wanglab/gogpt-training-data huggingface dataset:
Protein: Cofilin/actin-depolymerizing factor homolog (Protein D61) (Protein twinstar) (P45594)
Organism: Drosophila melanogaster (Fruit fly)
Function: Exhibits F-actin depolymerizing activity and regulates actin cytoskeleton dynamics. Required for cytokinesis in both mitotic and meiotic cells and for aster migration and separation. Promotes cell motility during ovary development and oogenesis. During larval development, required for the cell rearrangement needed for formation of terminal filaments which are stacks of somatic cells that are important for the initiation of ovarioles. Also required for border cell migration during oogenesis. During border cell migration, required for actin turnover and lamellipodial protrusion. Required for the establishment of planar cell polarity (PCP) where cells adopt a uniform orientation within the plane of an epithelium. During establishment of PCP, required for the redistribution of the PCP core proteins fz and stan/fmi to the proximodistal cell boundary. During pupal development, required for elongation of the retinal cell body and for rhabdomere morphogenesis. Required for mushroom body neuroblast proliferation and axon growth. Plays a role in the positive regulation of protein secretion. Plays a role in the regulation of nuclear localization of actin. Required for the maintenance of epithelial integrity by controlling cell junctions and is also necessary for cell survival and tissue growth through regulation of JNK and yki signaling.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus matrix {ECO:0000250}.
Interaction partners:
- LIM domain kinase 1
- Adenylyl cyclase-associated protein
- Profilin
- Actin-interacting protein 1
- Protein phosphatase Slingshot
- Cdc42 homolog
- Gelsolin
- Formin 3, isoform B
- Cortactin, isoform A
- Actin-related protein 2
Sequence:
MASGVTVSDVCKTTYEEIKKDKKHRYVIFYIRDEKQIDVETVADRNAEYDQFLEDIQKCGPGECRYGLFDFEYMHQCQGTSESSKKQKLFLMSWCPDTAKVKKKMLYSSSFDALKKSLVGVQKYIQATDLSEASREAVEEKLRATDRQ
Protein: Kunitz trypsin inhibitor 1 (AtKTI1) (Protein DROUGHT-REPRESSED 4) (AtDR4) (Q39091)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits Kunitz trypsin protease inhibitor activity.
Interaction partners:
- Acid phosphatase-like protein
- Heavy metal-associated isoprenylated plant protein 43
- Putative glutaredoxin-C12
- Heavy metal-associated isoprenylated plant protein 33
- Copper transport protein family
- At1g63840/T12P18_14
- Subtilisin-like protease SBT2.3
- Peptidyl-prolyl cis-trans isomerase
- Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 8
- Protein DETOXIFICATION 37
Sequence:
MKATISITTIFLVVALAAPSLARPDNHVEDSVGRLLRPGQTYHIVPANPETGGGIFSNSEEICPLDIFQSNNPLDLGLPIKFKSELWFVKEMNSITIEFEAPNWFLCPKESKGWRVVYSEEFKKSLIISTGGSSNPSGFQIHRVDGGAYKIVYCTNISTTTCMNVGIFTDISGARRLALTSDEALLVKFQKAATPKADLKTKLRMFPFY
Protein: Arginine--tRNA ligase, chloroplastic/mitochondrial (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) (Protein EMBRYO DEFECTIVE 1027) (O23247)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16251277}. Mitochondrion {ECO:0000250|UniProtKB:Q8RXK8}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase, cytoplasmic
- Proline--tRNA ligase, cytoplasmic
- glutamine--tRNA ligase
- Methionine--tRNA ligase, chloroplastic/mitochondrial
- Proline--tRNA ligase, chloroplastic/mitochondrial
- Isoleucine--tRNA ligase, chloroplastic/mitochondrial
Sequence:
MFIFPKDENRRETLTTKLRFSADHLTFTTVTEKLRATAWRFAFSSRAKSVVAMAANEEFTGNLKRQLAKLFDVSLKLTVPDEPSVEPLVAASALGKFGDYQCNNAMGLWSIIKGKGTQFKGPPAVGQALVKSLPTSEMVESCSVAGPGFINVVLSAKWMAKSIENMLIDGVDTWAPTLSVKRAVVDFSSPNIAKEMHVGHLRSTIIGDTLARMLEYSHVEVLRRNHVGDWGTQFGMLIEYLFEKFPDTDSVTETAIGDLQVFYKASKHKFDLDEAFKEKAQQAVVRLQGGDPVYRKAWAKICDISRTEFAKVYQRLRVELEEKGESFYNPHIAKVIEELNSKGLVEESEGARVIFLEGFDIPLMVVKSDGGFNYASTDLTALWYRLNEEKAEWIIYVTDVGQQQHFNMFFKAARKAGWLPDNDKTYPRVNHVGFGLVLGEDGKRFRTRATDVVRLVDLLDEAKTRSKLALIERGKDKEWTPEELDQTAEAVGYGAVKYADLKNNRLTNYTFSFDQMLNDKGNTAVYLLYAHARICSIIRKSGKDIDELKKTGKLALDHADERALGLHLLRFAETVEEACTNLLPSVLCEYLYNLSEHFTRFYSNCQVNGSPEETSRLLLCEATAIVMRKCFHLLGITPVYKI
Protein: CRISPR-associated exonuclease Cas4 (EC 3.1.12.1) (A3MTK6)
Organism: Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)
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). A ssDNA exonuclease that has 5' to 3' activity, yielding 5'-OH and 3'-phosphate groups. Has Mn(2+)-dependent endonuclease activity on circular ssDNA. Can unwind dsDNA; unwinding does not require ATP.
Interaction partners:
- CRISPR-associated endoribonuclease Cas2
- Translation elongation factor 1A GTP binding domain family
- Uncharacterized protein
- CRISPR-associated endonuclease Cas1
- K
Sequence:
MELLSPKPLCSVVNCEDLEKLDHVSALNELRREQEIFKLLPGIYAHRYDFRRVSPSIINDFEYCPRLLWVQHKLGLKLLSEKSVVSIIRGRILHERYERLLSQYENVVAEYKVEIGDLVGVVDLVIKRGGEYIPVEIKTGFSKEAHKTQLQIYISMLKARFGYLVYRNHVEVVHRNDAALDVLKKIREILSAREAPPAKCNSCIFKPICKNLL
Protein: Retrotransposon Gag-like protein 8C (Mammalian retrotransposon derived protein 8C) (A6ZKI3)
Organism: Homo sapiens (Human)
Interaction partners:
- Retrotransposon-derived protein PEG10
- Retrotransposon Gag-like protein 8A
Sequence:
MDGRVQLIKALLALPIRPATRRWRNPIPFPETFDGDTDRLPEFIVQTGSYMFVDENTFSSDALKVTFLITRLTGPALQWVIPYIKKESPLLNDYRGFLAEMKRVFGWEEDEDF
Protein: Very long-chain fatty acid transport protein (EC 6.2.1.-) (Very-long-chain acyl-CoA synthetase) (VLCS) (P38225)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acyl-CoA synthetase required for both the import of long chain fatty acids (LCFAs) (C14-C18) and the activation very long chain fatty acids (VLCFAs) (C20-C26) by esterification of the fatty acids into metabolically active CoA-thioesters for subsequent degradation or incorporation into phospholipids. The transport and fatty acyl-CoA synthetase activities are genetically separable and are thus independent activities. Esterifies VLCFAs in the peroxisome matrix. The VLCFAs are actively transported into peroxisomes by a PXA1-PXA2 heterodimeric transporter in the peroxisomal membrane.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}. Cell membrane {ECO:0000269|PubMed:17679730}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:22493507}; Multi-pass membrane protein {ECO:0000255}. Peroxisome {ECO:0000269|PubMed:11330068}.
Interaction partners:
- Long-chain-fatty-acid--CoA ligase 1
- Long-chain-fatty-acid--CoA ligase 4
- Sterol esterase TGL1
- Kinesin-like protein KAR3
- Sterol esterase 1
- Long-chain-fatty-acid--CoA ligase 3
- Long-chain-fatty-acid--CoA ligase 2
- NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Triacylglycerol lipase 3
Sequence:
MSPIQVVVFALSRIFLLLFRLIKLIITPIQKSLGYLFGNYFDELDRKYRYKEDWYIIPYFLKSVFCYIIDVRRHRFQNWYLFIKQVQQNGDHLAISYTRPMAEKGEFQLETFTYIETYNIVLRLSHILHFDYNVQAGDYVAIDCTNKPLFVFLWLSLWNIGAIPAFLNYNTKGTPLVHSLKISNITQVFIDPDASNPIRESEEEIKNALPDVKLNYLEEQDLMHELLNSQSPEFLQQDNVRTPLGLTDFKPSMLIYTSGTTGLPKSAIMSWRKSSVGCQVFGHVLHMTNESTVFTAMPLFHSTAALLGACAILSHGGCLALSHKFSASTFWKQVYLTGATHIQYVGEVCRYLLHTPISKYEKMHKVKVAYGNGLRPDIWQDFRKRFNIEVIGEFYAATEAPFATTTFQKGDFGIGACRNYGTIIQWFLSFQQTLVRMDPNDDSVIYRNSKGFCEVAPVGEPGEMLMRIFFPKKPETSFQGYLGNAKETKSKVVRDVFRRGDAWYRCGDLLKADEYGLWYFLDRMGDTFRWKSENVSTTEVEDQLTASNKEQYAQVLVVGIKVPKYEGRAGFAVIKLTDNSLDITAKTKLLNDSLSRLNLPSYAMPLFVKFVDEIKMTDNHKILKKVYREQKLPKGLDGNDTIFWLKNYKRYEVLTAADWEAIDAQTIKL
Protein: Mitosis-specific protein spo12 (Q10189)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in controlling mitotic cell cycle progression at the G2/M transition phase.
Interaction partners:
- Sulfite reductase subunit beta
- Fork head protein homolog 2
Sequence:
MSETQADSIAKSSVETTIQPLHQESATLRQQVLQKHELPKHALNVASPTDSLMSPCTAKLQAHKKKYYMKRKPPVMSLQNTLQSVQTEKE
Protein: TLE family member 3, transcriptional corepressor (H0YNT2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQRHYVMYYEMSYGLNIEMHKQTEIAKRLNTILAQIMPFLSQEHQQQVAQAVERAKQVTMTELNAIIGQQQLQAQHLSHATHGPPVQLPPHPSGLQPPGIPPVTGSSSGLLALGALGSQAHLTVKDEKNHHELDHRERESSANNSVSPSESLRASEKHRGSADYSMEAKKRKAEEKDSLSRYDSDGDKSDDLVVDVSNEDPATPRVSPAHSPPENGLDKARSLKKDAPTSPASVASSSSTPSSKTKDLGHNDKSSTPGLKSNTPTPRNDAPTPGTSTTPGLRSMPGKPPGMDPIGIMASALRTPISITSSYAAPFAMMSHHEMNGSLTSPGAYAGLHNIPPQMSAAAAAAAAAYGRSPMVSFGAVGFDPHPPMRATGLPSSLASIPGGKPAYSFHVSADGQMQPVPFPHDALAGPGIPRHARQINTLSHGEVVCAVTISNPTRHVYTGGKGCVKIWDISQPGSKSPISQLDCLNRDNYIRSCKLLPDGRTLIVGGEASTLTIWDLASPTPRIKAELTSSAPACYALAISPDAKVCFSCCSDGNIAVWDLHNQTLVRQFQGHTDGASCIDISHDGTKLWTGGLDNTVRSWDLREGRQLQQHDFTSQIFSLGYCPTGEWLAVGMESSNVEVLHHTKPDKYQLHLHESCVLSLKFAYCGKWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISADDKYIVTGSGDKKATVYEVIY
Protein: Molting defective, isoform E (A0A0C4DHB7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSANRRRRSASAASSIAAETATAATAATAEAISTAPSKEQLSPPIAGGSASADEDLLEMPRICRCCCKRDLKLLGLFEASQPTLANTTVASASAAASVASNKSSGTLAKTCATEAETETPQTLSANPVNPGTKATSSPSEAATTLSTSTRPASASFSSTSFSTSTSPMRRRTTNTTAPSASPAPRGRSSDNAVDYTLSGAHSSMDIVLEEMTIWMLNINRDDGLPQEICRQCMAQFLMVAKFRRKCVRMQQRLQDFAQEISDRQTARQAKRQQKVQKKTHDRWLQLEPTSHEEQQPIRKRRMVSESDGDSTAAAAAAEAATATATTPAKQVRTDFESLPPPKPSPQQHRVRKYRTLSIDCEMERPAASINASSMPWKTKAARKELSENWASSCSTAVMSPNRQRSSTSSSEHMSDLSVGPCCGFESDSNPSSTSNSARRTVILVKQQSPEKTSPMYDLMPRRGRRPRKAPIYMPAKRQRRSLVRKEPLYRKAQPVNEENKKSDQKDIYPKESRMEGLAPSCDEAIDSTSDAPMEVASNVVQKKCDEICLNGLIDSRNQLGAMEMEPVNEMIASNGVDKELTLSVQNNKETTSEEQIFEATSVIKESVQPEQSAEDIQVRTEIESIANDIRAEADLVQSEELTSSTETSESQPKAVEQLESMGKQESYALPQNMEAHESVQQTQTVDESDSADQREIIVSIPLEVLDENLQRRLCVDPETEAANRQSADPKEFALRPDDVNNNENDENFCQSATADSFNSAVALRTNKIEATPPGGTDSDDTDTDEVPIVPSGPTPMDFMAEFAKHCANGIEQLKVTTPVPSPTPSDLVPLNDLEAKQKLEVEMNDVETTLNGILNEMQDQHMYTPNCAHIDEFLTPADYATLTEQESSVSSPPNPFEQSSVAEPKDEKPSATEDPFDNSNFTNELIGFQNDIPCFENIETPEEGQNLHLELTQFLRDLQPSQSDPPAGEQVEKIEMETQPSTVQMDVQSNLPVQAADTQPQNESANHSPFESPISSPQVQSQIELQMEPQIETQMQPQIETRMQHDVLSVQSPQNHQPQVQSHDQSQMQHQIPPQIEPQIEVQNQEQNTLQLVPQAQHQVVPHVQLQSQLVPHVQTQGTTTTVTYEQIYQQHIVQQTVQQSSNKMQVISLPSAGSETTRQWQTQQSQQQQQVQWSSVGGLEAIKSAPVESVAPTTTTYYISASDLYPQQTETYTMLQPASNESYVIEQVNHQQQHCQQQIQMSQQQHQRQHQQQQAQQQQQPIMILIQQPEIQQPVASASNPQQAPLHIYNAATSNDVHQMQHTQRQQIRQQYQHQQYQRLQQPQQTRVVQSHPVLGMPGATSISTKVTPIPVTAARGRPLTLKCRFCHNGPRFSSSLEYSRHIIDLHPAVAPFNCPHCPMAFAGRTKRSQHILSHHVVQQYQCGQCSHVFPAQKALDVHIQRFHMTLKTDPSGAVKVEDVQLQITSERRPRGRPYKPRLQLQQHQLQPQQKLQVQQHQQQQKALQQLPQAQHHQQQQQPQLQQEVLQQVQQLQVQVQPQQHQQHQQVLQVQQPQQQPLMQPQSPHPSSTSGHSHANEQFEELQTLQAPPTVLTPPSTIVSVPSPQPMVYSQHITMPSPEQSEPDSTTTLRQYRKRGVIVGPQGPLHLATPVASPSPSSSPSSSTVDHIPPASPATPASPAPPPSPAVASTVQVSELRTSHHCLYCEERFTNEISLKKHHQLAHGALTTMPYVCTICKRGYRMRTALHRHMESHDVEGRPYECNICRVRFPRPSQLTLHKITVHLLSKPHTCDECGKQFGTESALKTHIKFHGELGYQCDGCDRTFEYLKELRKHRRTHSEMFYKCKFCPSSFMRFTNFRAHMKTHLPLGVFRNEDAASKSPSNNNSHASSDKLENPATPIEETPLTPMSSGGHLYHSPDEYPNSVESCAGNSVALESYATTP
Protein: Nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1) (EC 2.7.7.18) (Q9VC03)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- NAD-dependent histone deacetylase sirtuin-1
- Glutamine-dependent NAD
- NAD-dependent protein deacetylase Sirt6
- NAD-dependent protein deacylase Sirt4
- NAD-dependent protein deacetylase Sirt7
- NAD-dependent protein deacetylase Sirt2
- NAD
- NAD kinase 2, mitochondrial
- Nicotinate phosphoribosyltransferase
- Mitochondrial assembly of ribosomal large subunit protein 1
Sequence:
MIVKISWPKNNITSECFRRFGSFKRRSKSKKMSAFIEETKSLLPRIAFIACGCFSPPTPMHLRMFEIAKDHFEMQGTHRVVGGIISPTHDSYGKKGLASALDRCAMVKLATQSSNWIRLSDWEVHQNQWMRTQAVLQHHQNYINNHINSGGGGGDDGENTHLPGWLPRGLHDSRDPVHLKLLCGADLLESFAVPGLWAEADIEDIVANHGLVVITRAGSNPGKFIFDSDILTKYQSNITLITNWVPNEVSSTLIRRLLGRGQSVKYLLDDLVLEYIKRQRLFNFKSKYITDAVRPNHLLFNHAYTDNNKNANSYSIGDQLEQDMDESDTPSPQLQHTPTSRVFCCGEVPLRGSKVLRSGPGQAVQVITMQADEKEESQAKKQKISQVQL
Protein: Caspase recruitment domain family, member 10 (Q17RA1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPGRAEAGEAEEEAGAGSGSEAEEDALWERIEGVRHRLARALNPAKLTPYLRQCRVIDEQDEEEVLSTYRFPCRVNRTGRLMDILRCRGKRGYEAFLEALEFYYPEHFTLLTGQEPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLQREQQLQARGRVLEEERAGLEQRLRDQQQAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRARGPPPGAEEKEKEKEKEPDNVDLVSELRAENQRLTASLRELQEGLQQEASRPGAPGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDQYLQEMEDLRLKHRTLQKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTLTSLEGTKALLEVQLQRAQGGTCLKACASSHSLCSNLSSTWSLSEFPSPLGGPEATGEAAVMGGPEPHNSEEATDSEKEINRLSILPFPPSAGSILRRQREEDPAPPKRSFSSMSDITGSVTLKPWSPGLSSSSSSDSVWPLGKPEGLLARGCGLDFLNRSLAIRVSGRSPPGGPEPQDKGPDGLSFYGDRWSGAVVRRVLSGPGSARMEPREQRVEAAGLEGACLEAEAQQRTLLWNQGSTLPSLMDSKACQSFHEALEAWAKGPGAEPFYIRANLTLPERADPHALCVKAQEILRLVDSAYKRRQEWFCTRVDPLTLRDLDRGTVPNYQRAQQLLEVQEKCLPSSRHRGPRSNLKKRALDQLRLVRPKPVGAPAGDSPDQLLLEPCAEPERSLRPYSLVRPLLVSALRPVVLLPECLAPRLIRNLLDLPSSRLDFQVCPAESLSGEELCPSSAPGAPKAQPATPGLGSRIRAIQESVGKKHCLLELGARGVRELVQNEIYPIVIHVEVTEKNVREVRGLLGRPGWRDSELLRQCRGSEQVLWGLPCSWVQVPAHEWGHAEELAKVVRGRILQEQARLVWVECGSSRGCPSSSEA
Protein: Agouti related neuropeptide (F1MAG1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Melanocortin receptor 3
- Melanocortin receptor 4
- Appetite-regulating hormone
- Pro-neuropeptide Y
- Pro-opiomelanocortin
- Leptin
- Insulin-1
- Insulin-2
- Hypocretin neuropeptide precursor
- Cholecystokinin
Sequence:
MLTAMLLSCVLLLALPPTLGVHMGVAPLKGIRRSDQALFPEFSGLSLKKTAADRAEDVLLQKAEALAEVLDPQNRESRSPRRCVRLHESCLGQQVPCCDLCATCYCRFFNTFCYCRKLGTGTTNLCSRP
Protein: RNA-binding protein, putative (Q584Y8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pab1p-dependent poly
- Probable eukaryotic initiation factor 4A
- Nuclear cap-binding protein subunit 2
- PAB1-binding protein 1
- Regulator of nonsense transcripts 1, putative
- Eukaryotic release factor 3, putative
Sequence:
MWYSNLFVAKLPRHLCDGDLLQIFSNFNPLGAKIMLDPSTGNSKGFGFVLFDKEEEGRTAYERLNRKLVRVCNSSFNLLIYPSQHNGKAVTLPSRAVYIRNIPTTMGEREVQNFLSNLAPLEYCAMRGDHHGNPVWVVYAEFDTPQNAQRVLDKLHGNSNHFGGPPIMVKYADTDEAKRERRRRREEGRLAPGPALKGACLFPPPRPGVVSLNQTQVSQSATETSPSCSPAAHHVTKTKMVAPMVEVEPRAQPLYFSTSPVTAMPPLLPVDMSYDGAAATVPLQTADCPAANGVLVLGNGQQVFLTPNAVNLHPTKFNAPPTALLVPAVDTTLVPLPPQRTLVYGPW
Protein: Arsenical-resistance protein 3 (Arsenic compounds resistance protein 3) (As(III)/H(+) and Sb(III)/H(+)antiporter) (Q06598)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plasma membrane transporter that confers resistance to toxic metalloids by mediating extrusion of arsenite (As(III)) and antimonite (Sb(III)) out of cells. Displays low-affinity As(III)/H(+) and Sb(III)/H(+) exchange activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20655873, ECO:0000269|PubMed:21447319, ECO:0000269|PubMed:24291645, ECO:0000269|PubMed:26123064, ECO:0000305|PubMed:9374482}; Multi-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:9374482}.
Interaction partners:
- Metal resistance protein YCF1
- Arsenical-resistance protein 2
- Arsenical-resistance protein ARR1
- Glycerol uptake/efflux facilitator protein
Sequence:
MSEDQKSENSVPSKVNMVNRTDILTTIKSLSWLDLMLPFTIILSIIIAVIISVYVPSSRHTFDAEGHPNLMGVSIPLTVGMIVMMIPPICKVSWESIHKYFYRSYIRKQLALSLFLNWVIGPLLMTALAWMALFDYKEYRQGIIMIGVARCIAMVLIWNQIAGGDNDLCVVLVITNSLLQMVLYAPLQIFYCYVISHDHLNTSNRVLFEEVAKSVGVFLGIPLGIGIIIRLGSLTIAGKSNYEKYILRFISPWAMIGFHYTLFVIFISRGYQFIHEIGSAILCFVPLVLYFFIAWFLTFALMRYLSISRSDTQRECSCDQELLLKRVWGRKSCEASFSITMTQCFTMASNNFELSLAIAISLYGNNSKQAIAATFGPLLEVPILLILAIVARILKPYYIWNNRN
Protein: Apolipoprotein E (Apo-E) (P08226)
Organism: Mus musculus (Mouse)
Function: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles (By similarity). Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P02649}. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. {ECO:0000250|UniProtKB:P02649}.
Interaction partners:
- Prolow-density lipoprotein receptor-related protein 1
- Apolipoprotein A-I
- Apolipoprotein B-100
- Apolipoprotein C-I
- Apolipoprotein A-II
- Low-density lipoprotein receptor-related protein 2
- Very low-density lipoprotein receptor
- Amyloid-beta precursor protein
- Low-density lipoprotein receptor-related protein 8
- Apolipoprotein C-III
Sequence:
MKALWAVLLVTLLTGCLAEGEPEVTDQLEWQSNQPWEQALNRFWDYLRWVQTLSDQVQEELQSSQVTQELTALMEDTMTEVKAYKKELEEQLGPVAEETRARLGKEVQAAQARLGADMEDLRNRLGQYRNEVHTMLGQSTEEIRARLSTHLRKMRKRLMRDAEDLQKRLAVYKAGAREGAERGVSAIRERLGPLVEQGRQRTANLGAGAAQPLRDRAQAFGDRIRGRLEEVGNQARDRLEEVREHMEEVRSKMEEQTQQIRLQAEIFQARLKGWFEPIVEDMHRQWANLMEKIQASVATNPIITPVAQENQ
Protein: LD22513p (Reduction in Cnn dots 1, isoform B (EC 3.-.-.-)) (Q8T076)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKESGSVSKNQPQTSEARGSIITYSPSKFLTSVGTGRTTYSTHTHTTTATSAATTATKTNNLPMGGSSAAYYVVKAGSLGSAASMSGCIKVSSPPKGPPMAKSPALVVTSPCTPTESSSTISAPSESSFSEKMEHSYMRDTPVRSDVHNGLTPARNILVRHPPQCPSCHTYPPQHEELSEIQQAHVPPYDEVVAKEAMNECARIAKYVKNNNSDEQDWVARVNKFNWTPMQEMVFEKVCSILDQDQLARLANDKRQHEPIHRRISSDKSASRFRKLLASVAWESRITQWIHALLMEHLSPSYMASYLEILQTLKTKLPTLVDKMLFGRPLNNSQELLAPVMKKRWEPNIMPKSRQLTHNAIMVVLPNMPTTGTVSDRMQKWYQALSTITQVVQISLPNTNNRIGNQNLDHVAETIVSITRVKINELRTENPSRGIILVGFNAGAALALQVALSESVACVVCMGFAYNTIRGPRGTPDDRMLDIKAPILFVIGQNSARTSQEEMEGLRERMQSESSLVVVGSADDALRVPKSKRRIEGVTQSMVDYMVVEEIFEFVNRTLSNPPGPRMPTCLMHQQGYQRLPKQSPHILADGNANKAVQQMRKRKMDGGLDDSMGQPSKTKFVPHNDAQDYGDAQTTAGGSASLPKVITPGVLGKQLPPVNLAAGTKIKMIPSSQFVQIKSLPSQSKLINYTLNKPSVGTSSTANIGSVVKTLPCSSVSGQQIITLKTPSGQTQQFATAATSTGAAGSSTSTGTGQKKYTVFKNANGMTMLHLTKSVPTTGSSSGSANMDLSNIIDMPIVFADNEGNIPEHQQADKDIKPAPIRSANKSPLIISQKIIKEANKPSGMVTSGSITAVSKPGNIVLNKGLQQLLNSSPGGTLATQNKVVYLNRSTIKPMGNVAPGTHRVPIRIVSTPNTGGAVTTTASSSPIMVDPATGSKVAKTVNVQTIKPTGSVLAQGTIRQAGNVGTKSYLQMINTAPGASKTVAGDGKGSVRNIYFKSATGLKQLPVQMLGNRIPGGAVISSTASASSGSPGLRRVVNIGPVSKVTATSTTSSSIAATLTHNKM
Protein: FI18193p1 (Split discs, isoform B) (Split discs, isoform C) (Split discs, isoform F) (Q0KHX7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIKLKSLFRRGQGNSSSHSSNSSHKQQQNSSNNNRQKSQSSTSLNTAHEQQQQHSITAATTKFYAHQETASYERGVDVGDEGALLLTNQQQEQRRQQQQLLQQPQSNTLPQKKSKLKGQKQPKLLPVQQPHSNAPEPHDPQQPLMTSLAAVPQASATGSSSNSNINNNNALAALQDGGAAAAAAADFYQQLAAAATATATATSANGSNTSADSPVSSFPAAAAAVAVAAVAASSYQQQQQQQQLLNNEQQQQQLLEANNKMQELHKQMERFRSEQMQLETRITELLPYQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESLRNRLRDVVNSPLSDAEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPCLTPDWDKQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEMATRRSKLSFSRQDSRLSVKTLIESIENNKAQGKADESESHYSSTSSLNSGTPDLGTTPIIFPPSSDWHESIRLPVLQSTNLHVNVGNEVGAGQGTNTSSGSGGDLASTTKATLPLRDQQQLAITSTQSQVQNVSQPSTPATPSSAGSSSSGGLPFGNVSKSFISGERKDPLNMLAKNGGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLNINDMCQIERPDWMQVMSYVTAVYKYFET
Protein: Ribonucleoside-diphosphate reductase (EC 1.17.4.1) (Q5A0N3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Ribonucleotide-diphosphate reductase subunit
- Rnr22p
- Thymidylate kinase
- Nucleoside diphosphate kinase
- Guanylate kinase
- Uridylate kinase
- GTP:AMP phosphotransferase, mitochondrial
- Adenylate kinase
- Pyruvate kinase
- Ribonucleoside-diphosphate reductase
Sequence:
MYVYKRDGRKEPVRFDKITARVQRLCYGLNPNHVEPVAITQKVISGVYQGVTTIELDNLAAEIAATMTTIHPDYAVLAARIAVSNLHKQTTKQYSKVSKDLYEYINPKTGLHSPMISKETYDIIMEHEDELNSAIVYDRDFNYNYFGFKTLERSYLLRINGKVAERPQHLIMRVAVGIHGNDIPRVIETYNLMSQRFFTHGSPCLFNAGTPRPQMSSCFLLAMKDDSIEGIYDTLKSCALISKSAGGIGLHIHNIRSTGAYIAGTNGTSNGIIPMVRVFNNTARYVDQGGNKRPGAFALYLEPWHSDIFDFIDIRKNHGKEEIRARDLFPALWIPDLFMKRVEQNGDWTLFSPNEAPGLADVYGDEFEELYTKYEKENRGRQTIKAQKLWYAILGAQTETGTPFMLYKDSCNNKSNQKNLGIIKSSNLCCEIVEYSAPDEVAVCNLASIALPSFVENDEKSTWYNFDKLHQVTKVVTRNLNRVIDRNHYPVPEAERSNMRHRPIALGVQGLADAFMELRLPFDSQEARELNIQIFETIYHAAVEASIELAKEEGAYETYPGSPASQGLLQFDLWNRKPTELWDWDTLKQDLAKHGMRNSLLVAPMPTASTSQILGNNECFEPYTSNIYSRRVLAGEFQIVNPYLLKDLVDLGVWNDAMKSSIIANNGSIQALPNIPDEIKALYKTVWEISQKHIIDMAADRAAFIDQSQSLNIHIKDPTMGKLTSMHFYGWKKGLKTGMYYLRTQAASAAIQFTIDQKIAETAGHTVANLDKLNIKKYVNKGRVESENTSDAPYKSPSTEPTSLESSVADLKIKDEGEKPAEDKTIEELENDIYSAKVIACAIDNPESCTMCSG
Protein: Cyclopropane mycolic acid synthase MmaA2 (CMAS) (EC 2.1.1.79) (Cyclopropane-fatty-acyl-phospholipid synthase) (CFA synthase) (Mycolic acid methyltransferase) (MA-MT) (S-adenosylmethionine-dependent methyltransferase) (AdoMet-MT) (SAM-MT) (Q79FX6)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.
Interaction partners:
- Large ribosomal subunit protein bL25
Sequence:
MVNDLTPHFEDVQAHYDLSDDFFRLFLDPTQTYSCAHFEREDMTLEEAQIAKIDLALGKLGLQPGMTLLDIGCGWGATMRRAIAQYDVNVVGLTLSKNQAAHVQKSFDEMDTPRDRRVLLAGWEQFNEPVDRIVSIGAFEHFGHDRHADFFARAHKILPPDGVLLLHTITGLTRQQMVDHGLPLTLWLARFLKFIATEIFPGGQPPTIEMVEEQSAKTGFTLTRRQSLQPHYARTLDLWAEALQEHKSEAIAIQSEEVYERYMKYLTGCAKLFRVGYIDVNQFTLAK