lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Sodium-phosphate symporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MESFAPELLWMVVIGFLIAFVLAFGIGANDVANSFGTSVGSGVLTIRQACVLATICEISGAVLIGYKVSDTMRKGILEVGLYEGAEEVLMLGCVAALASSAVWLLVATFLKLPISGTHSIVGSTIGFSLVARGVQGLKWSTLGTIVGSWFISPVLSGIVSILLFLAIRRFILRAQEPLKAGFRSLPIFYGVTFFINVISVVLDGPKLLYMDNIPTWIALTASFGLSLLVALLTQLVVVPLQRRKIAKRLRAENPVKFNFEDSVESSPSGSPKKQRRPLSLVSEGKPLPAIAEITELVSLSDNSPRTFKLAPFGLAAKNNNALGEEYKIDPQLIKKAEDLLGKASLDNTDLTITSLNFIDEQQQQQQQQQNGRKLQECFKRMQSPKEEQKSKTNSIGTDLETGSTKATNNNLQVVESGGSLDLMISSTLSPNSSKVPLIESKEALNEQEEELKRTTGGGRRTSGAEETPEISMLFSFLQILTATFGSFAHGGNDVSNAIGPLIALYMIYREGSVMQQAESPIYILIYGGIGISVGLWLWGRRVIETIGNDLTKITSSTGFTIEVGAAITVLLASKIGLPISTTHCKVGSVVFVGHVSASGRKKKSQPNDQTDKETHNEVAPMDDGSVDWHLFRNIAYAWIVTVPVTALLSAGMMYVLCAIAVDDMGGA
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MEEVVSELGRRNISTGDVNNKELLVAVLRVVMEKEYSGTAVLYEKANIVVSKSSQGKKMTAMLCGRQQSDVSGLTLISGSEYGKAMSQSKKSANSAHSPVPKRQSVQKMSVPTTVPATEQQWTSPTTAPAPVQQCTIPATVSPPVQQWVTPTIAPAPVKQWITPTTAPAPQQQWITLSPTQMVQSNMEELDNFDGVASCSSSDTEDPQIVQTPQVKITERTLNKQGGAKQPKQCPHCEYTSLDSSNFRHHVLRHSNKKPFKCSHCDYATKTRPSLNRHMHIHTTREKPFSCKSCDFKTAHKKSLQTHMKTHTGEKPYMCEVCGHRSALAASLRTHMKVHSKEPFKCEICGYVAKNASHLESHMKTHTGELPYKCDFEGCSFTATKQVALQDHQKVHMKEKPFACDQCTYKSHNKYCLSDHMKIHTGEKPHACDQCDYRSVSSSGLFRHKFDKHTGQKLWPCDICGRQCFSEALLEKHKERHTREQGLLVCKECNYRTFDFVAMKEHKRIHTGERPYVCDKCDYKAALEKYLRLHMRKHSSEKPFKCPHCDHCTKRKDSLKSHIKNRHKCEITSDVTSTPDPRPLGLSQDMTLTPDPRPLGLSQDVTLAVLPRLYMEEVVSELGRRNISTRDVNNKELLVAVLRVVMEKEYSGTAVLYKKANIVVSMSSQGQKMTAMLCGRQQSDVSGLTLISGSEYGKATSQSQESANSAHSPVPKIQHVQKLTAPMTEQQWTSPTTAPAPVQQCTIPTTVSPPAQQWVTPTIASAPVQQWTTPSTAPAPEQQWITLSPTQMAQSSMEELDNFDGAAFSSSSDTEEPGIVQSPQVEITERASKDGAKELKQCPHCDYTSMDSSNFRKHFLRHSNKKRFKCSHCDYAGETKTRLREHTRIHTGEKPFSCKSCNFKTAHKTAFKYHMKTHTGEKPYMCEVCGHRAAQAASLRKHMKVHTKEPFKCEICGFIAIMASHLESHMKTHTGELPYKCDFEGCNFATTMQVKLQDHQKVHMKEKPFACDQCTYKSHNKYHLIDHMKTHTGEKPHACDQCNYRSVSSTGLFRHKLKKHEGEKLWPCDICGRKCFSEALLEKHKERHSREQGLLVCKECNYRTFDFMAMKEHKRVHTGERPYACDKCDYRASMQNYLRIHMRKHSSEKPFKCPHCDHCTKRKDCLKSHVKKKHKCELTP
The following text describes a protein:
Function:
Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSSDGDDYDVLVFGSCIVDFISYVPRLPKVGETLHGTRFATGNGGKGANQCVAAARLGSRTAFFGKLGDDPWGAAYRTALAAEGVNVEQVDLLPGESTGIAQINVADNGDNQIVIVTGANKRLAPVDAFRRPELFVRARVLVCQLETPIDGTIAAMQSFRGISILNAAPADTNLPRVILSLPSIFCVNETEAALIAGMPSVADVQQAKVATRKLQTMGCKTVIVTLGEKGAVFARALDDNGDGQVYHVKPLKVDKVVDTTGAGDAFIGALAHCLANYPDAKLGNCIAAANRVAAWSVQIPGTQSSFPRADEIELPADLATLQDQWGCV
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:
MDAVTEGTWAQGLTFPLELRLVLLGQTGVGKSATGNTILGAEEFPSRTSASGTTRHCQSGSVKIKGRRVTVVDMPGLLDTRLSPEETLFLRDRCLSLSDPGPHALLLVVKVGPFSDKDRRVADRVRELFGEEALRFTVVLFTRGDDLEQQSLEEFVRGNRDLQLLVQQCGGRCHLFNNKSRSDRAQVRELLNLIDRMATDNMVRQNGGGFYSSQRRIVNQSERKTQNTVQEGAANSVNKEEMRIVLVGKTGSGKSATGNTILGREAFTSRSTFESVTRHCEKAQGAGVSVIDTPGLCDTALTEEQVKREIVRSILLTSPGPHTFLLVMRFGRHTEEEVNTINTIISLIQQTSGLELQITS
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MQELYLLGVVPSRRFEAVVNSLSKTLDGPKTILEFWVVYRPKDVPPNLPRQPDSWLRLCSNIESHDETDTEWSKNTQWSMYLEGNSEPKREDKCGIRPVNRAKLTNGSVTEFVEKMGYEFSHEYIIQGLEYFFFDTTVRIYQTLIPSQQRSIKPPFHPMNEEQPWILHVYTHVADASNQVAMAKAEANLTKVKTLLSAFCDLKNVRL
The following text describes a protein:
Function:
Required for the female reproductive tract development and fertility.
Subcellular Localization:
Nucleus.
Sequence:
MDNSDILMNMMMQQMEKLPEHFSNSNPNPNPHNIMMLSESNTHPFFFNPTHSHLPFDQTMPHHQPGLNFRYAPSPSSSLPEKRGGCSDNANMAAMREMIFRIAVMQPIHIDPESVKPPKRKNVRISKDPQSVAARHRRERISERIRILQRLVPGGTKMDTASMLDEAIHYVKFLKKQVQSLEEHAVVNGGGMTAVAGGALAGTVGGGYGGKGCGIMRSDHHQMLGNAQILR
The following text describes a protein:
Function:
Probably has an essential role in embryogenesis, induces morphogenesis of imaginal disks, and may participate in multimolecular aggregates.
Subcellular Localization:
Secreted. Note=Secreted from the apical cell surface.
Domain:
The regions 203-253, 256-333 and 335-377 are thought to contain either alpha helical or beta pleated sheet motifs.
Sequence:
MKPVALILVFLAISQARVLNLPKEAIDIPVAIVEDKEPPVALSLVKEEVKAEEVKPEEVKPIAQEEKAKDLKEEVKPEIKPEIKEQPKPDIKDEIKEDLKADIKEELKEKIEEQINELPNAKPLELKEKSLEAEEKPQEIKEEVQQPEIKKEATEIKEEPAQNILKSLPAEETVVVPAEELSPNPVEQEQSENQDAAHPQVRQATQATPTQQSTTQGNFVQQLIQNSPIGQFLNQFQPQPAAAAAPAAAQVQADDAAAAAPATPAPTVPGFLNPQAAITSAQQAVQNAAQSAVNATTQAFQGIQQFASNLGNQFQNTLSSLTGQQQQAVSTTPRPPGPIQQFVNNVFGGNNNATAAAPPAQQSGNPLQGIINFLGGNRPQNAPAAAPATQATEKPAVDDKIDPANDEVGEFVPESDNELRASGENIDDSFEDAGVPSNEVIVVNDDAGEEGNAVQNHPVATDAVAL
The following text describes a protein:
Function:
E3 ubiquitin ligase that catalyzes the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. In response to bacterial infection, negatively regulates the phagocyte oxidative burst by controlling the turnover of the NADPH oxidase complex subunits. Promotes monoubiquitination of CYBA and 'Lys-48'-linked polyubiquitination and degradation of CYBB NADPH oxidase catalytic subunits, both essential for the generation of antimicrobial reactive oxygen species. Involved in the maintenance of cholesterol homeostasis. In response to high sterol concentrations ubiquitinates HMGCR, a rate-limiting enzyme in cholesterol biosynthesis, and targets it for degradation. The interaction with INSIG1 is required for this function. In addition, triggers ubiquitination of SCAP, likely inhibiting its transport to the Golgi apparatus and the subsequent processing/maturation of SREBPF2, ultimately down-regulating cholesterol biosynthesis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAAKEKLEAVLNVALRVPSIMLLDVLYRWDVSSFFQQIQRSSLSNNPLFQYKYLALNMHYVGYILSVVLLTLPRQHLVQLYLYFLTALLLYAGHQISRDYVRSELESAYEGPMYLEPLSMNRFTTALIGQLVVCTLCSCVMKTKQIWLFSAHMLPLLARLCLVPLETIVIINKFAMIFTGLEVLYFLGSNLLVPYNLAKSAYRELVQVVEVYGLLALGMSLWNQLVVPVLFMVFWLVLFALQIYSYFSTRDQPASRERLLFLFLTSIAECCSTPYSLLGLVFTVSFVALGVLTLCKFYLQGYRAFMNDPAMNRGMTEGVTLLILAVQTGLIELQVVHRAFLLSIILFIVVASILQSMLEIADPIVLALGASRDKSLWKHFRAVSLCLFLLVFPAYMAYMICQFFHMDFWLLIIISSSILTSLQVLGTLFIYVLFMVEEFRKEPVENMDDVIYYVNGTYRLLEFLVALCVVAYGVSETIFGEWTVMGSMIIFIHSYYNVWLRAQLGWKSFLLRRDAVNKIKSLPIATKEQLERHNDICAICYQDMKSAVITPCSHFFHAGCLKKWLYVQDTCPLCHCHLKNSSQLPGLGTEPAPQPPVAGAEQNIVLQEGPEPPDHETPPGPGAQEGSGDNSEYINRSSASREGDADPGDGPQIAEGEACPVASA
The following text describes a protein:
Function:
Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MSLLLLFLFNVFINVRTHGNTEIRIQSGISVYVRVHFCTYSTRCSSPLWKNIIPFEVIPEFPFVFEEYFTRPTLPNVIFTISIYDINDEEPLGLEQIVVPLTRHFSNFTVHTKNDSFLHFAVRNVCDENWRTHSCSIFCKDRSDSKFKCDDDDGYKCAPGYSGPNCDKVDCPFNCHNHGSCEVPGKCMCSQGFFGTYCEYCKPSTTCKHGAVLVNELGCHPYTCRCFEGYAGDNGDKDDVCYYAKPCRHGNCVSNVTVSGGFECICPKAFGGRRCEKRIARWDCSDEGYCQNKGVCSFVDGISRCRCAVGFTGKHCERKTAKTCLKKKCREGFICIIDNKKTGTMPCFNYSKTSSPSGSHARRTFSTS
The following text describes a protein:
Function:
Cell wall formation.
Subcellular Localization:
Secreted.
Sequence:
MNKPTILRLIKYLSISFLSLVIAAIVLGGGVFFYYVSKAPSLSESKLVATTSSKIYDNKNQLIADLGSERRVNAQANDIPTDLVKAIVSIEDHRFFDHRGIDTIRILGAFLRNLQSNSLQGGSALTQQLIKLTYFSTSTSDQTISRKAQEAWLAIQLEQKATKQEILTYYINKVYMSNGNYGMQTAAQNYYGKDLNNLSLPQLALLAGMPQAPNQYDPYSHPEAAQDRRNLVLSEMKNQGYISAEQYEKAVNTPITDGLQSLKSASNYPAYMDNYLKEVINQVEEETGYNLLTTGMDVYTNVDQEAQKHLWDIYNTDEYVAYPDDELQVASTIVDVSNGKVIAQLGARHQSSNVSFGINQAVETNRDWGSTMKPITDYAPALEYGVYESTATIVHDEPYNYPGTNTPVYNWDRGYFGNITLQYALQQSRNVPAVETLNKVGLNRAKTFLNGLGIDYPSIHYSNAISSNTTESDKKYGASSEKMAAAYAAFANGGTYYKPMYIHKVVFSDGSEKEFSNVGTRAMKETTAYMMTDMMKTVLSYGTGRNAYLAWLPQAGKTGTSNYTDEEIENHIKTSQFVAPDELFAGYTRKYSMAVWTGYSNRLTPLVGNGLTVAAKVYRSMMTYLSEGSNPEDWNIPEGLYRNGEFVFKNGARSTWSSPAPQQPPSTESSSSSSDSSTSQSSSTTPSTNNSTTTNPNNNTQQSNTTPDQQNQNPQPAQP
The following text describes a protein:
Function:
Transcription factor that acts synergistically with SOX11 and SOX4. Plays a role in neuronal development. Is implicated in an enhancer activity at the embryonic met-mesencephalic junction; the enhancer element contains the octamer motif (5'-ATTTGCAT-3') (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MATAASNPYLPGNSLLAAGSIVHSDAAGAGGGGGGGGGGGGGGAGGGGGGMQPGSAAVTSGAYRGDPSSVKMVQSDFMQGAMAASNGGHMLSHAHQWVTALPHAAAAAAAAAAAAVEASSPWSGSAVGMAGSPQQPPQPPPPPPQGPDVKGGAGRDDLHAGTALHHRGPPHLGPPPPPPHQGHPGGWGAAAAAAAAAAAAAAAAHLPSMAGGQQPPPQSLLYSQPGGFTVNGMLSAPPGPGGGGGGAGGGAQSLVHPGLVRGDTPELAEHHHHHHHHAHPHPPHPHHAQGPPHHGGGGGGAGPGLNSHDPHSDEDTPTSDDLEQFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLNKWLEEADSSTGSPTSIDKIAAQGRKRKKRTSIEVSVKGALESHFLKCPKPSAQEITNLADSLQLEKEVVRVWFCNRRQKEKRMTPPGIQQQTPDDVYSQVGTVSADTPPPHHGLQTSVQ
The following text describes a protein:
Function:
Forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding. Acts as a receptor for amyloid-beta protein 42, a cleavage product of the amyloid-beta precursor protein APP, and mediates its uptake and degradation by microglia. Binding to amyloid-beta 42 mediates microglial activation, proliferation, migration, apoptosis and expression of pro-inflammatory cytokines, such as IL6R and CCL3, and the anti-inflammatory cytokine ARG1. Acts as a receptor for lipoprotein particles such as LDL, VLDL, and HDL and for apolipoproteins such as APOA1, APOA2, APOB, APOE, APOE2, APOE3, APOE4, and CLU and enhances their uptake in microglia. Binds phospholipids (preferably anionic lipids) such as phosphatidylserine, phosphatidylethanolamine, phosphatidylglycerol and sphingomyelin (By similarity). Regulates microglial proliferation by acting as an upstream regulator of the Wnt/beta-catenin signaling cascade. Required for microglial phagocytosis of apoptotic neurons. Also required for microglial activation and phagocytosis of myelin debris after neuronal injury and of neuronal synapses during synapse elimination in the developing brain. Regulates microglial chemotaxis and process outgrowth, and also the microglial response to oxidative stress and lipopolysaccharide. It suppresses PI3K and NF-kappa-B signaling in response to lipopolysaccharide; thus promoting phagocytosis, suppressing pro-inflammatory cytokine and nitric oxide production, inhibiting apoptosis and increasing expression of IL10 and TGFB. During oxidative stress, it promotes anti-apoptotic NF-kappa-B signaling and ERK signaling. Plays a role in microglial MTOR activation and metabolism. Regulates age-related changes in microglial numbers. Triggers activation of the immune responses in macrophages and dendritic cells. Mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages. In dendritic cells, receptor of SEMA6D with PLEXNA1 as coreceptor and mediates up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival. Involved in the positive regulation of osteoclast differentiation.
Subcellular Localization:
[Isoform 1]: Cell membrane; Single-pass type I membrane protein; [Isoform 2]: Secreted.
Sequence:
MGPLHQFLLLLITALSQALNTTVLQGMAGQSLRVSCTYDALKHWGRRKAWCRQLGEEGPCQRVVSTHGVWLLAFLKKRNGSTVIADDTLAGTVTITLKNLQAGDAGLYQCQSLRGREAEVLQKVLVEVLEDPLDDQDAGDLWVPEESSSFEGAQVEHSTSRNQETSFPPTSILLLLACVLLSKFLAASILWAVARGRQKPGTPVVRGLDCGQDAGHQLQILTGPGGT
The following text describes a protein:
Function:
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. This subunit may anchor the endonuclease complex to the nuclear membrane. Probably carries the active site for 5'-splice site cleavage (By similarity).
Sequence:
MSKNHEVYKDALPISLAYPLPPIILTNPLTWIPYIYRYLFRKTPRQVQWQCQLHESDLSCVVTDSEAIKKFWTSGFFGKGNLSRSEPTWHTRTKRSLGLLGFDEDLVAEEVTARRRFQRKQFKAQRAYRENRARERQLLLENGKPIPASLEEDAELPEYLTKSLKDFSRVSENPYHITSVPNVEHLQLTFPEAFFLASLGVLRINYENPNFELLPILKLFANIVANSVALTHDYSLQQSHEDPIIEPDNKFLTELAAYFYFRQQGWVVKNGTKFSVDFLLYKKGPVFSHAEFAILLIPCVGNKQKYNMQWHEVHCLNRVIAQVKKSLILCYVQCPSIEDFNKIWKNQASMNEWDWAESVLRQYLIRCVTLRRWVPSRNRD
The following text describes a protein:
Function:
The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAAAAVQLPVPMDTTPAKANPSDSAISHIEDTDEYAKYKKLEKQLEHLDVMEDYIKLETRNLEKELLHAQEEVKRIQSVPLVIGQFLEAIDQDHAIVGSTTGSNYFVRVLSILDRELLKPGCSVALHKYSNSLVDVLPPEADSSIQMLRPDEKPDTSYADIGGLDMQKQEVREAVELPLTHGELYKQIGIDPPRGVLMFGPPGCGKTMLAKAVAAHTSASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENSPSIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRQDTLDPALLRPGRLDRKIEFPLPDRRQKRLVFTTITGKMNLSDDVDLEDYVARPDKVSGADINSICQEAGMHAVRENRYVVLAKDFEKAYKNVIKKDQNDFEFYK
The following text describes a protein:
Function:
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.
Domain:
Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence:
MEGRPPSGPTPMQEIDPPAMSTPSSPSQASTPSAVRDLTTSLAASLLSPEDGAAVPREQAIALFRRHLARFQASVREEFEAHRLHGTSAAKQLALHTDGMIRTLVDFTLDHALAGSIGPGARSLAVTATGGYGRGMLAPFSDIDLLFLTTDEPSADVSRVVEYILYFLWDLGLKVGHATRSIAQCIAEAEADTNRPHHIAGRPAAGPATRRCSPCSRPGYIVACVEAGAARFISDKHKERTARHNRFGDSPYLVEPNVKEGRGGLRDLQTLYWMCRYTFGTRHVSDLLAPGFSRLGLLTEQEAKRARRSWDFLWSVRLHLHYISGRAEERLTFDVQPVVGARMGYTRHGRQVGVERFMRHYFLTVREVMRLTHVLEPAVMRQALGPAANAPQADSAMRDAGFTVLDGQILPERGTSFDAEPIQMMRLLEWARTRKLPIHPLAMHQLIRWERRAASLRGDPEAARIFLELLCGTPPERIGRPPHSAEAENAAGEEVPSFHATAQDRRQGNAYWLHILNETGIMGRLMPDWSRIVGQMQFDTYHVFTVDEHTIEAIRIFGRIEHGAMADEIPQAYDLARNLQSRRALYMAILLHDIAKGRGGDHSELGSEIALDVCPEMGLTGEETETVSWLVLHHLLLSHTAFQRDIDDPKTILDLADTIQSPEALRLLLLLTIVDMRAVSPRVWNAWKATLLHELYMRVAEVLEGGLATTERDVRVARAKDAAAEILEDDGFKRADIDHFLGLGYGSYWLSFDQDTHARHAELIREAERHKAPLTVETQPLPARGVTEVTIYTADHPGLFSRMAGALAIAGASIVDARIHTLINGMALDTFWIQDAGGEAFEEPHQLARLSALVEQALSGRVDIPKEIVSAGRMRYGRRMRAIHVPPRVVIDNRASNTYTVIEINGRDRPGLLHDVTQAISDHKLQIASAHITTYGVRAVDVFYVKDLFGLKITDERRLGEIREALLHGLRQAEEAMTSEIGPPAESLIA
The following text describes a protein:
Function:
Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation.
Subcellular Localization:
Secreted, cell wall. Note=Is associated with the mother cell wall of sporulating cells.
Domain:
Contains an N-terminal catalytic domain and two C-terminal tandem repeat sequences that play an important role in peptidoglycan binding.
Sequence:
MVKIFIDPGHGGSDPGATGNGLQEKTLTLQIALALRTILTNEYEGVSLLLSRTSDQYVSLNDRTNAANNWGADFFLSIHVNSGGGTGFESYIYPDVGAPTTTYQSTIHSEVIQAVDFADRGKKTANFHVLRESAMPALLTENGFIDTVSDANKLKTSSFIQSLARGHANGLEQAFNLKKTSSSGLYKVQIGAFKVKANADSLASNAEAKGFDSIVLLKDGLYKVQIGAFSSKDNADTLAARAKNAGFDAIVILES
The following text describes a protein:
Function:
Probable transcriptional factor. Binds to the promoter of the SQUAMOSA gene.
Subcellular Localization:
Nucleus.
Sequence:
METGWRTSTCDGGDGGADAAAAGDGGAGDSGGHNSSYTHTAWNTWDISTTTPTPGTSFYNWTNPASVKATEASVVHALLFGVTGNNNSDTSGSGMHSNCMTDPHMMCLKLGKRHYCEDMAAESSRRDKQQYPFQYPNPYYQAADTSTTVSTPGVRVTSSPVPRCQVEGCHVALGNAKEYYRKHKVCEIHSKAPKVVVSGLQQRFCQQCSRFHGVTEFDEAKRSCRRRLKGHNQRRRKGTHSMVERRLGRSPSNPGCALSLLSSPETQSWNSSSDLSSRCSAALYELIAANRATSSVFLNQNFYHQPVALADTQMWDRYSNTTIGEVKQTPALEFGLLSMKERSKDPEPEEWTDYCWSSFGGANVM
The following text describes a protein:
Function:
Acts as a component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export.
Subcellular Localization:
Nucleus.
Sequence:
MSLPLLECKYVTEEFVREGKNGNYGTKLPSSVPMLRFLYELSWILVRGELPIQSCKAVLEGVEFLDKPSREELASCFADVVTQIAQDLTMSGDQRSRLIKLAKWLVESQTVPQRLFQERCEEEFLWEADMVKIKAQDLKGKEVRLNTRLLYQQTKFNLLREESEGYAKLATLLCRGSASSSHNASAATMGIIKSLIGHFDLDPNRVFDIVLDCFELEQDYDTFLNLIPIFPKSHASQILGFKFQYYQRLEVNSPVPVGLYKLTALLVKEEFINLESIYAHLLPKDEEVFEDYNVSSAKRFEEANKIGKINLAATGKDLMEDEKQGDVTVDLFAALDMESEAVTERLPELENNQTLGLLNGFLSVDDWYHANILFERLAPLNPVAHDQICSGLFRLIEKSITHSYRIARQTRFQSSSSASTVKLTPTANTTANRTYLDLPKEVFQMLVTVGPYLYRNTQLLQKICRVLRAYYLSALDLVRDGSNQEGSAYEVSRGHLKEVRLRVEEALGTCLLPSLQLVPANPAVGHEIWEVMSLLPYEARYRLYGEWEKDDEQNPLLLAARQVAKLDTRRILKRLAKENLKQLGRMVAKLAHANPMTVLRTIVNQIEAYRDMIAPVVDAFKYLTQLEYDILEYVVIERLAQSGRDKLKDDGINLSDWLQSLASFWGHLCKKYPSMELRGLFQYLVNQLKRGQGIELVLLQELVQQMANVQYTENLTEDQLDAMAGSETLRYHATSFGMMRNNKALIKSSNRLRDSLLPNDEPKLAIPLLLLIAQHRSLVVVNADAPYIKMVTEQFDRCHGILLQYVDFLSSAVSPTTAYARLVPSLDELVHTYHLEAEVAFLVFRPVMRLFKCRRNGDVSWPLDSGESMDADSEISESESSMILDVGTSEKAVTWSDVLDTVRTMLPSKAWNSLSPDLYATFWGLTLYDLHVPRNRYESEISKQHTALKTLEEVADNSSSAITKRKKEKERIQESLDRLTGELKKHEEHVASVRRRLSREKDTWLSSCPDTLKINMEFLQRCIFPRCTFSMADSVYCAMFVNMLHSLGTPFFNTVNHIDVLICKTLQPMICCCTEYEVGRLGRFLFETLKIAYHWKSKESVYEHECGNMPGFAVYYRYPNSQRVTFGQFVKVHWKWSGRITRLLIQCLESNEYMEIRNALIMLTKISGVFPVTRKTGINLEKRATKIKNDEREDLKVLATGVGAALSARKPHWVTDEEFSMGFLELKAPPVHTPKHASSQNGLLVGVSQGEPTGERATVNQQPESGGLGKDQMLKTKPLDGRTESIPSKSDQGHLKSKGGNPLDSQPSISKKSMEQKETDETPRISDENPVKPASKYSEAELKASSKRGASVNKSAKQDFGKDDGKSGKAIGRTSTADKDLNYLESRQSGLTKALSSTAANGSIATGSSKVKDDGAEALDAQKQSSRTVHSPRHEIVTSVRSSDRLQKRANAVEDSERISKRRKGDAEHKEHDSEPRSSDRDRSVEARLDLNKTVTDDQSTHRDQDRSKDKGYERQDRDHRERVDRSDKPRGDDVEKARDKSLERHGRERSVEKGLDKGTTRSYDRNKDERNKDDRSKLRHSEASLEKSHPDDHFHSQGLPPPPPLPPNIIPHSMAAKEDLERRAGGARHSQRLSPRHEEREKRRSEENLSVSVDDAKRRRDDDIRDRKRDDRETITVKGEEREREREREREREKSLPLKEDFEASKRRKLKREQQVPSAEPGEYSPMPHHSSLSTSMGPSSYEGRERKSSSMIQHGGYLEEPSIRLLGKEASSKMARRDPDPIAKSKSKNSNFLDIALESMTVNGKTTRGEQSGSGEIGSRE
The following text describes a protein:
Function:
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Sequence:
MPLFEVVQEKTTVVFDFGSAYTKCGFAGENAPRCIIPSHFIRKSGQIFYIHDKNLSDEELFDGLVEFLYILYFRELLVNTKDRKVVIVESIFTTSKFRNIIAKVFFEHYEASCRVPSIYFGSAHILSLLTLGVKVALVVDCGYRETLVLPVYHAFPIFQACELVPLGGKVIHQYLKAQLMEEATVSTESREELPLSSVHDQLDEKLLENIKVKTCIVTRFDRAQTIRAAKLDLDIQRPEPPLPVDYPINGKLILKIPGKIREETCELLFDRDDGDISLVTLIINSILKCPIDTRRELMENIVLMGGTTMLPGFKARVMNELKATVQEARYKEKFGKESVFKMHTAPCKENCTGWLGGALFGTLEIVLGVRSLTQEQYLSSNKHIPDWCYLTDHDEVVDDRFIVRETSFMGTPRSENPQ
The following text describes a protein:
Function:
Synthesizes nicotianamine, a polyamine which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Sequence:
MEAQCKEAAALVKKIASIHAALSKLPPLSPSSDADALFTTLVAACVTSSPAVNVTSLGPEAGRMRDDLVRLCADAEARLEAQCADALAALDGDPLDHLGRLFPFYDSYARLGELEHALLSRHAPDHLAVPARVAFLGSGSLPLSPLLVAARHMTDAAVDCYDRCAAANDRASRLLLRPRADDDEKRGGLAERMSFRTADVEDLTRDLAAYDVVLLAAPVGVSPGQKARVVAHLGEHMADGAVHVARSAHGARGFLCAVLEPADVARGGFQVLAVHHPDDRQVINSIIVARKVAAVGGLSQLAPPVLSPPCKCCEPKTPRRRLLPTTCHLDAMNEIRRRAW
The following text describes a protein:
Function:
Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.
Sequence:
MLRCPNSCSPKRFKQPRDTPNGLPRPRLSGAEAEPRFPGARRSALRSRGGRRHRPRGGRRCWPSSAHSAGKMSTAGGGRRRQAQVSRRISFSASHRLYSKFLSDEENLKLFGKCSNPNGHGHNYKVVVTVHGEIDPATGMVMNLADLKKYMEEAIMQPLDHKNLDMDVPYFADVVSTTENVAVYIWDNLQKVLPVGVLYKVKVYETDNNIVVYKGE
The following text describes a protein:
Function:
Essential multidomain scaffolding protein required for normal development (Probable). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells (By similarity). Required for proper embryonic elongation. Acts upstream of ajm-1 and becomes localized to apical junctions independently of ajm-1. With let-413, cooperatively regulates ajm-1 localization to apical junctions and the establishment of newly formed epithelia. Plays a role in assembling the adherens junction by clustering ajm-1 and other proteins, to form electron-dense structures; may form a compartment distinct to that of hmp-1 and associated proteins. Plays a role in the directed outgrowth of seam cells, towards neighboring seam cells, during larval development.
Subcellular Localization:
Membrane; Peripheral membrane protein. Apical cell membrane. Cell junction, adherens junction. Lateral cell membrane. Cytoplasm. Note=Localizes at the apical junctions. Localizes to the subapical membrane of epithelial cells. Localization at adherens junctions requires PDZ domains, lateral distribution requires SH3 domain and is let-413 dependent.
Domain:
PDZ domains are required for localization at the adherens junctions. SH3 domain is necessary for let-413 dependent lateral distribution. L27 domain is responsible for homooligomerization and interaction with ajm-1.
Sequence:
MSHESSEKAHKAIENVEDYCQTLTRHGNEELRTNLERVITTFKSNLMHSLLDIHDLYEQTLLSERKSDAEKNMEVRRVIERLEGGPHSYNSRPAATTSTSNYNLSSTTPLISDLRDRGGFSYLNGGGLGNGLGNGLGNGLLSSPYNSSSTHYLHERQRQTSHDGTWRETTTRTVDTPSGLERRVVEHTGVIDDHGRKWELENIVLEKGHTGLGFSITGGMDQPTEDGDTSIYVTNIIEGGAALADGRMRKNDIITAVNNTNCENVKHEVAVNALKSSGNVVSLSLKRRKDEAFLPIGGNFGGSTSYLRSGVTPSVSAGNLQHAIHSPSAPIHPPPPPPVHHGSLSQLSVGQYRSTRPNTSVIDLVKGARGLGFSIAGGQGNEHVKGDTDIYVTKIIEEGAAELDGRLRVGDKILEVDHHSLINTTHENAVNVLKNTGNRVRLLIQQGTGAIFNDSASQQFMPTTPILRPSSVQDYNRSQMGSQSHLSYGGPLNTSYSSQAPIAIPLEPRPVQLVKGQNGLGFNIVGGEDNEPIYISFVLPGGVADLSGNVKTGDVLLEVNGVVLRNATHKEAAEALRNAGNPVYLTLQYRPQEYQIFESKIEKLRNDVIAQSRMGTLSRKSEYVRALFDYDPSRENSVAPHRSMGFNYGDILHIINSSDDEWWTARKVHENGEETAEGVIPSKKRVEKRERLRRKQVNFNSGSQSLGRNSSTTGLENRRGSRSQLSFSRKFPFVKSTDRLNDLNEESSNVAEEPVWSYQAVEQQAINYVRPVIILGALKDRINDELVNRDPSKFSSCVPHTSRPPREGEVNGRDYYFVNKHNMEEDVKNNLFIEAGQFQNNLYGTSIQSVRDVANQGRHCILDVSGNAIRRLQSNANIQPISIFIKPSSAQQILELDSQLATNRQDDRAMSGEEAQAQYSRCHRIEQTFGDLFTQEISNVHSANDVLSKVYSIISRESQTPIWVPRH