lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Microtubule-associated protein regulating the stability and length of the microtubule-based axoneme of photoreceptors. Required for the differentiation of photoreceptor cells, it plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme.
Subcellular Localization:
Cell projection, cilium, photoreceptor outer segment. Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MSETPSTSFSMIRLTSSEGQVPSRHSNVTHPTVAKRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDNLSRKVPLPFGVRNISTPRGRHSITKLEELEDGESYVCSHNKKVLPVDLDKARRRPRPWLSSRSISTHVKLRSATATMPTTAPGLFRAPRRLVVFRNGDPKTRRVVLLSRRITQSFEAFLQYLTQVMQYPVAKLYATDGRKVPSLQAVILSSGAVVAAGREPFKPGNYDIQKYLLPVKLPGISHRVHRKGKAKIEKRKMSTHSVPRPQTDSLASEKTYDCFSDFSVAPENYLALETHDSQTLSTYPSEDGVEKSIVFNQDGTMTVVMKVRFKIKEETVKWTTTVNRADLSNDDEKSKISSYPGKTEDRSSSLKLVVPCSLSEDITDTTQQGSLTEEENTQMTEQQALSSSSAGWENASMEVGIQGSQKQVKHFYRPPTPGPRRMRQKKSVIGTVTVVSETEVQEKQFSYREEREVGEKSKYHMFTHSCSKMSSVSNKLVQISSDDERESALERTKESGPLKSHAINAGAIEITSQRVLKMCHNNALASTVPENSVVEEGTDDSAISGKATIKHFRTCGNANDSFSSTTADTTLTSGNNCPNVRTISEVPSVGSPVLTTGLVNEFAHCGLTEHPGNGRQISSPFASKKKKKSQQRMITSKDKKKVIETKGIPNKVGKIHRAGTIAQVVLLQDSGGLDKEGRVREEELDTSPMVIESHDIFPKGNSKFSKNFHKNKLNTVQNPKTQKLLAKRKSRPLKIKSIGELRKQETGQEDKVFLHSESKLCESNLEKQSLLHVFSSLEEDQKALHRSQSQVETVTENWKGMTKKSLVPKVNDLHVTVRNQRKQKGVKLKSGATVSEQHIATRADPLASLKKPDLTEGIPHHSVKSYIQRWLQNINPYPDFEHRKSAPLGQDRSNVVNYNSNGFPENNLPTTSSKGKSFLMESNKRKTKNANWKGNKNQETSKSLVVKDNGEQPNKHSCESQDESLYDSYLGPLHDNCTLSQTSINDPCTKSHLSTEKSRPEVKLVYQEMNFSTKRQTLEVAIQVDTMGENVPKDLLALLLQHLEAFIPNNQKHQNGISQLPGSLAEVVFPSAIYNSSTNLLLAWLLVLNLKRNMNSFCQSDAPKTTSRSSETAALLDVLKHVAITEEADDLKAAVANLVESTKTCSGPSGREQDTAPANCIAASLHSVDKCKENKSTQKSLLDEGYSVRGDCGPELCVLEMVSKSNNTPSEGHTVSMTYPPKGVNNQNDALFTSNDSSTMSQRSTHNASFLGEACLLTDSLCSHKACAQKDNIYEAACLSDETHIPIRDCKTIEFVNSKENKCTDNLELTEEIKTVDKVPKDLNILADSIDKNESDISTSSQNVNKLSSQGIFLSKTHLDSDKDYSPLEEFQNCPPKKIVNKKKSVSSDKEDSRTSEEPRSITNSVTSSERNATSELESFEESESQDTGIFNMKVRTEEKAAKESMQKESEARMSLELINISGRNIIEQGRRNTAFLETTGRGQVTPPSLVFCYDSNKNTEKEMSVGETKMRVKKIVDSMENESYTDSSLNCNKQHRSPGTLDWSDYGSDSESRYPCKALSYEHSDDTGQEREYPRGIVRRAIEKLYGKAEIIKPPFFHGSIHKSQVCPYNPVEVPCVKKTHFYESECQSLVSSEQVSRSSLMLQEFQEERQSEVDANGMGDSFGDSSIEKVTKPSEHGRVFMEKEKGKLIDNGKWLLRENHLWRVSLDNPGMYGNADTTSVDTLMDKNSIEVPYSHFGELAPGPTMAELSSSEIEEMTQPLEVKCNYFNFPHGSDSEPFGEDFLDAQNTNCPKEKIPNHHKEEKRNSPSERTCTPVTQTFASAGNKVHPVCSDVIKTQPLPGSSITHGALQEGDSLDKLYALCGQHCPILTVIIQPVNEEDRGFAYRKDSDIENSLGFQLWMEIYPFLLQSKKNMFTSESRKVNVGKQFTDNAIGNLCDRLYFKNMIDLVDKRANSLREEVNLNKVQLYLKKRFSDLLPSSSLVVWDMNSVSLTPSNWTDNFKSVDENNFINRFQNSRKNPNQVVREENSCQFHWELFGQVYLLDICQVEKSLHIKTRSKLEIYYILGGEVLFIWEEENQLNIIDIESPNDQNDL
The following text describes a protein:
Function:
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side.
Sequence:
MVPYVQISRINRPAGTFMLLWPCFWSISMAAPTGQLPDLSLLALFGTGAFVMRSAGCTINDMWDKDFDKQVERTNKRPLAAGKLTYPQAWGFLAGQLSAGLAVLLQLNWYSVAMGASSLALVAAYPTMKRFTYWPQAFLGLTFNYGALLGWAAVHGSCEWPVVLPLYAGGVAWTLVYDTLYAHQDKKDDVKIGVRSTALLFGDNTKPILNVFSAAAIAGFGTAGYMAGLDWPFFLGLTGGAAQLAWQVNTAKLDDPINLQTRFASNKWLGALMFASIVAGNVV
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase.
Sequence:
MPSKQTSSVREASFSINEQFGGRILKKEEQVFEQNAWDHVEWDEEHIEYAKQCIEKQKQNPVAEVEKYMEQPASFWDKFYERNEGNFFMNRRWLAQEFPEIMEALKEDAGEKRIIEVGCGAGNTIWPILGANKNPQLTVFGVDYSSKAIDVVKETPAFQESDIVQASVWDLAGSTLPENVEPESCDIVILIFCFSALAPEQWEQSISNITRLLKPGGLVLFRDYGRWDMTQLRAKGNRLLGDNFYIRGDGTRVYFFTNEELENVFGSNFAVLQNGVDKRLLVNRKKKVKMYRCWLQAKFQKKIQS
The following text describes a protein:
Function:
Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide.
Sequence:
MLQSARILLSVAHLLPCIIQRSESSSLPNETTSSSQQLPGNLNASSFQIPSLSSILPSANSTKALNGLNGLASPAPIAPLSPDALAKQSEFDRKNIPARPVHAAGAGAYGTFTVTTNFAQSQTSMDLFSNVGQTTPVTVRFSNALGEKGSFDTARNVRGFAMKFQTKQGAWDLVSNNAPVFFIRDPAKFPPLIQSQSRDPLNNLGNADTAFNYFPNNPETMNMFLRIFSSAGASRGWIHTNAWSINTYRWYKSDGTWSYVRINFETKQGVLNFTASEQAQISDPSYGARELYSSIQAGQFPRWTMFAQVLSPKDAENFRYNVLDDTKEWPTSLVVPQEIGVLELNKNPANYFTEVEKLAFSPANVIPGWAASQDPVLQMRLFAYSDSSRYRLGSGNPTKMKKRFLQNAQTLNNPAQILKNSAQMLNNPTQIPNGSTTTAPKYDSGHSLWINQALKSLNQISPIDFEQPSFFYGNLTQDQKSELIQNIAGGLSVVSSLDIQTNLINWLAKASPDLSQQVSSKLKMMTG
The following text describes a protein:
Function:
This enzyme has both lysozyme (acetylmuramidase) and diacetylmuramidase activities.
Subcellular Localization:
Secreted.
Sequence:
MPDLPFKIIDVSKWQNEIDFQAAKDNSQIQGVMIRSSYGSYDPKQIDTMFENHMRNAIASNMLIGTYHYGYARSVEQAEREADFAISVISPYKDYIKFPVAYGVEDAAMNVGKELVADMVIAFCNKVKAAGFKPMLYLNLVWANNYCNMDRINEAGIDVWLAEYNSYCKYTGPKTMWQFTDALSISGYPEPVDASWVYKNYE
The following text describes a protein:
Function:
Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.
Subcellular Localization:
Cell junction, adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, podosome. Cytoplasm, cytoskeleton.
Sequence:
MPVFHTKTIEQILEPVAEQVSHLVILHEQGEDGAAIPSLMKPIQAVSAAVNNLAKVGTAQIQTSKDEVLKLDTPEAINKVKSSADLLLDSAKLIEEDEYSKQGREKLIAGSRGILQGTSDLLLIFDEAEVRRICHVCRRVRDYLKVSEVVAGMEDLVTYVKNLTPGMTNLSDLVLQRSKDLTNALHADQLKTGVADLRNQLPNLISSMKIFVTTVDGSGVGSEASVHNRQYYVKNLSDIITEIIRVLQLVSTDQEILVDPTNVLQLKQVRDKMANNLIAANRWLNDPNAPPDTADELALRQTLDQAREIGSKAGGALGAKIMDKCNDIGIMTEKLAALRKQNKGNSAEARRLANQIQTALNGLLQDVDDALKNLEEIDEAFGVVSSKTPSAKEWLADPQAKPGPGTGSQDIRDIIGATRKIAKSLATNPQTAKDAAELMKMCDELDELMEKLDAYRERGEGHLPEARHLAKQAADKIGQINAKIGKALASGGLPQTLEAKLDVANRWLDHPGVEDGGKGMLAARSVMSDARKLAVECDNPVIKAALLQNAAECESLCNQLADLVKQGKGGSPEARRIAEELQQKLQELKQNMKLAVIGQVADEFSDTTTVLKQFVTAASAPKDVAGREEKFAERSQALTKQAQKLANLGIQAVATSELGAEEKVAKATLSAKKIQELTPQVINAGKIVLDYPENKLAKEHLKALTDEWTEHVDDLTEQVDDAMDVVDFIKASEDGIKKDHKTCMKALQDNQPTVALPAAGNIARRAHRILMAGKREVENTDDAAYVQELKGNLNNLSRTINPMVQATREYANNPNSNAAKDNVRECDDQLIAAVAQVRNTVEARRIEQQAKNIVIEEEPPPVPPLPQDCEAAPPVPPLPEEEEFPEEQEEDVPMMQAARELHEEARKWESKGNDIIATAKRMALLMAKMSHLVRGEEGRKSDLIACAKEIAKASNEVTRLANEVADKCSDRRIRTDMKKTLDRIPTISTQLRILSTVKAASLGDNMDMTKEEEEAAEQATEMLVHNAQNLMMSVKDTVRSAEAASIRIRTEAGVMMRWVRKS
The following text describes a protein:
Function:
Regulates lamellipodial actin dynamics in a Cortactin-dependent manner and is therefore likely involved in controlling actin branch density, actin-retrograde flow rates and lamellipodial protrusion. Functions by slowing the dissociation of Cortactin from Arp2/3 nucleated branches thereby increasing branch nucleation and junction stability. Associates with core striatin-interacting phosphatase and kinase (STRIPAK) complex to form CTTNBP2NL-STRIPAK complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (By similarity).
Miscellaneous:
MISCELLANEOUS: Named 'Nausicaa' after the princess in Homer's 'The Odyssey' who helps to ensure Odysseus' safe passage home from Phaeacia.
Subcellular Localization:
Cell projection, lamellipodium. Cytoplasm, cytoskeleton, stress fiber. Note=Localization to the lamellipodia is dependent on Cortactin.
Sequence:
MEQNSNSSVADTFAEAPATDADYGTENCSGSGMSVGDTVSANHEFQTMKPGPGVVHKVMPVANSASSATATNGRTRSEMPHSELVKMLYYLEGELQARDVCIAALRNERVKQLIAQLRTKRLQPNDPYAAIFRDKIALNGNLISRESSTQAAQAEMEVRQIIEQQMEQQYQMVSKQRATHVRMVNILTESLENNQRMLQELEEEKRKHENTTAQGDDITYGLELERNKLKQDLEEERAQVAKMEKDLKKLQETLEYERNRQKQIVLLLIAERKKILMKYIEEGKRSEDLAQILAEEKQRSDTIAEGLEEESKKSLRMEEELEKQTHAMEQERKVLFAKLAKEELRVKELEQELNALRSEHEALKKQQQLGGSGSSVAAAKARQFSDDACATPPMVNIAKIVQPTATVSSMPVSGPQTGIARSIAPGQNIRSAGIATAPTGTATAAIAPLTAVLNHTTTITTTTNNTTTSSNSNSSGSIGVAATAAAVAASVETAATVTVPMVAPPSPSPAKMQPTATIQRAPGGKYAALAAAAALDQTTTPHPHPVPIAVPPVTVPPAGARGAPPPIPTKPIVPPKREPSLSRLGSITGSSAIAAATAATTAAGTAKQN
The following text describes a protein:
Function:
Extracellular matrix serine protease secreted by pioneer neurons that plays a role in layering of neurons in the cerebral cortex and cerebellum by coordinating cell positioning during neurodevelopment. Regulates microtubule function in neurons and neuronal migration. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Domain:
The basic C-terminal region is essential for secretion.
Sequence:
ENVQFQWKQENLQVGEVYEACWALDNILIINSAHRQVVLEDNLDPVDTGNWL
The following text describes a protein:
Function:
Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the brca1-bard1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin (By similarity).
Subcellular Localization:
Nucleus. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
Domain:
The tandem UIM domains form a continuous 60 Angstrom-long alpha-helix and mediate binding to 'Lys-63'-linked ubiquitins. UIM1 and UIM2 bind to the proximal and distal ubiquitin moieties and recognize an 'Ile-44'-centered hydrophobic patch. Since UIMs don't interact with the 'Lys-63' isopeptide bond the UIM-linker region between the 2 UIM domains determines the selectivity for 'Lys-63'-linkage, and its length is very important for specificity (By similarity).
Sequence:
MGCRGQNCSEKRRAIRDHFIVISDSEGEEEKEVIRFGKNIAQPDGRRTSVKRKIAQMTEEEQLALAVRMSEQEANHVNYSQEEEDELLRKAIEESLHSCTVSEPCNTTTQQNTNTLHSTNRTLAAEDCSEKHPISQNCSLSEPPNNITVQQVYKETLSTNEPVKLQEHAEEKSFSQVSALFELPSGAAEQQMNKEAHSTERPVVTGDVVEEGHLSQTFTVSETPLSATQEMNTEDFTTSATFVTEEVGEALTQYSTVSSQSRHKSPVVLLMRLSQDIVESSSVILSPKCRDPFSDMESGMASSCPSNSSNFVSMLPHKALTLSPVFPKQLPRRLGLSPRKLFQGASLTSDSKEQEVDDQCSHCSESSELDYSVLPNSLQAEPFKSNTATEVLKENNTLLNGVTTEEQTGASNSCLDSQRQSGSTVHYYWGVPFCPKGEDPNLYTQVILCQLEVYEKSLKKAQRQLLRKMNFGEPVQLSAPPLRRTERGKADSQDSLSQESEDLKDEDSPRPVDDEEVDSEKPMNQCVSSSSRQPAESLEEESPIPAQDEQDNNSQLILFLNMNNSHSTSLPL
The following text describes a protein:
Function:
Transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MTMNKNMRRFNEQQIKSLEVMFEAESRPEAQIKHQLANELGLRPRQVGIWFQNRRARLKTKQVERNCCILKASYDSLASNFESLQRENRELLLQKLKKQLGKGHGNEKGRDPMFESKETPRILSESADQKTNMLLGDVNCRHAECTVDETGIQNIAQPMDGSQASPGDRHSLECSCLPDESGGNSQWWELWS
The following text describes a protein:
Function:
Involved in the biosynthesis of hydroxycinnamic acid amides, which play a role in defense against pathogens. Agmatine is the preferred acyl acceptor, lower activity is observed towards putrescine. The preferred acyl donor is p-coumaroyl-CoA, lower activity is seen towards feruloyl-CoA.
Sequence:
MALKVIKISRVSPATASVDPLIVPLSFFDLQWLKLNPTEQVFFYKLTESSSSRDVFYSSILPKLERSLSLILTHFRLFTGHLKWDSQDPKPHLVVLSGDTLSLTVAETDADFSRISGRGLRPELELRPLIPELPIYSDSGAVVSLQVTLFPKQGFCIGTTAHHVVLDGKTAEKFNKAWAHTCKHGTIPKILPTVLDRSVVNVPAGLEQKMLELLPYLTEDDKENGRTLKLPPVKEINAKDNVLRITIEISPENIEKLKERAKKESTRAELHLSTFVVTFAHVWTCMVKARSGDPNRPVRFMYAADFRNRLEPPVPVTYFGTCVLAMDFYKYKAKEFMGEDGFVNTVEILSDSVKRLASQGVESTWKVYEEGTKTMKWGTQLLVVNGSNQIGMYETDFGWGRPIHTETMSIYKNDEFSMSKRRDGIGGVEIGISLKKLEMDTFLSLFYKWIGN
The following text describes a protein:
Function:
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MSGPLLTEADAPVLDNSFRNVLVLYGLPDPEASKMAKLEKVIISKVLKDYHIVEHRFLVDEDGKGRGVAFLEFETVEAANTALVALDGYKLDKKHTFQACLLEDMDRILKTEDEFQAPPEEALDSKLNELQSWLLNSDCYDQVALRYQNMTSIGWNMRNRVNIACEREGWSELGVQWSPLGSYLATFHQPGISLWGTEKFERINKFAHMGVKFIDFSPCENYMVTFAPATPINEKDPRSIIIWNLKTGEQMRGFMPPRKYRSAHGEVEEMWPVFKWSHDDKYFARMTDADTLAVYDTESFKKLDNRGIQITGLQEFAWSPRDNVIAYWQPEIAQRPARMGILDIPRKEDLTTRNMFSVVACHLVWQKSGEHVCVHVVRHNKKKTQLYSDFQIFHMNGKDIPCDQLELHRPVVGFFWAPEGNRFAVISGQHPMTRVETYSLESRKIVKHPEHLDITCESVFWSPTSQHMILADRFKMNSQLVFVDANTMETIRIVEHAMVTDIEWDPTGRYVASIASASKTQVDTGYIMWSFQGNQLHKMNRKHFFQLLWRPRPKELINDDDLKEIRRNWKKYQTNFEAADKMMMDQADEETLQARRAMLEDWSDWQMSVEKRLSELRARLKKLRPEDQEDIVEIVETVEVPVKVEEVIVE
The following text describes a protein:
Function:
Involved in 20S proteasome assembly.
Sequence:
MVPEKTQYFIPSSPNLDQSIFKGSILILPVVSLANVPQLAIDLMIHSTQLGPIQKVGILDPQDHIPVIGAIDHLSDLPQSQDIRNQVTTPIQVYQSPDKLYTFVQQRSPVIKARKDLHVSKMKAWISTAGFASVLMLVSVDAAARSDSHLRHPSAFFHYIRANQPDPPTALRQIIQTRYASFLPQDAPGLPIFCAGGLAARLLAALTSSSPDTGSVEINTLVAYVAEGDNRLDAKAFACEVVSIFNHIRSGQSDLQAFCPDSLHEPVSWKASDSYQDRTRQDIYG
The following text describes a protein:
Function:
Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Sequence:
MNIATITLNPAIDQTVFVDHFQLNTVNRARAMQRDAGGKGVNVASFLADYGLSVTATGLLGAENPHIFERHFAAKGITDRFVRVPGATRIGVKIVDEANQQTTDINLPGLPPPPAALNTLIDVIDELAVNHEWFVLAGKLPPGVPIEFIPNLVARLRSFNCNVALDVSGPALIAGLQAQPSLVKPNLDELRQIDLLDGEGLEAVGNAARRINQMGVGLAIVSMGAQGAIFSDGTQLLHAIPPSVTVRSTVGAGDAMVAGTIAGLVEGLSLTEIARRATAFSLAALGSIGAHLPPRAELIALAAKVTVTVVDPAVTTVTPVDQ
The following text describes a protein:
Function:
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
Subcellular Localization:
Nucleus.
Sequence:
MYREPERVDDEEDKEDDAPVGYNPALRKRRRRRRKDTRTAGWVIEDSEGKNKYNGTFEGGQSSTYMLLVKNRHNDEFSVIPVEQWFRFKKPLNYRTLTLDEAEEMNNEKKRAVERWLMKHKLAGEDKSDAAGDSVSAPRVRTGALATATARTKTGEGDNIFGGTTEAKPRRAPRPKARGEGATGEDGGDFEEKFDDDESDAEIHNDAPQGIESDSDEDEFEVDPEGTGKLTETGQAMKDLLKRAQNGEMLENKEKDEEEDEEEEDNFTAKDMDVIKRDLGGNIIRDRSVAVGDAGASGDAKAGATVADGASTADSNGKAKAPTGADSGNGKRKAEEGRMKEETPSKAAKTSAASSSTKLTEAGVQQELIRYGGRMRTRDLLRKLKKLIVTDNDKALLKDILRTICDVEVDAIDGRLLVLKSQFR
The following text describes a protein:
Function:
TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MNFKTVISLFLVLFVSFVYCENGAELLFHKKIVEGPVVGKELPIQFIIYNVGSEPAYDISFIDNDFSNAEFEFVSGSSEGKWETLAPNSQVQTNLTVIPKKSGIYSLTSTVLNYRKTQTSSEFTVSSAASYSGMYVESQADYEKRTSLLIKEWITFFVLCAGAIALPYSISTYYKKNYENGIKK
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
METRRLEGKWENEEPDTEDPLDTIKREMDPVPGADNSLNNKWRSGSERSIQLRAAAVQVLHTIGSSNSPVEAEESSCPRNEKVSEGGKPYNCSKCGEPFSTKALLSAHKPIHQKKEPKCGRSSSKKKQRHLRSQAKDNPVTCRELEDKFSEKPHCKKGSLNTGSNIHNKEKPYTCTECGLSFTAMAKLLRHQGNQTVEKLFSCPFCGKCFPRNNCRLSHQKICGKSFSNLHTHQINQNKTKPFTCFECGETFSQIGTLRSHQRIHTGEKPFSCTECGKTFSQMSTLRSHQRIHTGEKPFTCSECGKSFSLNSTLHTHQRYHRKENNFVCGECGNRCYTKSQLLQHQRIHTGEKPFICTSCGRSFTRKKSLQDHQRLHTREKTELEESGTTLCA
The following text describes a protein:
Function:
VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MISWLARTAIFLRLTVPAMHAATNPGDNAAEFKALCAVIKLAKIQPSDLQPGTEAEKALKEIEVLNMSVADEKWQKQYGDGTEKFAWSTFESKLGDTDPKKHWKENWQNWLDTKKRLEAAKKTDEWKHTHPAPASSEARQVASKQIAALTAAATKLYQDFKTKADNLNTADREAVTSELAKALHGADKVTAEGQVTPHKTPDGVRSGTSCNAAASGQRLLTDLMCICAGQTQLTSKACTTTPLSTGWTGGFGNAATQQAELEAKCGTGYPADLTAENIENAVHGLEILVGRHSGTNNKGGYLGKDAGANCDGTDGNICADYTNYFKDAANTADAELPWAKHTRLAATALINRAKNFRAAEGLAERIETIKIQTESTFQLTQFTFPTQKAEAAEEELTTSKNKDCNNHKTNSTCTENKCKWEGTSETVGECKPKDGENKTNAAGTEGAAGATNSEAKKCSEKKKQEDCKDGCKWEGTECKDSSILENKQFALSMVSSAFVSLIF
The following text describes a protein:
Function:
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC3 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC9 and EXOSC5 (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Nucleus.
Sequence:
MAEAAGVPAESLAGCRARAARTVLDQVVLPGEELLLPDQEDGDGPGGAGERPLRLNAAARSRGRVVCGPGLRRCGDRLLVTKCGRLRHKEPGSGSGGGVYWVDSQQKRYVPVKGDHVIGIVTAKSGDIFKVDVGGSEPASLSYLAFEGATKRNRPNVQVGDLIYGQFVVANKDMEPEMVCIDSCGRANGMGVIGQDGLLFKVTLGLIRKLLAPDCEILQEVGKLYPLEIVFGMNGRIWVKAKTIQQTLILANILEACEHMTADQRKQIFSRLAES
The following text describes a protein:
Function:
Part of the Zra signaling pathway, an envelope stress response (ESR) system composed of the periplasmic accessory protein ZraP, the histidine kinase ZraS and the transcriptional regulator ZraR. The ZraPSR system contributes to antibiotic resistance and is important for membrane integrity in the presence of membrane-targeting biocides. ZraS is a member of the two-component regulatory system ZraS/ZraR. Functions as a membrane-associated sensor kinase that phosphorylates ZraR in response to high concentrations of Zn(2+) or Pb(2+) in the medium. Binds one zinc molecule with high affinity via its periplasmic domain, inducing a conformational change that is transmitted to the histidine kinase domain and leads to the activation of ZraR. The system has no direct role in zinc or copper resistance.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
Contains one high-affinity Zn(2+) binding site per monomer.
Sequence:
MRFMQRSKDSLAKWLSAILPVVIVGLVGLFAVTVIRDYGRASEADRQALLEKGNVLIRALESGSRVGMGMRMHHVQQQALLEEMAGQPGVLWFAVTDAQGIIILHSDPDKVGRALYSPDEMQKLKPEENSRWRLLGKTETTPALEVYRLFQPMSAPWRHGMHNMPRCNGKAVPQVDAQQAIFIAVDASDLVATQSGEKRNTLIILFALATVLLASVLSFFWYRRYLRSRQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVKPTHLALQAVDLNTLINHSLQLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLDAIFTPYFTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGSTFTLWLPVNITRKDPQG
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MSGTVKKVTDVAFKAGKKIDWDGMAKLLVTDEARREFFNLRRAFDEVNTQLETKFSQEPEPIDWEYYRKGIGTRLVDMYKQHYESIEIPKFVDTVTPQYKPKFDALLVELKEAEEKSLKESERLEKEIVNVQSLKKRISTMTADEYFAEHPELKKKFDDEIRNDNWGYSHYKEEQNA
The following text describes a protein:
Function:
May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MMSFPRMLSLCLSVLVILPLPLQSVDPLTIGAVGAVALGAYFKEHTYCRFAECCDDRNIPARIDELERSLERTLIGQHIVRQHIVPALKAHIASGNKSRKPLVISFHGQPGTGKNFVAEQIADAMYLKGSRSNYVTKYLGQADFPKESEVSNYRVKINNAVRDTLRSCPRSLFIFDEVDKMPSGVFDQLTSLVDYNAFVDGTDNTKAIFIFLSNTAGSHIASHLGSVMKNGRLREDTRLSDFEPLLRKAAYNMDGGMKKTTMIESHVIDHFIPFLPMEKAHVIKCLEAELLRWRRDPKQANNQKIIEDIINSSISYDRTHSLFAISGCKTLEKKVAMAIY
The following text describes a protein:
Function:
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MNELLLNVVDPLHQWFLGLGDGGVLLWTVLKILLIAVPVIVTVAFYVVWERKLIGWMHVRHGPMYVGMGIFQAFADVFKLLFKEILQPSSSHKAMFIIAPLLTLAPAFAAWSVVPFDAKLVLSNANVGLLYLLAMTSLGVYGIILAGWASNSKYAFLGAMRSAAQVVSYEIAMGFALVGVMIASGSVNLSQIVFAQAGSSGFFDWFLIPLFPLFIVYWVSGVAETNRAPFDVVEGESEIVAGHMVEYSGGAFALFFLAEYANMILVSFLISIFFLGGWLSPIQGWVTADISPWVNWLWTGGWPWLLMKVFFFASAYIWFRASFPRYRYDQIMRLGWKVFIPLTIVWIAVTALMVFYGVIQKGV
The following text describes a protein:
Function:
Binds to core histones and functions in the ATP-facilitated assembly of approximately regularly spaced nucleosomal arrays. May participate in parallel with other histone-binding proteins such as NAP-1; [Isoform 2]: Inactive for chromatin assembly. In vitro it appears to form a high molecular mass aggregate with the core histones.
Subcellular Localization:
Nucleus.
Sequence:
MAEESFYGVTLTAESDSVTWDVDEDYARGQKLVIKQILLGAEAKENEFNVVEVNTPKDSVQIPIAVLKAGETRAVNPDVEFYESKVTFKLIKGSGPVYIHGHNIKDDVEVVDMEEDDEEDDVAEDEEDEHPKKRAKIENAADGKNAKNNKKK