wanglab/gogpt-training-data huggingface dataset:
Protein: Exosome complex component RRP40 (Ribosomal RNA-processing protein 40) (Q8IPX7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events (By similarity). In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts such as antisense RNA species, and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm (By similarity). In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs (By similarity). The catalytic inactive RNA exosome core complex of 9 subunits is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes (By similarity). Required generally for normal embryonic and neuronal development. Also plays a critical role in the maintenance of neuronal function in mature flies by controlling the levels of specific mRNAs such as the synaptic regulator Arc1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NQT5}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NQT5}. Nucleus {ECO:0000269|PubMed:12490954}.
Interaction partners:
- FI01414p
- FI06805p
- Ribosomal RNA-processing protein 42
- Exosome complex component RRP4
- Exosome complex exonuclease RRP44
- FI07225p
- Csl4
- Exosome complex component RRP45
- Exosome complex component 10 homolog
- Nuclear nucleic acid-binding protein C1D
Sequence:
MSATSTIVMPGERIAAIEELAKSKRVILGPGLRRLDDTVVASKAGPLRHKEPGTFWVDNYQRRYIPARGDLILGIVRAKAGDLYRVDIGATDTASISYLAFEAASKKNRPDLIPGDLIYARVLNASADIEPELVCVNSVGKSGKLGVLTDGFFFKCSLNLGRMLLRENCPVLAALTRELPYEIAVGVNGRIWLKAHSLKETVALANAISALEQSGCAEIDKICGNLGDFLQA
Protein: Transcription factor ETV6 (ETS translocation variant 6) (ETS-related protein Tel1) (Tel) (P41212)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'. Plays a role in hematopoiesis and malignant transformation.
Subcellular location: Nucleus.
Interaction partners:
- Runt-related transcription factor 1
- NT-3 growth factor receptor
- Transcription factor ETV7
- Tyrosine-protein kinase ABL1
- Platelet-derived growth factor receptor beta
- Tyrosine-protein kinase ABL2
- Cysteine-rich hydrophobic domain-containing protein 2
- DNA-binding protein Ikaros
- GTPase NRas
- Polycomb group protein ASXL1
Sequence:
MSETPAQCSIKQERISYTPPESPVPSYASSTPLHVPVPRALRMEEDSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHILKQRKPRILFSPFFHPGNSIHTQPEVILHQNHEEDNCVQRTPRPSVDNVHHNPPTIELLHRSRSPITTNHRPSPDPEQRPLRSPLDNMIRRLSPAERAQGPRPHQENNHQESYPLSVSPMENNHCPASSESHPKPSSPRQESTRVIQLMPSPIMHPLILNPRHSVDFKQSRLSEDGLHREGKPINLSHREDLAYMNHIMVSVSPPEEHAMPIGRIADCRLLWDYVYQLLSDSRYENFIRWEDKESKIFRIVDPNGLARLWGNHKNRTNMTYEKMSRALRHYYKLNIIRKEPGQRLLFRFMKTPDEIMSGRTDRLEHLESQELDEQIYQEDEC
Protein: Complement C1q subcomponent subunit C (P02747)
Organism: Homo sapiens (Human)
Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
Subcellular location: Secreted.
Interaction partners:
- Complement C1q subcomponent subunit A
- Complement C1q subcomponent subunit B
- Complement C1r subcomponent
- Complement C1s subcomponent
- Complement C4-A
- Complement C4-B
- Plasma protease C1 inhibitor
- Complement C2
- V-set and immunoglobulin domain-containing protein 4
- Calreticulin
Sequence:
MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGYDGLPGPKGEPGIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPGPMGIPGEPGEEGRYKQKFQSVFTVTRQTHQPPAPNSLIRFNAVLTNPQGDYDTSTGKFTCKVPGLYYFVYHASHTANLCVLLYRSGVKVVTFCGHTSKTNQVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGFLLFPD
Protein: Integrase (EC 2.7.7.-) (EC 3.1.-.-) (P08320)
Organism: Enterobacteria phage P4 (Bacteriophage P4)
Function: Integrase is necessary for integration of the phage into the host genome by site-specific recombination.
Interaction partners:
Sequence:
MCPQMKLNARQVETAKPKDKTYKMADGGGLYLEVSAKGSKYWRMKYRRPSDKKEDRLAFGVWPTVTLAQARAKRDEAKKLLVQGIDPKVVQKEARAENSGAYTFEAIAREWHASNKRWSEDHRSRVLRYLELYIFPHIGSSDIRQLKTSHLLAPIKKVDASGKHDVAQRLQQRVTAIMRYAVQNDYIDSNPASDMAGALSTTKARHYPALPSSRFPEFLARLAAYRGRVMTRIAVKLSLLTFVRSSELRFARWDEFDFDKSLWRIPAKREEIKGVRYSYRGMKMKEEHIVPLSRQAMILLNQLKQISGDKELLFPGDHDATKVMSENTVNSALRAMGYDTKTEVCGHGFRTMARGALGESGLWSDDAIERQLSHSERNNVRAAYIHTSEHLDERRLMMQWWADYLDMNRNKYISLMIIQNTKKYLNKNSYWLIFKMSVK
Protein: Translation initiation factor IF-3 (P9WKJ9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00080}.
Interaction partners:
- Large ribosomal subunit protein bL20
- Large ribosomal subunit protein bL35
- Small ribosomal subunit protein uS13
- Translation initiation factor IF-1
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein uS10
Sequence:
MSTETRVNERIRVPEVRLIGPGGEQVGIVRIEDALRVAADADLDLVEVAPNARPPVCKIMDYGKYKYEAAQKARESRRNQQQTVVKEQKLRPKIDDHDYETKKGHVVRFLEAGSKVKVTIMFRGREQSRPELGYRLLQRLGADVADYGFIETSAKQDGRNMTMVLAPHRGAKTRARARHPGEPAGGPPPKPTAGDSKAAPN
Protein: Reticulophagy regulator 1 (Reticulophagy receptor 1) (Q9H6L5)
Organism: Homo sapiens (Human)
Function: Endoplasmic reticulum (ER)-anchored autophagy regulator which mediates ER delivery into lysosomes through sequestration into autophagosomes. Promotes membrane remodeling and ER scission via its membrane bending capacity and targets the fragments into autophagosomes via interaction with ATG8 family proteins. Active under basal conditions. Required for collagen quality control in a LIR motif-dependent manner (By similarity). Required for long-term survival of nociceptive and autonomic ganglion neurons.
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q8VE91}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:26040720}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:35239449}; Multi-pass membrane protein {ECO:0000255}. Note=(Microbial infection) Following SARS-CoV-2 infection, colocalizes with SARS-CoV-2 ORF3A protein at the endoplasmic reticulum. {ECO:0000269|PubMed:35239449}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Translocation protein SEC62
- Serine/threonine-protein kinase WNK1
- 60S ribosomal export protein NMD3
- GABA type A receptor associated protein like 1
- Microtubule-associated protein 1 light chain 3 beta
- Reticulon-3
- Cell cycle progression protein 1
- Atlastin-3
Sequence:
MASPAPPEHAEEGCPAPAAEEQAPPSPPPPQASPAERQQQEEEAQEAGAAEGAGLQVEEAAGRAAAAVTWLLGEPVLWLGCRADELLSWKRPLRSLLGFVAANLLFWFLALTPWRVYHLISVMILGRVIMQIIKDMVLSRTRGAQLWRSLSESWEVINSKPDERPRLSHCIAESWMNFSIFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLLCAFLCPLFKCNDIGQKIYSKIKSVLLKLDFGIGEYINQKKRERSEADKEKSHKDDSELDFSALCPKISLTVAAKELSVSDTDVSEVSWTDNGTFNLSEGYTPQTDTSDDLDRPSEEVFSRDLSDFPSLENGMGTNDEDELSLGLPTELKRKKEQLDSGHRPSKETQSAAGLTLPLNSDQTFHLMSNLAGDVITAAVTAAIKDQLEGVQQALSQAAPIPEEDTDTEEGDDFELLDQSELDQIESELGLTQDQEAEAQQNKKSSGFLSNLLGGH
Protein: Pumilio homology domain family member 6 (Q9UU76)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: RNA-binding protein involved in post-transcriptional regulation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribosome production factor 2 homolog
- Ribosome biogenesis protein brx1
- 25S rRNA
- Probable rRNA-processing protein ebp2
- Probable nucleolar GTP-binding protein 1
- Uncharacterized RNA-binding protein C4F6.14
- Uncharacterized RNA-binding protein C1827.05c
- Pumilio domain-containing protein C6G9.14
- Nucleolar protein 58
- ATP-dependent RNA helicase has1
Sequence:
MAIGKRKESTEVKKKDGSMNKRVKVAKLPKKVDSFSPKKKKNTTSSGSSESDSMSQNDKKKDSSLNESEDEDFAGFGESASENDELESAESEAENDEESSSQKSNSKESHAQRKKLQKERKAMKPFADTSLKAKSLWDKLRQKTSIKAEERKTIIAELFDLIRTNVKQLVFKHDMSRVVQTCVKFGSKQQRETICAELAGSYVDLCKSPYGKYLAIKIFKYGTPKMKEVILGEMYGNVVKMIRHREAAYVVEDAFREFTNLQQQRALICEFYGPEFQVFKDRTQDIHIDKLLIDHPEKRPSIMQNLWKTIEGSIAKGSIGFTMVHRAMLEFINHADSNEAKELLNLTKELIYEFVHTRDGSQVAMKLFALANAKDRKVMLKSLRPYLIETAKDSYGHLVVVAALDCTDDTIMTGKLLQAEFEGELLKLSADKFARRILLYVLVGWEDARYFSKENRELLRSLDSLKAKTSKKDPIVRRNELKATIGPLLISLISKAAGDMIAESLASQVLVDALLYAPCEKEEAVDATLKAFDGNPEQDNHLIHQIHCSRALKTLVQNGHWSGAEKQVVKAEDDLKVASKLIVIIKKYLVEWASGDGAFVVVAVLEALSDSEKQEFLKILRKHKNQLNKSEFRGTKKLLEML
Protein: Conserved protein (O53652)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Heme uptake protein MmpL11
- Putative transport protein Rv0205
- Probable conserved Mce associated membrane protein
- Heme-binding protein Rv0203
Sequence:
MTLAAEPHPAPPQQPTVAWSEPDVDRRVEFWPTVAIRSALESGDIATWQRIAAALKRDPYGRTARQVEEVLEGIPATGIANAFWEVLDRARTHLDANERAEVARQVGLLLDRSGLQRQEFASRIGVTAQDLTAYLDGIVSPSASLMIRMRRLSDRFVRAKSVRAADS
Protein: Probable proteasome subunit alpha type-6 (O14250)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable proteasome subunit beta type-3
- Probable proteasome subunit alpha type-5
- Probable proteasome subunit beta type-2
- Probable proteasome subunit beta type-1
- Probable proteasome subunit beta type-4
- Probable proteasome subunit beta type-7
- Probable proteasome subunit alpha type-3
- Probable proteasome subunit beta type-6
- Probable proteasome subunit alpha type-4
- Probable proteasome subunit beta type-5
Sequence:
MFRNQYDGDATTWSPQGRLHQVEYALEAIKQGSATVGLVSKTHAVLVALKRNAEELSSYQKKLIRIDDHIGIAIAGLAPDARVLSNYMKQEALSSKTLFTRPIPVRRLMSKVAEKAQINTQEYGRRPYGVGFLVIGYDESGPHLLEFQPSGLVLEYLGTSMGSRSQSARTYIERNLDTFPDSSREELILSALRALRDTLSKDQELTEENVSISVIGKDEKYTLYDQNDTKEWLDKLGDKGPAAARASRAAAEEPQAPTAEAILDSADAMETD
Protein: Zinc finger CCCH domain-containing protein 43 (AtC3H43) (Zinc finger CCCH domain-containing protein ZFN-like 6) (Q9STM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 68
- tRNA-dihydrouridine
- Zinc finger CCCH domain-containing protein 45
- E3 ubiquitin-protein ligase makorin
- Zinc finger CCCH domain-containing protein 5
- Zinc finger CCCH domain-containing protein 18
- Zinc finger CCCH domain-containing protein 44
- Zinc finger CCCH domain-containing protein 15
- Zinc finger CCCH domain-containing protein 6
- Zinc finger CCCH domain-containing protein 54
Sequence:
MVNSEEIADGFEPKPVSRSYSGDSSHDRSLSDLNHAAEDLSDKLKNVGLNEVTKEQSEKMMSVSESNGGLDSNAVVTINQEEEEEEEDRDGYGYGDGWSENESENVYPVRPGAEDCSFYMRTGSCKFGSSCKFNHPLARKFQIARDNKVREKEDDGGKLGLIDCKYYFRTGGCKYGETCRFNHTIPKSGLASAPELNFLGLPLRPGEVECPYYMRNGSCKYGAECKFNHPDPTTIGGTDSPSFRGNNGVSIGTFSPKATFQASSTSWSSPRHVNGTSPFIPVMLSQTHGVTSQNPEWNGYQASVYSSERGVFSPSTTYLMNNSSAETSMLLSQYRHQMPAEEFPERPDQPECSYYMKTGDCKFKFNCKYHHPKNRLPKLPPYALNDKGLPLRPDQNICTYYSRYGICKFGPACRFDHSVQPPYSTESSQAIVEPPQVSANGNESDGWN
Protein: Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase (EC 2.4.3.8) (Alpha-2,8-sialyltransferase 8A) (Ganglioside GD3 synthase) (Ganglioside GT3 synthase) (Sialyltransferase 8A) (SIAT8-A) (Sialyltransferase St8Sia I) (ST8SiaI) (Q64687)
Organism: Mus musculus (Mouse)
Function: Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid. Can catalyze the addition of a second alpha-2,8- sialic acid to GD3 to form GT3. Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b respectively.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Lactosylceramide alpha-2,3-sialyltransferase
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- Type 2 lactosamine alpha-2,3-sialyltransferase
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- Beta-hexosaminidase subunit alpha
- Alpha-
- Beta-hexosaminidase subunit beta
- Alpha-2,8-sialyltransferase 8E
- Alpha-
Sequence:
MSPCGRALHTSRGAMAMLARKFPRTRLPVGASALCVVVLCWLYIFPVYRLPNEKEIVQGVLAQRTAWRTNQTSASLFRRQMEDCCDPAHLFAMTKMNSPMGKSLWYDGELLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKMSGCGRQIDEANFVMRCNLPPLSSEYTRDVGSKTQLVTANPSIIRQRFENLLWSRKKFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLKDVGANQTVLFANPNFLRNIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVSIYGFWPFSVNMQGDPISHHYYDNVLPFSGYHAMPEEFLQLWYLHKIGALRMQLDPCEEPSPQPTS
Protein: Protein translocase subunit SecY (Protein transport protein SEC61 subunit alpha homolog) (Q8U019)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. Complements an E.coli temperature-sensitive secY mutation; deletion of the last 15 residues prevents complementation, which may indicate a role of this region in translocation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20855604}; Multi-pass membrane protein {ECO:0000269|PubMed:20855604}.
Interaction partners:
- Protein translocase subunit SecE
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL30
- Signal recognition particle receptor FtsY
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein uL15
- Signal recognition particle 54 kDa protein
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL4
Sequence:
MGARDIIYALERWFPEVERPKRRVPLRERFMWTGVALILYYVLAEIPVYGIPERIQDYFQFLRVVLAGRNGSILTLGIGPIVTAGIILQLLVGSEIIKLDLANPEDRRFYQALQRVFSVFMCFFEAAVWILGGAFGRVGVDVTYAIAVLMILQLAMGGIVLIILDELVSKWGIGSGISLFIAAGVSQTILTRSLNPLTDPNIIDPLTGQPAIVGAIPYFIQHILKGDLWGAIYRGGSAPDMLSVVATIVVFFIVVYFESMRVEIPLGYRGVTVRGSYPIRFLYVSNIPIILTFALYANIQLWARVLDRLGHPWLGRFDPTTGSPISGFVLYVIPPRNIFSVIDNPVRAIVYLILTVIFSLLFGYLWVELTGLDARSIARQLQRAGLQIPGFRRDPRTLEKVLQRYIPYVTFWGSLTVALIAVLADFLGALGTGTGILLTVGILYRFYEEIAREQITEMFPALRKLFGA
Protein: Torsin-1A (Dystonia 1 protein) (A0A494BZT7)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, growth cone {ECO:0000256|ARBA:ARBA00004624}. Nucleus membrane {ECO:0000256|ARBA:ARBA00004617}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004617}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MASARGGTGSVGLAAAPVRGRRENKQGGAGPGMKLGRAVLGLLLLAPSVVQAVEPISLGLALAGVLTGYIYPRLYCLFAECCGQKRSLSREALQKDLDDNLFGQHLAKKIILNAVFGFINNPKPKKPLTLSLHGWTGTGKNFVSKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQLWIRGNVSACARSIFIFDEMDKMHAGLIDAIKPFLDYYDLVDGVSYQKAMFIFLSNAGAERITDVALDFWRSGKQREDIKLKDIEHALSVSVFNNKNNSFTLSPRLECSGVTLPHCNLCLPGSSDSCASAS
Protein: Keratin-like protein KRT222 (Keratin-222) (Keratin-222 pseudogene) (Q8N1A0)
Organism: Homo sapiens (Human)
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
Sequence:
MELSQLLNEIRANYEKILTRNQIETVLSTRIQLEEDISKKMDKDEEALKAAQAELKEARRQWHHLQVEIESLHAVERGLENSLHASEQHYQMQLQDLETVIEGLEKELQEVRRGIEKQLQEHEMLLNTKMRLEQEIATYRHLLEKEEIRYYGCIQGGKKDKKPTTSRVGFVLPSAIINEISFTTKVPQKYENENVETVTKQAILNGSIVKESTEAHGTIQTEKVDEVIKEWEGSFFKDNPRLRKKSVSLRFDLHLAATDEGCLETKQDNLPDIEVRLIMRRSCSIPSIKPPSTAN
Protein: Internalin C (InlC) (Internalin-related protein A) (P71451)
Organism: Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness)
Function: A virulence enhancer that has at least 2 dissociable functions in infection; it impairs translocation of host transcription factor NF-kappa-B to the nucleus and antagonizes the function of the Tuba dynamin-binding protein, promoting bacterial spreading. Perturbs the morphology of host cell junctions by impairing host DNMBP (Tuba) and WASL interaction, altering cortical tension at the cell junctions and allowing bacteria to more efficiently form bacteria-filled cell protrusions which promote bacterial spreading within infected host tissue. Down-regulates the host inflammation response usually induced by Listeria infection. Interacts with host I-kappa-B kinase alpha (IKKA, CHUK), which prevents IKKA from phosphorylating NF-kappa-B inhibitor alpha (IKBA, NFKBIA) and thus delays degradation of phospho-IKBA. Translocation of host transcription factor p65 (a subunit of NF-kappa-B, RELA) into the nucleus is impaired, which prevents activation of NF-KB-regulated genes. Recognized by serum from healthy humans exposed to L.monocytogenes as well from patients who have recovered from listeriosis.
Subcellular location: Secreted {ECO:0000269|PubMed:8641748, ECO:0000269|PubMed:8878044, ECO:0000269|PubMed:8975898}. Host cytoplasm {ECO:0000269|PubMed:20855622}.
Interaction partners:
Sequence:
MLKKNNWLQNAVIAMLVLIVGLCINMGSGTKVQAESIQRPTPINQVFPDPGLANAVKQNLGKQSVTDLVSQKELSGVQNFNGDNSNIQSLAGMQFFTNLKELHLSHNQISDLSPLKDLTKLEELSVNRNRLKNLNGIPSACLSRLFLDNNELRDTDSLIHLKNLEILSIRNNKLKSIVMLGFLSKLEVLDLHGNEITNTGGLTRLKKVNWIDLTGQKCVNEPVKYQPELYITNTVKDPDGRWISPYYISNGGSYVDGCVLWELPVYTDEVSYKFSEYINVGETEAIFDGTVTQPIKN
Protein: GH18514p (Serpin 47C, isoform A) (Serpin 47C, isoform B) (Serpin 47C, isoform C) (Q7K508)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serpin 85F
Sequence:
MASGGTTAPSLSASPIVFARNLFRALNDEVPPVNMMVSPAGARSAMTLVFMGAGGKSADELRSKLILGVSNKSEVAKQHAESWTDECSCAKKGVALRLVTRLYVNEEEKIRTDFNDMALEFFNAEAYSLNYLNPEDSVKKVNKWLEKHTFYTVRNLFTPEVFNSDSSVILVNSLFFRAKWNKIFPQQLTQIDDFWINPRQRMEVSMMRQIGQFRYGESKKLKSQILQLPFERSNLTMMIILPTAIDGLPELEEKLGQLDMNEVAAKSLMKEVDVTIPKFRIECTVDLKVPLQKMGINSVFDAGQADLSDLFEMKTPQKISEARHKVFLNVTEFGCEVAPEAEVQPEVLKKNPDRKFFKADRPFVFAIRDRKNVYFVGHFVKP
Protein: MIP14002p (Q8IR83)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Vacuolar protein sorting-associated protein VTA1 homolog
- Pre-mRNA-splicing factor SPF27
Sequence:
MAEKKSQDNKDNVSGSQNRTSRVEAHVRQQEENNAIFARLFASLDAEHRKLKELEERRSQLIEEMKNLRSLLFVENKKLRQTVAPISGGNPLPIPATSASSVVKKSSEKPSGSRTSPIIKSARLERRPSNKSVTIADPPTQSLTTSERPKASSSQGLKKKENRRSLVVPARKNKHRITLDNLSNTREDMLDEFDESALATSVGSNLQTLEQRRSNLEEREDIDEVLVSLSALFTFVDSQFTDQAILPSTPDTDDSKTDEVIPNTDQDPSFYLPSADSLFKDILGPNSPSLEVKLPEESLQLQPADIVECSANVAEIVENEHETETETETD
Protein: Neurofibromin (O01398)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTQKPGEWASALLARFEDQLPNRIGAYGTQARMSQDQLVACLIHISRYRFSLVISGLTKMLQRVNEAALQNRHEPERCYFESLVIILTTLERCLTNQTKDTARFEEAMNVKLLLREISQFVDVQSDSNPNAAQLKALASKVLFALSQNHFSAVFNRISARIQELTSCSEENPDYNDIELIQHIDMDMIKLTKLLQETITKFRSKRAPPLILLYSLEKAIWNWIEYHPQEFQDLQRGTNRDISTCWEPLMDFVEYFKTENKKSKTLVWPLQMLLLILNPSCLEAVVNELQQSEKEKEKDKEKVASKSAQSTSRDKDFSAKQFIESIKRGLGQHSPSKQVTESAAIACVKLCKASTYINNTDSNNVVFKLVQFFINDLKALLFNPAKPFSRGQGYNFADIELMIDCWVSCFRINPHNIEALKVCLNLSSPQAYHFVIVCSLLRLAHIYVDFRLQNKNPFRIVNQPRLSWWPQTDVVHYRSAELRALFTDTLNKATQGYIAHTPLRYITSLTLKSKDTQKGLTRAEEGPAHKMLLLLLVRLIHADPTLLLNTQGKVAHEVQSSTLELINGLVSLVHQTTMPDVAQEAMEALLALHAPEKIEVWNPEAPINTFWDVSSQVLFSISQKLIQHQIANYTDVLKWLREILICRNTFLQRHKDYAHVGSQIAICKQAHIKMEVVFFMYLWSVDLDAVLTSLSCFGLLCEEAEICCSSDELTVGFIMPNYHIYQELAQLSTSATDSRICFFDNTHGNVLSRLTLQKRIMTLLRKIEHCVHGVQPAWEETFRNWEVSSKVLQTYPKCKGEDGQAEVFHRGMGKRRASHQSSEHDLEEQINEWANMTWFLLALGGVCLHKRSSSRQMLLQQSQNNASLGSLAQNSLYSSSTSSGHGSLHPSTVSLSTLPPAPPQDVSYCPVTQFVGQLLRLLVCSNEKIGLNIQKNVKELVGEEMSTQLYPILFDQVRAIVEKFFDQQGQVNVNVTDINTQFIEHTIYIMKSILDPKANKDPNNDQPSPSEHLGVTSIEGMMLGIVRYVRHLDMTVYAIRIKTKLCQLVEVMMKRRDDLAFRQEMKFRNKLVEYLTDWVMGTSHQIAPPSSADAAILTNTSLIFRDLDQACMEAVAALLRGLPLQPEESDRGDLMDAKSALFLKYFTLFMNLLNDCIDSSEAEKEMNNTPLLPPRPRMAAGKLTALRNATILAMSNLLGANIDSGLMHSIDLGYNPDLQTRAAFMEVLTQILQQGTEFDTLAETVLADRFEQLVQLVTMISDKGELPIAMALANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLDEEEETCFEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRLPPQLRSMCHCLYQVLSKRFPNLLQNNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFSKEQHMLCFNDFLRDHFEAGRRFFIQIASDCETVDQTSHSMSFISDANVLALHRLLWTHQEKIGDYLSSSRDHKAVGRRPFDKMATLLAYLGPPEHKPVDSHMMFSSYARWSSIDMSSTNFEEIMVKHQMHEKEEFKTLKSMNIFYQAGTSKSGYPVFYYIARRYKIGETNGDLLIYHVILTLKPFCHSPFEVVIDFTHTCSDNRFRTEFLQKWFYVLPTVAYENVHAVYIYNCNSWVREYTKFHDRILAPLKGNRKLLFLESPNKLTDFIDAEQQKLPGATLSLDEDLKVFSNALKLSHKDTKVAIKVGPTALQITSAEKTKVLAHSVLLNDVYYASEIEEVCLVDDNQFTLSITNESGQLSFIHNDCDNIVQAIIHIRNRWELSQPDSVTVHQKIRPKDVPGTLLNMALLNLGSCDPNLRTAAYNLLCALTATFDLKIEGQLLETQGLCIPSNNTIFIKSVSEKLATNEPHLTLEFLEESIQGFQRTTIELKHLCLEYMTPWLKNLVKFCKSNDDSKKLKVSQILDKLINLTIDQKEMYPSVQAKIWGSIGQIPELIDMVLDNFLHKSITYGLGSPQVEIMADTAVALASANVQLVSKKVITRICRVMDKSCTNPTQYLEQHMMWDDIAILGRYLLMLSFNNCLDVATSVPYLFHTITFLVCSGSPSMRASTHGLVINIIHSLCTCTNPSFSEEAQRVLRLSLDEFSLPKFYLLFGISKVKSAAVTAFRSSCRHPTDKWLGNERVTQPLPADRERLSLPSLEVITDALLEIMEACMRDVPDCEWLNTWTSLARSFAFCYNPALQPRALIVYGCISKSVTDHEVKQLLRILVKALESFNDLILIEALVMCLTRIQPLLRPESPIHRALFWVAISVLQLDEITLYGAGLALLEQNLHTLKSQGCFDKKETIAEVMMKTREKLEWHFKQLDHAVGLSFRSNFHFALVGHLIKGFRHPTPTTVSRTSRVLTMLLGIIAKPLHRDKFEVTPDSVAYLTALVAVSEEVRSRCHVKHALPRWPADLSSSVENGEASGGVQAIGLPLSRRQKSWDILDQSALQFARQHKVPTLQNARVLFKTQRSFSVPTTKDPNNATGIEERQERGSRSSVSNESNVLLDPEVLPDLSIQALVLTVLATLVKYSSDEGETRVLYQYLAEGSVVFPKVFPVIHSLLDQKINNILSVSHDQVVLNSVQNIIQNMLASEDPSQQQLHFLQSCGFGGLWRFAGPFTKYNMMGESSELFVNCLEAMVETCLPGDESAPVPPSPRPYNLSSSLSSLTLGSPTDKAFSSESLDFYDNCPGSVSSLRRASHSKSRAKHRINDSPSH