wanglab/gogpt-training-data huggingface dataset:
Protein: Myosin-IIIb (EC 2.7.11.1) (Q8WXR4)
Organism: Homo sapiens (Human)
Function: Probable actin-based motor with a protein kinase activity. Required for normal cochlear hair bundle development and hearing. Plays an important role in the early steps of cochlear hair bundle morphogenesis. Influences the number and lengths of stereocilia to be produced and limits the growth of microvilli within the forming auditory hair bundles thereby contributing to the architecture of the hair bundle, including its staircase pattern. Involved in the elongation of actin in stereocilia tips by transporting the actin regulatory factor ESPN to the plus ends of actin filaments.
Subcellular location: Cytoplasm, cytoskeleton. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q1EG27}.
Interaction partners:
- Espin
- Espin-like protein
- Whirlin
- Twinfilin-2
- Epidermal growth factor receptor kinase substrate 8-like protein 2
- Epidermal growth factor receptor kinase substrate 8
- Unconventional myosin-XV
- Gelsolin
- Myosin-IIIa
- Peripheral plasma membrane protein CASK
Sequence:
MKHLYGLFHYNPMMLGLESLPDPTDTWEIIETIGKGTYGKVYKVTNKRDGSLAAVKILDPVSDMDEEIEAEYNILQFLPNHPNVVKFYGMFYKADHCVGGQLWLVLELCNGGSVTELVKGLLRCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQYDSSYDARCDVWSLGITAIELGDGDPPLFDMHPVKTLFKIPRNPPPTLLHPEKWCEEFNHFISQCLIKDFERRPSVTHLLDHPFIKGVHGKVLFLQKQLAKVLQDQKHQNPVAKTRHERMHTRRPYHVEDAEKYCLEDDLVNLEVLDEDTIIHQLQKRYADLLIYTYVGDILIALNPFQNLSIYSPQFSRLYHGVKRASNPPHIFASADAAYQCMVTLSKDQCIVISGESGSGKTESAHLIVQHLTFLGKANNQTLREKILQVNSLVEAFGNSCTAINDNSSRFGKYLEMMFTPTGVVMGARISEYLLEKSRVIKQAAREKNFHIFYYIYAGLHHQKKLSDFRLPEEKPPRYIADETGRVMHDITSKESYRRQFEAIQHCFRIIGFTDKEVHSVYRILAGILNIGNIEFAAISSQHQTDKSEVPNAEALQNAASVLCISPEELQEALTSHCVVTRGETIIRANTVDRAADVRDAMSKALYGRLFSWIVNRINTLLQPDENICSAGGGMNVGILDIFGFENFQRNSFEQLCINIANEQIQYYFNQHVFALEQMEYQNEGIDAVPVEYEDNRPLLDMFLQKPLGLLALLDEESRFPQATDQTLVDKFEDNLRCKYFWRPKGVELCFGIQHYAGKVLYDASGVLEKNRDTLPADVVVVLRTSENKLLQQLFSIPLTKTGNLAQTRARITVASSSLPPHFSAGKAKVDTLEVIRHPEETTNMKRQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNDDREALQFSRERVLAQLRSTGILETVSIRRQGYSHRILFEEFVKRYYYLAFTAHQTPLASKESCVAILEKSRLDHWVLGKTKVFLKYYHVEQLNLLLREVIGRVVVLQAYTKGWLGARRYKRVREKREKGAIAIQSAWRGYDARRKFKKISNRRNESAAHNQAGDTSNQSSGPHSPVAAGTRGSAEVQDCSEPGDHKVLRGSVHRRSHSQAESNNGRTQTSSNSPAVTEKNGHSQAQSSPKGCDIFAGHANKHSVSGTDLLSSRICHPAPDQQGLSLWGAPQKPGSENGLAQKHRTPRRRCQQPKMLSSPEDTMYYNQLNGTLEYQGSKRKPRKLGQIKVLDGEDEYYKSLSPVDCIPEENNSAHPSFFSSSSKGDSFAQH
Protein: Methylmalonyl-CoA decarboxylase (MMCD) (EC 4.1.1.-) (Transcarboxylase) (P52045)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the decarboxylation of (R)-methylmalonyl-CoA to propionyl-CoA. Could be part of a pathway that converts succinate to propanoate.
Interaction partners:
- Methylmalonyl-CoA mutase
- Propanoyl-CoA:succinate CoA transferase
- GTPase ArgK
- 3-hydroxyadipyl-CoA dehydrogenase
- Fatty acid oxidation complex subunit alpha
- Propionate--CoA ligase
- Fatty acid oxidation complex subunit alpha
- Chromosome partition protein MukE
- 2-methylcitrate synthase
- Chromosome partition protein MukB
Sequence:
MSYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSKVFSAGHDIHELPSGGRDPLSYDDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELIFTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSEDYQEGMNAFLEKRKPNFVGH
Protein: Putative agmatinase 2 (EC 3.5.3.11) (Agmatine ureohydrolase 2) (AUH 2) (O42887)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Spermidine synthase
- Ornithine decarboxylase
- Putative agmatinase 1
- Putative agmatinase 3
Sequence:
MFTYQKIIQLALLLSGVCGALASIDTDSHLSPKVLEKLRPTENLAYEDDSLDDDTWRSKRWEFDYQYSGISTFAHLPHVRCLVEQSEDFDIAIIGVPFDTAVSHRPGARFGPKGIRSASSRQMAIRGFNPSLNVNPYESWAKILDCGDIPVSSYDNQLAVRQMTEGYIDLLSRKATASPASNNLKTAGLAKDGIFHPRLITLGGDHSIGLASLRALGHFYGNVSVIHFDSHLDTWNPKRYYPSYWHSDRADFTHGTMFWMASKEGLINNGTSIHAGLRTRLSGTDYYDYEEDNRVGFTFIEAQEIDEIGVNGIVERIKQVVGDTLVYLSIDIDVVDPGLAPGTGTPETGGWTTREMKSILRKLDGHLNLVGAEVVEVSPPYDDRAESTSLAASDFIFEILSSMVKHPLYDVKK
Protein: C2H2-type zinc finger-containing protein (Q54ET8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MINMIDNNKGINKLDAAIYYYLVEKGMAKTALSFSQEMNFDIGGLSPLLSNSSHLLSKGWEQLNSIGFFNNQNIHMTSSPISINSSNNNNNNNNNNSNGNNIHLNNSPPNNNNNNNNNNFFNPPNFLGNNNTNSNNNNNNNNNSNNKNSFLFQNPNQIANPSFFSSANPSTNNIIPPNPNPNSNNNNTGNSGGLILDNSATNFFQNVNSSDNNNNNNNNSGNNVNNNNTNQSIFLSSQKQPIQTEPKNNTNNTNNINPSNNNNNNNNNNNNNNNNNNSSSNNTNNNNNNNNIDNLQSSISSQLQLSSPPSSSPIATSAMSPNNLDTNQILHTIGCNIEHIHNQFCNMLFQNQTNSSPSLSTSHTSMNITNEPAKILDKKSQFSIQSQNDDNNTTNNNNNNNISNNNNNNNNSSNSSNNNNHGNNRNIHNHSHGHNQHNHGHGHNQHNHGHNHGHHNHGHGHNHGHHNHGHHNHGHNHNHNHGHNHNHGNHNNGQNTPIHNHFSSAPIPIGSNNNNNNKTTTTTTTTTTTTNSSSPSDGINFNLNSNSSDVESYLIKSIGEGGEEKFTCDYQSCGKSFSTLAIFKRHLKEHTGCKPFVCTEEGCNKRFSRKFDLKVHLRSHTGEKPYLCTFPGCSKRFARSSDLRLHQRIHTGEKPFVCDWEGCSKRFIRQADLKKHRKTHQLNNNNNAAAASSSSSSSSSHPHVHSVGCGHTAIAHEGHIDFLHDRHLHSMNHDHVDHSIEVSETNPTSCTPKFVCSHHPDGSSHSMDCGHEIVPHFDHYDFLVDGHLHHVHEGHCDNHGWVEVINNFMK
Protein: Serine or cysteine protease inhibitor (Serpin domain-containing protein) (G5EFH4)
Organism: Caenorhabditis elegans
Interaction partners:
- G-protein coupled receptors family 1 profile domain-containing protein
Sequence:
MSDSSSDEKMGLLLHSETDFGLSLLRQQNLTESFVFSPLSIALALSLVHVAAKGETRDEIRKALLNGATDEELEQHFSNISAGLLVAEKGTEVNVANHIFSRKTFTIKKLYLNDVKKLYNAGASQLNFEDQEASAEAINNFVSENTKGHIKKIINPDSISEELVAVLTNAFYFKANWQTKFKKESTYKREFFSSENSKRETEFLHSRNSNRKYSENGQFQVLSLPYKDTSFALSIFLPKTRFGLSEALQNLDSVTIQQLMSNTSNTLVNIAMPKWKIETALGLNRALMAVGIEKAFTDSADLSNFADGIYISQAAHKALIEVDEDGTVAAAATTISFSLTSVFIPAEEPIEFTADHPFLFILSKDNHPLFIGIHN
Protein: Probable transcriptional regulatory protein HAH1 (P53212)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823961}.
Interaction partners:
- Copper chaperone ATX1
- Uncharacterized membrane protein YGR026W
- mRNA-binding protein PUF3
- Tyrosine--tRNA ligase, mitochondrial
- Aspartate--tRNA ligase, mitochondrial
- Altered inheritance of mitochondria protein 18, mitochondrial
Sequence:
MLVRNRYLGELLKNSRSFSVLNSSVRSGHNKWSTIKHGKAKNDAERNKINNKFANQIAMSVKLGNGITDPSMNIRLATSIELANKNNVSKKVIENAIRKASGSSASGKDSNASELCVYEGMGPGGVAIVVEALTDNKNRTIGLIRSAFNKANGSMTPTLFFFDKKGYVTMVPPKMLDTEDKVLESVLEIQGIEDIAPVQEDAEDLECDTETETTGQTYEAVMEPADTNKVAALLKERGFHIRDLGIGYNAKPDMEVFVQGDETLEKLQKLTTALEDIDEVTSLYTNASNA
Protein: Thioredoxin peroxidase 1 (EC 1.11.1.15) (Q8IL80)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Thioredoxin-like protein
- Thioredoxin-like protein 2
- Thioredoxin 1
- Thioredoxin 3
- NADH-cytochrome b5 reductase, putative
- Peroxiredoxin
Sequence:
MASYVGREAPYFKAEAVFADNTFGEVNLHDFIGKKYVLLYFYPLDFTFVCPSEIIALDKALDAFKERNVELIGCSVDSKYTHLAWKKTPLTKGGIGNIQHTLISDITKSISRSYNVLFGDSVSLRAFVLIDKQGVVQHLLVNNLAIGRSVEEVLRIIDAVQHHEQHGDVCPANWKKGKVAMKPSEEGVSEYLSKL
Protein: Transmembrane 9 superfamily member 1 (MP70 protein family member) (hMP70) (O15321)
Organism: Homo sapiens (Human)
Function: Plays an essential role in autophagy.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:19029833}; Multi-pass membrane protein {ECO:0000269|PubMed:19029833}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:19029833}; Multi-pass membrane protein {ECO:0000269|PubMed:19029833}.
Interaction partners:
- Charged multivesicular body protein 2a
Sequence:
MTVVGNPRSWSCQWLPILILLLGTGHGPGVEGVTHYKAGDPVILYVNKVGPYHNPQETYHYYQLPVCCPEKIRHKSLSLGEVLDGDRMAESLYEIRFRENVEKRILCHMQLSSAQVEQLRQAIEELYYFEFVVDDLPIRGFVGYMEESGFLPHSHKIGLWTHLDFHLEFHGDRIIFANVSVRDVKPHSLDGLRPDEFLGLTHTYSVRWSETSVERRSDRRRGDDGGFFPRTLEIHWLSIINSMVLVFLLVGFVAVILMRVLRNDLARYNLDEETTSAGSGDDFDQGDNGWKIIHTDVFRFPPYRGLLCAVLGVGAQFLALGTGIIVMALLGMFNVHRHGAINSAAILLYALTCCISGYVSSHFYRQIGGERWVWNIILTTSLFSVPFFLTWSVVNSVHWANGSTQALPATTILLLLTVWLLVGFPLTVIGGIFGKNNASPFDAPCRTKNIAREIPPQPWYKSTVIHMTVGGFLPFSAISVELYYIFATVWGREQYTLYGILFFVFAILLSVGACISIALTYFQLSGEDYRWWWRSVLSVGSTGLFIFLYSVFYYARRSNMSGAVQTVEFFGYSLLTGYVFFLMLGTISFFSSLKFIRYIYVNLKMD
Protein: Heterodimeric geranylgeranyl pyrophosphate synthase small subunit, chloroplastic (Q39108)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase small subunit. The small subunit alone is inactive in vitro while the large subunit GGPPS1 catalyzes mainly the production of geranygeranyl-diphosphate in vitro. Upon association of the two subunits, the product profile changes and the production of gerany-diphosphate is strongly increased.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Geranylgeranyl diphosphate reductase, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- 1,8-cineole synthase 1, chloroplastic
- Phytoene synthase 1, chloroplastic
- Isopentenyl phosphate kinase
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Ent-copalyl diphosphate synthase, chloroplastic
- Geranylgeranyl pyrophosphate synthase 6, mitochondrial
- Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic
Sequence:
MLFSGSAIPLSSFCSLPEKPHTLPMKLSPAAIRSSSSSAPGSLNFDLRTYWTTLITEINQKLDEAIPVKHPAGIYEAMRYSVLAQGAKRAPPVMCVAACELFGGDRLAAFPTACALEMVHAASLIHDDLPCMDDDPVRRGKPSNHTVYGSGMAILAGDALFPLAFQHIVSHTPPDLVPRATILRLITEIARTVGSTGMAAGQYVDLEGGPFPLSFVQEKKFGAMGECSAVCGGLLGGATEDELQSLRRYGRAVGMLYQVVDDITEDKKKSYDGGAEKGMMEMAEELKEKAKKELQVFDNKYGGGDTLVPLYTFVDYAAHRHFLLPL
Protein: Uncharacterized protein (Q38CB7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAEERCLEGPMEYFFAALERQFPKQTALIGGAKSLTQAILRALDVLYPFVEALFVRFMDYAKSLSSHELNQILPLIAGFSICFFGGCFFTLFSTVEIVYLTSWDRIKKSAEVIHRNYVAAMEASRKDDAPGYGYTVTTGDESLSKNELLSRKLRIFLQSVDPVSVKEELAAVALAFMAVVAALRDRFAYYVTLGCILADTAPRFFPLKAILEESLPPELQKLAGPFSNFLFGALGTTIAVLASQYTITLHCATRGSKMLVDSALELAKTRGIVVQDVKVDDSWVKAFAFGLAVIGFTWQAANGFSLPFPLNLLLFPVTVLEWIVNVIFRASGSAVWATTLSV
Protein: Dehydrodolichyl diphosphate synthase complex subunit NUS1 (EC 2.5.1.87) (Cis-prenyltransferase subunit NgBR) (Nogo-B receptor) (NgBR) (Nuclear undecaprenyl pyrophosphate synthase 1 homolog) (Q96E22)
Organism: Homo sapiens (Human)
Function: With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length. Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19723497, ECO:0000269|PubMed:21572394}; Multi-pass membrane protein {ECO:0000303|PubMed:21572394}. Note=Colocalizes with Nogo-B during VEGF and wound healing angiogenesis. {ECO:0000269|PubMed:19723497}.
Interaction partners:
- Dehydrodolichyl diphosphate synthase complex subunit DHDDS
- Geranylgeranyl pyrophosphate synthase
- Farnesyl pyrophosphate synthase
- All trans-polyprenyl-diphosphate synthase PDSS1
- All trans-polyprenyl-diphosphate synthase PDSS2
- Reticulon-4
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein farnesyltransferase subunit beta
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Squalene synthase
Sequence:
MTGLYELVWRVLHALLCLHRTLTSWLRVRFGTWNWIWRRCCRAASAAVLAPLGFTLRKPPAVGRNRRHHRHPRGGSCLAAAHHRMRWRADGRSLEKLPVHMGLVITEVEQEPSFSDIASLVVWCMAVGISYISVYDHQGIFKRNNSRLMDEILKQQQELLGLDCSKYSPEFANSNDKDDQVLNCHLAVKVLSPEDGKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLPWHIRLTEIVSLPSHLNISYEDFFSALRQYAACEQRLGK
Protein: mRNA export factor (Immediate-early protein IE63) (Infected cell protein 27) (ICP27) (VMW63) (P10238)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Multifunctional regulator of the expression of viral genes that contributes to the shutoff of host protein synthesis and mediates nuclear export of viral intronless mRNAs. Early in infection, this immediate early (EI) protein mediates the inhibition of cellular splicing. This results in the accumulation of unprocessed 3'end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off early after virus infection. Later in the infection, it helps recruit cellular RNA polymerase II to viral replication sites and promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP. ICP27 binds to NUP62 which may provide facilitated viral mRNA export and may indirectly compete with some host cell transport receptors for binding and inhibit cellular nucleocytoplasmic transport pathways. Also stimulates translation of viral transcripts. Repression of host gene expression blocks the cell cycle at the G1 phase and prevents apoptosis. Seems to silence the 3' splice site of the promyelocytic leukemia (PML) intron 7a, thereby switching PML isoforms from PML-II to PML-V. This could be linked to the accelerated mRNA export induced by ICP27 which might not provide sufficient time for PML pre-mRNA to be spliced in the nucleus.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:9501050}. Host nucleus {ECO:0000269|PubMed:26062451, ECO:0000269|PubMed:9501050}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:9501050}.
Interaction partners:
Sequence:
MATDIDMLIDLGLDLSDSDLDEDPPEPAESRRDDLESDSSGECSSSDEDMEDPHGEDGPEPILDAARPAVRPSRPEDPGVPSTQTPRPTERQGPNDPQPAPHSVWSRLGARRPSCSPEQHGGKVARLQPPPTKAQPARGGRRGRRRGRGRGGPGAADGLSDPRRRAPRTNRNPGGPRPGAGWTDGPGAPHGEAWRGSEQPDPPGGQRTRGVRQAPPPLMTLAIAPPPADPRAPAPERKAPAADTIDATTRLVLRSISERAAVDRISESFGRSAQVMHDPFGGQPFPAANSPWAPVLAGQGGPFDAETRRVSWETLVAHGPSLYRTFAGNPRAASTAKAMRDCVLRQENFIEALASADETLAWCKMCIHHNLPLRPQDPIIGTTAAVLDNLATRLRPFLQCYLKARGLCGLDELCSRRRLADIKDIASFVFVILARLANRVERGVAEIDYATLGVGVGEKMHFYLPGACMAGLIEILDTHRQECSSRVCELTASHIVAPPYVHGKYFYCNSLF
Protein: UDP-Glucose Glycoprotein glucosylTransferase (Q9GPA0)
Organism: Caenorhabditis elegans
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- Nucleoside-diphosphatase uda-1
- Calnexin
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3
- Calreticulin
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Methylmalonic aciduria type A homolog, mitochondrial
- Glucosidase II subunit alpha
- Nucleoside-triphosphatase ntp-1
Sequence:
MNLTGLLIFFCHIAVLAALEKKGVHTSLKANWDSTSLLAEASEFIAEENEKLFVKFIDIVNKDVGTLNWEKLTDEQKYEYTIKTAGKVLSTSSVDLLKFALALRQYSPRVQSFQQIAVEYGEKCDVFVVVGEQVSCEYTKLEKMIKDAKTNSQVLESDHIFGEKDLKQAAILYGELGTTSFAKAWEKLSKLQKTKLIFRHFSKKTDSHPVSLSGYGVELAIKNTEYKAVDESSEKKNVEEDEADLFGFNIKLLKELHPDSVDAIESFRVNLKESDELTPLKRWELQDLSYQAAQKIVNAGPADAIGTLEEYSQNFPTHARALAKTSVSDLLRKEVLQNRKMLEKASIEVGETSLYINGINQDINSLDLFKLADLLKQENKLADGFHSMGINREYLSILVGMDTSDDEKTTYAVDHREGYPFFINNLDTDKKYKQWGNSVKLMLQPYYPGMIRPIARNLFSLVFVVDPSTSEGRKFLRIGQTFNSHDIAMRIGYIFAVNQDTKASGETDLGVALLNLFNFVSIDSSNADALKVLNNFLDDYRSKDPTIEDIKEFFEAKFSDASFSDVFGVNSDYDKGRKHGFEFVQKTGLNSAPKVLLNGFILDDEGVRGDNIEETIMMEVMKISPKIQRAIMEGKLTDRMNVGNWVLEQKDVMPRINKRILSAPSKKTYVEILGSMDCKSLKDVENLSDSDKAGCLLQTTKYLQKASADSILPVTLWVVADAEAASGRRFIYNSLQILKNSANSRVGIIFNPESVEKACESNSISSYIRAALDFLPMDQAKRLILKLSNEEYAADFISGKITFDDLSVGGMDTAKFLADKKKLDCERTRLESQIVKKVLDISSGGRVVVGNALQVGPLESSEHFEAADFKLLESMLLSRGAEVISSHLKKWEFDVSNGVGSNTVFSIAGHVGKHASSQKRTWVSIQGDEHSVVTLPADEMDRPAVDVLAVVDPLTMEAQKLGSILHLIKKVTNCEIKIVMNPKDKHSELPLKRFYRYAAASELSFDHNGNLNTNVVRFDNLPSKQLLTLSLQAPDSWIVEAVSAKYDLDNIKMEQANGDVTAEFALQHLLLDGQCFDEVSGQPPRGLQFTLGTDKNPKQFDTIVMANLGYFQLKANPGAWKLEIRDGKSSEIYKIGSHVGAEKIGEDVLQVVIDSFTGKSVRVRVEKREGMEERNLLSDDEEGVWSSLSNLVSSKEKTQEVINVFSLASGHLYERFMRIMIVSVMKNTKHPVKFWLLKNYLSPQFKETLPTLAKHYGFEYELIEYKWPRWLHQQKEKQRIMWGFKILFLDVLFPLDVQKVIFVDADQVVRADLMELMKFDLGNAPYGYVPFCESRKEMDGFRFWKQGYWANHLAGRRYHISALYVIDLQKFRQIAAGDRLRGQYQGLSGDPNSLANLDQDLPNNMIHQVKIKSLPQEWLWCETWCDDGSKKNAKTIDLCNNPLTKEPKLDSAARIIGEWKTYDDEIREVISGHSSDNPSDNVISENDDSHTEL
Protein: Phosphatidylserine decarboxylase proenzyme 2 (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 2 beta chain; Phosphatidylserine decarboxylase 2 alpha chain] (F4KAK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Contributes only to a minor proportion of PtdEtn production.
Subcellular location: Vacuole membrane {ECO:0000305|PubMed:17449644}; Peripheral membrane protein {ECO:0000305|PubMed:17449644}. Note=Tonoplast.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- CDP-diacylglycerol--serine O-phosphatidyltransferase 1
- Choline/ethanolaminephosphotransferase 1
- Choline/ethanolaminephosphotransferase 2
- Lysophospholipid acyltransferase 1
- Lysophospholipid acyltransferase 2
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 2
- Phospholipase D alpha 2
- Lecithin-cholesterol acyltransferase-like 4
- Phospholipase A
Sequence:
MGNGNSREAKESRRSRLRHKLQKFRIHRRHLRSSRNSAGMVIQRTVSAEDFSGIALLTLIGAEMKFKDKWLACVSFGEQTFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPESTCKSFNLLDPTSSNVVGSIFLSCAIEDPVETERRFAKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALLALQQEQEPIINNCPVCGEALQVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDRQASYGWMFKLSEWTHLSTYDVGLNTGSSASYIVVIDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMSSVESAQKIPRFLEFFKDQINMAEVKYPLQHFKTFNEFFIRELKPGARPIACMNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVNPNAFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNSKYCNVFTENKRTVAIISTAEFGKVAFVAIGATMVGSINFVRKEGEHVKKGDELGYFSFGGSTVICVFEKDAIGIDNDLLVNSGRSLETLVSVGMQLGVSTRTFARSTLI
Protein: ferric-chelate reductase (NADPH) (EC 1.16.1.9) (A0A1D8PKY2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Fth1p
- Siderophore transporter
- GPI-anchored hemophore PGA7
- High-affinity iron permease
- GPI-anchored hemophore RBT5
- Fre9p
- Hap43p
Sequence:
MAIPFDQQFFVEKDRNNKYEWLIFVLTFIVLAGHGILFYWIPRYLRVNNKRNNYFRLLKVWDAWTSCVHVWGDFYFQPSLVLLGILFVGLNVGFCFAEINDLDYQSRFYIISKRLSKVAVGNLPILLFAVMKNDLLTSITGLQHDRLEFVHKWLSRLMWVMITIHMGMACYYWLNLNFKIMIMIPPQIFGFMAYGSFSILNWASLKFIRQFAYDFFLVQHRIFAFMMLFFTFIHNQGNRAVVLISVHGLVIDRVVSKVFAYLHAKKSPTKGRCTFRIIDDSTISVVIPVSEAGYTSKSWYTRFLPKYKTWKAGQHIYLNVGKIKFFQYHPFTISSLAESGEMKLLIRVERGFTRKLMRHLEQVDHDEVTIKAMFHGPYGARYQPLITFDTCLFFAAGSGGAFTFPVCLDLLNQIDRRDQEGDVLFRPKNQFIKFVWAIRKQDNIEWFEDSLKQFAGRCSVDIYITQETKEELPLQRKNSIIEITKSLTNDYNILYGRPQIQDIIQQHSQSLGANQSMAVTSCGSPSFTNSIKHHCQSARRVKGAPEVYCYTESF
Protein: GH19218p (No long nerve cord, isoform B (EC 3.4.24.-)) (Q9V9Q9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSVNMNWTSPKIWAALFVTTLCLLDTQAAWAKKLNASQAFDDTWNTASDLENELEQQKRSKVQSAGGGGGAGGGPGQWSSWSDWSTCSRTCDGGIMHQMRRCGSPGSCRGESTRYRICNMQPCPEQQDFRSSQCSAYNDVPYDGTLYKWTPHYDYVEPCALTCRGHPAHLVEDISRETGDGNAEEAEHYDEQSVIVQLSARVQDGTRCRSGSLDMCIQGKCQRVGCDLKIGSTKKIDGCGVCGGDGNSCSQPLFNWEMAPMSQCSVTCGSGYKMSRPICRNRLTNADVDDTLCSVTNRPEASVEQCNTHSCPPRWIADDWSTCSRLCGHGYRERMVVCAEESNGIKTRVADIMCRTPKPPTQETCIIEECPHWEVEDWTGCSVSCGQGIQMRGVECKSTDGSLSAKCDPLTKPGSMQQCSTGIHCGGSLNKVGGTIIVGSSRSLNERSERQLDSSDADEDNEDENDEGDDVDDLESGQDTDDGEGLSYADQPLLYAHRTQSRLNQEAPDEPRTMHLMNGNSNNNFNRGEDESEGPSLDPTYIKDNEWSPCSVTCGEGIRRRTYNCKIFLEYSRTVATVNDSLCEGKKPHDEVERCVEDPCMLPSHGFDDQFPRDSIKVGVSEPGKTYVWREQGYTSCSASCLGGVEELIINCVREDNGRVVSPFLCSPETKPEARVRTCNDRPCPPRWNYSDYTPCSKSCGIGIKTREVQCIHEVTRGGDNTMVVPNSMCPQPPPADRQYCNVLDCPVRWEVGEWSKCSHTCGYGFKDRKVECKQIMAQEHKIERPESMCPSAKPADKKPCNVKPCPPEDPKPVIQINNSTHIQHDPKKTKITLKVGGAGLVFFGTQVKIKCPVKRYNRTKIKWSKDHKPLQRSRKYKVSKKGALRILDITFRDAGVYSCHAGLSSAEISIEVKAKPGQQIEELEQQETERLVREKSGTEALTSADMKSADGTGTSTAVGPNSHVNGSAQQHGSRRRQQQSERLQNGRERSRRPKSDGVQHADSSIMEDDVEPF
Protein: Ensconsin, isoform H (LD35939p) (F2FB68)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASLGGQHGNISTNPEVENTAKRPESREGSAERKDREEKLKYARDRQNEERHRKIEELRAQAEAAQRYREQKEEERRRRIEEIRTRDTEKRHQVEERKKAIFEAEKERREYILKKNQERESRIEVKKRDRNSIGFAFGSSTPRLLDVPADYGLVSPSAFWGQRRSTSISNVAGASLTRRSSERELADSGAKKRASSSTDRQDGSRSGNATPGGHFNNSRPGSAMSTSTNMSTSGLVPRRPATAPRKPRPASIAGTGMSLEEINKLKRDQKPPVKTTAASPSAQTTPKRTANLMSTSLIVTSSSSRLSSAEKKTPSKREPPVPKAASASKALPSRTASSERISRLTKEPKTKDTSAMTRSMIVTSSSTSTITKPAPAPVAPTSAPVPEQNGVAKEVEKTTADEPVPEAEVPTEAPVVVPSVSKAEKEALNTEKTEEGARQEEEQILAVESVPEALVTSINVEEKSDEGNEKEVPKPQEQAAPKKPSRSKENSEVRELTPPEGADLMTASMMAKKITTEEEAKAALAERRRLAREEAERQAELERQRLEAERLAEIKAQEEEAERQRLFEEESTRLAEEQRRGEEERLRKAIEEAQQREEEEKRRREEEEKQRVEREEAEKKAKEEAEKQRVEVAERLKREEKEREERRKRVEAIMLRTRKGGAATTPSKDANDKAAPAATAPENNSSSNSSVTGSSNNSAEGSPSAADSTPAPTATETVQEAPNSQAMYEQSVLDKENSLINSFSTMIIDENAKNLQQVSNGKLLVDFESTNTVPAVANGNGHIENVNNKNDINLLQDVVAPVATQLIDLSIESQDLHLNNNNSLLTSTAATTTLVTADSHENKDISLL
Protein: Retinal Mueller cells isomerohydrolase (EC 3.1.1.64) (All-trans-retinyl ester 13-cis isomerohydrolase C) (EC 3.1.1.90) (All-trans-retinylester 11-cis isomerohydrolase C) (Lutein isomerase) (Meso-zeaxanthin isomerase) (EC 5.3.3.22) (Retinal pigment epithelium-specific 65 kDa protein homolog C) (RPE56c) (A9C3R8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes both 11-cis retinol and 13-cis retinol, 2 stereoisomeric forms of retinoic acid from all-trans-retinyl ester. Acts as an alternative isomerohydrolase in retinal Mueller cells by catalyzing formation of 11-cis retinol, to meet the high demand for the chromophore by cones. Capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21676174}. Cell membrane {ECO:0000269|PubMed:21676174}; Lipid-anchor {ECO:0000269|PubMed:21676174}. Note=Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. {ECO:0000250|UniProtKB:Q28175}.
Interaction partners:
- Retinol dehydrogenase 10-B
- Retinol dehydrogenase 5
- Lecithin retinol acyltransferase b, tandem duplicate 2.
- Patatin-like phospholipase domain-containing 4.
- Lecithin retinol acyltransferase a
- Lecithin retinol acyltransferase b, tandem duplicate 1.
- Retinol dehydrogenase 20
- Retinol dehydrogenase 10-A
- O-acyltransferase
- O-acyltransferase.
Sequence:
MVSRLEHPAGGYKKVFESCEELAEPIPAHVSGEIPAWLSGSLLRMGPGLFEVGDEPFYHLFDGQALLHKFDLKDGRVTYHRRFIRTDAYVRAMTEKRVVITEFGTTAYPDPCKNIFSRFFTYFQGIEVTDNCLVNIYPIGEDFYACTETNFITKVDPDTLETVKKVDLCNYLSVNGLTAHPHIEADGTVYNIGNCFGKNMSLAYNIVKIPPLQEDKSDQFEKSKILVQFPSSERFKPSYVHSFGITENHFVFVETPVKINLLKFLTSWSIRGSNYMDCFESNDKMGTWFHLAAKNPGKYIDHKFRTSAFNIFHHINCFEDQGFIVVDLCTWKGHEFVYNYLYLANLRQNWEEVKKAALRAPQPEVRRYVLPLDIHREEQGKNLVSLPYTTATAVMRSDGTVWLEPEVLFSGPRQAFEFPQINYSKFNGKDYTFAYGLGLNHFVPDRICKLNVKSKETWIWQEPDAYPSEPLFVQSPDAEDEDDGVLLSIVVKPGVSQRPAFLLILKATDLTEIARAEVDVLIPVTLHGIYKP
Protein: Translocon-associated protein subunit delta (Signal sequence receptor subunit delta) (Q6IQ57)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
Interaction partners:
Sequence:
MKLVLTALLALCLSFCAAETCTDPVISPSSYTTTDALISSETVFIVELSLACANGAQSVALYADVNGKQFPVTRGQDVGKYQVSWSVPHKQASSGTYQVKFFDEESYSTLRKAQRNNEDVDAIKPLFSVNVDHRGAWNGPWVSTEVLAALIGIMVYYLAYSTKSAIQA
Protein: MYG1 protein C694.04c (Q9P7T6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MNNLVKIATHSGTFHADEALAVYMLRRLDRFSGAQIVRSRDPQVLDSCDIIVDVGGKYDGIKYFDHHQREFNDTFSPKYSTRLSSAGLIYKHFGREVIHAVLPQLKINEQDLETLYEKVYQSFVEGLDANDNGISAYPAGLKPSFKAAMSLPEMVSSFLPAWNSEKQDDQTYLECFQKASDLMGTWFVRSVEHYALSWLPAKTLAREAILKAKDSPILIVDQFFPWKGHLFDIEKELGIENQFKYAIYSDGKAWRVQAVSIDPTSFTCRLPLPEPWRGIRDEKLSELTGIPGCIFVHASGFIGGNQTFEGALEMARKALDFPQN