wanglab/gogpt-training-data huggingface dataset:
Protein: TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (ESK2) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I) (Q64729)
Organism: Mus musculus (Mouse)
Function: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P36897}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P36897}. Cell junction, tight junction {ECO:0000250|UniProtKB:P36897}. Membrane raft {ECO:0000250|UniProtKB:P36897}. Cell surface {ECO:0000250|UniProtKB:P36897}.
Interaction partners:
- Mothers against decapentaplegic homolog 3
- Transforming growth factor beta-1 proprotein
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 7
- Transforming growth factor beta-3 proprotein
- Growth/differentiation factor 11
- TGF-beta receptor type-2
- Growth/differentiation factor 8
- Transforming growth factor beta-2 proprotein
- Activin receptor type-2B
Sequence:
MEAAAAAPRRPQLLIVLVAAATLLPGAKALQCFCHLCTKDNFTCETDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGAVTTTYCCNQDHCNKIELPTTGPFSEKQSAGLGPVELAAVIAGPVCFVCIALMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEGIKM
Protein: Heme A synthase-mitochondrial ferredoxin fusion protein (Electron transfer protein 1) [Cleaved into: Heme A synthase etp1(cd) (HAS) (EC 1.17.99.9) (Electron transfer protein cox15-like domain); Mitochondrial ferredoxin etp1(fd) (Adrenodoxin homolog) (Electron transfer protein ferredoxin domain)] (Q10361)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: [Heme A synthase etp1(cd)]: Mitochondrion inner membrane {ECO:0000269|PubMed:11841224}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Mitochondrial ferredoxin etp1(fd)]: Mitochondrion matrix {ECO:0000269|PubMed:11841224, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
- Protoheme IX farnesyltransferase, mitochondrial
- Probable mitochondrial-processing peptidase subunit beta
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase 24 kDa subunit homolog C11E3.12, mitochondrial
- Sulfide:quinone oxidoreductase, mitochondrial
- NADH-ubiquinone oxidoreductase 51 kDa subunit homolog SPBC18E5.10, mitochondrial
- Apoptosis-inducing factor 1
- Protein sco1
Sequence:
MNISRSSGLMRQFLLQPLRKGCDISCLGRSSWRMSRSFSGSSVLNEINLSRTKNLFLNDCKFNKNSFEKFFARRLSNSVAPTPGGILQETEKIPSKKVAFWLLGSSALVLAIVVVGGITRLTESGLSITEWKPITGVIPPLTDEQWNQEFELYKKSPEFEKLNSHMTVDEFKNIFFWEWFHRVLGRGIGLTILLPSIYMIVTKRASPWLSKRLIGLTGLVGLQGVIGWWMVKSGLSEELFSDGSHPRVSHYRLATHLAAAVALYIGLVWTGHGILQRHAFLKSMKSGSTSQLTSMVSSVQKMKGFRTSVNSFVGLVLITLLSGAFVAGLDAGMIYCTFPEMGEGRLAPSKSELFDQRFCRKDDKSDLIWRNMIDNPSLVQLEHRILAITTFVAACGLFIFSRAKRNILPKKIKTSINVVTGVVTAQATLGIMTLIYVVPVPLAALHQAGSLVTLTAALSLAQRLHPEYALKNIRSWTKLISSPPKSSISSSILTQQRQFHTFRPSFHSEIKKPLPGTGIKVFFVTPEGREIMIEGNEEGACEGSVACSTCHVIVDPEHYELLDPPEEDEEDMLDLAFGLEETSRLGCQVLLRKDLDGIRVRIPAQTRNIRLERPKA
Protein: Transmembrane protein 59-like (Brain-specific membrane-anchored protein) (Q9UK28)
Organism: Homo sapiens (Human)
Function: Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of APP. Inhibits APP transport to the cell surface and further shedding.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:20427278}; Single-pass type I membrane protein {ECO:0000305|PubMed:20427278}.
Interaction partners:
Sequence:
MAAVALMPPPLLLLLLLASPPAASAPSARDPFAPQLGDTQNCQLRCRDRDLGPQPSQAGLEGASESPYDRAVLISACERGCRLFSICRFVARSSKPNATQTECEAACVEAYVKEAEQQACSHGCWSQPAEPEPEQKRKVLEAPSGALSLLDLFSTLCNDLVNSAQGFVSSTWTYYLQTDNGKVVVFQTQPIVESLGFQGGRLQRVEVTWRGSHPEALEVHVDPVGPLDKVRKAKIRVKTSSKAKVESEEPQDNDFLSCMSRRSGLPRWILACCLFLSVLVMLWLSCSTLVTAPGQHLKFQPLTLEQHKGFMMEPDWPLYPPPSHACEDSLPPYKLKLDLTKL
Protein: Protein SHI RELATED SEQUENCE 2 (Protein STYLISH 2) (O65517)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds DNA on 5'-ACTCTAC-3' and promotes auxin homeostasis-regulating gene expression (e.g. YUC genes), as well as genes affecting stamen development, cell expansion and timing of flowering. Synergistically with other SHI-related proteins, regulates gynoecium, stamen and leaf development in a dose-dependent manner, controlling apical-basal patterning. Promotes style and stigma formation, and influence vascular development during gynoecium development. May also have a role in the formation and/or maintenance of the shoot apical meristem (SAM).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Electron carrier/iron ion-binding protein
- Probable indole-3-pyruvate monooxygenase YUCCA4
- AT-hook motif nuclear-localized protein 11
Sequence:
MAGIFSLGGNNNNNGDEEEENQQQQKTNWVWYRSNANTNNINPSSSQQVWQIPPEQMLMHHHSHPQQQSLDLYPGHQIDVSDLATSSRSITISCRDCGNQAKKDCTHMRCRTCCKSRGFDCSTHVRSTWIPVARRRERQQQLHMSTSGGGGGSGSGGAGGGGSSIPKRHRDPTLPGTSSSSRLPSHSAGLEMGEASFPGEVSSDALFRCVKMSGVDDGGDGQYAYQTTVNIGGHLFKGILYDQGPESSYMSGGSGGSDHQSSSAGGGGGGHPFNPPVVTDGGGGVSSAMFVDPNSGGYYSSNMTTSVFMPPGTQFYQNPPRS
Protein: RE18101p (Q8SZ36)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKLLFGLLMTVLALSGVFTLPARNDPQDDAEVIKVPSRPQPESDFHNFRGVIDTGSGYPFLQPNPSSFNVGIFDSFDDLFRRLRTRLWPVIGRDSGEEGASPTGDSDDSSDGSGAGFPFGVRPLIPLDSKNANTTSTIKVVNGHKVEINETVYGDSNSVFKVRLVNVRPLESGEEVAQGVHTSGGDFQPALEPSTSAPPKKFEEFDEEDDDDRREPLEKQPQDNEVRDIDEPKSTTPTNTSYTTNLHTSAPIDSEFEASDISEDIVETQPEEQKNTMDQLQQMMEPLREEIRHEEDLEQEHEDKEYLERKEKKEREEFDSSDDEDGEATTPVVMSETFNDEWAEFDQDQDREHDRNEDQDHDLDFENDLNNEIDIEENFVPIDLSNDIAVNDLAAADPNFPINEDAEFIVHPAVIRTMPMFEKLSLGGPAK
Protein: Zinc finger CCCH domain-containing protein 14 (AtC3H14) (Q9C9N3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions probably as a transcriptional factor that activates genes involved in secondary cell wall biosynthesis. May play a role in both transcriptional and post-transcriptional regulation. Binds to ssDNA, dsDNA, and ribohomopolymers in vitro. Maybe involved in post-transcriptional regulation of its target genes. Targets RNA of a polygalacturonase, a well-known cell wall modifying gene. Functions redudantly with C3H15 to regulate secondary cell wall formation. C3H14 and C3H15 have overlapping roles in the regulation of secondary cell wall formation and anther development. C3H14 may contribute more to secondary cell wall thickening while C3H15 could be more important in anther development. May regulate at both the transcriptional and post-transcriptional levels the expression of many genes involved in various biological processes, particularly those associated with cell wall metabolism and pollen development.
Interaction partners:
- Zinc finger CCCH domain-containing protein 59
- Zinc finger CCCH domain-containing protein 3
- Transcription factor MYB46
- Zinc finger CCCH domain-containing protein 62
- RING-type E3 ubiquitin transferase
- Uncharacterized protein At2g35736
- Zinc finger CCCH domain-containing protein 28
- Zinc finger CCCH domain-containing protein 17
- Zinc finger CCCH domain-containing protein 39
- Zinc finger CCCH domain-containing protein 47
Sequence:
MEKLAASTVTDLACVTAINSSPPPLSPISEQSFNNKHQEEFAASFASLYNSIFSPESLSPSPPSSSSPPSRVDTTTEHRLLQAKLILEYDELNEHYELCLNRLQSLMTELDSLRHENDSLRFENSDLLKLIRISTSSSSSVSPPAPIHNRQFRHQISDSRSAKRNNQERNSLPKSISVRSQGYLKINHGFEASDLQTSQLSSNSVSSSQKVCVVQTKGEREALELEVYRQGMMKTELCNKWQETGACCYGDNCQFAHGIDELRPVIRHPRYKTEVCRMMVTGAMCPYGHRCHFRHSLTDQERMMMMMLTR
Protein: Nanog homeobox (D3ZS29)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- POU domain protein
- Sal-like protein 4
- Signal transducer and activator of transcription 3
- CD44 antigen
- SRY-box transcription factor 2
- Ribonuclease 3
- Steroid hormone receptor ERR2
- Zinc finger protein 281.
- Nuclear receptor subfamily 0 group B member 1
- Nucleus accumbens-associated protein 1
Sequence:
MSVDLSGPHSLPSCEEASNSGDSSPMPAVHLPEENYSCLQVSATEMLCTETASPPPSSGDLPLQDSPDSSSNPKLKLSGPEADEGPEKKEENKVLTKKQKMRTVFSQAQLCALKDRFQRQRYLSLQQMQDLSTILNLSYKQVKTWFQNQRMKCKRWQKNQWLKTSNGLTQKGSAPVEYPSIHCSYSQGYLMNASGNLPVWGSQTWTNPTWNNQTWTNPTWSNQTWTNPTWSNQAWSTQSWCTQAWNSQTWNAAPLHNFGEDSLQPYVPLQQNFSASDLEANLEATRESQAHFSTPQALELFLNYSVNSPGEI
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform B) (Q0E8U2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Uncharacterized protein, isoform D
- Uncharacterized protein, isoform D
- GEO13501p1
Sequence:
MADNAVQAQPNGLGPQKQKALELHFSQVSYSLKGATKGSTPIINEACGVFKSGRLTAILGPSGAGKSTLLNALAGFKLQGVTGQFLLNGRPRDIMSFRKMSAYIAQNFVMLNLLTVEETLRVSTDLKMPSSTAAQEKQKIIDDIIDILQLQSCRRTLVKNLSGGEHKRLSIGIELVTNPPIMFFDEPTSGLDCVGSYQVICHLQRLAHDGRIVVCVVHQPGSRLFQLFDDVLVLAHGEVLYAGEQREMLPTFAQSGHICPQYYNPADFALEVCSQSSTTERCESLITQNKMMHSTASNVVKLQVDEETALIDVHKDALDLSHLRGKEQVGFWTQLSVLLRRHLRSMSRDMFAVQMRLVMHVVVALLLGVVYWQIGGDAQKIVSNVSCLFFVILFVFAGNAMPSILLCMQDSAVFIREYYNGWYSLGAYYLSKVLADLPLQLTCPTMFISIGYFMTGQPPEFQRFAMCWALCVMTAFIGHFIGVIAGSLFTMQLAIFLVPSATIPFLLFSGFFIRLNELSWFLRPICDVSFFRYIFEGLMRAIYGYDRGELECYATSNFCYYRTAEQFLKDFQMEGNEFDWDMAVLGIFLILLLLAFFVTLNAVIRRALR
Protein: Transmembrane protein 131 homolog (Q9V7H4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein, isoform H
- Transport and Golgi organization protein 1
Sequence:
MPTQVQMRPLLRIFAEPILLILIFLFTLGAKGEKVLQETFLGLQEAPIHDLGDLRLVPSRLDFGTWSVGQARSQTVTLFNQHSNRTLQLNAVAGPSPAFYSSFLGTREVPPQGNTTFNVVFLPRQLGAIAADLLIHTSFGQAELAVQGEGSECPYRLKPLVGIKAPMNATLTPEIHMYNPHERPLQILEIYSSGGEFQLELPSGGSEGPQNLWKIPPHTLKPVIRISFHGRTAGNHSAYIRIKVAEQELDIFIPVEFEILPRHSVYARNPLADFGRVATLNAPDALQFKLDVRNDESRQLFGSYLRQIPGLSFDANNTSIVLDASLFEGDEIINDLLVINSNQSSTSPGADQPFTVLVRAEIFHGGLTFDRNATRFVTTSPEGVEGEPLERKRSLVVRNKFAIPLMLFNVSLTEPIDESILEVTLVGDPRILIQPDESVELLRLNLLNDQVPFKSFLRIETNVTVFKLPLVSCSGRLHVSTQPIVLNFRQESLEKAAYNLELDLGTVPFAEMSRDGFVILRNDNPVPVRITNWFFKHPKTVYSQSTFLGCRATAIGHPVSVENDTKGWHLCTEIRAGESAVFKVAIQTYEADATFGTLKVWTPYEVIRVRVKFEASVGHLEIDQEQLSFKNCFPGKMCTAVLSIRSSFTHPVHVKGISFALPVGLRFKDFNAKGTTIAPQTLTKVGRIYFDPASVCRNNCYIRESTNDLAIFPSVPGGGNGNSGVINNNLLYDGVELRQRTELFRQLRRQLSSMSLTLHSEELPPLELDFSITIEWPKLVQFQPIPPTPAIEVGQVQRQWITLTNPSQSPLLLDYFLSDPAFARRTQLSLPHEVIDVSSTSCYLTDKEVFSLPEAGDPILLPGGASLTIPITFSAQLPEKYCTLLHVRSNLTLYEAVWLQARAVQSQFRFGNRRPGAASPLLFEMATNQFQGCQSGNEAVVVTRSFTARNSGVIPIRIEGFLIGSLPCEDFGFKVMDCAGFDLGENEARKVEIAFSADFTTSAVKRSLTLLTNLTYDISYKLLAQMPAESVELCASLLVRPGWESSLKNAALVVLLASFGLVLVAAVFDAKAIMVQQNAYDAARNKGPLQPTFNLRNIVKLQAEEAAAKAESVQQQQKVKNGQLKELRKRTVVNSTNSKSKSKSSWSPWSMDMNALSKHLQKAKPKTVVSTPVTPPAASAPAAAPVPLPEAKPVKKSSTPSPQGVPISVQVRPQKKVKPTPAVVLGTTKPKQEVSTPVADQHEKSLAKSSPPQQENISPKPNKPPEQRVLKEQNGSAKKMGKTPGRERERERRSKDQKLTNGTGAGVGFRKPERKQRQKLNFGQTTNSTSPPESPDALKCISNPWETSSRVSFRDVLRTPQMAPTDNGFDWNHATSSSDLGPIGDNRKNATPPMVTSLWEPLSATASNSLFANTEVDFITPDAIYEQREREKPQWEQRSDLVMRQQLLLQQPQKLEFQLRQQEKISLLANMDPSNWATNWSPLGYSTWPNATAGIGVMRPPPGLEQSARQTHNLAQEQVSAGPASGTGAALHGESLPTQYDPFTSPSSIWSDTWRQSSQRNNHNHMN
Protein: Adenosine 3'-phospho 5'-phosphosulfate transporter 2 (3'-phosphoadenosine 5'-phosphosulfate transporter) (PAPS transporter 2) (Solute carrier family 35 member B3) (Q9H1N7)
Organism: Homo sapiens (Human)
Function: Mediates the transport of adenosine 3'-phospho 5'-phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. Compensates for the insufficient expression of SLC35B2/PAPST1 during the synthesis of sulfated glycoconjugates in the colon.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16492677}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nucleotide sugar transporter SLC35D1
- Solute carrier family 35 member D3
- Nucleotide sugar transporter SLC35D2
- GDP-fucose transporter 1
Sequence:
MDLTQQAKDIQNITVQETNKNNSESIECSKITMDLKFNNSRKYISITVPSKTQTMSPHIKSVDDVVVLGMNLSKFNKLTQFFICVAGVFVFYLIYGYLQELIFSVEGFKSCGWYLTLVQFAFYSIFGLIELQLIQDKRRRIPGKTYMIIAFLTVGTMGLSNTSLGYLNYPTQVIFKCCKLIPVMLGGVFIQGKRYNVADVSAAICMSLGLIWFTLADSTTAPNFNLTGVVLISLALCADAVIGNVQEKAMKLHNASNSEMVLYSYSIGFVYILLGLTCTSGLGPAVTFCAKNPVRTYGYAFLFSLTGYFGISFVLALIKIFGALIAVTVTTGRKAMTIVLSFIFFAKPFTFQYVWSGLLVVLGIFLNVYSKNMDKIRLPSLYDLINKSVEARKSRTLAQTV
Protein: Transcriptional activator VP30 (EbolaVP30) (eVP30) (Minor nucleoprotein VP30) (Q77DJ5)
Organism: Zaire ebolavirus (strain Kikwit-95) (ZEBOV) (Zaire Ebola virus)
Function: Multifunctional protein that acts as a viral transcriptional activator. Promotes read-through of an RNA hairpin in the NP open reading frame to enhance viral transcription. Mechanistically, nonphosphorylated VP30 hexamers form a ternary complex with the viral leader RNA. Clamps the RNA template and the complex VP35-polymerase L together, thereby increasing the polymerase affinity for the RNA template to increase transcription initiation despite the presence of RNA secondary structures. Assists also stop-start transcription at gene junctions to promote transcription of downstream genes. Interaction with NP plays a critical role in transcription initiation by recognizing the RNA stem loop (By similarity). Interaction with host RBBP6 interferes with NP-VP30 interaction and inhibits viral RNA synthesis. Also acts as a suppressor of RNA silencing by interacting with host DICER1 and TARBP2/TRBP.
Subcellular location: Virion {ECO:0000250|UniProtKB:Q05323}. Host cytoplasm {ECO:0000250|UniProtKB:Q05323}. Note=Present in viral inclusion bodies due to its interaction with NP. {ECO:0000250|UniProtKB:Q05323}.
Interaction partners:
Sequence:
MEASYERGRPRAARQHSRDGHDHHVRARSSSRENYRGEYRQSRSASQVRVPTVFHKKRVEPLTVPPAPKDICPTLKKGFLCDSSFCKKDHQLESLTDRELLLLIARKTCGSVEQQLNITAPKDSRLANPTADDFQQEEGPKITLLTLIKTAEHWARQDIRTIEDSKLRALLTLCAVMTRKFSKSQLSLLCETHLRREGLGQDQAEPVLEVYQRLHSDKGGSFEAALWQQWDRQSLIMFITAFLNIALQLPCESSAVVVSGLRTLVPQSDNEEASTNPGTCSWSDEGTP
Protein: Jasmonoyl--L-amino acid synthetase GH3.5 (EC 6.3.2.52) (Auxin-responsive GH3-like protein 5) (OsGH3-5) (Indole-3-acetic acid-amido synthetase GH3.5) (Jasmonate-amino acid synthetase JAR1) (Jasmonic acid-amido synthetase JAR1) (Protein JASMONATE RESISTANT 1) (OsJAR1) (Q6I581)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the synthesis of jasmonate-amino acid conjugates by adenylation. Catalyzes the conjugation of jasmonate (JA) to Ile when expressed in a heterologous system (E.Coli). Catalyzes in vitro the conjugation of jasmonate (JA) to Ile, Phe, Cys, Leu, Met, Ala, Val and Trp. Involved in the production of JA-Ile in response to infection by the rice blast fungus Magnaporthe oryzae. Required for the accumulation of the flavonoid phytoalexin sakuranetin in response to infection by the rice blast fungus. Involved in herbivory-induced JA-Ile accumulation. Involved in the production of JA-Ile in response to wounding. Required for modulation of light and JA signaling in photomorphogenesis. Required for normal seed development. Required for optimal flower opening and closing and anther dehiscence. May catalyze the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin (By similarity).
Interaction partners:
Sequence:
MTICSCEETINEFEMLTRDAARVQKDTLKKILEINASAEYLQNFGLGGRTDAESYKSCIPLCVHNDIEPYIQRIVDGDTSPVVTGEPITNLSLSSGTTHGKPKFIPFNDELLETTLQIYRTSYAFRNREYPIGQGKALQFVYGSKQVITKGGILATTATTNLYRRQRYKEGMKDIQSQCCSPDEVIFGPDFHQSLYCHLLCGLIYSEEVHSVFSTFAHSLVHAFQTFEEVWEDLCTDIRDGVLSKKVTAPSIREAVSKILKPNPELADSIYKKCIGLSNWYGVIPALWPNAKYVYGIMTGSMEPYLKKLRHYAGNLPLISADYGASEGWVGSNIDPTVPPEQVTYAVLPQVGYFEFIPLEKPIGEETENSASIHYIESDPVGLTEVEVGKIYEVVITNFAGLYRYRLGDVVKIARFHNSTPELQFICRRSLVLSINIDKNTEKDLQLAVEEASKFLEGEKLEVMDFTSFVERSSDPGRYVIFWELSGDASDEVLSSCANALDLAFIDAGYTGSRKIKTIGPLELRILRKGTFKEILDHFLSLGGAVSQFKTPRFVNPSNSKVLQILSRNVTQSYFSTAYGF
Protein: Fusion glycoprotein F0 [Cleaved into: Fusion glycoprotein F2; Fusion glycoprotein F1] (P04849)
Organism: Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5)
Function: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).
Subcellular location: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MGTIIQFLVVSCLLAGAGSLDPAALMQIGVIPTNVRQLMYYTEASSAFIVVKLMPTIDSPISGCNITSISSYNATVTKLLQPIGENLETIRNQLIPTRRRRRFAGVVIGLAALGVATAAQVTAAVALVKANENAAAILNLKNAIQKTNAAVADVVQATQSLGTAVQAVQDHINSVVSPAITAANCKAQDAIIGSILNLYLTELTTIFHNQITNPALSPITIQALRILLGSTLPTVVEKSFNTQISAAELLSSGLLTGQIVGLDLTYMQMVIKIELPTLTVQPATQIIDLATISAFINNQEVMAQLPTRVMVTGSLIQAYPASQCTITPNTVYCRYNDAQVLSDDTMACLQGNLTRCTFSPVVGSFLTRFVLFDGIVYANCRSMLCKCMQPAAVILQPSSSPVTVIDMYKCVSLQLDNLRFTITQLANVTYNSTIKLESSQILSIDPLDISQNLAAVNKSLSDALQHLAQSDTYLSAITSATTTSVLSIIAICLGSLGLILIILLSVVVWKLLTIVVANRNRMENFVYHK
Protein: Frizzled (Frizzled-1) (dFz1) (Q24760)
Organism: Drosophila virilis (Fruit fly)
Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Required to coordinate the cytoskeletons of epidermal cells to produce a parallel array of cuticular hairs and bristles.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Segment polarity protein dishevelled
- EGF-like domain-containing protein
- Protein Wnt
- Protein Wnt
- receptor protein-tyrosine kinase
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Glypican-6
- receptor protein-tyrosine kinase
Sequence:
MLLQPLLLLLLPALLQSAQRYDQTPLDASSYYRSDLTGSSASSLDGFPHHNRCEPITISICKNIPYNMTIMPNLIGHTKQEEAGLEVHQFAPLVKIGCSADLQLFLCSLYVPVCTILERPIPPCRSLCESARVCETLMKTYNFNWPENLECSKFPVHGGEDLCVAENTTASSSTPAPTRSAPKVTTRKHQISVDSPHRNIGFVCPVQLKTPLGMGYELKVGGKDLHDCGAPCHAMFFPERERTVLRYWVGSWAAICVASCLFTVLTFLIDSSRFRYPERAIVFLAVCYLVVGCAYVAGLGAGDSVSCREPFPPPVKLGRLQMMSTITQGHRQTTACTVLFMALYFCCMAAFAWWSCLAFAWFLAAGLKWGHEAIENKSHLFHLVAWAVPALQTISVLALAKVEGDILSGVCFVGQLDTHSLGGFLILPLCIYLSIGALFLLAGFISLFRIRTVMKTDGKRTDKLERLMLRIGFFSGLFILPALGLLGCLFYEYYNFDEWMIQWHRDICKPFSIPCPAARPPGTPEARPIFQIYMVKYLCSMLVGVTSSVWLYSSKTMVSWRNFVERLQGKEPRTRAQAYV
Protein: Protein ELF4-LIKE 4 (Q570U6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the central CCA1/LHY-TOC1 feedback loop in the circadian clock that promotes clock accuracy and is required for sustained rhythms in the absence of daily light/dark cycles.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Acetyl-CoA acetyltransferase 1
- Acetyl-CoA acetyltransferase 2
- 3-ketoacyl-CoA thiolase 5, peroxisomal
- 3-ketoacyl-CoA thiolase 2, peroxisomal
- 3-ketoacyl-CoA thiolase 1, peroxisomal
- Protein ANTHESIS POMOTING FACTOR 1
- Protein EARLY FLOWERING 3
- Protein GIGANTEA
- Isovaleryl-CoA dehydrogenase, mitochondrial
- AT4g33140/F4I10_70 superfamily protein)
Sequence:
MEGDVLSGFGDRHNMDGKLLQSFQKSFVDVQDILDQNRLLINEINQNHESKQPDNLGRNVGLIKELNNNIRRVASLYGDLSHSFARSVDASSEGESSGTLKSDGKANQKRFRSG
Protein: Trace amine-associated receptor 13e (Q5QNP8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDLSAQEYDASQFCFPAVNNSCLKGTHHVSTQTVVYLVLASAMTVTILGNSVVIISIAHFKQLQTPTNILVMSLALADLLLGLVVMPFSMIRSVDGCWYYGETFCLLHSSFDMFLTSVSIFHLIFIAVDRHQAVCFPLQYPTMITIPVAWVMVIISWSMAAFYSYGLVYSKANVEGLEEYIESIYCMGGCTLLFNALWGAIDTLVAFFLPCFVMIGLYARIFMIAKKHARKLGEANQHDNENLFKSSRRSERKAAKTLGIVVGAFVICWLPFFINSMMDPYINFSTPGVLFEAFVWLGYMNSAINPIIYGLFYPWFRKTLYLIITLRMFEPNSSDINVFTV