wanglab/gogpt-training-data huggingface dataset:
Protein: Nezukol synthase KSL3 (EC 4.2.3.183) (Kaurene synthase 3) (IrKSL3) (Miltiradiene synthase KSL3) (EC 4.2.3.131) (Terpene synthase 2) (IrTPS2) (A0A1X9ISH5)
Organism: Isodon rubescens (Rabdosia rubescens)
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities. Catalyzes the conversion of (+)-copalyl diphosphate ((+)-CPP) to nezukol and miltiradiene. The reaction mechanism proceeds via the ionization of the diphosphate group of (+)-CPP, followed by formation of an intermediary pimar-15-en-8-yl(+) carbocation and neutralization of the carbocation by water capture at C-8 to yield nezukol. Can interact with ent-copalyl diphosphate (ent-CPP) but seems unable to use it as substrate.
Interaction partners:
Sequence:
MSTLKLIPFSTSIDKQFSGRTSILGGKCCLQIDGPKTTKKQSKILVEKIRERISNGKVVEISASAYDTAWVAMVPSREMSGRPSFPECLDWIVENQNPDGSWGLNPFLVKDSLSCTLACLLALRKWGLPNHLLHKGIEFIESNISRAATDDENQVAPIGFNIIFPAMISYAKELDLTLTLPPSSLNALLRARDSEMIRREGKWEYVGEGLGDSCNWNQIIQKHQSRNGSLFNSPATTAAAAIHCRDHKCFDYLISVVNKCNGWAPTVYPMDIYARLCMIDTLQRLGIDCHFRVELDAIFDEIYRNWQEREEEIFSDVTCQALAFRLLRVKGYDVSSDGLEEFVEQEGFFNSVSMQHSNVGTVLELYRASQTRINEEENTLQKIHAWTKPFLTQQLLNKTIRHKPLQMQVEYDLKNFYGTVDRFQHRRTIDLYDAQASQILKTAYRCSAIHNEDFIRFSVQNFKICRAEYQKELDEINKWYAYFGMDLLSKGRNACEQAYVVTAGLIADVELSMARISFAQVILLITVFDDVFDRYGTREEALAVIHLIKEILTHYRWKAAPKECSQLVKTTFTALYDTVNETAAKAHALQGFCFKQQIISLWEELLECAVREKESLSGKNVSTLDEYLSFAPVTIGCELCVLTAVHFLGIQVSEEMLTSAEMLTLCWHGNVVCRLLNDLKTYSREREEKTVNSVSVQVGVSEEEAVAKVKEVLEYHRRKVVEMVYQSQGSNVPRECKELVWKTCKVAHCFYGYDGDEFSSPRDIVDDIKAMMFLGLPHLSTH
Protein: Phospholipid phosphatase 1 (EC 3.1.3.-) (EC 3.1.3.106) (EC 3.1.3.4) (EC 3.6.1.75) (Lipid phosphate phosphohydrolase 1) (PAP2-alpha) (Phosphatidate phosphohydrolase type 2a) (Phosphatidic acid phosphatase 2a) (PAP-2a) (PAP2a) (P60588)
Organism: Sus scrofa (Pig)
Function: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (By similarity). Through its extracellular phosphatase activity allows both the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (By similarity). It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P (By similarity). Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes (By similarity). May also have an intracellular activity to regulate phospholipid-mediated signaling pathways (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:8702556}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:Q61469}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lipin 2.
- Lipin 1.
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- 3-ketodihydrosphingosine reductase
- O-acyltransferase
- Acyltransferase
- Sphingomyelin phosphodiesterase 4 isoform 2.
- Phospholipase
- Phospholipase
- Sphingosine-1-phosphate phosphatase 2
Sequence:
MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGLFCNDESIKYPYKEDTIPYPLLGGIIIPFSIIVMIVGETLSVYFNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAKYSIGRLRPHFLDVCDPDWSKINCSDGYIENYICRGNAQKVKEGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAIVVAVYVSDFFKERNSPFKERKEEDSHTTLHETPTTGNHYRNSHQP
Protein: Junctional adhesion molecule A (JAM-A) (Junctional adhesion molecule 1) (JAM-1) (Platelet F11 receptor) (Platelet adhesion molecule 1) (PAM-1) (CD antigen CD321) (Q9Y624)
Organism: Homo sapiens (Human)
Function: Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity). Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (By similarity). Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration. Involved in platelet activation.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:11171323}. Cell membrane {ECO:0000269|PubMed:11171323}; Single-pass type I membrane protein {ECO:0000269|PubMed:11171323}. Note=Localized at tight junctions of both epithelial and endothelial cells. {ECO:0000269|PubMed:11171323}.
Interaction partners:
- Tight junction protein 1
- Integrin beta-2
- Occludin
- Afadin
- Tight junction protein 2
- Integrin alpha-L
- Cingulin
- Claudin-1
- Partitioning defective 3 homolog
- Claudin-7
Sequence:
MGTKAQVERKLLCLFILAILLCSLALGSVTVHSSEPEVRIPENNPVKLSCAYSGFSSPRVEWKFDQGDTTRLVCYNNKITASYEDRVTFLPTGITFKSVTREDTGTYTCMVSEEGGNSYGEVKVKLIVLVPPSKPTVNIPSSATIGNRAVLTCSEQDGSPPSEYTWFKDGIVMPTNPKSTRAFSNSSYVLNPTTGELVFDPLSASDTGEYSCEARNGYGTPMTSNAVRMEAVERNVGVIVAAVLVTLILLGILVFGIWFAYSRGHFDRTKKGTSSKKVIYSQPSARSEGEFKQTSSFLV
Protein: Lysophospholipid acyltransferase LPEAT2 (EC 2.3.1.23) (EC 2.3.1.n6) (EC 2.3.1.n7) (Lysophosphatidylethanolamine acyltransferase 2) (AtLPEAT2) (Q8S8S2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates. Exhibits strong acylation activity on lysophosphatidylethanolamine (LPE), and lower activity on lysophosphatidylcholine (LPC) and lysophosphatidylserine (LPS). Exhibits acylation activity on both LPE and LPC. Has a preference for 18:1-LPE over 16:0-LPE as acceptor. Palmitoyl-CoA (16:0-CoA) is a better acyl donor than oleoyl-CoA (18:1-CoA). Among several different acyl-CoA species the best acyl donor is eicosanoyl-CoA (20:0-CoA). Activity is calcium-independent. Its activity is essential for maintaining adequate levels of phosphatidylethanolamine (PE), LPE and LPC in the cells, which is crucial for plant growth regulation.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:33809440}; Single-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:33809440}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lysophospholipid acyltransferase 2
- Lysophospholipid acyltransferase 1
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4
- Lysophospholipid acyltransferase LPEAT1
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- Cardiolipin synthase
- S-protein homolog 13
- Phospholipase A2-alpha
- Lecithin-cholesterol acyltransferase-like 4
Sequence:
MADPDLSSPLIHHQSSDQPEVVISIADDDDDESGLNLLPAVVDPRVSRGFEFDHLNPYGFLSESEPPVLGPTTVDPFRNNTPGVSGLYEAIKLVICLPIALIRLVLFAASLAVGYLATKLALAGWKDKENPMPLWRCRIMWITRICTRCILFSFGYQWIRRKGKPARREIAPIVVSNHVSYIEPIFYFYELSPTIVASESHDSLPFVGTIIRAMQVIYVNRFSQTSRKNAVHEIKRKASCDRFPRLLLFPEGTTTNGKVLISFQLGAFIPGYPIQPVVVRYPHVHFDQSWGNISLLTLMFRMFTQFHNFMEVEYLPVIYPSEKQKQNAVRLSQKTSHAIATSLNVVQTSHSFADLMLLNKATELKLENPSNYMVEMARVESLFHVSSLEATRFLDTFVSMIPDSSGRVRLHDFLRGLKLKPCPLSKRIFEFIDVEKVGSITFKQFLFASGHVLTQPLFKQTCELAFSHCDADGDGYITIQELGEALKNTIPNLNKDEIRGMYHLLDDDQDQRISQNDLLSCLRRNPLLIAIFAPDLAPT
Protein: SSD domain-containing protein (Q18129)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- WaRThog
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- GRounDhog
- Warthog protein 1
Sequence:
MSWFDDKIHKVFFRVGENVHKFRLYFLLLSFAILTFSAFGFLWFTEQTTNDPQYVFSPANAPWRYERAVLTEHWPLDEEKFWPGKSYDLHGYVDVIASGRIHPDYGRPNILNIRYLDEVARINDYIIHNLTVPVDINGKHYDIAYTDLCMRYDWACYLNDHITMLMPKTRWGNFSGPFAELASDIINTQVNITYPIGWRGTEPIYFGALVGAPNLVDEEGHFDYASAIRLTYNTREGKVDQYGIEWRRKLSMWLTDKENPVSELLEFGVNHNMTLPEGLQDVADTLAPKFVGTCAILFTFSFLVSVVLRKHRTGQVMPDWVRSKPLVAAAGLMTPIMATVTSFGLILWCGFLYNAIVNVSPFLILCIGIDDLFIMCAEWHRTNPQHSPEKRIGKTLSEAAVAISITSLTDIATFAMGCYTTLPGVQMFCMYTCVQCFFCYVYQIIFLGPVLAYAAEMEQNGQHVLLIRKAVDPDKTESPVKLWLLSGSVNRQDQEARRRNSRKVAPVEKEGEKKSKFGEVVEKLEHTLEKHDDDPGHNSEETLVSKVFREIIGPFILQKSTQVCALLLYLVYISLAIGGCLNIKEGLDPKLLVRESFYLSKFYEIIDETFWREGLQMQVVVNNPPDLFTPETRKGFDEMMAEFENTQYTMHPNATMIWLRAYEHHLETEVHELNIEKPNSTVEWYTRCRDWLIVAGGRRLWQMDMVWANTTFEETPRITAFRFQLGLRNYRTPTDHTHSCKLMRSIADKYSMFNVTTFHEYYPFADQYLELTPSLFQNMISDLCTIFAVSWVMIPELICAVAIVLSIASINVGVLGFMSFWGVNLDSVSIITVIMCIGFSVDLSAHIAYAFSQSYGNSHARAVAALETLGWPVFLGASSTVLGILLLTLVDSYIVQIFFKTVFLVINFSILHGLIFLPIFLMKVVREVKEESPRDDQSVENEKPKIQIEMESQVAA
Protein: Uncharacterized protein (Q3V4B9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
GHLSPTTTPGEQGFHSHAPLQLLTQNRGHNPRESGGLAVPRLEDCTQVPAVNQHFRKLDQNDSSFLQHWDEWFGSMLAEWMPDKEYWSEKAELHPWQVQLRQLASVSPQAHQTP
Protein: Low-density lipoprotein receptor (LDL receptor) (P35952)
Organism: Rattus norvegicus (Rat)
Function: Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P01130}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P01130}. Golgi apparatus {ECO:0000250|UniProtKB:P01130}. Early endosome {ECO:0000250|UniProtKB:P01130}. Late endosome {ECO:0000250|UniProtKB:P01130}. Lysosome {ECO:0000250|UniProtKB:P01130}. Note=Rapidly endocytosed upon ligand binding. {ECO:0000250|UniProtKB:P01130}.
Interaction partners:
- Low density lipoprotein receptor adapter protein 1
- Proprotein convertase subtilisin/kexin type 9
- E3 ubiquitin-protein ligase MYLIP
- Apolipoprotein B-100
- Disabled homolog 2
- Clusterin
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Transmembrane protease serine 3
Sequence:
MSTADLMLRWAIALLLAAAGVAAEDSCGKNEFQCRDGKCIVSKWVCDGSRECPDGSDESPETCMSVTCRSGEFSCGGRVSRCIPDSWRCDGRTDCENGSDELDCSPKTCSLDEFRCQDGKCISRQFVCDQDWDCLDGSDEAHCAATTCGPAHFRCNSSSCIPSLWACDGDRDCDDGSDEWPQNCGAEDTAAEVVSSPCSSLEFHCGSSECIHRSWVCDGAADCKDKSDEENCAVTTCRPDEFQCADGSCIHGSRQCDREHDCKDMSDELGCINVTQCDGPNKFKCHSGECISLDKVCNSARDCRDWSDEPIKECKTNECLDNNGGCSHICKDLKIGYECLCPSGFRLVDGHQCEDIDECQEPDTCSQLCVNLEGSFKCECRAGFHMDPHTRVCKAVGSIGFLLFTNRHEVRKMTLDRSEYTSLIPNLKNVVALDTEVANNRIYWSDLSQRKIYSAVMDQGTSLSYDAIISGDLHAPDGLAVDWIHGNIYWTDSVPGTVSVADTKGVRRRTLFREKGSRPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTEDIQWPNGITLDLPSGRLYWVDSKLHSISSIDVNGGGRKTILEDEKQLAHPFSLAIYEDKVYWTDVLNEAIFSANRLTGSDVNLVAKNLMSPEDIVLFHNVTQPRGVNWCEATVLPNGGCQYMCLPAPQISAHSPKFTCACPDGMLLAKDMRSCLPEVDTVPTTQGTSTIGPVVTTSAAVSLKRKEDPSATRHKEDPSATRHNEDPSATSTSRQPGDTPELSTVESVTVSSQVQGDMAGRGDEVQRHGVGFLSIFLPIALVALLVFGAILLWRNWRLRNINSINFDNPVYQKTTEDEIHICRSQDGYTYPSRQMVSLEDDVA
Protein: Melanotransferrin (Melanoma-associated antigen p97) (CD antigen CD228) (P08582)
Organism: Homo sapiens (Human)
Function: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc.
Subcellular location: [Isoform 1]: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Plasminogen
- Transferrin receptor protein 1
Sequence:
MRGPSGALWLLLALRTVLGGMEVRWCATSDPEQHKCGNMSEAFREAGIQPSLLCVRGTSADHCVQLIAAQEADAITLDGGAIYEAGKEHGLKPVVGEVYDQEVGTSYYAVAVVRRSSHVTIDTLKGVKSCHTGINRTVGWNVPVGYLVESGRLSVMGCDVLKAVSDYFGGSCVPGAGETSYSESLCRLCRGDSSGEGVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGKTLPSWGQALLSQDFELLCRDGSRADVTEWRQCHLARVPAHAVVVRADTDGGLIFRLLNEGQRLFSHEGSSFQMFSSEAYGQKDLLFKDSTSELVPIATQTYEAWLGHEYLHAMKGLLCDPNRLPPYLRWCVLSTPEIQKCGDMAVAFRRQRLKPEIQCVSAKSPQHCMERIQAEQVDAVTLSGEDIYTAGKTYGLVPAAGEHYAPEDSSNSYYVVAVVRRDSSHAFTLDELRGKRSCHAGFGSPAGWDVPVGALIQRGFIRPKDCDVLTAVSEFFNASCVPVNNPKNYPSSLCALCVGDEQGRNKCVGNSQERYYGYRGAFRCLVENAGDVAFVRHTTVFDNTNGHNSEPWAAELRSEDYELLCPNGARAEVSQFAACNLAQIPPHAVMVRPDTNIFTVYGLLDKAQDLFGDDHNKNGFKMFDSSNYHGQDLLFKDATVRAVPVGEKTTYRGWLGLDYVAALEGMSSQQCSGAAAPAPGAPLLPLLLPALAARLLPPAL
Protein: Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial (MMSDH) (EC 1.2.1.27) (Aldehyde dehydrogenase family 6 member A1) (Malonate-semialdehyde dehydrogenase [acylating]) (Q9EQ20)
Organism: Mus musculus (Mouse)
Function: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q02253}.
Interaction partners:
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- 4-aminobutyrate aminotransferase, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Peroxisomal bifunctional enzyme
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
Sequence:
MAAAVAAAAAMRSRILQVSSKVNATWYPASSFSSSSVPTVKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSSPAVVMPTMGR
Protein: Rho-related GTP-binding protein RhoJ (Tc10-like GTP-binding protein) (Q9ER71)
Organism: Mus musculus (Mouse)
Function: Plasma membrane-associated small GTPase specifically involved in angiogenesis (By similarity). Required for endothelial cell migration during vascular development via its interaction with GLUL (By similarity). Elicits the formation of F-actin-rich structures, thereby regulating endothelial cell migration.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9H4E5}; Lipid-anchor {ECO:0000250|UniProtKB:Q9H4E5}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H4E5}. Note=Localization to the plasma membrane is regulated by GLUL. {ECO:0000250|UniProtKB:Q9H4E5}.
Interaction partners:
- Intersectin-1
- Intersectin-2
- Dedicator of cytokinesis protein 8
Sequence:
MSCRERTDSSCGCNGHEENRILKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVTVTVGGKQHLLGLYDTAGQEDYNQLRPLSYPNTDVFLICFSVVNPASYHNVQEEWVPELKDCMPHVPYVLIGTQIDLRDDPKTLARLLYMKEKPLTYEHGVKLAKAIGAQCYLECSALTQKGLKAVFDEAILTIFHPKKKKKGCLGCHGCCAII
Protein: Dynein light chain (Q7SZP6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU365010}.
Interaction partners:
Sequence:
GHPQKTTKATDFASQIYLAKILLTDNMTDRKAVIKNADMSEDMQQDAVDCATQAMEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
Protein: Homeobox protein OTX2-A (xOTX2-A) (Orthodenticle 2-A) (Orthodenticle-A-like protein A) (Q91813)
Organism: Xenopus laevis (African clawed frog)
Function: May play a central role in the initial events of axis formation and in particular in specifying anterior head regions and their spatial relationship with trunk structures. Activates the head organizer gene cer1 by acting synergistically with siamois and mix-A/mix.1 through the 5'-TAATCT-3' element of the cer1 promoter. Also binds as a complex with lhx1/lim1 and ldb1 to the gsc promoter to stimulate expression.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MMSYLKQPPYAVNGLSLTASGMDLLHQSVGYPATPRKQRRERTTFTRAQLDILEALFAKTRYPDIFMREEVALKINLPESRVQVWFKNRRAKCRQQQQQQQNGGQNKVRPSKKKTSPVREVSSESGTSGQFSPPSSTSVPVISSSTAPVSIWSPASVSPLSDPLSTSSSCMQRSYPMTYTQASGYSQGYAGSTSYFGGMDCGSYLSPMHHQLSGPGATLSPMGTNAVTSHLNQSPVALSSQAYGASSLGFNSTDCLDYKDQTASWKLNFNADCLDYKDQTSSWKFQVL
Protein: Frazzled, isoform C (A0A0B4LEX6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAITTNRSSRTLWNWLLSSCLIFQLIGSSLASQALSFTLEPQDAVVPEGHSVLLQCAGTASIGRGGKSKSNLPSSVSIRWRGPDGQDLVIVGDTFRTQLKNGSLYISSVEENRGLTGAYQCLLTAEGVGSILSRPALVAIVRQPDLNQDFLETYLLPGQTAYFRCMLGEANWQEGVKHSVQWLKDDLPLPLDKLRMVVLPNGALEIDEVGPSDRGSYQCNVTSGSSSRLSSKTNLNIKKPSDPGAENSVAPSFLVGPSPKTVREGDTVTLDCVANGVPKPQIKWLRNGMDLDFNDLDSRFSIVGTGSLQISSAEDIDSGNYQCRASNTVDSLDAQATVQVQEPPKFIKAPKDTTAHEKDEPELKCDIWGKPKPVIRWLKNGDLITPNDYMQLVDGHNLKILGLLNSDAGMFQCVGTNAAGSVHAAARLRVVPQGGHSTKSLQTFDNLTKRRKPFNSGEQLRTKSGGSFPFPDEDDDLDDNDSGTTRLRIPSGKLPKFEQPLNDRRFNILNAGSALPLDNQSKSYEDDDDDYDEDDPAKEALLEAYKQGEDAHKILDSWQQSKSKKSQQQKQSPASPDSPEQDPSVPHPGGKPLDSGLQARLPSQPRDLVAQIVKSRFVTLSWVEPLQNAGDVVYYTVYYKMNNSEREQKMVTKSHDDQQVNIQSLLPGRTYQFRVEANTNFGSGASSAPLEVSTQPEVNIAGPPRNFEGYARSHKEIYVKWEEPTVTNGEILKYRVYYSENDSGADLYHDSTALEAVLTELRPHTDYVISVVPFNRNGMGDSSAEIRVKTFSSTPSEPPNNVTLEVTSSSSITVHWEPPAEEDRNGQITGYKIRYRKFKDAPQVKSTPANIRYFELSNLDRNAEYQVKIAAMTVNGSGPFTEWNRANTLENDLDETQVPGKPIWISIHPGANNIALHWGPPQHPEIKIRNYVLGWGRGIPDENTIELKETERYHILKNLESNMDYVVSLRARNVKGDGPPIYDNIKTRDEEPVDAPTPLEVPVGLRAITMSSSSIVVYWIDTMLNKNQHVTDNRHYTVSYGITGSNRYRYHNTTDLNCMINDLRPNTQYEFAVKVVKGRRESSWSMSVLNSTYQNVPVTPPREVTVRLDEMNPPTVIVQWIPPKHTLGQITGYNIYYTTDTTKRDRDWSVEAFAGEETMLMLPNLKPYTTYYFKVQARTTKGANNAPFSALVSYTTSAAVTMQEPDTIAKGIDNEKLLYIIIAATAVVLLVVLLGVLLLCRRKPQSSPEHTKKSYQKNNVGVPKPPDLWIHHDQMELKNIDKGLHTVTPVCSDGASSSGALTLPRSVVHSEYEVETPVPGHVTNSLDKRSYVPGYMTTSMNGTMERPQYPRTQYSHQNRSHMTMEAGLSQQSLTQPQSNSMAQTPEHPYGGYDANFCNAGNAAAGNGCVSTIESSKRGHPLKSFSVPGPPPTGGATPVTKHTPAVTIRPQNQSPYKKPSFSAATPNRLQGGGSVVHSTDEIQRLAPSTSTEELNQEMANLEGLMKDLSAITANEFEC
Protein: Chitinase-like protein (EC 3.2.1.14) (Q6JX03)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- COBRA-like protein
- COBRA-like protein
Sequence:
MEAKWLVLFSVAAMLVALANCQESLKPLVKMVKGKKLCDKGWECKGWSKYCCNHTISDYFQTYQFEDLFAKRNTPVAHAVGFWDYHSFITAAAQYQPHGFGTTGEKLQNMKEVAAFLGHVGSKTSCGYGVATGGPLAWGLCYNKEMSPSKIYCDDYYKYTYPCTPGVSYHGRGALPIYWNYNYGETGEALKVDLLNHPEYLEDNATLAFQTAMWRWMTPMKKHQPSAHDVFVGNWKPTKNDTLAKRVPGFGTTMNVLYGDQVCGQGDSDSMNNMISHYLYYLDLLGVGREEAGPHDMLTCEEQEPFTVSPSSATSS
Protein: Zinc finger protein zas1 (Q9UTS5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Brix domain-containing protein C1B9.03c
- Protein yippee-like PJ691.02
Sequence:
MSNEESFTEKPLKKRSRAHRLGDPRFYCTYPDCPKSFTRKEHLRRHERTHENVKAFSCSFCNRAFARSDVLNRHVQQMHLQKQNLSERRMLNASCFLGFCVLAHDYVNLINARHFMIEHFLSLFAFCRTILFSLLTSFLLVPPPQFFHSEAGERPTPSVGAPSSLASSMDSVRVAPSMLAASHQIVPQYSENNPRVSNEPPRVTIENASLKPFSGYIKSHMSTSNFLNGEPDLNVNVDLSPFPNLPATVPITQAASTANAFQQPSNQFQTQKLPSGLDTRPVSSYPDELTQLESNPDSFSRLDLQGDCTCIFKNRSSIASSRTMDDVVRWLFSSGKRRQKYESSYPYQTQSNQIPSQDQYSDTDSNFLSYYFSASGPMYVPQKCPATVYNNLLNFLEGSFHLQPNFLAMFTLESVSSWLNAYWSMFHVRWPILHRGTFQITQAPLDLLLSMITLGMHSSNDLSIRSLAVEIHTTLRYNIYQKQEFGPPVSLWVYQALFLIQVFELFTSNLKQHRLAQMFHPVLIEAMRQAIPSDALTVRSETFGESNTPLTLQQWHKWITRESVKRIAFFVFALDSTSTLVFGNQPLLYVTDVSMPLLAEEHHWEAENFEVWAAQKPTIEPPTILHMLKAFVQCEQCESPLPKLSPWNMLLLLHGLLSVDISLKQKKFVPGMKLSKREIDGWCSLVFEAYQKWNRCYYSIFLNNNILPFGHPFVKECRSLYNLACIYSKTRLTYLQAFAKAVTDPVDGSVTSKTVAPLRYVKIWANTENARYSTSNALEILDMLLREKIESAPRYDTLIYHSWCYYVAALVLWSIGFALDEENKKTEEVTNLHSQMSRYVTKVRQALEQGEPLFAVVEKSKNPIILHVVLQALDVFPWDLLGEHKKIIQQLLSKGND
Protein: Ranatuerin-2PL (Palustrin-2b) (P84279)
Organism: Lithobates palustris (Pickerel frog) (Rana palustris)
Function: Antimicrobial activity against Gram-negative bacterium E.coli.
Subcellular location: Secreted {ECO:0000269|PubMed:11087945}.
Interaction partners:
Sequence:
GFFSTVKNLATNVAGTVIDTLKCKVTGGCRS
Protein: Alpha-defensin 24 (Defensin-related cryptdin-24) (Q5G865)
Organism: Mus musculus (Mouse)
Function: May have microbicidal activities.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Alpha-defensin 3
- Alpha-defensin 26
- Defensin, alpha, 22
- Defensin, alpha, 5
- Alpha-defensin 21
Sequence:
MKTLILLSALVLLAFQVQADPIQNTDEETKTEEQPGEEDQAVSVSFGDPEGASLQEESLRDLVCYCRARGCKGRERMNGTCSKGHLLYMLCCR
Protein: Basic phospholipase A2 BmjeTX-II (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (P86804)
Organism: Bothrops marajoensis (Marajo lancehead)
Function: Snake venom phospholipase A2 (PLA2) that induces blockade of neuromuscular contraction in an indirectly stimulated chick biventer cervicis nerve-muscle preparation. Does not inhibit contraction of chick biventer cervicic nerve-muscle preparation in response to treatment with acetylcholine or KCl. The neuromuscular blockade is mediated by inhibitory action at the presynaptic motor nerve endings. Lyses skeletal myoblasts and myotubes in vitro, and intramuscular injection causes local muscle necrosis. Induces edema in the mouse foot pad. Induces a transient increase of IL-6 levels. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|PubMed:20195718}.
Interaction partners:
Sequence:
DLWQWGQMILKETGKIPFSYYGAYGCYCGWGGRGGKPKAGTDRCCYVHDCCYGKLTSCPKTDDRYSYSRLDLTIVCGEDDPCKELCECDKKIAVCFRENLGTYNKKYRYHLKSCKKADKPC
Protein: Rho GTPase-activating protein 3 (Rho-type GTPase-activating protein 3) (Q8GYY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Involved in secondary wall pattern formation. In association with ROPGEF4, mediates local activation of ARAC10/ROP11 to initiate the distinct pattern of secondary cell walls in xylem cells.
Subcellular location: Cell membrane {ECO:0000305|PubMed:22984069}; Peripheral membrane protein {ECO:0000305|PubMed:22984069}. Note=Localized at plasma membrane in the secondary wall pits.
Interaction partners:
- Rac-like GTP-binding protein ARAC10
- Rop guanine nucleotide exchange factor 4
- Interactor of constitutive active ROPs 5
- Kinesin-like protein KIN-13A
- Rho GTPase-activating protein 6
- Protein IQ-DOMAIN 13
- Protein ACTIVITY OF BC1 COMPLEX KINASE 1, chloroplastic
- Outer membrane OMP85 family protein
- Interactor of constitutive active ROPs 1
- Rop guanine nucleotide exchange factor 1
Sequence:
MTNFSRSKSTGTIGFPEFKPTRPGPDKYENIHNDDDEYEEGHSTTSTDYYDASTPLSSHASRSGNGSGSGQLTVVDLLAAVLRKSLVMSCAMERGEDDVVASMDIGWPTEVKHVSHVTFDRFNGFLGLPSELEPEVPPRAPSASVSVFGVSAKSMQCSYDDRGNSVPTILLRMQKRLYTEGGLKAEGIFRINPDNGKEEHVRRQLNCGVVPRGIDVHCLAGLIKAWFRELPTGVLDVLTPEQVMRCNTEEDCSRLVILLPPVESAILDWAIGLMADVVEHEQFNKMNARNVAMVFAPNMTQMADPLTALIHAVQVMNFLKTLILMNLKERENADAKARWLKKQTSDPSEEWESQHSEILSPEKPNNNNPKFLRVATLCRLEADNEEEFWNIKKRNDHEGVLDTSSGNGNIGPVQRLCKHPLFQLSKSTKKAFVSNRDEGRKGREAWSSRLSSLPW
Protein: J-type co-chaperone jac1, mitochondrial (J-type accessory chaperone 1) (Q9UTL6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Co-chaperone required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria. Stimulates the ATPase activity of the mitochondrial Hsp70 chaperone ssc1, to mediate the transfer of iron-sulfur clusters from isu1 to grx5.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Iron sulfur cluster assembly protein 1, mitochondrial
- Frataxin homolog, mitochondrial
- Protein isd11
- Probable cysteine desulfurase, mitochondrial
- Meiotic drive suppressor wtf16
- DnaJ homolog 1
- Mitochondrial import inner membrane translocase subunit tim14
- Iron-sulfur cluster biogenesis chaperone, mitochondrial
- Monothiol glutaredoxin-5
- Iron-sulfur assembly protein 2
Sequence:
MLKQAGNQSFRPFISFAQKSLFNRQITGNHWIFARFKFYPLNKIVNYNHFHSSSCQSEAKNFYKQFEGDISDPPPKGPFDIDLGALKSSYLRKMKTLHPDVAQGKDAALAQRDSAELSKAYNTLKAPLTRAEYILQLQGINPVSEDISNSDPEFLMEIMDVHENISASRDSPEKLLQLSQENQGRKVQEINEIRKAMESSNWDSALLYVNRLRYWNTIDKILHDL