wanglab/gogpt-training-data huggingface dataset:
Protein: Serine peptidase inhibitor, Kunitz type, 2 (F6QKA3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAQLCEPRRGRALLALLASLLLSGAQAASRDLDVHESCGVSKVVGKCRASIPRWWYNVTDGTCQPFVYGGCEGNGNNYPSKEECLDKCAGITENTIDGLARSSDGASALSVPRKQDSADLAGEIFNYEEYCVPKAVTGPCRAAFPRWYYDVEKNSCSSFIYGGCRGNKNSYLSQEACMQHCSGKQMYPFLTPGTKAVILVGLFIMVLILLLGSSMVFLIRMVRRKQERALRTVWSTADDKEQLVKNTCVL
Protein: Matrix protein (Protein M) (Q9IK90)
Organism: Nipah virus
Function: Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane. Transits through the host nucleus before gaining the functional ability to localize and bud from the plasma membrane. Mediates together with fusion protein the incorporation of the glycoprotein to the viral particles. Participates also in the inhibition of the host interferon type I antiviral response by interacting with and thereby inhibiting host TRIM6.
Subcellular location: Virion. Host cytoplasm. Host cell membrane {ECO:0000269|PubMed:17005661, ECO:0000269|PubMed:19000317, ECO:0000269|PubMed:21085610}. Host nucleus {ECO:0000269|PubMed:21085610}. Note=During bud formation, associates at the inner side of the plasma membrane of infected cells. Nuclear-cytoplasmic trafficking is essential for budding and requires matrix ubiquitination. {ECO:0000269|PubMed:21085610}.
Interaction partners:
Sequence:
MEPDIKSISSESMEGVSDFSPSSWEHGGYLDKVEPEIDENGSMIPKYKIYTPGANERKYNNYMYLICYGFVEDVERTPETGKRKKIRTIAAYPLGVGKSASHPQDLLEELCSLKVTVRRTAGSTEKIVFGSSGPLNHLVPWKKVLTSGSIFNAVKVCRNVDQIQLDKHQALRIFFLSITKLNDSGIYMIPRTMLEFRRNNAIAFNLLVYLKIDADLSKMGIQGSLDKDGFKVASFMLHLGNFVRRAGKYYSVDYCRRKIDRMKLQFSLGSIGGLSLHIKINGVISKRLFAQMGFQKNLCFSLMDINPWLNRLTWNNSCEISRVAAVLQPSIPREFMIYDDVFIDNTGRILKG
Protein: 4-hydroxy-2-oxovalerate aldolase (HOA) (EC 4.1.3.39) (4-hydroxy-2-keto-pentanoic acid aldolase) (4-hydroxy-2-oxopentanoate aldolase) (P51020)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of 3-phenylpropanoate.
Interaction partners:
- Acetaldehyde dehydrogenase
- 2-keto-4-pentenoate hydratase
- 2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase
- 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
- 3-
- L-xylulose/3-keto-L-gulonate kinase
- Ketol-acid reductoisomerase
- 3-isopropylmalate dehydratase small subunit
- 3-isopropylmalate dehydratase large subunit
- DNA-binding transcriptional activator MhpR
Sequence:
MNGKKLYISDVTLRDGMHAIRHQYSLENVRQIAKALDDARVDSIEVAHGDGLQGSSFNYGFGAHSDLEWIEAAADVVKHAKIATLLLPGIGTIHDLKNAWQAGARVVRVATHCTEADVSAQHIQYARELGMDTVGFLMMSHMTTPENLAKQAKLMEGYGATCIYVVDSGGAMNMSDIRDRFRALKAELKPETQTGMHAHHNLSLGVANSIAAVEEGCDRIDASLAGMGAGAGNAPLEVFIAAADKLGWQHGTDLYALMDAADDLVRPLQDRPVRVDRETLALGYAGVYSSFLRHCETAAARYGLSAVDILVELGKRRMVGGQEDMIVDVALDLRNNK
Protein: Arylsulfatase K (ASK) (EC 3.1.6.1) (Glucuronate-2-sulfatase) (EC 3.1.6.18) (Telethon sulfatase) (Q6UWY0)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of pseudosubstrates such as p-nitrocatechol sulfate and p-nitrophenyl sulfate. Catalyzes the hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-glucuronate residues of chondroitin sulfate, heparin and heparitin sulfate. Acts selectively on 2-sulfoglucuronate and lacks activity against 2-sulfoiduronate.
Subcellular location: Secreted {ECO:0000269|PubMed:23986440}. Lysosome {ECO:0000269|PubMed:23986440}.
Interaction partners:
- Arylsulfatase I
- Arylsulfatase J
- Arylsulfatase B
- Arylsulfatase G
- Formylglycine-generating enzyme
- Arylsulfatase H
Sequence:
MLLLWVSVVAALALAVLAPGAGEQRRRAAKAPNVVLVVSDSFDGRLTFHPGSQVVKLPFINFMKTRGTSFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFKGLDPNYTTWMDVMERHGYRTQKFGKLDYTSGHHSISNRVEAWTRDVAFLLRQEGRPMVNLIRNRTKVRVMERDWQNTDKAVNWLRKEAINYTEPFVIYLGLNLPHPYPSPSSGENFGSSTFHTSLYWLEKVSHDAIKIPKWSPLSEMHPVDYYSSYTKNCTGRFTKKEIKNIRAFYYAMCAETDAMLGEIILALHQLDLLQKTIVIYSSDHGELAMEHRQFYKMSMYEASAHVPLLMMGPGIKAGLQVSNVVSLVDIYPTMLDIAGIPLPQNLSGYSLLPLSSETFKNEHKVKNLHPPWILSEFHGCNVNASTYMLRTNHWKYIAYSDGASILPQLFDLSSDPDELTNVAVKFPEITYSLDQKLHSIINYPKVSASVHQYNKEQFIKWKQSIGQNYSNVIANLRWHQDWQKEPRKYENAIDQWLKTHMNPRAV
Protein: E3 ubiquitin-protein ligase TRIM9 (EC 2.3.2.27) (Anomalies in sensory axon patterning protein) (asap) (RING-type E3 ubiquitin transferase TRIM9) (Tripartite motif containing protein 9) (M9MRI4)
Organism: Drosophila melanogaster (Fruit fly)
Function: E3 ubiquitin-protein ligase activity (By similarity). During embryonic and larval development, regulates the pattern of axonal projections of class IV nociceptive sensory neurons (C4da) downstream of netrin receptor fra. Regulates fine-scale topography of C4da axon terminals upon neuronal activity. During eye development, consolidates the attachment of R8 photoreceptor growth cones to the target medulla layer, probably downstream of fra.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:22084112}. Perikaryon {ECO:0000269|PubMed:22084112}. Note=Colocalizes with fra and pico. {ECO:0000269|PubMed:22084112}.
Interaction partners:
- FI24025p1
- Roundabout 1, isoform A
Sequence:
MEDELRCPTCKQLYANPVLLPCFHALCLGCALDIQTPYSPGSALPGAVNGAGAASAAGHNGLHGNGGGAGGGAAAPVTNPNGPGTRHSSHSSAASTASSNTGSESVTSDQDQSDKVSIFSEADSGVVCCSNTSRPVSYAGTGLLPGVGNVVAPPGAAYCLTCPLCRKLVFFDDGGVRNLPTYRAMEAIVDRFCAREALRCQMCETDPKVASLICEQCEIRYCDACRELTHPARGPLAKHTLVKPRGAAQQRESVCGEHEETLSQYCLSCKAPACGLCIGELRHQAHDVQSINVTCKAQKTELSHNLQQLSEKARSTTEFIQRLKGMSDKVTESCMEFERLVHAQCEALIQAIHDRREYLLEAIRMDKDTKIRILKDQQSNCTGKLQQTTGLIQFCIEALKETDSAAFLQVGSMLINRVTNTDMTWHQEVTNAAPRVSPIVDLTLDDAALARAIDNLNFIQMRAVKDGDERCPAAPMTPTILPSDCSAENNSVTVAWQPPNHSFVEGYVLELDDGSGGEFREVYCGKETICTVDGLHFNSMYNARVKAFNSAGEGEYSELIGLQTAEVAWFTFDPVLSGGAGSGLIFSKNNATVSVEGWEHRVALGSVGFSRGVHYWEFTIDNYTADTDPAFGVARIDVARNKMLGKDEKSFAMYIDRQRSWFQHNSIHERRVEGGITTGSTIGVLLDLERHTLSFLVNEMPQGSVAFRDLYGVFYPAVSINRGVTLTMHTAMDAPKMDYF
Protein: MICAL-like protein 1 (E1BBG2)
Organism: Bos taurus (Bovine)
Function: Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth (By similarity).
Subcellular location: Recycling endosome membrane {ECO:0000250|UniProtKB:Q8N3F8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N3F8}. Late endosome membrane {ECO:0000250|UniProtKB:Q8N3F8}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q8N3F8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N3F8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8N3F8}. Note=Localization to late endosomes is actin-dependent. Association to tubular recycling endosomes is regulated by RAB35 and ARF6. Interaction with tubulins achors MICALL1 to the centriole. {ECO:0000250|UniProtKB:Q8N3F8}.
Interaction partners:
- Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein
- ArfGAP with coiled-coil, ankyrin repeat and PH domains 2.
- Ras-related protein Rab-35
Sequence:
MAGPRGALLAWCRRQCEGYRGVDIRDLSSSFRDGLAFCAILHRHRPDLLDFDSLSKDNVFENNRLAFEVAEKELGIPALLDPNDMVSMSVPDCLSIMTYVSQYYNHFAGSGPAGVSSPRKGLVLSSPPSEASTPADPGDRAQGEECSSGSLSKQGSHRTPSSTCAACQQHVHLVQRYLADGKLYHRHCFRCRRCSSTLLPGAYRNGPEEGTFVCAEHCARLGPSGRSGARPGTPPQPKQQQLTEEAKEVEGGSPSPKATAGAEADVPKASPEGRPQVPTKPRVPGRPQELASPPASRPTPAPRKASESTAPTPPTPRPRSSLQQENLVEQGGGSGLVNGKLQEPPIPKPRGTPKLSERTPAPRKDPPWITLVQAEPKKKPAPLPPSSSPGPPPGQEGRQVENGGVDKAAPRGPEPKPYNPFEEEEEEPPAAPSPAPGPAPTPPESTPKSLHPWYGITPTSSPKTKKRPAPRAPSTSPLTLHASRLSRSEPPSATPSPALSVESLSSESSSQAPSEELLEPPVVPKSSSEPAVHAPGTPGTSASLSANSSLSSSGELVQPSMDRTPQASPGLAPNSRGSPGPPPAKPCSGTAPTPLVLVGDKSPAPSPGTSSPQLQVKSSCKENPFNRKPSPTASPSVKKATKGSKPARPPAPGHGFPLIKRKVQSDQYIPEEDIHGEIDTIERQLDALEHRGVLLEEKLRGGVNEGREDDMLVDWFKLIHEKHLLVRRESELIYVFKQQNLEQRQADVEYELRCLLNKPEKDWTEEDRGREKVLMQELVTLIEQRNAIVNCLDEDRQREEEEDKMLEAMIKKKEFQKETEPEGKKKGKFKTMKVLKLLGNKRDTKSKCPGDRS
Protein: Coxsackievirus and adenovirus receptor homolog (CAR) (Q90Y50)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May function as a homophilic cell adhesion molecule and be essential for tight junction integrity. May also be involved in transepithelial migration of leukocytes through adhesive interactions with jaml. The interaction between both receptors may also mediate the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P78310}.
Interaction partners:
- Sodium channel subunit beta-2
- Nudix-type motif 8.
Sequence:
MDMRTSFLCVTYVILLTGSACGLQITSTGQTSIEKASGESVKLDCQFTLASDDSGPLDIEWSLQPSDNQKEEKVVIVYSGDRAFEHYYDPLKGRVHFNSPDPKNGDASMNIMGLKATDTGTYQCKIKKVPGIASRKYLLTVMVRPSKPKCSAEGQTYVGKNMVLKCSSVEGTQPMEYIWERTSGNKLLPPLAILDKVTGTMTLKNATGDASGTYRCQAKNRVGTEECVVEVTITQPPNTAGIIAGVIICILLLLILLALILFCCCRARHKKKYEKEIAYEIREDVPPPKSRVSTARSFTSVGSQRSSLGSMSPSNLHEYSKPQYDKIPSEEYDRPPSHAPIPPPSRMAGPNLSRMGAIPVMIPAQNKDGSIV
Protein: Fibronectin type III domain-containing protein 4 (Fibronectin type III repeat-containing protein 1) [Cleaved into: Soluble FNDC4 (sFNDC4)] (Q3TR08)
Organism: Mus musculus (Mouse)
Function: Acts as an anti-inflammatory factor in the intestine and colon. Binds to and acts on macrophages to down-regulate pro-inflammatory gene expression. Affects key macrophage functions, including phagocytosis, by down-regulating many key pathways for macrophage activation, partly via by STAT3 activation and signaling. May be required to dampen the immunological response in colitis.
Subcellular location: [Fibronectin type III domain-containing protein 4]: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Soluble FNDC4]: Secreted {ECO:0000269|PubMed:27066907, ECO:0000269|PubMed:34016966}.
Interaction partners:
Sequence:
MPLAPPANSVETMASLMPLSPYLSPTVLLLVSCDLGFVRADRPPSPVNVTVTHLRANSATVSWDVPEGNIVIGYSISQQRQNGPGQRVIREVNTTTRACALWGLAEDSDYTVQVRSIGLRGESPPGPRVHFRTLKGSDRLPSNSSSPGDITVEGLDGERPLQTGEVVIIVVVLLMWAAVIGLFCRQYDIIKDNDSNNNPKEKGKGPEQSPQGRPVGTTRQKKSPSINTIDV
Protein: Peroxisomal catalase 1 (EC 1.11.1.6) (Catalase-2) (Q27487)
Organism: Caenorhabditis elegans
Function: Peroxisomal catalase involved in the oxidative stress response serving to protect cells from toxicity. Plays a role in maintaining normal lifespan. Plays a role in regulating the response to pathogens such as E.faecalis.
Subcellular location: Peroxisome {ECO:0000269|PubMed:10691967}.
Interaction partners:
- Catalase-2
- FMN hydroxy acid dehydrogenase domain-containing protein
- Superoxide dismutase
- 3-hydroxyanthranilate 3,4-dioxygenase
- Kynureninase
- Catalase
- Superoxide dismutase 2, mitochondrial
- Peroxiredoxin prdx-2
- Superoxide dismutase
- Thioredoxin domain-containing protein
Sequence:
MPNDPSDNQLKTYKETYPKPQVITTSNGAPIYSKTAVLTAGRRGPMLMQDVVYMDEMAHFDRERIPERVVHAKGAGAHGYFEVTHDISKYCKADIFNKVGKQTPLLIRFSTVGGESGSADTARDPRGFAIKFYTEEGNWDLVGNNTPIFFIRDPIHFPNFIHTQKRNPQTHLKDPNMIFDFWLHRPEALHQVMFLFSDRGLPDGYRHMNGYGSHTFKMVNKDGKAIYVKFHFKPTQGVKNLTVEKAGQLASSDPDYSIRDLFNAIEKGDFPVWKMFIQVMTFEQAEKWEFNPFDVTKVWPHGDYPLIEVGKMVLNRNPRNYFAEVEQSAFCPAHIVPGIEFSPDKMLQGRIFSYTDTHFHRLGPNYIQLPVNCPYRSRAHNTQRDGAMAYDNQQHAPNFFPNSFNYGKTRPDVKDTTFPATGDVDRYESGDDNNYDQPRQFWEKVLDTGARERMCQNFAGPLGECHDFIIKGMIDHFSKVHPDFGARVKALIQKQARSHI
Protein: Galactose mutarotase (EC 5.1.3.3) (Aldose 1-epimerase) (Q96C23)
Organism: Homo sapiens (Human)
Function: Mutarotase that catalyzes the interconversion of beta-D-galactose and alpha-D-galactose during galactose metabolism. Beta-D-galactose is metabolized in the liver into glucose 1-phosphate, the primary metabolic fuel, by the action of four enzymes that constitute the Leloir pathway: GALM, GALK1 (galactokinase), GALT (galactose-1-phosphate uridylyltransferase) and GALE (UDP-galactose-4'-epimerase). Involved in the maintenance of the equilibrium between the beta- and alpha-anomers of galactose, therefore ensuring a sufficient supply of the alpha-anomer for GALK1. Also active on D-glucose although shows a preference for galactose over glucose.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Galactokinase
- UDP-glucose 4-epimerase
- N-acetylgalactosamine kinase
- Galactose-1-phosphate uridylyltransferase
- Beta-galactosidase
- Aldo-keto reductase family 1 member B1
- Hexokinase-3
- Alpha-galactosidase A
- Hexokinase-4
- Lactase/phlorizin hydrolase
Sequence:
MASVTRAVFGELPSGGGTVEKFQLQSDLLRVDIISWGCTITALEVKDRQGRASDVVLGFAELEGYLQKQPYFGAVIGRVANRIAKGTFKVDGKEYHLAINKEPNSLHGGVRGFDKVLWTPRVLSNGVQFSRISPDGEEGYPGELKVWVTYTLDGGELIVNYRAQASQATPVNLTNHSYFNLAGQASPNINDHEVTIEADTYLPVDETLIPTGEVAPVQGTAFDLRKPVELGKHLQDFHLNGFDHNFCLKGSKEKHFCARVHHAASGRVLEVYTTQPGVQFYTGNFLDGTLKGKNGAVYPKHSGFCLETQNWPDAVNQPRFPPVLLRPGEEYDHTTWFKFSVA
Protein: Polyphosphate kinase (EC 2.7.4.1) (ATP-polyphosphate phosphotransferase) (Polyphosphoric acid kinase) (P0A7B1)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Can form linear polymers of orthophosphate with chain lengths up to 1000 or more. Can use GTP instead of ATP, but the efficiency of GTP is 5% that of ATP. Also exhibits several other enzymatic activities, which include: ATP synthesis from polyP in the presence of excess ADP, general nucleoside-diphosphate kinase activity, linear guanosine 5'-tetraphosphate (ppppG) synthesis and autophosphorylation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1331061}; Peripheral membrane protein {ECO:0000269|PubMed:1331061}. Note=Associated with the outer membrane in overproducing cells. {ECO:0000269|PubMed:1331061}.
Interaction partners:
- Exopolyphosphatase
- Inorganic pyrophosphatase
- Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase
- Phosphoribosylglycinamide formyltransferase
- Phosphoribosylformylglycinamidine cyclo-ligase
Sequence:
MGQEKLYIEKELSWLSFNERVLQEAADKSNPLIERMRFLGIYSNNLDEFYKVRFAELKRRIIISEEQGSNSHSRHLLGKIQSRVLKADQEFDGLYNELLLEMARNQIFLINERQLSVNQQNWLRHYFKQYLRQHITPILINPDTDLVQFLKDDYTYLAVEIIRGDTIRYALLEIPSDKVPRFVNLPPEAPRRRKPMILLDNILRYCLDDIFKGFFDYDALNAYSMKMTRDAEYDLVHEMEASLMELMSSSLKQRLTAEPVRFVYQRDMPNALVEVLREKLTISRYDSIVPGGRYHNFKDFINFPNVGKANLVNKPLPRLRHIWFDKAQFRNGFDAIRERDVLLYYPYHTFEHVLELLRQASFDPSVLAIKINIYRVAKDSRIIDSMIHAAHNGKKVTVVVELQARFDEEANIHWAKRLTEAGVHVIFSAPGLKIHAKLFLISRKENGEVVRYAHIGTGNFNEKTARLYTDYSLLTADARITNEVRRVFNFIENPYRPVTFDYLMVSPQNSRRLLYEMVDREIANAQQGLPSGITLKLNNLVDKGLVDRLYAASSSGVPVNLLVRGMCSLIPNLEGISDNIRAISIVDRYLEHDRVYIFENGGDKKVYLSSADWMTRNIDYRIEVATPLLDPRLKQRVLDIIDILFSDTVKARYIDKELSNRYVPRGNRRKVRAQLAIYDYIKSLEQPE
Protein: Heparan sulfate glucosamine 3-O-sulfotransferase 1 (EC 2.8.2.23) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1) (Heparan sulfate 3-O-sulfotransferase 1) (O35310)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site.
Subcellular location: Golgi apparatus lumen {ECO:0000305}.
Interaction partners:
- Antithrombin-III
- Heparan sulfate 2-O-sulfotransferase 1
- D-glucuronyl C5-epimerase
- Heparan-sulfate 6-O-sulfotransferase 1
- Heparan-sulfate 6-O-sulfotransferase 3
- Heparan-sulfate 6-O-sulfotransferase 2
- Exostosin-1
Sequence:
MTLLLLGAVLLVAQPQLVHSHPAAPGPGLKQQELLRKVIILPEDTGEGTASNGSTQQLPQTIIIGVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSQGLGWYLTQMPFSSPHQLTVEKTPAYFTSPKVPERIHSMNPTIRLLLILRDPSERVLSDYTQVLYNHLQKHKPYPPIEDLLMRDGRLNLDYKALNRSLYHAHMLNWLRFFPLGHIHIVDGDRLIRDPFPEIQKVERFLKLSPQINASNFYFNKTKGFYCLRDSGKDRCLHESKGRAHPQVDPKLLDKLHEYFHEPNKKFFKLVGRTFDWH
Protein: Vacuolar-processing enzyme gamma-isozyme (EC 3.4.22.34) (Asparaginyl endopeptidase gamma-VPE) (Gamma-VPE) (Q39119)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms. Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds.
Subcellular location: Vacuole {ECO:0000269|PubMed:8589932}. Lytic vacuole {ECO:0000269|PubMed:10417725}. Note=Localized in lytic vacuoles of wounded leaves. {ECO:0000269|PubMed:10417725}.
Interaction partners:
- Cathepsin B-like protease 2
- Cathepsin B-like protease 1
- Cysteine proteinase RD21A
- Cathepsin B-like protease 3
- Cysteine protease RD19A
- Cysteine proteinase
- Cysteine proteinase
- Thiol protease aleurain
- At4g19400
- Probable cysteine protease RD19C
Sequence:
MATTMTRVSVGVVLFVLLVSLVAVSAARSGPDDVIKLPSQASRFFRPAENDDDSNSGTRWAVLVAGSSGYWNYRHQADICHAYQLLRKGGLKEENIVVFMYDDIANNYENPRPGTIINSPHGKDVYQGVPKDYTGDDVNVDNLFAVILGDKTAVKGGSGKVVDSGPNDHIFIFYSDHGGPGVLGMPTSPYLYANDLNDVLKKKHALGTYKSLVFYLEACESGSIFEGLLPEGLNIYATTASNAEESSWGTYCPGEEPSPPPEYETCLGDLYSVAWMEDSGMHNLQTETLHQQYELVKRRTAPVGYSYGSHVMQYGDVGISKDNLDLYMGTNPANDNFTFADANSLKPPSRVTNQRDADLVHFWEKYRKAPEGSARKTEAQKQVLEAMSHRLHIDNSVILVGKILFGISRGPEVLNKVRSAGQPLVDDWNCLKNQVRAFERHCGSLSQYGIKHMRSFANICNAGIQMEQMEEAASQACTTLPTGPWSSLNRGFSA
Protein: Elongation factor family protein (F4K409)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MELSLSTSSASPAVLRRQASPLLHKQQVLGVSFASALKPGGGALRFPSRRPLPRPITCSASPSTAEPASVEVKKKQLDRRDNVRNIAIVAHVDHGKTTLVDSMLRQAKVFRDNQVMQERIMDSNDLERERGITILSKNTSITYKNTKVNIIDTPGHSDFGGEVERVLNMVDGVLLVVDSVEGPMPQTRFVLKKALEFGHAVVVVVNKIDRPSARPEFVVNSTFELFIELNATDEQCDFQAIYASGIKGKAGLSPDDLAEDLGPLFEAIIRCVPGPNIEKDGALQMLATNIEYDEHKGRIAIGRLHAGVLRKGMDVRVCTSEDSCRFARVSELFVYEKFYRVPTDSVEAGDICAVCGIDNIQIGETIADKVHGKPLPTIKVEEPTVKMSFSVNTSPFSGREGKYVTSRNLRDRLNRELERNLAMKVEDGETADTFIVSGRGTLHITILIENMRREGYEFMVGPPKVINKRVNDKLLEPYEIATVEVPEAHMGPVVELLGKRRGQMFDMQGVGSEGTTFLRYKIPTRGLLGLRNAILTASRGTAILNTVFDSYGPWAGDISTRDLGSLVAFEDGTSTSYALASAQERGQMFVGSGVDVYKGQIVGIHQRPGDLGLNICKKKAATNIRSNKDVTVILDTPLTYSLDDCIEYIEEDELVEVTPSSIRMCKNQKMAKKGRQ
Protein: Glucagon-like peptide 1 receptor (GLP-1 receptor) (GLP-1-R) (GLP-1R) (P43220)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor for glucagon-like peptide 1 (GLP-1). Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels. Plays a role in regulating insulin secretion in response to GLP-1 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:19861722, ECO:0000269|PubMed:26308095, ECO:0000269|PubMed:27196125, ECO:0000269|PubMed:28514449, ECO:0000269|PubMed:7517895, ECO:0000269|PubMed:8216285, ECO:0000269|PubMed:8405712}; Multi-pass membrane protein {ECO:0000269|PubMed:28514449}.
Interaction partners:
- Pro-glucagon
- Gastric inhibitory polypeptide
- Guanine nucleotide-binding protein G
- VIP peptides
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- Dipeptidyl peptidase 4
- Pituitary adenylate cyclase-activating polypeptide
- Natriuretic peptides A
- Glucagon-like peptide 2 receptor
Sequence:
MAGAPGPLRLALLLLGMVGRAGPRPQGATVSLWETVQKWREYRRQCQRSLTEDPPPATDLFCNRTFDEYACWPDGEPGSFVNVSCPWYLPWASSVPQGHVYRFCTAEGLWLQKDNSSLPWRDLSECEESKRGERSSPEEQLLFLYIIYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLSCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVLSEQWIFRLYVSIGWGVPLLFVVPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVNFLIFVRVICIVVSKLKANLMCKTDIKCRLAKSTLTLIPLLGTHEVIFAFVMDEHARGTLRFIKLFTELSFTSFQGLMVAILYCFVNNEVQLEFRKSWERWRLEHLHIQRDSSMKPLKCPTSSLSSGATAGSSMYTATCQASCS
Protein: Uncharacterized aminotransferase C777.03c (EC 2.6.-.-) (O74542)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Iron sulfur cluster assembly protein 1, mitochondrial
- Ergothioneine biosynthesis protein 1
- Frataxin homolog, mitochondrial
- Hercynylcysteine sulfoxide lyase
- Protein isd11
- NifU-like protein C1709.19c
Sequence:
MTVSEGIARIQAFRKQVPLVEKNENITFFNLSFQPPMNSIVANTINEYVDWGLYNPNPKPLWQQKAEETRELVAKYLNASSSDSIAFTRDTTEGLNLFQRSMHFQPGDNVVLLDGEHPNHGFGWISLQEAGLEVRLIPSKDIYYADASTFEPYVDEKTKAIGISSVMFHSGQLNNVKDICNKFRPENIHVLVDMTQQVGLSSIDVQELNVSACAFACHKGLSCPTGLGVLYVAPDVLPQLKNVPPIVGAGAIENLDANLLVNLNPIYFSTARRFEHLNKSLITTLCLNNYLSFLMDIGFENIEQYLRELGKSLVDELSKLGVTIIGSKDPKKRSTHSYVAKILNPEWDAFLKNEGVYASQYRDGIRLSLGLYNNAADISRLANTIKKGVLNKIPFN
Protein: Dermatan-sulfate epimerase-like protein (EC 5.1.-.-) (Q0VBN2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Carbohydrate sulfotransferase 14
Sequence:
MAFMFTEHLLFLTLMMCSFSTCEESVSNYSEWAVFTDDIQWLKSQKIQDFKLNRRLHPNLYFDAGDIQTLKQKSRTSHLHIFRAIKSAVTIMLSNPSYYLPPPKHAEFAAKWNEIYGNNLPPLALYCLLCPEDKVAFEFVMEYMDRMVSYKDWLVENAPGDEVPVGHSLTGFATAFDFLYNLLGNQRKQKYLEKIWIVTEEMYEYSKIRSWGKQLLHNHQATNMIALLIGALVTGVDKGSKANIWKQVVVDVMEKTMFLLKHIVDGSLDEGVAYGSYTSKSVTQYVFLAQRHFNINNFDNNWLKMHFWFYYATLLPGYQRTVGIADSNYNWFYGPESQLVFLDKFILQNGAGNWLAQQIRKHRPKDGPMVPSTAQRWSTLHTEYIWYDPTLTPQPPVDFGTAKMHTFPNWGVVTYGGGLPNTQTNTFVSFKSGKLGGRAVYDIVHFQPYSWIDGWRSFNPGHEHPDQNSFTFAPNGQVFVSEALYGPKLSHLNNVLVFAPSPSSQCNQPWEGQLGECAQWLKWTGEEVGDAAGEVITAAQHGDRMFVSGEAVSAYSSAMRLKSVYRALLLLNSQTLLVVDHIERQETSPINSVSAFFHNLDIDFKYIPYKFMNRYNGAMMDVWDAHYKMFWFDHHGNSPVANIQEAEQAAEFKKRWTQFVNVTFHMESTITRIAYVFYGPYVNVSSCRFIDSSSSGLQISLHVNSTEHSVSVVTDYQNLKSRFSYLGFGGFASVANQGQITRFGLGTQEIVNPVRHDKVNFPFGFKFNIAVGFILCISLVILTFQWRFYLSFRKLMRCVLILVIALWFIELLDVWSTCTQPICAKWTRTEAKANEKVMISEGHHVDLPNVIITSLPGSGAEILKQLFFNSSDFLYIRIPTAYMDIPETEFEIDSFVDACEWKVSDIRSGHFHLLRGWLQSLVQDTKLHLQNIHLHETSRSKLAQYFTTNKDKKRKLKRRESLQDQRSRIKGPFDRDAEYIRALRRHLVYYPSARPVLSLSSGSWTLKLHFFQEVLGTSMRALYIVRDPRAWIYSVLYGSKPSLYSLKNVPEHLAKLFKIEEGKSKCNSNSGYAFEYESLKKELEISQSNAISLLSHLWVANTAAALRINTDLLPTNYHLVKFEDIVHFPQKTTERIFAFLGIPLSPASLNQMLFATSTNLFYLPYEGEISPSNTNIWKTNLPRDEIKLIENICWTLMDHLGYPKFMD