wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-binding protein, putative (Q38AL7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Spliceosome-associated protein, putative
- Splicing factor 3B subunit 1, putative
- PRP1 splicing factor N-terminal domain-containing protein
- PHD finger-like domain-containing protein 5A
- Uncharacterized protein
- Splicing factor 3B subunit 10
- RNA-binding protein, putative
- Sm protein G
- Small nuclear ribonucleoprotein E
- U2 small nuclear ribonucleoprotein B, putative
Sequence:
MSDERILLVTGIPTKLCRGEELYKVFGNYGTIQQLRIGSDASTKGCAIVVYELCEAASAALEALHDFKVDRDRHLRVSVYDETRDRRALERRKRRREMKAEYSRNIASASAEVKAED
Protein: Secreted transmembrane peptide 9 (Peptide ARACIN 2) (Phytocytokine ARACIN2) (Mature form of ARACIN2) (mARACIN2) (Phytocytokine STMP3) (Precursor of secreted transmembrane peptide 9) (Q9FIW1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation (By similarity). Inhibits the fungal growth of Alternaria brassicicola, Sclerotinia sclerotiorum, Fusarium graminearum, yeast (Saccharomyces) and Botrytis cinerea, thus being an antimicrobial peptide (AMP). Prevents global growth and development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Endoplasmic reticulum {ECO:0000269|PubMed:25593351, ECO:0000269|PubMed:31001913}. Golgi apparatus {ECO:0000269|PubMed:31001913}. Note=Observed in a reticular pattern and a perinuclear ring (PubMed:25593351, PubMed:31001913). The precursor of STMP9 accumulates at the plasma membrane and is proteolytically cleaved to release the STMP9 in the apoplasm (PubMed:31001913). {ECO:0000269|PubMed:25593351, ECO:0000269|PubMed:31001913}.
Interaction partners:
Sequence:
MAMKNTSHVLLLSLLLCLMFVIGLVEASIPDDDMGPAIYTPPSGSCGAPISKYDFQVLAKRPPPCRRPRLENTEDVTHTTRP
Protein: Allantoicase (EC 3.5.3.4) (Allantoate amidinohydrolase) (Q54VL5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
Interaction partners:
- Probable allantoinase 2
- Probable allantoinase 1
- Leucine aminopeptidase
- Uricase
- General transcription factor 3C polypeptide 5
- Large ribosomal subunit protein eL42
- rRNA-processing protein FCF1 homolog
Sequence:
MVYANNNIDPNAPCYVSECAELLSDKVGGVVLGCTDQWFAECVNLIKHSAPVWDAEKYVDTGKWMDGWETKRHNPDHDWCIIKLGIPGVIYGFEIDTAYFTGNYPPHASIEALCDDSDPNFNTLKESNNWEVILNKSDLGSSCKKYFECKVEKRFTHIKFRIYPDGGVARLRAYGRVVKDWTLVIPGELVDLAAIENGGLVTQVSDHFYGNKNNIIMPGRSVNMGDGWETKRRRGPGNDWLTVKLAKEGIVKRIEVDTNWFKGNFPTSCSIDAIHSSSAPDETHLQDYEWTNILPNSPLCGHRRHFFQNELVNNDKPFTHIRLNIFPDGGVSRLRINCSLPDSKNNNNNNNNNNNNNTSNSFKTSDRQQ
Protein: FI20237p1 (Miles to go, isoform F) (Q9VJJ9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVRLNVAEQHSSSNNNGNISNSSISNTNGTIITSNNNAGGSCSSTTSSTTSLNSNPASPACTMVMLPAPQQHLLVQQQQQQQQQQQQQQQPQQPPPQLQQQHGPQQQQQQQQQQHSPSDGGSSNCSLPASPPLLQQTATPPQGAQIVPPVCALHHPQQQLALMAAMQHHHHLPPPHALHHAPLPPPPPNLPPPHENGHGGGGSGVAVGGGGISPNGGGGSSASSVSSLSSGSGGSGGQVNGLSNGTNGIAPLPPGQLYIQYPGEFYPPEYYIAPHPHEGICPQHPHHPHPHHHQPMCAMSTEYGPAVQMVSQNRPPPPMPVPVQVPQYVNENGTLTHVMLSPQQYQQLHPGQGHLHPAPFISANGTSHFYTPVAGYPGPGPAGNGPPHYHLPPPPPPQQQQQQPPQQPQQQAPQGPPPPQQQQQQQQQVAPPAVQGAPSTGSVGAAQGAPATATATHTHAHSHSHSHAHSHTHPQPHAHSPHSPSPPNYRDERSQRQHNKLLRKLEKQRESNPPHSPSPRRANELNGHNNNNIPPGVPLPGHLNNHHHAVNHQGRRLPQQHQGQAHQVAQQQQSQARNGNPQHPQRAGSSVGGASSVGTSEDGEDNSSLAGDDEEEYHRENSIIEQISAIEKPEVIDVTSRAAKIIWESPAIANTVTVDMRQLRYQVLLCDSGKQCKYKSLYQGEAYECIVQDLQPGQDYLVRLQVHYQKLTGTVSDPTEFRTPPCEPDQPPPPKLVSRTKNSINLRWAAPAANGASIQHYLLEYDEGRMPGQPQKFVELAKIKAKHYVIGKLQPTTVYSFRLAAVNEAGQSPYSPVASYSTSGNPPPVPKPPQLLASSSSSLKLGWERRAQDGDFLLQLQDAETGHGFLNTYKGTELQTECLQLRRASSYQFRLRSENEAGFSPWSPEVSYRTLAERPGRPGKPHAKGKIHGTQFKARWDAPSDSGGAEILCYHLELSAAGPAFERIYSGAETEAMCERLQPGTTYALRACCEGPAGQSPYSDIGHVTTEAVPPSAPPPPHCSDPPSPYAALLKLRPPEYNGGAPILEFEAQMRRLEQVQPPQLVYRGKQTYFVAQDLTPGGMYETQVRAINRIGAGSWSQWMRFTAAAAAPGVPEELRVLVKSATHLGVSWQPPLQENGAPVTSYTLKSASQERKEDDSEEEVKEPPSSEFHNCYQGPQTCAELRNLSPYTRYHFRIQASNSAGTGNSSDVISVCTPAAVPGAPQMQGYEFTAQEVTLNWTQPAAHGSPICSYNIEYGERTIATPDACTRYTVSGLMPETGYKFRVQAVNAIGAGAFSAYAKLTTQPAPPAPPRLECSGAGHNYIKLKWGENGNGKVVNSNPSGNGGDFTKYFVEMYVARAKQFQAVYSGTNCMCKVHKLQERSSYTFRIYAHTDRAGDGDYSEEFVFETSATLPANIKPPRVVQEGSVCLMELPGQLGMQLTLEWQHSKNSFNDRVEYELQYAVLGAAELEGESLSPKGRSSSSSGSSNGAPINLPNHDYRQLYRGPETKFTIDNLAAGTCYQFRVCPVRIAAGGELLYGQPSSPLRYQVPSELDPSSATCHHHLHGSTATPAMASSQRSSRKLSAGNGSTNGLHMRSVSASAISGASGVGADPVAIGRLQQELSGFNACADPQHHHHHHHHHHHQPCGGGVGGAGGISGATDSHHQHQHHMHHSHHMHHAHHPHTGMGGSSSNSSSSTAAAISSSLAQAGGLRRIVCKVTSLYSNRRRLSDQQKAVCIVVSFLVGTFLVAMLVNMLRG
Protein: Alpha,alpha-trehalose-phosphate synthase subunit Tps2, putative (EC 2.4.1.15) (Q4WWF5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Alpha,alpha-trehalose phosphate synthase subunit TPS3, putative
- Alpha,alpha-trehalose phosphate synthase subunit, putative
- Trehalase
- Alpha,alpha-trehalose-phosphate synthase 2
- Alpha,alpha-trehalose-phosphate synthase 1
- Glycogen [starch] synthase
- alpha,alpha-trehalose-phosphate synthase
- alpha,alpha-trehalose-phosphate synthase
- UTP--glucose-1-phosphate uridylyltransferase
- Alpha-glucosidase
Sequence:
MAANQDTPTKVPDGQPNPVMVGPGMKSLGEEAYTNASNATPSLETDKKHPLVNDAPSYFSQVPGTKQSSTVSDTALPGSPADAARDAKSPIELLRRLSLGRSPMIPDVDPREQYPGLNLTGRIISAAFCIPYKVGYRPGSDWDLKPRPGTSALFDSFAYLGSGETKWSHTLVGWTGEVEPIQDVSVPLQHIPVSSGARLPPALNGVAVPLNKAAAPVPVDSKQRPPSHPLLEGFRVSQEDRARLDAQLSSGRYGKIAPVWLSDESEEPEESSIFLEDQGRWRRYAEKELYPLLHYKQHGPTDGRSERKWWGDYVRMNRLFADRIIEEYQEGDIVWIHDYHLFLLPSLLRQRIPNIYIGFFLHAPFPSSEFMRCLAKRKEVLTGVLGANMIGFQTFSYSRHFSSCCTRVLGFDSNNAGVDAYGAHVAVDVFPIGIDVKAIQKAAYGYPEIEEAVVGLRTLYAGKKIIVGRDRLDSVRGVAQKLQAFEQFLERYPEWREKVVLIQVTSPTSVEEEKEDPENKIASQISNLVSTINGRFGSISFSPVKYYPQYLSQHEYFALLRVADVGLITTVRDGMNTTSLEYILCQHNTHGPLILSEFSGTAGTLSSAIHINPWDTTGVAEAINRALTMSPEEKKAQHVKLYKHVTTNTISTWSNHFVTRLLTNLSSFDQSVATPALDRAKLLKQYRKARKRLFMFDYDGTLTPIVKDPQAAIPSDRVLRTLKTLAADPRNAVWIISGRDQAFLDEWMGHIPELGLSAEHGCFIRQPRSDDWENLAESSDMGWQKEVMEVFQHFTERTQGSFIERKRVALTWHYRRADPEYGAFQARECRKMLEETVAKRWEVEVMAGKANLEVRPTFVNKGFIAARLVQEYGTDPAQAPEFVLCLGDDFTDEDMFRALKKSGLPAGHVFSVTVGASSKQTEASWHLLEPADVIGTISMLNNSSSAQEY
Protein: Ammonium transporter 2 (Q9BLG3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Ammonium transporter that mediates the excretion of ammonium from the prestalk cells from the slug. Controls ammonium homeostasis during growth and development. Ammonium has been shown to function as a morphogen at multiple steps during the development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19108721}; Multi-pass membrane protein {ECO:0000269|PubMed:19108721}. Endosome membrane {ECO:0000269|PubMed:19108721}; Multi-pass membrane protein {ECO:0000269|PubMed:19108721}. Lysosome membrane {ECO:0000269|PubMed:19108721}; Multi-pass membrane protein {ECO:0000269|PubMed:19108721}. Contractile vacuole membrane {ECO:0000269|PubMed:19108721}; Multi-pass membrane protein {ECO:0000269|PubMed:19108721}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:19108721}; Multi-pass membrane protein {ECO:0000269|PubMed:19108721}.
Interaction partners:
- Type-1 glutamine synthetase 1
- Acetyl-CoA hydrolase
- Rhesus-like glycoprotein B
- Cytochrome b5 reductase
- Cytochrome b5 heme-binding domain-containing protein
Sequence:
MEYLELNGTKEGLSAAVDDMWVLNATYLVFYMQAGFCMLEAGVVRAKNAKSIIMKSIIDTAIGSLLFWALGFGLAFGNADKASNPVIGTSHFFLINYQNLSFFAFQWAFCATSITIVSGSLAERVHVTSCLVYTIVMSAFIYPLSAHWVWSYNGWLRMIGFNGIIDFSGSIVVHIVGGCIGLVGTYLVGPRIGRFDSESGKPKPLPGHSITIYTLGAFIIWYGFYGFNTGSTLGISGGGIAIASRSAVTMTIIACASCATTLLAIKIKSGKYDVVKSVNSLLGGLVSSAAVCSLIDPWAAFIIGCVTSFVYLGCSHLLIKLRIDDPLDSSAIHLGCGIWGALSVGLFSTQENLSLVLKKSTNVYGLFFGGGFEQLGIQLLGIIIVMAWCFFCASILFTILKKFHLLRIEPTKELMGIDIDSAGGPAYQWDN
Protein: Putative serine acetyltransferase (EC 2.3.1.30) (Q9US33)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cysteine synthase 1
- Homocysteine synthase
- Cysteine synthase 2
- Tryptophan synthase
- Serine hydroxymethyltransferase, mitochondrial
- Probable phosphoserine phosphatase
- Homoserine dehydrogenase
- Threonine dehydratase, mitochondrial
- Homoserine kinase
- Serine racemase
Sequence:
MTVQTAERTITLVQAIWPKLRKEAEKQCEVNPWLAKDLARKILSKKTLRESLSCVLALPLDHVTGSSESMENWFYSILGLNDEKIIRSAMIDLDRLYTTNPACPDLISAFLSFRGFHALQLYRIAHGLWSEGDKTSAVLVQNWTAVAYGVDIHPAASIGDGLFLDHALGIVIGETAIVEDGVSIWHNVTLGSTFKDSGARHPVIRKNAMLCTGATVLGRVEVGENAVVAAGALVTKDVAPNRLALGSPARDVGPVPQYFGALTNPNCTNK
Protein: Hevein-like preproprotein [Cleaved into: CB-HEL; CD-HEL (EC 3.1.-.-) (RNase)] (P43082)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Fungal growth inhibitors. Neither CB-HEL nor CD-HEL have chitinase activity, but both have antimicrobial activities. CD-HEL has RNase, but no DNase activity.
Subcellular location: Vacuole {ECO:0000269|PubMed:22868784}. Note=associated with the tonoplast.
Interaction partners:
- Pathogenesis-related protein 5
- Defensin-like protein 16
- CAP superfamily protein
- Pathogenesis-related protein 1
- Pathogenesis-related protein 1
- Glucan endo-1,3-beta-glucosidase, acidic isoform
- Pathogenesis-related protein 1
- Regulatory protein NPR1
- Lipoxygenase 2, chloroplastic
- Pathogenesis-related protein 1
Sequence:
MKIRLSITIILLSYTVATVAGQQCGRQGGGRTCPGNICCSQYGYCGTTADYCSPTNNCQSNCWGSGPSGPGESASNVRATYHFYNPAQNNWDLRAVSAYCSTWDADKPYAWRSKYGWTAFCGPAGPRGQASCGKCLRVKNTRTNAAVTVRIVDQCSNGGLDLDVAMFNQIDTDGFGYQQGHLIVDYQFVDCGNELIGQPDSRNMLVSAIDRV
Protein: HNH nuclease domain-containing protein (O53196)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- Uncharacterized protein Rv2468c
- Probable alpha-glucosidase AglA
- Group 2 truncated hemoglobin GlbO
Sequence:
MAHGKKRRGHRSSGVAAGVTGPASCLHSVHSHRLASGVETHPPNRHESASIWNRRRVLLLNSTYEPLTALSMRRAIVMVICGKADVVHEDPSGPVIHSATRSILVPSVIQLRSYVRVPYRARVPMTRAALMHRDRFCCAYCGGKADTVDHVVPRSRGGAHSWENCVACCSPCNHRKGDRLLTELGWALRRAPLPPTGPHWRLLSAVKELDPSWARYLGEGAA
Protein: DNA-directed RNA polymerase I subunit RPA12 (DNA-directed RNA polymerase I subunit H) (Zinc ribbon domain-containing protein 1) (Q9P1U0)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors.
Subcellular location: Nucleus, nucleolus {ECO:0000305|PubMed:34887565}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerase I subunit RPA34
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerases I and III subunit RPAC1
Sequence:
MSVMDLANTCSSFQSDLDFCSDCGSVLPLPGAQDTVTCIRCGFNINVRDFEGKVVKTSVVFHQLGTAMPMSVEEGPECQGPVVDRRCPRCGHEGMAYHTRQMRSADEGQTVFYTCTNCKFQEKEDS
Protein: Nuclear pore complex protein Nup214 (214 kDa nucleoporin) (Nucleoporin Nup214) (Q80U93)
Organism: Mus musculus (Mouse)
Function: Part of the nuclear pore complex. Has a critical role in nucleocytoplasmic transport. May serve as a docking site in the receptor-mediated import of substrates across the nuclear pore complex.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P35658}. Note=Cytoplasmic side of the nuclear pore complex. {ECO:0000250|UniProtKB:P35658}.
Interaction partners:
- Nuclear pore complex protein Nup98-Nup96
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup88
- Exportin-1
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup153
- Nuclear pore complex protein Nup85
- Nucleoporin SEH1
- Nuclear pore glycoprotein p62
Sequence:
MGDEMDAMIPEREMKDFQFRALKKVRIFDSPEELPKERSSVLTISNKYGMLFAGGTNGLNVFPTKSLLIQNKPGDDPNKIVDTIQGLNVPMKFPVHHLALSCDSLTLSACMMSSEYGSIIAFFDVRTFSNQAKPLKRPFTYHKVSNDASGMVNDMKWNPTVPSMVAVCLADGSISVLQVTDVVKVCATLPPSTGVTCVCWSPKGKQLAVGKQNGTVVQYLPTLQEKKVIPCPPFYESDHPVRVLDVLWIGTYVFTIVYAGADGTLETCPDVVMALLPKKEEKHPEIFVNFMEPCYSSCTERQHHYYLSYIEEWDLVLAASAASTEVSILARQNDQTNWESWLLEDSSRAELPVTDKSDDSLPMGVAIDYTNEVEVTINEEKTLPPAPVLLLLSTDGVLCPFYMINQNPGVRSLIKTLELISTEGERQPKSSGSFPGTPSSPQAPQNLDAPATASSPLPPVSAAPTSTFPMPSAAGSPSVFSFGPSSFKSSASVTGEPPLYPTGSDSSRAAPGSGTSTFSFAPPSKGSLASTPAVAPVATSAAPFTFGFKPTLESTPMSSTPNTGMKPSFPPSASSVKVNLNEKFTAVASSAPVHSSTSTPSVLPFSSSPKPTASGPLSHPTPLPASSSSMPLKSSVSPSPAAGRSTQTAPSSAPSTGQKSPRVNPPVPKSGSSQAKALQPPVTEKQRPQWKDSDPVLAGIGEEIAHFQKELEELKARTAKACLQVGTSEEMKMLRTESDDLHTFLFEIRETTESLHGDISTLKTTLLEGFAGVEEAREQHGRNHDSGYLHLLYKRPLDPKSEAQLQEIRRLHQYVKFAVQDVNDVLDLEWDRHLEQKKRQRRLIVPERETLFNTLANNREIINQQRKRLNQLVDSLQQLRLYNHTAPWSLPSALSTQSNSHSFDSDLECLLKTTIESHTKPSPRVPGKLSPAKQAQLRNFLAKRKTPPVRSTAPASLSRSAFLSQRYYEDLDEGSSASSVAQPLEGEDARPTCTSVAQPLEGEDAQPICKEEEAVVPVPRHAPVVRTPSIQPSLLPQSMPFAKPHLIHSSSPAVMSSAVSTSATKVIPQGADSTMLATKTVKHGAPGPSHTVAAPQAAAAAALRRQMASQAPAMSTLTESTLKTVPQVVNVQELRSNPSPPSAAMGSAVQHSAAKTPHAVLTPVANSQAKQGSLINSFKPSGPTAASCQLSSGDKAVGQGTAKTESAATSTPSAAGQLNKPFSFASPGTFTFGTITPTPSSSFTATPGAGPPTKEPTQLEAFSFGGGGKPFSEAIPGNSPATGATSAPSTSVTAASLEDSAPSSSKPAAPPETTVSSASSKLETPPSKLGELLFPSSLAGETLGSFSGLRVGQAEDSTKPVSKASSTNLAGAQPAKPSGVSFPNTSVLGKPVEPAVTSSVSPAPAAPASALNVSTSSSSATVFGSVPLTSAGPPGLISFGGAALASSKASFSFGNQQTSSSTASSATPTSTSVAPSLPASFPTLSFGGLLSSPSASSLPVSSGKSTEEAAPPAVPDKSDSSEVSATTPSLPVQPQSTQASLQTSDPVKKEPVLVQTTDSSPSRPASSASFVASTESMPVTLGAPDSKIEAVSPASTFAGPGQAAVATAVLPGAGSAATEASGTPTTSTVSSSSPTSATETAVFGTATSGSSVFTQPPAASSSSAFSQLSSNTATAPSATPVFGQVAASITSTAAATPQASSSGFGSPAFGASAPGVFGQTAFGQTPAFGQATSSPASGFSFSQPGFSSVPAFGQSVSSTPASTSANVFGATSSTSSPGSFSFGQASTNTGGTLFGQNNPPAFGQSPGFGQGSSVFGGTSATTSTAAPSGFSFCQASGFGSSNTGSVFGQAANTGGSVFGQSSTSSGGVFGSGNATRGGGFFSGLGGKPSQDAANKNPFSSAGGGFGSTAAPNTSNLFGNSGAKTFGGFGSSSFGEQKPAGTFSSGGGSVASQGFGFSTPNKTGGFGAAPVFGSPPTFGGSPGFGGVPAFGSAPAFTSPLGSTGGKVFGEGTAAASAGGFGFGSSGNTASFGTLASQNAPTFGSLSQQTSGFGTPSSGFAGFGSGTGAFTFGSSNSSVQGFGGWRS
Protein: Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase) (Q9Z2A7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Highly expressed in epithelial cells of the small intestine and its activity is essential for the absorption of dietary fats (By similarity). In liver, plays a role in esterifying exogenous fatty acids to glycerol, and is required to synthesize fat for storage. Also present in female mammary glands, where it produces fat in the milk (By similarity). May be involved in VLDL (very low density lipoprotein) assembly (By similarity). In contrast to DGAT2 it is not essential for survival. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders. Exhibits additional acyltransferase activities, includin acyl CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax diester synthases. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20876538}; Multi-pass membrane protein {ECO:0000269|PubMed:20876538}.
Interaction partners:
- Diacylglycerol O-acyltransferase 2
- Patatin-like phospholipase domain-containing protein 2
- 2-acylglycerol O-acyltransferase 1
- 2-acylglycerol O-acyltransferase 2
- Phosphatidate phosphatase LPIN1
- Phospholipid phosphatase 2
- Acyl-CoA wax alcohol acyltransferase 2
- Phosphatidate phosphatase LPIN2
- Phosphatidate phosphatase LPIN3
- 1-acylglycerol-3-phosphate O-acyltransferase Pnpla3
Sequence:
MGDRGGAGSSRRRRTGSRVSVQGGSGPKVEEDEVRDAAVSPDLGAGGDAPAPAPAPAHTRDKDGRTSVGDGYWDLRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPAPCVIIASNIFVVAAFQIEKRLAVGALTEQMGLLLHVVNLATIICFPAAVALLVESITPVGSVFALASYSIMFLKLYSYRDVNLWCRQRRVKAKAVSTGKKVSGAAAQQAVSYPDNLTYRDLYYFIFAPTLCYELNFPRSPRIRKRFLLRRVLEMLFFTQLQVGLIQQWMVPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWFFHSCLNAVAELLQFGDREFYRDWWNAESVTYFWQNWNIPVHKWCIRHFYKPMLRHGSSKWVARTGVFLTSAFFHEYLVSVPLRMFRLWAFTAMMAQVPLAWIVGRFFQGNYGNAAVWVTLIIGQPVAVLMYVHDYYVLNYDAPVGV
Protein: Fidgetin-like protein 1 (EC 3.6.4.-) (Q6PIW4)
Organism: Homo sapiens (Human)
Function: Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation. May play a role in the control of male meiosis dynamic (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:23754376}. Cytoplasm {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8BPY9}. Note=Together with RAD51 and a subset of H2A histone proteins, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) treatment (PubMed:23754376).
Interaction partners:
- DNA repair-scaffolding protein
- DNA repair protein RAD51 homolog 1
- Fanconi anemia group M protein
Sequence:
MQTSSSRSVHLSEWQKNYFAITSGICTGPKADAYRAQILRIQYAWANSEISQVCATKLFKKYAEKYSAIIDSDNVESGLNNYAENILTLAGSQQTDSDKWQSGLSINNVFKMSSVQKMMQAGKKFKDSLLEPALASVVIHKEATVFDLPKFSVCGSSQESDSLPNSAHDRDRTQDFPESNRLKLLQNAQPPMVTNTARTCPTFSAPVGESATAKFHVTPLFGNVKKENHSSAKENIGLNVFLSNQSCFPAACENPQRKSFYGSGTIDALSNPILNKACSKTEDNGPKEDSSLPTFKTAKEQLWVDQQKKYHQPQRASGSSYGGVKKSLGASRSRGILGKFVPPIPKQDGGEQNGGMQCKPYGAGPTEPAHPVDERLKNLEPKMIELIMNEIMDHGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVINLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREASLGPIRSLQTADIATITPDQVRPIAYIDFENAFRTVRPSVSPKDLELYENWNKTFGCGK
Protein: HVA22-like protein a (AtHVA22a) (Q9S7V4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein
Sequence:
MGSGAGNFLKVLLRNFDVLAGPVVSLVYPLYASVQAIETQSHADDKQWLTYWVLYSLLTLIELTFAKLIEWLPIWSYMKLILTCWLVIPYFSGAAYVYEHFVRPVFVNPRSINIWYVPKKMDIFRKPDDVLTAAEKYIAENGPDAFEKILSRADKSKRYNKHEYESYETMYGEGYQY
Protein: UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (UDP-3-O-(3-OHC14)-GlcN N-acyltransferase) (EC 2.3.1.191) (Protein FirA) (Rifampicin resistance protein) (UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase) (P21645)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Prefers (3R)-3-hydroxytetradecanoyl-ACP over (3R)-3-hydroxyhexadecanoyl-ACP as the acyl donor in vitro, which is consistent with the structure of E.coli lipid A that contains over 95% (R)-3-hydroxytetradecanoate at the 2 and 2' positions.
Interaction partners:
- Lipid-A-disaccharide synthase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
- UDP-2,3-diacylglucosamine hydrolase
- Chaperone protein Skp
- Tetraacyldisaccharide 4'-kinase
- Lipid A biosynthesis lauroyltransferase
- 3-deoxy-D-manno-octulosonic acid transferase
- Outer membrane protein assembly factor BamA
Sequence:
MPSIRLADLAQQLDAELHGDGDIVITGVASMQSAQTGHITFMVNPKYREHLGLCQASAVVMTQDDLPFAKSAALVVKNPYLTYARMAQILDTTPQPAQNIAPSAVIDATAKLGNNVSIGANAVIESGVELGDNVIIGAGCFVGKNSKIGAGSRLWANVTIYHEIQIGQNCLIQSGTVVGADGFGYANDRGNWVKIPQIGRVIIGDRVEIGACTTIDRGALDDTIIGNGVIIDNQCQIAHNVVIGDNTAVAGGVIMAGSLKIGRYCMIGGASVINGHMEICDKVTVTGMGMVMRPITEPGVYSSGIPLQPNKVWRKTAALVMNIDDMSKRLKSLERKVNQQD
Protein: Black, isoform C (EC 4.1.1.-, EC 4.1.1.11, EC 4.1.1.15) (X2J8B3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLANAANNNNNNNNNITSTKDDLSSFVASHPAAEFEGFIRACVDEIIKLAVFQGTNRSSKVVEWHEPAELRQLFDFQLREQGESQDKLRELLRETIRFSVKTGHPYFINQLYSGVDPYALVGQWLTDALNPSVYTYEVAPLFTLMEEQVLAEMRRIVGFPNGGQGDGIFCPGGSIANGYAISCARYRHSPESKKNGLFNAKPLIIFTSEDAHYSVEKLAMFMGFGSDHVRKIATNEVGKMRLSDLEKQVKLCLENGWQPLMVSATAGTTVLGAFDDLAGISEVCKKYNMWMHVDAAWGGGALMSKKYRHLLNGIERADSVTWNPHKLLAASQQCSTFLTRHQQVLAQCHSTNATYLFQKDKFYDTSFDTGDKHIQCGRRADVFKFWFMWKAKGTQGLEAHVEKVFRMAEFFTAKVRERPGFELVLESPECTNISFWYVPPGLREMERNREFYDRLHKVAPKVKEGMIKKGSMMITYQPLRQLPNFFRLVLQNSCLEESDMVYFLDEIESLAQNL
Protein: Solute carrier family 35 member F1 (Q5T1Q4)
Organism: Homo sapiens (Human)
Function: Putative solute transporter.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:34269178}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MIPPEQPQQQLQPPSPAPPNHVVTTIENLPAEGSGGGGSLSASSRAGVRQRIRKVLNREMLISVALGQVLSLLICGIGLTSKYLSEDFHANTPVFQSFLNYILLFLVYTTTLAVRQGEENLLAILRRRWWKYMILGLIDLEANYLVVKAYQYTTLTSIQLLDCFVIPVVILLSWFFLLIRYKAVHFIGIVVCILGMGCMVGADVLVGRHQGAGENKLVGDLLVLGGATLYGISNVWEEYIIRTLSRVEFLGMIGLFGAFFSGIQLAIMEHKELLKVPWDWQIGLLYVGFSACMFGLYSFMPVVIKKTSATSVNLSLLTADLYSLFCGLFLFHYKFSGLYLLSFFTILIGLVLYSSTSTYIAQDPRVYKQFRNPSGPVVDLPTTAQVEPSVTYTSLGQETEEEPHVRVA
Protein: Cytochrome c-type protein NapC (P0ABL5)
Organism: Escherichia coli (strain K12)
Function: Mediates electron flow from quinones to the NapAB complex.
Subcellular location: Cell inner membrane; Single-pass membrane protein.
Interaction partners:
- Ferredoxin-type protein NapH
- Periplasmic nitrate reductase, electron transfer subunit
- Periplasmic nitrate reductase
- Ferredoxin-type protein NapG
- Ferredoxin-type protein NapF
- Chaperone NapD
- Cytochrome c-552
- Heme exporter protein B
- Cytochrome c biogenesis ATP-binding export protein CcmA
- Cytochrome c-type biogenesis protein CcmE
Sequence:
MGNSDRKPGLIKRLWKWWRTPSRLALGTLLLIGFVGGIVFWGGFNTGMEKANTEEFCISCHEMRNTVYQEYMDSVHYNNRSGVRATCPDCHVPHEFVPKMIRKLKASKELYGKIFGVIDTPQKFEAHRLTMAQNEWRRMKDNNSQECRNCHNFEYMDTTAQKSVAAKMHDQAVKDGQTCIDCHKGIAHKLPDMREVEPGF
Protein: CDGSH iron-sulfur domain-containing protein NEET (At-NEET) (Q9FLI7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important role in plant development, senescence, reactive oxygen homeostasis, and iron metabolism. Acts as an iron-sulfur transfer protein.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:22562611}. Mitochondrion {ECO:0000269|PubMed:22562611}.
Interaction partners:
- DET1- and DDB1-associated protein 1
- DNA damage-binding protein 1b
- DNA damage-binding protein 1a
- Splicing factor, CC1-like protein
- Bifunctional monothiol glutaredoxin-S16, chloroplastic
- Ferritin-3, chloroplastic
- Solute carrier family 40 member 3, chloroplastic
- Monothiol glutaredoxin-S14, chloroplastic
- Ferritin-4, chloroplastic
- Protein MITOFERRINLIKE 1, chloroplastic
Sequence:
MAIIASTFGTGLSYAGELPFKPVTGGEVGRKQQRMVVVRAEGGGGINPEIRKNEDKVVDSVVVTELSKNITPYCRCWRSGTFPLCDGSHVKHNKANGDNVGPLLLKKQ