lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
Subcellular Localization:
Nucleus, nucleolus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MDIFKVLSRGATIQRNGKHRKDLTLLNHAAPKDTQDNVDIEVARETDFFKTKTDTYSKKRVAEEAELDNEEEEEAPPPIISTPEEAVVFRNKHKINITGEDSPLPIGSFEDLITRFNLHPYLLANLKKNKYTDPTPIQCESIPTMLNGRDLIACAPTGSGKTMAYSIPMVEMLGKKKGSKDAKKGIKALVVAPTKELASQIFNAVFSLCVGVGKKKDELKPCLLDKSTADKLRNGKVSSQKYDICITTPLRLVSALNDGSLDLGSLDLVIFDEADKLFEKGFATQVDDILAACPSGIQKTLFSATIPASVEQLANSIMSTDPLRIIIGNKQAAAQTVEQKLVYAGNEEGKLVAIRQMAREGQLVAPVIIFLQSIDRAKALFKELVFDGINVDQIHGDMTAAKRASVIDRFRNGEVWVLICTDVLARGIDFRGINLVINYDVPQSAQSYVHRIGRTGRAGRLGKAVTFFTKEDATNVKVVVNVMKQSGQEVPDWLNNLAPLTQKERDNIKNRPIKRKKISTQHALANNKKKRAKQQMKGLKKMKKDDE
The following text describes a protein:
Function:
Involved in lipid metabolism and lipid droplet (LD) morphology, number, and size. Facilitates initiation of LD formation, and ensures that vectorial budding of LDs from the ER is directed towards the cytoplasm.
Miscellaneous:
MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Concentrates at endoplasmic reticulum lipid droplet junctions.
Sequence:
MKINVSRPLQFLQWSSYIVVAFLIQLLIILPLSILIYHDFYLRLLPADSSNVVPLNTFNILNGVQFGTKFFQSIKSIPVGTDLPQTIDNGLSQLIPMRDNMEYKLDLNLQLYCQSKTDHLNLDNLLIDVYRGPGPLLGAPGGSNSKDEKIFHTSRPIVCLALTDSMSPQEIEQLGPSRLDVYDEEWLNTIRIEDKISLESSYETISVFLKTEIAQRNLIIHPESGIKFRMNFEQGLRNLMLRKRFLSYIIGISIFHCIICVLFFITGCTAFIFVRKGQEKSKKHS
The following text describes a protein:
Function:
Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Subcellular Localization:
Cytoplasm.
Sequence:
MEELLSKQREECKELQSKITNLRKQLKEGNKKQKRALQQKISQMEADLSQKHATERQKLDKGDEETNETQQEDLLNTLLQQMEDTKITTAEKSSVQSSLNTKENTPQQPKKSRNRQKERLERRKAEMKKMSEQAELESEKMADLKNEEKKKFSKILEEAGLVAVDIPADGNCLFASISHQLNYHHNVKLNSQALRNKSADYVLKHCEQFEGFLLDEESGEVLPVSDYCNEIRNNSKWGSDIEIQALANSLEVPVHVYNTEGPVLKFNPSTVKFEKPLCIAYYQHLFGLGAHYNSLLYRDN
The following text describes a protein:
Function:
Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA.
Subcellular Localization:
Cytoplasm. Note=After completion of the hook-basal body structure, it is exported out of the cell through the completely assembled hook-basal body structures.
Domain:
The N-terminal domain is essential for export and the C-terminal domain possess the FliA binding site.
Sequence:
MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK
The following text describes a protein:
Function:
Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions.
Subcellular Localization:
Nucleus.
Sequence:
MGKGKVSAKPPTRKRMDKLDMAFSCPFCNHGSSVECLIDMKNLTGEANCQICQKSFSTTANGTSKSYIKLHIVPPNIAVDAILIGSQLENYAPGTSFGFVPSQPNDCNSGNGL
The following text describes a protein:
Function:
Required, together with the TRAPP II subunit TRS33, for TRAPP II complex assembly or stability, and for proper Golgi localization of TRAPP and the Rab GTPase YPT31.
Miscellaneous:
MISCELLANEOUS: Present with 8660 molecules/cell in log phase SD medium.
Subcellular Localization:
Golgi apparatus, trans-Golgi network.
Sequence:
MSLRPCFVSLIDESDKPILIYVPNEAENEMNDVLKYNVLSNISLDYFESALVEWHSLDSKPLLKSIFQLEGVSVFAMLIKQTGLKIVIGFEQKSLSGADDEFEAINQIFETVRKIYIRVKCNPLLVSGDEKSIIKSLERKFDELFISTEVEL
The following text describes a protein:
Function:
One of the extrinsic, lumenal subunits of photosystem II (PSII), which stabilize and protect the oxygen-evolving complex. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. Plays a role in the stability of the oxygen-evolving center on the luminal side of PSII. Required for optimal photoautotrophic growth in the absence of Ca(2+) or Cl(-), functions in optimizing PSII water oxidation/O(2) evolving activity. Requires PsbO to bind to PSII.
Miscellaneous:
MISCELLANEOUS: When crystallized in the presence of Zn(2+) this protein dimerizes, but neither Zn-binding nor dimerization are thought to be physiologically relevant.
Subcellular Localization:
Cellular thylakoid membrane; Lipid-anchor; Lumenal side. Note=Associated with PSII at the lumenal side of the thylakoid membrane, binds to the large lumenal domain of PsbC (CP43) between PsbO and PsbV. Contacts CP47 (psbB) and PsbO.
Sequence:
MSRLRSLLSLILVLVTTVLVSCSSPQVEIPTTYSPEKIAQLQVYVNPIAVARDGMEKRLQGLIADQNWVDTQTYIHGPLGQLRRDMLGLASSLLPKDQDKAKTLAKEVFGHLERLDAAAKDRNGSQAKIQYQEALADFDSFLNLLPQAS
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MAANFLRLLQRGGFQSHFSPKGGIQNSLQLRVSPKNCKGQKRNITGNPERYPGADFNYPKTKKFFWATPPKYHERLFLRDVAKYYALTGVPALIIITFINVFIGPAELSEIPEDYEPEDYEYHDHPITRFIVRNFMPPYQEVYEKMCAKIDFENEKRQWRQKHKMVDYLMKERGDGLYHYIPMTPTEVIDYSPKSDPDQ
The following text describes a protein:
Function:
ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Subcellular Localization:
Nucleus.
Domain:
The DBINO region is involved in binding to DNA.
Sequence:
MAAAPLRRGMMVMGRIARILPTRLSKSAITDSQPKHEGSWLYTLENPPNLSWLRPRQPGDTDDSEVGDLGKTLPEGIRLSLVNGDVSDSGSLINGCLRPEELHVDKSRLYNFTKVKKDRRWLKEMLLSDSSSSSDEEQPMTDEDLHEMLWLHKQQKLARQRFLRGGELSQYQHYSASLLYTQDKYHDSQKQRGNAKKLKKKKMKDGSLKIVKVKKEKMRIKKKRKKSEDQSDGDRRESGTIDERLMKRTLIRRKEADAKRRKLWALICRKEIPRTQRQKSSARNNTLSNAKKLAQLCQKERRREAQRSQKIAQQTVPRARRLVREMMVYWKKYEKVEKEHRKRVEKEAMEQRKLDDELREARRQQRKLNFLITQTELYAHFMGKKLKGNKMSASSDVHHILSKLDEPSDKSKIKSVSGGVLIDMENSDNYDARAMKMEALANAENAFRLQEAKRQAFDVNSQESGGSKKIALSQESFDVNFSLANPNISGEDHPQPNLFQGKLKTYQLKGMNWLISLYEQGISGILADEMGLGKTVQSIAFLSYLAETHNIWGPFLVVAPASTLHNWQQEVSRFIPQFKVLPYWGNQGDRKSLRKFWSQKQTHISDRNHAPFHLLITSYQLVVQDVRYFQRIKWQYIVLDEAQAIKSSSSVRWKILLGYQCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDNHEEFNEWFSKDIESHAENKSLIDQNQLSRLHMILKPFMLRRIKKDVENELSEKIEIKLVCGLTTRQKWLYQAVKQKISIDDLVYTSASSSATSATTSSLMNLVMQFRKVCNHPELFERRDVTSPVTVQLPPYVIPKLIYRKVPESECFSFLRFAGISLEEASMMMLGSPSHRLLLLLILLRKVMLLHHKRSWSPSKSSSSVLVPNLMEKKVVAVCELSYCSDRSAAYEHQELARGGPDESRNLLLYGSPEAVDMKEYRAHLFPPPLGGLEATQPSKGWSFVQMPNRNSVISDSGKLTVLDGLLTKLKLQGHRVLIYSQMTRMIDILEEYMTFRKHKYMRLDGSSKISDRRDMVADFQNNKDIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDEQAMDRAHRLGQTKQVTVYRLVTKNTIEERILQRAREKSEIQKMVISGGNFKPDALKPKEVVSLLLDDEELENKFLQRQAEKKADEQRKRRERKRKKGGTDEGTSSPSIEISETSTPPPKAKKGRKSKTSLFPPAPEGVPTASVPPSEASSVNGDASARLEGADADDISVMSLDEISMVSGDGSLYSMDAPPSSSATPFNEDSLLGDAEPKSETASPSTAEGKRGRGRGRARGRGRTRGRGTAPIRTSRGRGRGRGGTGVMAASAAASAAAAAASAAAYAAYGFTFQGTPTPPPPAARSSPVAFGSGGSTVPGSAVTHPVPRYDNSSANSSPARHRDVEN
The following text describes a protein:
Function:
Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. Essential for motility. Responsible for adhesion to mucin, which is the initial event in colonization by this organism of the airways of cystic fibrosis patients.
Subcellular Localization:
Secreted. Bacterial flagellum.
Sequence:
MAGISIGVGSTDYTDLVNKMVNLEGAAKTNQLATLEKTTTTRLTALGQFKSAISAFQTALTALNSNAVFMARTAKSSNEDILKASATQSAVAGTYQIQVNSLATSSKIALQAIADPANAKFNSGTLNISVGDTKLPAITVDSSNNTLAGMRDAINQAGKEAGVSATIITDNSGSRLVLSSTKTGDGKDIKVEVSDDGSGGNTSLSQLAFDPATAPKLSDGAAAGYVTKAANGEITVDGLKRSIASNSVSDVIDGVSFDVKAVTEAGKPITLTVSRDDAGVKDNVKKFVEAYNTLTKFINEQTVVTKVGEDKNPVTGALLGDASVRALVNTMRSELIASNENGSVRNLAALGITTTKDGTLEIDEKKLDKAISADFEGVASYFTGDTGLAKRLGDKMKPYTDAQGILDQRTTTLQKTLSNVDTQKADLAKRLAALQEKLTTQFNLLSAMQDEMTKRQKSITDNLASLPYGSGKKT
The following text describes a protein:
Function:
Acts as a primer for viral genomic replication. DNA terminal protein is covalently linked to the 5'-ends of both strands of the genome through a phosphodiester bond between the beta-hydroxyl group of a tyrosine residue and the 5'-phosphate of the terminal deoxyadenylate. This protein is essential for DNA replication and is involved in the priming of DNA elongation (By similarity).
Subcellular Localization:
Virion. Host nucleus.
Sequence:
MAKKKPVEKNGLVYKEFQKQVSNLKKAGLIPKTLDVRKVKPTKHYKGLVSKYKDVATGGAKLAAIPNPAVIETLEARGESIIKKGGKAYLKARQQINQRGQIVNPFTVRVTKRGEVVRRYRKTTPEGKPVYITQRELPIKFENMEQWLTELKAAGFQLQPGEQIYFTFNGNYSRRTYTSFDEAFNKFMTYDIIIDAVAGKLKVEDEADLVKSVGFQRISGPEAKAYNRNRIVLPEMQFSQAAKKKYKRRQKRGYGSKGV
The following text describes a protein:
Function:
May be involved in cell wall organization and biogenesis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MEGRKSEDEKNEAALACDVFESSNAKLPKNVFRSSFTWYCYEVINRSAFHIWLLLCLTLIVGWKVFSGIGGRRPSDSNMDGPQTKHKRNPGFLRRHSTIVILVISLAVSFSWEAFKMYRERTFGKQITQFAKEIIKSAPSTDMESWDRVAADFNSYMYENKLWNTEYFFC
The following text describes a protein:
Function:
This IE protein is a multifunctional protein capable of migrating to the nucleus, binding to DNA, trans-activating other viral genes, and autoregulating its own synthesis.
Subcellular Localization:
Host nucleus.
Sequence:
MASQRSDFAPDLYDFIESNDFGEDPLIRAASAAEEGFTQPAAPDLLYGSQNMFGVDDAPLSTPAVVIPPPSPTPEPRGGKAKRSPSAAGSGGPPTPAAAAQPASPAPSPAPGLAAMLKMVHSSVAPGNGRRATGSSSPGGGDAADPVALDSDTETCPGSPQPEFPSSASPGGGSPAPRVRSISISSSSSSSSSMDEDDQADGAGASSSSSSSSDDSDSDEGGEEETPRPRHSQNAAKTPSAAGSPGPSSGGDRPAAGAATPKSCRSGAASPGAPAPAPASAPAPSRPGGGLLPPGARILEYLEGVREANLAKTLERPEPPAGMASPPGRSPHRLPKDQRPKSALAGASKRKRANPRPIPQTQTQAPAEEAPQTAVWDLLDMNSSQATGAAAAAASAPAAASCAPGVYQREPLLTPSGDPWPGSDPPPMGRVRYGGTGDSRDGLWDDPEIVLAASRYAEAQAPVPVFVPEMGDSTKQYNALVRMVFESREAMSWLQNSKLSGQDQNLAQFCQKFIHAPRGHGSFITGSVANPLPHIGDAMAAGNALWALPHAAASVAMSRRYDRTQKSFILQSLRRAYADMAYPRDEAGRPDSLAAVAGYPAQAAAAAASQQQPEAPAPSVRVREAYTRVCAALGPRRKAAAAAAAPGTRAPRPSAFRLRELGDACVLACQAVFEALLRLRGGASAVPGLDPSEIPSPACPPEALCSNPAGLETAALSLYELRDLVERARLLGDSDPTHRLGSDELRLAVRAVLVVARTVAPLVRYNAEGARARASAWTVTQAVFSIPSLVGGMLGEAVSLLAPPTRSQQPSSSSPGGEPFSGSAAAEGSLQTLPPLWPTVPGKQSATVPSSHSQSPQHSQSGGGAGATTATCCRATQTNARSRGQQHQPQKARSPQAAASPAHLSQEAMPGSSSDDRAIHGRPRGKSGKRRSEPLEPAAQAGASASFSSSARGYDPSGPVDSPPAPKRRVATPGHQAPRALGPMPAEGPDRRGGFRRVPRGDCHTPRPSDAACAAYCPPELVAELIDNQLFPEAWRPALTFDPQALATIAARCSGPPARDGARFGELAASGPLRRRAAWMHQIPDPEDVKVVVLYSPLQDEDLLGGLPASRPGGSRREPLWSDLKGGLSALLAALGNRILTKRSHAWAGNWTGAPDVSALNAQGVLLLSTGDLAFTGCVEYLCLRLGSARRKLLVLDAVSTEDWPQDGPAISQYHIYMRAALTPRVACAVRWPRERHLSRAVLTSSTLFGPGLFARAEAAFARLYPDSAPLRLCRSSNVAYTVDTRAGERTRVPLAPREYRQRVLPDYDGCKDMRAQAEGLGFHDPDFEEGAAQSHRAANRWGLGAWLRPVYLACGRRGAGAVEPSELLIPELLSEFCRVALLEPDAEAEPLVLPITEAPRRRAPRVDWEPGFGSRSTSVLHMGATELCLPEPDDELEIDGAGDVELVVEHPGPSPGVAQALRRAPIKIEVVSDDEDGGDWCNPYLS
The following text describes a protein:
Function:
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (By similarity). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Nucleus. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.
Sequence:
MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGIGRAAGRGIPAGVPMPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAAAATASIAGAPTQYPPGRAGPPPPMGRGAPPPGMMGPPPGMRPPMGPPMGIPPGRGTPMGMPPPGMRPPPPGMRGPPPPGMRPPRP
The following text describes a protein:
Function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Sequence:
MVKAVAVLGSSDGVKGTIFFTQEGDGPTTVTGSVSGLKPGLHGFHVHALGDTTNGCMSTGPHYNPASKEHGAPEDENRHAGDLGNVTAGADGVANINVTDSQIPLTGPNSIIGRAVVVHADPDDLGKGGHELRKSTGNAGGRVACGIIGLQG
The following text describes a protein:
Function:
Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH.
Subcellular Localization:
Periplasm.
Sequence:
MNRIFIASFLILNSLLTLSCKDEKKEVVRKDDQTKRLEIASYPFPPDNVPTPERILLGKTLFFDPIVSGSNWISCASCHNPGLAWTDGLKTAVGHNMKILGKNTPTILNGAYGNKMFWDGRADNLEEQALGPITSPDEMNQNMEELILELKNIPGYKNLFSKAYPSEEISAATIGKAIASFERTIFSTESAFDRWKKGDKAALSESAQRGFTVFNGKANCSSCHQGEQFSDNGFHNIGLKNAVKEVGRFKIVPVKSMKGAFKTPGLRDVALTGPYMHDGSYTTLEEVIEHYDRGGDEKNNLDPNMLALKLTDQEKTDLVEFMKSLSGKRVSITIPEFPR
The following text describes a protein:
Function:
Acyltransferase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid. Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid. Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton. This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid. Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order. The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21. C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation. The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC.
Sequence:
MESIPLSPFDLQGSFSNIPYAFFYENTQSENDFMPFDFLKGSLWASLQRFPILTGRLRARSTGHIVVEVDAGNPNQPDIRETLCDSVHWSQLKESSFAWDAWPAGVATVGPVATAAADGEIKLLNIHVMRLAQNSGVILFINIPHYVVDGVGYFAFINHWAETMRMQQQQQEQENEARSRFSFDRGIIQRYLPTERAPLDPLTASIYGQRNLLVDWLAWLSPTTLGGLLSKTAAMARGEAHLFRIPRASLDQVHKDVQPYIPASARLSDNDLLVALISKTYIQSQPQPKPPTGFLSWLRPGQGQPESHCTVRIPCDVRRHLKVRERYTGNLLLGMMVRTPLAELARPTSSETLAAAALNVRQSIERVQPGLVAAYHDLIQANPTSHMRPLAFTATRTTTSLVTTSQVRFPMYEADFGSGKPCFVCLTPVFAGSYTMAAILPTPEGREGGVYVLLTSNVEAMQGIKKNQYWNGLVEIIW
The following text describes a protein:
Function:
Cell cycle regulatory protein that interacts with cdc2 in the control of the M-G1 transition.
Sequence:
MSLNTQIPEVLWAQRSNKDDAEKNVIYLTVLIPDAVDPKINLTPEKLVIDSKSGANAHYAVQIDFFKDIDVEKSKYSVTGRYIFFVLYKKELQEEFWPRLTKEKLRLHWLRTDFDRWVDEDEQEAQPEVSPFGAGGMPDLSALGGMGGMDFSQFGNLGGAGAGEDASDSEPELEEEEEVGSNEKKE
The following text describes a protein:
Function:
May function as somatic storage protein during early seedling development.
Sequence:
MALFQLLFLAIILATSHGSEMGVPHQIHLLRPQSGTAGHHVPGVSCLSWRLGVETNNIIGWTTVPAECEGYVGHYMLGHQYRKDSKIIADEAFLYAKSLELSGDGKDIWVFDIDETTLSNLPYYAEHGFGAEPYNSTLFNKWVVTSKAPALPESLSLYKRLLSLGIKIVFITGRTEDQRTVTTNNLKKAGYHTWMKLVLKTSSYSGKTAVFYKSSERGKLVKSGYRITGNIGDQWSDLLGTYTGNRTFKLPDPMYYIS
The following text describes a protein:
Function:
Required for proper chloroplast development, most likely through regulating plastid-encoded polymerase (PEP) dependent chloroplast transcription. Acts as a component of the transcriptionally active plastid chromosome that is required for plastid gene expression.
Miscellaneous:
MISCELLANEOUS: RNAi plants display abnormal plastids lacking internal membrane structures.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MASLLIFPHLHHFDSSLDRREVLVVRHSQASRRFLTPKASINGSGITNGAAAETTSKPSRKGRKKKQTSTVIEKDNTETDPELNPELADYDDGIEFPYDDPPLVCCFGAVQKEFVPVVRVHDNPMHPDMYSQWKMLQWDPPEFGRAPGGPPSNVAISHVRLGGRAAFMGKVGEDDFGDELVLMMNQERVQTRAVKFDENSKTACTRVKIKFKDGKMMAETVKEPPEDSLFASELNLAVLKEARIFHFNSEVLTSPTMQSTLFTAIQWSKKFGGLIFFDLNLPLPLWRSRNETRKLIKKAWNEANIIEVSQQELEFLLDEDYYERRRNYTPQYFAEDFDQTKNRRDYYHYTPEEIKSLWHDKLKLLVVTDGTLRLHYYTPTFDGVVIGTEDVLITPFTCDRTGSGDAVVAGIMRKLTTCPEMFEDQDVMERQLRFAVAAGIIAQWTIGAVRGFPTESATQNLKEQVYVPSMW
The following text describes a protein:
Function:
Scaffold protein in the commander complex that is essential for endosomal recycling of transmembrane cargos; the commander complex is composed of the CCC subcomplex and the retriever subcomplex (By similarity). Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2 (By similarity). Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity (By similarity). Involved in the regulation of membrane expression and ubiquitination of SLC12A2 (By similarity). Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits and by promoting their ubiquitination presumably involving NEDD4L. Promotes the localization of SCNN1D to recycling endosomes (By similarity). Promotes CFTR cell surface expression through regulation of its ubiquitination (By similarity). Down-regulates SOD1 activity by interfering with its homodimerization (By similarity). Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes (By similarity). Can bind one copper ion per monomer (By similarity). May function to facilitate biliary copper excretion within hepatocytes. Binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (By similarity). Involved in the regulation of HIF1A-mediated transcription; competes with ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA binding and impaired transcriptional activation by HIF-1 (By similarity). Negatively regulates neuroblastoma G1/S phase cell cycle progression and cell proliferation by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a FAM107A- and actin-dependent manner (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm. Endosome membrane. Cytoplasmic vesicle. Early endosome. Recycling endosome. Note=Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity).
Sequence:
MAAELEGSKCLSGLLSGLAQDTFYGHPGITEELLRSQLYPEVSLEEFRPFLAKMKGILKSIASADMDFNQLEAFLTALTKKQGGITSEQAAVISKFWKSHKTKIRESLMNQSCWDRGLRSLSWRVDGKSQSRHSAQIHTPVAIMELEIGKSGQESEFLCLEFDEVKVNQVLKKLSEVEESISTLMQPA
The following text describes a protein:
Function:
Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of dermatan sulfate.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MPPRKKEYGIKRASGSLVHFRAPVSATTIRRHSAVVPSVLTFAVIVASGGLLLMIEKGMLNSVQTPPPRANGRKVEYRLRSSSDTAADVESQIVQEIRNRTIRSVCGQRNMPHSVWSLSPLQRKTLLQHILVNDEHRFLYCYVPKVACSNWKRVLKVLSGALANVDIKVKMDHRADLVFLSDLPPEEIRHRLRHYFKFMFVREPMARLLSAYRNKFGEIEAYQRKYGAEIIRRYRKGYAKDKKISGNDVTFTEFTRYLVDEDPERMNEHWMPIYNLCQPCAIEYDFIGSYERLESDASYILERVGAPQHVRFPERQTWYKPVTKETLHYYLCTVPQKFLKELLPKYILDFSLFGYPLPNTTTEYCRH
The following text describes a protein:
Function:
Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
MAKDDYVPLFETRPFKGRILFRLFAASIFVGICFICIYRVRFLPEEGKVERWTWIGLFLAELWFSFYWFLTAVCRWDSVYRLPYKDRLSQRFDKELPGVDIFVCTADPLIEPPSLVINTVLSVMAYDYPPEKLSIYLSDDGGSDLTFYAMLEAATFSKQWLPFCKKFKVEPRSAEAYFRTAFEPREDPVKAREWLSVKKLYEDMKMRIETTTKLNRIPEDIRKQHKGFREWDFVSSKHDHQTILQILIDGRDPNAVDVEGRPLPTLVYLAREKRPQFHHHFKAGAMNALIRVSSRISNGPIILNVDCDMYSNNSESIKNSLCFFMDEEKGDEFAYVQYPQNFENLTKNELYGGSYRVIQKLEFPGLDANGGPCYIGSGCFHRREALCGKKYDKDCKVDWKRLHERKVKESASVLEETCKVLASCTFEQNTQWGKEMGLTYGCPVEDVITGLTIQCRGWKSIYLMPQREDFLGVSPTTLLQMLIQHKRWSEGHLQIFLSRYCSLLYGHKKIPLKLRLAYCPYNLWGANCLATLYYVAVPCLCLLRAISLFPKTSSLWVLPFAYVAFAHRAYSLGEFLWCGGTFQGWCNDQRMWMFKRTTSYFFGFFDTILKLLGYSKAAFVITAKIADDEVLKRYEQELIEFGATSPMFDILATLAMLNLFSSLGAIKKVILEADHSKVLDLFGLQILLCLLLVTINFPVYQALFFRKDNGRMPSSSVDGTLSTGFLTKTGSLKGALCWVPDDGHLILVCMCLKVLALVVDQLDYGDNICGAVLSIRFNEDILSVWNRNVSDHQAVMALRDSIKRHLKLPHSYVMEYKPHDASLRDNSSYRKAWLRG
The following text describes a protein:
Function:
May inhibit cardiomyocyte growth.
Subcellular Localization:
Secreted.
Sequence:
MQSSHCLPVVLLLCLTAAQRSCCLNEEEKQMMVELHNLYRSQVSPPAANMLNMKWDEDLAAFAKTYASKCVWGHNKDRGRRGENLFAITEGEMDLQLAVEQWYNEHEHYNLSNATCAEGQMCGHYTQVVWAKSERIGCGSHFCEKLEGVMETNVHVLVCNYEPPGNVKGQKPYKEGPQCSQCLEGYKCKNQLCEPTIGPEEAEVSPSLATAAPTSMATETSPNLATEAPLSLATKTSTSLNEGTSPSPRLSIETSLKSLETEASKTEPDRVEPTQDGPQELLSSSSSSFETQATTSLANNKLEEVPGTSNSAPPDLPQAGEANAMRGRTLALNSSLEDTENVIILGRSSGRLEFSLFGLLSCLLLSYFF
The following text describes a protein:
Function:
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Sequence:
MVDASADCQLADGTPKIHVLEPGKENWDVIRDVAHSGVQEEAFYVLDVGDIIRKHKEWKLKMPRVAPFYAVKCNDNRTVLETLASLGASFDCASKSEIAKVLDLGVETDRIIFANPAKQVSHIRYASSVNVQAMTFDNESELYKVKEHHPTAKMVLRIRCDAKRVQCPLGIKFGAFPKDAPRLVALAAKLGVDLVGISFHVGSGCDEPEVFERCIVIGRQIFDLAARDYGINMTLLDLGGGYPGNRGSSINSIAAIVNSSLDRHFPEGCGVDIIAEPGRYYVASAFTLATRIHGRRQLTNDDEDADGPRTPANTSYFYYINDGVYGSFNCMLYDHAVVTPLLLEPRPGPDFSCNIWGPTCDGLDRIATNAQLPLMDVGDWLIFEDMGAYTLAAAGCFNGFPVPKVYPVVQPHTWFFLKERAPYTESHFVMGSPSPLPAADLLPKISCAMEMYNNSSSNNNNNGTHLLMPSSVCSSSIDTEDPSTSDAVSTSSDGDVSDNYGDSADFLADLLEVTSVM
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Thought to function as a catalyst in the folding and modification of cuticle collagens.
Sequence:
MAAEKRVFLDISVDENLIGRIEIRLFVEDAPKTCENFRALCTGEVGMTPNNKARLHYKQNEFHRIVKKFMIQGGDITEGDGRGGFSIYGRYFDDEKFKLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDDKSKPLAKVLISNCGELVKKKKPLKTDEELAAALEEKNNNARDNEIPKCPKSWLYRDDDNEKKHEMRNDKRREYRSRRSRSRSHEKNRDYKKENRGDSSRSQPRRDENGITVRGRGGVRFRRERSATPEHWRRNAPTKWVHDSHKHPEEDLV