wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin (A0A060Y1P2)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Uncharacterized protein
- Fibronectin type-III domain-containing protein
- UDP-N-acetylglucosamine transferase subunit ALG13
- UDP-N-acetylglucosamine transferase subunit ALG13
- UDP-N-acetylglucosamine transferase subunit ALG13
- Tudor domain-containing protein
- Fibronectin type-III domain-containing protein
- Interleukin-7 receptor subunit alpha
- Fibronectin type-III domain-containing protein
- Interleukin 21 receptor, tandem duplicate 1
Sequence:
MTGFLTVLLFCIRLLERRTKKRGRWICLFWGFHYYPHQRLNIELWNCFIILSCLSATAHLPIAGAAETHGMTIDDVKELQSELKNLKSTIEKSDACLYAPTNDDIYNDNCIFKFMHCYLLELEVVLFEDMSVTDNYHDEIKTSIYHRKKRLEEHERQYNSSRCSPCEAQRVANSTIFLYNLERLLERIGQTVS
Protein: Claudin (Q5XIT8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, tight junction {ECO:0000256|RuleBase:RU060637}. Cell membrane {ECO:0000256|RuleBase:RU060637}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU060637}.
Interaction partners:
- Tight junction protein ZO-1
- Occludin
- Tight junction protein 3
- Claudin
- Junctional adhesion molecule A
- Claudin-1
- Tight junction protein 2
- Claudin-12
- Claudin-7
- Claudin
Sequence:
MASMGLQVLGISLAVLGWLGVILSCSLPMWRVTAFIGSNIVTAQTSWEGLWMNCVVQSTGQMQCKMYDSMLALPQDLQAARALMVISIIVGALGMLLSVVGGKCTNCMEDETVKAKVMITAGAVFIVASMLIMVPVSWTAHNVIRDFYNPLVASGQKREMGASLYIGWAASGLLLLGGGLLCCNCPPRRNEKPYSAKYSAARSVPASNYV
Protein: Osmosensory protein A (Putative SigF antagonist) (Putative anti-anti-sigma factor Rv0516c) (O33361)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of a signaling pathway that enables adaptation to osmotic stress through cell wall remodeling and virulence factor production. Unphosphorylated OprA forms a complex with the anti-anti-sigma-factor paralog Rv2638 that dissociates on OprA phosphorylation by PknD. Phosphorylation of OprA may stimulate the release of SigF from an inhibitory complex and enable the transcription of osmotically regulated genes, such as oprA and the ESX-1-associated virulence factor espA.
Interaction partners:
- Multidomain regulatory protein Rv1364c
- RNA polymerase sigma factor SigF
- Anti-sigma-F factor RsbW
- Carboxyltransferase domain-containing protein
- Carboxyltransferase domain-containing protein
- Uncharacterized protein Rv1354c
Sequence:
MTTTIPTSKSACSVTTRPGNAAVDYGGAQIRAYLHHLATVVTIRGEIDAANVEQISEHVRRFSLGTNPMVLDLSELSHFSGAGISLLCILDEDCRAAGVQWALVASPAVVEQLGGRCDQGEHESMFPMARSVHKALHDLADAIDRRRQLVLPLISRSA
Protein: Max dimerization protein 1 (Max dimerizer 1) (Protein MAD) (P50538)
Organism: Mus musculus (Mouse)
Function: Component of a transcriptional repressor complex together with MAX (By similarity). In complex with MAX binds to the core DNA sequence 5'-CAC[GA]TG-3' (By similarity). Antagonizes MYC transcriptional activity by competing with MYC for MAX binding (By similarity). Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q05195}.
Interaction partners:
- Paired amphipathic helix protein Sin3b
- Protein max
- Paired amphipathic helix protein Sin3a
- Myc proto-oncogene protein
- ETS translocation variant 3
- Histone deacetylase 2
- Forkhead box protein O3
- Myc box-dependent-interacting protein 1
- Histone deacetylase 5
- Probable ATP-dependent RNA helicase DDX20
Sequence:
MATAVGMNIQLLLEAADYLERREREAEHGYASMLPYSKDRDAFKRRNKPKKNSTSSRSTHNEMEKNRRAHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRRLEKLGAERTRMDSVGSVVSSERSDSDREELDVDVDVDVDVDVEGTDYLNGDLGWSSSVSDSDERGSMQSLGSDEGYSSATVKRAKLQDGHKAGLGL
Protein: Tubulointerstitial nephritis antigen (TIN-Ag) (Q9UJW2)
Organism: Homo sapiens (Human)
Function: Mediates adhesion of proximal tubule epithelial cells via integrins alpha3-beta1 and alphaV-beta3. This is a non catalytic peptidase C1 family protein.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:10752525, ECO:0000269|PubMed:1762287}.
Interaction partners:
- TERF1-interacting nuclear factor 2
Sequence:
MWTGYKILIFSYLTTEIWMEKQYLSQREVDLEAYFTRNHTVLQGTRFKRAIFQGQYCRNFGCCEDRDDGCVTEFYAANALCYCDKFCDRENSDCCPDYKSFCREEKEWPPHTQPWYPEGCFKDGQHYEEGSVIKENCNSCTCSGQQWKCSQHVCLVRSELIEQVNKGDYGWTAQNYSQFWGMTLEDGFKFRLGTLPPSPMLLSMNEMTASLPATTDLPEFFVASYKWPGWTHGPLDQKNCAASWAFSTASVAADRIAIQSKGRYTANLSPQNLISCCAKNRHGCNSGSIDRAWWYLRKRGLVSHACYPLFKDQNATNNGCAMASRSDGRGKRHATKPCPNNVEKSNRIYQCSPPYRVSSNETEIMKEIMQNGPVQAIMQVREDFFHYKTGIYRHVTSTNKESEKYRKLQTHAVKLTGWGTLRGAQGQKEKFWIAANSWGKSWGENGYFRILRGVNESDIEKLIIAAWGQLTSSDEP
Protein: Tektin (A0A0R4IRF0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|RuleBase:RU367040}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
- EF-hand domain
- Outer dynein arm-docking complex subunit 4
- Tektin 2
- Testis-expressed 9
- Growth arrest-specific 2-like 2.
Sequence:
MSRLMGPPDRFLPSEWKHANQEHYRSSEAGRKHSEKLTAECERLIEECNKSNKRMQHDTQKRLERRIQDIKFWRQELVQKFEQMVQEIETLIIYKSRVEKALESCSEPFQVTLQCLAERQKRVAIDLVHDEVEEELLKEKEVVEGVMVLLQRTLEQINEQIRLIRSVKYYLEKDLQDKFQAEHIDDFCSLLTNTSPDLNEGNSSFKYSGAAVTPEEWESLCNLNISKAEKEKNNSLSLRALVDSLLEQTARDMRRQYETTGRAFDLRIEETKTAKEQLENQLNELLAEIANQEKNQDALRLAVAEKEAPLKVAQTRLSTRSQRPNVELCHDPPQIQLLAQIKELTNHVQRLSEALELSESELKALAYNQLRLEEEIQVKTNSLYIDEVICHQLRQHITIQSF
Protein: Secreted frizzled-related protein 2 (FRP-2) (sFRP-2) (Secreted apoptosis-related protein 1) (SARP-1) (Q96HF1)
Organism: Homo sapiens (Human)
Function: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP2 may be important for eye retinal development and for myogenesis.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Protein Wnt-3a
- Protein Wnt-5a
- Protein Wnt-7b
- Protein Wnt-4
- Protein Wnt-2
- Low-density lipoprotein receptor-related protein 5
- Protein Wnt-11
- Protein Wnt-2b
- Proto-oncogene Wnt-1
- Protein Wnt-7a
Sequence:
MLQGPGSLLLLFLASHCCLGSARGLFLFGQPDFSYKRSNCKPIPANLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSLCVQVKDRCAPVMSAFGFPWPDMLECDRFPQDNDLCIPLASSDHLLPATEEAPKVCEACKNKNDDDNDIMETLCKNDFALKIKVKEITYINRDTKIILETKSKTIYKLNGVSERDLKKSVLWLKDSLQCTCEEMNDINAPYLVMGQKQGGELVITSVKRWQKGQREFKRISRSIRKLQC
Protein: Semaphorin-4A (Semaphorin-B) (Sema B) (Q9H3S1)
Organism: Homo sapiens (Human)
Function: Cell surface receptor for PLXNB1, PLXNB2, PLXNB3 and PLXND1 that plays an important role in cell-cell signaling (By similarity). Regulates glutamatergic and GABAergic synapse development (By similarity). Promotes the development of inhibitory synapses in a PLXNB1-dependent manner and promotes the development of excitatory synapses in a PLXNB2-dependent manner (By similarity). Plays a role in priming antigen-specific T-cells, promotes differentiation of Th1 T-helper cells, and thereby contributes to adaptive immunity (By similarity). Promotes phosphorylation of TIMD2 (By similarity). Inhibits angiogenesis (By similarity). Promotes axon growth cone collapse (By similarity). Inhibits axonal extension by providing local signals to specify territories inaccessible for growing axons (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22956603}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Plexin-D1
- Plexin-B1
- Plexin-B2
- Plexin-B3
- Neuropilin-1
- U4/U6 small nuclear ribonucleoprotein Prp3
- Aryl-hydrocarbon-interacting protein-like 1
- Membrane-associated phosphatidylinositol transfer protein 3
- Ceramide kinase-like protein
- Retinal-specific phospholipid-transporting ATPase ABCA4
Sequence:
MALPALGLDPWSLLGLFLFQLLQLLLPTTTAGGGGQGPMPRVRYYAGDERRALSFFHQKGLQDFDTLLLSGDGNTLYVGAREAILALDIQDPGVPRLKNMIPWPASDRKKSECAFKKKSNETQCFNFIRVLVSYNVTHLYTCGTFAFSPACTFIELQDSYLLPISEDKVMEGKGQSPFDPAHKHTAVLVDGMLYSGTMNNFLGSEPILMRTLGSQPVLKTDNFLRWLHHDASFVAAIPSTQVVYFFFEETASEFDFFERLHTSRVARVCKNDVGGEKLLQKKWTTFLKAQLLCTQPGQLPFNVIRHAVLLPADSPTAPHIYAVFTSQWQVGGTRSSAVCAFSLLDIERVFKGKYKELNKETSRWTTYRGPETNPRPGSCSVGPSSDKALTFMKDHFLMDEQVVGTPLLVKSGVEYTRLAVETAQGLDGHSHLVMYLGTTTGSLHKAVVSGDSSAHLVEEIQLFPDPEPVRNLQLAPTQGAVFVGFSGGVWRVPRANCSVYESCVDCVLARDPHCAWDPESRTCCLLSAPNLNSWKQDMERGNPEWACASGPMSRSLRPQSRPQIIKEVLAVPNSILELPCPHLSALASYYWSHGPAAVPEASSTVYNGSLLLIVQDGVGGLYQCWATENGFSYPVISYWVDSQDQTLALDPELAGIPREHVKVPLTRVSGGAALAAQQSYWPHFVTVTVLFALVLSGALIILVASPLRALRARGKVQGCETLRPGEKAPLSREQHLQSPKECRTSASDVDADNNCLGTEVA
Protein: RNA polymerase II degradation factor 1 (Q5B9A9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSEVQSRSSASRGRVSARGGRGGYSSRGGRGGSRSTKPDVTEPTYEDEGELGQMKKKYSDTLPMLKELFPDWTDEDLVFALEDADGDLEQAIDRISEGNVSQWGEVKKKTTDRSRPKPKEAQSTPTESATTAVRPGRGRGGFEGRGRARGDRGRGGRGGRAGTHANGTRTEKSSLPAEITPIADSATTTTATSSAETAAPETVSTTKDTPAMPEGTKKGWASLFAKPAVPPPQKKPAAPAPAPATAPPPAAPATEEPAPEPQPEEKPAEPDAAPAPAPAPAPVPVAVPLPADRAPQPAVPQPREEPQKATPTSADVSPAKDDLTKNNLAQIPDVSPPVPSATAASTVGSTVEPSAAATSTPARPTASALPTSAFKQNIRTPGTQRRVMEQQEAVVMPGNHAVDRAAVQFGSMGLNGEAADVDIDENREDTETRAQPPQHSPVAPRASLPPSTQAQAPPEAAAVSRPAPGLPPVPQATAAENTFSDFARYDSQKPYDPFTQPLTQPQPQVQEPFANQAPVQPTVTTGSEYSPFYAGDQRLPYNYYNAYGQSQDASLAQRAAGFGVSGAEAQPQIPTTQPPTRYGHVEAPNSGHTTPNPTLPGVTQTPAAHHMPTQGAHAYGYGYPYYSNPHYASYMSQQYGRNRPIYDDARRYEDQYMPHSSQYGYGSQYGPYGKGGMYGQPHGFSYDHSASPATAGSFNQGIPGRDSVYGRTGSAQPSESQQSAAGASAFGTGMTDVFGRSQAGFGQNQPIAQQTPVSSEETKAFDASKTGGPSPSLSQANRPGSATNTPGQSQSQTGLPPLQGQQTQQGFGGYPHLNPQYGGLGGLGGHQTAANQTHHQATGYGNYGGAGFGNYYGNTGRGGWGGNYGH
Protein: Large ribosomal subunit protein eL14B (60S ribosomal protein L14-B) (P38754)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein eL33A
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL21A
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL13A
- Large ribosomal subunit protein eL27A
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL23
Sequence:
MSTDSIVKASNWRLVEVGRVVLIKKGQSAGKLAAIVEIIDQKKVLIDGPKAGVPRQAINLGQVVLTPLTFALPRGARTATVSKKWAAAGVCEKWAASSWAKKIAQRERRAALTDFERFQVMVLRKQKRYTVKKALAKA
Protein: Interleukin-20 (IL-20) (Cytokine Zcyto10) (Q9JKV9)
Organism: Mus musculus (Mouse)
Function: Pro-inflammatory and angiogenic cytokine mainly secreted by monocytes and skin keratinocytes that plays crucial roles in immune responses, regulation of inflammatory responses, hemopoiesis, as well as epidermal cell and keratinocyte differentiation. Enhances tissue remodeling and wound-healing activities and restores the homeostasis of epithelial layers during infection and inflammatory responses to maintain tissue integrity. Affects multiple actin-mediated functions in activated neutrophils leading to inhibition of phagocytosis, granule exocytosis, and migration. Exert its effects via the type I IL-20 receptor complex consisting of IL20RA and IL20RB. Alternatively, can mediate its activity through a second receptor complex called type II IL-20 receptor complex composed of IL22RA1 and IL20RB (By similarity). Acts as an arteriogenic and vascular remodeling factory by activating a range of signaling processes including phosphorylations of JAK2 and STAT5 as well as activation of the serine and threonine kinases AKT and ERK1/2. Alternatively, can activate STAT3 phosphorylation and transcriptional activity in a JAK2, ERK1/2 and p38 MAPK-dependent manner in keratinocytes (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Interleukin-20 receptor subunit alpha
- Interleukin 20 receptor beta
- Interleukin-24
- Interleukin-22 receptor subunit alpha-1
- Interleukin-19
- Interleukin-22
- Interleukin-10 receptor subunit beta
- Interleukin-6 receptor subunit beta
- Interleukin-22 receptor subunit alpha-2
- Cytokine receptor common subunit gamma
Sequence:
MKGFGLAFGLFSAVGFLLWTPLTGLKTLHLGSCVITANLQAIQKEFSEIRDSVQAEDTNIDIRILRTTESLKDIKSLDRCCFLRHLVRFYLDRVFKVYQTPDHHTLRKISSLANSFLIIKKDLSVCHSHMACHCGEEAMEKYNQILSHFIELELQAAVVKALGELGILLRWMEEML
Protein: Angiopoietin-related protein 2 (Angiopoietin-like protein 2) (Q9R045)
Organism: Mus musculus (Mouse)
Function: Induces sprouting in endothelial cells through an autocrine and paracrine action.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MRPLCMTYWWLGLLATVGAATGPEADVEGTEDGSQREYIYLNRYKRAGESPDKCTYTFIVPQQRVTGAICVNSKEPEVHLENRVHKQELELLNNELLKQKRQIETLQQLVEVDGGIVSEVKLLRKESRNMNSRVTQLYMQLLHEIIRKRDNALELSQLENRILNQTADMLQLASKYKDLEHKFQHLAMLAHNQSEVIAQLEEHCQRVPAARPMPQPPPAAPPRVYQPPTYNRIINQISTNEIQSDQNLKVLPPSLPTMPALTSLPSSTDKPSGPWRDCLQALEDGHSTSSIYLVKPENTNRLMQVWCDQRHDPGGWTVIQRRLDGSVNFFRNWETYKQGFGNIDGEYWLGLENIYWLTNQGNYKLLVTMEDWSGRKVFAEYASFRLEPESEYYKLRLGRYHGNAGDSFTWHNGKQFTTLDRDHDVYTGNCAHYQKGGWWYNACAHSNLNGVWYRGGHYRSRYQDGVYWAEFRGGSYSLKKVVMMIRPNPNTFH
Protein: Glucose-induced degradation protein 8-A homolog (Two hybrid-associated protein 1 with RanBPM) (Twa1) (Q6PC55)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Acts as a positive regulator of Wnt signaling pathway by promoting beta-catenin (CTNNB1) nuclear accumulation (By similarity). Required for normal Wnt signaling and normal dorsoventral patterning during embryogenesis.
Interaction partners:
- Armadillo repeat-containing protein 8
- GID complex subunit 4 homolog
- E3 ubiquitin-protein transferase RMND5B
- WD repeat-containing protein 26
- Ran-binding protein 10
- Ran-binding protein 9
- Armadillo repeat containing 6.
- Armadillo repeat-containing 3
- WD repeat domain 26a.
- SPRY domain-containing 3
Sequence:
MSYSEKPEDITKEEWMDKLNNVHIQRADMNRLIMNYLVTEGFKEAAEKFRMESGIEPNVDLDSLDERIKIREMVLKGQIQEAIALINSLHPELLDTNRYLYFHLQQQHLIELIRLRETEAALEFAQSQLAEQGEESRECLTEMERTLALLAFDNPEESPFGDLLNMMQRQKVWSEVNQAVLDYENRESTPKLAKLLKLLLWAQNELDQKKVKYSRMTDLSKGTIEDPK
Protein: Venom prothrombin activator pseutarin-C non-catalytic subunit (PCNS) (vPA) (Venom coagulation factor Va-like protein) [Cleaved into: Pseutarin-C non-catalytic subunit heavy chain; Pseutarin-C non-catalytic subunit light chain] (Q7SZN0)
Organism: Pseudonaja textilis (Eastern brown snake)
Function: Snake prothrombin activator that attacks the hemostatic system of prey. This non-catalytic subunit is functionally similar to blood coagulation factor V. It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X. The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271. Cleavage at Arg-320 produces an active intermediate known as meizothrombin. Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271). Cleavage at Arg-271 releases active thrombin from its pro-fragment. This order of events is reversed if the protease component of prothrombinase is used on its own, suggesting that the 271 site is inherently more accessible to proteolysis. The complex converts prothrombin to thrombin in presence but also in the absence of membrane.
Subcellular location: Secreted {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:12730119}.
Interaction partners:
Sequence:
MGRYSVSPVPKCLLLMFLGWSGLKYYQVNAAQLREYHIAAQLEDWDYNPQPEELSRLSESDLTFKKIVYREYELDFKQEEPRDALSGLLGPTLRGEVGDSLIIYFKNFATQPVSIHPQSAVYNKWSEGSSYSDGTSDVERLDDAVPPGQSFKYVWNITAEIGPKKADPPCLTYAYYSHVNMVRDFNSGLIGALLICKEGSLNANGSQKFFNREYVLMFSVFDESKNWYRKPSLQYTINGFANGTLPDVQACAYDHISWHLIGMSSSPEIFSVHFNGQTLEQNHYKVSTINLVGGASVTADMSVSRTGKWLISSLVAKHLQAGMYGYLNIKDCGNPDTLTRKLSFRELMKIKNWEYFIAAEEITWDYAPEIPSSVDRRYKAQYLDNFSNFIGKKYKKAVFRQYEDGNFTKPTYAIWPKERGILGPVIKAKVRDTVTIVFKNLASRPYSIYVHGVSVSKDAEGAIYPSDPKENITHGKAVEPGQVYTYKWTVLDTDEPTVKDSECITKLYHSAVDMTRDIASGLIGPLLVCKHKALSVKGVQNKADVEQHAVFAVFDENKSWYLEDNIKKYCSNPSAVKKDDPKFYKSNVMYTLNGYASDRTEVLRFHQSEVVQWHLTSVGTVDEIVPVHLSGHTFLSKGKHQDILNLFPMSGESATVTMDNLGTWLLSSWGSCEMSNGMRLRFLDANYDDEDEGNEEEEEDDGDIFADIFIPSEVVKKKEEVPVNFVPDPESDALAKELGLIDDEGNPIIQPRREQTEDDEEQLMKASMLGLRSFKGSVAEEELKHTALALEEDAHASDPRIDSNSARNPDDIAGRYLRTINRGNKRRYYIAAEEVLWDYSPIGKSQVRSRAAKTTFKKAIFRSYLDDTFQTPSTGGEYEKHLGILGPIIRAEVDDVIEIQFKNLASRPYSLHAHGLLYEKSSEGRSYDDKSPELFKKDDAIMPNGTYTYVWQVPPRSGPTDNTEKCKSWAYYSGVNPEKDIHSGLIGPILICQKGMIDKYNRTIDIREFVLFFMVFDEEKSWYFPKSDKSTCEEKLIGVQSLHTFPAINGIPYQLQGLTMYKDENVHWHLLNMGGPKDIHVVNFHGQTFTEEGREDNQLGVLPLLPGTFASIKMKPSKIGTWLLETEVGENQERGMQALFTVIDKDCKLPMGLASGIIQDSQISASGHVGYWEPKLARLNNTGKYNAWSIIKKEHEHPWIQIDLQRQVVITGIQTQGTVQLLQHSYTVEYFVTYSEDGQNWITFKGRHSETQMHFEGNSDGTTVKENHIDPPIIARYIRLHPTKFYNRPTFRIELLGCEVEGCSVPLGMESGAIKNSEITASSYKKTWWSSWEPSLARLNLEGGTNAWQPEVNNKDQWLQIDLQHLTKITSIITQGATSMTTSMYVKTFSIHYTDDNSTWKPYLDVRTSMEKVFTGNINSDGHVKHFFKPPILSRFIRIIPKTWNQYIALRIELFGCEVF
Protein: L-ornithine N(5)-monooxygenase (OMO) (EC 1.14.13.196) (L-ornithine N(5)-oxygenase) (Siderophore biosynthesis protein A) (E9QYP0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: L-ornithine N(5)-monooxygenase; part of the siderophore biosynthetic pathway. Aspergillus fumigatus produces four types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake; and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of three N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA. SidA is highly specific for its substrate, only hydrolyzing l-ornithine, and has preference for NADPH over NADH, NADPH playing a role in stabilization of the C4a-hydroperoxyflavin intermediate. Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split. For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively. The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL. FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation. Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively. Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC. Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence.
Interaction partners:
- N
- bZIP transcription factor hapX
- GATA-type transcription factor sreA
Sequence:
MESVERKSESSYLGMRNMQPEQRLSLDPPRLRSTPQDELHDLLCVGFGPASLAIAIALHDALDPRLNKSASNIHAQPKICFLERQKQFAWHSGMLVPGSKMQISFIKDLATLRDPRSSFTFLNYLHQKGRLIHFTNLSTFLPARLEFEDYMRWCAQQFSDVVAYGEEVVEVIPGKSDPSSSVVDFFTVRSRNVETGEISARRTRKVVIAIGGTAKMPSGLPQDPRIIHSSKYCTTLPALLKDKSKPYNIAVLGSGQSAAEIFHDLQKRYPNSRTTLIMRDSAMRPSDDSPFVNEIFNPERVDKFYSQSAAERQRSLLADKATNYSVVRLELIEEIYNDMYLQRVKNPDETQWQHRILPERKITRVEHHGPQSRMRIHLKSSKPESEGAANDVKETLEVDALMVATGYNRNAHERLLSKVQHLRPTGQDQWKPHRDYRVEMDPSKVSSEAGIWLQGCNERTHGLSDSLLSVLAVRGGEMVQSIFGEQLERAAVQGHQLRAML
Protein: Pre-mRNA processing factor 31 (E7EU94)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLADELLADLEEAAEEEEGGSYGEEEEEPAIEDVQEETQLDLSGDSVKTIAKLWDSKMFAEIMMKIEEYISKQAKASEVMGPVEAAPEYRVIVDANNLTVEIENELNIIHKFIRDKYSKRFPELESLVPNALDYIRTVKELGNSLDKCKNNENLQQILTNATIMVVSVTASTTQGQQLSEEELERLEEACDMALELNASKHRIYEYVESRMSFIAPNLSIIIGASTAAKIMGVAGGLTNLSKMPACNIMLLGAQRKTLS
Protein: RING zinc finger-containing protein (Q86AD8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Cullin-3
Sequence:
MFVDSNGYQFYPQCFICKKLFTHPKTLRCNHSFCSDCLELNSFSRSKQMLYHCRICGDKTSSHEAWNNEQLTRYANEFKNYQLNGSIGGIVVNVNGNGHYNNNNNNNNNNININKNNNGGINNNINNNNNGIINGNGSGNGNGNGNGNGSSGGNTAPIGSPNMNGMKPPPPLLNSLNGITNLSNLNLGNINNNNNPSSPRGNAGGTVHQSPLLHHTSPSPIGSPAPSPYLLSSQLSPRSALPPQNGSGQFSPRIHPSSNSGGGGSSQFSPLMVPPLPLNPLSSPSMMQLLTDDETTSVSTLNKYNNNINNNSNHHQHLNHHQPQQPQPQVQPQSQPQPQPQSTFQTQSPIQPPPPIQQYYSKNNNNEQHPSFSNHSPNIFGGFSPLVNGPTNVYNVNVQQSPHIRPTNSSTSSSVPSSPVIMGSNNFNHINNNNNNNINSNNNNNNNNNENINNNHNQFLYSCNNNNNNNTNNINNNNNNNNNNNNIGSNNNNNNNNINNSHHIYKSNSNNNIFINNNSLINNSNNSNNNNITNNNNLIISQTYINDNIFFITNNECLLHNSEIQYYCFECCSGVCAKCIYIDNQHYGHALKSLNDILNETKQDYKATKQYLNQVRNKLHIQREISEQAIQCQPDLNTQKQKIKMKINTITQQLLNQVDQDFNEFKNSLEIKRNLINQLLSDIEFEHKQNKKNEQKQIQQNKRGHYSNNIIINSNNNSNNHQQQIINDQMEYLELGNSNPTSPALHSSSSSSSITSTSSSTSSSTSSISSSSSSSSSSKTSSPNSKGLIQQINSLMNKKKPLLQSIQNSIQVSNIERSSTWCLDLVENKLNLSSSSSSSSSQQQQQQQQQQQQQQQQQQQQQQQQQQQNKNNNNNNISAPNSPIQNKLIESNNEEIINIINSTSLNLIRKSNLTIKFTIRFIYAIGGQLKQSVECYSIQQNKWNYVSPMNFHRNRISAVFDGKQYIYVFGGECPGGFEKSVERYCIHDNKWVMGKEMPRERSRHATVFDGQRYIYIVGGKDQTWFSNQIDRFDILTQEYQSLKKMKVPRSDLSAIYDPRNGGSIYAIGGFNGKALDIIEQYDIQSDKWVKVGKMRKQRDGPGAVYDGNNHIYVMGGSFGGRKISNNLERMNIETWEWESLSDMKKPIDVRNSAIFDGTGNIYVIGGYFSEVLAENQCYNIEKNEWNYLEPMIEPREGNALTYVEFQV
Protein: Signal peptide peptidase-like 3 (SPP-like 3) (EC 3.4.23.-) (Intramembrane protease 2) (IMP-2) (Presenilin-like protein 4) (Q9CUS9)
Organism: Mus musculus (Mouse)
Function: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane protein substrates in or close to their luminal transmembrane domain boundaries. Acts like a sheddase by mediating the proteolytic release and secretion of active site-containing ectodomains of glycan-modifiying glycosidase and glycosyltransferase enzymes such as MGAT5, B4GAT1 and B4GALT1. Plays a role in the regulation of cellular glycosylation processes. Required to link T-cell antigen receptor (TCR) and calcineurin-NFAT signaling cascades in lymphocytes by promoting the association of STIM1 and ORAI1 during store-operated calcium entry (SOCE) in a protease-independent manner.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8TCT6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT6}. Golgi apparatus {ECO:0000250|UniProtKB:Q8TCT6}. Membrane {ECO:0000250|UniProtKB:Q8TCT6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TCT6}; Lumenal side {ECO:0000250|UniProtKB:Q8TCT6}.
Interaction partners:
Sequence:
MAEQTYSWAYSLVDSSQVSTFLISILLIVYGSFRSLNMDFENQDKEKDSNSSSGSFNGNSTNNSIQTIDSTQALFLPIGASVSLLVMFFFFDSVQVVFTICTAVLATIAFAFLLLPMCQYLTRPCSPQNKISFGCCGRFTAAELLSFSLSVMLVLIWVLTGHWLLMDALAMGLCVAMIAFVRLPSLKVSCLLLSGLLIYDVFWVFFSAYIFNSNVMVKVATQPADNPLDVLSRKLHLGPNVGRDVPRLSLPGKLVFPSSTGSHFSMLGIGDIVMPGLLLCFVLRYDNYKKQASGDSCGAPGPANISGRMQKVSYFHCTLIGYFVGLLTATVASRIHRAAQPALLYLVPFTLLPLLTMAYLKGDLRRMWSEPFHSKSSSSRFLEV