wanglab/gogpt-training-data huggingface dataset:
Protein: Short neurotoxin MS11 (Three-finger toxin) (3FTx) (P86094)
Organism: Micrurus surinamensis (Surinam coral snake)
Function: Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Binds to and inhibits the endogenous nicotinic acetylcholine receptors (nAChR) in the human rhabdomyosarcoma TE 671 cell line with an IC(50) of 266 mM. Not toxic to mice by intraperitoneal injection or to zebrafish by injection at the back dorsolateral region.
Subcellular location: Secreted {ECO:0000269|PubMed:18384102}.
Interaction partners:
Sequence:
LKCYGIFRKIMTCPQGQNICEKFAYSPMHNGWMYSWGCTSNCHKGPLDKCCSTDLCNY
Protein: Absent in melanoma 2 (Q5T3W0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVAQQESIREGFQKRCLPVMVLKAKKPFTFETQEGKQEMFHATVATEKEFFFVKVFNTLLKDKFIPKRIIIIARYYRHSGFLEVNSASRVLDAESDQKVNVPLNIIRKAGETPKINTLQTQPLGTIVNGLFVVQKVTEKKKNILFDLSDNTGKMEVLGVRNEDTMKC
Protein: PHD finger-like domain-containing protein 5A (PHD finger-like domain protein 5A) (Splicing factor 3B-associated 14 kDa protein) (SF3b14b) (P83871)
Organism: Rattus norvegicus (Rat)
Function: Involved with the PAF1 complex (PAF1C) in transcriptional elongation by RNA polymerase II, and in regulation of development and maintenance of embryonic stem cell (ESC) pluripotency. Required for maintenance of ESCs self-renewal and cellular reprogramming of stem cells. Maintains pluripotency by recruiting and stabilizing PAF1C on pluripotency genes loci, and by regulating the expression of the pluripotency genes. Regulates the deposition of elongation-associated histone modifications, including dimethylated histone H3 'Lys-79' (H3K79me2) and trimethylated histone H3 'Lys-36' (H3K36me3), on PAF1C targets, self-renewal and pluripotency genes. Regulates RNA polymerase II promoter-proximal pause release of the PAF1C targets and self-renewal genes, and the levels of elongating ('Ser-2' phosphorylated) RNA polymerase II in their gene bodies. Regulates muscle specification in adult stem cells by stabilizing PAF1C in chromatin to promote myogenic differentiation (By similarity). Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (By similarity). Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha.
Subcellular location: Nucleus {ECO:0000269|PubMed:12810571}. Nucleus speckle {ECO:0000250|UniProtKB:P83870}.
Interaction partners:
- Splicing factor 3B subunit 3
- Splicing factor 3B subunit 5
- Splicing factor 3b, subunit 2
- Splicing factor 3B subunit 4
- Splicing factor 3B subunit 1
- Splicing factor 3B subunit 6
- Splicing factor 3A subunit 2
- RNA-binding motif protein, X-linked 2
- Small nuclear ribonucleoprotein F
- U5 small nuclear ribonucleoprotein 200 kDa helicase
Sequence:
MAKHHPDLIFCRKQAGVAIGRLCEKCDGKCVICDSYVRPCTLVRICDECNYGSYQGRCVICGGPGVSDAYYCKECTIQEKDRDGCPKIVNLGSSKTDLFYERKKYGFKKR
Protein: Formin homology 2 domain containing, isoform D (M9MSK7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIVKMEPDELITFRVQYLVDSDPLSACTAFPIPVRAPTYAFATTMPLANQLGTILRLLNAPQSIDDAAIQVYKDGDYGAYLDLESSLAEQAEEIEGVNVSRKNSLVVRTQLNVRVQAIIEKLLSAQGSDLRRALFSLKQVFQEDKDLVHAFVALGGLNCLVRVGNCADQNYQNYILRALGQVMLYVDGMNGVMKHEPTMQWLYSLIASNYRSVVKTALKLLLVFVEYAESNCYVLVSAIHAVDASQGTLPWSNIMRLLKDYDNADAELVIYATSLINKTLAGLNDQDSFYDESDLLEQQGMETVIQRYMSKPGTDLDLLDQLQLYEAVLKFEDGESDGQRLPQNSMRKTQRYRPGANTTERRKSRRHSTDNSPASLTKVLPTTVLRMTPTQATVDEDSSGSTNSTEFSGGLFNEKKPRDGAGVTPGLRRRRERAERHKSFLKEQQEAAANGIFAALEQREGLGQIVTAIPATIQTGDSPPQSLQHEVPPCNNISGITNISNNNVSNLSCNDTPNNSLLVMSPSKQLLTGSHSISIINNSFDKASNNNQSEFLTKKNLFRERNSTVINGIMKNIQQTDSAYKKYENEANRLNNYYSQSPKHQIHQPIQPTPEVLLSPKKTLNASGFDFTPAPLSSTPVKCDVPPEPEPLSPVKKPAAAPPPPPPPPPPPPPPPGWWHAPIYNSPQARTLTSTNPELLPHPVDPSDMESEDQQLLLQLKRDHTVKDLTQKLSNLPMSPTQDSANRALVGDMSGLISKAKEGLAKSKSKGEISRSSSVDQDVKKSEPKKSENELHWEELVRNMTRPLNLCDLDFTDLRDDDEKDVLAPRSLGAGIPPPPPPLGGAIAPPPMMPPSLAPPPMYGYGGSLTNSVNSLNGSINGELVNGNNTIKKNKKTVKLFWKEVREDMIPQVVGKTIWDELPDANVDTQKLEHLFESRAKDLMTKKQQELNKSKEIIVLDHKRSNAINIAITKLPPPRAIKTAILKMDATVVTREGIDKLLNMLPTDEERGKIQEAQLSNPELPLGSAEQFLLTLASISELEARLKLWAFRLDFDNSEKEIAEPLMDLKQGIEILRQNRTFRSILSTLLSVGIFLNGAPVKGFQIEYLAKVPEVKDTVHKHSLLHHLCHMVMESSSDTSDLYSEIGPITRASKADFTDLAHNLNQLEAECKACWDRLKLIAKHDCPPPLKQKLVDFLADCAERIIILQIVHRRVMNRYRKFLLWLGMPQHSVAESRPNEFCRTLSEFALEYRTTRERVQQQLEKKANHRERNKTRGKLIIDMAKFKTKDDVADDELKKLLDTSSADQADGTLTWRRRRAEQLRSPITRQSEEQFTDGDDEILESLVKTATKAPGTRTTPRERKRTRHADRKSCKLTAQVIRLRSTSKTPIERIRFNEKVLVYIFSNRTQRAMSITSSWILSTRNTHYTIKNSTEKLLYIVIQILISHTKFQIYTSTCSFPYLFTIFSRLRSFCPLSFASLRICCLYWVLIYFHFVLLPLTHQSNKPIKNQIK
Protein: Plasminogen activator inhibitor 2 type A (PAI-2) (PAI2A) (Serpin B2) (P29524)
Organism: Rattus norvegicus (Rat)
Function: Inhibits urokinase-type plasminogen activator.
Subcellular location: Cytoplasm {ECO:0000250}. Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Tissue-type plasminogen activator
- Plasminogen activator inhibitor 1
- Urokinase-type plasminogen activator
- Vitamin K-dependent protein C
- Plasminogen
- Urokinase plasminogen activator surface receptor
- Albumin
- Interleukin-5
- Thyroglobulin
- Serpin B12
Sequence:
MEELSMANTMFALNLLKQIEQSNSTQNIFISPWSISSTLAIVFLGAQANTEEQMAKVLNFDKIGSYDLTPGNPENFHGCDFAQHIQRDNYPVAILQAQARDKIHSAFSSLSSTINTPRLGDYLLESANKLFGEKSARFKEEYIQRCKKYYSTEPEAVDFLECANEARKKINSWVKTQTKGEIPNLLPEGSVDEDTKMVLVNTIYFKGRWKTPFQKRLNGLYPFRVNLNESKPVQMMYLREKLNIGYIKDLKTQILELPYIGNISMFLLLPDEIEDSSTGLEMLEREINFDNFNKWISKETLDEDDVLVYIPKFKLAQNYELKPILQRMGMEDAFNKGKADFSGMSESNDLFLSEVFHQATVDVNEEGTVAAGGTGAVMTGRTGHGGPQFVADHPFLFFIMNNITRTILFVGRFSSP
Protein: Small ribosomal subunit protein eS7y (40S ribosomal protein S7-2) (Q9M885)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein uS12y
- Small ribosomal subunit protein eS19z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein uS15z
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein uS4c
- Small ribosomal subunit protein eS1z
- U3 small nucleolar ribonucleoprotein protein IMP3
Sequence:
MYSGQNKIHKDKGVAPTEFEEQVTQALFDLENTNQELKSELKDLYINQAVQMDISGNRKAVVIYVPFRLRKAFRKIHLRLVRELEKKFSGKDVIFVATRRIMRPPKKGSAVQRPRNRTLTSVHEAMLEDVAYPAEIVGKRTRYRLDGTKIMKVFLDSKLKNDTEYKLETMVGVYRKLTGKDVVFEYPVIEA
Protein: Phosducin-like protein 1 (Q04004)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Not essential for growth. Inhibits early G-protein signaling events following pheromone stimulation. May help create heterodimerizable beta-tubulin by facilitating the efficient transfer of nascent beta-tubulin polypeptides to the folding apparatus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Phosducin-like protein 2
- Tryptophan synthase
- Prefoldin subunit 3
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MEDKLDRYYTNVLSNAEKDKHTTVDSDDKSSGEENLDELLNELDRELDEDHEFLSAYRSERLQQISDHLKQVKKNVEDDGYGRLQCIDNEADAIQICTKTTMVVIHFELETFGKCQYMNEKLENLAKRYLTTRFIKVNVQTCPFLVNKLNIKVLPFVVGYKNGLEKVRYVGFSKLGNDPNGFDIRRLEQSLAHSGVIEDTFEIRKHSSVNTERFASTNHDRSESDSDLDI
Protein: Glutaredoxin-like protein (Q38FH2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- BolA-like protein
- BolA-like protein
- Anamorsin homolog
Sequence:
MRHCHMSFAYCFCPFSAHRSASSQGYTRLMRRLSGSTCLLTGVTRAGRWLPTTAPCLSLCSFFLTASRRKQSTSGIGGDVRDIEETHPDFQPRLVSADLAEDEIAMVKKDIDDTIKSEDVVTFIKGLPEAPMCAYSKRMIDVLEALGLEYTSFDVLAHPVVRSYVKEVSEWPTIPQLFIKAEFVGGLDIVTKMLESGDLKKMLRDKGITCRDL
Protein: Insertion element IS1 2 protein InsA (IS1b) (P0CF08)
Organism: Escherichia coli (strain K12)
Function: Absolutely required for transposition of IS1.
Interaction partners:
- Insertion element IS1 2 protein InsB
- Insertion element IS1 1 protein InsA
- Insertion element IS1 1 protein InsB
- Insertion element IS1 4 protein InsB
Sequence:
MASVSISCPSCSATDGVVRNGKSTAGHQRYLCSHCRKTWQLQFTYTASQPGTHQKIIDMAMNGVGCRATARIMGVGLNTIFRHLKNSGRSR
Protein: Tubulin polymerization-promoting protein (TPPP) (EC 3.6.5.-) (25 kDa brain-specific protein) (TPPP/p25) (p25-alpha) (Q7TQD2)
Organism: Mus musculus (Mouse)
Function: Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath. Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath. Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes. Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (By similarity). In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network. Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (By similarity). Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (By similarity). Plays a role in cell proliferation by regulating the G1/S-phase transition (By similarity). Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (By similarity).
Subcellular location: Golgi outpost {ECO:0000250|UniProtKB:D3ZQL7}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:D3ZQL7}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18028908}. Nucleus {ECO:0000269|PubMed:18028908}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O94811}. Note=Specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation (By similarity). Mainly localizes to the cytoskeleton (PubMed:18028908). Also found in the nucleus; however, nuclear localization is unclear and requires additional evidences (PubMed:18028908). Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies. During mitosis, colocalizes with LIMK2 at the mitotic spindle (By similarity). {ECO:0000250|UniProtKB:D3ZQL7, ECO:0000250|UniProtKB:O94811, ECO:0000269|PubMed:18028908}.
Interaction partners:
- Alpha-synuclein
Sequence:
MADSKAKPAKAANKTPPKSPGDPARAAKRLSLESEGANEGATAAPELSALEEAFRRFAVHGDTRATGKEMHGKNWSKLCKDCHVIDGKNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGRAPVISGVTKAVSSPTVSRLTDTSKFTGSHKERFDQSGKGKGKAGRVDLVDESGYVPGYKHAGTYDQKVQGGK
Protein: CRISPR-associated exonuclease Cas4 (EC 3.1.12.1) (Q97TX9)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). This protein is a 5' to 3' partially processive exonuclease that cleaves off single mononucleotides. Has a marked preference for ssDNA, although in vitro it also acts on dsDNA and ssRNA. Has low endonuclease activity with circular ssDNA. Binds ssDNA and can unwind dsDNA; unwinding does not require ATP.
Interaction partners:
- CRISPR-associated endoribonuclease Cas2 2
- CRISPR-associated endoribonuclease Cas2 1
- CRISPR-associated exonuclease Csa1
- CRISPR-associated endonuclease Cas1 2
- CRISPR-associated endonuclease Cas1 1
Sequence:
MITEFLLKKKLEEHLSHVKEENTIYVTDLVRCPRRVRYESEYKELAISQVYAPSAILGDILHLGLESVLKGNFNAETEVETLREINVGGKVYKIKGRADAIIRNDNGKSIVIEIKTSRSDKGLPLIHHKMQLQIYLWLFSAEKGILVYITPDRIAEYEINEPLDEATIVRLAEDTIMLQNSPRFNWECKYCIFSVICPAKLT
Protein: RNA polymerase II subunit B1 CTD phosphatase RTR1 (EC 3.1.3.16) (RNA polymerase II-associated protein 2 homolog RTR1) (Regulator of transcription 1) (P40084)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase that dephosphorylates 'Ser-5' of the CTD and regulates RNA polymerase II during the transition from 'Ser-5' to 'Ser-2' phosphorylation.
Subcellular location: Cytoplasm. Nucleus. Note=Shuttles constitutively between the cytoplasm and the nucleus.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
Sequence:
MATIEDIKETALIPFQKHRQLSMHEAEVITLEIIGLLCDSECKDEKTLKYLGRFLTPDMYQDLVDERNLNKRCGYPLCGKSPERIRDPFSMNDTTKKFLLENNPYAYLSHYCSKFHFRCSQFYQVQLSDEALFARTGVHLFEDPEQDKHDIDFKVTLFEELLREKASEEDIKSLISGLKKLGLNPDSGTTEKDDTELEDDLSKWLAQIKIVENDNPSILGDFTRED
Protein: Histone H1.8 (Histone H1oo) (Oocyte-specific histone H1) (Oocyte-specific linker histone H1) (Q8VIK3)
Organism: Mus musculus (Mouse)
Function: May play a key role in the control of gene expression during oogenesis and early embryogenesis, presumably through the perturbation of chromatin structure. Essential for meiotic maturation of germinal vesicle-stage oocytes. The somatic type linker histone H1c is rapidly replaced by H1oo in a donor nucleus transplanted into an oocyte. The greater mobility of H1oo as compared to H1c may contribute to this rapid replacement and increased instability of the embryonic chromatin structure. The rapid replacement of H1c with H1oo may play an important role in nuclear remodeling.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus. Chromosome. Note=In the germinal vesicle oocyte, localizes to the condensed chromosomes. In the 1-cell embryo found in condensed maternal metaphase chromatin but not in the sperm head. Following second polar body extrusion, detected in the swollen sperm head as well as in the second polar body. Reduced expression in the nucleus in 2-cell embryo is seen as compared to 1-cell embryo.
Interaction partners:
- Histone H1t
- Testis-specific H1 histone
- H1 histone family, member X
- Histone H1.9
- Histone H1.1
- Histone H1.5
Sequence:
MAPGSVSSVSSSSFPSRDTSPSGSCGLPGADKPGPSCRRIQAGQRNPTMLHMVLEALKAREARQGTSVVAIKVYIQHKYPTVDTTRFKYLLKQALETGVRRGLLTRPAHSKAKGATGSFKLVPKPKTKKACAPKAGRGAAGAKETGSKKSGLLKKDQVGKATMEKGQKRRAYPCKAATLEMAPKKAKAKPKEVRKAPLKQDKAAGAPLTANGGQKVKRSGSRQEANAHGKTKGEKSKPLASKVQNSVASLAKRKMADMAHTVTVVQGAETVQETKVPTPSQDIGHKVQPIPRVRKAKTPENTQA
Protein: ABC transporter C family member 6 (ABC transporter ABCC.6) (AtABCC6) (EC 7.6.2.2) (ATP-energized glutathione S-conjugate pump 8) (Glutathione S-conjugate-transporting ATPase 8) (Multidrug resistance-associated protein 8) (Q8VZZ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pump for glutathione S-conjugates.
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- ABC transporter A family member 10
- ABC transporter A family member 6
- ABC transporter A family member 8
- ABC transporter A family member 5
- ABC transporter G family member 34
- ABC transporter A family member 4
- ABC transporter A family member 2
- ABC transporter A family member 7
Sequence:
MENPIDSLLLQPIYLSVLSFFLNLVLLLILFGSWLFKKRVACEDTDAIMNEEFKHISFSYNKLVLICCVSLSVFYSVLSLLSCLHWHTNGWPFLDLLLAALTWGSISVYLFGRYTNSCEQKVLFLLRVWWVFFFVVSCYHLVVDFVLYKKQEMVSVHFVISDLVGVCAGLFLCCSCLWKKGEGERIDLLKEPLLSSAESSDNEEVTAPFSKAGILSRMSFSWMSPLITLGNEKIIDIKDVPQLDRSDTTESLFWIFRSKLEWDDGERRITTFKLIKALFLSVWRDIVLSALLAFVYTVSCYVAPYLMDNFVQYLNGNRQYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSMIYEKGLTLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAFPATILVMLANYPFAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYNSSAINSVLWAAPSFISATAFGACLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRIASFLCLDDLQQDVVGRLPSGSSEMAVEISNGTFSWDDSSPIPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMELVGAHTEALATIDSCETGYASEKSTTDKENEVLHHKEKQENGSDNKPSGQLVQEEEREKGKVGFTVYKKYMALAYGGAVIPLILVVQVLFQLLSIGSNYWMTWVTPVSKDVEPPVSGFTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIGVIVQVAWQVLIVFIPVVAACAWYRQYYISAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELLSTFAFASSLVILVSAPEGVINPSLAGLAITYALNLNTLQATLIWTLCDLENKMISVERMLQYTNIPSEPPLVIETTRPEKSWPSRGEITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSLFSKLVAEYTTSSESKSKRS
Protein: CDP-diacylglycerol--inositol 3-phosphatidyltransferase (CDIPT) (EC 2.7.8.11) (Phosphatidylinositol synthase) (Q8SX37)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content (By similarity). The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme (By similarity). Required for the regeneration of the signaling molecule phosphatidylinositol 4,5-bisphosphate (PtdInsP2) from phosphatidic acid (PA) and maintenance of its steady supply during signaling, thus playing an essential role during phospholipase C-mediated transduction. This function is essential in photoreceptors for light-activated recycling of PtdInsP2 during phototransduction. As a key enzyme of the phosphoinositide pathway, indirectly involved in the polarized secretion of basal membrane (BM) proteins in follicle epithelial (FE) cells through promoting PtdInsP2 synthesis in the apical and lateral plasma membranes of FE cells. PtdInsP2 controls the localization of Crag and perhaps the localization and expression of strat, both of which are essential for restricting the secretion of BM proteins to the basal surface.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:24828534}; Multi-pass membrane protein {ECO:0000255}. Lateral cell membrane {ECO:0000269|PubMed:24828534}; Multi-pass membrane protein {ECO:0000255}. Note=In follicle cells, detected at the apical and lateral regions of the plasma membrane. {ECO:0000269|PubMed:24828534}.
Interaction partners:
- Phosphatidate cytidylyltransferase, photoreceptor-specific
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidylinositol 4-kinase alpha
- Phosphatidylinositol 4-kinase beta
- Probable cardiolipin synthase
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphatidylinositol-3-phosphatase SAC1
- phosphatidylinositol-3,5-bisphosphate 3-phosphatase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Inositol-1-monophosphatase
Sequence:
MTIAEHDNVFIFVPNLIGYARIVLALIAFWFMSTNYVISGWCYVTSALLDAVDGQAARAFNQSTRFGAMLDQLTDRCGTTGLLVTLAYFYPRYMFWFQLSIAIDVACHWLFMQTSVVVGRSSHKVNDNFIMRLYYQKDILTFMCCVNELFYVCLYLLHFTYGPLIFGASLFKILAFLTGPFAVLKALISVMHAYVAGIDLAAVDVRERQERRQKSEPVSGKKVE
Protein: Estradiol 17-beta-dehydrogenase 2 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase type 2) (17-beta-HSD 2) (Testosterone 17-beta-dehydrogenase) (EC 1.1.1.239) (Q62730)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the NAD-dependent oxidation of highly active 17beta-hydroxysteroids, such as estradiol (E2), testosterone (T), and dihydrotestosterone (DHT), to their less active forms and thus regulates the biological potency of these steroids. Oxidizes estradiol to estrone, testosterone to androstenedione, and dihydrotestosterone to 5alpha-androstan-3,17-dione. Also has 20-alpha-HSD activity (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P37059}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P37059}.
Interaction partners:
- Estradiol 17-beta-dehydrogenase 1
- Dehydrogenase/reductase SDR family member 11
- 17-beta-hydroxysteroid dehydrogenase type 3
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Aromatase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- Estrogen sulfotransferase Ste2
Sequence:
MNPFSSESAWLCLTATAVLGGMLLCKAWSSGQLRSQVVCLAGLWGGACLLSLSLLCSLFLLSVSCFFLLYVSSSDQDLLPVDQKAVLVTGADSGFGHALAKHLDKLGFTVFAGVLDKEGPGAEELRKNCSERLSVLQMDVTKPEQIKDVHSEVAEKIQDKGLWAVVNNAGVLHFPIDGELIPMTVYRKCMAVNFFGAVEVTKVFLPLLRKSKGRLVNVSSMGAMIPFQMVAAYASTKAAISMFSAVIRQELAKWGVKVVTIHPGGFQTNIVGSQDSWDKMEKEILDHFSKEIQENYGQEYVHTQKLALPVMREMSNPDITPVLRDIQHAICAKNPSSFYCSGRMTYLWICFAAYSPISLLDYILKNYFTPKLMPRALRTAS
Protein: Putative mannan endo-1,6-alpha-mannosidase C1198.06c (EC 3.2.1.101) (Endo-alpha-1->6-D-mannanase C1198.06c) (Q9P6I4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Autophagy-related protein 17
- Autophagy protein 13
Sequence:
MNIYSVGLFYFFLVFIGAQAMDLDITDYQSIDNTVNIMMKDLMNYWNASSQAFVASYWWVTGATMGALLYNYELFNNDTYVDLISSSLLYNAGSGFDYQPSFEYFNLGNDDQGMWAAAAMDAAEANFSPPNSTEHSWLELTQAAFNRMSGRWDSSTCGGGLRWQAFAWLNGYSYKASVSNALLFQLSSRLARFTNESVYSDWANKIWDWTTDVGFVNTTTYAVYDGADTSTNCTTLDPSQWSYNIGIFMVGAAYMYNYTGETVWRERLDGLISHATSYFFTDDIAWDPQCEYFDDCNSDQTAFKGIFMQSFGNTIRLAPYTYDTLYPLIQTSAAAAAKQCCGGYSGTSCGIYWFWNNGTWDDNYGVQEQFSALQAVQMLMIEYAPEIATLASSTDNRSNSTYASNVVINDTNTTTTIVVKEKDRGGAGFLTFLSAIFILGASIWALVEDEEGKIPSRGKKGIAISS
Protein: Serine racemase (EC 5.1.1.18) (D-serine dehydratase) (D-serine ammonia-lyase) (EC 4.3.1.18) (L-serine dehydratase) (L-serine ammonia-lyase) (EC 4.3.1.17) (Q7XSN8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine.
Interaction partners:
- tryptophan synthase
- Tryptophan synthase
- alanine--glyoxylate transaminase
- Threonine dehydratase
- phosphoserine phosphatase
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- glycine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
Sequence:
MGSRGGSGGDGAESHGYAADIHSIREAQARIAPYVHKTPVLSSTSIDAIVGKQLFFKCECFQKAGAFKIRGASNSIFALDDDEASKGVVTHSSGNHAAAVALAAKLRGIPAYIVIPRNAPACKVDNVKRYGGHIIWSDVSIESRESVAKRVQEETGAILVHPFNNKNTISGQGTVSLELLEEVPEIDTIIVPISGGGLISGVALAAKAINPSIRILAAEPKGADDSAQSKAAGKIITLPSTNTIADGLRAFLGDLTWPVVRDLVDDIIVVDDNAIVDAMKMCYEMLKVAVEPSGAIGLAAALSDEFKQSSAWHESSKIGIIVSGGNVDLGVLWESLYKR