wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-1,2-mannosyltransferase MNN2 (EC 2.4.1.-) (Q59WF4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Alpha-1,2-mannosyltransferase required for cell wall integrity. Responsible for addition of the first alpha-1,2-linked mannose to form the branches on the mannan backbone of oligosaccharides. Addition of alpha-1,2-mannose is required for stabilization of the alpha-1,6-mannose backbone and hence regulates mannan fibril length; and is important for both immune recognition and virulence. Promotes iron uptake and usage along the endocytosis pathway under iron-limiting conditions.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Putative alpha-1,3-mannosyltransferase MNN1
- Mannan polymerase complex subunit MNN9
- Glutamyl-tRNA
- Glycolipid 2-alpha-mannosyltransferase 1
Sequence:
MIAKQKIKILIGVIIVIATYHFIVSSNVRSKDLSDLVDLGSSDKSTTENERPKNNIVTNNRLDNPPNEDIPHAEPDSPPQEPPKSGNKPDFSIFFEGLEKFAIKQPGIKDKYTSEKAKEKFSTDDNFLFGKEYLENVLDIPQATFKELKDSHKRYVDEHIPKMLQRVKTFGSLAPSDKEWESYKGSSGYIIVGGGRFTWLSFLVIKQLRATGAKLPVEMFIATESDYEKEFCEKVLPKYNARCNVFDYKLADDLKKRFDIGGYQYKMLALLSSKFENVLYLDSDNFPTRNVDYLFESDLYKENNLLLWPDAWARTTNPKYYEIAGVPVKENKLRYSKYDEKQAGGKDKLKPLSEYTFKDSWYHDFEGTLPDPTSETGMFMVNKSSHLKTLLLCLYYNVFGPQYYYPLLTQGSAGEGDKETFIAAAHVMKEPWYQCARQFKWTGYVSKVDNKFTSKALAHYDPVQAQDTTRQDVDIIFMHLSYPKFYPNWLADNHDLVYADTDEHIRMYSSINKNVGYDFDLRVMQFFTEGLCPNYYDSKTGKPIENIPHIDYTNDYMGNHLMYVKDEEQNNIDRCNKVFIPHLKWLKETAEIPTVVS
Protein: Adenylyltransferase and sulfurtransferase uba4 (Ubiquitin-like protein activator 4) [Includes: Adenylyltransferase uba4 (EC 2.7.7.-); Sulfurtransferase uba4 (EC 2.8.1.-)] (Q09810)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-adenylate (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}.
Interaction partners:
- Ubiquitin-related modifier 1
- Probable 3-mercaptopyruvate sulfurtransferase
- Probable cysteine desulfurase, mitochondrial
- Cytoplasmic tRNA 2-thiolation protein 1
- Cytoplasmic tRNA 2-thiolation protein 2
- Elongator complex protein 4
- Elongator complex protein 1
- Elongator complex protein 5
- Elongator complex protein 3
- Mitochondrial tRNA-specific 2-thiouridylase 1
Sequence:
MNPQEKIICSSNGLELSLDEYSRYGRQMLLSEIGLPGQLSLKRSSVLVIGAGGLGCPAMQYLVAAGIGTLGIMDGDVVDKSNLHRQIIHSTSKQGMHKAISAKQFLEDLNPNVIINTYLEFASASNLFSIIEQYDVVLDCTDNQYTRYLISDTCVLLGRPLVSASALKLEGQLCIYNYCNGPCYRCMFPNPTPVVASCAKSGILGPVVGTMGTMQALETVKLILHINGIKKDQFDPYMLLFHAFKVPQWKHIRIRPRQQSCKACGPNKMLSREFMESSPKEYTTICDYVPTLSKQLAPIRRISALDLKNLIETSPHITFLDVREPVQFGICRLPLFKNIPLSEVDSLQNLSGKVCVICRSGNTSQTAVRKLQELNPQADIFDVVAGLKGWSTEVDPNFPLY
Protein: Candida glabrata strain CBS138 chromosome D complete sequence (Q6FVR1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome F complete sequence
- assimilatory sulfite reductase
- Cystathionine beta-synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- Sulfite reductase subunit beta
- cystathionine gamma-synthase
- Aspartate aminotransferase
- Aspartate aminotransferase
- Aspartate aminotransferase
- Candida glabrata strain CBS138 chromosome H complete sequence
Sequence:
MPSHFDTLQLHAGQENPDDNNHRPRAVPIYSTTSFVFNDSQHGAQLFGLEVPGYIYSRFQNPTNNVLEERIAALEGGAAALAVSSGQAAQTLAVAGLAHNGDNIVSTSFLYGGTYNQFKVAFKRLGIEARFVEGDKPEDFEKLFDERTKAVYLESIGNPKYNVPDFENIVAVAHKHGIPVVVDNTFGAGGFFCQPIKYGADIVTHSATKWIGGHGTTIGGIIVDSGKFPWKDYPEKFPQFSKPAEGYHGTVYNETYGNLAYIVHVRTELLRDLGPGMSPFAAFLLLQGVETLSLRGERHGQNALALAKWLEKNPHVAWVSYPGLPSHSHHENAKKYLSNGFGGVLSFGVKDLPNADKETDPFKLAGAQVVDNLKIASNLANVGDSKTLVIAPYFTTHQQLSDPEKLASGVTKDLIRVSVGTEFIDDIIADFEQSFAKVYGSN
Protein: Heat shock protein 90 alpha family class A member 1 (A0A1D5PUL6)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MPEAVQTQDQPMEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKDLKINLIPNKHDRTLTIVDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRLDNGEPLGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPIRLFVEKERDKEVSDDEAEEKEEEKEEKEEKTEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDEEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFMRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHVYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKAKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDTAAEEASPAVTEEMPPLEGDDDTSRMEEVD
Protein: Serine/threonine-protein kinase pelle (EC 2.7.11.1) (Q05652)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays an essential role in the Tl receptor signaling pathway that establishes embryonic dorsoventral polarity; the signal directs import of dl into ventral and ventrolateral nuclei, thereby establishing dorsoventral polarity. Tub recruits pll to the plasma membrane and protein-protein interaction activates pll.
Subcellular location: Cell membrane {ECO:0000269|PubMed:7635064}. Cytoplasm {ECO:0000269|PubMed:7635064}. Note=Associates with the plasma membrane during interphase syncytial blastoderm embryos, more specifically at the membrane invaginations around the nuclei.
Interaction partners:
- Protein Tube
- GH01161p
- LD20892p
- Protein pellino
- NF-kappa-B inhibitor cactus
- LD40663p
- Protein toll
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Embryonic polarity protein dorsal
Sequence:
MSGVQTAEAEAQAQNQANGNRTRSRSHLDNTMAIRLLPLPVRAQLCAHLDALDVWQQLATAVKLYPDQVEQISSQKQRGRSASNEFLNIWGGQYNHTVQTLFALFKKLKLHNAMRLIKDYVSEDLHKYIPRSVPTISELRAAPDSSAKVNNGPPFPSSSGVSNSNNNRTSTTATEEIPSLESLGNIHISTVQRAAESLLEIDYAELENATDGWSPDNRLGQGGFGDVYRGKWKQLDVAIKVMNYRSPNIDQKMVELQQSYNELKYLNSIRHDNILALYGYSIKGGKPCLVYQLMKGGSLEARLRAHKAQNPLPALTWQQRFSISLGTARGIYFLHTARGTPLIHGDIKPANILLDQCLQPKIGDFGLVREGPKSLDAVVEVNKVFGTKIYLPPEFRNFRQLSTGVDVYSFGIVLLEVFTGRQVTDRVPENETKKNLLDYVKQQWRQNRMELLEKHLAAPMGKELDMCMCAIEAGLHCTALDPQDRPSMNAVLKRFEPFVTD
Protein: DNA topoisomerase 1 (EC 5.6.2.1) (DNA topoisomerase I) (Q04750)
Organism: Mus musculus (Mouse)
Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the BMAL1 promoter.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P11387}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11387}. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli. {ECO:0000250|UniProtKB:P11387}.
Interaction partners:
- DNA topoisomerase 2-beta
- DNA topoisomerase 2-alpha
- Tyrosyl-DNA phosphodiesterase 1
- Poly [ADP-ribose] polymerase 1
- RNA-binding motif protein, X chromosome
- RNA binding motif protein, X-linked-like-1
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- Ribonuclease H2 subunit A
- Cell division cycle and apoptosis regulator protein 1
- DNA topoisomerase 3-alpha
Sequence:
MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKDKDKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKERRKEEKIRAAGDAKIKKEKENGFSSPPRIKDEPEDDGYFAPPKEDIKPLKRLRDEDDADYKPKKIKTEDIKKEKKRKSEEEEDGKLKKPKNKDKDKKVAEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPESVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNDEKNTITNLSKCDFTQMSQYFKAQSEARKQMSKEEKLKIKEENEKLLKEYGFCVMDNHRERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFPGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENVPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQSKIDAKKDQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMTDEDYEF
Protein: Glycerate 2-kinase (GCK) (EC 2.7.1.165) (2-phosphoglycerate forming glycerate kinase) (O58231)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-phosphoglycerate. It can also utilize GTP, CTP, UTP, ADP or pyrophosphate as phosphate donor.
Interaction partners:
- Enolase
- phosphopyruvate hydratase
- Glyoxylate reductase
- Pyruvate kinase
- 621aa long hypothetical aldehyde:ferredoxin oxidoreductase
- 581aa long hypothetical aldehyde:ferredoxin oxidoreductase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- 625aa long hypothetical formaldehyde:ferredoxin oxidoreductase
- Tungsten-containing aldehyde ferredoxin oxidoreductase
- 622aa long hypothetical aldehyde:ferredoxin oxidoreductase
Sequence:
MIAMDIREIGLRLVGEAIKAADPYRAVLNAVKVSDDKIIVQGKEFEIKGKVYVIALGKAACEMARAIEDILDVEDGVAVTKYGYGKELKRIKVIEAGHPIPDEKSILGAKEALSILNRARENDIVFILISGGGSALFELPEEGISLEDLKLTTDLLLKSGAKIHEINTVRKHISKVKGGKLAKMIKGTGIVLIISDVVGDNLEAIASGPTVKDPTTFEDAKRILELYDIWEKVPESVRLHIERGLRGEVEETLKEDLPNVHNFLIASNSISCEAIAREAQRLGFKAYIMTTTLEGEAKDAGLFIGSIVQEIAERGRPFEPPVVLVFGGETTVTIEGKGGKGGPNQEIALSATRKISDLEALIVAFDTDGTDGPTDAAGGIVDGTTYKKLREKGIDVEKVLKEHNSYEALKKVGGLLFTGPTGTNVNSIVIAIVTSKRGRT
Protein: GOLD domain-containing protein (Q57YT0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037847}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00037847}. Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003827}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003827}.
Interaction partners:
- GOLD domain-containing protein
- COP-coated vesicle membrane protein erv25, putative
- Cytosolic coat protein, putative
Sequence:
MIVPSLNGRLFSFLFIFLTVGQLSHPSPAEAFATKIEPHSRECFVESVPAGASLAFLFRVTDGGSFDIDAVMTATTVAPLETLDDTSRLHFSEKLRPLRDNAQTTVINEWRRATEGSQTYTAPTVSETKHGLPAEVTVCFDNSFARRSPKWVSFQFLRHEGLEEDPQASMTAEAKVEAELHKHGSVLFELATATERLRLVGESDRVKHESLARIIQAGLIGNIVLLAVMAVYQYRTLTRFLLRCKPQ
Protein: Protein Wnt-8c (CWnt-8) (P51030)
Organism: Gallus gallus (Chicken)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. Is likely to signal over only few cell diameters. May be involved in the regulation of axis formation and in the rhombomere specification.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Low-density lipoprotein receptor-related protein
- Porcupine O-acyltransferase.
- Wnt inhibitory factor 1
- Notum, palmitoleoyl-protein carboxylesterase.
- Protein wntless homolog
- Cerberus
- Frizzled-1
- Frizzled-7
- Frizzled-4
- Frizzled-2
Sequence:
MRGSTFLLLSIVGIYGAILNAAAWSVNNFLMTGPKAYLTYSSSVAAGAQSGMEECKFQFGWERWNCPESALQLSTHNRLRSATRETSFVHAISSAGVMYTLTRNCSLGDFESCGCDDSRNGRVGGRGWVWGGCSDNVEFGERISKLFVDALETGHDTRALINLHNNEVGRLAVKATMKRACKCHGVSGSCSIQTCWLQLADFREIGNYLKMKYDQAHKLEMDKRRMRAGNSADSRGATAETFHHVHSTELVFLEDSPDYCTRNASLGHHGTEGRECLQTGKNLSQWERRSCRRLSTECGLKVEERRTEVVSSCNCKFHWCCTVRCEQCRQLVAKHFCARRDAAVANHTKRRNKGHRR
Protein: ABC-type glutathione-S-conjugate transporter (EC 7.6.2.3) (Q8T9C5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Vacuole membrane {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
Interaction partners:
Sequence:
MADDTSSPMDRFCGSTFWNATETWYTNDPDFTPCFEQTALVWTPCAFYWAFVIFDFYYLKASLDRNIPWNKLNVSKALVNLGLLVITALDLIMALVKKGGDSELPLYDLDVWGPIIKFATFLLVFIFIPLNRKYGVQTTGCQFIFWFLLTVLSIPRCRTEVRLDAERQKILNSQQPSEQDFSWEEYQFVSFFIFFTFTSIMLILNCFADGMPRQTKYQRGENEIPELSASFLSRITYQWFDKMALKGYRNPLKEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKNYKNKARVEPKAQFSNGNVTFENPHGEKNGRKKGLASIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRINTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLIDENNVLDATKTFVSLSLFNILRFPLTMLPMLITNLVQTQVSVNRINKFLNSEELDPNSVLHDSSKPHPMSIENGEFSWGDEITLRNINIEVKKSSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQHLQEGNEEEEELNQIKRQISSTADVPELLGTVEKAIKLARTESLSDSISVTSADSLMGGGGSLRRRTKRQDSHDSVASAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDMYLGVYGAFGFGQVLSKYLSGLALAIGGLHCSMNVFNKLLNTGLKWPMELFDTTPLGRILSRYSKDVDTVDSVLPAITVQLLNTCFGVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPWELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSMAKDANLV
Protein: Dem-like protein (Putative Dem protein) (Vacuolar import/degradation, Vid27-related protein) (Q9SZB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uveal autoantigen with coiled-coil/ankyrin
- Nuclear protein
- Phospholipase A1-IIdelta
- Kunitz trypsin inhibitor 2
- soluble epoxide hydrolase
- AT2G24420 protein
- Peroxisomal membrane protein 13
- GTP-binding nuclear protein Ran-1
- GDSL esterase/lipase ESM1
Sequence:
MGASHSHEDLEICSSDEDEYEEYEEGREGEEEEETFQDSRDDTLGISSSGGRRLRPKSPSSSLDDVEAKLQALKLKYPLTQSAPSTQNSARLFRYINGNTPKAKWVTAEKLTAYCFVKTNKGDEDDEDDDENGDVENEWWILKVGSKIREKVSDEMQLKAYKDQRRVDFVAKAVWAMKFASSEDFSVFVSSYNNCLFENNHGVEFNEANKAKIYGKDFIGWANPEAADDSMWEDADDILLQSPGGGSATPARDTQDLTEAFEEATSEGIHSLALGALDNSFLVGDSGIQVFKNMRQGIQGKGVCVNFEPGYGRTHSSAPKKALLMRAETNMLLMSPMSQTPHSRGIHQLDIETGKIISEWKFEKDGVDISMSDITNDGKGAQLDPSASTFLGLDNNRLCRWDMRDRYGMVQDLATANTPVLNWAQGHQFSRGTNFQCFATTGDGSIVVGSLDGKIRLYSSNTMRQAKTAFPGLGAPVTHVDATFDGKWIVGTTDTYLIVICTLFTDKSGKTKTGFEGRMGNKIAAPRLLKLRPLDAHLAGSDNKFRNAQFSWVTEDGKQERHVVATVGKFSVIWNFQQVKNGSHECYHDQEGLKKCYCYKIVLRNESIVDSRFMNDNFAISGSPEAPLVIATPMKVSSFSLSSKR
Protein: Long chain acyl-CoA synthetase 6, peroxisomal (AtLACS6) (EC 6.2.1.3) (Q8LPS1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation (Probable). Preferentially uses palmitate, palmitoleate, oleate, linoleate and eicosenoate as substrates. Can use myristate and linolenate as substrates. May play a regulatory role both in fatty acid import into glyoxysomes and in fatty acid beta-oxidation. Functions redundantly with LACS7 in lipid mobilization for beta-oxidation during seed germination, which is essential for postgerminative growth and seedling establishment.
Subcellular location: Peroxisome {ECO:0000269|PubMed:12366803, ECO:0000269|PubMed:12481085}. Glyoxysome membrane {ECO:0000269|PubMed:12481085}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Peroxisomal acyl-coenzyme A oxidase 1
- Acyl-coenzyme A oxidase 2, peroxisomal
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Acyl-coenzyme A oxidase 3, peroxisomal
- ABC transporter D family member 1
- Acyl-coenzyme A oxidase 4, peroxisomal
- Probable acyl-CoA dehydrogenase IBR3
Sequence:
MDSSSSSSSAAARRRINAIHSHLVTSSRSSPLLRSNPTAGEFCLDNGYSVVLPEKLNTGSWNVYRSAKSPFKLVSRFPDHPDIATLHDNFEHAVHDFRDYKYLGTRVRVDGTVGDYKWMTYGEAGTARTALGSGLVHHGIPMGSSVGIYFINRPEWLIVDHACSSYSYVSVPLYDTLGPDAVKFIVNHATVQAIFCVAETLNSLLSCLSEMPSVRLVVVVGGLIESLPSLPSSSGVKVVSYSVLLNQGRSNPQRFFPPKPDDVATICYTSGTTGTPKGVVLTHANLIANVAGSSFSVKFFSSDVYISYLPLAHIYERANQILTVYFGVAVGFYQGDNMKLLDDLAALRPTVFSSVPRLYNRIYAGIINAVKTSGGLKERLFNAAYNAKKQALLNGKSASPIWDRLVFNKIKDRLGGRVRFMTSGASPLSPEVMEFLKVCFGGRVTEGYGMTETSCVISGMDEGDNLTGHVGSPNPACEVKLVDVPEMNYTSADQPHPRGEICVRGPIIFTGYYKDEIQTKEVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVGQCFIYGDSFNSSLVAVVSVDPDVLKSWAASEGIKGGDLRELCNNPRVKAAVLSDMDTVGREAQLRGFEFAKAVTLVLEPFTLENGLLTPTFKIKRPQAKEYFAEAITNMYKELGASDPSANRGL
Protein: DNA excision repair protein ERCC-8 (Ercc8 protein) (Excision repair cross-complementing rodent repair deficiency, complementation group 8) (Q5XJ81)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLGFLYARQTGLDDPVRLRRAESTRRVLSLELNHNRDVDRIHGNGINTLDIEVIDGRYMLSGGSDGVIVIYDLENNSKKPQYTCKAICTVGRSSRHVHKFSVETVQWYPHDTGMFVSSSFDKTMKVWDAETLKPADEFQFDGNVYCHHMSPIARKHSLVAVGTKDPKVQLCDLKSGSRIHILQGHRGEILSVRWSPRYEHILATASTDSRVRIWDVRRASGSLFTLDQHNGDKSKASSEAVNTAHNGRVNGLCFTADGLHLLTTGTDDRMRLWNSGTGENTLVNYGKVVNESRKGLKFTVSRGCSPEFVFVPCGSSVAVYGLHSGELITMLRGHYNNVDCCEFHPDYQELYSGGKDCNILAWVPVLRQPDVDDEETNTKRGGTQAAINPAFADAWSSDED
Protein: Nucleotidyltransferase family protein (Q84WU1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ypt/Rab-GAP domain of gyp1p superfamily protein
- Exportin-4
- DExH-box ATP-dependent RNA helicase DExH9
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1
- Zinc finger C3H1 domain protein
- At5g59460)
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2
- Zinc finger CCCH domain-containing protein 41
- Protein RRP6-like 3
- Nucleotidyltransferase family protein
Sequence:
MEDSDAKTEAPAFVYDTLPPLSFSDSNQSPPPTHEESHQYSVFRKEISDFPDDTTPVESATVDFFSLDVEGETTENGVEPVTPVVVASKKKSKKRKKDEEPRLESNWFSENSFSKIPMLQLHKEIVDFCDFLLPTQAEKAERDAAVESVSSVIKYIWPSCKVEVFGSYKTGLYLPTSDIDVVILESGLTNPQLGLRALSRALSQRGIAKNLLVIAKARVPIIKFVEKKSNIAFDLSFDMENGPKAAEFIQDAVSKLPPLRPLCLILKVFLQQRELNEVYSGGIGSYALLAMLIAFLKYLKDGRSAPEHNLGVLLVKFFDFYGRKLNTADVGISCKMGGSFFSKYNKGFLNRARPSLISIEDPQTPENDIGKSSFNYFQIRSAFAMALSTLTNTKAILSLGPNRSILGTIIRPDRVLSERKGGQNGDVTFNSLLPGAGEPLPLESNGKTNGGLFCNWELEEEEEEGSFPRGNDITPVVDTPGKKSKESSRKKKKKSKKNKEVDEDDEEEGTSTKKKKKKRRRNIVGLTWTY
Protein: Pelophylaxin-3 (Q2WCN6)
Organism: Pelophylax fukienensis (Fukien gold-striped pond frog) (Rana fukienensis)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000255, ECO:0000269|PubMed:16139927}.
Interaction partners:
Sequence:
MFTLKKSLLLVFFLGTISLSLCEDERNADEDDGEMTEEVRRGLMDSLKGLAATAGKTVLQGLLKTASCKLEKTC
Protein: Missing-in-metastasis, isoform B (A8DY50)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLSLERDSSALGSLFQQIINDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGASKEIGTALTRVCLRHKAVETRLKTFTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQTDGLQSLMDSHMQDVTLRRAELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSELGHLQEAMQSIALVTKEPSVLPQASEELIHDAKASINLYPESPGGGSGSQGGGCSNSLGSRKSSVCSISSMNSSGSSNSPGHHHYPRSLSQTSNATNQTANVSTWPPHSQDGVDTLPPTADRPHTISTAYEKGHQRPPLTVYTFQNPETIHESGSCLNNGTAAPNGQPLSGQATPATQKSPAASLSRPPLPVRCSSLERPLSAQSNHRQGSGNNLLQRQCPSPIPAHITKELSAAHHAQQQQQQQNQQPQTPPTYVNMSELATMAALKQTNQQQKPSTPPLQQQSSIDSTSSQHSNDSTGSHQLLQQQQQHHQSQQNHHSATATRSHSISSTASSLHSHPSIDSTVACGSLVGQHNHSTSTNTNTTSPSSGSSTPQNHYSPLLTNSPTSTAAGTPSGSSLGPGSGLGFVYQVSSPTPPSSEVLKITEQAAAGQDQGPANSVADETDERSRASVLQKASMFEKAAAAAAVSPPAPMQIASGSPASGGGTRRSEAEQQEMDKSFEDSIQALNNLIGELDSFQREIDEGKVKPPSNIISGSTTSSNNNNTTTSSISSSDNNNLPATSNIEPCAISNQTNSSGCGTDISDTTSDELAGDDMDVRRRDRDRDRDLLGASDSELSRCYVSETSSLTGGLTAGGYENPTFAHFAANANREDAVSLASDSVCLGQPRHAYVDTCSDSGSAVVVIYDHQIPNTPDIEFVKQNSEIVVLRTKDPQPHALQLHEMRELQQLPANLAGSPDSSPDSAGGQAPPTATVAPAKQRLSSFRATSEQQLQLLGRGSPQRGKTPSEQAVQSRPQDQHFPQTQQQDIDGSSPPVELARRQLPPKPTSLSIFNGPVPTAGDRPVVPRKSDFKADLDAKIRRQKQKVKQQLQQQQQQQQQEQQETQQQQQAPQEQQHSPQSPQTRNCNVTNQQAANITASASAFATATASTDPYPNPNHRMPNQNQTATSNHTQCKTPTMALSPSSPRGHLPLSSSSLSSLPLPATTSSPSNARPSMLPASDRPPAHPYVCSNAPANPHHANSISNANAHLKPCITPRPASLSGGAAGGGSTRIGRRSSINQSKPPPPVRRSSSVTPSPNASVGLQQQPQHATLSQQNHQLSSSSEHLPPPPPFMLDAMPQIPSSALKVSETVRALAAMRHQPASPVSLRRMQQQQQQQLQQQQQQQVQQQQPLLQSAHNSPLKEDLTVYYDSYLDLHAYAQALASGQQPGGQQMANQQRFTLQQQHQHLHQPQQPPVYQVDATFRTSSPAAGGGGGGGIYAQPKLVNSMSSFRTSSPSPNGHAHPLPPTQPKANPNLIAQLNARLSGKQQQHQQQQHIEGIYGNQQAPGGESIYMRSGLSMSQPQQQQHFDDYATSTNIEKTGSIRAKTKAEFLENLNAKLAKQGMSGRAFAVRNLINSKALPDPRICHESLMDQIKRGATLKRNQKINDRSAPKIH
Protein: Sodium/nucleoside cotransporter 1 (Concentrative nucleoside transporter 1) (CNT 1) (Na(+)/nucleoside cotransporter 1) (Sodium-coupled nucleoside transporter 1) (Solute carrier family 28 member 1) (E9PXX9)
Organism: Mus musculus (Mouse)
Function: Sodium-dependent and pyrimidine-selective transporter. Exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit) (selective for pyrimidine nucleosides and adenosine). Transports uridine, cytidine, thymidine, and nucleoside-derived drugs. It has the following selective inhibition: adenosine, thymidine, cytidine, uridine >> guanosine, inosine.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O00337}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}. Apical cell membrane {ECO:0000250|UniProtKB:O00337}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}.
Interaction partners:
- Equilibrative nucleoside transporter 2
- Equilibrative nucleoside transporter 1
- Equilibrative nucleoside transporter 3
- Equilibrative nucleoside transporter 4
Sequence:
MADDTPRQRESISLTPVAHGLENMGAEFLEIMEEGQLPHRHSSLPEGGGSRSKAVWKPFSRWRSLQPTVQARSLCREHWQLFEWISKGLLSTAYIGFLIVACLLDFPRALALFVITCVVLVFLAYNLLKRLLGSKLKKCVKFQGHSCLSLWLKRGLALAAGLGVILWLSLDTAQRPEQLVSFAGICVFLVLLFAGSKHHRAVSWRAVSWGLGLQFVLGLFVIRTEPGFVAFQWLGDQIRVFLSYTEAGSSFVFGEALVKDVFAFQVLPIIVFFSCVMSVLYYLGLMQWVILKIAWLMQVTMGTSATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEVHVVMTGGYATIAGSLLGAYISFGIDASSLIAASVMAAPCALALSKLVYPEVEESKFRSEEGVKLTYGDAQNLVEAASAGAAISVKVVANIAANLIAFLAVLAFINAALSWLGDMVDIQGLSFQLICSYVLRPVAFLMGVAWEDCPVVAELLGIKLFLNEFVAYQELSQYKQRRLAGAEEWLGDKKQWISVRAEILTTYALCGFANFSSIGIMLGGLTSMVPQRRSDFSQIVLRALITGAFVSLVNACVAGILYVPRGVEVDCMSLLNQTVSSSSFEVYLCCRQVFQNTSLEFGQEALHNCCRFYNHTVCT