIAMSRRKVIVKRLNAIQNFGAMDVLCTDKTGTLTQDNIFLEHHLDVSGVKSSRVLMLAWLNSSSQSGARNVMDRAILRFGEGRIAPSTKARFIKRDELPFDFVRRRVSVLVEDAQHGDRCLICKGAVEEMMMVATHLREGDRVVALTETRRELLLAKTEDYNAQGFRVLLIATRKLDGSGNNPTLSVEDETELTIEGMLTFLDPPKESAGKAIAALRDNGVAVKVLTGDNPVVTARICLEVGIDTHDILTGTQVEAMSDAELASEVEKRAVFARLTPLQKTRILQALQKNGHTVGFLGDGINDAPALRDADVGISVDSAADIAKESSDIILLEKDLMVLEEGVIKGRETFGNIIKYLNMTASSNFGNVFSVLVASAFIPFLPMLAIHLLIQNLMYDISQLSLPWDKMDKEFLRKPRKWDAKNIGRFMLWIGPTSSIFDITTFALMWYVFAANNVEAQALFQSGWFIEGLLSQTLVVHMLRTQKIPFIQSRATLPVLLTTGLIMAIGIYIPFSPLGAMVGLEPLPLSYFPWLVATLLSYCLVAQGMKRFYIKRFGQWF | Mediates magnesium influx to the cytosol. ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate Part of the mgtC/mgtB operon. Induced by low extracellular levels of Mg(2+). Decreases Mg(2+) influx. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIB subfamily. |
Q672V5 | MGFFHDFLSRPTTYAILAVLVIPVTALAWDRLPPLLPSAKRLLVGKKNPSKITSLECPYSYIRQIYGTHHWAPFVDKLSPSLKTERPAKYHMILEIMDGIHLCLMLVDDISDGSDYRKGRPAAHHIYGPSETANRAYYRVTQLLNRTGHEFPELAPWLLQCLEEILEGQDLSLVWRRDGLSAFPVQPEERVAAYRQMAYLKTGALFRLVGQLVLENQSYDDTLSTVAWYSQLQNDCKNVYSSDYAKAKGAIAEDLRNGELSYPIVVALNVPKGQYVVPALEFRSPHNIRQALRVIQSDQVRNICLTEMKKSAVSIQDWLALWGRNEKMDMKSEK | Prenyl transferase; part of the ATM1 gene cluster that mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin with acute neurotoxic effects (PubMed:19801473, PubMed:2867895). Synthesis of geranylgeranyl diphosphate (GGPP) by AtmG (a GGPP synthase) precedes condensation of GGPP with indole 3-glycerol phosphate, followed by epoxidation and cyclization by AtmM (a FAD-dependent monooxygenase) and AtmC (a prenyltransferase) to produce paspaline (PubMed:19801473). AtmB is also essential for paspaline production, but its exact role has not been identified yet (PubMed:19801473). AtmP, a cytochrome P450 monooxygenase, subsequently converts paspaline to 13-desoxypaxilline via PC-M6 by removal of the C-30 methyl group and oxidation at C-10 (PubMed:19801473). AtmQ, a cytochrome P450 monooxygenase, then catalyzes the oxidation of 13-desoxypaxilline, first at C-7 to produce paspalicine and then at C-13 to form paspalinine (PubMed:19801473). Finally, AtmD prenylates paspalinine to form aflatrem (PubMed:19801473). Secondary metabolite biosynthesis. The onset of expression correlates with the onset of aflatrem biosynthesis in stationary cultures (PubMed:15528556, PubMed:19801473). Expression is induced by the developmental and secondary metabolism regulator veA (PubMed:16988822). Expression is also regulated by nsdC (PubMed:26686623). Belongs to the FPP/GGPP synthase family. |
A9JPE1 | MSTPKSDTCSPHQALARGMGFKNHHERLWWATFGPLLEKLLALCNYPVSLQYQHLSFIYHHLLPYLGPYPTVENGFAWKTAYSPDGTPAEVSLNFDGPKKTVRMDHVPISQWSGTPKDPFCQNVALELTKSLAGTLPDFTWDWFNHFVQTMFIPEPATDVVLAREPPNFRRMAMQSVNGCDLLTAGVRVKPVFNALWKSIETGIPHDKLLFDSIRNNTELFGAYLPALQVIEDYCQSDRAKEFQTRGCFLSFDATSIKDARLKVYLHGPQTAYMKVEDAFTLGGRLSNPNIQTGVKELRKLWYAVLNLPSDFPESEDLPATDDLYQGWLVNYELRPNNPVPEPKVYIPVAINNKDQDSIVQGLQEFFDRHESMDVRDYRDIFETLFLDAKNPTGIHHFITFSYKAHPYVTCYYKPHLEPVPAKELEESDVKGLSK | Indole diterpene prenyltransferase; part of the ATM2 gene cluster that mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin with acute neurotoxic effects (PubMed:19801473, PubMed:2867895). Synthesis of geranylgeranyl diphosphate (GGPP) by AtmG (a GGPP synthase) precedes condensation of GGPP with indole 3-glycerol phosphate, followed by epoxidation and cyclization by AtmM (a FAD-dependent monooxygenase) and AtmC (a prenyltransferase) to produce paspaline (PubMed:19801473). AtmB is also essential for paspaline production, but its exact role has not been identified yet (PubMed:19801473). AtmP, a cytochrome P450 monooxygenase, subsequently converts paspaline to 13-desoxypaxilline via PC-M6 by removal of the C-30 methyl group and oxidation at C-10 (PubMed:19801473). AtmQ, a cytochrome P450 monooxygenase, then catalyzes the oxidation of 13-desoxypaxilline, first at C-7 to produce paspalicine and then at C-13 to form paspalinine (PubMed:19801473). Finally, AtmD prenylates paspalinine to form aflatrem (PubMed:19801473, PubMed:24038699). The onset of expression occurs at 60 h old stationary cultures and the steady-state levels correlates with the onset of aflatrem biosynthesis at 108 h (PubMed:19801473). Expression is regulated by nsdC (PubMed:26686623). Belongs to the tryptophan dimethylallyltransferase family. |
Q672V6 | MISGVPDRWKVVASSLSSNLDASYPTSSSLSTEPIDTRSSSPQGSASTPVDKEKIIRGPVDYLLKCPGKDIRRKLMQAFNEWLRIPEDRLNIIAEIVGLLHTASLLIDDIQDSSKLRRGIPVAHSIFGVAQTINSANYAYFAAQEKLRELNRPKAYEIFTEELLRLHRGQGMDLYWRDSLTCPTEEEYIEMISNKTGGLFRLAIKLMQLESEVTSDFLGLVDLLGVIFQIRDDYQNLQSDLYSKNKGFCEDLTEGKFSFLIIHSINSNPGNQQLLNILRQRSEEESVKKYAVEYIRSTGSFAYCQDRLASFLHEAKMMVNVLEDNVGFSKGIYDILAFLL | Geranylgeranyl pyrophosphate synthase; part of the ATM1 gene cluster that mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin with acute neurotoxic effects (PubMed:19801473, PubMed:2867895). Synthesis of geranylgeranyl diphosphate (GGPP) by AtmG (a GGPP synthase) precedes condensation of GGPP with indole 3-glycerol phosphate, followed by epoxidation and cyclization by AtmM (a FAD-dependent monooxygenase) and AtmC (a prenyltransferase) to produce paspaline (PubMed:19801473). AtmB is also essential for paspaline production, but its exact role has not been identified yet (PubMed:19801473). AtmP, a cytochrome P450 monooxygenase, subsequently converts paspaline to 13-desoxypaxilline via PC-M6 by removal of the C-30 methyl group and oxidation at C-10 (PubMed:19801473). AtmQ, a cytochrome P450 monooxygenase, then catalyzes the oxidation of 13-desoxypaxilline, first at C-7 to produce paspalicine and then at C-13 to form paspalinine (PubMed:19801473). Finally, AtmD prenylates paspalinine to form aflatrem (PubMed:19801473). dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate (2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate Binds 3 Mg(2+) ions per subunit. The onset of expression correlates with the onset of aflatrem biosynthesis in stationary cultures (PubMed:15528556, PubMed:19801473). Expression is induced by the developmental and secondary metabolism regulator veA (PubMed:16988822). Belongs to the FPP/GGPP synthase family. |
Q68DC9 | MAASEAAAAAGSAALAAGARAVPAATTGAAAAASGPWVPPGPRLRGSRPRPAGATQQPAVPAPPAGELIQPSVSELSRAVRTNILCTVRGCGKILPNSPALNMHLVKSHRLQDGIVNPTIRKDLKTGPKFYCCPIEGCPRGPERPFSQFSLVKQHFMKMHAEKKHKCSKCSNSYGTEWDLKRHAEDCGKTFRCTCGCPYASRTALQSHIYRTGHEIPAEHRDPPSKKRKMENCAQNQKLSNKTIESLNNQPIPRPDTQELEASEIKLEPSFEDSCGSNTDKQTLTTPPRYPQKLLLPKPKVALVKLPVMQFSVMPVFVPTADSSAQPVVLGVDQGSATGAVHLMPLSVGTLILGLDSEACSLKESLPLFKIANPIAGEPISTGVQVNFGKSPSNPLQELGNTCQKNSISSINVQTDLSYASQNFIPSAQWATADSSVSSCSQTDLSFDSQVSLPISVHTQTFLPSSKVTSSIAAQTDAFMDTCFQSGGVSRETQTSGIESPTDDHVQMDQAGMCGDIFESVHSSYNVATGNIISNSLVAETVTHSLLPQNEPKTLNQDIEKSAPIINFSAQNSMLPSQNMTDNQTQTIDLLSDLENILSSNLPAQTLDHRSLLSDTNPGPDTQLPSGPAQNPGIDFDIEEFFSASNIQTQTEESELSTMTTEPVLESLDIETQTDFLLADTSAQSYGCRGNSNFLGLEMFDTQTQTDLNFFLDSSPHLPLGSILKHSSFSVSTDSSDTETQTEGVSTAKNIPALESKVQLNSTETQTMSSGFETLGSLFFTSNETQTAMDDFLLADLAWNTMESQFSSVETQTSAEPHTVSNF | Transcription factor. Plays a crucial role in cell survival and RAD51 foci formation in response to methylating DNA damage. Involved in regulating the activity of ATM in the absence of DNA damage. May play a role in stabilizing ATM. Binds to the DYNLL1 promoter and activates its transcription. Interacts via its C-terminus with ATM. Interacts with DYNLL1; this interaction inhibits ATMIN transcriptional activity and hence may play a role in a feedback loop whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN. Nuclear, in discrete foci during G1 phase. Ubiquitously expressed in normal tissues and cancer cell lines with highest levels in placenta and skeletal muscle. Extended N-terminus. Truncated N-terminus. |
Q8C311 | MAATEAAAADSAGPAPGVPATPASTRGAAAASSPWRPPESRLQGSRPRPARARAAAPVPPARELIQPTVSELSRAVRTNILCTVRGCGKILPNSPALNMHLVKSHRLQDGIVNPTIRKDLTTAPKFYCCPIKGCPRGPDRPFSQFSLVKQHFMKMHAEKKHKCSKCSNSYGTEWDLKRHEEDCGKTFQCTCGCPYASRTALQSHIYRTGHEIPAEHRDPPSKKRKMESYLQNQKLSSKTTEPLSDQAAPRQDAAEPDAPEVKPAASLEDSCSAHTKKQSVATPPRCPQKLLLPKPKVALVKLPVMQFSPVPVFVPTAESSAQPVVLGVDHSSAAGTVHLVPLSVGALILSLDSEACSLKESLPLSKIISPVVEPMNTGVQVNLGKSLCSPLQEVGSVCQRTSISSSNVQTDLTYASANLIPSAQWLGPDSSVSSCSQTDLSFDSQVSLPVSVHTQTLVPSSKVTSSIAAQTDAFIDACFQPGGVSRETQTSRMQNRTNDSVPVGHTGLCGDIFESVHASYSVPTDTIMSSSLVAETGTHGLPPQSDPKILGQVMEKSAPVLNFSTQNGLLPAHTMTDNQTQTIDLLSDLENILSSNLPGQTLDNRSLLSDTNPGPDAQLPAGSAQNSGIDFDIEEFLSASNIQTQTEESELSSMSTEPVLESLDIETQTDVLLSDPSTQPYGFRAGSGFLGLEMFDTQTQTDLNFFLDSSPHLPLGSILKHSSFSMSTDSSDTETQTEGACPARHLPALESKVQLSSTETQTMSSGFEPLGNLFLTSNETQTAMDDFLLADLAWNTMESQFSSVETQTCAELHAVSSF | Transcription factor. Plays a crucial role in cell survival and RAD51 foci formation in response to methylating DNA damage. Involved in regulating the activity of ATM in the absence of DNA damage. May play a role in stabilizing ATM (By similarity). Binds to the DYNLL1 promoter and activates its transcription. Interacts via its C-terminus with ATM. Interacts with DYNLL; this interaction inhibits ATMIN transcriptional activity and hence may play a role in a feedback loop whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN. ATMIN. Nuclear, in discrete foci during G1 phase. Contaminating sequence. Potential poly-A sequence. Truncated N-terminus. |
Q9SVS2 | MYHPNMFESHHHMFDMTPKNSENDLGITGSHEEDFETKSGAEVTMENPLEEELQDPNQRPNKKKRYHRHTQRQIQELESFFKECPHPDDKQRKELSRELSLEPLQVKFWFQNKRTQMKAQHERHENQILKSENDKLRAENNRYKDALSNATCPNCGGPAAIGEMSFDEQHLRIENARLREEIDRISAIAAKYVGKPLMANSSSFPQLSSSHHIPSRSLDLEVGNFGNNNNSHTGFVGEMFGSSDILRSVSIPSEADKPMIVELAVAAMEELVRMAQTGDPLWVSSDNSVEILNEEEYFRTFPRGIGPKPIGLRSEASRESTVVIMNHINLIEILMDVNQWSSVFCGIVSRALTLEVLSTGVAGNYNGALQVMTAEFQVPSPLVPTRENYFVRYCKQHSDGIWAVVDVSLDSLRPSPITRSRRRPSGCLIQELQNGYSKVTWVEHIEVDDRSVHNMYKPLVNTGLAFGAKRWVATLDRQCERLASSMASNIPACDLSVITSPEGRKSMLKLAERMVMSFCTGVGASTAHAWTTLSTTGSDDVRVMTRKSMDDPGRPPGIVLSAATSFWIPVAPKRVFDFLRDENSRSEWDILSNGGLVQEMAHIANGRDPGNSVSLLRVNSGNSGQSNMLILQESCTDASGSYVIYAPVDIIAMNVVLSGGDPDYVALLPSGFAILPDGSARGGGGSANASAGAGVEGGGEGNNLEVVTTTGSCGGSLLTVAFQILVDSVPTAKLSLGSVATVNSLIKCTVERIKAALACDGA | Probable transcription factor involved in cell specification and pattern formation during embryogenesis. Binds to the L1 box DNA sequence 5'-TAAATG[CT]A-3'. Plays a role in maintaining the identity of L1 cells, possibly by interacting with their L1 box or other target-gene promoters; binds to the LIP1 gene promoter and stimulates its expression upon imbibition (PubMed:24989044). Acts as a positive regulator of gibberellins (GAs)-regulated epidermal gene expression (e.g. LIP1, LIP2, LTP1, FDH and PDF1) (PubMed:24989044). Functionally redundant to PDF2 (PubMed:24989044). Seems to promote cell differentiation (PubMed:25564655). Interacts with GAI/RGA2, RGA/RGA1/GRS, RGL2/SCL19 and PDF2 (PubMed:24989044). Interacts with AIL7/PLT7, ANT, BBM and AIL1 (PubMed:25564655). First expressed in the apical cell after the first asymmetric division of the zygote. Expressed in all proembryo cells until the eight-cell stage, and then restricted to the protoderm in the 16-cell proembryo. Not detected in the torpedo stage, but reappeared later in the L1 layer of the shoot apical meristem in the mature embryo. After germination, the L1 layer-specific expression pattern is maintained in the vegetative shoot apical meristem, inflorescence, floral meristems, and the young floral organ primordia. Finally, expressed in the protoderm of the ovule primordia and integuments and gradually restricted to the endothelium surrounding the embryo sac. Stimulated during seed imbibition (PubMed:24989044). Induced by gibberellins (GAs) and repressed by DELLA proteins in an ATML1- and PDF2-dependent manner (PubMed:24989044). Upon seed imbibition, increased GA levels in the epidermis reduce DELLA proteins (e.g. GAI/RGA2, RGA/RGA1/GRS and RGL2/SCL19) abundance and release, in turn, ATML1 and PDF2 which activate LIP1 expression, thus enhancing germination potential (PubMed:24989044). Plants missing both PDF2 and ATML1 have reduced levels of L1 box/ gibberellic acid (GA)-regulated putative targets, including LIP1, LIP2, LTP1, FDH and PDF1, in the presence of GA and during seed germination, thus leading to a delayed germination upon imbibition (PubMed:24989044). In plants missing HDG3, HDG7, HDG11, PDF2 and ATML1, increased cell division leading to cell overproliferation (PubMed:25564655). Belongs to the HD-ZIP homeobox family. Class IV subfamily. Probable cloning artifact leading to a deletion into the sequence. |
Q672V4 | MCDKDRFKVIIVGGSVAGLTLAHCLQRAGIDHVVLEKNSDLSPQVGASIGIIPNGGRILDQLGLFDAVERMTYPLSIATITYPDGYSFRNNYPKTVDERFGYPIAFLDRQKFLEILHTSYPDPSNIHTNCRVTHIRRHDSHMEVVTSSGQEYTGDLVVGADGVHSVIRSEMWKLADALEPGRVSKREKRSMKVEYACVFGISLPVPGLKVGDQVNAFHDGLTIITIHGKNGRVFWFVIKKLDDMYTYPDTVRFSSADAVRTCENIVHFPLVNGATFGHVWENREVTSMTALEENIFNTWYADRIVCIGDSIHKMTPNIGQGANTAIEDATVLTNLLYDRLSKNGHKKLARQELLQLLREFQSQRFRRVNKIYQDSRFLVRLHARDGIVKSLLARYIVPYMTELPADLASKSIADSPTIGFLPLPSRSGPGWLQWSRKQRRPATPWILVLLVIVVSFGLHSPELVIPTFWSNSLVSKTVE | FAD-dependent monooxygenase; part of the ATM1 gene cluster that mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin with acute neurotoxic effects (PubMed:15528556, PubMed:19801473, PubMed:2867895). Synthesis of geranylgeranyl diphosphate (GGPP) by AtmG (a GGPP synthase) precedes condensation of GGPP with indole 3-glycerol phosphate, followed by epoxidation and cyclization by AtmM (a FAD-dependent monooxygenase) and AtmC (a prenyltransferase) to produce paspaline (PubMed:19801473). AtmB is also essential for paspaline production, but its exact role has not been identified yet (PubMed:19801473). AtmP, a cytochrome P450 monooxygenase, subsequently converts paspaline to 13-desoxypaxilline via PC-M6 by removal of the C-30 methyl group and oxidation at C-10 (PubMed:19801473). AtmQ, a cytochrome P450 monooxygenase, then catalyzes the oxidation of 13-desoxypaxilline, first at C-7 to produce paspalicine and then at C-13 to form paspalinine (PubMed:19801473). Finally, AtmD prenylates paspalinine to form aflatrem (PubMed:19801473). Secondary metabolite biosynthesis. The onset of expression correlates with the onset of aflatrem biosynthesis in stationary cultures (PubMed:15528556, PubMed:19801473). Expression is induced by the developmental and secondary metabolism regulator veA (PubMed:16988822). Belongs to the paxM FAD-dependent monooxygenase family. |
A9JPE0 | MDKLTATLAKVNYPSEVENGSMLLVVTLVILFLWFIIPSPVKRSNVSVPTVTLFNPYLPEFLSRVWFNSTAATVIYKGYRQHKDRAFRLLKPDGDIIVLSNKYVEELRQLPLTTLNALEAVFEDHVGKYTTILDDSHLHTEVIQKRLTPAINRLIPRIIDELDHGFAVEMPECEDKWVLIRPYEVFLRLVARAGARVFVGPDFCRTEKWLTASIDFTKNIFMTITLLRPIPSFLHPIIGPMLPSSRSLDTQLRYVQDELLGPEIVKRRQRQASGDPDYEKPDDFLQWMIDLAQNDKEGDPGNIAHRLLGLTSMAVVHTSAMSITHGLYDLITMAQWLEPLRQEIQEAMPDWKSSSYSSLVSLRRLDSFLKESQRFNPPGELSFHRVVKKDLVLSDGLRLPKGTHICMASGPIGMDTKYVSDPTTFDAFRYVDGDKAQSQFVHTSATSMHFGLGRYACPGRFFATFVLKAILSRFLVEYEFRFGPDQVGRPKNMLLGDKIVPNTSVDVYVRKRTGSRSTA | Cytochrome P450 monooxygenase; part of the ATM2 gene cluster that mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin with acute neurotoxic effects (PubMed:19801473, PubMed:2867895). Synthesis of geranylgeranyl diphosphate (GGPP) by AtmG (a GGPP synthase) precedes condensation of GGPP with indole 3-glycerol phosphate, followed by epoxidation and cyclization by AtmM (a FAD-dependent monooxygenase) and AtmC (a prenyltransferase) to produce paspaline (PubMed:19801473). AtmB is also essential for paspaline production, but its exact role has not been identified yet (PubMed:19801473). AtmP, a cytochrome P450 monooxygenase, subsequently converts paspaline to 13-desoxypaxilline via PC-M6 by removal of the C-30 methyl group and oxidation at C-10 (PubMed:19801473). AtmQ, a cytochrome P450 monooxygenase, then catalyzes the oxidation of 13-desoxypaxilline, first at C-7 to produce paspalicine and then at C-13 to form paspalinine (PubMed:19801473). Finally, AtmD prenylates paspalinine to form aflatrem (PubMed:19801473). Secondary metabolite biosynthesis. The onset of expression occurs at 60 h old stationary cultures and the steady-state levels correlates with the onset of aflatrem biosynthesis at 108 h (PubMed:19801473). Belongs to the cytochrome P450 family. |
P27112 | MGKADNYELYSVELGPGPGGDMAAKMSKKKKAGGGGGKRKEKLENMKKEMEINDHQLSVAELEQKYQTSATKGLSARLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLALALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILAAQGCKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTAQGLVVNTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFVVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCHLYLSEKDYPPGYAFDVEAMNFPSSGLCFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPRNPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEGWFPLLCVGLRPQWEDHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEMCQIADVLIRKTRRLSAFQQGFFRNRILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPMPFGLLIFVYDEIRKLGVRCCPGSWWDQELYY | The catalytic subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells (PubMed:10722662, PubMed:24188822). Uses ATP as an energy source to pump H(+) ions to the gastric lumen while transporting K(+) ion from the lumen into the cell (PubMed:10722662, PubMed:24188822). Remarkably generates a million-fold proton gradient across the gastric parietal cell membrane, acidifying the gastric juice down to pH 1 (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). The release of the H(+) ion in the stomach lumen is followed by binding of K(+) ion converting the pump conformation back to the E1 state (PubMed:10722662, PubMed:24188822) (By similarity). ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) + K(+)(in) + phosphate The gastric H(+)/K(+) ATPase pump is composed of the catalytic alpha subunit ATP4A and the regulatory beta subunit ATP4B (PubMed:10722662, PubMed:11909858). Interacts (via the P-domain) with ATP4B (via N-terminus); this interaction stabilizes the lumenal-open E2 conformation state and prevents the reverse reaction of the transport cycle (By similarity). Localized in the apical canalicular membrane of parietal cells. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. |
Q6LD86 | MGKENYELYSVELGTGPGGDMAAKMSKKKAGGGGGKKKEKLENMKKEMEMNDHQLSVSELEQKYQTSATKGLKASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLALALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILSAQGCKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTAQGLVVSTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFVVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQLYLNEKDYPPGYTFDVEAMNFPSSGLCFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRMPVDQVNKKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPRNPRRDRLVNEPLAAYSYFQIGAIQSFAGFADYFTAMAQEGWFPLLCVGLRPQWEDHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEMCQIADVLIRKTRRLSAFQQGFFRNRILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPMPFGLLIFVYDEIRKLGVRCCPGSWWDQELYY | The catalytic subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells (PubMed:20921224, PubMed:22448261). Uses ATP as an energy source to pump H(+) ions to the gastric lumen while transporting K(+) ion from the lumen into the cell (PubMed:20921224, PubMed:22448261). Remarkably generates a million-fold proton gradient across the gastric parietal cell membrane, acidifying the gastric juice down to pH 1 (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). The release of the H(+) ion in the stomach lumen is followed by binding of K(+) ion converting the pump conformation back to the E1 state (PubMed:20921224, PubMed:22448261) (By similarity). ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) + K(+)(in) + phosphate The gastric H(+)/K(+) ATPase pump is composed of the catalytic alpha subunit ATP4A and the regulatory beta subunit ATP4B. Interacts (via the P-domain) with ATP4B (via N-terminus); this interaction stabilizes the lumenal-open E2 conformation state and prevents the reverse reaction of the transport cycle. Localized in the apical canalicular membrane of parietal cells (By similarity). Localized in the apical canalicular membrane of parietal cells (By similarity). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. |
Q92126 | MGKKEQYDMYSVEMEREGDGAMDVKVMKKNKASKKKEKLESMKKEMDINDHEITVEELEQKYTTSVSKGLKSAFAAEVILRDGPNELKPPKGTPEYIKFARQLAGGLQCLMWVAAVICLIAFGIEESQGDLTSADNLYLAITLIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVVRDGDKFQINANQLVVGDLVEIKGGDRVPADIRIITSQGCKVDNSSLTGESEPQTRSPEYTHESPLETRNIAFFSTMCLEGTATGIIINTGDRTIIGRIATLASGVGNEKTPIAIEIEHFVDIIAGLAIFFGATFFVVAMVIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLARKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHSADTTEDQSGQSFDQTSDTWRALSKVVSLCNRAFFKSGQDGIPVPKRIVIGDASETALVKFSEITVGNVMEYRERFKKVTEVPFNSTNKFQLSIHELQDPLDLRYLMVMKGAPERILERCSTIMIKGQELPLDEQWKEAFQTAYMDLGGLGERVLGFCHLYLNEKEYSRGFNFDTEEMNFPTSGLCFAGLISMIDPPRATVPDAVMKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRIPVEQVNKRDARACVINGGQLKEMSSEELVEALKLHPEMVFARTSPQQKLIIVESCQKLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELAPYLIYITASVPLPLGCITILFIELCTDIFPSVSLAYERAESDIMHLKPRNPRRDRLVNEALAVYSYFQIGIIQSFAGFVDYFTVMAQEGWFPAYVLGLRSHWENQHLQDLQDSYGQEWTFSQRLYQQYTCYTVFFISYEICQISDVLIRKTRRLSVFQQGFFRNKVLVIAIVFQLCLGNFLCYCPGMPNVFNFMPIRFQWWLVPLPFGILIFVYDEIRKLGVRRHPGSWFDKEMYY | Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for acid production in the stomach. ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) + K(+)(in) + phosphate Composed of two subunits: alpha (catalytic) and beta. Exclusively expressed in stomach mucosa. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. |
P33704 | MAALQEKKSCSQRMEEFQRYCWNPDTGQMLGRTLSRWVWISLYYVAFYVVMTGIFALCIYTLMCTLDPYTPDYQDQLKSPGVTLRPDVYGEKGLDISYNVSDNRTWVDLVNILHNFLEGYSPTSQEDNINCTSEKYFFQDVFGAPNHTKFSCKFMADMLQNCSGLTDPNFGFAEGKPCFIIKMNRIVNFLPSNSTAPRADCTFLDQHKDDRPLQVEYYPPNGTFSLRYFPYYGKKAQPHYSNPLVAAKLLNVPRNTEVLIVCKILADYVTFDNPHDPYEGKVEFKLTIQQ | The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle (By similarity). The ATPase pump is composed of two subunits: alpha (catalytic) and beta (regulatory). Interacts with alpha subunit ATP12A; this interaction is required for the formation of a functionally active pump and targeting at the plasma membrane (By similarity). Interacts (via N-terminus) with alpha subunit ATP4A (via the P-domain) (By similarity). Localized in the apical canalicular membrane of parietal cells. The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties. N-glycosylation is necessary for assembly and functional expression of the pump at the plasma membrane. Belongs to the X(+)/potassium ATPases subunit beta family. |
B1B0N8 | MAALQEKKTCGQRMEEFQRYCWNPDTGQMLGRTLSRWVWISLYYVAFYVVMTGLFALCLYVLMQTVDPYTPDYQDQLRSPGVTLRPDVYGEKGLEIVYNVSDNRTWADLTQTLHAFLAGYSPAAQEDSINCTSEQYFFQESFRAPNHTKFSCKFTADMLQNCSGLADPNFGFEEGKPCFIIKMNRIVKFLPSNGSAPRVDCAFLDQPRELGQPLQVKYYPPNGTFSLHYFPYYGKKAQPHYSNPLVAAKLLNIPRNAEVAIVCKVMAEHVTFNNPHDPYEGKVEFKLKIEK | The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle (By similarity). The ATPase pump is composed of two subunits: alpha (catalytic) and beta (regulatory). Interacts with alpha subunit ATP12A; this interaction is required for the formation of a functionally active pump and targeting at the plasma membrane (By similarity). Interacts (via N-terminus) with alpha subunit ATP4A (via the P-domain) (By similarity). Localized in the apical canalicular membrane of parietal cells. The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties. N-glycosylation is necessary for assembly and functional expression of the pump at the plasma membrane. Belongs to the X(+)/potassium ATPases subunit beta family. |
Q9D6Y2 | MAALQEKKSCSQRMAEFRHYCWNPDTGQMLGRTPARWVWISLYYAGFYVVMTGLFALCIYVLMQTIDPYTPDYQDQLKSPGVTLRPDVYGERGLKISYNVSENSSWAGLTHTLHSFLAGYTPASQQDSINCTSEKYFFQESFAAPNHTKFSCKFTADMLQNCSGLADPSFGFEEGKPCFIIKMNRIVKFLPSNNTAPRVDCTFQDDPQKPRKDTEPLQVEYYPPNGTFSLHYFPYYGKKAQPHYSNPLVAAKLLNVPKNMQVSIVCKILADHVTFNNPHDPYEGKVEFKLTIQK | The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle (By similarity). The ATPase pump is composed of two subunits: alpha (catalytic) and beta (regulatory). Interacts with alpha subunit ATP12A; this interaction is required for the formation of a functionally active pump and targeting at the plasma membrane (By similarity). Interacts (via N-terminus) with alpha subunit ATP4A (via the P-domain) (By similarity). Localized in the apical canalicular membrane of parietal cells. Expressed in parietal cells (at protein level). The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties. N-glycosylation is necessary for assembly and functional expression of the pump at the plasma membrane. Belongs to the X(+)/potassium ATPases subunit beta family. |
P18434 | MAALQEKKSCSQRMEEFQRYCWNPDTGQMLGRTLSRWVWISLYYVAFYVVMSGIFALCIYVLMRTIDPYTPDYQDQLKSPGVTLRPDVYGEKGLDISYNVSDSTTWAGLAHTLHRFLAGYSPAAQEGSINCTSEKYFFQESFLAPNHTKFSCKFTADMLQNCSGRPDPTFGFAEGKPCFIIKMNRIVKFLPGNSTAPRVDCAFLDQPRDGPPLQVEYFPANGTYSLHYFPYYGKKAQPHYSNPLVAAKLLNVPRNRDVVIVCKILAEHVSFDNPHDPYEGKVEFKLKIQK | The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle (PubMed:29618813, PubMed:19387495). The ATPase pump is composed of two subunits: alpha (catalytic) and beta (regulatory). Interacts with alpha subunit ATP12A; this interaction is required for the formation of a functionally active pump and targeting at the plasma membrane (By similarity). Interacts (via N-terminus) with alpha subunit ATP4A (via the P-domain) (PubMed:19387495, PubMed:29618813). Localized in the apical canalicular membrane of parietal cells. Stomach. The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties. N-glycosylation is necessary for assembly and functional expression of the pump at the plasma membrane. Parietal cell autoantigen associated with autoimmune gastritis. Belongs to the X(+)/potassium ATPases subunit beta family. |
P18597 | MAALQEKKSCSQRMEEFRHYCWNPDTGQMLGRTLSRWVWISLYYVAFYVVMTGLFALCIYVLMQTIDPYTPDYQDQLKSPGVTLRPDVYGEKGLEIHYNISDNRTWTSLTHTLRSFLAGYSPAAQVDNINCTSKTYFFQESFGAPNHTKFSCKFTADMLENCSGLTDPSFGFKEGKPCFIIKMNRIVRFLPSNSTPPRVDCTFLDMPHQALTPLQVEYYPPNGTFSLHYFPYYGKKAQPHYSNPLVAAKLLNVPTNTEVVVLCKILADHVTFDNPHDPYEGKVEFKLKIQK | The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells (PubMed:7485470, PubMed:10722662, PubMed:11909858). Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump (PubMed:7485470, PubMed:10722662, PubMed:11909858). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2) (By similarity). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle (By similarity). The ATPase pump is composed of two subunits: alpha (catalytic) and beta (regulatory). Interacts with alpha subunit ATP12A; this interaction is required for the formation of a functionally active pump and targeting at the plasma membrane (PubMed:7485470). Interacts (via N-terminus) with alpha subunit ATP4A (via the P-domain) (PubMed:11909858, PubMed:10722662) (By similarity). Localized in the apical canalicular membrane of parietal cells. The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties. N-glycosylation is necessary for assembly and functional expression of the pump at the plasma membrane. Belongs to the X(+)/potassium ATPases subunit beta family. |
P18598 | MAALQEKKSCSQRMAEFRQYCWNPDTGQMLGRTPARWVWISLYYAAFYVVMTGLFALCIYVLMQTIDPYTPDYQDQLKSPGVTLRPDVYGERGLQISYNISENSSWAGLTHTLHSFLAGYTPASQQDSINCSSEKYFFQETFSAPNHTKFSCKFTADMLQNCSGLVDPSFGFEEGKPCFIIKMNRIVKFLPSNNTAPRVDCTFQDDPQKPRKDIEPLQVQYYPPNGTFSLHYFPYYGKKAQPHYSNPLVAAKFLNVPKNTQVLIVCKIMADHVTFDNPHDPYEGKVEFKLTIQK | The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump (By similarity). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle (By similarity). The ATPase pump is composed of two subunits: alpha (catalytic) and beta (regulatory). Interacts with alpha subunit ATP12A; this interaction is required for the formation of a functionally active pump and targeting at the plasma membrane (By similarity). Interacts (via N-terminus) with alpha subunit ATP4A (via the P-domain) (By similarity). Localized in the apical canalicular membrane of parietal cells. Stomach. The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties. N-glycosylation is necessary for assembly and functional expression of the pump at the plasma membrane. Belongs to the X(+)/potassium ATPases subunit beta family. |
Q96252 | MFKQASRLLSRSVAAASSKSVTTRAFSTELPSTLDSTFVEAWKKVAPNMDPPQTPSAFMKPRPSTPSSIPTKLTVNFVLPYTSELTGKEVDMVIIPASTGQMGVLPGHVPTIAELKPGIMSVHEGTDVKKYFLSSGFAFLHANSVADIIAVEAVPLDHIDPSQVQKGLAEFQQKLASATTDLEKAEAQIGVEVHSAINAALSG | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
Q40089 | MFRHSSRLLARATTMGWRRPFSTDLPAETAADSTFVEAWKKLIPNVDPPKTPSAYMAPRPATPSSIPSKLTVNFVLPYSSELAGKEVDMVIIPATTGQMGVLPGHVATIAELKPGVMSVHEGNDVSKYFVSGGFAFIHANSFADIIAVEAVPLDRIDANLVQKGLAEFTQKLNTASTDVEKAEAQIGVDVHSALNAALTG | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
B4F8Z1 | MASLPLCRSPSSLLPSWPHRPISASFNPKNPSSPVAAHVSVQETPPQPQDPSPPSDSNPNGTRPSSSSNTRFLWVNPNSPRAADVARARAGSGRRARLASAAAALGACETTESAVEAALQAAFPEPPSEQDAVIVLNTAAATRAETAVLALRWFLGNAKVRKKVILYNVVLKLLRKKRLWSETEALWAEMLRDGVQPDNATFSTVISCARACGLHSKAVEWFDKMPEFGCSPDMLTYSAVIDAYGHAGNSEAALRLYDRARAEKWQLDPVICSTVIKVHSTSGNFDGALNVFEEMKAIGVRPNLVVYNTMLDAMGRALRPWVVKTIHREMVDQQVQPSRATYCCLLHAYTRARYGEDAMAVYRLMKDEAMGIDVMLYNMLLSMCADIGYVDEAEEIFRDMKASMGAHSKPDSWSYSSMVTLYSSTANVLSAEGILNEMVEAGFKPNIFVLTSLIRCYGKVGRTDDVVRSFGMLQDLGIIPDDRFCGCLLSVAANTPAEELGKVISCIERSNVQLGAVVKLLVDRSSSESFREAARELLRSSRGVVKMPYCNCLMDLCVNLNQMEKACALLDAAQQLGIYANIQTRTQTQWSLHLRGLSVGAALTTLHVWMNDLYTSLQTGNEGLPPLLGIHTGQGKNTYSDRGLAAMFEAHLKELDAPFHEAPDKAGWFLTTNVAAKQWLESKAASELVTV | Involved in translation and accumulation of chloroplast ATP synthase subunits. Interacts with the 5'-UTR of the chloroplast bicistronic atpB and atpE mRNA and activates its translation by facilitating ribosome association with the mRNA (PubMed:22708543). Required for accumulation and activity of the chloroplast ATP synthase. Enhances atpA translation and is required for accumulation of specific processed atpF and psaJ transcripts (PubMed:22708543, PubMed:23735295). Required for the stabilization of bicistronic rpl16 and rpl14 mRNAs (PubMed:23735295). Pale green leaf phenotype. Belongs to the PPR family. P subfamily. |
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