wanglab/gogpt-training-data huggingface dataset:
Protein: ABC-2 type transporter transmembrane domain-containing protein (Q8CDR1)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MASWESRKLLLLLWKNFTLKRRKFGTLVSEIVLVLLLSIVLLTTRHLLSIKKIEALYFPDQPISTVPSFFRASVTSFYPWELAYVPSNIMVVENIVKNVKNDLNLHMKVIGFPSESDFEDYARSTVNSRNILAAIVFGHNFANSSDPLPKKVKYYLRFSDIKKNINSGAYYQGDTWLTKFLFHSLRLVGPRNPYEADGGSPGYITEGFLAVQHALDKAIMLHHGGADAAALFNDISLFIQRFPYPAYYHDYFYLFATTFIPLTVACTFFFNHYVLVWSIVWEKENRLKEYQLMIGLRNWMFWVAYFFTFLCLYFINIIVMCMVLFVKIEPAPIFQYNDPTLVFIFLLFYAISSIFFSFMVSTLFNKVSLAMSLGSFLFFLTYFPAVAMHQSFERMPSKQKLIWSFDFNVGMAFGFRFLVNTDAKKTGMKWSNIFLSTDSDSFLFAYVLGMLLADAFIYGLVAWYIEAVFPGEYGVPKPVEFFLDALLLVWRTTSTKTRNHPIL
Protein: Uncharacterized protein AFUA_6G02800 (Q4WCX9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
Sequence:
MKFSPAYLLAFAPIVAAHFRLQYPTSRGFNADTMANFPCGDLAQSSNRTQVSLSSGSFPVALRMGHDETAVEVLLALGNDPGTNFNITLHPTFRIEGLGEFCLPNVVFDESVLGTKITDGMNATLQVQSNGDPSGGLYACADIQFSTTAQDEKPSSCTNNTGISAIAFTGAAAERNANESTADGQAQSGSSGSSSDSGSHSGHSSATQTSSTTASSTAGAVALETAAWGILGAAVVGGLAVL
Protein: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA) (Q9Z2I9)
Organism: Mus musculus (Mouse)
Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03220}.
Interaction partners:
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
Sequence:
MAASMFYGRQLAAAALRSHRPQTTLRAAAQVLGNSGLFNKHGLQVQQQQQRTLSLHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFTSGLKGGVKIVFSPEEAKAVSSQMIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGIKKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDWSQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQAILVNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSEIVTLAKEAHVDVKFQLPI
Protein: Tissue factor (Coagulation factor III) (B0UY88)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Coagulation factor VII.
- Coagulation factor IX
- coagulation factor Xa
- Coagulation factor VII precursor
- Centrosomal protein 170Ab.
Sequence:
MGIQTVICSALFLAFLALVNGSPASMDVGKLTKATNVSWTSYNFKTILSWGPKPVNYTYTVEFSRTNRDKQRNPHCIRSTETECDLTNDLDINEVYSAEVLSEPLPSMNIDQVEPPYSRSKIFRPYDDTLIGRPQFTLTVSIDKKLVLTIQDPITALHKDNRSLNIRDIFKKNLKYKVAYSKAGSTGKKIKVVEESRAEFNRLDEDQSYCFSVAAYIPNRKGDKRLGEWSLPKCSPQESKSLFEEYGLAVIGGAALATLAFVIAVIVLIVVCCKRAQKQTPTAKETIV
Protein: Casein kinase II subunit beta-3 (CK II beta-3) (O81275)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a complex role in regulating the basal catalytic activity of the alpha subunit. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis. CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation. Stimulates the binding of CCA1 to promoters (Probable).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16926165}. Nucleus {ECO:0000269|PubMed:16926165}.
Interaction partners:
- Casein kinase II subunit alpha-1
- Casein kinase II subunit alpha-3
- Casein kinase II subunit alpha-4, chloroplastic
- Casein kinase II subunit alpha-2
- Protein CCA1
- FACT complex subunit SSRP1
- Casein kinase II subunit beta-1
- Ribosomal RNA-processing 7 protein
- Nucleolar protein
- FACT complex subunit SPT16
Sequence:
MYKERSGGGGGGSSRSEILGGAIDRKRINDALNKKLEKSSTSTTTSRVFSSKDKDPFSFTSTKTQLPDVESETDSEGSDVSGSEGDDTSWISWFCNLRGNDFFCEVDEDYIQDDFNLCGLSGQVPYYDYALDLILDVDASNSEMFTDEQHEMVESAAEMLYGLIHVRYILTTKGMAAMTEKYKNCDFGRCPRVFCCGQSCLPVGQSDIPRSSTVKIYCPKCEDISYPRSKFQGNIDGAYFGTTFPHLFLMTYGNLKPQKPTQSYVPKIFGFKVHKP
Protein: Spermiogenesis protein SPE-29 (G5ED71)
Organism: Caenorhabditis elegans
Interaction partners:
- CX domain-containing protein
- SPE-12
- Spermatocyte protein spe-27
- Spermatocyte protein spe-8
- Serine/threonine-protein kinase spe-6
- Domain of unknown function DX domain-containing protein
- Uncharacterized protein
- Palmitoyltransferase spe-10
- Trypsin-like protease try-5
- Dendritic cell-specific transmembrane protein-like domain-containing protein
Sequence:
MTNSHTHNGNRIWFICSWENGPICYGMALDLIGGISLIAFSVLLVGVIFFGWFGIFPKVIRRKLHD
Protein: Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.-) (SET domain-containing protein 7) (D4ADE5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR037249}. Chromosome {ECO:0000256|PIRNR:PIRNR037249}.
Interaction partners:
- Forkhead box O3
- Forkhead box protein O1
- Forkhead box O4
- Forkhead box O6
- SUZ12 polycomb repressive complex 2 subunit
- Polycomb protein EED
- [histone H3]-lysine
- [histone H3]-lysine
- DNA
- [histone H3]-lysine
Sequence:
MDSDDEVVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCWIHYPDGGSLVGEVNEDGEMTGEKIAYVYPDQRTALYGKFIDGEMLEGKLATLMATEEGKPHFELTSGSSVFHFDKSTSSCISSDALLPDPYESERVYVADSLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCVYDMFVHPRFGPIKCIRTLRAVEAEEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQQK
Protein: Arginine vasotocin (B9VJ17)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MPDSTIPLLCVLGLLALSSACYIQNCPRGGKRSFPDLPRQCMSCGPGDRGRCFGPNICCGEGMGCYVGSPEAAGCVEENYLPSPCEAGGRVCGSEGSCAASGVCCDSESCVLDPDCL
Protein: Inward rectifier potassium channel C-terminal domain-containing protein (Q382T2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU003822}.
Interaction partners:
Sequence:
MSSRMSQKLRGHSLAPKRQKPLVNPELLLASPTDSTRGGSKQFVRAFNDDGCLSTREVGVRWFNFALLSIFYTLRSQPWSLLITYTILLYVGILFVFSAAYVVWARGCGAQDGSTWVSALYFTVVSFAANGGYVGEQQDTMLDPHHVCFTGRTLIVTLLSFGNIIFVGLVAALVVGKAAYGEELGHRIVFSDFCSLAMAPGTKDRDCWDLTFRMANSSSSKALAHGQLRLFIVTSEPTDNSRHQRKRRKSSVDRTETRRHATSSHHHIDDKSKRSGQLSKHLEHHISDGTVQTETHPHRREGELDDVTRMDRESREWADAESHIVEVLAEEHLKRKRGREHTSKRQVLSSPATSSCSSDADGGASFGGATGSGCSYVPINSPESALKQVSIQVEELRWTCSGEKHLDGRDGRLLLWFPVDITHTINRYSPLYRYVKHNMTNSLCTLNSLQVASPAIPQEAISEEEGGPAATAAFPCSFQLVVIFDATEMESGRHISARHTYAADDIIKHYRFSNKVVRMSPEKREVLVDYHYFNEMLSDVVSPLHRTERVRTR
Protein: Protein isd11 (O60068)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for mitochondrial iron-sulfur (Fe-S) protein biosynthesis.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Iron sulfur cluster assembly protein 1, mitochondrial
- Frataxin homolog, mitochondrial
- Probable cysteine desulfurase, mitochondrial
- Putative glutamine amidotransferase PB2B2.05
- GTP-binding protein ypt1
- Iron-sulfur cluster assembly factor IBA57
- Putative acyl carrier protein, mitochondrial
- Monothiol glutaredoxin-5
- GrpE protein homolog
- J-type co-chaperone jac1, mitochondrial
Sequence:
MSVSKQHVVRLYRNILKTSKLFPYTYREYTIRRTRDKFKELKVESDPAKFEQGIKDSEKLLEIIQRQSIINGMYNKRNLVVEGIDDTAEGEVKKSFENASQS
Protein: Beta-parvin (Affixin) (Q9HBI1)
Organism: Homo sapiens (Human)
Function: Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration.
Subcellular location: Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cytoplasm, myofibril, sarcomere. Cytoplasm, myofibril, sarcomere, Z line. Note=Constituent of focal adhesions. Detected at the tips of the leading edge of cells. Colocalizes with F-actin at the tips of lamellipodia.
Interaction partners:
- Rho guanine nucleotide exchange factor 6
- LIM and senescent cell antigen-like-containing domain protein 1
- Scaffold protein ILK
- Paxillin
- Alpha-parvin
- Ras suppressor protein 1
- Alpha-actinin-1
- Actin, cytoplasmic 1
- Gamma-parvin
- Talin-1
Sequence:
MSSAPRSPTPRPRRMKKDESFLGKLGGTLARKRRAREVSDLQEEGKNAINSPMSPALVDVHPEDTQLEENEERTMIDPTSKEDPKFKELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWALRWSVDSIHGKNLVAILHLLVSLAMHFRAPIRLPEHVTVQVVVVRKREGLLHSSHISEELTTTTEMMMGRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQKVHNVSFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE
Protein: Protein tyrosine phosphatase, receptor type, O (A0A8I5YC57)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGHLPRERRGGRRLLPLLGLFVLLKIVSTFHVTVRDDNNIVVSLEASDVVSPTSVYVVRVAGESKNYFFEFEESNGTLPPPVVFKATYHGLYYIISLVVVSGNVVTKPSRSITVLTKPLPVTSVSIYDYKPSPETGVLFEIHYPEKYNVFSRVNISYWEGKDFRTMLYKDFLKGKTVFNHWLPGICYSNITFQLVSEATFNKSTLVECSGVSHEPKQHRTAPYPPRNISVRFVNLNKNNWEEPSGSFPEDSFIKPQDAIGRDRPFHFPEETPETPASNASSGWPDPNGTEYESTSQPYWWDSASAAPENEEDFVSVLPADYDTEATLGRTEKPTADPFSAFPVQMTLSWLPPKPPTAFDGFNILIEREGNFTDYLTVDEEAHEFVAELKEPGKYRLSVTTFSSSGACETRKSQSAKSLSFYISPTGEWIEELTEKPQHVSVHVLSSTTALLSWTSSQENYNSTIVSVVSLTCQKQKESQRLEKQYCTQVNSSKPVIENLVPGAQYQVVMYLRKGPLIGPPSDPVTFAIVPTGIKDLMLYPLGPTAVVLSWTRPYLGVFRKYVVEMFYFNPTTMTSEWTTYYEIAATVSLTSSVRIANLLPAWYYNFRVTMVTWGDPELSCCDSSTISFITAPVAPEITSVEYFNSLLYISWTYGDATTDLSHSRMLHWMVVAEGRRKIKKSVTRNVMTAILSLPPGDIYNLSVTACTERGSNTSMLRLVKLEPAPPKSLFAVNKTQTSVTLLWVEEGVADFFEVLCQKLGSGHDGKLQEPVAVSSHVVTISSLLPATAYNCSVTSFSHDSPSVPTFIAVSTMVTEVNPNVVVISVLAILSILLIGLLLVTLVILRKKHLQMARECGAGTFVNFASLEREGKLPYSWSKNGLKKRKLTNPVQLDDFDSYIKDMAKDSDYKFSLQFEELKLIGLDIPHFAADLPLNRCKNRYTNILPYDFSRVRLVSMNEEEGADYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSRIIVMLTQCNEKRRVKCDHYWPFTEEPIAYGDITVEMVSEEEQEDWASRHFRINYADEAQDVMHFNYTAWPDHGVPPANAAESILQFVYTVRQQATKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQLMWLKKKQQFCISDVIYENVSKS
Protein: Peroxiredoxin-1 (EC 1.11.1.24) (HBP23) (Heme-binding 23 kDa protein) (Thioredoxin peroxidase 2) (Thioredoxin-dependent peroxide reductase 2) (Thioredoxin-dependent peroxiredoxin 1) (Q63716)
Organism: Rattus norvegicus (Rat)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06830}.
Interaction partners:
- Sulfiredoxin-1
- Thioredoxin
- Peroxiredoxin-5, mitochondrial
- Superoxide dismutase
- Thioredoxin, mitochondrial
- Thioredoxin reductase 1, cytoplasmic
- Superoxide dismutase, mitochondrial
- Parkinson disease protein 7 homolog
- Glutathione reductase
Sequence:
MSSGNAKIGHPAPSFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWINTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITINDLPVGRSVDEILRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVNKSKEYFSKQK
Protein: Trehalose-6-phosphate phosphatase (TPP) (EC 3.1.3.12) (Osmoregulatory trehalose synthesis protein B) (Trehalose 6-phosphate phosphatase) (Trehalose-phosphatase) (P31678)
Organism: Escherichia coli (strain K12)
Function: Removes the phosphate from trehalose 6-phosphate (Tre6P) to produce free trehalose. Also catalyzes the dephosphorylation of glucose-6-phosphate (Glu6P) and 2-deoxyglucose-6-phosphate (2dGlu6P).
Interaction partners:
- Trehalose-6-phosphate synthase
- Cytoplasmic trehalase
- Periplasmic trehalase
- Trehalose-6-phosphate hydrolase
- PTS system trehalose-specific EIIBC component
- PTS system glucose-specific EIIA component
- Catalase HPII
- Transaldolase A
- Potassium binding protein Kbp
- Fructose-bisphosphate aldolase class 1
Sequence:
MTEPLTETPELSAKYAWFFDLDGTLAEIKPHPDQVVVPDNILQGLQLLATASDGALALISGRSMVELDALAKPYRFPLAGVHGAERRDINGKTHIVHLPDAIARDISVQLHTVIAQYPGAELEAKGMAFALHYRQAPQHEDALMTLAQRITQIWPQMALQQGKCVVEIKPRGTSKGEAIAAFMQEAPFIGRTPVFLGDDLTDESGFAVVNRLGGMSVKIGTGATQASWRLAGVPDVWSWLEMITTALQQKRENNRSDDYESFSRSI
Protein: Tropomyosin alpha-1 chain (Alpha-tropomyosin) (Tropomyosin-1) (Q5KR49)
Organism: Bos taurus (Bovine)
Function: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress fibers. {ECO:0000250|UniProtKB:P04692}.
Interaction partners:
Sequence:
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Protein: Tumor necrosis factor receptor superfamily member 6B (Decoy receptor 3) (DcR3) (Decoy receptor for Fas ligand) (M68) (O95407)
Organism: Homo sapiens (Human)
Function: Decoy receptor that can neutralize the cytotoxic ligands TNFS14/LIGHT, TNFSF15 and TNFSF6/FASL. Protects against apoptosis.
Subcellular location: Secreted.
Interaction partners:
- Tumor necrosis factor ligand superfamily member 14
- Tumor necrosis factor ligand superfamily member 6
- Tumor necrosis factor ligand superfamily member 15
- Tumor necrosis factor receptor superfamily member 25
- Tumor necrosis factor receptor superfamily member 1A
- Tumor necrosis factor ligand superfamily member 8
Sequence:
MRALEGPGLSLLCLVLALPALLPVPAVRGVAETPTYPWRDAETGERLVCAQCPPGTFVQRPCRRDSPTTCGPCPPRHYTQFWNYLERCRYCNVLCGEREEEARACHATHNRACRCRTGFFAHAGFCLEHASCPPGAGVIAPGTPSQNTQCQPCPPGTFSASSSSSEQCQPHRNCTALGLALNVPGSSSHDTLCTSCTGFPLSTRVPGAEECERAVIDFVAFQDISIKRLQRLLQALEAPEGWGPTPRAGRAALQLKLRRRLTELLGAQDGALLVRLLQALRVARMPGLERSVRERFLPVH
Protein: Protein SUBSTANDARD STARCH GRAIN 4, chloroplastic (Translocon at the inner-envelope- membrane of chloroplasts SSG4) (W0RYD3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Part of the inner chloroplast membrane translocon complex (TIC) which associates with the outer chloroplast membrane translocon complex (TOC) and forms a supercomplex involved in protein precursor import into the chloroplast stroma (By similarity). Required for the regulation of starch granule size in amyloplasts.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000250|UniProtKB:F4ISL7}; Single-pass membrane protein {ECO:0000255}. Plastid, chloroplast intermembrane space {ECO:0000250|UniProtKB:F4ISL7}. Plastid, chloroplast {ECO:0000269|PubMed:24335509}. Plastid, amyloplast {ECO:0000269|PubMed:24335509}.
Interaction partners:
Sequence:
MSHCLRASPFLSPPPPLLHPSRRRRHRQGGCIHTSPGTRPLVARARFDPPPLLRLKVSDSSDCPAPHHPHSQHQPLLPTRRQQQQPPPPYQALVASLAPLWREGLFLVRCSVFAAALSVAAALSWYAQLRARSFVESRLLPAACAALGEFLQREVHLGRVRSVSPLGITLHTCSIGPHAEEFSCAEVPVMKIRVRPFASLRRGRVVVDAVLSEPSALVAQRKDFSWLGLPAPSEGSPKRHSGEEGIDYRTKTRRLAREKAAEQWNEERDKAAREAAEMGYIVPSAQSISPSIDEMMEDDGPVDTGKSSPHLCPDEMHRKDHHIDAGIDSSSKHADLEKSFGVKARIPGISFWSRMIPNPSRRRYRRKAHSKLISDTDNSSQQRILRRSAYAAVAYFQNECSGNPDDSLPGPGESSSDGGHTNGGGEEGSPNDGPTEYSETTSMDYGELPPEKSNFASTMLIGNTDVLNGSSHNQQPSQISSHSWENNEQVSEAPVLKKRKNISEDDYRQEFDFGAFGSCTYAHNWLSFWPFQLKGFPVGFNAPSASLNVQIQKLRSLFAIGPGDNSAELSQGVGQIHPGAVQQTLPITLDSVYFNGGNLMLLGYGDQEPREMKHANGHIKFKNSYNRVHVHVTGNCMEWRQDRTSQGGGYLSTDVFVDIAEQTWHANLNVVNAFAPLFERILEIPVVWNKGRATGEVHLCMSKGDSFPSIHGQLDVKGLAFQILDAPSSFSDIVATLSFRGQRVFLHNASGWFGDAPVEASGDFGLNPEDGEFHLMCQVPSVEVNALMKTMKMRPLMFPLAGAVTAVFNCQGPLDAPVFVGSGIVSRKSLSVSGMLPSAASEAVMQNKESGAVAAFDHIPFTHVSANFTFNLDNCVADLYGIRACLLDGGEIRGAGNVWICPEGEGDDSAMDINLSGSILLDKVLHRYIPGGIQLIPLKIGELNGETRLSGSLIRPKFDIKWAAPNAEDSFSDARGNIVIAHDYIMVNSSSVSFDLNTHIQTSYIDDYLLHKEMYQRKKIMPLIVEGVDLDLRMRGFEFAHIASSIPFDSPRPLHLKASGRFKFQGKVVKYSQLVDEKNHGAIQGTIDQSKLENDVSRLVGEISLSGIKLNQLMLAPQSTGFLSISPDSIMLNATGRPDENFSIEVNVPLFFGTHEAIQDGRLLSIFLQKGQLRSNICYHPENLTSLEVRNLPLDELEFASLRGFVQKAELQLNFQKRRGHGLLSVIRPKFSGMLGESLDIAARWSGDVITMEKSVLEQANSKYELQGEYVFPGTRDRFPMESQSNGFIEKAMGGHLGSMMSSMGRWRMRLEVPGAEVAEMLPLARLLSRSTDPAIRSRSKELFMQTLHSVGFNAESLRDQLKALEMYPDWLDDDTIEDITLPGLAELRGYWRGSLDASGGGNGDTMADFDFNGEDWEWGTYKTQRVLASGSFSNNDGLRLDKLFIQKDNATLHADGSILGPLTNLHFAVLNFPVGLIPALVQAIESSTTDSIHFLRQWLTPIKGILHMEGDLRGTLAKPECDVQIRLLDGTIGGIDLGRAEVLASVTPTSRFVFDANFEPTIQSGHVNIQGSVPVTYVDSNSIEEDLEGGDGKQGIIRIPVWAKDRGLTNDISETRIMRDKPDEGWEFQLAESLKGLSWNMLEPGEVRINADIKDGGMTLITALSPYSNWLQGYAEVLLQVKGTVDHPVVDGSASFHRATVASPFLRTPLTNFAGNVHVISNRLCISSMESRVGRKGRLSMKGTLPLHNIEPSANDKIELKCEVLDIRAKNILSGQVDSQLQVTGSILRPDVSGMIRLSHGEAYLPHDKGNGAVATRLSSNKSISVPAGFDQRTVSRDVSHFLGSLSTSPDGQQSETERTPEHGSFKPNIDARLNDLKLTFGPELRIVYPLILNFAVSGDLELNGMVHPKYIRPKGVLTFENGEVNLVATQVRLKNDHLNVAKFEPDLGLDPILDLVLVGSEWQFKIQSRASMWQDNLVVTSTRSVDQDVLSPSEAAKVFESQLAESLLEGDGQLAFKKLATATLETLMPRIEGKGEFGQARWRLVYAPQIPSLLSVDPTVDPLKSLANNISFATEVEVQLGKRLQASVVRQMKDSEMAMQWSLIYQLTSRLRVLFQSTPSNRLLFEYSATSQG
Protein: Metabotropic glutamate receptor 5 (mGluR5) (Q3UVX5)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current. Plays an important role in the regulation of synaptic plasticity and the modulation of the neural network activity (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Metabotropic glutamate receptor 1
- Muscarinic acetylcholine receptor M5
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Muscarinic acetylcholine receptor M1
- Muscarinic acetylcholine receptor M3
- Calcium/calmodulin-dependent protein kinase type II subunit gamma
- Homer protein homolog 1
- Guanine nucleotide-binding protein subunit alpha-11
- Major prion protein
Sequence:
MVLLLILSVLLLKEDVRGSAQSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRDSLISSEEEEGLVRCVDGSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLRSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNLRNPWFQEFWQHRFQCRLEGFAQENSKYNKTCNSSLTLRTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAMKPIDGRKLLDSLMKTNFTGVSGDMILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDDEVWSKKNNIIRSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYVFDEYTCKACQLGSWPTDDLTGCDLIPVQYLRWGDPEPIAAVVFACLGLLATLFVTVIFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCMFVPKVYIILAKPERNVRSAFTTSTVVRMHVGDGKSSSAASRSSSLVNLWKRRGSSGETLRYKDRRLAQHKSEIECFTPKGSMGNGGRATMSSSNGKSVTWAQNEKSTRGQHLWQRLSVHINKKENPNQTAVIKPFPKSTESRGQGAGAGGGSGPGAAGAGSAGCTATGGPEPPDAGPKALYDVAEAEERFPAAARPRSPSPISTLSHLAGSAGRTDDDAPSLHSETAARSSSSQGSLMEQISSVVTRFTANITELNSMMLSTAAAPGPPGTPICSSYLIPKEIQLPTTMTTFAEIQPLPAIEVTGGAQPATGPSPAQETPAGAEAAPGKPDLEELVALTPPSPFRDSVDSGSTTPNSPVSESALCIPSSPKYDTLIIRDYTQSSSSL
Protein: (R)-linalool synthase 1, chloroplastic (EC 4.2.3.26) (Terpene synthase TPS-Lin 1) (PsTPS-Lin-1) (F2XFA6)
Organism: Picea sitchensis (Sitka spruce) (Pinus sitchensis)
Function: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (R)-linalool.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MAFVSIAPLASRCCVHKSFVSSREVKPLCRTIPTLGRCRRGKTVTPSISMCWTATVLDDGVQRRIANHHSNLWHDSFIQSLSTPYGETSYLERADKLIGEVKEIINSISVEDGELITPLNDLIQRLSIVDNIERLGIDRHFKNEIKSVLDYVYSYWNEKGIGCGRESVITDLNSTALGLRTLRLHGYPVSSDVLEQFKDQNGQFACSAIQTEGEIKSVLNLFRASLIAFPGEKVMEDAEIFSTIYLKEALLTIPVCSLSREIAYVLEHGWHTNLPRLEARNYIDVFGQDPIYGTPNIKMTQKLLEIAKLEFNIFHSLQQKELKHLSRWWKDSVFSQLTFPRHRHVEYYTLASCIDIDPQHSSFRLGFAKISHLGTVLDDIYDTFGTMDELELFTAALKRWHPSATKWLPEYMKGVYMMLYETVNEMAREADKSQGRDTLNYARQAWEAYIDSYMKEAKWISSGFLPTFEEYLDNGKVSFGYRIGTLQPILTLGTPFPHHILQEIDFPSSLNRLACSILRLKGDIHTYQAERSRGEKSSCISCYMKDNPGSTEEDAVTYINAMVNKSLKELNWEFLRPDSNAPITSKKHAFDILRAFYHLYKHRDGFSVARNEIRNLVKTTVIEPVPL
Protein: Basic leucine-zipper 58 (F13B4.8 protein) (F21F23.3 protein) (Putative bZIP transcription factor) (Q9LMY8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Alpha/beta-Hydrolases superfamily protein
- Putative defensin-like protein 288
- F-box/FBD/LRR-repeat protein At1g13570
- Defensin-like protein 268
- ATG8-interacting protein 2
- BZIP transcription factor family protein
- Defensin-like protein 286
- Ceramide synthase 1 LOH3
- Probable transcription factor At4g00390
- Protein LOL1
Sequence:
MNTIPAELTGYFHYLPPDKYNNQTPIMESEYFNMPSSPTSCSSFYHLNGLINNNNYSSSSNGQDLMTSNNSTSDEDHQQSMVIDERKQRRMISNRESARRSRMRKQRHLDELWSQVIRLRTDNHCLMDKLNRVSESHELALKENAKLKEETSDLRQLISEIKSHNEDDNSFLRELEDSISNSRSDSNQSGRDFELC
Protein: 2OG-Fe dioxygenase family protein (Q1GXZ5)
Organism: Methylobacillus flagellatus (strain ATCC 51484 / DSM 6875 / VKM B-1610 / KT)
Interaction partners:
Sequence:
MVRPASRSERASLRIMNINPWRCEVSEKLLKQVNDKVSLCEKIAAEGFSFVPGQQIREWLLASNSEALQDWQAFDASWDGMPLDEYMADGGRYRRRRFATLSAATEGPIMLEPHQPHYQSREYNSLNGGIARIYEPIPPAVIQGQTMQSILQLSRDLFSHLRPQTRWHIEAHQFRIETNQHERGQPAPEGVHRDGVDYVLVMMVKRVNISSGTTTLHNLDKVVLDSFTLTNPLDCALVDDRRCMHGVTPVEQIDPAKAAYRDVLVVTFTAKL