lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Putative transcription factor. Isoform 3 may play a role in early spermatogenesis.
Miscellaneous:
MISCELLANEOUS: Antibodies against TCFL5 are present in sera from patients with Chagas disease (also called American Trypanosomiasis), a disease caused by Trypanosoma cruzi. Two different epitopes that mimic Trypanosoma cruzi antigens have been identified: R1 and R3 epitopes, which are recognized by T- and B-cells, respectively.
Subcellular Localization:
Nucleus.
Sequence:
MSGPGPREPPPEAGAAGGEAAVEGAGGGDAALGEPGLSFTTTDLSLVEMTEVEYTQLQHILCSHMEAAADGELETRLNSALLAAAGPGAGAGGFAAGGQGGAAPVYPVLCPSALAADAPCLGHIDFQELRMMLLSEAGAAEKTSGGGDGARARADGAAKEGAGAAAAAAGPDGAPEARAKPAVRVRLEDRFNSIPAEPPPAPRGPEPPEPGGALNNLVTLIRHPSELMNVPLQQQNKCTALVKNKTAATTTALQFTYPLFTTNACSTSGNSNLSQTQSSSNSCSVLEAAKHQDIGLPRAFSFCYQQEIESTKQTLGSRNKVLPEQVWIKVGEAALCKQALKRNRSRMRQLDTNVERRALGEIQNVGEGATATQGAWQSSESSQANLGEQAQSGPQGGRSQRRERHNRMERDRRRRIRICCDELNLLVPFCNAETDKATTLQWTTAFLKYIQERHGDSLKKEFESVFCGKTGRRLKLTRPDSLVTCPAQGSLQSSPSMEIK
The following text describes a protein:
Function:
Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta. Outcompeted by LRRC32/GARP for binding to LAP regulatory chain of TGF-beta; May play an integral structural role in elastic-fiber architectural organization and/or assembly.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MGHAGFAVFVVVAVALLSLGGAHKETTGEREEGAQTGQQSPGISQGHPFSSTGHSPGSESPLLSPRAASPQDGHRSKTPREALDSAPRDDTQRAVRHPQSQQQRTRVNRRQSSKISSANRRLVGPNVCGGQQCCSGWAVAPGTNRCIKPDCQPPCQNRGSCSRPHTCVCRSGFQGPRCEDVVPEQVYIRERGTLRRIEPGNNPFQRDRPQRRPSERDGTDATKAQTPRPSASKLSVHSGSQTRRDPLDSSPQHSGTSRTVKRYPSSSGPITSNALPSTNGNAHSVDPSWYNHRNGHSNTPSGPSSGSHRQTNNRQLQGQFNNVLVPAGANLTSNLDRIKIVFTPMMCNRVCNAGRCYNNCEKGDITTVYSEASQQQQQQQPSKSQGFRLFFCQIPCLNGGRCIGRDLCWCPSNSTGKFCHLAAPPPARPTPHSRTLTARHGAKSPSQSMYTLPLSNQQVSLHPSLVNVHIQHPPEAEVQVHQVARVQPGQRLANTEGVHSVQQRSQPGNGHEHPSEHGSRQFPSRGHENGHARTHSRQNEIVGRCFQETVDGQCGKPLPGLTKQDDCCGSIGASWGLNKCQKCPTKPAYAVIANGQVQCPKGFKRMNATHCQDINECLLPGICKNADCVNTKGSYRCTCKPGYMLDAARSHCVSDKAVSEERASCYRSVSSGFCSLPLANHLTKQICCCSRVGKAWGHGCDRCPLPGSDHFKEICPAGHGYTYSRSDVQISVRQLEDDELQSTGVSLEEQYPQFPSSQPSLLFPSEPQHPSYPQTPQVPQYPDYHNMPQIPHHPLSPQHPSYSENEEAERTEGEEFLLPSAVVTDSPLKHPGINKCSSIPSICGRGKCISVQTGYTCLCDPGFKLSALQTNCIDVNECDEDPCEGKGHCINSYGSYTCQCHSGYSQVITQNRKFCQDINECSMPNKCQNGNCVNTEGSYTCECNSGFAKSWRDQCEDLDECKDPSSCPSGICINTLGSFQCQACSPGLRLINERCVDVNECLNQTVCGRGRCVNTQGSYRCNCFHGYKLSPDNVCQDVEECVLPEVCNHGLCVNLDGTHECTCNHGYQVTPDRKSCEDVNECATGNACPVGICINTAGSYTCQNCRPGFGPSADGLRCEDIDECARGDMCLGGVCANTEGSFICTRCTAGYRVSLDQQSCEDIDECQSISTCANGICLNSEGSYSCEHCPAGYRVSHDGEFCKDIDECALPTTCPKGTCTNTEGSYMCVVCQPGFRVSEDGQQCNDVNECLGSSVCPGQMCLNTQGSYTCRSCQTGFQPSEDGHTCQDINECQTPDVCPTGVCTNTEGSFSCMTCAPGFTVAPNGLSCEDVDECNNDNVCVRGQCINTYGSFLCLCEAGFKFSVDTADCDDQDECKEFGSSVCGAWRCQNTIGSYSCQSGILEEDWDKCDSEINCGEHGFCENTNSSFHCNCDKGYTNPAGDVTQCVDVNECETSSALCGEALCENYDGSFLCICPNDNEEFDPITNRCRSMAMIDPEHIYPVIPFTDERKECYYNLNDANYCNNVLSRNTTKQECCCTAGAGWGDNCEIHTCPLPGKDDYNQLCPHGSGILPLSDSLRQSHGDGLPYIDADECEMFGSEICKNGQCSNIFSTYTCFCRSGYYYDNIRFECVDFDECQFGNTCENGACVNTAGSFNCFCSPPLVLDDSQRHCISLNSTEETIEYGQDVHEDICWQRLEGDNMCADPHSERRTTFTECCCLHGVAWSGQCAFCPSKDSADYATMCNLPWEGGSDSLRDQIGVEYGPEGPPYWGNYGGPAGTYENSESVPLFNDHDYNVQQPPVRVPVVRPGSHPHPVNPYSVQHNAFEGLQAEECGILNGCENGRCVRVQEGYTCDCFDGYELDLSKMACVGKLVGHVRLSLLFPVE
The following text describes a protein:
Function:
DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation (Probable). Ensures the correct splicing of genes involved in immunity to promote longevity in response to infection by pathogenic bacteria such as S.aureus.
Subcellular Localization:
Nucleus.
Domain:
The third RNA recognition motif, called PUMP domain, is atypical and may rather mediate homodimerization and/or protein-protein interactions.
Sequence:
MEENSADIENRPVAAFRPAVSVPMPVLPQDGEVFVGPGGKKDAQKIGLGLSKLSSKRKDDIQMAKKYAMDISIKQILLRQQKQQQENQQRQQMYSQALSIMSRIYVGSISFEIREDMLRRAFDPFGPIKSINMSWDPATGHHKTFAFVEYEVPEAALLAQESMNGQMLGGRNLKVNSMMFQEMRLPQNMPQAQPIIDMVQKDAKKYFRVYVSSVHPDLSETDLKSVFEAFGEIVKCQLARAPTGRGHRGFGYLEFNNLTSQSEAIAGMNMFDLGGQYLRVGKCVTPPDALTYLQPASVSAIPASVSVACAAITAKVMAAEAAAGSSPKTPSESGGSRAASPAPRAQSPATPSSSLPTDIENKAVISSPKKEPEEIEVPPLPPSAPDVVKDEPMEIEEEEEYTIPEEKPKPVAIVPPPGLAIPSLVAPPGLIAPTEIGIVVPNPSFLAQQQQKIEEKIEEEEEARTERVKLSTSQRKKMKREKLNQMTFEEKMAQVLGQQKAVQNQRMADPVTFGALDDTVAWKDPSNEDQTSEDGKMLAIMGPGRGGDNVASMALALMDGGSSLMLANNAKAKEAAAALALEPKKKKKVKEGKKIQPKLNTAQALAAAAKAGEMSDALKNEVMNSEDASLASQEGLEIRGNDARHLLMTKLMRTNRSNVIVLRNMVTPQDIDEFLEGEIREECGKYGNVIDVVIANFASSGLVKIFVKYSDSMQVDRAKAALDGRFFGGNTVKAEAYDQILFDHADYTG
The following text describes a protein:
Function:
Sodium-phosphate symporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MLSWVISPLVAGAFSGIIYAITRAYVLRADPDQAIRRQRLFVALLISIILAVTIVFVCIRSPWPSEDFRLAGTILFSTMLPLAVGVVAYYWLLPRVFHNYAPSYIDVKTPLVHAEQHHPRRRERSSDTRLVIRSTSSSERFASTNSMAESAADASEMAPVENEETADLHAYADQYSGLIEANFELLQVLSASYLAFSHGAQDVSNAIGPVTAILDVYRGGSVEVDITPPIWLMALGGAGICTGLFFFGHYVMSTLGGNLTKITPSRGFSVELGTGLAVLLASFLKLPISSTHCAVGAVVAVGLLNRQGTKAVSWSLLWKVVGSWIVTLPTAGLLSAGFYAALRPVVAAVELGPAEMLLRCFGNCSALLDTYA
The following text describes a protein:
Function:
FAD-dependent monooxygenase required for two non-consecutive steps during ubiquinone biosynthesis. Required for the C5-ring hydroxylation during ubiquinone biosynthesis by catalyzing the hydroxylation of 4-hydroxy-3-(all-trans-polyprenyl)benzoic acid to 3,4-dihydroxy-5-(all-trans-polyprenyl)benzoic acid. Also acts downstream of coq4, for the C1-hydroxylation during ubiquinone biosynthesis by catalyzing the hydroxylation of 2-methoxy-6-(all-trans-polyprenyl)phenol to 2-methoxy-6-(all-trans-polyprenyl)benzene-1,4-diol. The electrons required for the hydroxylation reaction are funneled indirectly to coq6 from NADPH via a ferredoxin/ferredoxin reductase system.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MKLPGGTIICAKNASSYYDAVIVGGGMVGNAMACSLGANKSFQSKRVLLLDAGRSPSLSSFESGAPFNNRVVATSPTSIDIFKKLGVWERINSHRAKKVNRLFVFDSCSTSEIEFERGQNEEVAYIIENDLIVGSLYEKLADYKNVDVKTGAKVEVCFIPNGLENMATIKLENGDVIETSLLIGADGVNSKVRHASNVDYTTFNYNQHGLVGIVNIETANGKNETAWQRFTTLGPVALLPLSDTISGLTWSTSPEEAQRLKQLPADQFVDELNSALFSQDDQLPYVNQAIFALNKMNPFRTETFGRKAEGTTPPHIISVQDKSRASFPLGFGNAHSYITTRCALIGDAAHRMHPLAGQGVNLGWSDVQILDKILGDAVREGADIGSITYLREYDSAAQKHNLPVMVSVDLLNRIYRTDAPAIVAARAFGLNAFNSLGPVKNFLMNYLSAHR
The following text describes a protein:
Function:
Quinone oxidoreductase that may play some additional role beyond quinone reduction. Potential redox sensor protein. Overexpression induces retardation of growth.
Sequence:
MIAITGATGQLGHYVIESLMKTVPASQIVAIVRNPAKAQALAAQGITVRQADYGDEAALTSALQGVEKLLLISSSEVGQRAPQHRNVINAAKAAGVKFIAYTSLLHADTSPLGLADEHIETEKMLADSGIVYTLLRNGWYSENYLASAPAALEHGVFIGAAGDGKIASATRADYAAAAARVISEAGHEGKVYELAGDSAWTLTQLAAELTKQSGKQVTYQNLSEADFAAALKSVGLPDGLADMLADSDVGASKGGLFDDSKTLSKLIGHPTTTLAESVSHLFNVNN
The following text describes a protein:
Function:
Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Cell projection, cilium. Golgi apparatus. Membrane; Single-pass type I membrane protein.
Sequence:
MGPSPWTCLILGYLLSGLRRGACQPPFPTIVPDEEELVVSLHMSFSLRCTGDSEVSWQFPTLDDGSPGVSVRSEENNSGSFVAVLEVANASAVHTGLYTCYYNHTQTQEAEAEGRDVYVYVPDPDVAFVPSVMVDHFIVVEEDDSTVIPCRSTDPQARVTLHASDGKEVSAFYDSRQGFLGHFDMGSYTCETTIRGRKFQTLEFNVYTLRATPEIVVEMEAPKTVYKTGETIVVTCAVLDNEVVDFQWNYPGKVRDKGIIKLDEIKVPSIKLVYTLTVPEATAKDGGDYECAARHATKEAKQIKKVTITVHERGFVRLQPGFGPVEAVNLHEVRHFGVELEAYPPPRVSWLKNDVSLTENLTEITTSLEKIQEIRYQSKLKLIRAKEEDSGHYTIVVQNEDDIMNYTFELLVQVPASILDLVDDHHGSAGGQTVRCVAEGTPLPDVDWMVCRDIKKCNNETSWTLLTANASDIAVEAHVGDRDTMESQVTFQQVEETLAVRCLAKNHLGAVTRELKLVAPALRSELTVAAAVLVLLVIVIVSLIVLVIIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDNFLTRHPEKTKKELDIFGMSPADESTRSYVILSFENNGDYMDMKQADATQYVSMLERKESSKYSDIQRSLYNRPASYKKKSVSDSEVTDLLSDDGSEGLGLLDLLSFTYQVSRGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNSEPEKRPSFYHLSEIVESLLPGHYKKSYEKIHRDFLKSDHPAVARMRVESDEPYVGVTYKNEEKLKEWESGLDEQRLSADSGYIIPLPDLEPGLEDELGKRNRHSSQTSEESAIETGSSSSTFVKREDETIEDIDLMDDDIGIDSSDLVEDSFL
The following text describes a protein:
Function:
Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is required for transcription of ribosomal protein genes and genes involved in the integrity of the cell wall. Together with HTL1, LDB7, NPL6, RSC3 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity.
Subcellular Localization:
Nucleus. Note=Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.
Sequence:
MMDMQVRKVRKPPACTQCRKRKIGCDRAKPICGNCVKYNKPDCFYPDGPGKMVAVPSASGMSTHGNGQGSNHFSQGNGVNQKNVMIQTQYPIMQTSIEAFNFSFNPSVDTAMQWTKAASYQNNNTNNNTAPRQNSSTVSSNVHGNTIVRSDSPDVPSMDQIREYNTRLQLVNAQSFDYTDNPYSFNVGINQDSAVFDLMTSPFTQEEVLIKEIDFLKNKLLDLQSLQLKSLKEKSNLNADNTTANKINKTGENSKKGKVDGKRAGFDHQTSRTSQSSQKYFTALTITDVQSLVQVKPLKDTPNYLFTKNFIIFRDHYLFKFYNILHDICHINQFKVSPPNNKNHQQYMEVCKVNFPPKAIIIETLNSESLNNLNIEEFLPIFDKTLLLEFVHNSFPNGDTCPSFSTVDLPLSQLTKLGELTVLLLLLNDSMTLFNKQAINNHVSALMNNLRLIRSQITLINLEYYDQETIKFIAITKFYESLYMHDDHKSSLDEDLSCLLSFQIKDFKLFHFLKKMYYSRHSLLGQSSFMVPAAENLSPIPASIDTNDIPLIANDLKLLETQAKLINILQGVPFYLPVNLTKIESLLETLTMGVSNTVDLYFHDNEVRKEWKDTLNFINTIVYTNFFLFVQNESSLSMAVQHSSNNNKTSNSERCAKDLMKIISNMHIFYSITFNFIFPIKSIKSFSSGNNRFHSNGKEFLFANHFIEILQNFIAITFAIFQRCEVILYDEFYKNLSNEEINVQLLLIHDKILEILKKIEIIVSFLRDEMNSNGSFKSIKGFNKVLNLIKYMLRFSKKKQNFARNSDNNNVTDYSQSAKNKNVLLKFPVSELNRIYLKFKEISDFLMEREVVQRSIIIDKDLESDNLGITTANFNDFYDAFYN
The following text describes a protein:
Function:
Polytopic transmembrane protein that inhibits regulated intramembrane proteolysis (RIP) of CREB3L1, inhibiting its activation and the induction of collagen synthesis. In response to ceramide, which alters TM4SF20 membrane topology, stimulates RIP activation of CREB3L1. Ceramide reverses the direction through which transmembrane helices are translocated into the endoplasmic reticulum membrane during translation of TM4SF20, this mechanism is called 'regulated alternative translocation' (RAT) and regulates the function of the transmembrane protein.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Ceramide alters the direction through which transmembrane helices are translocated into the endoplasmic reticulum membrane during translation of TM4SF20.
Domain:
The first transmembrane helix plays a critical role for the insertion orientation in the endoplasmic reticulum membrane.
Sequence:
MTCCEGWTSCNGFSLLVLLLLGVVLNAIPLIVSLVEEDQFSQNPISCFEWWFPGIIGAGLMAIPATTMSLTARKRACCNNRTGMFLSSLFSVITVIGALYCMLISIQALLKGPLMCNSPSNSNANCEFSLKNISDIHPESFNLQWFFNDSCAPPTGFNKPTSNDTMASGWRASSFHFDSEENKHRLIHFSVFLGLLLVGILEVLFGLSQIVIGFLGCLCGVSKRRSQIV
The following text describes a protein:
Function:
Serine protease (By similarity). Plays a role in innate immunity against infections by parasite P.berghei and by Gram-negative bacteria such as E.coli. In response to P.berghei infection, contributes to the clearing of parasite ookinetes independent of melanization, an innate immune response which consists in the deposition of melanin pigments on invading pathogens and parasites.
Subcellular Localization:
Secreted. Note=Secreted in the hemolymph.
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:
MRWLVCLIVSWCSLVPLGATVGQSLNSGDPCQTPSGTAGTCEPVKNCSYVRKILKSPDFSHYDTTYLDTLKCGDLMVPMRKKPIPLLCCPKFSNSPTCGAQQLADRIYFGEETERGAHPWAALLFYNVGRNRTVPKCGGALISERYVITAAHCTVDKPNWKLLYVRFNEFNTSSADNCTTENDEVICREDYAVESIVPHPEYDMHNISRPNDICILRLASDVTFNDYVRPICLPFDPDVQQLPIVDEIFTVTGWGETEDRRPSDTQKHVELPGLEHEACNSVYAVANVTLSDKQLCIGGLNGSDSCRGDSGGPLMREVRGGWFLIGVVSFGARFCGTQNLPGVYTNVAKYLDWMETVMFVERYL
The following text describes a protein:
Function:
In the absence of glucose, represses the transcription of the gapA operon, which encodes five key glycolytic enzymes. Binds specifically to the cggR-gapA promoter region and blocks the progression of the RNA polymerase, leading to the arrest of the transcription.
Domain:
Contains an N-terminal DNA-binding domain and a large C-terminal effector-binding domain. Contains two distinct sugar-binding sites with different affinities.
Sequence:
MNQLIQAQKKLLPDLLLVMQKRFEILQYIRLTEPIGRRSLSASLGISERVLRGEVQFLKEQNLVDIKTNGMTLTEEGYELLSVLEDTMKDVLGLTLLEKTLKERLNLKDAIIVSGDSDQSPWVKKEMGRAAVACMKKRFSGKNIVAVTGGTTIEAVAEMMTPDSKNRELLFVPARGGLGEDVKNQANTICAHMAEKASGTYRLLFVPGQLSQGAYSSIIEEPSVKEVLNTIKSASMLVHGIGEAKTMAQRRNTPLEDLKKIDDNDAVTEAFGYYFNADGEVVHKVHSVGMQLDDIDAIPDIIAVAGGSSKAEAIEAYFKKPRNTVLVTDEGAAKKLLRDE
The following text describes a protein:
Function:
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Sequence:
MEPLKSIIAKVATGAILTREEAASAFDSMMSGDATPSQIGGLLIGMRVRGETVEEVTGAASAMRNLMPKVEMQCDPIDITGASDGAMRPLNVSTCASFIVAGAGVPVAKYVNRAATLRSSTADVLASLGVKVDLKPDAIARCVHEAGIGFMFASAGYPAMQRISQIRSVLGTHTMFNLIEALSNPAGVKRQILGVFARKWVQPLAYVLKNLGADSVWVVHGSDGLDEISLAGTSFVAAVEAGTVRTFEVTPEEAGLSRYRADALESCDCESHAIALEKVLDGLPGPFRDAALLNAAAALVVAGRASNLQQGVALGQESLDHGAAAARLTRLIAVSNA
The following text describes a protein:
Function:
A probable ATP-dependent DNA helicase implicated in DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates (By similarity). In male germline stem cells (GSCs), plays a role in GSCs maintenance during larval germline development by modulating the expression of genes such as Stat92E and preventing DNA damage-induced checkpoint activation. May play a role in female germline stem cell maintenance.
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MPESLIAGIPVHFPFEPYPVQRAYMEKVIHCLRDGTNGVLESPTGTGKTLSLLCSSLAWIRTRQSEHQKQMVKMEKADFSGLGGGAPGGDLSELAKTMGRANNWGVPKVIYASRTHSQLTQAMRELKRTAYANMRSVVLGSRDQLCIHPEVMREQGNSNKTNMCKLRVHSKTCSFQMRVESRKDHPDLRGPTIMDIEDLVKVGQRLKICPYFASRELVPQADITFMPYNYLLDPKARKANKIELGNTIVILDEAHNIEKICEESASVQIKSSDVAMAIEDVTHIMQVFASGESQDMAGDEPKDFTLDDLTLLKEMLLELEKAIDAIVVDNAVDGTTFPASMMYELLGKANFTYGNVATIVSLLDKLVQYLLVASQQMSIRKGGTFTLLSDLLTIVFANKEDVMSKVYASFKVHVLVEESKQGHGKQQGAKQQGGWLGKGTIAAATGLSKVAKIINFWCFNPGFGMEQLLNTQVRSVILTSGTLAPLKPLIAELAIPVAQHLENPHIVDQSQVYVKIIGTGPDRQQLISNYANRDNPKYISSLGQTILNVARIVPDGLLVFFPSYPMLNKCVDAWQASGLWADISCKKPIFLEPRSKDQFTSTMEEFYQAIRDSKGAVFMAVCRGKVSEGLDFADRNGRAVIITGLPFPPLKDPKVILKRRYLEANRTRENQLLSGQEWYNLDATRAVNQAIGRVIRHRNDYGAILLCDSRFKDASQVQQLSKWIRGHLGDRPQCSPFGPIVRELRQFFKNAEANMKLPDERETDSPLETVCKTEDEPLAAIPKVKREPGSNATFKSANESAIKVEMANSIKTWTPADYASAAGHKLGGAAPNAMDFMSRLDSNVSSIDFNCCTDSKSGSSGLVKIHKRERSSPTAPESSSQVTKKRYKLVENIKVEPSSSQAKEAPEERAAFLRELRSLVTQDQFRRFGKALLEYKNGTYESFQALMAILLDVLSAPKVRYMLVGMRKYLKNEHKDEFDRRVGNL
The following text describes a protein:
Function:
Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia.
Subcellular Localization:
Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Sequence:
MAHLVVQIIGFLCGCIGMILAWVITFMPQWRVSVILENDGSQNFRLDGQWISRFDGLWSTCVNQVQNAQQCKSYDSVISVSTDIKAGRVLMSFAVILSFLACLFSFIGLVLTRFQNKYGKHCLILTSGILYIISIVLMVIPVIWVTANIVCQACEPYCKGGFRIELGEALFLAWPAIGFLLVGGIMLCWACPSRHQQETCIYSTPQDHGVACRVRPTDRELSDCYNKIEYI
The following text describes a protein:
Function:
Involved in pre-mRNA splicing. Important for bud site selection.
Miscellaneous:
MISCELLANEOUS: Present with 1900 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MPRIKTRRSKPAPDGFEKIKPTLTDFEIQLRDAQKDKSSKLAAKSNEQLWEIMQLHHQRSRYIYTLYYKRKAISKDLYDWLIKEKYADKLLIAKWRKTGYEKLCCLRCIQKNETNNGSTCICRVPRAQLEEEARKKGTQVSFHQCVHCGCRGCASTD
The following text describes a protein:
Function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Miscellaneous:
MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MANKVIQLQKIFQSSTKPLWWRHPRSALYLYPFYAIFAVAVVTPLLYIPNAIRGIKAKKA
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MAVVLGYRGDGLLRVGLRKFMQLRESRNLRDLRGIIEEKERSKEEEHHVKIEEKTHLQTDGILKRRDKNSFTCTQCGKILASKSKLKVHMRIHTGEKPFTCTQCGKSFSISSSLNLHMRIHTGEKPFTCTQCGKSFSHLSPFNKHMRIHTGEKPFTCTQCGKSFSLSTSLNLHMRIHAGEKPFTCTRCGKSFNCSSNLSKHMMIHTGEKPFTCTQCEKSFRISSSLNLHMRIHTGEKPFTCTQCGNSFSQSSSLNKHMRIHTGEKPFTCTQCGKSFNRSEHLNLHMRIHTGEKPFTCTECEKSFTCSSHLNRHMRKHTGEKPYACTQCGKIFSQSSCLNLHMVSHNGEKP
The following text describes a protein:
Function:
Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis. Can reduce small soluble hydroperoxide such as H2O2. Can reduce cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides. Cannot reduce phosphatidycholine hydroperoxide (By similarity).
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MAYIAKSFYDLSAIGLDGEKIDFNTFRGRAVLIENVASLUGTTTRDYTQLNELQCRFPRRLVVLGFPCNQFGHQENCQNEEILNSLKYVRHGGGFQPTFSLTQKCDVNGQNQHPVFAYLKDKLPYPYDDPFSLMTDPKLIIWSPVRRSDVSWNFEKFLIGPEGEPFRRYSRTFQTINIEPDIKRLLKVAI
The following text describes a protein:
Function:
Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1.
Sequence:
MYNNHTPISPSSSSSACHPSSSNTHATSLPSANSTNPNQQQQTQMYHQQQQPQQYQQQQPQHYSPSFDHTNPIGITPQLTQSAPEVTTLPTILITYKHPGSSNSRSVKARIDRNVPLDEVIRQLCRSTQLALDDPAEMFCLRDASNNELITPDNVFSKIENGMSSLKLVKSPTIEARDIAEKLASVNITESNQAQHNQDHLKAIKLPLFSLKDYLREPEFSSEFQERGGSRELLRLCKTSTGNTLAYALSALKETMGAHPSRPFGKSGDQYAPINVLRPTTAILKVIAHDSSASPRLAFGAICGVIEAAGEKEDLFGLLARRIGSGSTSDFSLSQVSFALVNALMRAALWEDARQDYVGWFMERMERAGIRRAVLRLGEGRADEAFDEVESDILTFQRNLVLMNRRLIRTTVNSEVPEHVEQLMEMASRARDLDARHNDTREEGDEERTGEDELEARKWKTLGFDSANLLDDFEKVGVLGLKLMYRFMNTRSVEFDKFIAEQLLKPDGRRCPLAKASNKCTEILIDLYEWNVADAQADQLITVFKPFMLNYPKLHHLALDFFKLMWNESGATTHDFERVGVLVRSHLRNALRNHEDSKGSVKTSWMNLVREFENGEYMKVRDRQMQELAMEDSMWNKTPVRNLRGKLYQNAFEFVKTQRINTLLAGCWFPHYPERILPANSNHGNSGSKLGFSVPSLRAHSQFNNSKNSNGLLDPNHNIVPRWRFYRLAPNKKHLHYFETPQPVPVSSGVEELPDRIDVSLITSVLSGSGTNNNLKQQQQHQQQQQQQQVRDGSQENSHFDRRPSLTRRMSSASSASTSDSFVMLANDSHSKKSGQQQGYQSHQANISLMNGDHLLLRLFPSNSHIYSEWFDGLNLIKSLTNQTPYQPIEDHNHNAHELPSNLAAAQNHNNSLIKNAHANPNLQHQHFSSAVEGTMTTQETAELVYSLTQIGTMIKLLDLTGERVDVPNQLNVPPVPLSSNFFYASEGQIF
The following text describes a protein:
Function:
Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to GNAT1. Involved in phototransduction; key element in the recovery phase of visual transduction.
Subcellular Localization:
Membrane; Peripheral membrane protein. Note=Targeted to the membrane via its interaction with RGS9BP.
Sequence:
MTIRHQGQQYRPRMAFLRKIEALVKDMQDPDTGVRVQNQKVKVVSIPHAMTGSDVLQWISQRLWISGLEAQNLGNFIVKYGYIYPLQDPRNLTLKPDSSLYRFQTPYFWPTQQWPAEDVDYAIYLAKRNIKKKGILEEYEKENYNFLNKKINYKWDFVIMQAREQYRAGKERNKVDRCALDCQEKAYWLVHRCPPGANNVLDYGLDRVTNPNEDQKQTVVSVRKEIMYYRQALMRSTVKSSVSLGGIVKYSEQFSSNDAIMSGCLPSNPWITDDTQFWDLNAKLVDIPTKMRVERWAFNFSELIRDPKGRQSFQHFLRKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMDITVKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKEMLAKAIEPQGTTRKSSSLPFMRRHLRSSPSPVILRQLEEEAKAREAATTVDITQVMSKLDRRSQLRKEPPPK
The following text describes a protein:
Function:
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MASLGGLQNVSGINFLIKEGPKVNAKFELKPPPYPLNGLEPVMSQQTLEFHWGKHHKTYVENLKKQVVGTELDGKSLEEIIVTSYNKGDILPAFNNAAQVWNHDFFWECMKPGGGGKPSGELLELIERDFGSFVKFLDEFKAAAATQFGSGWAWLAYRARKFDGENVANPPSPDEDNKLVVLKSPNAVNPLVWGGYYPLLTIDVWEHAYYLDFQNRRPDYISVFMDKLVSWDAVSSRLEQAKALITSA
The following text describes a protein:
Function:
Accessory subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and two primase subunits, the catalytic subunit PRIM1 and the regulatory subunit PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively.
Subcellular Localization:
Nucleus.
Sequence:
MSASPQQLAEELQIFGLDCEEALIEKLVELCVQYGQNEEGMVGELIAFCTSTHKVGLTSEILNSFEHEFLSKRLSKARHSACKDSGHAGARDIVSIQELIEVEEEEEILLNSYTTPSKGSQKRTISTPETPLTKRSVSTRSPHQLLSPSSFSPSATPSQKYNSRSNRGEVVTSFGSAQGVSWSGRGGAGNISLKVLGCPEVLTGSYKSMFQKLPDIREVLTCKIEELGSELKEHYKIEAFTPLLAPAQEPVTLLGQIGCDSNGKLNNKSVILEGDREHSSGAQIPVDLSELKEYSLFPGQVVIMEGINTTGRKLVATKLYEGVPLPFYQPTEEDGDFEQSMVLVACGPYTTSDSITYDPLLDLIAVINHDRPDVCILFGPFLDAKHEQVENCLLTSPFEDIFKQCLRTIIEGTRSSGSHLVFVPSLRDVHHEPVYPQPPFSYSDLSREDKKQVQFVSEPCSLSINGVIFGLTSTDLLFHLGAEEISSSSGTSDRFSRILKHILTQRSYYPLYPPQEDMAIDYETFYVYAQLPVTPDVLIIPSELRYFVKDVLGCVCVNPGRLTKGQVGGTFARLYLRRPAVDGVERQSPCVAAQVVRI