lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Regulates the endosomal recycling back to the neuronal plasma membrane, possibly by connecting early and late recycling endosomal domains and promoting segregation of recycling endosomes from early endosomal membranes. Involved in the localization of recycling endosomes to dendritic spines, thereby playing a role in the maintenance of dendritic spine morphology. Required for the activity-induced AMPA receptor recycling to dendrite membranes and for long-term potentiation and synaptic plasticity; [GRASP-1 C-terminal chain]: Functions as a scaffold protein in neurons to facilitate MAP3K1/MEKK1-mediated activation of the JNK1 kinase by phosphorylation, possibly by bringing MAP3K1/MEKK1 and JNK1 in close proximity.
Subcellular Localization:
Early endosome membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein. Cell projection, axon. Cell projection, dendrite. Synapse. Note=Localizes to recycling endosomal tubules that are emanating from early endosomes.
Sequence:
MAQALSEEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKAQEVEVLLSEKEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEGVPGAAGPHVDGELLRLQAENTALQKNMAALQERYGKEAVRPSAVSEGQGDPPGDVLPISLSPMPLAEVELKWEMEREEKKLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQNTELAAELKHRQADYEELMGQKDDLNSQLQESLRANSRLLEQLQEMGQEKEQLIQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEMLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLLQQEQEQEETLKQCREQHAAELKGKEEELQNVRDQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEELVLSEMNSPSRTQTGDSSSVSSFSYREILKEKESSAIPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQEKWMLEEKVKHLEVSSASMAEDLCRKSAIIETYVMDSRIDVSVAAGHTDRSGLGSVLRDLVKPGDENLREMNKKLQNMLEEQLTKNMHLHKDMEVLSQEIVRLSKECVGSPDPDLEPGEAN
The following text describes a protein:
Function:
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Sequence:
MTDFHNKPNIQIMFDSLAPTYDKINGILSLGLHIAWNNALVSLLGETNHLLDLCAGTGRVALSYVQNYPRASATLVDFSTKMLENVQKRHPSAPFSYITSDVTHLPLPDNTFRLASMAYGLRNLSYPLEALREVYRVLQPGGHLGILELTRPATYNPVYLLHKLYLNLVVPSVGRFYSGNSYAYSYLKESIRDLPRDAALEAIFHAAHLRPIRKRKLLFGTATIWILEK
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MALEQSFGEPIIGFGSDEDISLKKRNSVPVPMANAGNLMECFDCNICLDSAHDPVVTLCGHLYCWPCIYKWIQVENSAPGSEETPTCPVCKSHISNSSLVPLYGRGTSSEECRSNEAQVDVVVPHRPQAIWTTATQVNTSSPPSSHVHQQLSHTSLYYPPSSIHHQQFFPHAFGGYAAIAPSTFRGSGMTRLFSPMVVMFSEMFLARMLGGSDASSFSYPYLSPHPIPGVGSSRMRRQEMQMDKSLNRLSIFLFWTIY
The following text describes a protein:
Function:
Transcriptional regulator. Involved in neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3').
Subcellular Localization:
Nucleus.
Sequence:
MFVKSETLELKEEEEVLMLLGSASPASATLTPMSSSADEEEDEELRRPGSARGQRGAEAEQGVQGSPASGAGGCRPGRLLGLMHECKRRPSRSRAVSRGAKTAETVQRIKKTRRLKANNRERNRMHNLNAALDALREVLPTFPEDAKLTKIETLRFAHNYIWALTETLRLADHCAGAGGLQGALFTEAVLLSPGAALGASGDSPSPPSSWSCTNSPASSSNSTSPYSCTLSPASPGSDVDYWQPPPPEKHRYAPHLPLARDCI
The following text describes a protein:
Function:
Involved in gross chromosomal rearrangements (GCRs) and telomere healing.
Sequence:
MVLQYPQNKILVLSDHPHNFLKTQFLQDLFHCSSTGISIVKDQTWENRYYKVHFDLYIDSCKEIPVWVEEFITPECEPLRNVMAGIILITDIRQTKPQELLHQFMIAAHRNTFVVLANVNEEVEQDEIDELNEIWSNAFTNVIEFVNWKRSKPTVNHNDYGEKLGLDRIQEIIDTHDWLNCEVQPATKIREEIPNEMPLEQIIRNLQSARLKYKSIENSSEADAFANEMADELSRYL
The following text describes a protein:
Function:
May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation.
Subcellular Localization:
Cytoplasm, perinuclear region. Endoplasmic reticulum. Golgi apparatus. Note=Localized to perinuclear structures corresponding to Golgi and endoplasmic reticulum.
Sequence:
MSILLSPPSLLLLLAALVAPATSTTNYRPDWNRLRGLARGRVETCGGUQLNRLKEVKAFVTEDIQLYHNLVMKHLPGADPELVLLSRNYQELERIPLSQMTRDEINALVQELGFYRKSAPEAQVPPEYLWAPAKPPEEASEHDDL
The following text describes a protein:
Function:
Transcription factor, which has both transcriptional activation and repression activities. Binds numerous promoters of genes and therefore can be involved in many processes (By similarity). Also modulates chromatin accessibility (By similarity). Required for normal brain development and neural precursor differentiation.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MPGFTCCVPGCYNNSHRDRDLRFYTFPKDPTQREIWLKNISRAGVSGCFSTFQPTTGHRVCSVHFPGGRKTYTIRVPTLFPLRGVNERRSRRGRSRKVSAVVPIITSVVSTANETAPLEEDEEEGDIENTTVVQIGQNGQYIAPVDLTSSGDGSCITAVVSGGEESAVHESCSVADFALCGADHSYSLTTGTTSTELLRKLNEQRDIIALMEIKMKEMKNTIRQLRVTEARLQDELRQREQERERLICANTIIKRKL
The following text describes a protein:
Function:
Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutylpyrimidine dimers (CPDs), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. Required for plant survival in the presence of UV-B light. Not involved in the repair of (6-4) photoproducts.
Sequence:
MAMNTSVAFASCGAVHPGRIRTLKPSASSPSIPTAGPVVYWMFRDQRCRDNWALIHTVDIANRTKSPVSVVFNLFHRFLGAHSRQLGFMIHGLRQLQSSLHSLGIPFFLVRGDVVENLPRFVRECKATAVVTDFTPLREVRKWKEAICECLLDVPFYEVDAHNVVPVWVASPKLEYSARTLRLKINKLLPEYLVEFPQSFSPTEEWKADLPVKIDWDHLIHDVVRDGGDEVPMVDWCVPGENAAMEMLMGSKSGFLTKRIKGYLNDRNNPTKPNGLSCLSPYLHFGQISAQRCALEARIFKKSSSQSVDAFLEELIVRRELADNFCYYQPQYDSIHGAWDWAHTTLMNHASDKREHIYMKVELENAKTYDPLWNASQLEMVHSGKMHGFMRMYWAKKILEWTIGPEEALSIAIYLNDKYEIDGRDPCGYVGCMWSICGVHDQGWRERPVFGKIRYMNYAGCKRKFDVDGYIAYVRKLVGETKKRKIESLLSNPTSKVPKND
The following text describes a protein:
Function:
Probable serine protease which plays an essential role in the innate immune response against bacteria and protozoa infection by activating the melanization cascade. In the susceptible strain G3, appears to be dispensable for ookinete elimination which occurs by lysis.
Subcellular Localization:
Secreted. Note=Secreted into the hemolymph. Recruited by CLIPA8 to microbial surfaces where it is cleaved into the two chain active form.
Domain:
The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence:
MCILTLVERKHLKNMVHVRLLVMMHILIIYSTFGAVRRPINIRVLEGNSCDTPQVIGGKCMNISLCDPAFVHSIAYQEHTPVCQQNAFYRVICCQPFLDFCENSKQFQIMHGIEAEPGMFPHLARLGLKSEEDGIAWTCSANIISERFLLTAAHCNPVNIAGLGCAESMQCDQQNTVKSFISNPKYKTSFKYHDIALVELEQNIRFNKRVLPICPYISKTDLHESEDLVIAGWGATESHFQSPRLMFATVRTVLQNDCKDHYASLLKASPNKKLHQGITDEMYCAQGALVDNVTEYIDACSGDSGGPLQTKQNNNLYLIGVISTGFGCGSSSPGLYTRVASYFGWIKETVSATRDN
The following text describes a protein:
Function:
Plays an essential role in viral DNA replication. Binds to ssDNA with high affinity and localizes to cytoplasmic factories where nascent viral genomes accumulate. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation.
Miscellaneous:
MISCELLANEOUS: This protein is synthesized in the early as well as at the intermediate time of infection.
Subcellular Localization:
Host cytoplasm. Note=Localizes in cytoplasmic virus factories, where it is associated with viral DNA.
Sequence:
MSKVIKKRVETSPRPTASSDSLQTCAGVIEYAKSISKSNAKCIEYVTLNASQYANCSSISIKLTDSLSSQMTSTFIMLEGETKLYKNKSKQDRSDGYFLKIKVTAASPMLYQLLEAVYGNIKHKERIPNSLHSLSVETITEKTFKDESIFINKLNGAMVEYVSTGESSILRSIEGELESLSKRERQLAKAIITPVVFYRSGTETKITFALKKLIIDREVVANVIGLSGDSERVSMTENVEEDLARNLGLVDIDDEYDEDSDKEKPIFNV
The following text describes a protein:
Function:
The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF11, together with TAF13 and TBP, play key roles during promoter binding by the TFIID and TFIIA transcription factor complexes.
Subcellular Localization:
Nucleus.
Domain:
TBP and TAFII18 bind to distinct domains of TAFII28.
Sequence:
MDNLGESPTDKAGEPGESEETRATPGAPVSADTEGIPEETDQVGDADSKEAAAEESELKSQDVSDVTAAEREDPSLLTPAAKKLKLDTKDKKEKKQKVDEDEIQKMQILVSSFSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGEMPPLQPKHMREAVRRLKSKGQIPNSKHKKITFF
The following text describes a protein:
Function:
Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins (By similarity). Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MFIRNVKLIKPSPVRFISPIPFSFPISRSIKISSIRYFTNKSTSNFKSTSSSSSLKSTSTSTSTSTSKTTPKTLSKPPPKVKPPIQDNDTTSSGSSSSENSESFMLKSLFKTIWPKNNLNFKIRVIIALSLLVGAKILNVQVPFYFKQIIDTMNIDWTNEVGVFSTVIGSLILAYGGARFGAVLFGELRNAIFASVAQSAIRRVAYNTFVKLLNMDLQFHLSRQTGGLTRAIDRGTKGISYVLSAMVFHIIPITLEISIVCGILTYNYGASFAAMTFVTMLAYSIFTIQTTAWRTKFRRQANNADNQAANVALDSLINYESVKIFNNELYQASKYDKALMKYQQSSVKIATSLAFLNSGQNFIFTSALTAMMYMGCQGVYTGELTVGDLVLINQLVFQLSVPLNFLGSVYRELKQSLLDMENLFQLQNQPIRIKEIPNAPPLKLNNNNNNNNNNNNNNNNSLPGEIRFENVSFGYHPDRPILNNASFTIPAGQKVAIVGPSGSGKSTILRLIFRFYDINQGRILIDGQDISKVSLESLRKLIGIVPQETPLFNDTILENIRYGRLDASDEEIYRVINQVQLNKLIDDLPDGVQTIVGERGMMISGGEKQRLAMARLLLKRAPITFFDEATSALDTHTEQALLKTIRSVFKQQHQTNVSIAHRLRTIADADKIIVLNKGQVVEEGTHWQLLNEQPNSLYAQLWNIQENLDIEKELLQGDEEEEELTEKLKLDKQELEQEAKLFNSQTFEKK
The following text describes a protein:
Function:
Required for the distributive chromosome segregation of non-exchange chromosomes during meiosis. May be a microtubule motor required to hold distributively 'paired' chromosomes at the metaphase plate until anaphase.
Miscellaneous:
MISCELLANEOUS: The nod(DTW) mutation is a cold-sensitive recessive lethal mutation.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MEGAKLSAVRIAVREAPYRQFLGRREPSVVQFPPWSDGKSLIVDQNEFHFDHAFPATISQDEMYQALILPLVDKLLEGFQCTALAYGQTGTGKSYSMGMTPPGEILPEHLGILPRALGDIFERVTARQENNKDAIQVYASFIEIYNEKPFDLLGSTPHMPMVAARCQRCTCLPLHSQADLHHILELGTRNRRVRPTNMNSNSSRSHAIVTIHVKSKTHHSRMNIVDLAGSEGVRRTGHEGVARQEGVNINLGLLSINKVVMSMAAGHTVIPYRDSVLTTVLQASLTAQSYLTFLACISPHQCDLSETLSTLRFGTSAKKLRLNPMQVARQKQSLAARTTHVFRQALCTSTAIKSNAANHNSIVVPKSKYSTTKPLSAVLHRTRSELGMTPKAKKRARELLELEETTLELSSIHIQDSSLSLLGFHSDSDKDRHLMPPPTGQEPRQASSQNSTLMGIVEETEPKESSKVQQSMVAPTVPTTVRCQLFNTTISPISLRASSSQRELSGIQPMEETVVASPQQPCLRRSVRLASSMRSQNYGAIPKVMNLRRSTRLAGIREHATSVVVKNETDAIPHLRSTVQKKRTRNVKPAPKAWMANNTKCFLDLLNNGNVKQLQEIPGIGPKSAFSLALHRSRLGCFENLFQVKSLPIWSGNKWERFCQINCLDT
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. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A). Modulates PP2A activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSAPIPPSSQELSTEKKKNLPSDKASCMVLSPQRKCSMLFAGRGNSEEMAPPLQQSFMIPRKEINMVSDMGKWKRSQAYADYMGFILTLNEGVKGRKLTCEYNVSEPIEKLVALLNTLDRWIDETPPVDQPSRFGNKAFRTWYAKLDQEAENLVATVIPKHLADAAPEVAVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQMAIVFKVFNRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPNLEPRHFVDEKVVNENHKDFMFLECILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIQPVTS
The following text describes a protein:
Function:
Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar.
Subcellular Localization:
Periplasm.
Sequence:
MTSTQRLWSGALPLLTALIVSIAATASLAGPRARDLGVPFEGTPGALNAITDVAGVEVGHTTVISGDGAMVIGKGPYRTGVTIIHPLGKTSLDGVAAGRAVINGTGEWTGMHLVDEVGQFLGPIALTGTGNVGLVHQSMMDWSVGKVPEEALFSRLLPVVAETLDNRLNDVFGHGLTRDHVFAALDGAKGGPVAEGNVGGGTGMIAYTFKGGIGTSSRVVSAGDTRYTVGVLVQANHGDRNDLRIAGVQIGKEIKGAWPEVNGIVAAGPDAGKPQDKNSLLIVIATDAPLMPHQLERMARRAALGVGRNGSTAGALSGEFALAFSTSHVIPLGGKPRLPAIINDTDSETMNALFRGVVQATEEALVNQLVASETMTGANNAKVYGIPHDQLARIMKARFPRR
The following text describes a protein:
Function:
Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3.
Sequence:
MVRNDVGALVLLLLISVMVISERYLLDRTMAANFFPARFCTETRERSSLQNKRRCRVGYLLSESKEKRIPFHTFKKEYRNSSIDLVKVDVNRSVAAQGPFDVFIHDFTDIVREAEEGDTKAEMFVAELSEYVSRHPNMVVMNPVASWRLLHDRLGAQGVAAEVVKLLNDPDVIVPNRVYLEKSGVKNMMKNLKMAGVTFPFVCKSSSLLLAEHHKMTLVYGRRGLESLDLPCAAESFTNHSGILHKIYVIGDTHFVYARPSLKNFAMSDDLPNVQFSTSDVAKSDSVSPLNAGKRGEPTSQTSPVSDEKISRISDRMRHVLGSSLIGIDVIVQDGTGNHVIIDVNDFPGYHEVGTREFQTALLQLLRTGPCSCIGS
The following text describes a protein:
Function:
Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis.
Sequence:
MNIAEFHQNIEQVWQKIEEELENQGADVDCETQGSVFTITFDNRTQIVINKQEPLLELWIASKLGGFHFAFKNGDWVSNDGQRFWDCFVEACAAHGENVQF
The following text describes a protein:
Function:
Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Subcellular Localization:
Nucleus.
Sequence:
MAAASAATQVAHAASSAQQATRSMRTGVLIHPSTAHSGRFLVLPHPRTLVPTYYLSASSSTSSSISTDQLYELSTLQDSKHDRSWMISRLNQVISSGQLDILSRIDARFLVVSLLYSVLGDGKYRSREDMFEQIALELHVRRSEELCEAIPELKARLATGKDSAEGQQNEWTDVVVFEKLEVTKRALEDVADVQDLPNGEQAYRLSLPKTFALLDSKHSTLSQQSTFISAPNTLGRTFERSWPHDSDPSPYVSLPSPDKEAQDCQDAQQLRSQIAAEIIATYLPDKLAAEYFAHLGIKVDQ
The following text describes a protein:
Function:
Catalytically inactive regulatory factor of DNA methyltransferases that can either promote or inhibit DNA methylation depending on the context. Essential for the function of DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their catalytic domain. Acts by accelerating the binding of DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases. Recognizes unmethylated histone H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by recruitment or activation of DNMT3 (By similarity). Plays a key role in embryonic stem cells and germ cells. In germ cells, required for the methylation of imprinted loci together with DNMT3A. In male germ cells, specifically required to methylate retrotransposons, preventing their mobilization. Plays a key role in embryonic stem cells (ESCs) by acting both as an positive and negative regulator of DNA methylation. While it promotes DNA methylation of housekeeping genes together with DNMT3A and DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter of bivalent genes. Interacts with the EZH2 component of the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B with the PRC2/EED-EZH2 complex, leading to maintain low methylation levels at the promoters of bivalent genes. Promotes differentiation of ESCs into primordial germ cells by inhibiting DNA methylation at the promoter of RHOX5, thereby activating its expression.
Subcellular Localization:
Nucleus.
Sequence:
MGSRETPSSCSKTLETLDLETSDSSSPDADSPLEEQWLKSSPALKEDSVDVVLEDCKEPLSPSSPPTGREMIRYEVKVNRRSIEDICLCCGTLQVYTRHPLFEGGLCAPCKDKFLESLFLYDDDGHQSYCTICCSGGTLFICESPDCTRCYCFECVDILVGPGTSERINAMACWVCFLCLPFSRSGLLQRRKRWRHQLKAFHDQEGAGPMEIYKTVSAWKRQPVRVLSLFRNIDKVLKSLGFLESGSGSGGGTLKYVEDVTNVVRRDVEKWGPFDLVYGSTQPLGSSCDRCPGWYMFQFHRILQYALPRQESQRPFFWIFMDNLLLTEDDQETTTRFLQTEAVTLQDVRGRDYQNAMRVWSNIPGLKSKHAPLTPKEEEYLQAQVRSRSKLDAPKVDLLVKNCLLPLREYFKYFSQNSLPL
The following text describes a protein:
Function:
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MENDSWTTLLGEYQSRKATKMPSNKSMFVLGDTSCDSSTLIAKLKGCNATTAQQLNGLLKFALNERSFPHTLILLTLSMAAPWNWMDQLQYWMKVLDNHIGGLEIDAELKHQCMARLMAKWQSYSDLGSDPLRNSPCKRSNELVPLPLEDAVLTSNLGMEVIVVVKRSDQMATLRRELNYREEHFDFMQQAIRRAGLQYGASLVYTTVKNNINCDLLLQYLKHRIYGLPFGTSASVVEKDAVFVPAGWDSVQKISILYESL
The following text describes a protein:
Function:
As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs.
Sequence:
MASSGGELGSLFDHHVQRAVCDTRAKYREGRRPRAVKVYTINLESQYLLIQGVPAVGVMKELVERFALYGAIEQYNALDEYPAEDFTEVYLIKFMNLQSARTAKRKMDEQSFFGGLLHVCYAPEFETVEETRKKLQMRKAYVVKTTENKDHYVTKKKLVTEHKDTEDFREDLHSEMSGFCKAAEALNTSAGNSNPYLPYSCELPLCYFSSKCMCSSRGPVDRASDSSKDGRNHHKTMGHYNHNDSLRKTQINSLKNSVACPGAQKAITSSEAVDRFMPRTTQLQERKRRREDDRKLGTFLQTNPSGNEIMIGPLLPDISKVDMHDDSLNTTANLIRHKLKEVISSVPKPPEDKPEDVHTSHPLKQRRRI
The following text describes a protein:
Function:
Within the IPP (ILK-PINCH-PARVIN) complex, binds to F-actin, promoting F-actin bundling, a process required to generate force for actin cytoskeleton reorganization and subsequent dynamic cell adhesion events such as cell spreading and migration.
Subcellular Localization:
Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MLGVVGMTNSNMANALANAICERCRAGFAASEKIVNSNGELYHEQCFVCAQCFQQFPEGLFYEFEGRKYCEHDFQMLFAPCCHQCGEFIIGRVIKAMNNSWHPECFRCDICQQVLADIGFVKNAGRHLCRPCHNREKARGLGKYICQKCHAIIDEHPLIFKNDPYHPDHFNCANCGKELTADARELKGELYCLPCHDKMGVPICGACRRPIEGRVVNAMGKQWHVEHFVCAKCEKPFLGHRHYERKGLAYCETHYNQLFGDVCFHCNRVIEGDVVSALNKAWCVNCFACSTCNTKLTLKNKFVEFDMKPVCKKCYEKFPLELKKRLKKLSEPLARK
The following text describes a protein:
Function:
Catalyzes the conversion of quinonoid dihydrobiopterin into tetrahydrobiopterin.
Sequence:
MVYRVHRKCMQIAHCTSSGGRCKGREIFTPSFLTNHMRGSDKDRCKLIYRTTNCIHTAETHTLFDRLMNKSVIELGPVDSIGHSADATRQKLINKLKVEKPYQEYVQAKLKIQEACFVQEHRARSRLSPGYGGNRSPGYNDVRSPGYDRSPGYNDGGRSPGFGGRSPGHSGRSPGYGDARGRSPGFSGGRSPRYDAGRSPGYAEGEGGRSPGYGGGGRSPGYGGGGRSPGYGASGRSPAYQDRSEATFDDLSTTFNPDALLGSYKEKSTKTEPQLRTVKQEPRDDLFSSSDTASNATPTTSNASRKRPPSPMSSMSSVPIKVVNQTPTGYATRFSQPTQPVRPTGNGMSSDTANSSSSYNHLTPNNHHNGTTRSAVPPPRIPHNQATPSSSAQPAPNGIASSSSHNHRPPPPPPPPSYPNQAQWMPPNERGPGYGQPPPMHYGGYPGSYLPAPGTPMPGMGMNWPQVNGNGGPMPFQNGQSGYVQPMIHPNPYQNRPGGPPPTSYGAGQAQPQIPNTGPPRPVGPSPIGWPEWTERAIEASMTRGAVEVGDDLIMRMAWSTIKLPLIKYARMSSQRVLVYGGKGALGSALVHSFKTRGYWVLSVGENESADASISVPKDCSSVVDQEKHVLSEVARTLSDGCKLDAILCVAGGWAGGNAANEAMVRNADLMVRQSVWPSLIAARLAALHLAPNGLLQFTGAATAVAGTPGMIGYGLAKAAVHQLTASLAAEKSGLPSGATVLAILPSTLDTPMNRKWMPKADHSSWTPLPWVGDLLHSFISTPSSRPVSGTLLKLETIAGESTAVPSKI
The following text describes a protein:
Function:
Metal-dependent single-stranded DNA (ssDNA) exonuclease involved in mitochondrial genome maintenance.
Subcellular Localization:
Mitochondrion.
Sequence:
MLKNVAWLRRVTHQKINKFISSSSLFSISSCSSQKVKDILTFPLTHNHETPPTIETTKKLPSVTRILSATKPPEQQLILLNWKKKMIAEMGEEGFNQMQKDTLSAGSACHSSIEEYLKGTPLDKICPKENSTQLWKSVRPVLADVGAVGNTEFKVVHSHLGYSGYLDCNAVYKGTMCVIDWKTSKKRRYRIQDCYDDPVQVVAYAGALNHSSASSNQITHGLVVKIYHDGQTASVFCMNEFMMDYYWQKWLQRLSQFHKMNK
The following text describes a protein:
Function:
Required for the assembly and integrity of muscle dense bodies, which establish the adhesion sites of the muscle cells to the extracellular matrix. Decreased localization of unc-95 to dense bodies and their subsequent dissociation plays an important role in ecdysis during molting. Involved in the organization of the muscle sarcomeric structure and thereby required for locomotion.
Subcellular Localization:
Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Cytoplasm, myofibril, sarcomere, M line. Cell junction. Cell junction, focal adhesion. Note=Localized in the cytoplasm in comma stage embryos, and gradually becomes more localized at the membrane in the 1.5- and 2-fold stage embryos. In the threefold embryo, associated with dense bodies at the cell membrane, but also present in the cytoplasm. Nuclear localization from the threefold stage embryo as well. In adult animals, localized in dense bodies, M-lines, muscle-muscle cell boundaries, cytoplasm and nucleus. Decreased localization to dense bodies during the L2/L3 molt.
Sequence:
MTISPQPSHQQFESYQWTTESRSSQQRHGTGTPSQDGRLSAIPDPVERHVARWRSESRNSNKDKVFRNDEEFSQQDEIVNGTLTALKNDVEQTTEIIRRKQEQMRMERRQFQTEMEVNGRISIDPTDDWLAARLKAVSSDDMNQQLVKLKQDQRQNAVTDTLAALVYDVNATTEVLRRGQRGRDGEDGNKKKKEEIEYTLRLTPAPEEQIPQRPKIPEDDNMETDDYSRQYGVQMSEETDSLRRRRARSTTPRRTLHISGSPPPPAAAVCAYCSEEIDGAILTALAPNSERAQKFHTYHFMCTYCQKALNMHGTYREHDLKPYCHDCFYKLYNGLQYAPDDHQASIEKLI
The following text describes a protein:
Function:
Triacylglycerol formation by an acyl-CoA independent pathway. The enzyme preferentially transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol, thus forming an sn-1-lysophospholipid. Involved in epoxy and hydroxy fatty acid accumulation in seeds. Has complementary functions with DAG1 that are essential for triacylglycerol synthesis and normal development of both seeds and pollen.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MPLIHRKKPTEKPSTPPSEEVVHDEDSQKKPHESSKSHHKKSNGGGKWSCIDSCCWFIGCVCVTWWFLLFLYNAMPASFPQYVTERITGPLPDPPGVKLKKEGLKAKHPVVFIPGIVTGGLELWEGKQCADGLFRKRLWGGTFGEVYKRPLCWVEHMSLDNETGLDPAGIRVRAVSGLVAADYFAPGYFVWAVLIANLAHIGYEEKNMYMAAYDWRLSFQNTEVRDQTLSRMKSNIELMVSTNGGKKAVIVPHSMGVLYFLHFMKWVEAPAPLGGGGGPDWCAKYIKAVMNIGGPFLGVPKAVAGLFSAEAKDVAVARAIAPGFLDTDIFRLQTLQHVMRMTRTWDSTMSMLPKGGDTIWGGLDWSPEKGHTCCGKKQKNNETCGEAGENGVSKKSPVNYGRMISFGKEVAEAAPSEINNIDFRGAVKGQSIPNHTCRDVWTEYHDMGIAGIKAIAEYKVYTAGEAIDLLHYVAPKMMARGAAHFSYGIADDLDDTKYQDPKYWSNPLETKLPNAPEMEIYSLYGVGIPTERAYVYKLNQSPDSCIPFQIFTSAHEEDEDSCLKAGVYNVDGDETVPVLSAGYMCAKAWRGKTRFNPSGIKTYIREYNHSPPANLLEGRGTQSGAHVDIMGNFALIEDIMRVAAGGNGSDIGHDQVHSGIFEWSERIDLKL