lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in pre-arranging the maintenance of the active cell proliferation during root primordium development. Does not seem to be involved in cell cycle progression.
Sequence:
MKLFLRNAFKTLNPKRKLATTILPSINLILVKPFSQSTTIPKKQDRVRDHGYDNYMEVEKKIRKVVKFHSLILSQPNHTIAISLLDTLARRLGLGFKQHEPGAFLLKFPHVFEIYEHPVQRILYCRLTRKALDQIRHEHEAVLDQIPDAVTRLRKLVMMSNTGRIRLEHVRIARTEFGLPEDFEYSVILKHPQFFRLIDGEETRDKYIEIVEKDPNLSICAIERVREIEYRTKGIDAEDVRFSFVVNFPPGFKIGKYFRIAVWKWQRLPYWSPYEDISGYDLRSMEAQNRLEKRSVACIHELLSLTVEKKITLERIAHFRNVMNLPKKLKEFLLQHQGIFYISTRGNYGKLHTVFLREGYKRGELVEPNDVYLARRRLAELVLMSPRKAKVDAELVRYRDGLDDEDDVE
The following text describes a protein:
Function:
DNA-binding protein that binds to the 5'GGGAATRCC-3' Ikaros-binding sequence. Interacts with SPI1 and MITF to repress transcription of the CTSK and ACP5 promoters via recruitment of corepressors SIN3A and CTBP2. May be involved in the development of central and peripheral nervous systems. Essential for the inhibitory function of regulatory T-cells (Treg). Mediates FOXP3-mediated gene silencing in regulatory T-cells (Treg) via recruitment of corepressor CTBP1.
Miscellaneous:
MISCELLANEOUS: Eos is a Greek word for rising sun.
Subcellular Localization:
Nucleus.
Domain:
The N-terminal zinc fingers are involved in sequence-specific DNA binding; C-terminal zinc fingers mediate homodimerization.
Sequence:
MHTPPALPRRFQGGGRVRTPGSHRQGKDNLERELSGGCAPDFLPQAQDSNHFIMESLFCESSGDSSLEKEFLGAPVGPSVSTPNSQHSSPSRSLSANSIKVEMYSDEESSRLLGPDERLLDKDDSVIVEDSLSEPLGYCDGSGPEPHSPGGIRLPNGKLKCDVCGMVCIGPNVLMVHKRSHTGERPFHCNQCGASFTQKGNLLRHIKLHSGEKPFKCPFCNYACRRRDALTGHLRTHSVSSPTVGKPYKCNYCGRSYKQQSTLEEHKERCHNYLQSLSTDAQALTGQPGDEIRDLEMVPDSMLHPSTERPTFIDRLANSLTKRKRSTPQKFVGEKQMRFSLSDLPYDVNASGGYEKDVELVAHHGLEPGFGGSLAFVGTEHLRPLRLPPTNCISELTPVISSVYTQMQPIPSRLELPGSREAGEGPEDLGDGGPLLYRARGSLTDPGASPSNGCQDSTDTESNHEDRIGGVVSLPQGPPPQPPPTIVVGRHSPAYAKEDPKPQEGLLRGTPGPSKEVLRVVGESGEPVKAFKCEHCRILFLDHVMFTIHMGCHGFRDPFECNICGYHSQDRYEFSSHIVRGEHKVG
The following text describes a protein:
Function:
Possible ligand of InR/insulin-like receptor.
Subcellular Localization:
Secreted.
Sequence:
MSLIRLGLALLLLLATVSQLLQPVQGRRKMCGEALIQALDVICVNGFTRRVRRSSASKDARVRDLIRKLQQPDEDIEQETETGRLKQKHTDADTEKGVPPAVGSGRKLRRHRRRIAHECCKEGCTYDDILDYCA
The following text describes a protein:
Function:
ATPase which is preferentially stimulated by single-stranded DNA and is involved in homologous recombination repair (HRR). Has a DNA-binding activity which is independent of its ATPase activity (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MAEALRRVLNAGCAARPGEDGAAGPPLLLLGAPRSAQTSLLFAAALEAAGEGRGSVLFVTRRPLQSLPLSTPTAREHWRLQKVRFQYPSSIQELLQLLASAHEAPAPTPSLLLLDGLEEYLAEDPSAQEAAYLAALLLDTAAFFSHRLGANGSCGLVVALETQKEAEADAPHLPLLKRYFPAQCWLQPDALGLGQHCCLRASLELGKLSPRTEWSVSFLPCGEMKVTPWLAQASKLSPEKKDSSAGSQSLTLGCDNLPGPGSPLDGILTSETGADSKT
The following text describes a protein:
Function:
Part of the binding-protein-dependent transport system for glutamine; probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MYHWDFGILWSYRWLFLNGLGVTVGFTVVIVVLGLVFGLFGAFGSLSRLKAVRLVALTFIEAFRCTPILVQLIWFYYALPILAGVEMTPITASALALSLYGGSFYSEIIRGGIVSIDKGQSEAGAALGMTPGQAMRRIVLPQAIKRMIPALMNQSIIQFKNTSLVSVLAVPDLVYQSQVAAHDSYRPLETYTAVAVAYAAILIPLTIIVRRGEKRLAVGE
The following text describes a protein:
Function:
RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion (By similarity). Binds both poly(A) and poly(U) homopolymers. Phosphorylation by PTK6 inhibits its RNA-binding ability. Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer (By similarity). Can regulate alternative splicing of neurexins NRXN1-3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. Regulates cell-type specific alternative splicing of NRXN1 at AS4 and acts synergystically with SAM68 in exon skipping. In contrast acts antagonistically with SAM68 in NRXN3 exon skipping at AS4. Its phosphorylation by FYN inhibits its ability to regulate splice site selection (By similarity). May function as an adapter protein for Src kinases during mitosis.
Subcellular Localization:
Nucleus.
Sequence:
MGEEKYLPELMAEKDSLDPSFVHASRLLAEEIEKFQGSDGKKEDEEKKYLDVISNKNIKLSERVLIPVKQYPKFNFVGKLLGPRGNSLKRLQEETGAKMSILGKGSMRDKTKEEELRKSGEAKYAHLSDELHVLIEVFAPPGEAYSRMSHALEEIKKFLVPDYNDEIRQEQLRELSYLNGSEESGRGRGIRGRGIRITPTAPSRGRGGAVPPPPPPGRGVLTPRGTTVTRGALPVPPIARGVPTPRARGTAAVPGYRAPPPPAHDAYEEYGYDDGYGGEYDDQTYEAYDNSYVTPTQSVPEYYDYGHGVNEDAYDSYAPEEWATTRSSLKAPPPRSARGGYREHPYGRY
The following text describes a protein:
Function:
May be a regulator of keratinocyte proliferation or differentiation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDRKKDSDKQLEPPAAFGVPRSTEPRGLIPPSHFQSRSAPPLPGPVGLPWGATSLSNWEAAELKQENQRLKDELQRWRKKGEKLEEAGNRKRSLDREAEPLSACHTMAMSQQAEIISHQLHEIQRLEAELASLRVASVQQEAVAVARENTLVNLQGELAELKSQSQAEATALKTELEEVKKGSRLETEALREELEELRRRSRLEADSLRQELELAKERHALELGLAQGELQGALEKAEAERKRYEERAQEGLQTLHKEHQTELLRLSEVYGAEVASLKNQVCVLQQDLETHHKETVQLREKKDDLQNQLSMAKAELASQNALMLQLKTYVGEQESRQPTSELEHLRNRVQQLEDEKEALKITAELLQVRLASLTDILTLQETELSKKVQLQDPLQSDSSQKLQGLLTCWREKVFSLLVQLKSQELSHRNAIKQLDWKVKDLEEEVESREQKVALLSHSLEDKTAEANMEQVRNKTLQAEALRSKELAQKLQIRAEAAENALKGLGDLASRVNQHLLGQEETWKATLSRLAGLGNRVAFAAKRVDTIQGLVCQKIALAKLQQEDKVSIMKLTEKIQPSYEDLQAELQMLHEERDQLSMELKRGAQLIERKVAEAREKVESDLQDLREKSQSLQEALEAKAMMEQALRQQQEDTERQLEKVCQDLQKSEESEEGLRHELGQMRAEYEKALQEKVTEVEMQLRKDLSEMEKCLNEARREHTQAVVALRQTERQAARDKARSEELAKLQESATQQEVARLEKRMQELERDKNLLMVTLKEEGLLAQHKQNRRLAIRGPEESTGKTGHKPPSKGINTLPCNFLLLMLQETSLGCFPTPSTLNVCRHSFFSMMMMMMMMMYFLPASPDSSRRGTTQSKIHFHKYV
The following text describes a protein:
Function:
Anion-transporting ATPase. Catalyzes the extrusion of arsenite.
Sequence:
MRLILYLGKGGVGKTTTSAATAVRAAELGYRTLVVSTDVAHSLADALDTPLGSLPTQITERLWGQEINVLDEVREHWGELRVYLSNLLRRRGVDEVAAEELAIIPGMEEVVSLLHIRRQAREGNFDVVIVDAAPTGETVRLLTMPETFQWYAARVMDWEPTTLKVARPLVKQLVPATDVFAKLERLTKGVEALRATLTDPQISSYRLVVNPERMVIKEAQRASTYLALFGYPVDGVVLNRVLPVDQVEGAFMQELARIQQGYRQMVYDLFRPLPIWESPYFARDLAGIEDLAMVGRRLFGDDDPVKVHFIGKTQEIVKQGDEYVLRLPLPHVEIGKVSMTKRGDELFIEIGNFRRDMLLPTTLAERPARRAYFRNGVLEVFFGPPETLSLKTDAQEESTPS
The following text describes a protein:
Function:
Transcriptional activator that binds DNA to the AC cis-elements 5'-ACCTACC-3', 5'-ACCAACC-3' and 5'-ACCTAAC-3' of promoters and specifically activates lignin biosynthetic genes during secondary wall formation mediated by SND1.
Subcellular Localization:
Nucleus.
Sequence:
MGKGRAPCCDKTKVKRGPWSPEEDIKLISFIQKFGHENWRSLPKQSGLLRCGKSCRLRWINYLRPDLKRGNFTSEEEETIIKLHHNYGNKWSKIASQLPGRTDNEIKNVWHTHLKKRLAQSSGTADEPASPCSSDSVSRGKDDKSSHVEDSLNRETNHRNELSTSMSSGGSNQQDDPKIDELRFEYIEEAYSEFNDIIIQEVDKPDLLEIPFDSDPDIWSFLDTSNSFQQSTANENSSGSRATTEEESDEDEVKKWFKHLESELGLEEDDNQQQYKEEESSSSSLLKNYELMIH
The following text describes a protein:
Function:
A cytochrome P450 monooxygenase with a key role in vitamin D catabolism and calcium homeostasis. Via C24-oxidation pathway, catalyzes the inactivation of both the vitamin D precursor calcidiol (25-hydroxyvitamin D(3)) and the active hormone calcitriol (1-alpha,25-dihydroxyvitamin D(3)). With initial hydroxylation at C-24 (via C24-oxidation pathway), performs a sequential 6-step oxidation of calcitriol leading to the formation of the biliary metabolite calcitroic acid. Hydroxylates at C-24 or C-25 other vitamin D active metabolites, such as CYP11A1-derived secosteroids 20S-hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin.
Subcellular Localization:
Mitochondrion.
Sequence:
MSCPIDKRRPLIAFLRRLRDLGQPPRSVTSKAHVKRAPKEVPLCPLMTDGETRNVTSLPGPTNWPLLGSLLEIFWKGGLKKQHDTLAEYHKKYGQIFRMKLGSFDSVHLGSPSLLEALYRTESAHPQRLEIKPWKAYRDHRNEAYGLMILEGQEWQRVRSAFQKKLMKPVEIMKLDKKINEVLADFMGQIDELRDERGRIQDLYSELNKWSFESICLVLYEKRFGLLQKDTEEEALTFIAAIKTMMSTFGKMMVTPVELHKRLNTKVWQAHTLAWDTIFKSVKPCIDHRLERYSQQPGADFLCDIYQQDHLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQRLLREIQSVLPDNQTPRAEDVRNMPYLKACLKESMRLTPSVPFTTRTLDKPTVLGEYTLPKGTVLTLNTQVLGSSEDNFEDADKFRPERWLEKEKKINPFAHLPFGVGKRMCIGRRLAELQLHLALCWIIQKYNIVATDSEPVEMLHLGILVPSRELPIAFCPR
The following text describes a protein:
Function:
Probably part of a periplasmic ABC transporter complex futA1A2BC (TC 3.A.1.10.2) involved in Fe(3+) ion import (ferric iron). This protein and futA1 (slr1295) are subunit proteins that have redundant or overlapping substrate-binding functions (Probable). The differing subcellular locations of futA1 (predominantly thylakoid lumen) and futA2 (predominantly periplasmic) suggest they may fulfill different roles; Plays an important role in protecting the acceptor side of photosystem II (PSII) against oxidative damage, especially under iron-limiting growth conditions; Plays an undefined role in copper supply to thylakoid proteins.
Subcellular Localization:
Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side. Periplasm. Note=Binds Fe(3+) in the periplasm.
Sequence:
MTTKISRRTFFVGGTALTALVVANLPRRASAQSRTINLYSSRHYNTDDALYDAFGEVNLIEASAEELIERIQSEGANSPGDILFTVDAGMLWRAEQAGLFQPVRSGKLNERIPENLRHPDGLWYGFTQRARVLYYSRDRVNPADLSTYEALADPQWRGKILVRPSSNVYNLSLTASRIAIHGEPETRRWLQGLVGNFARQPEGNDTAQIRAIAAGIGDVAIANSYYYIRLQKSTDPADQEVVEKVSLFFPNTGSGERGTHVNVSGAGVLKNAPNRDAAIAFLEYLASDDAQRYFAEGNNEYPVIPGVPIDPVLAAHGQLKGDPLNVSNLGRYQPDSARLMNEVGWQ
The following text describes a protein:
Function:
Part of the ABC transporter complex DrrAB involved in daunorubicin and doxorubicin resistance. Responsible for energy coupling to the transport system. Binds ATP or GTP.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MNTQPTRAIETSGLVKVYNGTRAVDGLDLNVPAGLVYGILGPNGAGKSTTIRMLATLLRPDGGTARVFGHDVTSEPDTVRRRISVTGQYASVDEGLTGTENLVMMGRLQGYSWARARERAAELIDGFGLGDARDRLLKTYSGGMRRRLDIAASIVVTPDLLFLDEPTTGLDPRSRNQVWDIVRALVDAGTTVLLTTQYLDEADQLADRIAVIDHGRVIAEGTTGELKSSLGSNVLRLRLHDAQSRAEAERLLSAELGVTIHRDSDPTALSARIDDPRQGMRALAELSRTHLEVRSFSLGQSSLDEVFLALTGHPADDRSTEEAAEEEKVA
The following text describes a protein:
Function:
Subunit of the replication factor C (RFC) complex which acts during elongation of primed DNA templates by DNA polymerases delta and epsilon, and is necessary for ATP-dependent loading of proliferating cell nuclear antigen (PCNA) onto primed DNA. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Can bind single- or double-stranded DNA.
Subcellular Localization:
Nucleus.
Sequence:
MSMDIRAFFGRGGSATKPAKAPEPAKTPTVKRKAVIISDDEDETKASPSRSSKKPEQNSPSTTGAVKKRRVIESDDEEKSPAKGRHESTKPKPEKLKPVNVADVFSSAPVKRVELPKIPKKKTLEPVEQVKLEELDDDEVIPVTPQPDKKMARKDRNGNERSEKRTPEKPKATPPESKPVKRETSEERPTVSKKSPVKQKSVEQQSASPSREKVSSKAKKKSDSDAADYKDPNESILTDEERHERKRMSAILYQKFKNRQGPANPGSKEIPEGKPNCLQGLQFVITGVLESMERDECAQVIKDLGGKVVGAVSKKCTHMVVGDDAGPKKIAQAEELGIVTLSEDELLDLIRVKSGQKPLKKSSSVKEAESAGGSSTSSKRKESPKEEKEIKKMKTDPSPRKSPKELKTESSKGRSPGKATVDRKSEHSKEAVKVKVEKSPSKQPSDGAKTSPRKLEPSTTVKRELSDYQKDIKSVDNMAWVEKYKPSSTKQIIGQMGANSNVQRLTVWLSSWYKNNDGTKKHAKPNPWVKNDSGAAFKAALLSGPPGVGKTTTATLVCKELGFDTVEFNASDTRSKRLLKEEVSELLNSKSLAGYFGGRSEKVSSKHVLLMDEVDGMAGNEDRGGMQELIALIKESHIPVICMCNDRNHPKIRSLVNYCFDLRFNRPRVEQIKGAMMSVCFKEQLKLSPGVLEEIIAGTGGDVRQTLNHLALYSAGKSMAASLSVDSAKKHADSAKKDIKIGPWDVIRKVFSAEDHKHMTLNDKADLFFHDYNIAPLFVQENYLKVQPKAPRTEWLDRIALTADSLSRGDMVERRIRSNMAWSLLPVQAMFSSVMPGEFMEGHFTGQINFPGWLGKNSKSMKRKRLAQEIHDHTRVATSGSRQAIRLDYAPHLLRSIVQPLQHRGAEGVHDSLEVIKEYRLLREDIDSLVELSTWPKRKSPLDSVDGKVKAALTRAYNKAIGPYSYSAMATVKKKVHDAGQDEMDGLYGEDGEQGGATQVESDEEEKEENIDDNAFIKIKKKPAAGATSAASSKASTSKASTAKAGGAKGKKK
The following text describes a protein:
Function:
Involved in the polymerization and cross-linking of spore peptidoglycan. May be required for synthesis of the spore germ cell wall, the first layer of peptidoglycan synthesized on the surface of the inner forespore membrane.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MDAMTNKRLRLTLKTVRAFIFLGAFAALAAAAVFMTVILIAKYQGAPSVQVPQSTILYASDGSKLGETNYGEKRYWVPLKDMNPTIVKATVAIEDQNFYDHHGFDYKRMAGAALADLKAFAKVQGASTITQQYARNLYLEHDKTWKRKWNEAFYTIRLEQNYSKDEILEGYLNTIYYGHGAYGIEAASRLYFGKHAKNLTDAEAALLAGIPKGPSGYSPYVNETKAKERQKTIVRMMEKQQMISQKKADELIKEPLSYQPLNKQVSKRKAPYFYDNAMRELEKKLGMTREQIETSGLNVYTTVDKRMQRIAEETITETVNAGSDIQVGFSAIDPRTGNVLALVGGRDYQKSPFDRTTQAKRQPASTIKPLLYYKAIQSGFTPVTLMKSEETEFQIDAKGETYSPSNYNGYYANKPITLLQALALSDNIYAVKTHLFLGTNKLVKTAKEFGITAHLQALPSLALGTEPVRPIEMVNAYAMLANGGKKIEPTFISRVTDAAGHVLYENPNQHKQVLDEKAAFVTASMMTGMFDIDLNGYTSVTGRTIANRLTRTYAGKSGTTSADSWMIGFNPKLAAGVWTGYDKNSTIDSVEEKSYAKTIWADFMEDALKGEPETAFKPPKGVTGVYIDPETGYSSGPGCAAKHYTYFVKGTEPANVCYGAEPAKQTKDRLPSKEKPASEKKWWDKWLGRHH
The following text describes a protein:
Function:
Formins play an important role in the nucleation of actin and the formation of linear actin filaments.
Domain:
The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).
Sequence:
MDNHSSSSNPSSLSSSSSSSSSSSSFLSDHVKKEEQNGLDTIKEEIENKIENEEEEEKIEEKPIEKVEEEKIIVQKEEEEKIEEEPIEKEEEKKVEEEKFEQDNINTTVEAKTLETSTEPIATEVVDEKSITSNNENLEEQQKEDVISIPPPQQEQQEQQEQQEKQKEETKPSIREEVKEKIKGKLSEIKEEIKDIKEEIKHVIREEVTEPIIVVENNNSPPPPPPPPSITVQSSSPVSSQISSPVSSPVSSPKPSVTFNEDGRKRKEGGITASISSEDIMALSSSTSTNNKGIPKENKRTASTILRSKSSPNPGANNPNHNKDGNNSSSSSSSNNNSDNNNNSDNNSNNNNINNNNSSSNNLNYDSSDIDTEAIPKFYHDFKIHRGTSSCVYCGENTRLWSTSYKCFFCGVVCHKKCLDSMNTIPCSSAIHNIKGKNRSQTISGYAPPNSLALQAPPYISVAKPSSITNSSSKSTPSLLSAPPSQSNSNNSSPNISSKSNPNSPITTSATTTTTTATISSLSPTSISSPPIASEQPPSPLLQQQQQQQQQQQQQQQQQQQQQQQQQQISTTQLQDLNNTSEKPDDDMINLMFDTLMVDLDLNLPASKLSTTQKWLLLEQKFKLKKDELLPEYFINALKEQPSKSIFQSLVVILRTNVTKNWMCSFVQLNGVEILFEILSKSKRKDYKDDCLSCIGKVMSNPIGLNSVAQLPMAPKTITKVLRSKQYCIKSKAMAIELLTVMLLDKYVPGGCSLVLKALTKTKEKKRFSFFVRFIKDNESLELKTKALCFINVLIFEMEDMNVRVNIRSEFLRLGLYTYLREIKKTITHEKTLFTQIEIFEEMMNEDTQELDLRLEDLKRQLGIDIDDVDQVFKALKNTTSKSGLNRQLLNILQNLLVIKACDPTDGVKYFILCDTLVKQISLHKGGFEDPSNFDFRGLMVGLESATAEVTLNRKLGELEKQNIDKAMKIQEQDINIKSLLDLLKQLKDGGTAPDASMIKKIEEMIKQMEPPPPPISVKSPDDPNNAAPIVVAPIPPPPPPISGAPPPPPPPPPPMKGGAGPPPPPPPPGKLGAKKPPAGVQCRPPPKVPKPSHPLKAYQWVKLAPVKVNDSLFDKLGPMNDINLPWNQIEEEFAAKVIVREKKAIVKPKGPTQVIDPKLGQNISIFLSQFKGVEPKQLITYIQSMDESKMSRDQVKQISKLLPSREDLAALKEFLQAEDRSKLSIADQYCIDIGAFPFASEKISMFLLKSELKSRLDEVKPQIAAVSVACDEVYKSKKLIRIIEIILVLGNFINYGTPRGDISGYKLDSLIKLSDTKSSDLSSNLINTFVKYCQEKEPNLLTFADELPSLTTARKTIWSGVVADVSSIGRDVHSVKQIVETLQKSNEPFNQSIIDFLATASTEVEKLRKLLESTQENFKKLCKYFAEEEGKSQPEEFFDIFGRFITLFENATTQLQQQKEEQLKEEKRLQQKQQRQERAVRKLTTSNESASASPNHAKSTDDKSDEDDDIVNDLLMAVRDGDAFRQAKGRRRTTHQIATSKMISNNLDPSKILPTSPNKN
The following text describes a protein:
Function:
Rho GTPase-activating protein involved in the signal transduction pathway (By similarity). Regulator of the contractile vacuole network as well as involved in driving vacuole emptying.
Subcellular Localization:
Cytoplasm. Contractile vacuole. Note=Localized to tubules of the contractile network.
Sequence:
MNVENQDPNIMVIPNNNLGPIDGNNISPAMNDENSNNGSSFLKNLVNTGTNLLFSSSSSIASPPNLGGLSNDSTNNNSNSNNTIDSSKPLSFENDMSDGYEALVRRSEIAIDQCKELLDFFKKRASEEEKYSKNISNMFSKFKVKDDHDTFQKGVSLLNKINDAESTIHRSFSQNITTNLYHPLNEAIKDMEKSRKRLLEDGKKLKNDLKDSIENVKKSNQKYEKLCREMEQAKLELIEEGNDTKSGKVETLEKKLEKTKLASIKAEDEYKEQINETNEFISGVYQNRLSENLREFQQFELTRLEIMKSNIRNYIGFMKDIPQALQCEIDSTKGFVDIIDPEVDLQNYIMNNSNPKKVLLPFIFEAYNDHKPFVDQHNQNSSSSSSTNALNYASPMSASGSITNTITSQSGSTIISNGASQPIEIPSPQPISEQQQIPPQQQQQQQQAQVPPTSINQSSSPPVNPMGRQQSLKENIFGFFNKATTNLKSSTSSLLTKDGNSTTSSNTSTSNSNQLSKSGIGLPIINTNSIFGVELEVLIENDNSKKKGNGVELEVPLILTQFVQALLKLESFKMDGVFVSLPSHFNIQQEKQKLDQTGTLENITDVYLIASLFKNWIGDLPNPLISYAIYQEIIEAPDNAWKIIESGIPILHRRVLHYIIDFLVDFVNCSKMDTHSISLIFTPVLIRSPFNGDSLLNSKKEVAVIENMIIDSLETKRGNYILKRNLPIIPDDENSDDDDDDSGHIDDENNSSTSGENDINTTNINNNNNVNSNNDTNNNNNNSNTTTTNNNNNNDSNNSNSTNNNNNNNNNNTNNDDNESNNSGYGVSSNGNNINSSVGGSVTHHFLYQTTPTNNVTPVLSDFFDTNSSNGSSKANTNTHNLGVRNSSNISFDTISTNQSDSEPVLVEYDNDDFDILSYK
The following text describes a protein:
Function:
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. May target the cAMP phosphodiesterase regA for degradation leading to an increase in cAMP and PKA activity. Promotes development of prestalk cells as opposed to prespores within the developing fruiting body. Required for culmination and fruiting body development.
Sequence:
MQYVNGNDISSQSIHEVLELAFSTKIPWTKLEYESSEKHIIHSYSSHERGIYLSKGVAEFNISPENMYELLLDISSRSKWDFHCREAHIIEEYDHLNHIIHLNFTNPLISNLDMNLYRSCKYDPQERLFVIAMRSIELEDGDVDQFECLPNGWVIQGLRGQKDKCKMTFVQQCDLRDIELQRIPGYKSFNSKERLEDFQFLTLFPATVSGRLAKIFESIELYISNNVKDIETKDIRISIMEKAEKEVNEMFGTTNPDYGWKIYLKKLDMEILIKKTTSGYYMIGKGSFSSRYSPELLADVLYQKNPFEWDTFYDKTKLVESINSSIREVEVHYRMWRNTITMRLLQSVKKGPGNFSSVHWRSICSPNYQVADGIEVHYLPTALLNYGLGDGSFTSFLAAIEVKGYPTPWEEEMVTKMFAARIISNQNSIINHVNKLTGGSEMIRELPVIPSVQHHCGDVGSHIGTPQVYNAMVENFADILLDEGNKDGNVVSSKNKRKRNKNNENKNNNNDNIIDEEIEQEEENIEKDQQQTQQQQTQKQQQQQQQQQKTQQQPQQQQQQPQEQQQNHSQLKKEIKPTRPSIRFTYLLSNSSSGQRPIAWYESKKQPFLFLVSDSSERKGKIQRKTYYFSNSGFDNLPEEVVQIIFSNLSAINIVNLSLVCKRFKMATDSPILWKNLYKSNPLFHKKTPKRKQIIHSNLSNDENKVNSNSGDSADGSSSQEEEEQQQQNQQQNQQQNQQQQQQQTFDLSNINLNDPISLLMVFTNGIIPQNLSPTEIINVGGIVSQIDLNDLSNVETLIQQLPHQVLSLIQMNTLDAKIQHLSMISGMPATIGQESPINKNSSDNPKPNAYNKRDNNSYIPDEEFINWKSHYTEKHKQSKRWVNMEPIRITPLKGHNRAIKAVKSEGNSAITVSTEKKIKFWNLNTGQCIGDYEGESGVLSVEYDHTQKSSCIWPLSDYTKVHIGHKNGTVTMVDFIEQPIEVIHTSRPTNLADGFDFTFPGKYLIWEHTIIHYWDVETSTLLWNELNAHTKKITQSKIVAQHELSNKGIVFTTSSDKSAKVWDLTNGTCINTLVGHSYAVNCIEPIGDYMALTGSTDKTLKLWDLRQASTFISSYSTKHTGPIRCISYQEKNGIVLSGSDDGSIIAFNLDNWNLSNISVVKKPIFNNVIGNIGTTTTTTTTTTTTTTTTTSTTNNTNVPEIPKINLGTFKDSKRLHNHESAVTCIESDEAGFISGSQNGLVLRWDF
The following text describes a protein:
Function:
Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Sequence:
MSEAEKKATIASGAEAAAPVAAQPPADSTAVVADASTIAVSTETAQEKAGKDETPAPIAAIAEPAASEAAAAPEESAPAAAAVVPKEPAAASEETKAPAAETAATPAPAAATSAAPEATKEKDAADAPAAAEKTGVAKLWEVCQAHEHKEIWGVTLQDPSSDVPTEIVLTKFLNANDGDVPKAVDQLTKTLDWRNKMKPLELLKKSFSRAKFGGLGYVTNHSEAADSKDPALKEVFTWNIYGNVKSMEETFGDLQQFIEWRVALMELALQELNIAGASAPHTITAENDPYKIYQVHDYKSISFLRQPASVKAASKETISVFSTVYPELLKEKFFVNVPVVMGFMYGLMKLFVAPKTLKKFHPMSDGGALAREFGGSKVKTLGDAMPKEYGGKGEELKATGKETMLD
The following text describes a protein:
Function:
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MVASGFLLIASFMLVLFVLSRPLGGFLARLIEGEPFSALQKVEAGLWRCSGVKNAEMNGWQYALAILCFNLLGIVLLFVLLMTQGSLPLNPEHLPGMSWHLALNTAVSFVTNTNWQAYSGENTLSYLSQMAGLTVQNFLSAATGIAVAFALIRAFARHSATTLGNAWVDLVRITLYVLLPIALIIALIFVSQGVLQNLDDYLHITTLEGVQQTLPMGPVASQEAIKVLGTNGGGFFGANSAHPFENPTAFSNFVQMLAIFLIPCALCFAFGQVVGDNRQGHALIWAMSLIFIVAVVVVMYAELAGNPHLSPLGADSNSNMEGKESRFGILATSLYAVVTTAASCGAVNAMHDSFTALGGMIPLWLMQIGEVVFGGVGSGLYGMLLFVLLTVFIAGLMIGRTPEYLGKKIDVFDMKMTALAILVTPTIVLLGTALALCTEAGRAGILNPGAHGFSEVLYALSSAANNNGSAFAGLSVNTPFYNLLLAAAMFIGRFGVILPVLAIASSLVAKKRQPAGNGTLPTGGLLFIGLLIGTVLLVGALTFIPALALGPVAEHLQVWLAH
The following text describes a protein:
Function:
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Subcellular Localization:
Cytoplasm.
Sequence:
MVETKSIAPEFKKYLKFDSNNSNIRVGVAMSGGVDSSTVAYLLKQQGYDIFGVTMKTFKDEDSDAKKVCDDLGIEHYILDVRDEFKEKVVDYFVNEYMNGRTPNPCMVCNRYIKFGKMLDFILSKDASFMATGHYTKLKNGLLSVGDDSNKDQVYFLSQIEKNKLSKIIFPVGDLEKTKLRELAEQLGVRVYSKKDSQEICFVDDGKLKQFLIENTKGKAEKPGNIVDKNGNILGKHKGFSFYTIGQRKGLGISSEEPLYVLAFDRKTNNIIVGQNEDLFRDELIATRLNLFSVSSLEGLDNLECFAKTRSRDILHKCLLKKDGDNFQVKFIDNKVRAITPGQGIVFYNNDGNVIAGGFIEK
The following text describes a protein:
Function:
Growth factor active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. It binds to the receptor FLT1/VEGFR-1. Isoform PlGF-2 binds NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent manner. Also promotes cell tumor growth.
Subcellular Localization:
Secreted. Note=The three isoforms are secreted but PlGF-2 appears to remain cell attached unless released by heparin.
Domain:
Isoform PlGF-2 contains a basic insert which acts as a cell retention signal.
Sequence:
MPVMRLFPCFLQLLAGLALPAVPPQQWALSAGNGSSEVEVVPFQEVWGRSYCRALERLVDVVSEYPSEVEHMFSPSCVSLLRCTGCCGDENLHCVPVETANVTMQLLKIRSGDRPSYVELTFSQHVRCECRHSPGRQSPDMPGDFRADAPSFLPPRRSLPMLFRMEWGCALTGSQSAVWPSSPVPEEIPRMHPGRNGKKQQRKPLREKMKPERCGDAVPRR
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Sequence:
MAPKPGFYAVATGRHPGVYKTWPAAEEQVKGFPSAKYKKFATEQEAKDFVTAAGDALPSQPPPIGKRKRAEMEDSKAPPVDTHFQATSPATVASPASLPPKLQKIAQQGFSFTKSVPHYLVVYTDGSAKGNGQVGSRAGAGVWWGSRGEASKQNWAERVPGEPQTNNRGELLAVIRAIERCPFPDIPLEIRCDSQYTISCMTIWLPKWMNNNFRNSYKQEVINTDLIKHLLVLLRRRGAAGRVKFKYVPAHSGVEGNEAADRLARTGGALPFVSDESNWLDPEDEVVPCDSETNPTEVELEIDEDWLMTAEELAALEQQLV
The following text describes a protein:
Function:
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. In the mitochondrion, functions as a redox switch between two lipoylation routes. Senses the oxidation state of lipoate and determines which downstream enzymes will be lipoylated. In low reducing conditions, uses lipoate in its oxidized ring form to lipoylate glycine cleavage system H-protein GCVH. In high reducing conditions and together with LipL2, uses reduced lipoate (dihydrolipoate) to lipoylate the E2 component of the branched chain alpha-ketoacid dehydrogenase complex BCKDH-E2/BCDH and the E2 component of the alpha-ketoglutarate dehydrogenase complex KDH. LipL1 is responsible for catalysing the activation of lipoate, forming lipoyl-AMP while LipL2 is required but is not capable of catalyzing this reaction.
Subcellular Localization:
Mitochondrion.
Sequence:
MKRIFRLVRRCHYSTEKRTNGPLVLVSNNQNIHFNLSLENFLLNNYNDLLKYLNINTIEKFNEPILFLWRNNRSIIIGKNQNIWSECNLKNIKEDGVLVARRFTGGGAVYHDLGNVCFTFLNNNINTSSNFLIILNTLKNHFNIEAKTQGRNDITVNDQKCSGSAFKKIKDVFLHHGTILINLEKNILNKYLTPDKIKYIKHGVSSVNARTINLSEINNNITCENLCIALIKEFTKFYEQNYKENINNIKNLENNINNSNFQNKEQININNTNENNLINNTNIIPNDITVHYIDQNNNITKNPEFLKYYNLLKDWDWCYGKTPKFQNHIWKQFTFGKLELFFNVSNGFIKDGNIFSDCLDINLIDHLKSIFNNDIKYSKEDISIFFKKLNVENKNYLDEVRSWILQEL