lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MQNREQILAMLTTILVDEFEIDADAITPDANLYEELDLDSIDAVDLVIKLQQLTGKKIQPDEFKSVRTVNDVVNAIEGLVKD
The following text describes a protein:
Function:
Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes; Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. Also deubiquitinates non-histone proteins, such as ribosomal protein RPS27A: deubiquitination of monoubiquitinated RPS27A promotes maturation of the 40S ribosomal subunit. Also mediates deubiquitination of tektin proteins (TEKT1, TEKT2, TEK3, TEKT4 and TEKT5), promoting their stability.
Subcellular Localization:
Nucleus.
Domain:
The UBP-type zinc finger binds 3 zinc ions that form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. It recognizes the C-terminal tail of free ubiquitin.
Sequence:
MGKKRTKGKTVPTDDSSESLEPMCRHIRKGLEQGNLKKALVNVEWNICQDCKTDNKVKDKSEEETEENPSVWLCLKCGHQGCGRNSQEQHALKHYLTPRSEPHCLVLSLDNWSVWCYLCDDEVQYCTSNRLGQVVDYVRKQAGITTPKSAAKDNGNIELENKKLEKESKNEQEREKKENMAKENPSTNSPSQITVKGLSNLGNTCFFNAVMQNLSQTPVLRELLKEVKMSGTIVKIEPPDLALTEPLEINLEPPGPLTLAMSQFLNEMQETKKGIVTPRELFSQVCKKAVRFKGYQQQDSQELLRYLLDGMRAEEHQRVSKGILKAFGSSTEKLDEELKNKVKDYEKKKSVPSFVDRIFGGELTSTIMCDECRTVSLVHESFLDLSLPVLDDQSAKKSINDKNLKKTMEDEDKDSEEEKDNDSYMKERNDIPSGTSKHLQKKAKKQAKKQAKNQRRQQKIQGKVLHLNDICTVDHPEDNECEVEMSPQEEVDMNTNHISQEEVVHKDSYVNQKDLNGQEKMIEIVTDNQKSTEEVDMKNTNMDNDLGVLASSPAECSRDLNGAHLKEGSDGEVDISSSFKDLSLNAALQPDEINIEILDDSHTPGTKVYEVVNEDPETAFCTLANRETFNTDECSIQHCLYQFTRNEKLRDANKLLCEVCTRRQYNGPKANIKGERKHVYTNAKKQMLISLAPPVLTLHLKRFQQAGFNLRKVNKHIKFPEILDLAPFCTLKCKNVAEENTKVLYSLYGVVEHSGTMRSGHYTAYAKARTANSHLSNLVLHGDIPQDFEMQSTKGQWFHISDTHVQAVPTTKVLNSQAYLLFYERVL
The following text describes a protein:
Function:
Acts as a chaperone that facilitates biogenesis and trafficking of functional transporter heteromers to the plasma membrane (By similarity). Associates with SLC7A9 to form a functional transporter complex that mediates the electrogenic exchange between cationic amino acids and neutral amino acids, with a stoichiometry of 1:1. SLC7A9-SLC3A1 transporter has system b(0,+)-like activity with high affinity for extracellular cationic amino acids and L-cystine and lower affinity for intracellular neutral amino acids. Substrate exchange is driven by high concentration of intracellular neutral amino acids and the intracellular reduction of L-cystine to L-cysteine. SLC7A9-SLC3A1 acts as a major transporter for reabsorption of L-cystine and dibasic amino acids across the brush border membrane in early proximal tubules (By similarity). Associates with SLC7A13 to form a functional complex that transports anionic and neutral amino acids via exchange or facilitated diffusion. SLC7A13-SLC3A1 may act as a major transporter for L-cystine in late proximal tubules, ensuring its reabsorption from the luminal fluid in exchange for cytosolic L-glutamate or L-aspartate (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Apical cell membrane; Single-pass type II membrane protein.
Sequence:
MNEDKDKRDSIQMSMKGCRTNNGFVQNEDIQEQDPDSRDTPQSNAVSIPAPEEPQLKVVRPYAGMPKEVLFQFSGQARYRVPREILFWLTVVSVFLLIGATIAIIIISPKCLDWWQAGPMYQIYPRSFKDSDKDGNGDLKGIQEKLDYITALNIKTIWITSFYKSPLKDFRYAVEDFKEIDPIFGTMKDFENLVAAVHDKGLKLIIDFIPNHTSDKHPWFQSSRTRSGKYTDYYIWHNCTHANGVTTPPNNWLSVYGNSSWQFDEERKQCYFHQFLKEQPDLNFRNPAVQEEIKEIIKFWLSKGVDGFSFDAVKFLLEAKDLRNEIQVNTSQIPDTVTRYSELYHDFTTTQVGMHDLVRDFRQTMNQFSREPGRYRFMGTEVSAESTERTMVYYGLSFIQEADFPFNKYLATLDTLSGHTVYEAITSWMENMPEGKWPNWMIGGPETSRLTSRVGSEYVNAMNMLLFTLPGTPITYYGEEIGMGDISITNLNERYDTNALLSKSPMQWDNSSNAGFTEANHTWLPTNSDYHTVNVDVQKTQPSSALRLYQDLSLLHARELLLSRGWFCLLRDDNHSVVYTRELDGIDKVFLVVLNFGESSTVLNLQETISDVPTKLRIRLSTNPASKGSDVDTHAVSLEKGEGLILEHSMKTLLHHQKAFRDKCFISNRACYSSVLDLLYSSC
The following text describes a protein:
Function:
Required for biogenesis of the 60S ribosomal subunit.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSSIYKALSGKNQKKKDGNAGAEKQYMNKQRVLLISSRGVTYRHRHLIQDLHSLMPHSRKEPKLDTKKDLGQLNEIAELYNCNNVAFFEARKHQDLYMWLSKPPNGPTVKFYLQNLHTMDELNFTGNCLKGSRPVLSFDKRFDTQPQYRLFKEMFIHTFGVPPQARKSKPFIDHVMSFSIVDDKIWVRNYEISHAARNNSEYEDKQDEDISLVEIGPRFVMTPILILEGAFGGPKIYENKQYVSPNVVRAQLKQEAAKEARARADAAVQRKIKRRDNVLAMDPLSNDALFKN
The following text describes a protein:
Function:
Potassium transporter.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MDLESAIGGHPIKKDSWRAVLTLAYQSLGVVYGDLSTSPLYVYKSTFAEDIKHSETNEEIYGVLSFVFWTLTLIPLIKYVFIVLRADDNGEGGTFALYSLLCRHARVSSLPNCQLADEDLSEYTKDGVDLTNKKTCGSRLKSTLEKHRVLQRVLLVLALIGACMVIGDGVLTPSISVFSAVSGLELSMAKPHHRYVEVPVACAILVILFAIQHYGTHRVGFLFAPVVITWLLCISAIGLYNIFYWNPHVYRALSPYYMYKFLKKTQRGGWMSLGGILLCMTGSEAMFADLGHFSQLSIKIAFSFVVYPSLVLAYMGQAAYLSQHHGDSNYQVGFYVSVPEKLRLPVLVIAILAAVVGSQAVITGTFSIIKQCSALGCFPRVKIVHTSSKIHGQIYIPEINWTLMLLCLAITIGFRDTKRMGNASGLAVITVMLVTTCLMSVVIILCWHKSFVYAIAFILIFGSIESLYFSASLIKFREGAWVPIALSLIFLIVMYVWHYGTRKKYEFDVQNKVSINWLLGLGPSLGIVRVRGIGLIYTELVAGIPAIFSHFVTNLPAFHQVLVFLCIKSVPVPHVRPGERFLVGRVGPKEYRLYRCIARYGYRDIHKDDMEFEKDLVCSIAEFIRSEKAETSVKLEDAEESERMTVVGTSSTNVDGVRMCEDEGETAETSEVREIKSPKKLRKRVRFLVPESPQMETEARRELQELMEAREAGMAFIMGHSYVKAKRGSGWVKKVVINYGYDFLRRNSRGPSYAWSVPHASTLEVGMVYQV
The following text describes a protein:
Function:
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. Acts together with the RNase R to eliminate defective 70S ribosomes, but not properly matured 70S ribosomes or individual subunits, by a process mediated specifically by the 30S ribosomal subunit. Involved in the processing of 16S, 23S and 5S rRNAs, with a particularly strong effect on maturation at both the 5'- and 3'-ends of 16S rRNA as well as maturation of the 5'-end of 23S and 5S rRNAs.
Subcellular Localization:
Cytoplasm.
Sequence:
MSQVILDLQLACEDNSGLPEESQFQTWLNAVIPQFQEESEVTIRVVDTAESHSLNLTYRGKDKPTNVLSFPFEVPPGMEMSLLGDLVICRQVVEKEAQEQGKPLEAHWAHMVVHGSLHLLGYDHIEDDEAEEMEALETEIMLALGYEDPYIAEKE
The following text describes a protein:
Function:
Structure-specific DNA-binding protein involved in DNA repair by promoting RAD51-mediated homologous recombination. Acts by stimulating D-Loop formation by RAD51: specifically enhances joint molecule formation through its structure-specific DNA interaction and its interaction with RAD51. Binds single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures: has a strong preference for branched-DNA structures that are obligatory intermediates during joint molecule formation. Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during homologous recombination and DNA repair. WDR48/UAF1 and RAD51AP1 also have a coordinated role in DNA-binding to promote USP1-mediated deubiquitination of FANCD2. Also involved in meiosis by promoting DMC1-mediated homologous meiotic recombination.
Subcellular Localization:
Chromosome. Nucleus. Chromosome, telomere. Note=Colocalizes with RAD51 to multiple nuclear foci. Colocalizes with DMC1 on meiotic chromatin.
Sequence:
MVRPTRNRKPINYSQFEDSGNDSDDDFISSSTPVNKSKTVPKVLKQDKPKPNLKNLQKEEVLPTEPPKKRVALDDKVFQRGLEVALALSVKELPTLTNQVKKSKEKSTDKQGKEKTENTGKPPRVSNCSVASDDVEDLDKITEEGDASSVEGERKSPSQAKAPRRRAPSEGSDGSSANDTESESATGEGSESDPDFDESKESDEDFGVRRSKESKKKTVQKKPAGEKKERKSKPKCEASVTSVDPAPAAIKSGSPSLPQAVGLPSEATRKPAIMCSPSAESKRPKWVPPAASGSRNSSSNALAGTPAKSPSQSLRLGLSRLAPVKRLHPSATSSQVR
The following text describes a protein:
Function:
Promotes meiotic crossing over formation through its interaction with CNTD1 by participating in the crossover differentiation step of crossover-specific recombination intermediates.
Subcellular Localization:
Nucleus. Chromosome. Note=Co-localized at crossover sites with CNTD1. Localizes on synapsed chromosome only in mid/late pachytene spermatocytes.
Sequence:
MDPGEPAPKPFQQPEKPGRVRRRKTRRERNEALAGSRQPLTYQHPPVASRDPHMVLRNSVAPTAAKLVVITQGRLSRDHRGLFNHEVKSLDVARLLSSESLELGTPALTTKSSPSPGRGQQPSLQSRGKENQVPGGSGPGPPSPPQLPDLEQLLGELQCQLILPRAFPRRNLVQEARDAIVGTLQACHGCVPDLTLVLRGCQPHLPGTDPGALKRQRMTPSWINSPEQAPGEGRQRRRQGTKELTFAVPPTSSTPTVHQVSLAPPKGPWPPPLSSLPSPSGAAWGPPTAFDLLKSIWLVATPPPPRPWGIGPPQLLPQPPSPLLPRSSALDWSPSPPAPLPSLSWMVAQSSPEAWSFPPMRLY
The following text describes a protein:
Function:
Acts as a ribosome collision sensor. Detects stalled/collided disomes (pairs of ribosomes where the leading ribosome is stalled and a second ribosome has collided with it) and endonucleolytically cleaves mRNA at the 5' boundary of the stalled ribosome. Stalled/collided disomes form a new interface (primarily via the 30S subunits) that binds SmrB. Cleaved mRNA becomes available for tmRNA ligation, leading to ribosomal subunit dissociation and rescue of stalled ribosomes.
Domain:
Has a probably flexible N-terminal domain and a conserved C-terminal SMR domain; the N-terminal domain is required for ribosome binding via uS2.
Sequence:
MKKKTTLSEEDQALFRQLMAGTRKIKQDTIVHRPQRKKISEVPVKRLIQEQADASHYFSDEFQPLLNTEGPVKYVRPDVSHFEAKKLRRGDYSPELFLDLHGLTQLQAKQELGALIAACRREHVFCACVMHGHGKHILKQQTPLWLAQHPHVMAFHQAPKEYGGDAALLVLIEVEEWLPPELP
The following text describes a protein:
Function:
Acyltransferase which catalyzes the transfer of an acyl group from an acyl-CoA towards a lysophospholipid producing a phospholipid and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. Acts on lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) and lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE), and to a lesser extend lysophosphatidylcholine. Prefers oleoyl-CoA as the acyl donor and 1-oleoyl-LPE as acceptor. May play a role in neurite outgrowth during neuronal differentiation.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAARPPASLSYRTTGSTCLHPLSQLLGIPLDQVNFVACQLFALSAAFWFRIYLHPGKASPEVRHTLATILGIYFVVFCFGWYAVHLFVLVLMCYGVMVTASVSNIHRYSFFVAMGYLTICHISRIYIFHYGILTTDFSGPLMIVTQKITTLAFQVHDGLGRKAEDLSAEQHRLAVKAKPSLLEYLSYHLNFMSVIAGPCNNFKDYVAFIEGRHIHMKLLEVNWTQRGFQSLPEPSPMGAVIQKLCVTLMSLLLFLTLSKSFPVTFLIDDWFVHKANFLSRLWYLYVVMQAAKPKYYFAWTLADAVHNAAGFGFNGMDTDGKSRWDLLSNLNIWKIETATSFKMYLENWNIQTSTWLKCVCYERVPWYPTVLTFLLSALWHGVYPGYYFTFLTGVPVTLAARAVRNNYRHHFLSSKARKIAYDVVTWAVTQLAVSYTAAPFVMLAVEPTISLYKSVFFFLHIICLLIILFLPIKPHQPQRQSRSPNSVKKKAD
The following text describes a protein:
Function:
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Subcellular Localization:
Nucleus.
Sequence:
MIQQLPMVNVELMISNLRILVESKQFSSAEFLGNFVISVPNQQKTPHQNIISFSLFGDSLFGKNEFVRSLKYFKQSLDILFKVYNNPNNNNNNNNKQADFDNKQFEYELKYKISLCYIKINRNNLAISYLESIPFSSRGLDTHLTIARLYKDIGKEKSKECIISYKEVIKLCPLCLEAINSLKEMGENVDQVLIPSINKFQQKNNSFNSNNIIDLSWISLLSMSQYEMKRNQPEKSLILLKKVESKFSTNLYVLEKLALSYLYHDEPSIINTFNIFQKIRLLDPYYIGSMDIFCSLLKRRSLQFELNKVCNDLVASNPYCAETWTSVALFYFLKENVEKSLENVDRAISIKESHEFAHSLKGEILLSLDEPREALPSLERAFQLSKNILTARELVRCHLILNQMKEALVVAETINNLSPDYSKTMALLGMVLANQPEEREEARKILTKALTLSPHCTDTVLTLSKLNVVEGRFQEAIDILNSQLEYQETDLMHTEIAGVYLTKDYHEDAMIHYNSALEINPQYEPASRGIARLELIMKGIDPDQELDQENDDDDQEEGEGENDQEENDDDDNDDDDEYIS
The following text describes a protein:
Function:
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MSPQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVVGEDNQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRARGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVQARNEGRDLAREGNEIIRSACKWSPELAAACEIWKAIKFEFEPVDKLD
The following text describes a protein:
Function:
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Subcellular Localization:
Cytoplasm.
Sequence:
MNFGNVSTAMITPFDNKGNVDFQKLSTLIDYLLKNGTDSLVVAGTTGESPTLSTEEKIALFEYTVKEVNGRVPVIAGTGSNNTKDSIKLTKKAEEAGVDAVMLVTPYYNKPSQEGMYQHFKAIAAETSLPVMLYNVPGRTVASLAPETTIRLAADIPNVVAIKEASGDLEAITKIIAETPEDFYVYSGDDALTLPILSVGGRGVVSVASHIAGTDMQQMIKNYTNGQTANAALIHQKLLPIMKELFKAPNPAPVKTALQLRGLDVGSVRLPLVPLTEDERLSLSSTISEL
The following text describes a protein:
Function:
Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form. The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form.
Subcellular Localization:
Cell projection, dendritic spine. Cell projection, axon. Synapse.
Domain:
The central Dbl homology (DH) domain functions as a guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form. The C-terminus is a Rho-GAP domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. The protein has a unique structure having two opposing regulatory activities toward small GTP-binding proteins.
Sequence:
MEPVSHQDMPRLSWIDTLYSNFNYGTDGYDAEGNEEHKNSREGSETMPYIDESPTMSPQLSARSQDSVDGVSPTPTEVLLPGGESESDKGLLMRKLVLSGVLASEEIYINQLEALLLPMKPLKATASTSQPVLTLQQINDIFYKIEDIYQMHKDFYDKLCPIVQQWDNKTTVGHLFQKLATQLGVYKAFVDNYKFALETAEKCSQCNVQFFKISEDLKVKGPKDSKEQPQSVTMEALLYKPIDRVTRSTLVLHDLLKHTPTDHPDYPLLQDALRISQNFLSSINEDIDPRRTAVTTPKGEPRQLVKDGFLVELSENSRKLRHLFLFTDLLLCAKLKKTTVGKHQQYDCKWYIPLADLVFPSLEESEPIHQLHATPDYEIEEMKAKISVLKSEIQKEKKSNKGSSRAIERLKKKMFEYESWLLLYSPTIPFRIHNKNGKSYLFLLSSDYERSEWREAIQKLQKKDLQALALSPFELQVLTASCFKLRTVHNVPIISHKDDDESPGLYGFLHVIVKSAKGFSHSSNFYCTLEVDSFGYFVSKAKTRVFRDTSEPEWNEEFEIELEGSQCLRILCYETCYDKSKLNKDNNEIVDKIMGKGQIQLDPQGVQSKNWHDDVIEMNGIKVEFSMKFSSRDMSLKRTPSKKQTGVFGVKISVVTKRERSKVPYIVRQCIEEVEKRGIEEVGIYRISGVATDIQALKAAFDANSKDILMMLSDMDINAIAGTLKLYFRELPEPLLTDRLYLAFMEGIALSDPAAKENCMMHLLRSLPDPNLITFLFLLHHLKKVAENEPINKMSLHNLATVFGPTLLRPSEVEIKGHMNLASDIWSHDVMAQVQVLLYYLQHPPISFSELKRSTLYYSTDV
The following text describes a protein:
Function:
Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs). Plays a role in chemotaxis and sensory perception. Required for entry into and exit from the dauer larval stage and this may be mediated by daf-12, daf-16 and daf-41. Controls the behavioral response, namely the avoidance response, and pathogen-responsive gene expression in the response to pathogenic bacteria such as E.coli and P.aeruginosa.
Subcellular Localization:
Cell projection, cilium. Note=Shuttles at the same rate as intraflagellar transport (IFT) complex B proteins such as osm-1, osm-5 and osm-6 along the cilia of the amphid and phasmid sensory neurons.
Sequence:
MRPNLLWVDKILDENNEAGVCIYDLAFKPDGSELLLAADNKVYLFDVNEGGQMQTLKGHKDLVYTVAWSHNGELFASGGADKLVILWNEKHEGTLRYSHTDVIQCMMFNPCNQILLTCALNEFGLWSTADKNVIKQRSVVRCCSCAWNTDGTIFAIGHGDGTITLRKGTNATEEPSIIIQRDNEPIWGIAFSSNRTFASRDSQGNPMGIDEIMAVIDWNKTLSFYSLDGTFIESKNLEFEPHCISYCLNGEYLLIGGSDKILKIYTRKGVLLGTVAQMDHWIWSVTVRPNSQTVAMGCVDGTIACYNLVFSTVHCVDHARYANRKSMTDVFVQNLEYRTSSNICCHDLVKKMSLYDTKLAVQLSDKIQIYKQTGGVSKNERRKQLKYTLQDTIRKDLSFSLMVVTHGHLVVCNDEKLECYDFKGIKKRSWNMKSIVRYLRVLGGPAHRETLVLGTTDGGVYKVFIDNDYPILLDSRKTAIKCIDINANRTVLASIEDTLVCKWSDIATGETLLQEPGCYSVVFNTVNENLFAFTTNNMLHVRTLAAPGHTTRGVGYVLGFVKNRTFCLVQYNLIPLEVPYTIHLYQYIERGDFKEALRIACLGVVKNDWKYLANKALDALEFDVARKAYKRVRDRKMLRMVWELKKMKSNGEPDAILRATILAYTKKFREAAKIFKENGFENRAMELFTDMRMFDDVQEVMTTASGETKKMLMRKRASWARDANQPKIAAEMLISSGDLDKAALLIIDNDWLELAIEISHKIDRSDLETMKKLSAYFIRKHEFGLASRIFQSINDMKSIVDMHVNAGHWTDAFAIADRHPKYVEDVYLPYARFLAERDRFEEAQKAFHRAGKEQEAMHVLEQLTSNSVNENRFADAGFYYWLLSQQYLDRSQTEENLTLLNKAKEAASLADAYYAYYPVFIFCSQPFSFERNENILNMARYLTFTPYIDNISKVFVYFTIAKIANEMGAYKSARTALDQLTNLRVLPQFELDGQIEVMTLNIRAKPFTDVESMQPMCYRCGLNNPLLGGMSCIHCETPFIISFVSFDILPLIEFKIENDISFDEAKELIESEPPLSDDDYNPLRGLKKGIKEIILNRESLSKLEQGHVIIQTFPPPLAPKFLFNVMPSITIAQCKGCNKVFDLDDFEMACLRKGHCPFCRTSYDRNEAFFVDEEEDEDNTNIPSFGQFSRFS
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSGIPTIVTLDEPLSVLAVPDSELKKQALAKVKEALDPLSEQYSVLDQIHVQDMDAEMVWAQAKMVIDGVCDKMIGEVFPKYGKIQPDSEQEDEEEESDDESQYESAQEEVPGEEVVGEEEDEGVDVFDDGDEDDEDDTEEDNEGSDVDMDMDNLVDDYEDEEEKEDDDEEEEEEEEEEDDSGGEEKPDKFGLNDGFFDIDKFNKQIMAMEADNFGEDGPDFDWNKELGEQSDDSVDDIKYDDFFGKAKFDKKLQYEQRVAKRQKLAEQALENKDEESDDESDNEAGSDDNEADFDMEGSGDENEYEDMINSVKKDLFEEDIAEDTPEHLSTFEKQQREIMKQIAQYEKENVGEKKWTLKGEARAAQRTKDSLLEEDLDFERGAKPVPVMTQAVTESLEDMIKARIKSGQFDDLPRRFFDDLPQFKKSKLIEVSEQKSQKSLADLYEAEAMGETEPSTTNEPPNEMRDAAHREIEDLYADVAYTLDSLSSWTYKPKPTKSIQIVTNAPAISMEEAQPQALAQEEQLAPQEVYKPEVADKRERLAGSTGLPQTKAEMTREERKRAKKKEKIARGKQLAEKEERQRSLAVHSKEGDAKGSKAQVMETLKQGNVTVIGKRGEKRGLDGKLKRDQKAKDGYSLKL
The following text describes a protein:
Function:
Required for assembly of smooth septate junctions (sSJs), together with Ssk and mesh. Important for barrier function of the midgut epithelium.
Subcellular Localization:
Apicolateral cell membrane; Multi-pass membrane protein. Cell junction, septate junction.
Sequence:
MGIGYGASDEQLEKQIGCVKYTLFCFNIVAWMISTALFALTVWLRAEPGFNDWLRILEAQSFYIGVYVLIGISIVMMAVSFLGCLSALMENTLALFVFVGTQVFGFIAIVAGSAVLLQFSTINSSLQPLLNVSLRGFVATSEYTYSNYVLTMIQENIGCCGATGPWDYLDLRQPLPSSCRDTVSGNAFFNGCVDELTWFFEGKTGWIVALAMTLGLLNVICAVMSFVLVQAVKKEEEQASNYRR
The following text describes a protein:
Function:
Segment polarity protein. Functions together with arm to transduce the Wingless (Wg) signal in embryos and in developing adult tissues. Acts as a transcriptional activator, but in the absence of arm, it binds to gro and acts as a transcriptional repressor of wg-responsive genes.
Subcellular Localization:
Nucleus.
Sequence:
MPHTHSRHGSSGDDLCSTDEVKIFKDEGDREDEKISSENLLVEEKSSLIDLTESEEKGHKISRPDHSPVFNKLDTHAPSFNMGYLVSPYSYANGSPSGLPVTMANKIGLPPFFCHNADPLSTPPPAHCGIPPYQLDPKMGLTRPALYPFAGGQYPYPMLSSDMSQVASWHTPSVYSASSFRTPYPSSLPINTTLASDFPFRFSPSLLPSVHATSHHVINAHSAIVGVSSKQECGVQDPTTNNRYPRNLEAKHTSNAQSNESKETTNDKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHELSREEQSKYYEKARQERQLHMELYPGWSARDNYGYVSKKKKRKKDRSTTDSGGNNMKKCRARFGLDQQSQWCKPCRRKKKCIRYMEALNGNGPAEDGSCFDEHGSQLSDDDEDDYDDDKLGGSCGSADETNKIEDEDSESLNQSMPSPGCLSGLSSLQSPSTTMSLASPLNMNANSATNVIFPASSNALLIVGADQPTAQQRPTLVSTSGSSSGSTSSISTTPNTSSTVSPVTCMTGPCLGSSQERAMMLGNRFSHLGMGLSPPVVSTSTSKSEPFFKPHPTVCNNPIFALPSIGNCSLNISSMPNTSRNPIGANPRDINNPLSINQLTKRREYKNVELIEASESKTIVAHAATSIIQHVAVNGYHANHSLLNSNLGHLHHQLNNRTENPNRSEQTMLSVSNHSVNSSECHKESDSQAIVSSNPPNAGSSDNGVISVS
The following text describes a protein:
Function:
Palmitoyltransferase that could catalyze the addition of palmitate onto protein substrates including the D(2) dopamine receptor DRD2, GSK3B or MAVS. Mediates GSK3B palmitoylation to prevent its AKT1-mediated phosphorylation leading to activation of the STAT3 signaling pathway. Also catalyzes MAVS palmitoylation which promotes its stabilization and activation by inhibiting 'Lys-48'- but facilitating 'Lys-63'-linked ubiquitination.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Domain:
The C-terminal di-lysine motif confers endoplasmic reticulum localization; The DHHC domain is required for palmitoyltransferase activity.
Sequence:
MDFLVLFSFYLAFLLICVIMICIFTKSQRLKAVVLGGAQVCARVTPQCFQRAVQTLLHQLFHTRHPAFLALHLLLQGLVYAEYTYEVFSYCRELEFSLPCLLLPYVLLSVNLVFFTLTCSTNPGTITKTNVLLLLQVYEFDEVMFPKNSRCSTCDLRKPARSKHCRVCDRCVHRFDHHCVWVNNCIGAWNTGYFLIYLLTLTASAATIAILSAAFLLRLVAVSNLYQETYLDDLGRFQAVDTGFLIQHLFLAFPRIIFLLGFVIVLSLLLAGYLCFALYLAATNQTTNEWYRGDWAWCQHWPLVAWSPSAEPQIHQNIYSHGLWSNLQEVFIPATPSYKKKKR
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Sequence:
MIEYMEYVLRQFERTTSWDRDYSYENITATSDNLLQFEIPDSLNLQISNQSTPNTFNTFELSNRSIINGSLSYLYTDCGQLDKIVQNSLKVPLQQRVDTYQCLRPGRTLGTSFRSQMLLYGRMYWPGSILEAMYCKRLTPQSQLVLKSLLSAAGESSILTLYWQRNAPWGSQDIVFSTNELLLGYRFLHNLSPGRSHEGSPHGQSTLSLGAEFWLGISNLLPGCSTALRYCTHATNTGKPITLTLSLNPLFGHISSSYSVKFSPGTTFCSKYDFNVYSIESNLSFGCEFWKSSAAAHKQATNEEETSIEVATETPVSDPRYCGAVPGARSFDQIRPFAELPSDNQLYHQLMMPNSSNALIDNVNLPFPSPLLRYPPEKSVTDKFAAMIDATQFTSVLKMSSSLRDKNLRLLWEGKYKGFLVSAGAELTTIPLEAPKTINEITAQQVPRPLWLRPAKFGIQIQYST
The following text describes a protein:
Function:
Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling.
Subcellular Localization:
Vacuole, aleurone grain. Endoplasmic reticulum. Protein storage vacuole. Note=Localizes in protein storage vacuoles in cotyledons of developing and mature beans. Synthesized and assembled into trimers in the endoplasmic reticulum, and transported to the protein storage vacuoles by the dense vesicles.
Sequence:
MMRVRFPLLVLLGTVFLASVCVSLKVREDENNPFYLRSSNSFQTLFENQNGRIRLLQRFNKRSPQLENLRDYRIVQFQSKPNTILLPHHADADFLLFVLSGRAILTLVNNDDRDSYNLHPGDAQRIPAGTTYYLVNPHDHQNLKIIKLAIPVNKPGRYDDFFLSSTQAQQSYLQGFSHNILETSFHSEFEEINRVLLGEEEEQRQQEGVIVELSKEQIRQLSRRAKSSSRKTISSEDEPFNLRSRNPIYSNNFGKFFEITPEKNPQLRDLDIFLSSVDINEGALLLPHFNSKAIVILVINEGDANIELVGIKEQQQKQKQEEEPLEVQRYRAELSEDDVFVIPAAYPFVVNATSNLNFLAFGINAENNQRNFLAGEKDNVVRQIERQVQELAFPGSAQDVERLLKKQRESYFVDAQPQQKEEGSKGRKGPFPSILGALY