lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Adenine glycosylase active on G-A mispairs.
Sequence:
MFDFGDARQLPWRDIAKADGDPNQKAYAVWVSEIMLQQTRVTTVIEYYKRWMKKWPTVVDLARASIEEVLQVWAGLGYYQRARRLHKGAQKVVRDLGGLFPNTPKHLAREIPGVGCYTAAAVASIAFGHRAGAVDGNVARVYSRMRLLGATLGSSPSERALWAAANEAVCPVRPGDFNQAVMELGARVCTLMSWDATQLYPHKAAKKEPRRETHAVSVLRSGDRYLLLRKTGQGRLLEGLWEFPNRQVDPQGSAKKSQDEERRVVLQIGAQLLNSAGGKKRARRLGEVTHLFSHIHATYCVYETTLDEECETEGSWMSAAEVESSGVSTAMKKVLSLAAGRAIET
The following text describes a protein:
Function:
Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAQRGLAAEFWQVPAVTRAYTSACVLTTAAVVRPAPACPPAPAPAPGLLAPPNPALSCPRSSWSSSPPSSSTSTRDFTTGNSQVLGEVESRGRGGPSQPGAPCPLPPRRSGGWSPPSSSSGPWASASSSTCSYCILWGGAGRGGPGGRGCPRGGLAAGEGSYSSPRYRYCRMLEEGSFRGRTADFVYMFLFGGALMTLFGLLASLFFLGQAFTVMLVYVWSRRNPSLRMNFFGLLNLQAPFLPWVLLAFSLLLGNSILVDLLGIAVGHIYYFLEDVFPYQPGGKKLLLTPGFLNLPAGPRQPQATSQWARPRSRGAAGRGRWPRAAAAPARRKGKGARLGRLPRGPGAHQAGAVLARRRMRLGSRLSS
The following text describes a protein:
Function:
Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines (By similarity). May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization (By similarity). May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Note=Also found as a soluble form.
Sequence:
MAKGFYISKTLGILGILLGVAAVCTIIALSVVYAQEKNRNAENSATAPTLPGSTSATTATTTPAVDESKPWNQYRLPKTLIPDSYRVILRPYLTPNNQGLYIFQGNSTVRFTCNQTTDVIIIHSKKLNYTLKGNHRVVLRTLDGTPAPNIDKTELVERTEYLVVHLQGSLVEGRQYEMDSQFQGELADDLAGFYRSEYMEGDVKKVVATTQMQAADARKSFPCFDEPAMKAMFNITLIYPNNLIALSNMLPKESKPYPEDPSCTMTEFHSTPKMSTYLLAYIVSEFKNISSVSANGVQIGIWARPSAIDEGQGDYALNVTGPILNFFAQHYNTSYPLPKSDQIALPDFNAGAMENWGLVTYRESSLVFDSQSSSISNKERVVTVIAHELAHQWFGNLVTVAWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSSPADEIKTPDQIMELFDSITYSKGASVIRMLSSFLTEDLFKKGLSSYLHTYQYSNTVYLDLWEHLQKAVNQQTAVQPPATVRTIMDRWILQMGFPVITVNTNTGEISQKHFLLDSKSNVTRPSEFNYIWIAPIPFLKSGQEDHYWLDVEKNQSAKFQTSSNEWILLNINVTGYYLVNYDENNWKKLQNQLQTDLSVIPVINRAQIIHDSFNLASAKMIPITLALDNTLFLVKEAEYMPWQAALSSLNYFTLMFDRSEVYGPMKRYLKKQVTPLFFYFQNRTNNWVNRPPTLMEQYNEINAISTACSSGLKECRDLVVELYSQWMKNPNNNTIHPNLRSTVYCNAIAFGGEEEWNFAWEQFRNATLVNEADKLRSALACSKDVWILNRYLSYTLNPDYIRKQDTTSTIISIASNVAGHPLVWDFVRSNWKKLFENYGGGSFSFANLIQGVTRRFSSEFELQQLEQFKADNSATGFGTGTRALEQALEKTRANIDWVKENKDAVFKWFTENSS
The following text describes a protein:
Function:
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Subcellular Localization:
Mitochondrion.
Sequence:
MHVVAAKPLFLTKEDVSSDVLPNEREILKSQEESSRKPQIAIEKMVEGRLRKTKMKIQTRGRCNTSGLGDPITLIAFDMASMLELLIFPLMCSIELANCAEKLCHSWNSPIIYLASEGYLLHAIPLSKIFSFPIVYFDFGVALRLIPEDSDRSPQDHSIWNFLLAMSNLLIIPAGVRNRNIMYVGMESSTELISVTLPPRTNLSLPSGQFLLTFSNHCILNPRRFGFSS
The following text describes a protein:
Function:
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Sequence:
MWVGTFHGLCNRLLRMHYRDAGLVQTFQILDTADQLASIKRMVKANNVDDEKFPPKEIQKFINACKEDGQRPGDLEAHDPHRRRLIELYQRYQEQCEREGVVDFGELLLRAYELLSRNAPIREHYQRRFKHILVDEFQDTNVLQYRWLRLLAGDQACMFAVGDDDQSIYAFRGANVGNMADFERDYARGNVIRLEQNYRSCGHILDSANALIENNSGRLGKNLWTDSGEGELVRISELASDALEAQWIVDEVRALIAEGKPRREIAILYRSNAQSRVIEHRLFSQGLPYKVYGGHRFFERQEIKHVLAYLRLMDNADDDTAFLRVVNFPTRGIGARSVEQLADLARERGTSLLRAIPYLQGRAAASLMRFSNLIQDMASQAQILSLPELIEHVVHDSTLLAHYQADREGAERLENLQELVNAATAYAQEQGKELFLTGAKPIACAVCHTLADAGSAGAIGPDLDELKPGKEQILKVMKEGMGAMPSFAQTMSDEERDAVATYALAALPILLLIRVQKFGRRLFVGIVMQDAGRATLFIQPDLANAGTIPDALSMLALIWQTWADAQVTALRKPVKRRAGGIEPAVKPIQPVQQPLRKFVLDAAAGHLPDMRDMFAMAYLHIVDEGVVHISGQNHVVTGSARMPEDIQHGIGGPPQLVLQLGQGLPIHQTGRAAWHAAVMPPARACIKHNQRGLGAQHIVPLTKFQQLLDERVLCVVFKTLMLIGRLGPDGDRVQHGLKDLGAVAPGLTQHIRHQRIAHDLS
The following text describes a protein:
Function:
Involved in the transposition of the insertion sequence IS5.
Sequence:
MSTFFQQTAQAMIAKHIDRFPLLKLDQVIDWQPIEQYLNRQKTRYLRDHRGRPACPLLSMFKAVLLGQWHNLSDPELEHSLITRIDFNLFCRFDELSIPDYSTLCRYRNRLAQDDTLSELLELINRQLTEKGLKVEKASAAVVDATIIQTVGSKQRQAIEVDEEGQVSGQTTLSKDKNARWTKKNSLYKLGYKQHTRTDAEGYIEKLHITPANAHECKHLSPLLEGLPEGTTIYADKGYDSAENRQHLEEHQLQDGIMRKACRNRPLTETQTKRNRYLSKTRYVVEQSFGTLHRKFRYARAAYFGLICARCRLKGSPDA
The following text describes a protein:
Function:
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence:
MSVQQEAAVDGEALEVWIDQDLCTGDGICAQYAPEVFELDIDGLAYVKGADDELLQAPGATTPVPLTLLTDVVDSAKECPGECIHVRRVSDRAEIYGPDSE
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MDWDKLKVFHAAAEAGSFTHAGEQLGLSQSAVSRQVSALEQELSVSLFHRHARGLILTEQGDLLFRTAHDVFMQLQAARAKLTDSRERPSGDLKITTTPGVGINWLIPRLGEFTALYPEIRISLIVTDEELDLSMREADVAIRTRKPTQPDLIQRKLFAMGFHAYCSPDYIKRFGTPRTLEELDSHRIITLSDGTFAPHLQNRNWLVEAGRNGSGPREAYFRVNNILGLVRACQQGLGIAALPDYLIEEQSRLVQLFGESDSIQLDTYFVYPEELKTVARVQVFRDFVVSKAQRWPS
The following text describes a protein:
Function:
Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MMQPVTKTSAPRMLHLLSFLLASVIDQGSSSLVCLFNSVEDLTCNWIPLKNVTNAPCNITAFVDYGDSNKSKTFQLHGAGTKSYRLILKDYNLIPGDDIVLDVFCHNGKKWENVDHLTMKPFVNIQLDPPLNVQMENISKHSCILTWELNVLSHYLTDKLEYEVKYKVYNSGEDDRILPILQDQKWVKIENLSPDTLYEAAIRAKIQKSRNYNSTWSHWSIPTTWKTKPTEPPNILLPVLLVGSLVIVCISITVLGKSTLLKCLKKTVKIQLPNPDEFFPSLNAVHGGDIQKWLSPVTSIDAFHIATAHPEVSVLEIMQKESQESSPLTRKEYSTNVNTPETSGYSSSSCFSNGGYFFFQHDGNSFGIQPCKVYFTYDPLAQEGSGSEDADSCSYKVLHETVDNSQLSPTYNIMAAQENSSFLQEAKSPTQTSEGGSGDFSSLETISTKSSVEEDSNQNAIVLSRSLGQFSMVYSSLPEKIDTGNNGTEVVQNVDLPISSIEDDSSAFLQSIMQNQSQVNVPCRAASHRQFSTSSDGYLSLRDLQSHYSHHSV
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MSVYGWETADGAHRYRRKAKKTGTVVFHTDERVDTTFDRLQKEVIVEKLHFSRKEAEEALADPHHRANSVKTALMTASTAKVLQKTMNFKALLPCQAQCYRGIFNGRDVILHSRTGSGKTLAYALPLIERHLLLEQHQQPASVGAAAGPFLLVFVFSNDLAMQTMSVLEKIYGKQTTLRIAVAGFDDLHPTSDGRAVDILVGTLRSIDEAIRGHRVAAAATAAEEAEAQRDAHLPGKKRPRSARKPQQAVAAAAEEEDDDDGDAAASMSDSNEDEAIAGHGDTREAGIISPARVRAIVVDEVDITLGPHFSAMGRRMKSLLKFIRKANGSLADGLLNDFRAHHYVLCGATIPNWVLKAGFLGVKKYHYQLVAVGSAKLPPHLECFHQICSVADRVRTATRLLTENTAFNGRVVVFGTLKQLTALEAGLHTATATTNAGATEAKTTTPSPSAKKGGKKGNGTSAAAAAAAASSSSLSSSSSLIARALTSQKDELDRMAAIEDFNCGVAQVLLCTDIAARGLDFTEVDTVLMLNLPRDALASDTFVHRAGRTARVGRPGRCILLHDASEAAVVDAIAKSTHVVFKALGPALAAAAGASADALRGGKVKTSAAVNAGASDVALTSMKLVVRNPFRYTKPNVKVPSAMHVFNANLDEPLKALLEDIREEGGSNGEVVLFRVPVSHVHEVKQRLWKYTLQEA
The following text describes a protein:
Function:
Histone-like nucleoprotein that binds to the viral dsDNA and responsible for wrapping and compacting the viral DNA about 4-fold. Forms a nucleoprotein complex in which the DNA adopts a right-handed toroidal conformation winding around a protein core. Binds ito most, if not all, the viral genome, although with different affinity, the highest one corresponding to the genome ends. The formation of the nucleoprotein complex at the genome ends, activates the initiation of viral DNA replication. The binding of p6 would recruit the complex formed by the TP and the DNA polymerase to the origin. Protein p6 also represses early transcription from promoter C2, and, together with protein p4, represses transcription from promoters A2b and A2c and activates late transcription from promoter A3. Protein p6 is therefore involved in the early to late transcription switch. The formation of the nucleoprotein complex at the right end of the phage genome where the early promoter C2 is located affects local topology, which may contribute to the promoter repression.
Domain:
The N-terminus is involved in DNA-binding.
Sequence:
MAKMMQREITKTTVNVAKMVMVDGEVQVEQLPSETFVGNLTMEQAQWRMKRKYKGEPVQVVSVEPNTEVYELPVEKFLEVATVRVEKDEDQEEQTEAPEEQVAE
The following text describes a protein:
Function:
Functions as a GTPase-activating protein (GAP) for RhoA/Rho1 during gastrulation by converting it to an inactive GDP-bound state.
Sequence:
MDAHSRFAPRLPGPAINPIVDNSDEPQPSLSDLHDFEPKLEFDDTELLAPSPLEKDVMVGDFVLAEDPELEPEEDVNPLEDDFEDQLREQSENFQTPRNKCDFLGTDKQGRHIFGIYASRFPEKSQLEGFVREIIKEIEPFVENDYILVYFHQGLKEDNKPSAQFLWNSYKELDRNFRKNLKTLYVVHPTWFIRVIWNFFSPFISDKFRKKLVYISSLDELRQALGLNKLKLPDNICDLDDKLNPSRKPSTPPPSSNINASRQQQHKMATTHQFGVPLKFIVMNSPCLNSIPPIVRKCVDSLSITGVIDTEGIFRRSGNHSEIMALKERVNRGEDVDLKSVNVHVIAGLLKSFLRDLAEPLLTFELYEDVTGFLDWPKEERSRNVTQLIREKLPEENYELFKYIVEFLVRVMDCEDLNKMTSSNLAIVFGPNFLWSRSTSTSLEEIAPINAFVDFVLQNHKDIYLIDVNQRTVSVD
The following text describes a protein:
Function:
Phosphoribosyltransferase which catalyzes the formation of UMP from uracil in vitro and thus may be involved in UMP biosynthesis via the salvage pathway. May also participate in the first step of UMP synthesis by catalyzing the formation of orotidine 5'-phosphate, a UMP precursor, from orotate.
Sequence:
MTAATATANGNHSIEDPVVMKVQAASPIQETDFFENLYQMECFRTGEFYLKSGQMTPIYIDLRRIMSSPRVLRMAAQAMCEKIVASNLKFDYVVGVPYAALPLATLVSDILNVPMLMKRKEAKAYGTKQLIEGVYQPGGTVLLVEDVVTSGESIRETAEAIRNENLLVTDAIAVLDRQQGATANLAEDNLNFLSFLTMEKILDGLITKNEMTEERKHEIIAHLAKPF
The following text describes a protein:
Function:
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
Subcellular Localization:
Cytoplasm.
Sequence:
MNQYVAQFLAYIADERKMSANTTIAYRTDLDQLCAFLHERGIEHWSDVDSETMMAFVINLKEKRYANSTMARRLAAIKSFFSFLKERNVIHHDPTDQLDAPRVDRFPPRAISQHQVDELLEVPLQNGTPEGIRDKAMLEVLYATGMRVSELVALNVDDVAFDHRTVRCRGRQGRERTIPLSDPALTALEEYLDIARPQLARQAPDDPEALFLNHRGKRLTRQGFWLILKTYAEQVGMHDLTPHMLRHSFAAHQLRNGVDLRELQERLGHASIATTQMYAHLAEESS
The following text describes a protein:
Function:
Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Also has I-branching enzyme activity by converting linear into branched poly-N-acetyllactosaminoglycans.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MSLMAHVRRKLCRGHLLRCTLPLTLLLFLTVGLKHLAIDCNLAHNNDIPMGSCMASYYTALNLSAPGEKNCHRIIQGDTEEARRALLDNLMVKKRRLVATDGDYINATSDCKFFRERRKYITFSLSQVEQDFPIAYSMVIHDNIEMFERLLRAVYTPHNIYCVHVDKKSPESFQQAARAITSCFDNVFVASKLESVVYASWRRVQADLNCMEDLLQSNVQWRYLINTCGTDFPIKTNAEMVKALKSLNGHNSMESEIPPNYKKRRWEYHFELKEDSNKIVQTNTRKKPSPLPVPVFSGNAYIVVTRNFVNSLFVNPTAKKFIMWAKDTYSPDEYMWATLHRFAEMPGHMPAHQKYDTSDINAIARLVKWQSLEGDMNKGAPYIPCTGTHRRQVCVYGTGDLNWMVQQHHFFANKFDPKVDDNAIQCLEEYLRYKTFHPTENVA
The following text describes a protein:
Function:
Subunit e, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary 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. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Part of the complex F(0) domain.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MVPPVHVSPLIKTARWSALLVGIIYGKRRYDNLKPIAEEERRIEEEEKKVREEQERIAKQLAEANEDTILK
The following text describes a protein:
Function:
Docking protein that plays a role in tyrosine kinase-based signaling related to cell adhesion and cell spreading. Regulates PTK2/FAK1 activity, focal adhesion integrity, and cell spreading.
Subcellular Localization:
Cell junction, focal adhesion. Cytoplasm, cytoskeleton.
Sequence:
MKVNVSCDLSTLFFAGFLYVCIYFKKRENALAKALYDNKAECSDELAFRRGDILTVLEQHVVGSEGWWRCSLHGRQGLAPANRLQLLAGPQALPPPTIPSDAPEPPVAPQNIYQVPSVPKGTASSSTYEKMEGWVTSPARAATLPAQGVYQVPALAAQLLSERTRCSTQQHLFTLPRACRASVPNITSELYDVPSMQSRESLLTQSGATPPAARKGSVLLRSPRCFQEEQQFYNVPSSSEKAGAVIQDSAVGNLYDVPPKRETDASKKKSQKKYWGHCNTLPNPRKSEWIYDIPISPEKTGLKQNSSVHSTENQVLYDIPPARYKALTTNAEANVVNPQLYDIPPTQRKLTFPDVPLYDVPSSKDVLLQQNGSCDVPPSLPAPNAENQISGGNVYDIPKGLPTAMQPKKEMEKNSNHSGNQAYHIPAQLSRDTKPEHDRLPMCGHDNSADSKNSTISMSSNSSSESSSASSSEEPDKEIKLDLEVAIETLTRLQHSVSSSVASLMIFVSSKWRLQEHLEKNIEEIHRAIDHIKVSLGEFLAFARALKVNASYLTDNNLQIRIKKQLEILMNSFQILTETREALNNCNWSLEALVLKKPYSNPDDLDRFVMVARTIPDDLKRFVSIIIANGKLLFRKNEKEQEMKQPRVSPGYKMPKQITSPRRIEIDSLPVSAPDKPNPSQGSNETTKENVSEDCEYVQLQVLPSTKKNAVRSQQDSAKKVVIPEQCRLCFGALHKAIAVFNNSLSSKQPPEVFISHSKLIIMVGQKIVDSLCQDTQLREARSDVLHSSSRFCSLLKNLALATKNAAIQYPNADAMRELQNKNDELYKYTQQFRAMLE
The following text describes a protein:
Function:
Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse. Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ). Specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts: recruited to DSBs by NBN following phosphorylation by CDK1, and promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends. Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage. During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity). Binds preferentially to DNA Y-junctions and to DNA substrates with blocked ends and promotes intermolecular DNA bridging.
Miscellaneous:
MISCELLANEOUS: Binds one Zn(2+) atom per dimer. Zn(2+)-binding is not required for homotetramerization.
Subcellular Localization:
Nucleus. Chromosome. Note=Associates with sites of DNA damage in S/G2 phase. Recruited to DSBs by the MRE11-RAD50-NBN (MRN) complex following phosphorylation by CDK1, which promotes interaction with NBN. Ubiquitinated RBBP8 binds to chromatin following DNA damage.
Domain:
The PXDLS motif binds to a cleft in CtBP proteins; The damage-recruitment motif is required for DNA binding and translocation to sites of DNA damage.
Sequence:
MNISGSSCGSPNSADTSSDFKDLWTKLKECHDREVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSLGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEEESEHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNPCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT
The following text describes a protein:
Function:
Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function.
Subcellular Localization:
Cytoplasm, perinuclear region. Membrane; Lipid-anchor. Synapse, synaptosome.
Sequence:
MATQEELPSDLSLHGKFAQLMAQQAPVTITVAATQDGNWPFRLGGGAPFCPCIYITAVQQDPDADRGDMMLEAGDEVIMVNDQILIGKSLAEVHDILHTQPEATRLTVRKLPDETPSGVEFFLRRTTEAFNAKMEQFGATRKTYEALEGHVSLYLRRLEALAHVQQEYGQLLENASTTETNRALHSRMTGVAKSHKSYYFSVAEILPKAKFVREQLHTYLTIAIPDAKQTQDRYMQARNQYLALCIRVAEMAAEQARDREQDQVDNDVKTGNYYFRFTLREAGRLAARHAQLRQDLTEKLQMLEAKSGIWKTFEFSFFALSAPLSDAHSLNNSPNLAQHRIASSSSH
The following text describes a protein:
Function:
Heme detoxifying enzyme that converts heme to crystalline hemozoin (beta-hematin) to protect the organism from the toxic effects of heme. During its development, P.falciparum proteolyzes vast amounts of host hemoglobin, leading to heme release.
Miscellaneous:
MISCELLANEOUS: HDP is critical for survival, suggesting it could be a potential malaria drug target.
Subcellular Localization:
Vacuole. Host cytoplasm, host cytosol. Note=Delivered to the food vacuole, the site of hemozoin formation, via a unique trafficking route. Initially secreted into the cytosol of infected red blood cells. A subsequent endocytosis of host cytosol delivers HDP to the food vacuole.
Sequence:
MKNRFYYNLIIKRLYTRSGGLRKPQKVTNDPESINRKVYWCFEHKPVKRTIINLIYSHNELKIFSNLLNHPTVGSSLIHELSLDGPYTAFFPSNEAMQLINIESFNKLYNDENKLSEFVLNHVTKEYWLYRDLYGSSYQPWLMYNEKREAPEKLRNLLNNDLIVKIEGEFKHCNHSIYLNGSKIIRPNMKCHNGVVHIVDKPIIF
The following text describes a protein:
Function:
Binds the stem-loop structure of replication-dependent histone mRNAs. Is associated with translationally inactive histone mRNA stored in oocytes. Could be a specific translational repressor. Not involved in histone pre-mRNA processing.
Subcellular Localization:
Cytoplasm. Note=Binds the stem-loop structure of replication-dependent histone mRNAs. Is associated with translationally inactive histone mRNA stored in oocytes. Could be a specific translational repressor. Not involved in histone pre-mRNA processing.
Sequence:
MPQTLLPEPWMVINGNTAMEDLFGVPSRSRFLSAPGLLSKEECPLNLSGNELRSEFAESISCTEQTYGANTVSVGVDTELDLLEFGRSDFRMATSPDAVGYETDEATLHRRQKQIDYGKNTVGYQCYLQQVPKTERKSGVHPRTPNKSKKYSRRSWDMQIKLWRRDLHAWDPPSQNSFQEDHSFKQTQRLLESWLQESNSLQNPDMDWLGLQLSSLQNLGYSEDQIQNSFDWLQFRGHTNDYTYPHWIGL
The following text describes a protein:
Function:
Probable polyketide synthase.
Miscellaneous:
MISCELLANEOUS: Encoded by one of the numerous copies of polyketide synthase genes and clustered as a pair pks16/pks17 in chromosome 2.
Domain:
Modular protein that is responsible for the completion of one condensation-processing cycle. The beta-ketoacyl synthase region is responsible for the actual condensation reaction while the acyl/malonyl transferase region is responsible for incorporating carboxylic acids units onto an acyl carrier protein (ACP) domain (By similarity).
Sequence:
MTFNNIKDENNDDIAIIGMGFRFPGGGNNPYQFWNQLSNKMDGISKIPTEKWSRSFYEQKYINNEYGGVLKDEEWKNFDPLFFGISPKEAPIIDPQQRLLMTTLWEAFEDANIKPSTFRGSDTAVFIGMMNTDYQRCQFRDISYVNPYITPGTAGSFISNRLSFSFDLRGPSMTLDTACSSSLNAVYLGCQAIANGDSKMAIVGGVNGIFDPCFSMTFSGLNMLGHKGQCRSFDAGADGYIRSEGGGVCILKKYSDAIKDGDRIYCVIKGGSSNVDGYNAKTNIIQPSMKAQGENIEIALKKSGVNPSDIYYIEAHGTGTPVGDPIEIEAISRIFKDNHTPDAPLYIGSVKSNIGHLESAAGIASLIKVALSLKNRSLVPNIHFEKPNPLIKFEDWNIRVVTDEIQFPINKLINMGINCFGLSGSNCHMILSEAPINYDELLKTTNNNSTSSSSNDDKKEYLIPFSANCNISLDKYIEKLISNQSIYKDTILFKDFVKHQTISKSNLIKRKVITASDWDDFLNKRNETTSTSSLTSTISAPASSTPVIYVFTGQGPQWRDMGKALYETESVFKDAIDHCDKLLANYFGYSILQKLLSLESEDSPEIHHPILAQPSIFLIQVGLVALYKSFGISPSIVVGHSFGEIPSALFSDVISLETAVKIVYYRGLAQNLTMGTGRLLSIGIGADAYLEKCALLYPEIEIACYNDPNSIVITGSEQDLLGAKSTLSAEGVFCAFLGTPCSFHSSKQEMIKEKIFKDLSDLPESNVPCVPFFSTITGSQLSHKGFYNVQYIYDNLRMPVEFTKAISNIFNFIEENESYKNAIFLEIGPHPTLGFYIPKCKPSNSTITSKPIIVSPLHKKKEELTQFKLAISTLYCNGVEIDFASGQQLLPTSSSSGGGDISSFKESTNKLPRYQWDFEEYWDEPNQSKMVKRGPSNNLLGHDQFAGNTLMELFIDIDKSAHQYLKGHKIKGKYLFPGSGYIDNILRQFNGQDITIFNLEFSNPFFLKDGVQHHLQTSITPTTKGEFKVEFFIKDNRNSTKWTKTSNGRIGLFKHNPKNNKLDIEKLKSQCSFTTLTKSEVYNKLLLLSLPYGPTFQRVESCSIGDGCSFFKLSMSPCSEFDKDFLNPSIIDCAFHGLLVLSEGPQEIVFDRLQDMKFYSSNVPSTRPQFIYAFAKFDKIEGNSTHGSLNIILEDGTLLISIKNVKCTSLIRLKKQSIKYPSQNVYSHHWQSKDSPLTLIENQLIEEKSSESKINFEKLLNDKLFNYYLIRLLNQSIKSEFIEFDYKTSTVDTLDIGSKNAKLLEKIQSILNPIDSLDQSIDITSLKQAIIVKSSFKNEIKLVEKSIKRIVSLLKGGESEHFSPSNPSSPNDTPRNNSNNCSSKNNAASSDDADDDTNNEETINQLNNEPFNFSNSQFISNQNQLISKTIVNSFDRLINSIEIGEKKLIKIIDLSSIYQNYQLSKLLLLQLNQLLINLSNNNNIEIEYTIPSNTKNIDSITEETKSISNVLNIKYRSFDLQDDLESNGYLNSNYDLIITSLLLVSTNSIDSNEVLSKLYKLLLPKGQLILMEPPKGVLSFNLLFANDFKQSLEIKSEQEIKSLIIYCGFTKIETNLNTKDDEEQQQPPPPSILIVQAEKRDIESMSLTFSSDPKSLNSSYSNCIFIVSKEQKENPTSYIQEYFDITEFFCQNATIIEADDSELLTKTIESGVGKNDIIFFLVSLEELTIENYKQVTMQYTLVNQILLRNNLSTRFALLTYDSQNGGKNYLGSSLIGTFRYFLEFRSLNIFSIDVDKDSIDNLTLFLRLVDLSTIGDRETIVRNNKIFVQKIFKEPKLLSPSNNYEKNTNNLFLYSNSNLDFSFQSKEKLLHGCVEIKVMSTGINYKDSLFYRGLLPQEVFSKGDIYSPPFGLECAGYITRVAPSGVTRFKVGDQVVGFASHSLSSHVTTHQNKIVLKPENISFNEAAAVCVVYATSYYSIFHIGAFIADKESILVHSATGGVGLASLNLLKWKRNQLKKHGNSEISNDASIYATVGSKEKIDYLQEKYGDLITAIYNSRDTEYCDEIKQQSAQGGVDLILNTLSGDYLSSNFRSLSQVGRIMDLSVTQLVENDSLDFSNFKYHVGYNTIDLDRATKYNSKIIRDILTEVFDAISDGSLENIPVKVFPAIQVKTAIEYINERVHIGKIVVDFENFEQDILKPALQEKENPIQLNKVKKLEHTCDTLNNTILITGQTGIAVHILKWIISGSVLNSNKSQQQVTDFIILSRSSLKWELENLINQTKHKYGDRFRFHYKSVNIADLNSTRTAIDQVYSSCKNVSPIKSVLHFATVYEYILPENITQTVIDNTHNPKAVGAINLHNLSIEKDWKLENFILFSSIGAIIGGSKQCAYSSANLVLDSLSNYRKSIGLASTSINWGGLDAGGVAATDKSVASFLEGQGILLVSLSKILGCLDSVFQPSNSHLSNFMLSSFNIDNLLSSAPQMKRKMDHHLTNYKTSSASSDDSLGDSGSTQAKVISTISELLSIHPSKLNLDTRLKDYGIDSLLTVQLKNWIDKEFTKNLFTHLQLSSSSINSIIQRISSKSTSTSTPNPTNTSKQTATKKT