wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional trans-3-hydroxy-L-proline dehydratase/2-epimerase (Bifunctional t3LHyp dehydratase/2-epimerase) (PaLhpL) (Trans-3-hydroxy-L-proline 2-epimerase) (T3LHyp 2-epimerase) (t3LHypE) (EC 5.1.1.-) (Trans-3-hydroxy-L-proline dehydratase) (T3LHyp dehydratase) (t3HypD) (EC 4.2.1.77) (Trans-L-3-hydroxyproline dehydratase) (Q9I489)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Bifunctional enzyme catalyzing both the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C) and 2-epimerization of t3LHyp to cis-3-hydroxy-D-proline (c3DHyp). No dehydratase activity with L-proline, trans-4-hydroxy-L-proline (t4LHyp), cis-4-hydroxy-L-proline (c4LHyp), D-proline, cis-4-hydroxy-D-proline (c4DHyp), trans-4-hydroxy-D-proline (t4DHyp) or L-serine as substrates. Displays neither t4LHyp epimerase nor proline racemase activity. Is likely involved in a degradation pathway that converts t3LHyp to L-proline, which would allow P.aeruginosa to grow on t3LHyp as a sole carbon source.
Interaction partners:
- Cis-3-hydroxy-L-proline dehydratase
- Amino acid ABC transporter periplasmic binding protein
- Amino acid ABC transporter ATP binding protein
- Amino acid ABC transporter membrane protein
- Delta
- Probable dihydrodipicolinate synthetase
- 2,5-dioxovalerate dehydrogenase
- Probable permease of ABC transporter
- 2,5-dioxovalerate dehydrogenase
Sequence:
MRSQRIVHIVSCHAEGEVGDVIVGGVAAPPGATLWEQSRWIARDQDLRNFVLNEPRGGVFRHANLLVPAKDPRAQMGWIIMEPADTPPMSGSNSLCVATVLLDSGILPMREPLTRLLLEAPGGLIEARAECRDGKAERVEIRNVPSFADRLDAWIEVEGLGSLQVDTAYGGDSFVIADARRLGFALRADEAAELVATGLKITHAANEQLGFRHPTNPDWDHLSFCQLAAPPERRDGVLGANNAVVIRPGKIDRSPCGTGCSARMAVLQAKGQLRVGERFVGRSIIGSEFHCHIESLTELGGRPAILPCLSGRAWITGIHQYLLDPDDPWPQGYRLSDTWPGGHC
Protein: PopZ (Q9A8N4)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
- Chromosome-partitioning protein ParB
- MipZ
- Histidine protein kinase DivJ
- Cell cycle transcriptional regulator CtrA
- Zinc finger/thioredoxin putative domain-containing protein
- Lysozyme
- Sensor protein DivL
- Cell division protein FtsZ
- Endoglucanase
- Chromosomal replication initiator protein DnaA
Sequence:
MSDQSQEPTMEEILASIRRIISEDDAPAEPAAEAAPPPPPEPEPEPVSFDDEVLELTDPIAPEPELPPLETVGDIDVYSPPEPESEPAYTPPPAAPVFDRDEVAEQLVGVSAASAAASAFGSLSSALLMPKDGRTLEDVVRELLRPLLKEWLDQNLPRIVETKVEEEVQRISRGRGA
Protein: Formate dehydrogenase (FDH) (EC 1.17.1.9) (NAD-dependent formate dehydrogenase) (Q59QN6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03210}.
Interaction partners:
- Formate dehydrogenase
- Formate dehydrogenase
- Malate synthase
- Malate dehydrogenase, cytoplasmic
- S-formylglutathione hydrolase
- Kynurenine formamidase
- Formamidase
- Phosphoenolpyruvate carboxykinase
- Malate dehydrogenase
- Malate dehydrogenase
Sequence:
MGKPKVLMVLYAGGNHAKEETRLLGTVENELGIRKLVEEHGYELVTTTDKEPAPTSAFDENLEDAEIIITTPFFPAYVNKERIAKAPKLKLCITAGVGSDHYDLDALNERGIAAIEVTGSNVVSVAEHAVMTMLILIRNYGEGHAQATKGTWDVAAVAKDEFDLEDKVIATVGAGRIGYRILERLVAFNPKKLLYYDYQPLPEEAINKLNAASKLFNGVDNIVERVEKLEDLVSQADVVTINCPLYEKSRGLFNKDLISKMKKGSYLVNTARGAIVDPEAVADAVNSGHIAYGGDVWPVQPAPKDMPWRTMHNPYGEAYGNAMTLHVSGTSLDAQARYANGVKQILTEYFNKTYNYRPQDVIVIDGDYATKAYGQREKK
Protein: ICP27 (Multifunctional expression regulator) (UL54) (Q9J0X9)
Organism: Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1)
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
Interaction partners:
Sequence:
MATDIDMLIDLGLDLSDSDLDEDPPEPAESRRDDLESDSNGECSSSDEDMEDPHGEDGPEPILDAARPAVRPSRPEDPGVPSTQTPRPTERQGPNDPQPAPHSVWSRLGARRPSCSPERHGGKVARLQPPPTKAQPARGGRRGRRRGRGRGGPGAADGLSDPRRRAPRTNRNPGGPRPGAGWTDGPGAPHGEAWRGSEQPDPPGGPRTRSVRQAPPPLMTLAIAPPPADPRAPAPERKAPAADTIDATTRLVLRSISERAAVDRISESFGRSAQVMHDPFGGQPFPAANSPWAPVLAGQGGPFDAETRRVSWETLVAHGPSLYRTFAGNPRAASTAKAMRDCVLRQENFIEALASADETLAWCKMCIHHNLPLRPQDPIIGTAAAVLDNLATRLRPFLQCYLKARGLCGLDELCSRRRLADIKDIASFVFVILARLANRVERGVAEIDYATLGVGVGEKMHFYLPGACMAGLIEILDTHRQECSSRVCELTASHIVAPPYVHGKYFYCNSLF
Protein: RRM domain-containing protein (Q2UNI5)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Nudix hydrolase domain-containing protein
Sequence:
MADNVPAQTPSTLPPPPQTSAAPGQQYDGAQGNGQANPSHMPPPPRPPVVIPQNTNPIPTAITSPMSGNMMSPTSAGGYVRRAAPEPNKRALYVGGLDQRVTEDILKQIFETTGHVVSVKIIPDKNKFNSKGYNYGFVEFDDPGAAERAMQTLNGRRIHQSEIRVNWAYQSNSTNKEDTSNHFHIFVGDLSNEVNDEILQQAFSAFGSVSEARVMWDMKTGRSRGYGFVAFRDRADADKALGSMDGEWLGSRAIRCNWANQKGQPSISQQQAMAAMGMTPTTAFGHHHFPTHGIQSYDMVVQQTPQWQTTCYVGNLTPYTTQNDLVPLFQNFGYVLETRLQADRGFAFIKMDSHENAAMAICQLNGYNVNGRPLKCSWGKDRPPTGQFDNFSGQQGNSPFNNSPAPYFPQYGGPGGPMTPQGPNPAGRGWDQSGMGGQNYGQVPGNAGYGRGQAAPASGWNQANNANFGNGFGGYQA
Protein: Cell division protein ZapC (FtsZ-associated protein C) (Z-ring-associated protein C) (P75862)
Organism: Escherichia coli (strain K12)
Function: Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00906, ECO:0000269|PubMed:21216995, ECO:0000269|PubMed:21216997}. Note=Colocalizes with FtsZ at division sites. Localization to the Z ring is dependent on FtsZ and independent of FtsA, ZipA, ZapA or ZapB.
Interaction partners:
- Cell division protein FtsZ
- Cell division protein ZapB
- Cell division protein ZapD
- Cell division protein ZapA
- Cell division protein ZipA
- Cell division protein FtsN
- Cell division protein FtsA
- Nucleoid occlusion factor SlmA
- Septum site-determining protein MinC
- Cell division protein ZapE
Sequence:
MRIKPDDNWRWYYDEEHDRMMLDLANGMLFRSRFARKMLTPDAFSPAGFCVDDAALYFSFEEKCRDFNLSKEQKAELVLNALVAIRYLKPQMPKSWHFVSHGEMWVPMPGDAACVWLSDTHEQVNLLVVESGENAALCLLAQPCVVIAGRAMQLGDAIKIMNDRLKPQVNVDSFSLEQAV
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (P79689)
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:
Sequence:
MLRDGNVAVMPPRRTAVALLALCGLLAVGDALKCNCTACESTGYVCETDGACMASTSYINGQEEQQVRICIPRVSLVPPGQPIYCLSAKGLLNTHCCYTDFCNSINLQIPNGIPDGKGGSWGPVELVAVIAGPVFLFCLLLIVGVLLFQHHQRNYNHRQRLDVEDPSCDHLYLAKDKTLQDLIFDLSTSGSGSGLPLFVQRTVARTIVLQEIIGKGRFGEVWRGRWRGGDVAVKIFSSREERSWFREAEIYQTIMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNHYSVTIEGMIKLSLSAASGLAHLHMEILGTQGKPGIAHRDLKSKNILVKKNGIFAIADLGLAVRHESITDTIDIAPNQRVGTKRYMAPEVLDETINMKHFDSFKCADIYALGLVYWEIARRCNAGGIHEDYKLPYYDLVPSDPSIEEMRKVVCDQRLRPKWPNWWQSYEALRVMGKIMRECWYANGAARLTALRIKKTLSQLSVQEDIKI
Protein: Splicing factor 3B subunit 1 isoform X1 (Splicing factor 3b, subunit 1) (F1QQZ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Splicing factor 3B subunit 5
- MCG1346-like protein
- Splicing factor 3B subunit 3
- Splicing factor 3B subunit 2
- Splicing factor 3B subunit 4
- Splicing factor 3B subunit 6
- ATP-dependent RNA helicase DDX42
- Splicing factor 3A subunit 2
- Small nuclear ribonucleoprotein polypeptide A'
- RNA-binding motif protein, X-linked 2
Sequence:
MAQIAKTHDDIEAQILEIQGKKAALVVEGGDQGVGLDSTGYYDQEIYGGSDSRFDGYLTSIAANEQEDDDDEDSSTSLLVQKKPGYHAPVAILNSIPQSDEQYDPFAEHRPQKISDREDEYKKRRQKMIISPERHDPFADGGKTPDPKVQVRTYMDVMKEQQLSKEEREIRLQMVEKAKAGELKAVNGSAASQAAAKRKRRWDQTADQTPSNSTPKKVSSWDQADGGSETPGHTPGHTPSNSRWDETPGRPKGSETPGATPSTRMWEPTPSHTPAGAATPGRDTPGHATPGHGGATSSVRKNRWDETPKTERETPGHGSGWAETPRTDRGDESVGETPTPGASKRKSRWDETPASQMGSSTPLLTPGKTPLGTPAMNMATPTPGHLMSMTPEQLQAWRWEREIDERNRPLTDEELDAMFPEGYKVLPPPAGYVPIRTPARKLAATPTPIGGMTGFHMQTEDRSMKQVNDQPSGNLPFLKPDDIQYFDKLLVEVDESTLSPEEQKERKIMKLLLKIKNGTPPMRKAALRQITDKAREFGAGPLFNQILPLLMSPTLEDQERHLLVKVIDRILYKLDDLVRPYVHKILVVIEPLLIDEDYYARVEGREIISNLAKAAGLATMISTMRPDIDNMDEYVRNTTARAFAVVASALGIPSLLPFLKAVCKSKKSWQARHTGIKIVQQIAILMGCAILPHLRSLVEIIEHGLVDEQQKVRTISALAIAALAEAATPYGIESFDSVLKPLWKGIRQHRGKGLAAFLKAIGYLIPLMDAEYANYYTREVMLILIREFQSPDEEMKKIVLKVVKQCCATDGVEANYIKTEILPPFFKHFWQHRMALDRRNYRQLVDTTVELANKVGAAEIISRIVDDLKDEAEQYRKMVMETIEKIMGNLGAADIDHKLEEQLIDGILYAFQEQTTEDSVMLNGFGTVVNALGKRVKPYLPQICGTVLWRLNNKSAKVRQQAADLISRTAVVMKTCQEEKLMGHLGVVLYEYLGEEYPEVLGSILGALKAIVNVIGMHKMTPPIKDLLPRLTPILKNRHEKVQENCIDLVGRIADRGAEYVSAREWMRICFELLELLKAHKKAIRRATVNTFGYIAKAIGPHDVLATLLNNLKVQERQNRVCTTVAIAIVAETCSPFTVLPALMNEYRVPELNVQNGVLKSLSFLFEYIGEMGKDYIYAVTPLLEDALMDRDLVHRQTASAVVQHMSLGVYGFGCEDSLNHLLNYVWPNVFETSPHVIQAVMGALEGLRVAIGPCRMLQYCLQGLFHPARKVRDVYWKIYNSIYIGSQDALIAHYPLIFNDEKNSYVRYELEYFL
Protein: Glutamate receptor 4 (GluR-4) (GluR4) (AMPA-selective glutamate receptor 4) (GluR-D) (Glutamate receptor ionotropic, AMPA 4) (GluA4) (Q9Z2W8)
Organism: Mus musculus (Mouse)
Function: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P19493}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19493}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P19493}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19493}. Cell projection, dendrite {ECO:0000250|UniProtKB:P19493}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P42262}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P42262}.
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 1
- Glutamate receptor 3
- Voltage-dependent calcium channel gamma-2 subunit
- Disks large homolog 4
- Protein shisa-9
- Voltage-dependent calcium channel gamma-4 subunit
- Voltage-dependent calcium channel gamma-3 subunit
- Disks large homolog 3
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MRIICRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDAPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLDKLKNKWWYDKGECGPKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEAIRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP
Protein: Aspartate and glycine-rich protein (P86736)
Organism: Haliotis asinina (Donkey's ear abalone) (Ass's ear abalone)
Subcellular location: Secreted {ECO:0000269|PubMed:21050442}.
Interaction partners:
Sequence:
GDGENGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGNGYFDDDDWDDFDWDDDDWNDNGNGDNGDDDDFWDDWDDDRFDDDRFDDDRFDDDRFDDDRWDDDDNDDWDDDDRWGDDDNDDWDDDDRWGDDDNDDWDDDDRWGDDDNDDWDDDDRWGDDNGNGNGNGNGNGNGDDDDDNGGYAFLRRALARASARARAAASAAGRSRGGSGGSGGSGGSGGSARARARARARAFASARASSGNGVNGGNGKKRSYTSY
Protein: Ring finger protein 4 (D6RA71)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSTRKRRGGAINSRQAQKRTREATSTPEISLEAEPIELVETAGDEIVDLTCESLEPVVVDLTHNDSVVIVDERRRPRRNARRLPQDHADSCVVSSDDEELSRDRDVYVTTHTPRNARDEGATGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPI
Protein: Acetylcholine receptor delta subunit (Acetylcholine receptor subunit delta precursor) (Cholinergic receptor, nicotinic, delta (muscle)) (Q75XT1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
- Acetylcholine receptor subunit alpha
- 43 kDa receptor-associated protein of the synapse
- Docking protein 7.
- Acetylcholinesterase collagenic tail peptide isoform X2 of asymmetric acetylcholinesterase)
- Muscle, skeletal receptor tyrosine-protein kinase isoform 3 precursor
- Cholinergic receptor, nicotinic, beta 1
- glutamine--fructose-6-phosphate transaminase
Sequence:
MMKTVLLTASLLCFIFQECCGRNEEERLINYLFKERGYNKELRPVQNKDETVDIYLALTLSNLISLKEVDETLLTNVWMEHGWKDHRLTWNESEYDIPVLRLPPSMVWLPEIVLENNNDAQFQVAYYCNVLIYSSGDMYWLPPAIFRSSCSINVNYFPFDWQNCSLKFSSLTYNAKEISLNLKMEQENTTYYKVEWIIIDPEGFTENGEWEIVHKPARRNIYKSIPKESNKHQDITFYLIIKRKPLFYIVNIIIPCVLISFLASLVYYLPADSGEKMTLSISVLLAQSVFLLLISQRLPETSMAVPLIVKYLMFIMVLVTVVVLNCVIVLNLHFRTPSTHVMTEWTKEFFLERLPRLLHMSLPVEDQPVPESALPRRSSSLGYIAQAEEYYSVKSRSELMFEKQSERHGLAARPTPKATYTSSNDSEVSEQLYNEMKPAVEGANYIVKHMHDKNDYNEEKDNWSGIARTVDRLCFYVVTPVMMIGTICIFLMANYNQPPALPFQGDPFSYTEENRRYL
Protein: GH07529p (Major facilitator superfamily transporter 14, isoform A) (Major facilitator superfamily transporter 14, isoform B) (Major facilitator superfamily transporter 14, isoform C) (Q8MRP7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Major facilitator superfamily transporter 16, isoform B
Sequence:
MTTALTMVKTGGKYANEKFFGVRHVQCILCFFCLAMSYAWRVNLSVALVAMTDNSTSLAQNNTNTGVAPSEPGFDFFNSERYYNFTQKEKGNLQASFFFGYIVTQVPGGYIAQRYGAKTMLMYGLGIAALITMLSPMSLQFGWVALAVMRFVMGLAQGAVHPATHALLAKWSPADERGMLGTLCYSGAQFGTVVMLATSGFIADSVLGWPSIFYLGGACGFIWMVFWYLFSASTPEEHRLISPGELKYITDSRSDGKMQSAEKLAPTPWKAIFSSLPFLSLLVVHCTHIFGYWLLLMQIPTYMKKIYHVDIKKGALLSSLPYMVMLLLSFFFVWLSKVLQKKEGMSLSFNRKIFNSIGHWIPMLSLIALGYVPADNAPLAVTLLTLTVGISGATYLGFQVNHIDLSPNYAGTLMGITNCAANVMSGIAPVIVGQIVVDETSVTEWRLVFLLAAAFYFLGNLLFVIFGRTEVQWWDSPRDNKEDAEQGTPLAPNGQVK
Protein: Imidazolonepropionase (EC 3.5.2.7) (Imidazolone-5-propionate hydrolase) (Q9HU91)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00372}.
Interaction partners:
- Probable histidine/phenylalanine ammonia-lyase
- Urocanate hydratase
- Histidine ammonia-lyase
- N-formylglutamate deformylase
- Formimidoylglutamate deiminase
- Formimidoylglutamase
- Histidine utilization repressor
- Probable permease of ABC transporter
- Quaternary amine transport ATP-binding protein
- Probable binding protein component of ABC transporter
Sequence:
MKRLWQHCHAATLKGGKYSIVEDAALVTDGPLIHWIGPRAELPPGDYAERIDLGGAWLTPGLIDCHTHAVFGGNRSGEFEQRLEGVSYAEIAAAGGGIASTVRATREASEEELLASARKRLEPLLRDGVTALEIKSGYGLDLASERKMLRVIRRLGERLPATVRSTCLAAHALPPEYAGRADDYIEHICSTMLPALAGEGLVDAVDAFCEHLAFSPAQVERVFIAARELGLPVKLHAEQLSSLHGSSLAARYRALSADHLEYMTEDDARAMGEAGTVAVLLPGAFYLLRETQLPPIDALRRHGVAMAIASDLNPGTSPALSLRLMLNMACTLFRLTPEETLAGVTLHAARALGLEASHGSLEVGKLADFVAWDIERPAELAYWLGGDLPKRVIRHAEEVYRG
Protein: Platelet-activating factor acetylhydrolase (PAF acetylhydrolase) (EC 3.1.1.47) (1-alkyl-2-acetylglycerophosphocholine esterase) (2-acetyl-1-alkylglycerophosphocholine esterase) (LDL-associated phospholipase A2) (LDL-PLA(2)) (PAF 2-acylhydrolase) (Q60963)
Organism: Mus musculus (Mouse)
Function: Lipoprotein-associated calcium-independent phospholipase A2 involved in phospholipid catabolism during inflammatory and oxidative stress response. At the lipid-aqueous interface, hydrolyzes the ester bond of fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Specifically targets phospholipids with a short-chain fatty acyl group at sn-2 position. Can hydrolyze phospholipids with long fatty acyl chains, only if they carry oxidized functional groups (By similarity). Hydrolyzes and inactivates platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), a potent pro-inflammatory signaling lipid that acts through PTAFR on various innate immune cells. Hydrolyzes oxidatively truncated phospholipids carrying an aldehyde group at omega position, preventing their accumulation in lipoprotein particles and uncontrolled pro-inflammatory effects (By similarity). As part of high-density lipoprotein (HDL) particles, can hydrolyze phospholipids having long-chain fatty acyl hydroperoxides at sn-2 position and protect against potential accumulation of these oxylipins in the vascular wall (By similarity). Catalyzes the release from membrane phospholipids of F2-isoprostanes, lipid biomarkers of cellular oxidative damage (By similarity).
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:18434304}. Note=Associates with HDL particles in plasma. {ECO:0000269|PubMed:18434304}.
Interaction partners:
- Lysophosphatidylcholine acyltransferase 2
- Lysophosphatidylcholine acyltransferase 1
- Cholinephosphotransferase 1
- Platelet-activating factor acetylhydrolase IB subunit alpha1
- Platelet-activating factor acetylhydrolase IB subunit alpha2
- Choline/ethanolaminephosphotransferase 1
- Platelet-activating factor acetylhydrolase IB subunit beta
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Lysophospholipid acyltransferase LPCAT4
- Lysophosphatidylcholine acyltransferase 2B
Sequence:
MVPLKLQALFCLLCCLPWVHPFHWQDTSSFDFRPSVMFHKLQSVMSAAGSGHSKIPKGNGSYPVGCTDLMFGYGNESVFVRLYYPAQDQGRLDTVWIPNKEYFLGLSIFLGTPSIVGNILHLLYGSLTTPASWNSPLRTGEKYPLIVFSHGLGAFRTIYSAIGIGLASNGFIVATVEHRDRSASATYFFEDQVAAKVENRSWLYLRKVKQEESESVRKEQVQQRAIECSRALSAILDIEHGDPKENVLGSAFDMKQLKDAIDETKIALMGHSFGGATVLQALSEDQRFRCGVALDPWMYPVNEELYSRTLQPLLFINSAKFQTPKDIAKMKKFYQPDKERKMITIKGSVHQNFDDFTFVTGKIIGNKLTLKGEIDSRVAIDLTNKASMAFLQKHLGLQKDFDQWDPLVEGDDENLIPGSPFDAVTQVPAQQHSPGSQTQN
Protein: Interferon 1AK3 (Interferon, alpha 7) (Interferon-alpha) (Q75UL5)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Interferon regulatory factor 3.
- Uncharacterized protein.
- Interferon alpha/beta receptor 1
- RELA proto-oncogene, NF-kB subunit.
- Nuclear factor NF-kappa-B p105 subunit
- Uncharacterized protein.
- Platelet-derived growth factor receptor alpha
- Receptor protein-tyrosine kinase.
- Janus kinase 2.
- Interleukin-10 receptor subunit beta
Sequence:
MALPCSFSVALVLLSCHSLCCLACHLPDTHGLRNWRVLTLLGQMRRLSAGSCDHYTNDFAFPKELFDGQRLQEAQALSVVHVMTQKVFHLFCPDTSSAPWNMTLLEELCSGLSEQLDDLEACPLQEAGLAETPLMHEDSTLRTYFQRISLYLQDRNHSPCAWEMVRAEIGRSFFSSTILQERIRRKE
Protein: Histamine H4 receptor (H4R) (HH4R) (Q91ZY2)
Organism: Mus musculus (Mouse)
Function: The H4 subclass of histamine receptors could mediate the histamine signals in peripheral tissues. Displays a significant level of constitutive activity (spontaneous activity in the absence of agonist) (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9H3N8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H3N8}.
Interaction partners:
- Histidine decarboxylase
Sequence:
MSESNSTGILPPAAQVPLAFLMSSFAFAIMVGNAVVILAFVVDRNLRHRSNYFFLNLAISDFLVGLISIPLYIPHVLFNWNFGSGICMFWLITDYLLCTASVYNIVLISYDRYQSVSNAVSYRAQHTGIMKIVAQMVAVWILAFLVNGPMILASDSWKNSTNTKDCEPGFVTEWYILTITMLLEFLLPVISVAYFNVQIYWSLWKRRALSRCPSHAGFSTTSSSASGHLHRAGVACRTSNPGLKESAASRHSESPRRKSSILVSLRTHMNSSITAFKVGSFWRSESAALRQREYAELLRGRKLARSLAILLSAFAICWAPYCLFTIVLSTYPRTERPKSVWYSIAFWLQWFNSFVNPFLYPLCHRRFQKAFWKILCVTKQPALSQNQSVSS
Protein: At5g63050 (Embryo defective 2759) (Q6NM17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVLVTHKLQGSHVLSPWSSPTWTRGLCLKRPVTTVHFVERKDKHLRLKQKCCFSLGSPCNGGLRAKPFRVTSFKGGIQNNESGGSEGGKKVTNNSVKLSYRSDDDENNVNGSPKAQNTSFSYTSETEDSMTGQPAIQKLFKKWLTLLRTQSPIQVIDETLGGEQVPQTTKQETETEIRKAESLQSTKNTVWSWFWSLDAAIKIPLLLFVPAFLAVYAICGAEVTKELSPMWVVGPLIIALYIKMFQGLCSLYAFCFNQTIKMIRNLPSYYLVAYQYIADGKLKDDVKALVFKPVVAIKNTDYKELTRTKLKQFQEWIIEKYLDFVESVWPYYCRTIRFLKRANLI
Protein: Large-conductance mechanosensitive channel (P9WJN5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. The force required to trigger channel opening depends on the nature of the membrane lipids; the presence of phosphatidylinositol enhances mechanosensitivity of the channel. May participate in the regulation of osmotic pressure changes within the cell.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00115, ECO:0000269|PubMed:23875651, ECO:0000305|PubMed:9856938}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00115, ECO:0000269|PubMed:9856938}.
Interaction partners:
- 6,7-dimethyl-8-ribityllumazine synthase
- S-adenosylmethionine synthase
- MoaB/Mog domain-containing protein
Sequence:
MLKGFKEFLARGNIVDLAVAVVIGTAFTALVTKFTDSIITPLINRIGVNAQSDVGILRIGIGGGQTIDLNVLLSAAINFFLIAFAVYFLVVLPYNTLRKKGEVEQPGDTQVVLLTEIRDLLAQTNGDSPGRHGGRGTPSPTDGPRASTESQ
Protein: CS domain-containing protein (Q38DY5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Heat shock protein, mitochondrial, putative
- Heat shock protein 83
- Lipophosphoglycan biosynthetic protein, putative
- Serine/threonine-protein phosphatase T
- Serine/threonine-protein phosphatase
- Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein
Sequence:
MHIPTKWAERNDKLYITLQVASAKDVNITFTDKTIKISGQGVTQRSSEPHELKDEITLLKEIVPEKSSFKVLGVSIQVCAAKKDEGYWNKLVDQPTSSTKNWLSVDWNLWKDEDEADEVPAGFGDYGDLSNMMNMGGMDMGGMDMGAMDDDSDDEEEDAPADLKDLEE
Protein: Homeobox protein Nkx-2.8 (Homeobox protein NK-2 homolog H) (Homeobox protein Nkx-2.9) (O70584)
Organism: Mus musculus (Mouse)
Function: Possible role in the specification of a distinct subset of neurons.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MATSGRLGFTVRSLLNLPEQDAKPRVRREQQTCVPQTAAWLESECSHYLSSDESGLETSPADSSQLASLRRESPGSDPEKRRKRRVLFSKAQTLELERRFRQQRYLSAPEREQLARLLRLTPTQVKIWFQNHRYKLKRGRAPGITEPSDMAASSDLHAAPGLLRRVVVPVLVHDRPPSNNGRGEGTSAVPQDKCSARLATACPVPGYTAFGPGSALGLFPAYQHLAPPALVSWNW
Protein: RNA-binding protein (Q382D5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAPKSAAKPAASGKNAPAPKSAPAAKSAPPAKASAPKNDPKKNAPKAAAPKPAATAPKAAAAKEAKARPAAGTHNGVYVKNWGQGSVTDATRIFSAAGKVVSAQIRRRRYAIIFFENAAAVRKAIDLFNEKEVLGAKVTVSPAKTSPKPDPHEGSSVVFLSPIFRTSTTNGQIRELFTGMRVLRIRTYRQNYAYVYLDSAAAAQKFVKEKNGTEFRGKKLRVALSTRSLQKEKDRAERANLLSDAHNFKKDAKKDIKRDDKKDPKKDSRRNEKKDAKRK
Protein: Uncharacterized protein C4F10.09c (O36021)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized NOC2 family protein C1142.04
- rRNA biogenesis protein rrp5
- Uncharacterized NOC2 family protein C1B3.09c
- Pescadillo homolog
- mRNA export factor elf1
- Nucleolar complex-associated protein 3
- Uncharacterized RNA-binding protein C4F6.14
- Ribosome biogenesis protein enp2 homolog
- Brix domain-containing protein C1B9.03c
- Ribosome biogenesis protein erb1
Sequence:
MATLYPKPKRGQKIIFNEEGEGTIDTKPQGVMFDPGVPWYNIPLPELHEDKKFVNVDHVSELETRGLLLLKEDSERFSETLGHGTADKRMLQTLISSGTTSDRISALTLLVQESPIHAVKALETLLSICSKKSRNEATQAITTLKDLFIGGLLPDRKLKYMKQQSCLGSKNVTDKHLMVWAFESFLKSFYFKYIQIIEALSFDALLFVKSQMVSTIYDLLKAKPEQEQNLLKLLINKLGDKENKIASKASYSILQLEASHPAMKLVITKEIERFIFAPSTSRTSCYYTLITLNQTVLTHKQVDVANLLIEIYFVFFTKLLFALEKEEVADAPTLEKKSLQSDSKNKKSQKRKKDEDLRKEAEENVNSRVISAVLTGVNRAYPFAEVNSEKFDKHMNTLFAITHTASFNTSVQVLMLIFQASASRDFISDRYYKSLYESLLDPRLTTSSKQSLYLNLLYKSLIIDNNIPRVRAFIKRMVQVSAWQQPPLVTGLFHVMHQLVIATTALRSMFTNAEIHDFDGDEEEVFKDVEEDDVSEDQKVDSDKDGKLSDKQSHSAYVVGNVSVSTKKEHLSYDGRKRDPQYSNADGSCLWEIHPFLNHFHPTVSLLAKSLVYGEKILGKPNLSLHTLNHFLDKFAYRNPKKSAAARGHSIMQPLAGGLSKGYVPGSTYSGVPMNSEQFTSKKQEEIPVDELFFYRFFNDKYIKGKQARKTKVDRDEEGEIDEDEVWKALVDSKPQLEMDEEESDFDSEEMDKAMTDMGSDSEQSADENDNESMASEEKPMFSDEENLSEIAHSEDEFDDTVDFFEDENDLLPFNETDDEEEIQTVDHSETHSHKKKKRKAIKDLPVFADAESYAHLLEN