lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Part of the ABC transporter complex FhuCBGD involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Partially required for the transport of desferrioxamine.
Subcellular Localization:
Cell membrane; Lipid-anchor. Membrane raft; Peripheral membrane protein. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion.
Sequence:
MKKNILLVGMLVLLLMFVSACSGTASKGSSSDSASEKTEMRTYKSPKGNVNIPAHPKRIVTDFYAGELLSVGANVVGSGSWSFDNPFLKSKLKNVKDVGDPISVEKVMELQPDLIVVMNEENVDKLKKIAPTVVIPYNTAKNVEDTVSMFGDIAGAKDQAKSFMADFNKKAEAAKKKIAGVIDKDATFGIYENTDKGEFWVFNDNGGRGGQAVYNALGLKAPEKIEQDVIKKGEMKQLSQEVIPEYAADYMFITDYNPKGESKTLDKLENSSIWKNLDAVKHNRVFINDFDSFYPYDPISVSKQVDIITDMLIKRAEENKK
The following text describes a protein:
Function:
Transcriptional activator involved in jasmonate (JA) signaling pathway during spikelet development. Binds to the G2 region G-box (5'-CACGTG-3') of the MADS1 promoter and thus directly regulates the expression of MADS1. Its function in MADS1 activation is abolished by TIFY3/JAZ1 which directly target MYC2 during spikelet development.
Subcellular Localization:
Nucleus.
Sequence:
MNLWTDDNASMMEAFMASADLPAFPWGAASTPPPPPPPPHHHHQQQQQQVLPPPAAAPAAAAFNQDTLQQRLQSIIEGSRETWTYAIFWQSSIDVSTGASLLGWGDGYYKGCDDDKRKQRSSTPAAAAEQEHRKRVLRELNSLIAGAGAAPDEAVEEEVTDTEWFFLVSMTQSFPNGLGLPGQALFAAQPTWIATGLSSAPCDRARQAYTFGLRTMVCLPLATGVLELGSTDVIFQTGDSIPRIRALFNLSAAAASSWPPHPDAASADPSVLWLADAPPMDMKDSISAADISVSKPPPPPPHQIQHFENGSTSTLTENPSPSVHAPTPSQPAAPPQRQQQQQQSSQAQQGPFRRELNFSDFASNGGAAAPPFFKPETGEILNFGNDSSSGRRNPSPAPPAATASLTTAPGSLFSQHTPTLTAAANDAKSNNQKRSMEATSRASNTNNHPAATANEGMLSFSSAPTTRPSTGTGAPAKSESDHSDLEASVREVESSRVVAPPPEAEKRPRKRGRKPANGREEPLNHVEAERQRREKLNQRFYALRAVVPNVSKMDKASLLGDAISYINELRGKLTALETDKETLQSQMESLKKERDARPPAPSGGGGDGGARCHAVEIEAKILGLEAMIRVQCHKRNHPAARLMTALRELDLDVYHASVSVVKDLMIQQVAVKMASRVYSQDQLNAALYTRIAEPGTAAR
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain (By similarity).
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MAYASRFLSRSKQLQGGLVILQQQHAIPVRAFAKEAARPTFKGDEMLKGVFFDIKNKFQAAVDILRKEKITLDPEDPAAVKQYANVMKTIRQKADMFSESQRIKHDIDTETQDIPDARAYLLKLQEIRTRRGLTDELGAEAMMFEALEKVEKDIKKPLLRSDKKGMDLLVAEFEKGNKKLGIRKEDLPKYEENLELSMAKAQLDELKSDAVEAMESQKKKEEFQDEEMPDVKSLDIRNFI
The following text describes a protein:
Function:
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Sequence:
MSDSAVQRSSGRGRFITFEGGEGTGKSTQIKKLADRLKAARMRTLVTREPGGSPGAEIMRHLVLSGMGKLLGPEAETLLFAAARDDHVHTVIEPALKQGIWVLCDRFADSTRAYQGSLGSVSPGLINAMQRVTIGDLKPDLTIILDLPVEIGLQRAAARRGSGTPDRFEGEQLSFHQGLREAYRKIAADEPARCVLIDANSDPDTVAGRVWSALRDRLLPTPASVVSV
The following text describes a protein:
Function:
Probable transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MDSSSQDEKWVERDFLNLNESGVNSSSPKRQAEEEVEEFQGENVTTNREKRPKLETLNLSLSLPDVSLSLTASNALQNNVERPMPTRSIQSLAPSRDNTCSNDFTAASLSYSYSHPFSHNPSCSLTHNSTEYYEYSVGRDDQIWCGGEGTNGSVHSRFRPIGDGSVALNNHGGGGGGGGFSMIQGSRVMNKDSCNNSLYKTTSSDNLSFFPSELPARPRVETNSGDSRKKDSENLRGLESMDGGRARKLSRPERILREIVSEAIPIMAQIIQELSDETLESVKEYLKNLFLMSEKREELMALKKRLERRSDLSKETLSKCHKDQLAILVAVKMGLGSFLSAKIQLPVNKLVEIFLYMRCRNVNCQSILPVDDCDCKICSTNKGFCSSCMCPVCLNFDCANNTCSWVGCDVCSHWCHAACGIQRNLIKPGPSLKGPSGTSEMQFHCIGCGHASEMFGFVKDVFLHCAKDWGLDTFVKELDCVTKIFKGSNDFKGKELQKKAAELVSKLENKVMSPSEACNFIIRFFNNADSMSDFTASGTSLNDLIVTQASVQKDAIPIPPATSLPPKYTIYNMTSSSGRRDSMSNDLFKKDLIGDLKVEDEIRFGKLSKNDGFDSLESVVRIKEAEARMFQNKADEARREADEYKRMVCARTEKLEEEYAHKLSKLCLRETEERRRKKLEELKVLEDSHCDYLKMKRMQAEIAGLLERMEATKQQWV
The following text describes a protein:
Function:
Adhesion G-protein coupled receptor (aGPCR) for N-docosahexaenoylethanolamine (synaptamide), an omega-3 fatty acid lipid highly enriched in the brain. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase. ADGRF1 is coupled to G(s) G proteins and mediates activation of adenylate cyclase activity. Also able to couple to G(q), G(i) and G(12)/G(13) G proteins; additional evidence is however required to confirm this result in vivo (By similarity). Involved in the development of neurons and cognitive function. In liver, involved in fat accumulation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
The Stachel sequence (also named stalk) in the C-terminal part of the extracellular domain (ECD) functions as a tethered agonist. In the inactivated receptor, the Stachel sequence (also named stalk) is embedded in the GAIN-B domain, where it adopts a beta-strand conformation. On activation, the Stachel moves into the 7 transmembrane region and adopts a twisted hook-shaped configuration that forms contacts within the receptor, leading to coupling of a G-alpha protein, which activates signaling.
Sequence:
MRIGLLWLVPLFTLTEGTDGFLQQKNDGRRTKEIVSMVEERHPVHEYEVLLQVTYRDPEEKRELKRFLKLLKSPSPSLRGPSKIIRVKATTYCRSRKGFLECACEDSYTWFPPSCLDPQNCCLHTTGPVPSCNCSLRGLRQSINFCERAKVWGTFEIDEKFPEDLWNSSSDVYAHYTVGIENQLKEAYRRVHGFESVRVTQFRKGSIVVGYEVTGSTSPPELLFAIEQEAEKAQEALRRQFPVKYGSFRVFGKAPCNSISFGFGSENDEYTVPCSSGFTGSMTVRCQSSGWQITRESCVLSQLEELKKELRMIAGKITEAGVASLVQNLSTILLQSPSTTVGNLGSVVSLLSNISSLSLANSLTVSNLTLMNVINIADHILDSASITNWTILLQDAKDASSQLLKTLESISSLIPSMALPLNFSGKFIDWKGTPVTQIQSTRGYNYQMEMRQNASLPIRGHVFIEPDQFQKSHPKTIISMASLTFGDILPITQRGNAWVNGPVISTLIQNYSISEIFLNFSKIKGNLTQPRCVFWDFSQLQWSNAGCQLVNETLDTVLCRCSHLTSFSMLMSPFVPSSVVPVVKWITYIGLSISIASLILCLIIESLFWKQTKRSQTSYTRNICLVNIAVSLLIADVWFIIAATVDPSVSPSGVCVAAVFFTHFFYLAVFFWMLVLGILLAYRIILVFHHMALTTMMAIGFCLGYGCPLLISIITLAVTQPSNSYKRNDVCWLNWSDKSKPLLAFVVPALTIVAVNLVVVLLVLRKLWRPAVGERLNQDDKATAIRMGKSLLVLTPLLGLTWGFGIGTMANSHNLAWHVLFALLNAFQGFFIFCFGILLDTKLRQLLSNKLTTLSSWKQTSKRNASDTVTQPKCLRTFNILQHRGMYALSHTGDSSSDITLTQFLSTE
The following text describes a protein:
Function:
Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases.
Subcellular Localization:
Cytoplasm.
Sequence:
MSREPIKYNVSELSSELDEGYICPICLESYFKKEIYQCKEGHCSCKECWIKSLENKKECMQCKIKVNSFNELSRARQVERFLLKICVCCPYSFKNIIRVDESEKLIKDGWGCNEIVKLEELDNHIENCNFRFVKCKYYEIGCMDQIRYNQNEFHISKCEYQPLNCTHCSNVYLLKIMEQHYLECPSMLIDCKECNEKIKREEMYMHIDKECQEVVISCKFLQFGCNDKIKRKNLENHLDQTNHSKHLSTVLESLINKNNQLSNSIDYLTKGKELMASTIEDLVIKNNLLLNSIDYLTKGKEYMASTIEDLNIKNNLLSDSINELIKGKELMASTIEDLVIKNNLLLNSIDYLTKGKEYMSSTIEDLNIKNNLLSDSINELIKGKENLIIKNNQLSNSIDELLKGKENLIIKNNELSNSIAELSRGKEYKNKWIISNYSKIFHSPGQFLKSPPFGYAPYFFHILIYKNGMDTSDIGNIGVFLSSGDNNNQKNISFSIALLNYYSENNYSYSFKNSDITPSGFGWNCFINGNHMNIITGYVKEDDKVEFEFTLTYPPPNPLLSN
The following text describes a protein:
Function:
Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Sequence:
MNILIKNADIITCNASDDVLQGAFLGIKDGYIDFIDTKEDALKDFKADRIIDAKGKLVMPGLVNAHTHSGMTILRNFANDLALEDWLFGNVLPVEEKLTPEDIYWGTLLGIAEMIKSGTTTFADMYLHMEEVARAVSETGIRANLCRSPLKDSDKSVEDAVRCFEYFKKWDNSFNGRIKVYIEVHSVYLFDEPSLRMSAEVAKEINTGIHIHVQETLKECEDSNKKYGMSPAEICCKTGIFDVPVIAAHCVHLSDGDMGIIRDKGVNVIHNPTSNLKLGSGIAKVDDMLKNGINVALGTDGAASNNNLNMFEEMHLAALIHKGVHMDPTLIGASCALKMATVNGAKALGFGGEIGEISKGMKADLILIDMDKTHLCPVNDPVSAVVYSAQSSDVDTVIIDGNIVMENRELKTIDEEKVKFNVKEIAKRVLR
The following text describes a protein:
Function:
Part of the ABC transporter complex FepBDGC involved in ferric enterobactin uptake. Responsible for the translocation of the substrate across the membrane (Probable).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MIYVSRRLLITCLLLVSACVVAGIWGLRSGAVTLETSQVFAALMGDAPRSMTMVVTEWRLPRVLMALLIGAALGVSGAIFQSLMRNPLGSPDVMGFNTGAWSGVLVAMVLFGQDLTAIALSAMVGGIVTSLLVWLLAWRNGIDTFRLIIIGIGVRAMLVAFNTWLLLKASLETALTAGLWNAGSLNGLTWAKTSPSAPIIILMLIAAALLVRRMRLLEMGDDTACALGVSVERSRLLMMLVAVVLTAAATALAGPISFIALVAPHIARRISGTARWGLTQAALCGALLLLAADLCAQQLFMPYQLPVGVVTVSLGGIYLIVLLIQESRKK
The following text describes a protein:
Function:
May play a role in phosphate homeostasis. Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
The SPX domain has high affinity for inositol polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol pentakisphosphate (5-InsP7). Its affinity for inorganic phosphate is tow to three orders of magnitude lower.
Sequence:
MKFGKYLQRRQVSAWKKKYVFYKSFKKQIKSIKRAKTEEELYIGNESQIQIELTAIPINKSISKIPPPSQSSSSPSQSQSQIEIPLQSIEPTTTTTTTAATSSSSSSTTTTNVNSKTIINSSGGSIKSNNSNPLSQSSIIQRGPVIIRENNIEREEKKFDSMLQEEFDKVNTFFKQQEDEFIHQFNDIKQKVVAMSEICKNSSSKSLKDAISEDSPRLGKFSHLFYNPSIIKKRNSSNLTSSAIKDDGVGGASSNSQRYAQSSPSSSSSSSPSAMAVKAIAHAANAETYWNPGSLKLGKIRRSLKRAMEENYREIQALKEYTSLNMIAFRKIFKKYDKVLQSDSSVDGMKLVQQQYFVKSKKLVVIEREIESLYTNTFKHGNRRNAMAKLRVPKEYNAPPKVVFLTGGLSGMSLILFIFCIRYMINNVAIIYFDSPTPLHFLSMFMLHRMIGIPILLLWYFGILLYVTSGKNINLFLILGWDARTNITHYHILFLASGLTFLWTLSLFLYTYLAIHIDGKLPILFPFLLIAIVLFIVFCPFNIIFRPSRYWLIHTFARIFSAPFLPVKFKDFFFGDQFTSLSIVLSDLEYVICFFVSDLWTDGDICWRINPYIKPCLVCVPPLLRALQSLRRFKDTKQNIHMMNFGKYSLTMLSTVTSSIANSKLLTDSSHKKGTLALWIIISIVSTIYSLGWDFLMDWGVLRTHSRNFLLRDHLFYRHKWVYYFAMITNTLMRGSWTINVSFEALSSRTKELIVLATAVIEVTRRFQWNFFRLENEHLSNVGKFRAFDLKIPDILNTQSQQQQQQQQQQQQQQQQQQQQQQQQQEEIGANELLGNNGEPIVGDSKTVITSDDFINGTSKQEGTIDLDRAQFQYSKNDLEDKIEESIINNKNNNNNECTPFSENSFYNNDHSGDENSNE
The following text describes a protein:
Function:
Required for the deacetylation of acetylated sterols (By similarity). Has a role in meiosis.
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MISLSLLYRILTLPIILVGTTILYFTIGTNFPHDELRHNLLSTLFCSSMLHLSKGLTVKDVRIFFHDSIGSTLLKNRKKLNSENELPNYGEKFTHKYDNQDMPDSVWLAKVNGMTKSDPIILHLHGGMMALPYDKVILVGLSNLYKLFSTTMNRPPSILLVDYSLVSQGYTYPKQVRECLNVYQVLISKGFRNITVLGESAGGTLILSFLYQISELSKLNKVVWPKGVALISPWLDLTNAKKIGSYRANDGLDVICYETLNRFGKAYVNNEESLFTSSVVNINMNCDISIWSKIPPIQDGKVLVLFGENEVFRDEILSWTSKIGLLKAYPNRVLMDKQGIHIGLFLEESPSIGPGMTNLDIWKKKFSVNSLYTFLRETFEE
The following text describes a protein:
Function:
Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). May be involved in sensitivity to quinine by regulating egl-4 activity through the production of cGMP. Promotes the calcium flux to the cytoplasm in ASJ sensory neurons upon removal of a nitric oxide (NO) stimulus and is thereby involved in the behavioral avoidance response to NO-producing organisms like P.aeruginosa.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Domain:
The protein kinase domain is predicted to be catalytically inactive.
Sequence:
MIDGEAYFEKNSTGKLGSWGWRDVNLQFIICTLPVPIYFVVVAIWTINGASNSYRFPFLQTYMILTDRFWLFFRCFTIVAWCGWCSNYIFFPCLMNAILYIISLSLSRDTTFILFIFYQMNKLITVIRDFSYSVYNWCYETVIGENTRKYKMTWKVPKESLKIIVNKNADARMQRELENRTAKDEANALTSRRRVFGSYALIGTQRAEFIQFRQIKHIDITNASLDFLYNLKQLKHDNLANFYGIQLNDDLNTMTILHALVERGTLEEFCLDRDFGMDETFKSAFMRDILKGLQYLHLSPVAYHGHLHAATCLIDINWVLKIALYGVTNFVCDNFDAENITMPDRSDYTISYAQYVCFPPEHIREYDATGKLPTRFVRGSKQGDIYCVGMIFYMMIEREDPYRLIHSVERPGSGLMMEILDHNLMPFISNNETQEDTLLDKCKECWNRDPEKRPTIENLRNAIAICYADSKGNLIDQMIRMNEKYADELETLVAARSADLALAQMQTMRLLNEMLPASIAKDLKNGVIAPARSYASATVMFVQICDFIVILKRRPPKEVIGFLNDIFDQFDTVIKRHDAYKVETTGETYMVASGVPNENEGRHVFEVAEMSLEIRAISLSYTLENDKNYKLRVRIGFHAGPIAAGVIGIKNPRYCLFGDTVNFASRMQSNCPPLQIQTSEITARMLLATHEYKLVKRGIVHVKGKGEVNCYWLNEHIHKDEEIEESGTISHPLES
The following text describes a protein:
Function:
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate.
Sequence:
MSTPAYLTKLESIPKEKFLFGPSPISYLPNLTAVLGGKVKLYAKREDCNSGLAYGGNKVRKLEYLVADAKAKGCNTLVSVGGVQSNHTRAVTAVAVASGLKAVTVQEKWVPIDPPLYSETGNILLSRLMGGDVRLNQETFDIRHKKATEDAFKDVEAKGGKPYYIPAGASDHPLGGLGFTNWVVELAKQEKELGVFFDVVIVCSVTGSSHAGTVVGAVAEGRKRKIIGIDASGKPEATRNQVLKIARNTAALLDERLEIKEEDVILDDRFHAGIYGIPDDETIAAMKLAAQTDAFITDPVYEGKSMAGMIRLVKEGAIKEGSNVLYIHLGGQPALNAYSSYFPHA
The following text describes a protein:
Function:
Exerts an anti-apoptotic effect in the immune system and is involved in responses to infections.
Subcellular Localization:
Cytoplasm, cytosol. Endoplasmic reticulum. Golgi apparatus. Mitochondrion.
Sequence:
MDIMKADEKKDDFEEDGTDSENEIDSVLDSSTGFAPHDKLYENLQNLAETSLNSSTNLHVSEELRIMLLGARGSGKSSTGNTILAYNAFKSDMQLSRVTQFCDKASGNIGGRPVAIIDTPGLNIIGSTEKEVTREILKSISLYSPGPHVFLLVMPVGNLTNDDKSMHKLIESMFGERIWQYTIIVFTHGDRLEGKAANDVIACSDIELREFIHKCSGGFHFFNNKDDTNDESVIDLLKKVETLVAINGKSCYTSSFYPATERKIRKKMEKLLEKRKEQIVQMERETVVRCKTEQEVERKKRELWRKEEDNARRKAEKKSVKHLGRKSST
The following text describes a protein:
Function:
Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins.
Subcellular Localization:
Secreted.
Sequence:
MKVLWSLLGLFLLYLSTECLLPPSKEELNQMSQVGEKYLDRQIENAISGVKEMKTVMERSEEEHKRMLSEMEKTQKEKENALKTAQEMKEKLSEEQSVCNETMEALWEECKPCLRKTCVKFYSRTCRSGSGLVGRQLEEILNRTSPISIFINGQSIETLLSEDQQQTRHFQDLEESYTEVSDGVENMFTDSMKVFDHMQMFHHPGFFPSRFQFPSMFGGHEGSTHAGRIYRSPMHDSLFHSLQSLFRPMERSMSMFGKNEERNFTSEGWKLNEKVTTDDKMTCKEIRRNSFGCVKLKDECEKCQQIQHIDCSGKRPLEGPLKEELERALGKAEEFTQEFNNLLNIFQEQMFNTSSLLDLFNKQFGWVSSLANHTQNEDGFFQIQAVMSKGSDNAENPADTRVSVKLFDGPDMIYTVPGDIPWSDPKFSEVVAQEALDRYKQNAVITKL
The following text describes a protein:
Function:
Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Antagonizes the activity of nodal/activin signaling during gastrulation to suppress mesendoderm formation. Acts maternally to inhibit vegt and beta-catenin-activated gene transcription, probably by forming a transcriptional repression complex on the promoters of target genes. Binds to an octamer motif in interspersed RNA.
Subcellular Localization:
Nucleus.
Sequence:
MDQPILYSQTSFPNFTYSPGVVQDGGNYQYLGNYNAPSYPQPFFHVPVIKSEFGAHEEETPGSCHAASFDWNLYPHFQISNQAASNSSGDPSPEGRTEEDGSVSEGRSSSSPSPNSPLVPSFAQYWHYPSWQQGNLTNQAHTLFDGGDEKPQQSRHSPTASLGSGASNTEDEEVPSAISSRAERGLCSPSPNNASCGPGTEEDGMTLEEMEEFAKELKQKRVALGYTQGDIGHALGILYGKMFSQTTICRFESLQLTFKNMCKLKPLLEQWLGEAENNDNLQEMIHKAQIEEQNRKRKMRTCFDTVLKGQLEGHFMCNQKPGARELTEIAKELSLEKDVVRVWFCNRRQKEKSKFRMSKGHEFVGGASPGSIQSEHISFTPIPANSQDYGLASLHPNRAPFYPPPFPRNELFPHMAPGISMGVLTG
The following text describes a protein:
Function:
Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
Sequence:
MASSMSLKLTCVVVFCMVVGAPLAQGAISCGQITSALAPCIAYLKGNGAGSAPPACCNGIRSLNSAAKTTPDRQAACSCIKSAATGISGINYSTAAGLPGKCGINIPYKISPSTDCKSIK
The following text describes a protein:
Function:
Orphan receptor. Has spontaneous activity for beta-arrestin recruitment. Shows a reciprocal regulatory interaction with the melatonin receptor MTNR1B most likely through receptor heteromerization.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein.
Sequence:
MEEPPPPRPPASMALLGSQHSGAPSAAGPPGGTSSAATAAVLSFSTVATAAAAALGNLSDASGGGTAAAPGGGGLGGSGAAREAGAAVRRPLGPEAAPLLSHGAAAAAQALVLLLIFLLSSLGNCAVMGVIVKHRQLRTVTNAFILSLSLSDLLTALLCLPAAFLDLFTPPGGSAPAAAAGPWRGFCAASRFFSSCFGIVSTLSVALISLDRYCAIVRPPREKIGRRRALQLLAGAWLTALGFSLPWELLGAPRELAAAQSFHGCLYRTSPDPAQLGAAFSVGLVVACYLLPFLLMCFCHYHICKTVRLSDVRVRPVNTYARVLRFFSEVRTATTVLIMIVFVICCWGPYCFLVLLAAARQAQTVQAPSLLNVVAVWLTWANGAINPVIYAIRNPNISMLLGRNREEGYRTRNVDAFLPSQGPGLQARSRSRLRNRYANRLGACSRMSSSNPASGVAGDVAMWARKNPVVLFCREGPPEPVTAATKQPKSEAGDTSL
The following text describes a protein:
Function:
Component of the glyceraldehyde dehydrogenase which is involved the nonphosphorylated Entner-Doudoroff pathway. Catalyzes the oxidation of D-glyceraldehyde to yield glycerate. When the artificial electron acceptor 2,6-dichlorophenol-indophenol (Cl2Ind) is used, the enzyme shows a broad substrate range (glyceraldehyde-3-phosphate, formaldehyde, acetaldehyde, propionaldehyde and isobutyraldehyde), but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo.
Subcellular Localization:
Cytoplasm.
Sequence:
MLVVKKGEGVKVRVRVNGVWYEKYVSPRTLLVDFIRDELGLTGTKVGCDTTTCGACTVIMNGKSVKSCTVLAAQADGAEITTIEGLSSDSKLHPIQEAFKDNFALQCGFCTAGMIMQTYFFLKEHPNPTEEEVRDGIHGNICRCTGYQNIVKAVLDASKRLRS
The following text describes a protein:
Function:
Involved in male fertility. Required for manchette development and acrosome biogenesis during spermiogenesis. Binds in vitro to phospholipids, including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidic acid (PA). Contrary to other profilin family members, does not bind to actin in vitro.
Subcellular Localization:
Cytoplasm.
Sequence:
MNQAQSLLIEGLTSTKHVAHAAIIKIDDGSILASTPGFGIQSQAQTFIQAFLQDLLEIRREGLYFKDHYYKCVRADDNAIYLKGKDYGLILVKTRSLVLVGTYCQGMYPSVCVEALEKLADYFREKGN
The following text describes a protein:
Function:
Surface antigen mediating adhesion and aggregation in S.cerevisiae.
Sequence:
MSSFNSNSNPANAQNLSSFQFQPPKEDVIFDTHQMSLSVPQSRYYASSMMQQSQQGQPQSQTSQQQQQQPFLMNIPPAFTQTQPQQMLYAMPPLQTQQPSSSSATTNNVVPPHHYNQQQSQQQQQQQQQYQQMQPQPNNMQFFDNTIPNYLIMNQTISPSQTQTTAQPNISYYNYSTQPQLQSAQPISHSQPQPQPQATQPRSNRSRSQTSFSKPRGSRQVSGSGRSTGAKKQSAITSGSTGTGPARNADTGMTSVANSTSTTTMTTTNNNNKLSVSAPVNVIYANLPERLQQVLPAPPLSRAPVRPDVTVNLTSKRAKRKSKFTPEQDDMIVNLKKKGKSWVEIAEITGVGSYLAARNRFQVIVGQQGNNNSSAWDNTDKLFLNQLLDAGEIEKWRFICCELNKSTNKNFTDYECREMIRQLFWLNPASFGVNEETIIESQKEKKLTEKTIEQREQQRKKRASANHSPPDSDSITNTNNNQQEVKYIDPQYKNYQSQLMPNQNTGSGATKISSTTPPPPSQALSNNVNTMNKNIVSSALGGTSFSQEQHSLHSNQHHHNHQQHPLIHHHQYQQQSSLPPPPTIPSTIPTSSLSIQQQQQQQQQQLYNKQFY
The following text describes a protein:
Function:
May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein.
Sequence:
MSDSEKGHAPETSDEPVNLKFNMNVSDRDPNGINEHLKVSFSEVFAEPHGNYSFDAIWKLSYTIFEGSKLWCYRIISAIFALPCALFCGCYFACVVFGQIWAYTPCIRGLSILFGCMFKMITLCVQVCCNPVNDSVARILSRIRFYHVNSGSLPTVKQDVKDFDENVALTTASLKVV
The following text describes a protein:
Function:
Required for normal photoreceptor differentiation between Ras and Raf for EGFR signaling in the eye and for mitogen-activated protein kinase phosphorylation. Probably acts together with Cnk to promote Raf activation, perhaps by recruiting an activating kinase.
Miscellaneous:
MISCELLANEOUS: 'Aveugle' means 'blind' in French.
Subcellular Localization:
Cytoplasm. Membrane; Peripheral membrane protein.
Sequence:
MGEETINSTQNKTRTKTTRPKAVYLWTVSDVLKWYRRHCGEYTQYEQLFAQHDITGRALLRITDSSLQRMGVTDNRDREAIWREIVKQRLKTDIMEIRDMERLNIY
The following text describes a protein:
Function:
Acts downstream of piRNA production to promote mediator complex-dependent endogenous siRNA biogenesis from piRNA-target mRNAs in the RNA interference pathway in germ cells. Not required to identify target mRNA by the piRNA pathway. Plays a role in both spermatogenesis and oogenesis and in maintaining fertility over multiple generations, probably by directing mutator-dependent silencing to piRNA-targeted genes.
Subcellular Localization:
Cytoplasm, perinuclear region. Note=Localizes to perinuclear foci in germ cells, called SIMR foci, which are distinct from Mutator foci, P granules and Z granules. SIMR foci are stacked, with znfx-1 localizing between simr-1 and pgl-1. Its localization at SIMR foci is adjacent to the mutator complex protein mut-16. Perinuclear localization is not dependent on mut-16.
Domain:
Tudor domain specifically binds peptides with symmetrically dimethylated arginines (sDMA) and may facilitate protein-protein interactions. The Tudor domain contains the conserved arginine and aspartic acid residues, which play a structural role, but lacks two of the four conserved aromatic residues, so it is unclear whether it is functional to recognize a methylated substrate.
Sequence:
MSNEKQQWDDAYCLAEEMHDAGRPFKREELNIADQFICSRFSTIFEYDPYKDTYGFRNQELTHAIPVKSKCRHISDVDILELKKNTANADIRFPSYLNICPVYAMHPFTVLAFDLSKPVPMGMNASMENAAPNMKSPTEAEITPGTIYIFKHRDNKCYRCVILFEDGDNNVSDADRKYMVAFLDTPQVVSVKLKTLFHLGKFTIESYPCALYCCRAVGILEIRKDFGADLNGQINEFYKDKVKRKSGVHALIYKKDDRGDKLIFDCPSILGTSMTMALEIKDVIGHRSVAENDPTALSYDELVSKQLPTVDIDDHNSSVVLDLEESVIAQELGSTNGADCPCNNDNIDDFMQSQRQNPLDNNRDNWDRINESRSSMQSFAINQSQAITANPTPQPTFDESSGEVQTIPESINNLALNGRYLEDGRGTEEIREERSVESRQIGNQVVSQASCNYLEARQNSTQTANAESVCAIISESHAALPTDIQVIPSQHVLNENNHTVLPSVAPIIRNATGHSHIFGRQIPSPAFRRESLSSGNSIQVATFAATTGPCGSNTSRPTAQNTANSSINQDMSISNSSTNARLITIAQDNLNDTENWPNSEREQSATEMESGAEATTNSAVDEFAQVSDDMKGLADSMINFLRLTANSNNQDAFKANIFAMELISTKIPNQLTKRFFTLKIAEAKSLAEGFN
The following text describes a protein:
Function:
Strongly up-regulated in Mhc mutants suggesting a role in muscle function.
Sequence:
MTDVPEPVRKCASLLKGTKSDTEKFAALFMVTKLVKGKDCNAAGKKLLFEAIGFPFLKKLLVSKDLPNDCPPLVYKSVALSILTCFCQEEELATHKDIIDAIPTLLEIVEQADDEDYEDNLIVVSEAYSCLKSIASHEPGQQALLATGAIPKMSQIYSAQSFQTDEALHLIVLLVKQFGVVSWPEDPTAFHALIQRIALDMETDDTERKYELCRILADILITCRREIVINSLEGQIWPESLFKGCGDILKAKIGPKQRDPALHLIATTLHVLGIQWAFMDEQKTFFLQLLQLGAIEVRMQMDEKKLETTFKQAELLTCCFSILEHCIEYMATDQLDLEPKEKQTTYTALKGAFNQVLAVLTRVSQDKIRESSNPKDKKFVFAIVKVLSAWLAQETTAMRPAIYKLLPFMLKVANESFQELKTWRAGTREGEPPIDVLRIMLPALCHFAVEEEARRVLFTHKQDEVLLESLEFYFSIAHWKRPPIPRAERLKRMNEPDPVPTPEQQAEMKVARSAIVALCNILMNFTVLEPKKAEDGPTFANLLKFVVENLPELKDTPDNLVIHGNLAVLGLLLLKQQSKKVKQNDFSICRYIQATIRFLWDAYNIDESNDPTALVVSIAYKGYWSDLSELWFLGMQTMCGVLPLVPWLSEFALESGWAEGIVKTLKKVKIGTLPANVKSAYEDFLSQLVDVNGDVQAVLKKADALRVCRNHRMMDLGKKLFGD
The following text describes a protein:
Function:
The inner membrane transporter component of the MexAB-OprM efflux system that confers multidrug resistance. Functions as the major efflux pump for n-hexane and p-xylene efflux. Has been shown in one study to be involved in the active efflux of the autoinducer N-(3-oxododecanoyl) homoserine lactone, thereby playing an indirect role in quorum-sensing; but has been shown in another study not to be involved in efflux of this autoinducer. Over-expression of the pump increases antibiotic and solvent efflux capacities. Implicated in the secretion of the siderophore pyoverdine.
Miscellaneous:
MISCELLANEOUS: Pyridopyrimidine derivatives, such as ABI-PP, are not exported by the MexAB-OprM efflux pump, bind tightly to a MexB hydrophobic pocket and so potentiate the activities of antibiotics such as erythromycin.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSKFFIDRPIFAWVIALVIMLAGGLSILSLPVNQYPAIAPPAIAVQVSYPGASAETVQDTVVQVIEQQMNGIDNLRYISSESNSDGSMTITVTFEQGTDPDIAQVQVQNKLQLATPLLPQEVQRQGIRVTKAVKNFLMVVGVVSTDGSMTKEDLSNYIVSNIQDPLSRTKGVGDFQVFGSQYSMRIWLDPAKLNSYQLTPGDVSSAIQAQNVQISSGQLGGLPAVKGQQLNATIIGKTRLQTAEQFENILLKVNPDGSQVRLKDVADVGLGGQDYSINAQFNGSPASGIAIKLATGANALDTAKAIRQTIANLEPFMPQGMKVVYPYDTTPVVSASIHEVVKTLGEAILLVFLVMYLFLQNFRATLIPTIAVPVVLLGTFGVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVMAEEGLSPREAARKSMGQIQGALVGIAMVLSAVFLPMAFFGGSTGVIYRQFSITIVSAMALSVIVALILTPALCATMLKPIEKGDHGEHKGGFFGWFNRMFLSTTHGYERGVASILKHRAPYLLIYVVIVAGMIWMFTRIPTAFLPDEDQGVLFAQVQTPPGSSAERTQVVVDSMREYLLEKESSSVSSVFTVTGFNFAGRGQSSGMAFIMLKPWEERPGGENSVFELAKRAQMHFFSFKDAMVFAFAPPSVLELGNATGFDLFLQDQAGVGHEVLLQARNKFLMLAAQNPALQRVRPNGMSDEPQYKLEIDDEKASALGVSLADINSTVSIAWGSSYVNDFIDRGRVKRVYLQGRPDARMNPDDLSKWYVRNDKGEMVPFNAFATGKWEYGSPKLERYNGVPAMEILGEPAPGLSSGDAMAAVEEIVKQLPKGVGYSWTGLSYEERLSGSQAPALYALSLLVVFLCLAALYESWSIPFSVMLVVPLGVIGALLATSMRGLSNDVFFQVGLLTTIGLSAKNAILIVEFAKELHEQGKGIVEAAIEACRMRLRPIVMTSLAFILGVVPLAISTGAGSGSQHAIGTGVIGGMVTATVLAIFWVPLFYVAVSTLFKDEASKQQASVEKGQ