wanglab/gogpt-training-data huggingface dataset:
Protein: Succinate--CoA ligase [ADP-forming] subunit alpha-1, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha-1) (SCS-alpha-1) (P68209)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
Sequence:
MSRQVARLIGSLSSKARRCSTGGSEVFPSCQSLTSLTQSRSFASDPHPPAAVFVDKNTRVLCQGITGKNGTFHTEQAIEYGTKMVAGVTPKKGGTEHLGLPVFNSVAEAKADTKANASVIYVPAPFAAAAIMEGIEAELDLIVCITEGIPQHDMVRVKHALNSQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGKIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIGGTAEEDAAALIKASGTEKPVVAFIAGLTAPPGRRMGHAGAIVSGGKGTAQDKIKSLNDAGVKVVESPAKIGSAMYELFQERGLLKQ
Protein: CORL (Fussel, isoform B) (Fussel, isoform D) (D1YSG4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- BTB/POZ domain-containing protein 9
Sequence:
MDLNENFKMASISVAHFDRMENCQTSQRSNHVSSVLLYGVQIVSLHIEGQERLCLAQISNTLLKQFSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPVSSRRCGMITRREAERLCKSFLGDNTPPRLPDDFAFNVQHKCAWGCRGSFLPSRYNSSRAKCIKCSYCGMFFSPNKFIFHSHRITTNDRYVQPDAANFNSWRRHMSLSGNDYDEKIIHAWEDVKAMFNGGTRKRLVGSSINPRSPGSPTQSTAVSSGVGSSSCGSPTSFERDTNEVDGKSGSSLPQRSQIDSQYNYGTVAAAAAVVGVTAVAAATVGVPFNLHGSTVLSPLHSLRNERDLSIMPISRNFVVDYMWQQKDQHYQQPYARKIPSGDNSDSSLDFDSWVKPDSNNPIPNANSVRTSDNCSFNIKNESHSSIYGIIKNHKLSGVPNSGLNLSDYNIPSILNCSAFKPVVASTAIVSTSLYTRSNESTRTDCNNPAQSTRTTTVLTHNSISASSHQIVGHKTFSPILGKIHSNPEKNRIVSVFASSSTGNADDNDDDDEVVDIETTEDEGKFTVQHADSPKTQYDAISGSDSPSRSPSTSTNIDVEQDVDVDIITTDTEDQLELSVGRYSTENTSHSLSFFQAEKIQISDLSPNTKTSSGDNETNTLKDAKGINGNLQILARRKRNKLQKDRCLSKRTVSKCVSDKSLIKGLAANELSSSLQIQQHVAFPVFLKSQLHSLRPQQAQQVVSLTTNSVAESNKWSYPVGNIEPLCCYQTSGNKNSLV
Protein: Woronin body major protein hexA (Q4WUL0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Major component of Woronin bodies, fungal-specific organelles that occlude septal pores in order to separate intact from damaged compartments. HexA binds directly or indirectly to the Woronin body tether that in turn is anchored at the rim of the septal pore. Woronin bodies are important for stress resistance and virulence.
Subcellular location: Cell septum {ECO:0000269|PubMed:23332467}. Cytoplasm {ECO:0000269|PubMed:23332467}. Note=Localizes at Woronin bodies, fungal-specific organelles that plug the septal pore in case of physical damage (PubMed:23332467). Binds to the septal pore in a lah-dependent manner (PubMed:23869404). {ECO:0000269|PubMed:23332467, ECO:0000269|PubMed:23869404}.
Interaction partners:
- 40S ribosomal protein S3
- 60S ribosomal protein L35
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S6
- 60S ribosomal protein L5, putative
- Deoxyhypusine synthase
- 60S ribosomal protein L23
- Small ribosomal subunit protein eS1
- Ribosomal protein L16a
- 60S ribosomal protein L21, putative
Sequence:
MYSVESKFERDSRRDAQRTANLDFDARVPIPFSVFPSSYRSDAVPETTLTRVEGEVNLDRTSHVEREDTRTSAPLPDPRVYGREEVDIHISKDRLHAPSRKGDDFQVIYEDRAHKDSRVPEVELSRERWKRSENNAKQNKNKNNTSTRRSGDVLKAVSAKKVAPQAQTRADEKASYQLTQKARYRESTSRYEPLPPKPVYDQALESQLDITEREYRRRTDPTYDVNLSYGRHQAPVDSYQAYQPQQTSDVSLHRSKTEIDVSYDKAYTPKPLETRKGDSFSRSELTVESVPSRPSSASSISQVKVLKPYTAIDQPPARKMGYYDDDGNYHSFRRGVERAVDRITHPFHHHHHHHDREEVVIADERGPVRYRDGVREDVRIVEPRASKTTAESVPIPCHFIRIGDILILQGRPCQVIRISVSPQTGQHRYLGVDLFTRQLQEESSFVSNPSPSVVVQTMLGPVYKTYRILDLHEDGTITAMTETGDVKQALPVVTQGQLFRKIRDAFSEGRGSVRALVINDGGRELVVDYKVIHGSRL
Protein: Zinc finger-interacting factor 1 (Protein zif-1) (P34482)
Organism: Caenorhabditis elegans
Function: Probable substrate recognition component of a CBC (Cul2-ElonginB-ElonginC) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Ensures germline precursor cell asymmetry by targeting germline proteins for destruction if expressed in non-germline cells. This process also requires elc-1, cul-2, rbx-1 and ubc-2.
Interaction partners:
- Zinc finger protein mex-5
- CCCH-type zinc finger protein oma-1
- Pharynx and intestine in excess protein 1
- Zinc finger protein mex-6
- RNA-binding protein pos-1
- C3H1-type domain-containing protein
- Elongin-C
- PIP-1
- CCCH-type zinc finger protein oma-2
- Elongin-C
Sequence:
MSECSASTSQLSTFCVNEIPWKLVPQTCDEFSEYEFIDEKYRRLSDVESFVWKWSPCGRYGIDLPGGRDVINQQLRDRMAVFDLHTNKWTLYTMDRGAFEIPRVCFLYWARNDIIGTITLVKDYEAGPDDEIPLKFKQSFFYVSHETQTLVYSGSCKYRTNKTIVASYWYHIFENRRGEPFIDHNNYLWLVFSNGVDSLILLPFIPTSTCFKAKCVSFDMNDIVSQFTGIRVFLDPFVSSHYVPWVYRNDVNFFIRIDSHSFIEEQNRDYGLDPQIDNPETKPHRGVFQLRVNLKDVIEKGEKDAIHAVNPETIETRFNRGDIELWRKISDELRQEHQSIAQHGKMVVVQRWSHFTVDMGLSKKMRTRVADLDARDYCCSHKPRNSSFCCIDLDSERIKAVDALILGTDVVLPHPSGSVFLFRYKENYGMSYCELPFFQPLSLKLKCIQVLKESVEIDPSYYRIKCCLKMQEELEKETAENLCTINIQQ
Protein: Gastrin [Cleaved into: Big gastrin (Gastrin-34) (G34); Gastrin] (P04563)
Organism: Rattus norvegicus (Rat)
Function: Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine.
Subcellular location: Secreted.
Interaction partners:
- Gastrin/cholecystokinin type B receptor
- Somatostatin
- Cholecystokinin
- Cholecystokinin receptor type A
- Secretin
- Potassium-transporting ATPase alpha chain 1
- Pancreatic polypeptide prohormone
- Potassium-transporting ATPase alpha chain 2
- Pro-glucagon
- Gastrin-releasing peptide
Sequence:
MPRLCVCMLVLVLALATFSEASWKPRSQLQDASSGPRTNGALEQHQLEKLGPASHHRRQLGPQGPQHFIADLSKKQRPPMEEEEEAYGWMDFGRRSAEEEDQYN
Protein: Ceramide glucosyltransferase (EC 2.4.1.80) (GLCT-1) (Glucosylceramide synthase) (GCS) (Glycosylceramide synthase) (UDP-glucose ceramide glucosyltransferase) (UDP-glucose:N-acylsphingosine D-glucosyltransferase) (O88693)
Organism: Mus musculus (Mouse)
Function: Participates in the initial step of the glucosylceramide-based glycosphingolipid/GSL synthetic pathway at the cytosolic surface of the Golgi. Catalyzes the transfer of glucose from UDP-glucose to ceramide to produce glucosylceramide/GlcCer (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine). Glucosylceramide is the core component of glycosphingolipids/GSLs, amphipathic molecules consisting of a ceramide lipid moiety embedded in the outer leaflet of the membrane, linked to one of hundreds of different externally oriented oligosaccharide structures. Glycosphingolipids are essential components of membrane microdomains that mediate membrane trafficking and signal transduction. They are implicated in many fundamental cellular processes, including growth, differentiation, migration, morphogenesis, cell-to-cell and cell-to-matrix interactions. They are required for instance in the proper development and functioning of the nervous system. As an example of their role in signal transduction, they regulate the leptin receptor/LEPR in the leptin-mediated signaling pathway. They also play an important role in the establishment of the skin barrier regulating keratinocyte differentiation and the proper assembly of the cornified envelope. The biosynthesis of GSLs is also required for the proper intestinal endocytic uptake of nutritional lipids. Catalyzes the synthesis of xylosylceramide/XylCer (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) using UDP-Xyl as xylose donor.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:10430909}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R0E0}.
Interaction partners:
- Beta-1,4-galactosyltransferase 6
- Lysosomal acid glucosylceramidase
- Ceramide kinase
- Sphingomyelin phosphodiesterase 2
- Non-lysosomal glucosylceramidase
- Sphingolipid delta
- Acid ceramidase
- Sphingomyelin phosphodiesterase
- Ceramide synthase 2
- Ceramide synthase 3
Sequence:
MALLDLAQEGMALFGFVLFVVLWLMHFMSIIYTRLHLNKKATDKQPYSKLPGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMPAYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEKVGLVHGLPYVADRQGFAATLEQVYFGTSHPRSYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRGWRFSMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVASLIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMTIYIFLSALWDPTISWRTGRYRLRCGGTAEEILDV
Protein: Cyclic dof factor 3 (Dof zinc finger protein DOF3.3) (AtDOF3.3) (H-protein promoter-binding factor 2a) (Q8LFV3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence (By similarity). Regulates a photoperiodic flowering response. Transcriptional repressor of 'CONSTANS' expression.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Adagio protein 3
Sequence:
MMMETRDPAIKLFGMKIPFPSVFESAVTVEDDEEDDWSGGDDKSPEKVTPELSDKNNNNCNDNSFNNSKPETLDKEEATSTDQIESSDTPEDNQQTTPDGKTLKKPTKILPCPRCKSMETKFCYYNNYNINQPRHFCKACQRYWTAGGTMRNVPVGAGRRKNKSSSSHYRHITISEALEAARLDPGLQANTRVLSFGLEAQQQHVAAPMTPVMKLQEDQKVSNGARNRFHGLADQRLVARVENGDDCSSGSSVTTSNNHSVDESRAQSGSVVEAQMNNNNNNNMNGYACIPGVPWPYTWNPAMPPPGFYPPPGYPMPFYPYWTIPMLPPHQSSSPISQKCSNTNSPTLGKHPRDEGSSKKDNETERKQKAGCVLVPKTLRIDDPNEAAKSSIWTTLGIKNEAMCKAGGMFKGFDHKTKMYNNDKAENSPVLSANPAALSRSHNFHEQI
Protein: LD03185p (Q8T0H5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMSCPIPMPMPISSLHKSEFEPVNIGVKRGSDELLSQAAVMAPASDNNNQDLATKKAKLEPGTVLAGGIAKASKVIHLRNIPNESGEADVIALGIPFGRVTNVLVLKGKNQAFIEMADEISATSMVSCYTVTPPQMRGRMVYVQFSNHRELKTDQGHNNSTAHSDYSVQSPASGSPLPLSAAANATSNNANSSSDSNSAMGILQNTSAVNAGGNTNAAGGPNTVLRVIVESLMYPVSLDILHQIFQRYGKVLKIVTFTKNNSFQALIQYPDANSAQHAKSLLDGQNIYNGCCTLRIDNSKLTALNVKYNNDKSRDFTNPALPPGEPGVDIMPTAGGLMNTNDLLLIAARQRPSLSGDKIVNGLGAPGVLPPFALGLGTPLTGGYNNALPNLAAFSLANSGALQTTAPAMRGYSNVLLVSNLNEEMVTPDALFTLFGVYGDVQRVKILYNKKDSALIQMAEPQQAYLAMSHLDKLRLWGKPIRVMASKHQAVQLPKEGQPDAGLTRDYSQNPLHRFKKPGSKNYQNIYPPSATLHLSNIPSSCSEDDIKEAFTSNSFEVKAFKFFPNKHIEP
Protein: Splicing factor PTSR1 interacting protein (Q38BV4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDAIPPEYDKDTKERIYRQEWLEYFNYIGWDRAVSEHPEQYYSIFPGGHHHALHNMNNGGSVMGDIMGKQENIGSIGVSAPILGNQRPAGGASYRAGILAPPVMTTASAAAKMFLDDGSSSGSDGDSRYSSRSSSSSSDASSLDGSKERDGEVNRGQRRYERAAEAGASEADTKKSASNRRRHRSGSGTKRRSRSRHRHRDKSRRRSTNNDKKSGRKRERSKDAEESRARRDDKPPRNEQKTGRRDERRERDNKHRSNDRDERRHHHHRSDKPHGSEHGRNRDRERDRERERDRDRGRERERERDRDRDWDRRKEKAPAGGGSSNGSRSHKGHYILHEGNDKFRGRGDGSISAGGDRYDDRREDARQRRQRDEGRYRR
Protein: Guanine nucleotide exchange factor MSS4 homolog (Guanine nucleotide exchange factor stratum) (Q9VLP3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Guanine-nucleotide-releasing protein that acts on members of the sec4/ypt1/rab subfamily such as Rab8. During egg development, essential for establishing and maintaining epithelial cell polarity by regulating the correct polarized deposition of basal membrane (BM) proteins such as trol/Pcan and vkg/Coll IV to the basal surface of follicular epithelial (FE) cells. Likely to function by restricting the activity of the vesicle transport regulator Rab8 to the basal membrane, and thus directs BM protein-containing vesicles to the basal side of the FE cells. This function is independent of the Crag/Rab10 regulation of polarized BM protein secretion in the FE.
Subcellular location: Basal cell membrane {ECO:0000269|PubMed:28228250}; Peripheral membrane protein {ECO:0000269|PubMed:28228250}. Note=Diffuse intracellular localization early in oogenesis which later becomes basally enriched in follicular epithelial cells. {ECO:0000269|PubMed:28228250}.
Interaction partners:
- AT17867p
- Cdc42 homolog
- FI01544p
- ADP-ribosylation factor 6
- Rho-type guanine nucleotide exchange factor, isoform F
- Chaperone Ric-8
- FI09914p
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
- Regulator of chromosome condensation
- LD44762p
Sequence:
MTEEADFSEQITDGKNKSNVRCQFCNCLMLKAQEGTYNQEEVDVPLMTQKQDRTADSLNSEPLKDFWLVKDMMTFENIGFSNTVDGRKFLVCADCERGPVGYHDLSTRHCYLALKRVVHKDT
Protein: Lipoprotein-releasing system transmembrane protein LolE (P75958)
Organism: Escherichia coli (strain K12)
Function: Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Lipoprotein-releasing system ATP-binding protein LolD
- Outer-membrane lipoprotein carrier protein
- Lipoprotein-releasing system transmembrane protein LolC
- Outer-membrane lipoprotein LolB
- Macrolide export ATP-binding/permease protein MacB
- Outer membrane lipoprotein RcsF
- Peptidoglycan-associated lipoprotein
- N-acetyl-D-glucosamine kinase
- Lipopolysaccharide export system ATP-binding protein LptB
- Outer membrane protein assembly factor BamA
Sequence:
MAMPLSLLIGLRFSRGRRRGGMVSLISVISTIGIALGVAVLIVGLSAMNGFERELNNRILAVVPHGEIEAVDQPWTNWQEALDHVQKVPGIAAAAPYINFTGLVESGANLRAIQVKGVNPQQEQRLSALPSFVQGDAWRNFKAGEQQIIIGKGVADALKVKQGDWVSIMIPNSNPEHKLMQPKRVRLHVAGILQLSGQLDHSFAMIPLADAQQYLDMGSSVSGIALKMTDVFNANKLVRDAGEVTNSYVYIKSWIGTYGYMYRDIQMIRAIMYLAMVLVIGVACFNIVSTLVMAVKDKSGDIAVLRTLGAKDGLIRAIFVWYGLLAGLFGSLCGVIIGVVVSLQLTPIIEWIEKLIGHQFLSSDIYFIDFLPSELHWLDVFYVLVTALLLSLLASWYPARRASNIDPARVLSGQ
Protein: Zinc finger (C3HC4-type RING finger) family protein (F4ICB5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSNEDSLPPFTLFGLDDVENYGLVTEADNSLPLDIHNQVFQLVEKGNQSFKESRFEEAISSYSKANSIKPLDPIVLGNRSAAYIRFGQYLKQRSASISEYKPLNGFDMSMLGELALKDADKLMSLQSSLVKSYITKACALMLLERYEVARDTILSGLQIDPFSGPLRSNLQELEKVMPNSMRKTHGMAERSDDFDCTVCLKLLYEPATTPCGHTFCRSCLFQSMDRGNKCPLCRTVIFMTPRTCAVSVTLNNIIEKNFPEEYAERKSEQDTLVHLGNESMPLFVMDVIIPCQKLSLHIFEPRYRLMVRRIMEGNHRMGMVALDSATGSPVDVACEVEITECDPLPDGRFVLELESHRRCRIVKAWDQDGYRVAEVEWVKDIPPQSEQGKADLRELTTSAASFARSWLDRAKEAARQGDRRRLEILLNVESMIPTPQDPERFSFWLATLTDRRPSERLELLRLQDTGEVLDYRLVQIARQISLFHQSLSFDC
Protein: Peroxisomal membrane protein 11C (Peroxin-11C) (AtPEX11c) (Q9LQ73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in peroxisomal proliferation. Promotes peroxisomal duplication, aggregation or elongation without fission.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:17220199, ECO:0000269|PubMed:20179140}; Multi-pass membrane protein {ECO:0000269|PubMed:17220199, ECO:0000269|PubMed:20179140}.
Interaction partners:
- Peroxisome biogenesis protein 19-1
- Mitochondrial fission 1 protein B
- Mitochondrial fission 1 protein A
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein 11B
- Peroxisome biogenesis protein 16
- Peroxisomal membrane protein 11A
- Peroxisome biogenesis protein 3-1
- Peroxisome biogenesis protein 19-2
- Peroxisome biogenesis factor 10
Sequence:
MSTLETTRAELGLVVVYLNKAEARDKICRAIQYGSKFLSDGQPGTAQNVDKNTSLARKVFRLFKFVNDLHALISPVPKGTPLPLVLLGKSKNALLSTFLFLDQIVWLGRTGIYKDKERAEILGRISLFCWMGSSVCTSLVEVGELGRLSASIKKLEKEIGNKDKHQNEQYRAKVEKSNERSLALIKAGMDVVVAFGLLQLAPKKVTPRVTGAFGFASSLISCYQLLPSHPKSKMV
Protein: Hydroxynaphthalene reductase arp2 (EC 1.1.-.-) (Conidial pigment biosynthesis oxidase arp2) (E9QUT3)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Hydroxynaphthalene reductase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall. The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA. The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening. 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone. The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN. 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone. Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN. Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin. DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize. DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins. DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses. DHN-melanin protects also conidia against amoeba predation.
Subcellular location: Endosome {ECO:0000269|PubMed:26972005}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase
- Fatty acid synthase subunit beta
- Fatty acid synthase subunit alpha
- Scytalone dehydratase arp1
- Conidial pigment polyketide synthase alb1
- Laccase abr2
- Multicopper oxidase abr1
- Heptaketide hydrolyase ayg1
Sequence:
MVNTCTYLPLSGKVALVTGGGRGIGAGIALELARRGASVAINYGHSAKSAQEVVEAIQAIGRQAVAIQADLTCVPNIESLIQEVVRHFGRLDIVVSNSGMEKFKPLEETTLEDFNEVFNLNTRAQMFVARYAYDHIQPGGRVILMSSIAAGLGVPGHALYAGSKAAIEGFTRCLAADFGRKGCTVNAIAPAGVKSDMWRENAWRYAPGCDKSSSLEEIETALASGSPLKRCGVPEDIGKVVSFLASPDAEWVNGEFFSPPPCKGPLPGGDLEC
Protein: Uncharacterized protein (Q383D1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Ubiquitin-like domain-containing protein
- Manganese/iron superoxide dismutase C-terminal domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MRRFCTARVSSYVKRAPLLLPRGGRRWRSGAGTTADGGGEKEYIADSFESTAGSNAYAAMELAAEARREIHELWLSAETALEREKRVQQVAALIEKYKLDPSTPREADVSRGLGDAFDRLLLLCLPLGKTDAKGTDNLERLMHLAGRNGRELSVRTIQHLFARTDSFAEALAVFYTMRRCHVAMNMEAYYSMLYSLQRLEEEGWGQHFRNEYEENGAPSEQAMDFIVKGISNALLPENKPWLGRVMFQDRNVPDRRYDTRDFDELDTAWTQRYKSGTPAGAH
Protein: Mediator of DNA damage checkpoint protein 1 (A0A1U9XBC1)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEDTQAIDWDVEEEEETEQSSESLRCNVEPVGRLHIFSGAHGPEKDFPLHLGKNVVGRMPDCSVALPFPSISKQHAEIEILAWDKAPILRDCGSLNGTQILRPPKVLSPGVSHRLRDQELILFADLLCQYHRLDVSLPFVSRGPLTVEETPRVQGETQPQRLLLAEDSEEEVDFLSERRMVKKSRTTSSSVIVPESDEEGHSPVLGGLGPPFAFNLNSDTDVEEGQQPATEEASSAARRGATVEAKQSEAEVVTEIQLEKDQPLVKERDNDTKVKRGAGNGVVPAGVILERSQPPGEDSDTDVDDDSRPPGRPAEVHLERAQPFGFIDSDTDAEEERIPATPVVIPMKKRKIFHGVGTRGPGAPGLAHLQESQAGSDTDVEEGKAPQAVPLEKSQASMVINSDTDDEEEVSAALTLAHLKESQPAIWNRDAEEDMPQRVVLLQRSQTTTERDSDTDVEEEELPVENREAVLKDHTKIRALVRAHSEKDQPPFGDSDDSVEADKSSPGIHLERSQASTTVDINTQVEKEVPPGSAIIHIKKHQVSVEGTNQTDVKAVGGPAKLLVVSLEEAWPLHGDCETDAEEGTSLTASVVADVRKSQLPAEGDAGAEWAAAVLKQERAHEVGAQGGPPVAQVEQDLPISRENLTDLVVDTDTLGESTQPQREGAQVPTGREREQHVGGTKDSEDNYGDSEDLDLQATQCFLENQGLEAVQSMEDEPTQAFMLTPPQELGPSHCSFQTTGTLDEPWEVLATQPFCLRESEDSETQPFDTHLEAYGPCLSPPRAIPGDQHPESPVHTEPMGIQGRGRQTVDKVMGIPKETAERVGPERGPLERETEKLLPERQTDVTGEEELTKGKQDREQKQLLARDTQRQESDKNGESASPERDRESLKVEIETSEEIQEKQVQKQTLPSKAFEREVERPVANRECDPAELEEKVPKVILERDTQRGEPEGGSQDQKGQASSPTPEPGVGAGDLPGPTSAPVPSGSQSGGRGSPVSPRRHQKGLLNCKMPPAEKASRIRAAEKVSRGDQESPDACLPPTVPEAPAPPQKPLNSQSQKHLAPPPLLSPLLPSIKPTVRKTRQDGSQEAPEAPLSSELEPFHPKPKIRTRKSSRMTPFPATSAAPEPHPSTSTAQPVTPKPTSQATRSRTNRSSVKTPEPVVPTAPELQPSTSTDQPVTSEPTSQVTRGRKSRSSVKTPETVVPTALELQPSTSTDRPVTSEPTSQATRGRKNRSSVKTPEPVVPTAPELQPSTSTDQPVTSEPTYQATRGRKNRSSVKTPEPVVPTAPELRPSTSTDRPVTPKPTSRTTRSRTNMSSVKTPETVVPTAPELQISTSTDQPVTPKPTSRTTRSRTNMSSVKNPESTVPIAPELPPSTSTEQPVTPEPTSRATRGRKNRSSGKTPETLVPTAPKLEPSTSTDQPVTPEPTSQATRGRTNRSSVKTPETVVPTAPELQPSTSTDQPVTPEPTSQATRGRTDRSSVKTPETVVPTAPELQASASTDQPVTSEPTSRTTRGRKNRSSVKTPETVVPAAPELQPSTSTDQPVTPEPTSRATRGRTNRSSVKTPESIVPIAPELQPSTSRNQLVTPEPTSRATRCRTNRSSVKTPEPVVPTAPEPHPTTSTDQPVTPKLTSRATRRKTNRSSVKTPKPVEPAASDLEPFTPTDQSVTPEAIAQGGQSKTLRSSTVRAMPVPTTPEFQSPVTTDQPISPEPITQPSCIKRQRAAGNPGSLAAPIDHKPCSAPLEPKSQASRNQRWGAVRAAESLTAIPEPASPQLLETPIHASQIQKVEPAGRSRFTPELQPKASQSRKRSLATMDSPPHQKQPQRGEVSQKTVIIKEEEEDTAEKPGKEEDVVTPKPGKRKRDQAEEEPNRIPSRSLRRTKLNQESTAPKVLFTGVVDARGERAVLALGGSLAGSAAEASHLVTDRIRRTVKFLCALGRGIPILSLDWLHQSRKAGFFLPPDEYVVTDPEQEKNFGFSLQDALSRARERRLLEGYEIYVTPGVQPPPPQMGEIISCCGGTYLPSMPRSYKPQRVVITCPQDFPHCSIPLRVGLPLLSPEFLLTGVLKQEAKPEAFVLSPLEMSST
Protein: Cofilin (Actin-depolymerizing factor 1) (Q6FV81)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus matrix {ECO:0000250}. Note=Throughout the cytoplasm (but not on the cytoplasmic cables) and major component of the cortical actin cytoskeleton. {ECO:0000250}.
Interaction partners:
- Actin
- Profilin
- Adenylyl cyclase-associated protein
- Coronin
- F-actin-capping protein subunit beta
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- NEDD8-conjugating enzyme UBC12
- Actin-related protein 3
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MSRSGVAVADESIQAFNDLKLGMKYKFVLFSLNDAKTEIVVKETSSDPSYDAFLEKLPENDCLYAVYDFEYQISESEGKRSKIVFFTWSPDTASVRPKMVYASSKDALKRALNGVAIEIQGTDFSEVSYEAVLEKVSRGAGSH