lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Acts as a component of the translation initiation factor 2B (eIF2B) complex, which catalyzes the exchange of GDP for GTP on the eukaryotic initiation factor 2 (eIF2) complex gamma subunit. Its guanine nucleotide exchange factor activity is repressed when bound to eIF2 complex phosphorylated on the alpha subunit, thereby limiting the amount of methionyl-initiator methionine tRNA available to the ribosome and consequently global translation is repressed.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MFDPRAGAPKRWASQSQDFQAVILVGYGENLYPFNQGTNVISKALLPVGNVPIINCVIDWVLAAGLLDILIIVPNAFHDQIADHIAEAYNKSTHSRVRINLRKNSEGERDEDEGDSEEKDGTARILKKFRSFIKSDFVLLPCDISPPSYLPLKTILDKHRSSPKAVMTSVFYEPIESVKDAEEKILVGLDKTSDELLLITPLEGMEEDLELRMSLLNRHPTLSLTTRILDAHVYVFRRTFLDLLATRRAKDLSSMKEQVVPWLVKGGWQRGLGERWEPILDPPSRDPLAEALARSTTAPPSRSLLHPSSSPSSDRTPLPQTSPASPSGDADTMYSSGILPTAPSRTRKGFKPEWKCQVLVITPPPAPPAPAPVQGKGGKQDKSRAPVYEPEHLIRANSLAGYWELNRRFIKSLSSTTPAAKSAQPVRNIIPEDAGTAPAISPAAQISPDSVLGEGTRVGEKTSIKKCIIGRHCVIGKGAKLNNCVIWDFVTVEENARIENSIICSNGRIGEKAQVKDCEFGTGFEAKPGAILKGERLIAGQEA
The following text describes a protein:
Function:
Activated phosphatidylinositol-specific phospholipase C enzymes catalyze the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) involved in G-protein coupled receptor signaling pathways. PLCB4 is a direct effector of the endothelin receptor signaling pathway that plays an essential role in lower jaw and middle ear structures development; Catalyzes the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3).
Subcellular Localization:
Cell membrane.
Sequence:
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPSCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIRSGAIPKDPKILAALEAVGKSENDLEGRIVCVCSGTDLVNISFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFMTNTNGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPVAFSYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDENAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRLKPEVEKKQLEALRSMMEAGESASPANILEDDNEEEIESADQEEEAHPEFKFGNELSADDLGHKEAVANSVKKASDDLEHENNKKGLVTVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGTYVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKKFLSITEKRADQMRAMGIETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAALASGVEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQLLKSCHAVSQTQGEGDAADGEIGSRDGPQTSNSSMKLQNAN
The following text describes a protein:
Function:
Involved in pre-mRNA splicing as component of the spliceosome. Combines RNA-binding and PPIase activities. Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins. Inhibits KMT2A activity; this requires proline isomerase activity.
Subcellular Localization:
Nucleus.
Domain:
The RRM domain mediates both interaction with RNA and with KMT2A (via the third PHD-type zinc-finger), but has much higher affinity for the KMT2A PHD-type zinc-finger.
Sequence:
MATTKRVLYVGGLAEEVDDKVLHAAFIPFGDITDIQIPLDYETEKHRGFAFVEFELAEDAAAAIDNMNESELFGRTIRVNLAKPMRIKEGSSRPVWSDDDWLKKFSGKTLEENKEEEGSEPPKAETQEGEPIAKKARSNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEVTEGLDVLRQIEAQGSKDGKPKQKVIIADCGEYV
The following text describes a protein:
Function:
Involved in promoting a consistent pattern of asymmetric cell division and fate assignment, perhaps by regulating apoptosis of specific cells, including in the Q neuroblast lineage. Downstream target of MAP kinase mpk-1.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Midbody. Chromosome. Note=Before first cell division of the Q neuroblast lineage, localized diffusely in cytoplasm and concentrated in the nucleus. Around metaphase, localized to the centrosomes and subsequently inherited by both daughter cells. Before anaphase, localized near the region of the membrane that eventually forms the furrow and as anaphase continues, concentrated within the furrow and remains there, eventually localizing to the midbody. During telophase, localized to chromatin.
Domain:
DEP domain is required for function, perhaps regulating the apoptotic fate of the Q.pp neuroblast, but appears dispensable for subcellular localization.
Sequence:
MSSSRHFSIPYDEDVVHSVILENTPSPPPKPPRGILRKEAPMKPQRSALKIEPARDDDKENNSQPQARSQFKAKDTMEQMQSYFKRSISVLRKSEEHFTGAEAADILTAYIETHRNEFPRDNIGRSNAVKLLEIWLESNTIQSVESHQKKFVDSERTFYRLGGDSESLYIVNTPIASRNHDDSASVSRSESSRRSNSIKRLFSPFVRRNRSNSRGRDKDKDNLKDGSSTNLKSTWSLFSSSSEKNEKKLKKAEQQLIKEEEAEVYELSLFHLLSLIDVEFLEDVALPVQDSKNNASFLSSILGKVGLGASEERLDPHQEDHMDLLIETHPLIRDASQWFQMARCCAPLLYFEAKPVASNHKTSHNEQLYLWCRAALDAVKNRLEKMTQNGSSPLFPSEFAPLLTKIAQQLINDMDSGEKLSTAVMYIFLMVPHPIRKTIDQLVQWLQLTMRTDAVEDLRSPYYLGKKDPRRYKENVNVIIGELSSFIFPRGCMTNVQQDIFIETLVELRQKGKLGQRPAQLESSLRAKSVNGQIKWQRKERKHNSLEGDLTPVRYTVRRESIRSKTSKSKDGLNETDSALVTMINSVIDNKELSLTEKKKQLMNFKKFYPKLYNDFFPGMI
The following text describes a protein:
Function:
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MATSTTMSHQAIGSVVSQRPFKASQFLKEPLNNVPMKFRQKRFKIEATASQISVVDNTFLSPSPSKNKPHESKKKSNEAALILIRHGESLWNEKNLFTGCVDVPLTQKGVGEAIEAGKKISNIPVDLIFTSSLIRAQMTAMLAMTQHRRKKVPIILHNESVKAKTWSHVFSEETRKQSIPVIAAWQLNERMYGELQGLNKKETAERYGTQQVHEWRRSYEIPPPKGESLEMCAERAVAYFEDNIKPELASGNNVMIAAHGNSLRSIIMYLDDLTSQEVTTLDLSTGVPLLYIFKEGKFMKRGSPVGSTEAGVYAYTKRLAQYREKLDAAATI
The following text describes a protein:
Function:
Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species.
Subcellular Localization:
Cytoplasm. Peroxisome. Secreted.
Sequence:
MTADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDRFQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKSRLHPVQERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTIEEIEDAFQGNLCRCTGYRPILQGFRTFARDGGCCGGSGNDLNCCMNQKTDHKITLSPSLFNPEEFTPLDPTQEPIFPPELLRLKDTPQKQLRFEGERVTWIQASTLQELLDLKAQDPEAKLVVGNTEIGIEMKFKNMLFPKMVCPAWIPEPVEHGPEGISFGASCPLSLVEKTLLDAVANLPAHQTEVFKGVLEQLRWFAGKQVKSVASIGGNIITASPISDLNPVFMASGAKLTIVSTGTRRTVRMDHTFFPAYRKTLLAPEEILLSIEIPYSREGEYFSAFKQASRREDDIAKVTSGMRVLFNPGTAQVKELALCYGGMHDRTVSALQTTRKQISNFWNEELLQNVCAGLAEELSLAPDAPGGMVEFRRTLTLSFFFKFYLTVLQKLGIQNSKDKCGKLDPTHASATLLFQKDPPANVQLFQEVPKGQCEEDMVGRPLPHLAAAMQASGEAVYCDDIPRYENELSLRLVTSTRAHAKIKSIDTSEAQKVPGFVCFISADDVPGSNITGIGNDEMVFAKDKVTCIGHIIGAVVTDTREHAQRAAQAVRITYEDLPAIITIEDAIAKDSFYEPELKIEKGNLTKGFSEADNIVSGELYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTTKTQSFVANMLGVPANRILVRVKRMGGGFGGKETRSTVVSTAVPLAAYKTGRPVRCMLDRDEDMLITGGRHPFLARYKVGFMKTGRVVALKVEHYSNAGNTLDLSQSIMERALFHMDNCYNIPNIRGTGRICKTNLPSNTAFRGFGGPQGMLIAEHWMSEVAVTCGLPAEEVRRKNMYKEGDLTHFNQKLEGFTLPRCWEECLASSQYHARKREADKFNEENCWKKRGLSIIPTKFGISFTVPFLNQAGALVHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAASVSTDINGQAVYEACQTILKRLEPFKKKNPSGSWEDWVTAAYLDAVSLSATGFYKTPNIGYSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPSEFRVSLLRDCPNKKAIYASKAVGEPPLFLAASIFFAIKDAICAARAGNPDCKTKKLFQLNSPATPEKIRNACVDQFTRLCVTGTAESCKPWSVRV
The following text describes a protein:
Function:
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Subcellular Localization:
Cytoplasm.
Sequence:
MVLKNAIALTGGIGTGKSTTIKILESQGYKILDADKIAHQLLQEHRFKIAQHFGSDILEKDILNRKKLGAIVFQDAHELKWLEDFLHPLIREHMLKKAYELEKNHQAYFLDIPLFFEVGGKKCYPVSKVVLVYASRALQIERLLERDKLKEAEILQRLACQMDIEQKRAMSDYIIDNSSSLKDLNKQVERFLKTLL
The following text describes a protein:
Function:
Acts as a receptor for hemoglobin or the hemoglobin/haptoglobin complex of the human host and is required for heme uptake.
Miscellaneous:
MISCELLANEOUS: This protein is subject to phase-variable expression associated with alteration in the length of the CCAA repeat region. This mechanism is called slipped-strand mispairing. Addition or loss of CCAA repeat units would change the reading frame and result in introduction of stop codons downstream of the repeat region. This may be a mechanism of regulation and a way to avoid the immunological response of the host (By similarity).
Subcellular Localization:
Cell outer membrane; Multi-pass membrane protein.
Sequence:
MTNFKFSLLACSIAFALNASTVYAAQPTNQPTNQPTNQPTNQPTNQPTNQPTNQPTNQPTNQPTNQPTNQPTNQNSNVSEQLEQINVSGSSENINIKEKKVGETQISAKKLAKQQASDSRDLVRYETGITVVETGRTGASGYAVRGVDENRVGIMVDGLRQAETLSSQGFKELFEGYGNFNNTRNSIEIENVKTATITKGADSLKSGSGALGGSVIFETKDARDYLIDKDYYLSYKRGYQTMNNQNLKTLTLAGRSKKFDILIIDTTRDGHEIENYDYKIYPNKQADLRAVGPTREKADPYQITRQSTLIKLGFQPNENHRLSVALDDSTLETKGIDLSYALRPYSTAGNEKYGERIINDQSKRKNIQFSYENFSQTPFWDHIKLSYSSQKITNKARSDEYCHQSTCNGVSNPQGLHLVEEGGVYKIVDKNGDKLTYNKNAGWYGQFQNKNGENVDNDIDSTGGSLDSVLIDCERLNCKNKFQVFVEKDEEGKDKYEYEERDIIVETLPNGKKYGKITLKKGKTPLWDDVYQEESARFLFPKSYGYSTDFVNDRDLNTNTQQIKLDLDKEFSLWHTQHSLKYGGFYEKTLKSMVNHQYNTVANVQWWAGNFFCNKLENGKRTPAPDYSHRCSLMNTDKGKETYLIPVTTKNNVLYFGDNVQLTSWLGLDLNYRYDHVKYLPSYDEKIPVPNGLITGLFKKFGPKDYVYGSKYSKPADYTDCTYNSDCYKKNFKDNLALLLRKTDYKHHSYNLGLNLDPTDWLRVQLKYANGFRAPTSDEIYMTFKHPQFSIQPNTDLKAETSKTKEVAFTFYKNSSYITLNAFQNDYRNFIDLVEVGPRPIEEGSTIAYPFHQNQNRDRARVRGIEIASRLEMGDLFEKLQGFHLGYKFTYQKGRIKDNGLNPKYKEFLELNKDKHPEYEAIARKPQPMNALQPTTSVYNIGYDAPSQKWGVDMYITNVAAKKAKDSFNSQWTSMVKRKEKIYGNEKDAEASTANGKEVKDSRGLWRNNRYTVIDTIAYWKPIKNLTFTAGVYNLTNKKYLTWDSARSIRHLGTINRVETATGKGLNRFYAPGRNYRMSVQFEF
The following text describes a protein:
Function:
Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone.
Sequence:
MTDTVGIVIVSHSKDIAKGTADMVRQMVGSEVKVAFCGGNPDGGLGTSVSLIIDAINDAWSAKGVAILVDLGGAETNSEMAVEMLEPARRDLVVVCNAPIVEGAVMAATEAAGGSSLAQVKAVAEELSAD
The following text describes a protein:
Function:
Plays a role in determining ER morphology.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Sequence:
MVYFFTKKNYSFEKEFLAMESRMANMESKIKSSKFFHNNIYKKIIFYGIIIDLIIAIISYGVSSSLNTLPEKTSLLFYFILFSIVLFAFAKFYRFLIEKLIKYYENKYGKLFISLEKLVEERKRNINFEETKKLCEKYDDIINNNRDQNHAQQSPETQGSITPQTQGSITPQIQGPKTPQIQQPKAPQIQQQPQQPPQQQQQQQTPKKQQQQQQQQQQQQQQQQQQQQQQQIKETTQNFRNRWLNKIIDYLAPNDQLKLICGNCNTNNGSLPSEYFPNKFRCIRCGYLNFKNENLGQ
The following text describes a protein:
Function:
Converts proline to delta-1-pyrroline-5-carboxylate.
Sequence:
MFPTSTSPASRQLVCNVGHARARTIASALGPAAASISRHHVSHSILMVGRINGVGRTYATRLIHSSTNRPKPTDHLTINNASSLPATGGSQSSEMPKTPGPSPLAVLPLTNVLRSWMTTTVSSSPFLLPPSLAVMSVLAHTTNPVLNPDRNPLLRAFLKKTFYAQFCAGENPAEVRQTIDSLKQIGFSGVILGYAREVVLTDSETKDLASCAAEGGAAAEECIRTEINPWAEGTMETVRLASPGDFVALKFTGAGRQALYSLSKQLPPSEALGSAIDGICNLAAERGVRLLFDAEQNALQPGIDDWTLDYMRRYNKSNAVVYGTYQAYLKSTPATLSKHLAIAASEGFTLGVKLVRGAYLGADPRYLICDTKADTDGQYDGIAEALLRKTWSGPLQPPVPQSGSAEKETTNFPDVGVVLATHNRESVLKGKALLDSGVAKLGYEQVAFAQLQGMADEVSCELVAGPHETPKEMEMAAEKESEKGSEKGSEMVNKPQVYKYLVWGSTGECMKYLLRRAYENRDAVQRTRSGREAMGREVRRRVKGLFGVSS
The following text describes a protein:
Function:
Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBC12.
Sequence:
MERYDRQLRLWGALGQDSLNRSRVCVVGPATPLLQEVFKNLVLAGISSLTWLKVECAVQSGSLFLAELKKDLEPLASKQLEYEENDLRKTLQQPQYDWTRFSVVILTCIGEQTAMLDLNEIRRQRGTKFPPVLNTFVSGFYGYIYLVLSETHFVLQAHPDSKKYDLRLQNPWPELINYVDTFDLSKMDTATFSGIPYTVLLMKCIAKLERDGNNGRITIDQMKKVLDQICLPLGNDVIYEPNYVEAKRYAYLACSQNDCCKELEDLLRNLEISDYGNDWHDTYNYEILTLLLTLKNIAKENGELSFQPLTGTLPDMESTTENYIRLKKLYEVKAKLDKSRVEESLARSKKIVSQDVLETFCSHYGEVRKILPPKSDLLGIFSTSNALLDALVMVQFWEQPAVTAEDKDEFIGLRVDDNYSVMAFFGGAVVQEAIKLITHHYVPIDNLFLYNGINNSSATYKI
The following text describes a protein:
Function:
Metallothioneins have a high content of cysteine residues that bind various heavy metals.
Sequence:
MDLSCSCATGGSCTCASSCKCKEYKCTSCKKNCCSCCPMGCAKCAQGCT
The following text describes a protein:
Function:
Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Functions redundantly with other dishevelled family members throughout development. During embryonic and larval development, controls cell migration and/or cell fate specification of hypodermal cells, hypodermal seam cells, vulval precursor cells and, through distal tip cell migration, somatic gonad precursor cells. In early embryos, regulates the orientation of the mitotic spindle of blastomeres and specifically, along with dsh-2, is required for the correct mitotic spindle orientation of the ABar blastomere division plane. Controls the polarity and the asymmetric localization of downstream components of the wnt/beta-catenin asymmetry pathway, and in particular, controls the asymmetric localization of the wnt receptor lin-17/Frizzled in ectodermal blast B cells. May act redundantly with dsh-2 to regulate the expression and nuclear localization of the beta-catenin homolog wrm-2, but alone seems to be required for the polarity of wrm-2 during the asymmetric cell division of hypodermal seam cells. Also, maintains the polarity and migration of QL neuroblasts in larvae. During the embryonic development of touch receptor neurons, may act redundantly with dsh-1, downstream of wnt signaling ligands and the wnt receptor lin-17/Frizzled, to direct the growth of neurites of touch receptor neurons towards the anterior of the body of the worm and towards the PLM touch receptor neuron and other tail neurons. May play a role in the guidance of posterior D-type motor neuron axons along the anteroposterior axis.
Subcellular Localization:
Cytoplasm, cell cortex. Cell membrane. Cell junction. Cytoplasm. Note=Mainly localized to the cell cortex, but localizes to the cytoplasm following dorsal intercalation during hypodermal morphogenesis. Localizes in puncta in the cytoplasm during interphase prior to seam cell division. Localizes in puncta in the cell cortex or cell membrane prior to and after asymmetric blast B cell division.
Domain:
The DEP domain is required for cell membrane localization.
Sequence:
MEPPCTSDCSQIKVFYYLDDETTPYVSVIEAREGVATLGNFKNSFTKRGYKYYAKELDPDIQREVKVELTTDSDRLRKSQNGFYEIFLVSTPGYGTLPRNSGTMTRPQRTALDKRRRRSADFDATPYSDASLAPSTIVSRRAGEHLAELYTSNSEDPYQYDEHTRRTGDDSSLYEPLAARDMNKIYDDDRRRKKQKKERFRRPYVPSTISSATESSVNSGLPRILEIYLPMKNVPYLGLSVCTIDGHIFVSEIAPEGAVEKDGRVNVGDQILQVNRVSFEELSGPQAVRSLREAASSKRPITLYISKFARGAPSEYDDPLASMASETMPLDVGVWVETAVQNTEKMKALGLDPQEQTATTIDDGTLPFTSTASDDEERMLYDQRRNGIPRALIEEAERKRENEQNEKIEQLTEMIDPIIVVRSMARPDSGLAVKNRKWLKILVPMSFIGRDLVDWLVDHMADIHNRKKARIYAARLLAAGLIRHVVSKLTFTEKCYYVFGDGILGNDRNSTDTTGTSGTTMRVEATTEVTYVGSPAPHALAARVGRNIPHRLETTTLSPVAHDQTWLRRRRDCESPMTNDYASMVGESQIGMNPVGNYHVFGTKNNHRQVPAPSQVTSSSLTNGSGGLGGPPPTPLSSTMVLAASPIQSQNAVNHDFDGENSSNSRTRILRT
The following text describes a protein:
Function:
Involved in lipid metabolism and lipid droplet (LD) morphology, number, and size. Supports the formation of small-sized LDs and modulates triacylglycerol accumulation. Induces probably a reorganization of the endoplasmic reticulum into LD-forming domains.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Localized to the lipid droplet-forming sites.
Domain:
The N-terminal domain (1-230) determines the lipid droplet size.
Sequence:
MESESESSSTHSSCDRFLDAEDEFFYDSFSNHYDCLNSSPPANLRRRRLPMDTDSSSSSSTSSLESCEKRSTVGENDELEVSLVDFETIEIDVDVTDSANSSIDSISEKGEDFEVIDSCTDTEKNMGENDSGRVDPFTVTTLNDERGEIYTGPEYTSTDWSLTSLVIRSIEFQVSLMITFIRFPPWLISKCLSFVFDPYRTMRRGRRYLVSWIVGLCDSGLKDDKPVLELVRRVTWGLFCAVYVGIMLFALLVSAFMISGFVITYLAHEPLVIKESLNFDYTKSSPEAYVPISSCAGVAFGLSGKESIETGKVKGLKDRTEITVSMTLPESEYNRNLGMFQVRVDFLSASGHVLASSRRPCMVKFSSEPIRLVQTLLKIAPLVTGYVSEIQTLNLKLKGLVEKDIIPTACLKIMIEQRAEFRPGAGIPEIYDASLFLESKLPFLKRIIWNWRKTLFVWISMSLFIMELLFALVFFRPLIIPRTGQRTQQRDGTHSINNNLYLDGQAGSR
The following text describes a protein:
Function:
Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Early endosome. Membrane; Multi-pass membrane protein.
Sequence:
MGASSDNVTGFVLAVCSSVFIGSSFIIKKMGLKKAGATGKRAGAGGHAYLYEPWWWFGMISMIVGEVANFAAYAFAPALLVTPLGALSIIFSAILAHFILKERLHIFGVLGCALCMVGSTTIVLHAPHERVIHSVKEVWQLATEPGFLIYMCIVVVVVCILIFYCAPRYGTTYLVIYVGICSLTGSITVMSVKAVSIAMKLTLEGNNQFIYFQTWFFTIIVIGCCLLQINYLNKALDTFNTAVVSPIYYVMFTSFTIFASIIMFKEWDTQDASQIATEVCGFITILSGTFLLHKTKDMGNRPIESPVFVSTPQNVSSHSGT
The following text describes a protein:
Function:
Plays a role in the recruitment of the exosome to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Nucleus.
Sequence:
TLGRMVDDDYPQELNDVFRSFDSKLSTAEKTLQPLFKNQRCDLTREMEPLEIAKLDLVTAYAVNSFYWTYLIASGVNPKTHPVKQELDRIKTYMGKVNEIENRKNAPRLEKEAAKRFIRSAMFDSDDKKKDEDHKPTSTVDQPKPSAPTSDPKTPESSLPKQQSSNKDWNKKRTNKRRRSKSSKKKKVDES
The following text describes a protein:
Function:
Uptake of 3-(3-hydroxyphenyl)propionate (3HPP) across the cytoplasmic membrane. Transport is driven by the proton motive force. Does not transport benzoate, 3-hydroxybenzoate or gentisate.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSTRTPSSSSSRLMLTIGLCFLVALMEGLDLQAAGIAAGGIAQAFALDKMQMGWIFSAGILGLLPGALVGGMLADRYGRKRILIGSVALFGLFSLATAIAWDFPSLVFARLMTGVGLGAALPNLIALTSEAAGPRFRGTAVSLMYCGVPIGAALAATLGFAGANLAWQTVFWVGGVVPLILVPLLMRWLPESAVFAGEKQSAPPLRALFAPETATATLLLWLCYFFTLLVVYMLINWLPLLLVEQGFQPSQAAGVMFALQMGAASGTLMLGALMDKLRPVTMSLLIYSGMLASLLALGTVSSFNGMLLAGFVAGLFATGGQSVLYALAPLFYSSQIRATGVGTAVAVGRLGAMSGPLLAGKMLALGTGTVGVMAASAPGILVAGLAVFILMSRRSRIQPCADA
The following text describes a protein:
Function:
May mediate microtubule plus end-directed vesicle transport.
Subcellular Localization:
Cytoplasmic vesicle, autophagosome. Endosome. Lysosome.
Sequence:
MAGSSGESQLQRIIRDLQDAVTELNKEFTEAGEPITDDCVSLHKFSYKLEYLLQFDQKEKSTLLGHRKDYWDYFSDCLAKVKGANDGIRFVKSISELRTSLGKGRAFLRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLNPKMSSDIIGHLYELTEVQFDLASRGYDLDSAWPTFARRTLSSLGSSAYLWKPPSRSSSMSSLVSNYLQAQEIPSSPNGNNFLNNEPLEGLDELHTELDQAELRQKELQDQIHHLEKENQTLQAAVSFEQQQAQAERENSGRIREENVRLTKMLEELEKQREISYCTQGTVQDLQKCLQVLELNAAEKQSEYSARLEELEASKRTLTRKQKNEELIAKTLLNEKGQQTKQYESALKFEELQKKVRTVEQEKVDACKLNDKHLSQLKVTEEELHLKDDARKELELKLENLTISSKGKEAADLQIQLKDSLECVKSLGGKLEEEREEKVELERSFSLKKTRMEQEVKNTMDQLVLLEIKLSELSQRVNSLEEQKSELVSERDYLRKILEKMEQQKLEDKWRALELREENKLLDENLQNATRQSQVLEERVKTLQKDYQELKQNEDTMKESLSVLEAKLQSTKEHCLQMENNLSSLRKNEESLKTLLKEKDEALQCLESQCKKFQGEIERCRKKVKILEAEKADIENMCLHQTKVIESISSEKTSLEKAQLEHTAEVGRLQEKMMDLQAKFQQTVAEKEKLQGKLDIHETVLNEHKSLALQLKEQNEALNRNHVQELLQCQEQEEGLKKERDQKVHQKAEMEKSVLCLTDELSRVKQCLEMVNMENMEIKDLLHRTNTEMAELGIQICTLTSEKADAEEKLSQLMEELSATKERAAKDQEELHNALSRLSQEKEGLQEKLEDSEIYAATVPDLRTQLETAERQAQSLQEFSKEELSAVKFQLSTEIINYQTKFKAVNEECEHLQRELEKRSQQVSIAEEALKDMQVGCIYGWDKPLSEVLESTYICVLVDLTNGLNICYDNLNKMKSDRDSNEKKLLAELDDLTRTKQFLEERLIELLRDKDALWQKSDALEFQQKLTAEQRWLGDAEVSSCLDCQKEFGWMNRRHHCRLCGRIFCYYCCNNYAMSKQTGKKERCCQSCFKKASNSGSNVTQEESTSSLLASPLSLVQRVIGRKVLNDYLLSLFPRNSTLSSLTFDESDDLQMIQDVEICLLKSGELMLKLPLTAEDIFKFGEANRELFIKSNTYSTIPITVIETGLTISWVFSSEPKSISFSVVYQESEEAPLDQSKVLIPMTRCNSHKETIHGKVKVRNPGIYILIFDNTFSRFISKKVFFHLAAQRPIIYDGSDFP
The following text describes a protein:
Function:
Accepts electrons from ETF and reduces ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MIRSSRLLRVKPQRAVRGVQRVSRAIPSGVTHIPRATVTAHVSNFSTFRVVRQQQFSEDELDVLNSEREKDFVDVAIVGGGPAGLSAAIKIKQLDNEHGNGDLRVIVLEKAPDMGSHILSGAVLEPRALDELIPEWRDDPPEPMTLVTEETMRFFTKKWAIPIPEPPQMHNKGKNYIVSLNQVTKWLAEKAEEVGVEVYPGFSVSELVYRDGNVVGVATNDMGRAKDGKPLDSFERGMEFYARTTLLAEGCHGSLSKQAISKYDLRKDSEPQTYGIGIKEVWEVPDEVFKSGYVAHGLGWPLDTETYGGGFMYHFGDNLVAVGLVTGLDYKNPYISPFKEFQRMKHHPFFAKVLSEGTCIQYGARALNEGGLQSIPKLSFPGGALIGCSAGFLNVPKIKGTHTAMKSGMLAAETIWEQFQAENEAGTPLVVSEAEDLEPELFKTIDLANYEQKFKDSWIYDELHEVRNVRPSFHNPLKNWGGLLYSGIDTFLLRGRVPWTLKHATTDSAATEPASKHKEIDYPKPDGKLSFDLLTSVSRTGTNHDEDEPVHLKLTSDPADAPFKINTEADLAKHTADNWEKYKGVEARFCPAGVYEYIEDDAGDGVRFQINSQNCIHCKTCDIKVPGQNINWTVPQGGDGPKYSMT
The following text describes a protein:
Function:
Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Able to recognize and bind denatured glycoproteins, which are modified with complex-type oligosaccharides. Also recognizes sulfated glycans. Does not bind high-mannose glycoproteins (By similarity).
Sequence:
MGAQPSRRRMTEAQHMALAELPPELLLQVLSHVPPRALVTRCRPVCRAWRDLVDGPSVWLLQLARDRSAEGRALYALAQSCPADRNGHDDFPLCALARFCLLAPLGRNLIYNSCGEQGFRGWEVEHGGNGWAVEKNLTMVPGAPSQTCFVTSFEWCFKRQLVDLVKEGVWQELLDSAQIEIYIADWWGARENCGCIYRLRVRLLDEHENEVVKFSASPNPVLQWTERSCRQVSPDCSLNPGLLQGLSRLH
The following text describes a protein:
Function:
Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier, possibly by linking ZO proteins to the actomyosin cytoskeleton.
Subcellular Localization:
Cell junction, tight junction. Note=Localizes to the apical junction complex composed of tight and adherens junctions.
Domain:
Deletion of the TJP1/ZO1 interaction motif (ZIM) decreases but does not abolish colocalization with TJP1/ZO1.
Sequence:
MERDIYGDMADQHIPVGQGVQIRFIGDLKENGKPRGKRSKQDSYGVAVRVQGIDGQPFVVLNSGDKAKSSFGVQIKSQEPYLNASNTSPPNYQNYSSKPRGPSRSISSESELPENPYGSRGYRPSSSHYSSASDEEQKPRGNIRGSDGLSSLPRPLQASRREELRRSQSHSSLLEPDVEESYDYDHHYSERSSTLDTTYSQSSRDSAWSRSSQKKIDNGDYPSLGYRSATSQQSTSVSNKTKKNGLSTSSPSNQSNEDIDTKPLSSVDSLINKFDIKGQVRGRTARRSQALKDERKRSQSLDGRKNYHDTADSREIIVEKQNEVQTMREPVNASNRSFNRQTLERGDISKTRLTKEWLDQDREEPVILKQQRTVQSEFQLKSTPDLLRDQQPDGSDPTREMIFGILREGSLESENTLRKKTSILLEKLPSLQVQPGEDTISLGSQKKELERKVAELQRQLDDEMKQRMKLETSQGRPKAGMQRLEIELEESKEECSRLKELYEKKKNELSAMSQELMEVRMGKEQVETKLRTMEDKLMDSKEELSHLRAKGGTSPDKLALLKELEEVQDELDEVLQIRQKQEELLRQKDRELTALKGALKDEVANHDKDLDRVREQYQNDMQQLRKNMDNVSQDQLSLESERQKINQVVRNLQRELEESSDEISQWKEMFQKNKEELRSTKQELLQMKLEKEESEDELKETRDRFSLLQSELAQVKKGSVDPGEVASVRKELQRVQDQLKQLSVDKQKVEENLQQREREMSALKGTLKEEVSGRDRETVRLREQLQSEVMHVKKENEGLAKESRRIQDQLKQVLLEKQRHEETVHQRERELSVLKGALKDEVSGRDRETEKLRERLEQDALMTKRSYEELVKINKRLESEKTDLERVRQVIENNLQESREENDDLRRKILGLEAQLKETNTFCDDLQRAESRLKDKINKLEAERKRMEDSLGEVADQEQELAFVKRDLESKLDEAQRSLKRLSLEYEELQECYQEEMKQKDHLKKTKNELEEQKRLLDKSMDKLTRELDNMSNESRGSLQLLQTQLEEYREKSRKEIGEAQKQAKEKTAEAERHQFNSSRMQEEVQKLKLALQELQVEKETVELDKQMISQRLQSLEQDIESKKRVQDDRSRQVKVLEDKLKRMEAELDEEKNTVELLTDRVNRSRDQMEQQRAELNQERSRGQDLECDKISLERQNKELKNRLASMEGQQKPSVNVSHLEAKLQEIQERLQLEEREKATLLSTNRKLERKLKELNIQLEDERLQVNDQKDQLNLRVKALKRQVDEAEEEIERLEGLRKKAVREMEEQQEINEQLQTRVKVMEKESKRKPIRPAHDDDLSSDGEFGGPYDPSSITSLLTESNLQTSSC