wanglab/gogpt-training-data huggingface dataset:
Protein: Polyamine oxidase 1 (AtPAO1) (EC 1.5.3.16) (EC 1.5.3.17) (N(1)-acetylpolyamine oxidase) (Spermine oxidase) (Q9FNA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Flavoenzyme involved in polyamine back-conversion. Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine and its acetyl derivatives. Substrate preference is thermospermine > norspermine > spermine > N(1)-acetylspermine. No activity detected when putrescine, spermidine or N(1)-acetylspermidine are used as substrates. Plays an important role in the regulation of polyamine intracellular concentration (Probable). Involved in the production of hydrogen peroxide in response to salt and cold stresses.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:26973665}.
Interaction partners:
- Spermine synthase
- Spermidine synthase 2
- Spermidine synthase 1
- Amine oxidase [copper-containing] zeta, peroxisomal
- Amine oxidase [copper-containing] alpha 3, peroxisomal
- Amine oxidase [copper-containing] gamma 2
- Amine oxidase
- Amine oxidase [copper-containing] alpha 2, peroxisomal
- Probable polyamine oxidase 5
- Aldehyde dehydrogenase family 3 member H1
Sequence:
MSTASVIIIGAGISGISAAKVLVENGVEDVLILEATDRIGGRIHKQNFGDVPVELGAGWIAGVGGKESNPVWELASRFNLRTCFSDYTNARFNIYDRSGKIFPTGIASDSYKKAVDSAILKLKSLEAQCSGQVAEEAPSSPKTPIELAIDFILHDFEMAEVEPISTYVDFGEREFLVADERGYECLLYKMAEEFLVTSHGNILDYRLKLNQVVREVQQSRNGVVVKTEDGSVYEANYVIVSASIGVLQSDLLSFQPLLPRWKTEAIQKCDVMVYTKIFLKFPQCFWPCGPGQEFFIYAHEQRGYFTFWQHMENAYPGSNILVVTLTNEQSKRVEAQSDQETMKEAMSVLRDMFGATIPYATDILVPRWWNNRFQRGSYSNYPMISDNQLLQNIKAPVGRIFFTGEHTSEKFSGYVHGGYLAGIDTSKSLLEEMKQSLLLQPLLAFTESLTLTHQKPNNSQIYTNVKFISGTS
Protein: PMS1 homolog 2, mismatch repair system component (A0A0G2JW47)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEPTEGASTECAKAIKPIDGKSVHQICSGQVVLSLSTAVKELIENSVDAGATSIDLRLKDYGVDLIEVSDNGCGVEEENFEGLALKHHTSKIREFADLTQVETFGFRGEALSSLCALSDVTISTCHVSASIGTRLVLDHNGKIIQKTPCPRPKGTTVSVQNLFYTLPVRHKEFQRNIKKEYAKMVQVLQAYCIISAGIRVSCTNQLGQGKRQPVVCTSGSSGMKENIGSVFGQKQLQSLVPFVQLPPSDSVCEEYCLSACGTPQSPFRISGFISQCTHGAGRSSTDRQFFFINQRPCDPAKVSRLVNEVYHMYNRHQYPFVVLNVSVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLMGMFDSDANKLSVNQQPLLNVEGNLVKLHTAEVGEQENSPSLRITAEEKRVASVSRLREAYSLHRTTETKSWGPETPELKQSFPSQKRGVSSSCPSDIISYRGLCGSQDKLVSPTDSPGDCMDREKGEKDSGLSSTSAGSEEGFSTPEVASSFSSDCNVSSPEDRPSQENTNCGEQFLEVDDHLSGTGHHLKPEDNGYKCRASLPPTRLSPSNAKRFRTEDRPSNVGVPQNTSAAEVDVAVKINKKIVLLDFSLSSLAKQMKQLQHLKQQSKSEHNYRKFRAKICPGENQAAEDELRREIRKSMFAEMEILGQFNLGFIVTKLKEDLFLVDQHAADEKYNFEMLQQHTVLQAQRLITWVHPSFRARSAPLQMKQLVPAAVCRHAYIPQTLNLTAVNEAVLIENLEIFRKNGFDFIIDEDAPVTERAKLISLPTSKNWTFGPQDIDELIFMLSDSPGVMCRPSRVRQMFASRACRKSVMIGTALSASEMKKLISHMGEMDHPWNCPHGRPTMRHIANLDVISQN
Protein: Oxidized low-density lipoprotein receptor 1 (Ox-LDL receptor 1) (Lectin-like oxidized LDL receptor 1) (LOX-1) (Lectin-like oxLDL receptor 1) (Lectin-type oxidized LDL receptor 1) [Cleaved into: Oxidized low-density lipoprotein receptor 1, soluble form] (Q9EQ09)
Organism: Mus musculus (Mouse)
Function: Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Membrane raft {ECO:0000250}. Secreted {ECO:0000250}. Note=A secreted form also exists. Localization to membrane rafts requires palmitoylation (By similarity). {ECO:0000250}.
Interaction partners:
- Heat shock 70 kDa protein 1B
- Apolipoprotein B-100
- Scavenger receptor class B member 1
- Platelet glycoprotein 4
- C-reactive protein
- Protein-lysine 6-oxidase
Sequence:
MTFDDKMKPANDEPDQKSCGKKPKGLHLLSSPWWFPAAMTLVILCLVLSVTLIVQWTQLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKEQEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANFSGPCPQDWLWHKENCYLFHGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSPFWIGLHRKKPGQPWLWENGTPLNFQFFKTRGVSLQLYSSGNCAYLQDGAVFAENCILIAFSICQKKTNHLQI
Protein: Small ribosomal subunit protein eS10y (40S ribosomal protein S10-2) (Q9FFS8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein eS26x
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS28z/eS28y
- Small ribosomal subunit protein eS12z
- Small ribosomal subunit protein eS24z
- Large ribosomal subunit protein uL4y
- Small ribosomal subunit protein eS1z
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein eS24y
Sequence:
MIISETNRREISKYLFKEGVLFAKKDFNLPQHPLIESVPNLQVIKLMQSFKSKEYVRETFAWMHYYWFLTNEGIDFLRTYLNLPSEIVPATLKKQQKPLGRPFGGGGDRPRGPPRGDGERRFGDRDGYRGGPKSGGEYGDKAGAPADYQPGFRGGAGGARQGFGRGAGGFGGGAAGSDLP
Protein: Mannosyltransferase (EC 2.4.1.-) (Q9VBV8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}.
Interaction partners:
- Dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase Alg3
- Dol-P-Man:Man
- Dolichyl-phosphate beta-glucosyltransferase
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dol-P-Glc:Glc
- Dolichol-phosphate mannosyltransferase subunit 1
- GH17155p
Sequence:
MAPPAARARYIANKADNQILSKKPPKRPGLNGNNKTKEATPAGKKKDKDAKKRNQPTSGGQEKGLPNPIMPSVQTAFKTFVSARLCSAIWAYIADCDETFNYWEPLHYIINGHGLQTWEYSPQFGLRSYTYLLLQGVPGYFYQKLFNPSPILIFYMVRCMLGFGCAVMERYMYKSICQEFGIHIGRLWLIFQLFSVGMFVSSTALLPSSFSMYFGCAALAAWWQQNYCFAIFLTAISALLGWPFAALIGIPLVLEMLLRQRDWKTFVQWTLISGATVAIPMIAIDTSYFGKLTFAPLNIVWYNVFTSHGPNIFGTEPLSYYIINGFLNFNIIWLLALQLPIMLVIDYLIVPAKSKSTLNFPHYISLAPLYLWLLVFFAQPHKEERFLFPIYPLISLCGAITVDVYQRIFFRMKSVVFKIKAGVHYLDHSMFIAILVMVTSTLLGLSRVFALYRNYHAPMDLMLELNQFKATPQYDPDVIYNVCIGKDWHRYPGSFFFPAKNFRLRFLKSEFRGMLPAYYDEGQNATKVVQPYFNDLNQENEHMYFDYDRCDFLVDFDEGKYTALEPNYSKRSKDWSVMKSLPFLIPEKSHKVLRAFYVPFLTDNHIQYGDFNLLKRKTKRNGR
Protein: Abscisic acid receptor PYL3 (PYR1-like protein 3) (Regulatory components of ABA receptor 13) (Q9SSM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA. Can be activated by both (-)-ABA and (+)-ABA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus {ECO:0000250|UniProtKB:O49686}. Cell membrane {ECO:0000250|UniProtKB:O49686}. Note=Localizes at the plasma membrane in the presence of a CAR protein. {ECO:0000250|UniProtKB:O80920}.
Interaction partners:
- Protein phosphatase 2C 16
- Protein phosphatase 2C 56
- Protein phosphatase 2C 77
- Protein phosphatase 2C 37
- Abscisic acid receptor PYL1
- Probable protein phosphatase 2C 78
- Probable protein phosphatase 2C 24
- Protein phosphatase 2C 3
- Protein phosphatase 2C 7
- Probable protein phosphatase 2C 75
Sequence:
MNLAPIHDPSSSSTTTTSSSTPYGLTKDEFSTLDSIIRTHHTFPRSPNTCTSLIAHRVDAPAHAIWRFVRDFANPNKYKHFIKSCTIRVNGNGIKEIKVGTIREVSVVSGLPASTSVEILEVLDEEKRILSFRVLGGEHRLNNYRSVTSVNEFVVLEKDKKKRVYSVVLESYIVDIPQGNTEEDTRMFVDTVVKSNLQNLAVISTASPT
Protein: GTP-binding protein YPT53 (P36019)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for transport in the endocytic pathway and for correct sorting of the vacuolar hydrolases suggesting a possible intersection of the endocytic with the vacuolar sorting pathway.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 33
- Rab proteins geranylgeranyltransferase component A
- Vacuolar protein sorting-associated protein 9
- Protein MUK1
- Vacuolar protein sorting-associated protein 21
- GTP-binding protein YPT52
- Vacuolar segregation protein PEP7
- Rab GDP-dissociation inhibitor
- cAMP-dependent protein kinase regulatory subunit
- Vacuolar protein sorting-associated protein 8
Sequence:
MDKHTAAIPTLTIKVVLLGESAVGKSSIVLRFVSDDFKESKEPTIGAAFLTKRITRDGKVIKFEIWDTAGQERFAPLAPMYYRNAQAALVVFDVTNEGSFYKAQNWVEELHEKVGHDIVIALVGNKMDLLNNDDENENRAMKAPAVQNLCERENLLYFEASAKTGENIYQIFQTLGEKVPCPEQNTRQSSTHDRTITDNQRIDLESTTVESTRETGGCNC
Protein: Berberine bridge enzyme-like A (NtBBLa) (EC 1.1.1.-) (F1T160)
Organism: Nicotiana tabacum (Common tobacco)
Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids.
Subcellular location: Vacuole {ECO:0000269|PubMed:21343426}.
Interaction partners:
- Cytochrome P450 CYP82D47
- L-aspartate oxidase
- L-aspartate oxidase 2-b, chloroplastic
- L-aspartate oxidase 2-a, chloroplastic
- L-aspartate oxidase
- Nicotine N-demethylase CYP82E4
Sequence:
MFPLIILISFSLASLSETATGAVTNLSACLINHNVHNFSIYPTSRNYFNLLHFSLQNLRFAAPFMPKPTFIILPSSKEELVSTIFCCRKASYEIRVRCGGHSYEGTSYVSFDASPFVIVDLMKLDDVSVDLDSETAWAQGGATIGQIYYAIAKVSDVHAFSAGSGPTVGSGGHISGGGFGLLSRKFGLAADNVVDALLIDADGRLLDRKAMGEDVFWAIRGGGGGNWGIVYAWKIRLLKVPKIVTTCMIYRPGSKQYVAQILEKWQIVTPNLVDDFTLGVLLRPADLPADMKYGNTTPIEIFPQFNALYLGPKTEVLSISNETFPELGVKNDECKEMTWVESALFFSELADVNGNSTGDISRLKERYMDGKGFFKGKTDYVKKPVSMDGMLTFLVELEKNPKGYLVFDPYGGAMDKISDQAIAFPHRKGNLFAIQYLAQWNEEDDYMSDVYMEWIRGFYNTMTPFVSSSPRGAYINYLDMDLGVNMVDDYLLRNASSSSPSSSVDAVERARAWGEMYFLHNYDRLVKAKTQIDPLNVFRHEQSIPPMLGSTQEHKYSSE
Protein: Octanoyltransferase (EC 2.3.1.181) (Lipoate-protein ligase B) (Lipoyl/octanoyl transferase) (Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase) (P60720)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}.
Interaction partners:
- Lipoyl synthase
- Lipoate-protein ligase A
- UPF0250 protein YbeD
- Glycine cleavage system H protein
- Acyl carrier protein
- Enoyl-[acyl-carrier-protein] reductase FabI
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- Uncharacterized HTH-type transcriptional regulator YbeF
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MYQDKILVRQLGLQPYEPISQAMHEFTDTRDDSTLDEIWLVEHYPVFTQGQAGKAEHILMPGDIPVIQSDRGGQVTYHGPGQQVMYVLLNLKRRKLGVRELVTLLEQTVVNTLAELGIEAHPRADAPGVYVGEKKICSLGLRIRRGCSFHGLALNVNMDLSPFLRINPCGYAGMEMAKISQWKPEATTNNIAPRLLENILALLNNPDFEYITA
Protein: Proline-rich nuclear receptor coactivator 1 (Proline-rich protein 2) (Protein B4-2) (Q12796)
Organism: Homo sapiens (Human)
Function: Nuclear receptor coactivator. May play a role in signal transduction.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- mRNA-decapping enzyme 1A
- C4b-binding protein alpha chain
Sequence:
MTVVSVPQREPLVLGGRLAPLGFSSRGYFGALPMVTTAPPPLPRIPDPRALPPTLFLPHFLGGDGPCLTPQPRAPAALPNRSLAVAGGTPRAAPKKRRKKKVRASPAGQLPSRFHQYQQHRPSLEGGRSPATGPSGAQEVPGPAAALAPSPAAAAGTEGASPDLAPLRPAAPGQTPLRKEVLKSKMGKSEKIALPHGQLVHGIHLYEQPKINRQKSKYNLPLTKITSAKRNENNFWQDSVSSDRIQKQEKKPFKNTENIKNSHLKKSAFLTEVSQKENYAGAKFSDPPSPSVLPKPPSHWMGSTVENSNQNRELMAVHLKTLLKVQT
Protein: Multiple C2 and transmembrane domain-containing protein 1 (Q6DN14)
Organism: Homo sapiens (Human)
Function: Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:D4ABL6}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome {ECO:0000250|UniProtKB:D4ABL6}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A1ZBD6}.
Interaction partners:
Sequence:
MEPRAAAAGEPEPPAASSSFQARLWKNLQLGVGRSKGGGGGRAGGPERRTADTPSPSPPPPVGTGNAPARGSGAGSRWSGFKKRKQVLDRVFSSSQPNLCCSSPEPLEPGGAGRAEQGSTLRRRIREHLLPAVKGPAAASGAAGGTPPGGRSPDSAPSSSSASSSLSSSPQPPPRGDRARDEGARRQGPGAHLCHQKSSSLPGTACLEQLLEPPPPPAEPARSPAESRAPETGEEHGSSQKIINTAGTSNAEVPLADPGMYQLDITLRRGQSLAARDRGGTSDPYVKFKIGGKEVFRSKIIHKNLNPVWEEKACILVDHLREPLYIKVFDYDFGLQDDFMGSAFLDLTQLELNRPTDVTLTLKDPHYPDHDLGIILLSVILTPKEGESRDVTMLMRKSWKRSSKELSENEVVGSYFSVKSLFWRTCGRPALPVLGFCRAELQNPYCKNVQFQTQSLRLSDLHRKSHLWRGIVSITLIEGRDLKAMDSNGLSDPYVKFRLGHQKYKSKIMPKTLNPQWREQFDFHLYEERGGVIDITAWDKDAGKRDDFIGRCQVDLSALSREQTHKLELQLEEGEGHLVLLVTLTASATVSISDLSVNSLEDQKEREEILKRYSPLRIFHNLKDVGFLQVKVIRAEGLMAADVTGKSDPFCVVELNNDRLLTHTVYKNLNPEWNKVFTFNIKDIHSVLEVTVYDEDRDRSADFLGKVAIPLLSIQNGEQKAYVLKNKQLTGPTKGVIYLEIDVIFNAVKASLRTLIPKEQKYIEEENRLSKQLLLRNFIRMKRCVMVLVNAAYYVNSCFDWDSPPRSLAAFVLFLFVVWNFELYMIPLVLLLLLTWNYFLIISGKDNRQRDTVVEDMLEDEEEEDDKDDKDSEKKGFINKIYAIQEVCVSVQNILDEVASFGERIKNTFNWTVPFLSWLAIVALCVFTAILYCIPLRYIVLVWGINKFTKKLRSPYAIDNNELLDFLSRVPSDVQVVQYQELKPDPSHSPYKRKKNNLG
Protein: Probable dehydratase YbiW (EC 4.2.1.-) (P75793)
Organism: Escherichia coli (strain K12)
Function: Probably shows dehydratase activity.
Interaction partners:
- Putative pyruvate formate-lyase 3-activating enzyme
- Probable pyruvate-flavodoxin oxidoreductase
- Probable dehydratase PflD
- PFL-like enzyme TdcE
- NADP-dependent malic enzyme
- Formate acetyltransferase 1
- Propionate--CoA ligase
- D-malate dehydrogenase [decarboxylating]
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Acetaldehyde dehydrogenase
Sequence:
MTTLKLDTLSDRIKAHKNALVHIVKPPVCTERAQHYTEMYQQHLDKPIPVRRALALAHHLANRTIWIKHDELIIGNQASEVRAAPIFPEYTVSWIEKEIDDLADRPGAGFAVSEENKRVLHEVCPWWRGQTVQDRCYGMFTDEQKGLLATGIIKAEGNMTSGDAHLAVNFPLLLEKGLDGLREEVAERRSRINLTVLEDLHGEQFLKAIDIVLVAVSEHIERFAALAREMAATETRESRRDELLAMAENCDLIAHQPPQTFWQALQLCYFIQLILQIESNGHSVSFGRMDQYLYPYYRRDVELNQTLDREHAIEMLHSCWLKLLEVNKIRSGSHSKASAGSPLYQNVTIGGQNLVDGQPMDAVNPLSYAILESCGRLRSTQPNLSVRYHAGMSNDFLDACVQVIRCGFGMPAFNNDEIVIPEFIKLGIEPQDAYDYAAIGCIETAVGGKWGYRCTGMSFINFARVMLAALEGGHDATSGKVFLPQEKALSAGNFNNFDEVMDAWDTQIRYYTRKSIEIEYVVDTMLEENVHDILCSALVDDCIERAKSIKQGGAKYDWVSGLQVGIANLGNSLAAVKKLVFEQGAIGQQQLAAALADDFDGLTHEQLRQRLINGAPKYGNDDDTVDTLLARAYQTYIDELKQYHNPRYGRGPVGGNYYAGTSSISANVPFGAQTMATPDGRKAHTPLAEGASPASGTDHLGPTAVIGSVGKLPTAAILGGVLLNQKLNPATLENESDKQKLMILLRTFFEVHKGWHIQYNIVSRETLLDAKKHPDQYRDLVVRVAGYSAFFTALSPDAQDDIIARTEHML
Protein: Anion exchange protein (E9PUP3)
Organism: Mus musculus (Mouse)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
Sequence:
MKLPGQGDFESSDAHENAHSEEPDSGLGPGPGLNGPSGIDIGESQVSKDPLLFIQLNELLGWPQALEWRETGRWLLFEEKLDMGAGRWSAPHVPTLELPSLQKLRSLLAEGIVLLDCQAQSLLELVEQVVSGESLSPELRGQLQALLLQRPQHHIQTMGIRPCRESNAFRKASRDEDAPLKHQNPLRQKLPAGAEAAAVLAGELGFLEQPLGAFVRLRNPIVLEPLTEMILPSRFFCLLLGPPTLGRSYHEMGRAAAVLLSDPQFQWSVRRASHLPDLLAALDAFLQEVTALPPGRWDRTARIPPPKYLPSQHKRFPSKLQEVTSLSRQSAALAEDKHHHGPHTPIPELQRTGRLFGGLIQDVRRKACWYTSDFLDALHPQCFSAVFYIYLATVTNAITFGGLLGDATEGAQGVLESFLGTAVAGAAFCLMAGQPLTILSSTGPVLVFERLLFSFSRDYSLDYLPFRLWVGIWVTAFCLALVATEASLLVRYFTRFTEEGFCALISLIFIYDAMGKMLNLIRAYPIQRPGSSAYGCFCQYPGTGGNTSEWTSAKLKDTEDILSVPGLVNASFLPPPECIRQGGHPLGPSCHTVPDIAFFSLLLFFTSFLCAIALKHIKNSRFFPSVVRKVLGDFSSVLAILLGCGLDTFLGLATPKLLVPTEFKPTLSGRGWLVSPFGANPWWLSVAAALPALLLSILIFMDQQITAVILNRAEYRLQKGAGFHLDLFCVAVLMLFTSALGLPWYVSATVISLAHIDSLRRESKACIPGEAPNFLGIREQRLTGLVVFVLTGVSIFLAPVLKFVKRVQLLLMPRKHQPDMLLLRHVPLSRVHLFTAIQLACLGLLWVVKSTPAAIVFPLMLLGLVAIRKALEWVFSPQELLWLDELMPEEEETIPENRSEPEHLFSGNDSEDSELMYQPKAPEINISVN
Protein: Protein transport protein HofC homolog (P36646)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Protein transport protein HofB homolog
- Prepilin peptidase-dependent protein D
- DNA utilization protein HofQ
- Putative type II secretion system protein E
- Type II secretion system protein H
- Type II secretion system core protein G
- Prepilin leader peptidase/N-methyltransferase
- Prepilin peptidase PppA
- Putative type II secretion system protein M
- Uncharacterized protein YggR
Sequence:
MASKQLWRWHGITGDGNAQDGMLWAESRTLLLMALQQQMVTPLSLKRIAINSAQWRGDKSAEVIHQLATLLKAGLTLSEGLALLAEQHPSKQWQALLQSLAHDLEQGIAFSNALLPWSEVFPPLYQAMIRTGELTGKLDECCFELARQQKAQRQLTDKVKSALRYPIIILAMAIMVVVAMLHFVLPEFAAIYKTFNTPLPALTQGIMTLADFSGEWSWLLVLFGFLLAIANKLLMRRPTWLIVRQKLLLRIPIMGSLMRGQKLTQIFTILALTQSAGITFLQGVESVRETMRCPYWVQLLTQIQHDISNGQPIWLALKNTGEFSPLCLQLVRTGEASGSLDLMLDNLAHHHRENTMALADNLAALLEPALLIITGGIIGTLVVAMYLPIFHLGDAMSGMG
Protein: UPF0014 membrane protein STAR2 (Protein SENSITIVE TO ALUMINUM RHIZOTOXICITY 2) (Q5W7C1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Associates with STAR2 to form a functional transmembrane ABC transporter required for detoxification of aluminum (Al) in roots. Can specifically transport UDP-glucose.
Subcellular location: Membrane {ECO:0000269|PubMed:19244140}; Multi-pass membrane protein {ECO:0000269|PubMed:19244140}.
Interaction partners:
- Protein STAR1
Sequence:
MMASMAALLQRLLVVVNQVDPGAPGFWREFLVGMLKPVAATAVVAMAVALSFTQRLGLEGEMLYAMARAFLQLSVIGFVLQFIFTQKSAAWILLAYLFMVTVAGYTAGQRARHVPRGKHIAAVSILAGTSVTMALLVALRVFPFTPRYIIPVAGMMVGNAMTVTGVTMKKLREDVGMQRGVVETALALGATPRQATARQVRRSLVIALSPVIDNAKTVGLIALPGAMTGLIMGGASPLEAIQLQIVVMNMLMGASTVSSILSTYLCWPAFFTGAFQLNDAVFAAD
Protein: Chaperone MoxR1 (Q79FN7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- UPF0353 protein Rv1481
- Uncharacterized protein Rv1480
- Peptidoglycan endopeptidase RipA
- Peptidoglycan endopeptidase RipB
- Coproporphyrin III ferrochelatase
Sequence:
MTSAGGFPAGAGGYQTPGGHSASPAHEAPPGGAEGLAAEVHTLERAIFEVKRIIVGQDQLVERMLVGLLSKGHVLLEGVPGVAKTLAVETFARVVGGTFSRIQFTPDLVPTDIIGTRIYRQGREEFDTELGPVVANFLLADEINRAPAKVQSALLEVMQERHVSIGGRTFPMPSPFLVMATQNPIEHEGVYPLPEAQRDRFLFKINVGYPSPEEEREIIYRMGVTPPQAKQILSTGDLLRLQEIAANNFVHHALVDYVVRVVFATRKPEQLGMNDVKSWVAFGASPRASLGIIAAARSLALVRGRDYVIPQDVIEVIPDVLRHRLVLTYDALADEISPEIVINRVLQTVALPQVNAVPQQGHSVPPVMQAAAAASGR
Protein: Anionic trypsin-2 (EC 3.4.21.4) (Anionic trypsin II) (Pretrypsinogen II) (Serine protease 2) (P07146)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Carboxypeptidase A1
- Chymotrypsinogen B
- Bile salt-activated lipase
- trypsin
- Trypsin-5
- Mannose-binding protein C
- Mannose-binding protein A
- Chymotrypsin-like elastase family member 3B
- Carboxypeptidase B
- Chymotrypsin-like elastase family member 2A
Sequence:
MSALLILALVGAAVAFPVDDDDKIVGGYTCRESSVPYQVSLNAGYHFCGGSLINDQWVVSAAHCYKYRIQVRLGEHNINVLEGNEQFVDSAKIIRHPNYNSWTLDNDIMLIKLASPVTLNARVASVPLPSSCAPAGTQCLISGWGNTLSNGVNNPDLLQCVDAPVLPQADCEASYPGDITNNMICVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCAQPDAPGVYTKVCNYVDWIQNTIADN
Protein: Fatty acyl-CoA reductase 2 (Far2) (EC 1.2.1.84) (Q7TNT2)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reduction of saturated but not unsaturated C16 or C18 fatty acyl-CoA to fatty alcohols. A lower activity can be observed with shorter fatty acyl-CoA substrates. It may play a role in the production of ether lipids/plasmalogens and wax monoesters which synthesis requires fatty alcohols as substrates (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:15220348}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q96K12}.
Interaction partners:
- Dihydroxyacetone phosphate acyltransferase
- Alkyldihydroxyacetonephosphate synthase, peroxisomal
Sequence:
MSMIAAFYSNKSILITGATGFLGKVLMEKLFRTSPHLKVIYILVRPKSGQTLQERVFQILNSKLFEKVKEVCPNVHEKIRPISADLNQRDFAISKEDVQELLSCTNIIFHCAATVRFDAHLREAVQLNVTATQQLLLMASQMPKLEAFIHISTAFSNCNLSHIDEVIYPCPVEPRKIIDSMEWLDDSIIEEITPKLIGDRPNTYTYTKALGEIVVQQESGNLNVAIVRPSIVGATWQEPFPGWVDNLNGPSGLIIATGKGFLRSIKATPMAVADVIPVDTVVNLTIAVGWYTAVHRPKSTLIYHSTSGNLNPCNWYKMGLQVLATIEKIPFESAFRRPNADFTTSNFTTHYWNTVSHRVPAIIYDFYLRLTGRKPRMLKLMNRLLKTISMLEYFINHSWEWSTNNTEMLLSELSPEDQRVFNFDVRQLNWLEYIENYVLGVKKYLLKEDLAGIPKAKQHLRRLRNIHYLFNTALFLIIWRLLIARSQMARNVWFFIVSFCYKFISYFRASSTLKV
Protein: Serpina3h protein (A2RTV1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAGVSPAVFGIPDVTLERNTVAVHEVQENITSGDSLTVASSNTDFAFSLYRKLVLKNPDENVVFSPFSISAALALLSLGAKGNTLKEILEGLKFNLTGAPEPDIHQGFRYLLDLLSQPGDQVQISTGSALFIEKHLQILAEFKEKARALYQAEAFTADFLQPRQATKLINDYVSNQTQGKIKELISDLDKSTLMVLVNYIYFKGKWKMPFDPHDTFNSVFYLDEKRSVNVSMMKIEELTTPYFRDDELSCTVVELKYTGNASAMFILPDQGRMQQVEASLQPETLRKWKNSLKPRRIDELHLPKFSISTDNSLEHILPELGIREVFSMQADLSAITGTKDLRVSQVVHKAVLDVAETGTEAAAATGVKLILLCRKIYSMTIYFNRPFLMIISDTKAHIALFMAKVTNPK
Protein: Glucose-6-phosphate isomerase (EC 5.3.1.9) (A0A2U3TZU2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVALCSLQHLGSSDPRALPTLPTATSGQRPAKRRRKSPAMAALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGHILVDYSKNLVTEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLHVALRNRSNTPILVDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKTITDVINIGIGGSDLGPLMVTEALKPYSSGGPRVWYVSNIDGTHIAKTLAQLNPESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNTTKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLALLGIWYINCFGCETHAMLPYDQYLHRFAAYFQQGDMESNGKYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKMIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMRGKSTEEARKELQAAGKSPEDLERLLPHKVFEGNRPTNSIVFTKLTPFMLGALVAMYEHKIFVQGIIWDINSFDQWGVELGKQLAKKIEPELDGSAQVTSHDASTNGLINFIKQQREARVQ
Protein: Pheromone P-factor receptor (Q00619)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Receptor for the peptide pheromone P-factor, a mating factor of S.pombe. Pheromone signaling is essential for initiation of meiosis in S.pombe; P-factor signaling alone may be sufficient.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Mating factor M secretion protein mam1
- Pheromone M-factor receptor
- Guanine nucleotide-binding protein subunit beta
- Regulator of G-protein signaling 1
- Guanine nucleotide-binding protein alpha-1 subunit
- Pro-P-factor
- E3 ubiquitin-protein ligase pub2
- E3 ubiquitin-protein ligase pub1
- E3 ubiquitin-protein ligase pub3
- Casein kinase I homolog 1
Sequence:
MRQPWWKDFTIPDASAIIHQNITIVSIVGEIEVPVSTIDAYERDRLLTGMTLSAQLALGVLTILMVCLLSSSEKRKHPVFVFNSASIVAMCLRAILNIVTICSNSYSILVNYGFILNMVHMYVHVFNILILLLAPVIIFTAEMSMMIQVRIICAHDRKTQRIMTVISACLTVLVLAFWITNMCQQIQYLLWLTPLSSKTIVGYSWPYFIAKILFAFSIIFHSGVFSYKLFRAILIRKKIGQFPFGPMQCILVISCQCLIVPATFTIIDSFIHTYDGFSSMTQCLLIISLPLSSLWASSTALKLQSMKTSSAQGETTEVSIRVDRTFDIKHTPSDDYSISDESETKKWT