wanglab/gogpt-training-data huggingface dataset:
Protein: Gliding motility protein MglB (Q1DB03)
Organism: Myxococcus xanthus (strain DK1622)
Interaction partners:
- Mutual gliding-motility protein MglA
- GTP-binding protein
- Gliding motility protein
- GTPase
- Uncharacterized protein
- Uncharacterized protein
- PatA-like N-terminal domain-containing protein
- PatA-like N-terminal domain-containing protein
- PatA-like N-terminal domain-containing protein
- PatA-like N-terminal domain-containing protein
Sequence:
MGTQLVMYEEEFTKINAVCDRLTKDANAKVVFLVDKNGQLISSAGQTQNIDTTSLASLTAGNVAAMGGLAKLIGENEFPNQFHEGAKDSLYMTIVGSRVVLVVIFDNRTSLGLVRLRIKKASDELTKIFESLVKKTDSPGAGSPFAEISDDDIDNLFSE
Protein: R-spondin-4 (Roof plate-specific spondin-4) (hRspo4) (Q2I0M5)
Organism: Homo sapiens (Human)
Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Leucine-rich repeat-containing G-protein coupled receptor 4
- Leucine-rich repeat-containing G-protein coupled receptor 6
- E3 ubiquitin-protein ligase ZNRF3
- E3 ubiquitin-protein ligase RNF43
- Leucine-rich repeat-containing G-protein coupled receptor 5
- Furin
Sequence:
MRAPLCLLLLVAHAVDMLALNRRKKQVGTGLGGNCTGCIICSEENGCSTCQQRLFLFIRREGIRQYGKCLHDCPPGYFGIRGQEVNRCKKCGATCESCFSQDFCIRCKRQFYLYKGKCLPTCPPGTLAHQNTRECQGECELGPWGGWSPCTHNGKTCGSAWGLESRVREAGRAGHEEAATCQVLSESRKCPIQRPCPGERSPGQKKGRKDRRPRKDRKLDRRLDVRPRQPGLQP
Protein: Pyrin domain-containing protein 1 (PAAD-only protein 1) (Pyrin-only protein 1) (cellular POP1) (cPOP1) (Q8WXC3)
Organism: Homo sapiens (Human)
Function: Associates with PYCARD/ASC and modulates its ability to collaborate with MEFV/pyrin and NLRP3/cryopyrin in NF-kappa-B and pro-caspase-1 activation. Suppresses kinase activity of NF-kappa-B inhibitor kinase (IKK) complex, expression of NF-kappa-B inducible genes and inhibits NF-kappa-B activation by cytokines and LPS.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12656673}. Note=Recruited to specks formed by PYCARD within the cytoplasm. {ECO:0000269|PubMed:17178784}.
Interaction partners:
- Apoptosis-associated speck-like protein containing a CARD
- NACHT, LRR and PYD domains-containing protein 1
- Interferon-inducible protein AIM2
- NACHT, LRR and PYD domains-containing protein 6
- Caspase-1
- NLR family CARD domain-containing protein 4
- Proteinase-activated receptor 3
- NACHT, LRR and PYD domains-containing protein 3
- NACHT, LRR and PYD domains-containing protein 7
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MGTKREAILKVLENLTPEELKKFKMKLGTVPLREGFERIPRGALGQLDIVDLTDKLVASYYEDYAAELVVAVLRDMRMLEEAARLQRAA
Protein: Crossover junction endonuclease MUS81 (EC 3.1.22.-) (P91153)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU369042}.
Interaction partners:
- ERCC1-like central domain-containing protein
- Structure-specific endonuclease subunit SLX1 homolog
- DNA repair endonuclease XPF
- GEN1 Holliday junction resolvase homolog
- RecQ-like DNA helicase blm-1
- DNA repair protein RAD51 homolog
- SAP domain-containing protein
- DNA topoisomerase 3
- Exonuclease 1
- Meiotic recombination protein spo-11
Sequence:
MSNQSKRVTVRIEHSKNTFFEKVLKFQHQEQEDRKLKYVLHKAHENLRKCPFEILTIVDLKNVQGIGENIALKLEETWNVACRENNGQDPTLRSIKKFTTDDYRRFLTNRKSTTERMKDAKRLEKQKSTKTIVDIENEFESDGDDDKQPSVPLTKTKSFQVSKPVQPSLIRSQSGNLSSSSSTSSSSSNSSDPLSFRLLTCRPFEQPTVYLIADNREHRNNPRFKSVIEHLVKKEDIRVDIRSLSVGDYIWICRKIDGTEIVMDWVVERKTWDDLQSSIRGGRYDEQKGRLNMAPMKNRVYLIEAQHKGDVACEQAVASTLSNGGYLIQRCSDTRDTAAFLKEVTIRLQNKAAIEEISGVPFSQLQNLLQKKKAETVKEAWVRQLMVCPGMSQNRAEAIADRFPSMVSLLSYFRANGDDAPIRLLQLLPQLTRPITRNLFKFFVQ
Protein: Multiple C2 domain and transmembrane region protein 5 (Q9LXU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 16 kDa phloem protein 2
Sequence:
MQKPGQNIDFALKETSPKIGAGSVTGDKLCSTYDLVEQMHYLYVRVVKAKELPGKDVTGSCDPYVEVKLGNYRGMTKHFEKRSNPEWKQVFAFSKERIQASILEVVVKDKDVVLDDLIGRIMFDLNEIPKRVPPDSPLAPQWYRLEDRHGRKVKGELMLAVWMGTQADEAFSDAWHSDAATVGPEGVTHIRSKVYLSPKLWYVRVNVIEAQDLIPHDKTKFPEVYVKAMLGNQTLRTRISQTKTLNPMWNEDLMFVVAEPFEEALILAVEDRVAPNKDETLGRCAIPLQNVQRRLDHRPLNSRWFNLEKHIMVEGEQKEIKFASRIHLRIFLEGGYHVLDESTHYSSDLRPTAKQLWKPSIGLLEVGIISAHGLMPMKSKDGKGTTDAYCVAKYGQKWIRTRTIVDSFTPKWNEQYTWEVFDTCTVITFGAFDNGHIPGGSGKDLRIGKVRIRLSTLEADRIYTHSYPLLVFHPSGIKKTGEIQLAVRFTCLSLINMLHMYSQPLLPKMHYIHPLSVLQLDSLRHQAMNIVSARLNRAEPPLRKEIVEYMLDVDSHMWSMRRSKANFFRIMNVLSGLIAVGKWFDQICNWRNPITTILIHVLFIILVLYPELILPTVFLYLFLIGIWNFRWRPRHPPHMDTRLSHADAVHPDELDEEFDTFPTSRSSEIVRMRYDRLRSIGGRVQTVIGDLATQGERFLSLLSWRDPRATTLFVLFCLIAAIVLYVTPFQVVALLAGIYVLRHPRFRHKLPSVPLNLFRRLPARSDSLL
Protein: CRM-domain containing factor CFM3B, chloroplastic (Protein CRM FAMILY MEMBER 3B) (AtCFM3b) (Protein SUPPRESSOR OF RFC THREE 2) (F4JVH1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds specific group II introns in chloroplasts and facilitates their splicing. Exhibits non-specific action during plastid rRNA biogenesis; RFC3 prevents unaccurate splicing to improve the accuracy of plastid rRNA processing. Acts on subgroup IIB introns. The substrates of the subgroup IIB also require the CRM domain proteins CAF1 or CAF2, with a simultaneous binding of CFM3B and CAF1 or CAF2. Required for seed development.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18799595}. Plastid {ECO:0000269|PubMed:32143506}. Note=Localized to root plastids. {ECO:0000269|PubMed:32143506}.
Interaction partners:
- Protein REGULATOR OF FATTY ACID COMPOSITION 3
- At4g39040
- RNA-binding KH domain-containing protein
- CRS2-associated factor 2, chloroplastic
Sequence:
MAINSSHHFCPMTTTTTTSAKFVDSLGSSFCKFHGTSSSISLRSYRFGFSFMKNVKRLSCEGSSSSSSSRNENWNRTQKQNQFRPSKVVLNRRKDERFSDLGVISGENSSRSGDVGGGSGSSSTMEKIVEKLKKYGFVDEDQFQDKEVEQERRIEKSSVEERFYVEERRGGFSEESPFGVYGGNDEVKFPWEKVSSMEKKELVNGEWTAKKESRYSLAEMTLSEFELNRLRNVMFRTKSKMRVTGAGVTQAVVDAIQEKWKGSEIVRLKIEGSSALNMRRMHEILERKTGGLVIWRSGTSIALYNYKGGSNRDGSGNMNKQVYRRAERLPSSLPTSTVDQSVQLVNLPQLEKEPTVVGNKDRTSPQEVEYEDEINELLEGLGPRYTDWQGGYPLPVDADLLPGIVPGYEPPFRALPYGVRSTLGTKEATSLRRIATVLPPHFALGRSRQLQGLATAMVKLWQKSLIAKVALKRGVQLTTSERMAEDIKRLTGGMLLSRNKDFLVFYRGKSFLSLEVGEALMEKEMLVRTLQDEEEQARLRASSALVVPSIKANQQLARTLQDKEEQARPSALVLPSTKANQNLVSAGTLGETLDATGKWGKNLDNDDHVEEMKQEVEKVRSAKLVRKLERKLAFAEKKLLKAERALAKVEESLKPAEQRTDLEGITEEERFMFQKLGLKMKAFLLLGRRGVFDGTVENMHLHWKYRELIKILVKAKTLEGAQKVAMALEAESGGILVSVDKISKGYAVIVYRGKDYKRPTTLRPKNLLTKRKALARSLELQKREALIKHIEAIQTRSEQLRAEIEQVELVKDKGDETLYDKLDMAYSSDEETEETDGEEDDVYLDTYEDEGEDDEEGGIQANGSLSETDVEFGSDESDTDFGDNSASSTTPETTFVELQNEELDVQP
Protein: Inner membrane complex protein 1c, putative (Q8IK01)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MADSIKSSNSFQKLDNIDAKETSTVDRKWVALTAYQPVDVVTKTVEVPIIKTVEKYVPKTIIQEKIIHVPKNVTHIVEKIVEVPEVKYIEKIVEVPHIHYKNKYVPKIEIVEKVVERQKIIEKWHDKIVEVPQIKEVVRFKQIEDSEEIIKYVPRNSKNIDWEDEYKKYTESKGLQRYSLDQNNIYQQANSFNQFNENAYNQNAFNRSYELLNKQSSVKSQNNASGENFSQMNFYNQYSGANFEQERSIQASNFEPSGSMQLKRLSSEEIKPAGCCSAACT
Protein: Glycine N-methyltransferase (EC 2.1.1.20) (Q9QXF8)
Organism: Mus musculus (Mouse)
Function: Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy), a reaction regulated by the binding of 5-methyltetrahydrofolate. Plays an important role in the regulation of methyl group metabolism by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P13255}.
Interaction partners:
- Sarcosine dehydrogenase, mitochondrial
- Dimethylglycine dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Peroxisomal sarcosine oxidase
- Serine hydroxymethyltransferase, mitochondrial
- Alanine--glyoxylate aminotransferase
- Glycine dehydrogenase
- 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
- Glycine amidinotransferase, mitochondrial
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
Sequence:
MVDSVYRTRSLGVAAEGLPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVMSVDASDKMLKYALKERWNRRKEPSFDNWVIEEANWLTLDKDVLSGDGFDAVICLGNSFAHLPDCKGDQSEHRLALKNIASMVRPGGLLVIDHRNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGTGRDGSPGFSKFRLSYYPHCLASFTELVRAAFGGRCQHSVLGDFKPYKPGQAYVPCYFIHVLKKTD
Protein: Annexin (P93158)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
TLKVPVHVPSPSEDAEWQLRKAFEGWGTNEQLIIDILAHRNAAQRNSIRKVYGEAYGEDLLKCLEKELTSDFERAVLLFTLDPAERDAHLANEATKKFTSSNWILMEIACSRSSHELLNVKKAYHARYKKSLEEDVAHHTTGEYRKLLVPLVSAFRYEGEEVNMTLAKSEAKILHDKISDKHYTDEEVIRIVSTRSKAQLNATLNHYNTSFGNAINKDLKADPSDEFLKLLRAVIKCLTTPEQYFEKVLRQAINKLGSDEWALTRVVTTRAEVDMVRIKEAYQRRNSIPLEQAIAKDTSGDYEKFLLALIGAGDA
Protein: Large ribosomal subunit protein bL21m (50S ribosomal protein L21, mitochondrial) (Protein NUCLEAR FUSION DEFECTIVE 1) (Q8L9A0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein binds to 23S ribosomal RNA in the presence of protein L20 (By similarity). Required for karyogamy during female gametophyte development, when the two polar nuclei fuse to form the diploid central cell nucleus, and during double fertilization of the egg cell and the central cell.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16698901}.
Interaction partners:
- Small ribosomal subunit protein uS9m
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- 50S ribosomal protein L33
- Large ribosomal subunit protein uL3m
- 50S ribosomal protein L20
- Large ribosomal subunit protein bL9c
- Ribosomal protein
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein mL46
Sequence:
MASLRCFRELSRRATTVFSINQTRSISSFHGIEFSGTSISHGTVIPNRSLTRNLPWYSHWYRSQDRCFSSNTKDTDEDEESSEGEDDDEEEGEDFEDSADMEVEREYSPAEKVEEAEEIGYKVMGPLKPSERLFKPYEPVFAIVQIGSHQFKVSNGDSIFTEKLKFCDINDKLELTKVLLLGSASQTIIGRPILPDATVHAVVEEHALDEKVLIFKKKRRKNYRRTRGHRQELTKLRITDIQGIEKPEPKIVHKPSKEAVTEQTKAELVA
Protein: Peroxiredoxin-like 2A (Peroxiredoxin-like 2 activated in M-CSF stimulated monocytes) (Protein PAMM) (Redox-regulatory protein FAM213A) (Q9CYH2)
Organism: Mus musculus (Mouse)
Function: Involved in redox regulation of the cell (By similarity). Acts as an antioxidant (By similarity). Inhibits TNFSF11-induced NFKB1 and JUN activation and osteoclast differentiation (By similarity). May affect bone resorption and help to maintain bone mass (By similarity). Acts as a negative regulator of macrophage-mediated inflammation by inhibiting macrophage production of inflammatory cytokines, probably through suppression of the MAPK signaling pathway.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BRX8}. Secreted {ECO:0000269|PubMed:26438880}. Note=Secreted from mature adipocytes but not from preadipocytes. {ECO:0000250|UniProtKB:Q9BRX8}.
Interaction partners:
Sequence:
MGMWSIGVGAVGAAAVALLLANTDMFLSKPRKAALEYLEDIDLKTLEKEPRTFKAKELWEKNGAVIMAVRRPGCFLCRAEAADLMSLKPKLDELGVPLYAVVKEQVKREVEDFQPYFKGEIFLDEKKKFYGPERRKMMFMGLIRLGVWYNSFRAWNGGFSGNLEGEGFILGGVFVIGSGKQGILLEHREKEFGDRVNPLSVLEAVKKIKLQTPASGRS
Protein: Methionine--tRNA ligase, mitochondrial (EC 6.1.1.10) (Mitochondrial methionyl-tRNA synthetase) (MtMetRS) (Q9VFL5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Tyrosine--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
- Probable arginine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- leucine--tRNA ligase
- Lysine--tRNA ligase
- leucine--tRNA ligase
- asparagine--tRNA ligase
- Methionyl-tRNA formyltransferase, mitochondrial
- cystathionine gamma-lyase
Sequence:
MLIRRIKCLRYLGTRYNSSHYVTTPIFYVNAAPHIGHLYSAVIADAHCRYQRLRYPEQDVRLCTGTDEHGTKIQQAASLHGVPVAKYCDDISQRYREVFRSASIQQDDFIRTTEDRHKRAVANFWRTLHTRGHIYSAAYSGWYCVSDETFLTDSQLRLDEATGTRYSLESGHPVEWTEETNYMFRLSQFQDDVRHWVKTEARVRPAKFEKILLDTLSEPLPDVSVSRPSNRVHWAIPVPDDDSQTVYVWLDALVNYLSSVGYPDEKFSAHWPPAQQVIGKDILKFHGIYWTAFLLAAGLEPPGQLYVHSHWTVDGQKMSKSKHNVVDPLQAAQQYTMEGLRYFLLREGVAHSDGNYSHVKAQRILNSELADTLGNLLSRASAKSLNPGQIYPSPSAEHLADLLRSLDVAKRLQDSLLQLSERCESHYECNHFHLVADTTMAALHAANNFFESSKPWTLKAGAPDGNQARLETIIAMTMDALRLSGIVLQPIIPQLANRLLDKLSVPTAQRGWNYLAESFATSPNSSNSPAGLGESRQLDGQTSALLFQRILEETSAKEVKEQKPQPAKRSKSKKKERRETMS
Protein: Meiotic recombination protein rec7 (P36625)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved primarily in the early steps of meiotic recombination.
Interaction partners:
- Meiotic recombination protein rec24
- Meiotic recombination protein rec15
- Meiotic recombination protein rec6
- Meiotic recombination protein rec12
- Meiotic recombination protein rec14
- Linear element protein rec10
- Mei4-dependent protein 2
- Linear element-associated protein hop1
- Linear element protein Mug20
- Linear element protein rec27
Sequence:
MNIFPIVKYSVAEDSYTTDSSHINWSHYSDGGFTLSLTSGLLQIRQHEELIQSINLLDLWHQLIPGTKEKCLTLLSRAPCMNIRAFTNNVMKRFQVKFPSDVHYMKAKVEFEKLGLVFKDAKSSSEKKQFNNSQSQSNNSQELSLMNNAYNKSSAQQPNLLLQPSYIPMTQTATTAVNNSTNYVNPAPLQHVMPNAEIFSNTPPLKRFRGDAGMTQMPLRSDTSIESITASQQPTWDENVVITSSPFNPNRNAYSYGANSQYPIIAATPLNSQTQASWVAQPENQAYANLIPSPPTTSQILPTELTEEEKQLRSKVLFYLKQDSFIQLCQSLERVWNKM
Protein: Charged multivesicular body protein 2B (F1M8B7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Charged multivesicular body protein 1A
- Similar to RIKEN cDNA 1500016L11
- Charged multivesicular body protein 1B2
- vesicle-fusing ATPase
- Charged multivesicular body protein 3
- Vacuolar protein sorting-associated protein 4A
- Charged multivesicular body protein 4B
- Charged multivesicular body protein 7
- Charged multivesicular body protein 4c
- Mixed lineage kinase domain-like protein
Sequence:
MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACRVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD
Protein: Vomeronasal 2, receptor 65 (A0A3B2WCT5)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLSFMSFFLILEYFLLLSVAHPKCFWRIKQNENKVGDVEDNCFFYIYTRQGPLLNDPFNGNPDILLTTRNIHLILALLFAIKQINRNIHILPNISLIVNVNCAKKEDLQMTNMYSNRDATIPNYNCKHGRRILTVLTGPRWFSSAILGPFLHIFAIPQVAPFLENNKFIIPSEYQYRRGKLDTEYDILYAMDLLPALGLNVKIGKFSQHFLHFQQLYIAEDMIDWTIDIRQTLQSVCSVPCSVGFRKFIQKGKAVCCFDCTPCPENEISNMTDMDQCVKCPNDQYANIKQTHCLKKVVTFLAYEDPLGMTLTCLALLFSALTTVILSILLKHQDNPIVKANNRLLSYILLISLIFCFLCSLLYIGHPHMATCILQQTTFAVVFTVAVSTILAKTITVVMAFKITDPRKKIRQMLVTRAPNYIIPICTMIQLILCGTWIGTSPPFVDSDPHFEHGHIIIVCNKGSVIAFYCVLGYLGLLALGSFTVAFLARNLPDRFNEAKFLTFSMLVFCSVWITFLPVYHSTKGKAMVVVEIFSILTSSAGLLVCIFFPKCFTILLKQKVNFTQKFSDTHSKIEYNH
Protein: Interleukin (C8TE57)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDRRYRISFLTLFLAGCLQGNPIPRLLAGIDYLEENITCPDSVFYTPTDVEDSCIVAALACSIKELDTVKVECLDKAVHLESMQHHISMTATALQKTIDKENSTTDTSECICEDKRLEKSFKDFIQNIRHLTQAHAAKRLSS
Protein: Macrophage-expressed gene 1 protein (Macrophage gene 1 protein) (Mpg-1) (Perforin-2) (P-2) (PFN2) (mPFN2) (Protein MPS1) [Cleaved into: Macrophage-expressed gene 1 protein, processed form] (A1L314)
Organism: Mus musculus (Mouse)
Function: Plays a key role in the innate immune response following bacterial infection by inserting into the bacterial surface to form pores. By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence. Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria. Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol. Required for the antibacterial activity of reactive oxygen species and nitric oxide.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:26402460, ECO:0000269|PubMed:26418746, ECO:0000269|PubMed:35471730}; Multi-pass membrane protein {ECO:0000269|PubMed:32064340, ECO:0000269|PubMed:36245269}. Note=Bacterial infection induces translocation of the cytoplasmic vesicles to bacterium-containing phagocytic vesicles and fusing of the vesicles. {ECO:0000269|PubMed:26402460}.; SUBCELLULAR LOCATION: [Macrophage-expressed gene 1 protein, processed form]: Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:37347855}; Multi-pass membrane protein {ECO:0000269|PubMed:32064340, ECO:0000269|PubMed:36245269}. Note=Proteolytically processed in lysosomes, leading to its maturation and forms pores in the membrane of antigen-containing phagosomes. {ECO:0000269|PubMed:37347855}.
Interaction partners:
Sequence:
MNSFMALVLIWMIIACAEADKPLGETGTTGFQICKNALKLPVLEVLPGGGWDNLRNVDMGRVMDLTYTNCKTTEDGQYIIPDEVYTIPQKESNLEMNSEVLESWMNYQSTTSLSINTELALFSRVNGKFSTEFQRMKTLQVKDQAVTTRVQVRNRIYTVKTTPTSELSLGFTKALMDICDQLEKNQTKMATYLAELLILNYGTHVITSVDAGAALVQEDHVRSSFLLDNQNSQNTVTASAGIAFLNIVNFKVETDYISQTSLTKDYLSNRTNSRVQSFGGVPFYPGITLETWQKGITNHLVAIDRAGLPLHFFIKPDKLPGLPGPLVKKLSKTVETAVRHYYTFNTHPGCTNVDSPNFNFQANMDDDSCDAKVTNFTFGGVYQECTELSGDVLCQNLEQKNLLTGDFSCPPGYSPVHLLSQTHEEGYSRLECKKKCTLKIFCKTVCEDVFRVAKAEFRAYWCVAAGQVPDNSGLLFGGVFTDKTINPMTNAQSCPAGYIPLNLFESLKVCVSLDYELGFKFSVPFGGFFSCIMGNPLVNSDTAKDVRAPSLKKCPGGFSQHLAVISDGCQVSYCVKAGIFTGGSLLPVRLPPYTKPPLMSQVATNTVIVTNSETARSWIKDPQTNQWKLGEPLELRRAMTVIHGDSNGMSGGEAAGITLGVTIALGIVITLAIYGTRKYKKKEYQEIEEQESLVGSLATDATVLNGEEDPSPA
Protein: Non-toxic nonhemagglutinin type A (NTNHA) (Botulinum neurotoxin type A non-toxic component) (Q45914)
Organism: Clostridium botulinum
Function: Assembles with botulinum neurotoxin type A (BoNT/A) and protects it against pH-mediated inactivation or protease activity at pH 2.6 (the pH of the animal gastrointestinal tract) but not at pH 6.0. Necessary for neurotoxicity.
Interaction partners:
Sequence:
MNINDNLSINSPVDNKNVVVVRARKTDTVFKAFKVAPNIWVAPERYYGESLSIDEEYKVDGGIYDSNFLSQDSEKDKFLQAIITLLKRINSTNAGEKLLSLISTAIPFPYGYIGGGYYAPNMITFGSAPKSNKKLNSLISSTIPFPYAGYRETNYLSSEDNKSFYASNIVIFGPGANIVENNTVFYKKEDAENGMGTMTEIWFQPFLTYKYDEFYIDPAIELIKCLIKSLYFLYGIKPSDDLVIPYRLRSELENIEYSQLNIVDLLVSGGIDPKFINTDPYWFTDNYFSNAKKVFEDHRNIYETEIEGNNAIGNDIKLRLKQKFRININDIWELNLNYFSKEFSIMMPDRFNNALKHFYRKQYYKIDYPENYSINGFVNGQINAQLSLSDRNQDIINKPEEIINLLNGNNVSLMRSNIYGDGLKSTVDDFYSNYKIPYNRAYEYHFNNSNDSSLDNVNIGVIDNIPEIIDVNPYKENCDKFSPVQKITSTREINTNIPWPINYLQAQNTNNEKFSLSSDFVEVVSSKDKSLVYSFLSNVMFYLDSIKDNSPIDTDKKYYLWLREIFRNYSFDITATQEINTNCGINKVVTWFGKALNILNTSDSFVEEFQNLGAISLINKKENLSMPIIESYEIPNDMLGLPLNDLNEKLFNIYSKNTAYFKKIYYNFLDQWWTQYYSQYFDLICMAKRSVLAQETLIKRIIQKKLSYLIGNSNISSDNLALMNLTTTNTLRDISNESQIAMNNVDSFLNNAAICVFESNIYPKFISFMEQCINNINIKTKEFIQKCTNINEDEKLQLINQNVFNSLDFEFLNIQNMKSLFSSETALLIKEETWPYELVLYAFKEPGNNVIGDASGKNTSIEYSKDIGLVYGINSDALYLNGSNQSISFSNDFFENGLTNSFSIYFWLRNLGKDTIKSKLIGSKEDNCGWEIYFQDTGLVFNMIDSNGNEKNIYLSDVSNNSWHYITISVDRLKEQLLIFIDDNLVANESIKEILNIYSSNIISLLSENNPSYIEGLTILNKPTTSQEVLSNYFEVLNNSYIRDSNEERLEYNKTYQLYNYVFSDKPICEVKQNNNIYLTINNTNNLNLQASKFKLLSINPNKQYVQKLDEVIISVLDNMEKYIDISEDNRLQLIDNKNNAKKMIISNDIFISNCLTLSYNGKYICLSMKDENHNWMICNNDMSKYLYLWSFK
Protein: Large ribosomal subunit protein bL17m (54S ribosomal protein L8, mitochondrial) (YmL8) (P22353)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein bL28m
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein bL33m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS11m
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein uL5m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS12m
Sequence:
MTVGIARKLSRDKAHRDALLKNLACQLFQHESIVSTHAKCKEASRVAERIITWTKRAITTSNSVAQAELKSQIQSQLFLAGDNRKLMKRLFSEIAPRYLERPGGYTRVLRLEPRANDSAPQSVLELVDSPVMSESHTVNRGNLKMWLLVKSVINDDANQLPHNPLTLQNLHKVAKFKAEAQLHGEIMLIKQVLLKEMSLPYDEALENERTQALLKEVYSSSLPKKTKKPSSYVMVPRP
Protein: RNA-binding protein (Q585J6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- CCHC-type domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MHSRGVYNRGEPYNKHGRANYHQPRPSDTSAGAIVAIAPASGGSGAVVSQVAGSDRGGPRRLTFNNFRTFSARNKKTPLDANTSAAPNTKLWQLSEQVSFYCNKCRRDNIISDSLAIDAVHQLMLCTRCFTRIIRPRTYRPSRVVPFPSLLSWLNYTPSRVMEMSEDIASRPAEAVAPSADRVAVPTIPGGSRPTHIQQLPATAMNTVSNAGNVGGALLARGMTAASQQQQSLESSKHPCHRVWGSCLHGETCLFRGAPYDLCICFLMGLCNGDEATCNLLHQRVFALPDAEAPMPLQRCEGDLEDPGSAWGKWVGKKKNSANSAEWQLWNNGPILELINRHAPATPVAVAEEKGGDNVKPRIKLHFADISAALKGLQK
Protein: Ferric-chelate reductase (NAD(P)H) (EC 1.16.1.10) (O29428)
Organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Function: Catalyzes the reduction of bound ferric iron (Fe(3+)) in a variety of iron chelators (siderophores) using NAD(P)H as the electron donor, resulting in the release of Fe(2+). Not active with uncomplexed Fe(3+). Also reduces FMN and FAD, but not riboflavin.
Interaction partners:
- Rubrerythrin
- Rubrerythrin
- Flavoprotein
- Flavoprotein
- Uncharacterized protein AF_0829
- Desulfoferrodoxin homolog
- Ferritin, putative
Sequence:
MDVEAFYKISYGLYIVTSESNGRKCGQIANTVFQLTSKPVQIAVCLNKENDTHNAVKESGAFGVSVLELETPMEFIGRFGFRKSSEFEKFDGVEYKTGKTGVPLVTQHAVAVIEAKVVKECDVGTHTLFVGEAVDAEVLKDAEVLTYADYHLMKKGKTPRTATVYFESK
Protein: Protein virB2 (P09776)
Organism: Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Function: VirB proteins are suggested to act at the bacterial surface and there play an important role in directing T-DNA transfer to plant cells.
Subcellular location: Cell outer membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRCFERYRLHLNRLSLSNAMMRVISSCAPSLGGAMAWSISSCGPAAAQSAGGGTDPATMVNNICTFILGPFGQSLAVLGIVAIGISWMFGRRSLGLVAGVVGGIVIMFGASFLGQTLTGGS
Protein: Sideroflexin-1-3 (Q9VN13)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial amino-acid transporter that mediates transport of serine into mitochondria.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:30442778}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- N-alpha-acetyltransferase 20
- GH10714p
Sequence:
MSPLPRVNIDEPKYDQNSYLGRAKHFFLLTNPLNVLASASKLEEARQIVIKYRAGKDVPECKTIDDVWRAKYLYDSAFHPETGEKQIVIGRMAAQMPMNTIITGGMMAFYKSTPAVVFWQWFNQTFNAIVNYTNRSGTSPISQQQLVTSYCLATSGALVTALSLNHAVKNMNPLLGRLVPLVAVGAANCINIPCMRMQELRNGVTLFDEHSNEMGISKKAAVVGISTVILSRIAMAIPGMTLTPVLMNVLEKRGFLAKYPRSNAPIQTLFCGFVLIFATPLGCAFFKQRADIKVDSLESEVRDSIRKKRPELETVWFNKGL