lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Thiol protease that possesses high activity toward the cathepsin synthetic substrate Arg-Arg-7-amino-4-methylcoumarin (RR-AMC) and the papain substrate Gly-Arg-Arg-AMC (GRR-AMC). Can cleave the papain substrate Phe-Arg-AMC (FR-AMC) and the caspase-3 substrate Asp-Glu-Val-Asp-rhodamine 110 (DEVD-R110). Has no activity towards the caspase-6 substrate VEID-AMC, caspase-8 substrate IETD-AMC and caspase-1 substrate YVAD-AMC. Plays a central role in plant programmed cell death (PCD). In addition to its role in protein degradation, may cleave and/or degrade a number of target proteins, activating signaling towards PCD. Contributes to the increase of caspase-3-like activity after UV-C-induced PCD and is required for abiotic stress-induced PCD. Functions redundantly with CATHB1 and CATHB2 in basal defense and distinct forms of plant programmed cell death (PCD). Participates in the establishment of basal resistance against the bacterial pathogen Pseudomonase syringae pv. tomato DC3000. Required for full levels of PCD during resistance (R) gene-mediated hypersensitive response (HR). Involved in the regulation of senescence, a developmental form of PCD in plants. May be involved in the degradation of seed storage proteins during seed germination.
Subcellular Localization:
Vacuole.
Sequence:
MAVYNTKLCLASVFLLLGLLLAFDLKGIEAESLTKQKLDSKILQDEIVKKVNENPNAGWKAAINDRFSNATVAEFKRLLGVKPTPKKHFLGVPIVSHDPSLKLPKAFDARTAWPQCTSIGNILDQGHCGSCWAFGAVESLSDRFCIQFGMNISLSVNDLLACCGFRCGDGCDGGYPIAAWQYFSYSGVVTEECDPYFDNTGCSHPGCEPAYPTPKCSRKCVSDNKLWSESKHYSVSTYTVKSNPQDIMAEVYKNGPVEVSFTVYEDFAHYKSGVYKHITGSNIGGHAVKLIGWGTSSEGEDYWLMANQWNRGWGDDGYFMIRRGTNECGIEDEPVAGLPSSKNVFRVDTGSNDLPVASV
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MTFLKTCSSSLISLLLISQTFLQIQVQSATNNDPLSKLIALTKAGKGVAPLNDKLYDEIISGPRNFSVTVVLTALGSQFQCQPCQIFDLEYQLLARQWAKQPTKIRNTHFFAMLDFKEGKNTFTKLGLNTAPQARTFLANEGPEAVTDVKKQVLSYDFNKGGPRGLTAELFSDWAINSANLPPFFKRPPNYGRIFAASCILLATIILIKVAWPLVKFVLTSRFIWAAALLPVILLMISGQMWCQIRSPPYMVKQPNGAPSYIAGGYSNQYGVETQVIASLYGVLAFAAYTLAFTVSKLDDPIRQRVAVYVWLGVFLTISSMLLNIFRMKNSGYPFKLFL
The following text describes a protein:
Function:
Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.
Sequence:
MRRPSLALLALSSLPFGSARQPASFSIHQDLLAHPQFEVIFSDSYVFEADAFALLEAANKTPKPTPASDGAHDGSTTRTDLTSAIRESATANADTDNGDESIGGTSPLRETYELIAHPPMRYLCSIPIIAPPPALNKTATELAKAEEAREVTRAYNKGWELMRGLENQCLHFVSGWWSYQYCYGKSIVQYHAVPNPKGGPPLRDKNSQEYILGTSLPPSSHSQKGKQIEVPNNEQKQLSPPPNTELQAKDNQRYLVQRLDGGTICDLTGRPRTIEIQYHCNPALSGDRIGWIKEVTTCAYLMVIHTPRLCADVAFLPPKETKAHPITCRQIITSDEEALSFNQRRKNTIDSAAAAAAAVTTEDQKQGSESGSPEKLSYQGLTVAGIPIGARRILPSTHVLPLPRHLQQQRQEAQQGNLLEALTKAAFKADVFGDYGDDNNNNNNNHHPKAGKGRKAAGAGKGQSGQKEMKKMRISERDIDKLGLDQQTLDALREEIRAAGLDPDRNLNDEREAGGEIVWEFYADVSGDEDDGAVAEEGKEVFVWYEDEDEGGEPAEAGKDQKESKKGGNGEGSGSGSEEGSKEEYYRDEL
The following text describes a protein:
Function:
Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Required for the accumulation of coenzyme A in the mitochondrial matrix (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MATTSVSSPKSKPSWVSFLSGGLAGVTAKSAVAPLERVKILYQIKSELYSLNSVYGSMLKIVENEGIKGLWRGNSATILRVFPYAAVQFLSYETIKNHLVADKSSSFQIFLAGSAAGGIAVCATYPLDLLRARLAIEIHKKPTKPHHLLKSTFTKDGVKGIYRGIQPTLIGILPYGGISFSTFEFLKRIAPLNEIDENGQISGTYKLIAGGIAGGVAQTVAYPFDVVRRRVQTHGFGDAKAVVNLEHGTLRTIAHILKEEGILALYKGLSINYVKVIPTASIAFYTYEYLSNFFNKL
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MSLLRCVLSSSRPLSMRLVGLKPIPRSDGVKMIVRWGSGGPRMLRYRMILGSQHEYFKKLVFQYFLIGAIPAAAIILYSNLFVGDAVLCDHDPELYEPEEYEYYKHPISRFLAKYVMENPKISYYKEIYIIERNQRIERQRRLINQVETLQALEGMGAFPLHKDPSLPRFMVDDLDDFAEAHNFKDNPDKKF
The following text describes a protein:
Function:
The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates YPT6 by exchanging bound GDP for free GTP. It is thereby required for efficient fusion of endosome-derived vesicles with the Golgi. The RIC1-RGP1 participates in the recycling of SNC1, presumably by mediating fusion of endosomal vesicles with the Golgi compartment. May also be indirectly involved in the transcription of both ribosomal protein genes and ribosomal RNA.
Miscellaneous:
MISCELLANEOUS: Present with 78 molecules/cell in log phase SD medium.
Subcellular Localization:
Golgi apparatus membrane; Peripheral membrane protein.
Sequence:
MFIKQSEKNTPKCLYKKKGKVRVLLTGSCKKLNTWKMHLWPVSPPQLLRIPPRNAELGEGTKIDDCNILQSMTLPQANVLIMLTPTRVLIYNFKPMALVASHERTMASLKEFGDNRSMKRSAPYNDIIEGLISKKDSQYLLWHQGKLIFYVMTDKNFLLTYQILKNCTNEIIFKEYGIPVIEPLLMSEEEANSAEYDYNNDDDTLTVFDKNSSSRIIQNGFGITKEKGFLHFLSNQENIDELPVKKLELRLKVVLKFDYEIIDMIGIKTFSKVGDGRYEEVLIVLFPHGLQILTISDFKVSKSSLVEVKKGSKTIVCNKQLMVLSHDSVEKQTIVSIIDIEKQAVEAIPLTDTPDELLTCLEVNGYLVVVYKEKIICFDTRIKKVSHSWKPPFVIKLCDKINDKILLLVSEDSVNIHFYTEFGNLLFATYFDEDDYNGDNNNDNSKDKNEKKAAEYKISDFVCLDKSLITVSHSGKYQVWKLWEEIKQTQFDFRNPKCYVLTNTNNDVIIYSPVTSSSINNDNLQVIKLPTKTFNNHIAFVKINSSLRLFATYVSNKNILLIHNLETNMWSSFADQNVLDLHWLGDNYLVCHMKNDDGSTNLKCLQIPLQEANPDVELSDYVMWEYNVPENTIVFSLHVNTLSRYKLLKMKSKNHNASEKQPDALLKTAEIILVTDTQTIVFDVISTVHPCGLNIIKKFYQYLKINIPIDVLPNKIEWIINMKEGLLFFADRKFIKLGKVDGGGWQTLTLLDNIEKIIDVIRDEIFVVQGHNYVVYSLEDLWDDKKPLVSIPIEEDLYPISTTPETATTHTLHCIFNARFSKLVVKHQIYLDQLILAKLEDNTDLEDISHNYRFLKPYKFALEKILSTKILRSDSLDDILKLIKMYDNTDPEHNISPPTHSGMLEIISNCLRKIETKYWNHLFTNLKMTPRDLLALCIEENEAKMLGVLLLVFLNYDEKDLGDDLHFKKSDLGTEESKALNDNSTKKSEKSVTNLLKDEELMLKVLELLVTSAANATDPIKATDSWDMCFQLIRLLKELDRENNTQLVQKALERFK
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MPRLCLNKLLSLSVTLTFIVLCSLNYGQANYKKSATQLTLGERVQQLTELSKKRPVIRLNAEKFKQYVRASPRNYSFIIMFTALSPHRQCSICSQANEEFQIVASSFQSLAYTNRLFFGLVDYDEGPEVFAQLKQNSAPVFLHFSEKGPLKKGDQMDIQRIGFGADSIARWIAERTEVQRHSLGSSGYTRARMQHSVLGVCGSGLAACNRLLLNDLGGDLHVNRLRHHSRDFVVFDDVVGTMAELADIRSFMLAAILFKKRRAKRHKRSGAA
The following text describes a protein:
Function:
Specifically hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP may protect cells against undesired salvage of m(7)GMP and its incorporation into nucleic acids. Also has weak activity for CMP. UMP and purine nucleotides are poor substrates.
Subcellular Localization:
Cytoplasm.
Sequence:
MLLINPLDVAPSGLKMPEFQKKSVHIKDPERVEEIICGLVKGGASKLQVITDFDMTLSKFSHNGKRCPTCHNIIDNCKLITDECRKKLFQLKEKYYAIEIDPDLSIKEKYPYMVEWYTKSHTLLIDQRLQKNKLAEAVRDSDVKLKEGYEMFFDLLHKHSIPVFIFSAGLGDILEEVIHQAGVYQPNVKVISNFMEFDENGIITGFKGELIHVYNKHDGALRNTEYFAHLKDNSNIILLGDSLGDLTMADGVPNVENILKIGFLNDKVEELIEKYMDSYDIVLVKDDTLDVANSVIQKIL
The following text describes a protein:
Function:
Plays an essential role in early steps of chloroplast development. May be involved in the redox control of plastid gene expression by maintening the redox state around chloroplast nucleoids. May positively regulate plastid-encoded RNA polymerase (PEP) activity, through binding to FSD2.
Subcellular Localization:
Plastid, chloroplast stroma, chloroplast nucleoid.
Sequence:
MLQSIHLRFSSTPSPSKRESLIIPSVICSFPFTSSSFRPKQTQKLKRLVQFCAPYEVGGGYTDEELFERYGTQQNQTNVKDKLDPAEYEALLKGGEQVTSVLEEMITLLEDMKMNEASENVAVELAAQGVIGKRVDEMESGFMMALDYMIQLADKDQDEKRKSLLEVVKETVLSHLTKKCPPHVQVIGLLCRTPKKESRHELLRRVAAGGGAFESENGTKLHIPGANLNDIANQADDLLETMETRPAIPDRKLLARLVLIREEARNMMGGGILDERNDRGFTTLPESEVNFLAKLVALKPGKTVQQMIQNVMQGKDEGADNLSKEDDSSTEGRKPSGLNGRGSVTGRKPLPVRPGMFLETVTKVLGSIYSGNASGITAQHLEWVHQKTLQVLEEIAY
The following text describes a protein:
Function:
Might function as an inhibitor of Lys-specific proteases. Might influence the maturation of megakaryocytes via its action as a serpin.
Subcellular Localization:
Cytoplasm.
Sequence:
MASLAAANAEFCFNLFREMHDNQGNGNVFFSSLSLFAALALVRLGAQDDSLSQIDKLLHVNTASGYGNSSNSQSGLQSQLKRVFSDINASHKDYDLSIVNGLFAEKVYGFHKDYIECAEKLYNAKVERVDFTNHLEDTRRNINKWVENETHGKIKNVIGEGGISSSAVMVLVNAVYFKGKWQSAFTKSETINCHFKSPKCSGKAVAMMHQERKFNLSVIEDPSMKILELRYNGGINMYVLLPENDLSEIENKLTFQNLMEWTNPRRMTSKYVEVFFPQFKIEKNYEMKQYLRALGLKDIFDESKADLSGIASGSRLYISRMMHKSYIEVTEEGTEATAATGSNIVEKQLPQSTLFRADHPFLFVIRKDDIILFSGKVSCP
The following text describes a protein:
Function:
Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).
Sequence:
MEIINKFLDLEALLSPTVYEKLKNFDEEKLKRLIQKIREFKKYNNAFILLDEKFLDIFLQKDLDEIINEYKDFDFIFYYTGEEEKEKPKEVKKEIKKETEEKIEKEKIEFVKKEEKEQFIKKSDEDVEEKLKQLISKEEKKEDFDAERAKRYEHITKIKESVNSRIKWIAKDIDAVIEIYEDSDVSGKSTCTGTIEDFVKYFRDRFERLKVFIERKAQRKGYPLKDIKKMKGQKDIFVVGIVSDVDSTRNGNLIVRIEDTEDEATLILPKEKIEAGKIPDDILLDEVIGAIGTVSKSGSSIYVDEIIRPALPPKEPKRIDEEIYMAFLSDIHVGSKEFLHKEFEKFIRFLNGDVDNELEEKVVSRLKYICIAGDLVDGVGVYPGQEEDLYEVDIIEQYREIAMYLDQIPEHISIIISPGNHDAVRPAEPQPKLPEKITKLFNRDNIYFVGNPCTLNIHGFDTLLYHGRSFDDLVGQIRAASYENPVTIMKELIKRRLLCPTYGGRCPIAPEHKDYLVIDRDIDILHTGHIHINGYGIYRGVVMVNSGTFQEQTDFQKRMGISPTPAIVPIINMAKVGEKGHYLEWDRGVLEVRY
The following text describes a protein:
Function:
Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with msh2 to form MutS beta, which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to 13 nucleotides long. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis (By similarity).
Sequence:
MPRLKLPKSFKDELESEKTTTTSSRKKAPVVDPKQTLMSSFFTPVSKSTDTKEINNKEDKDEDKDKDKDNKKTKKSKDTSDNEDMVDDNNKQQKEKKATPNKSNSPQSPQTSKSPLTRRSSANGNSDSKIDNKEKEKEKEKEKEKDKSTPTKTTSSRVKKDTEVSKSIPPKLSKQTKKKQISSDNDIYDDEKDSEEEDLEDDHDDEEEKVVVKKPSKPTSKSITAKPASTKATTTTTTTTTTTSTGRTRVNRVNLDISFSSESEEDEKPKKKIIGKKRKKKDDSDFDSESESDTISEASEVEPESEEDLDSFKFNSKKKNNNKNNNNKKKNDEYEDEEEDEDDELFKDIEMKDKPEEEEKEEEGDPIVIGSGRVVLPKGTPDFQPDPKAGKKLLKAHLEIQSKEEAKRLQQANGGGGDGGGGQIKGSDDEDEEVKKPTKGGSKASAKKKGPAYTPLEQQYIAIKKENPDTVLMVECGYKYKFFGEDAEVANKVLNIYSYVAKNFLNCSIPTQRLFFHLRRLVMAGYKVGIVEQTETAALKAISSSKSQPFERKLTRVYTSSTFIDDDIDDQLTSSSPQFLVSFYESTPKNKNDDVIKKQRDNEEEGIDSSNESSTSTISFVAVSVKTGEIIYDTFKDNVMRSQLETILTHIKPSEILIPPTTTTVNKQKVNNGIGTNHYYFSNLTSKCLKTYTKSTNVRTQAMDSQLYDYEYSLGKLIDFYEDESNNNNNNNNCEDVLKFVKSTLNKEQIICLGILLSYLNEFIHFGSILKVESNFKAFRVSNHLVLPHSTIVNLELLVNESDNKEKGSLIWLMNRTSTFSGSRMFINWICKPLNQLELIKERQDAVEELVNGIKTNSPPIVSIISLFKSHIPDLQRNLSRIYYKVQCTPKEFLNTMTSLQRIVELFKEINNNNSSYKFNSTLLNSIFKLQNDNKDGDSDSFDYIGGEDKLSKRIKYFLSNINKETAKEYGTVGCDKSNLWVDLEKYEKIRETKEKIEQVEKEFKNVLKNIRKELSKPSLEYHHMPGLGLEYLLELPPSFKAVPKSWIKVNSTQKMARYHAPEVLEQLKILSQSRETLKIQSQESWISFLGEFSVDYSLFSNFVNKISNLDCLFSLAKVSSLEGYIRPQFVKEKKDGGIQIENGRHPVVEAILSGSDGSYVPNTIELRESACKSMIITGPNMGGKSSLLRQTALIVIMAQVGCFVPATSCSLSVFDAIYTRMGARDSIGTGKSTFFIELEETSDILKNSTQNTLVILDELGRGTSTNDGVAIAYSTLKYIVEVMKCYCLFVTHYPLLAQLELQYPTQVGNFHMGYLEEKQDQQLQKSVIPKVIFLYKLVKGAAQNSYGLNIARLAGLPMEVIADALKKSNEMKESITRRANLSDGKDQQQIENEIKSIIKNWNSNRTTLNSNDLLQFIEKFKSIQLKL
The following text describes a protein:
Function:
Involved in spliceosome assembly.
Subcellular Localization:
Nucleus speckle. Nucleus, Cajal body.
Sequence:
MADPKELQTNLTQYRAQLSQVDAALTTDPDNEELLKLKQDLEEVINLTLDLLKVNVKVPEAELPNAKWKVGHRCQAVWTQDGNYYPATIDLISDDLSTCTVTFDYGNTEIVKLDSLKDISAASAGDKRPSDNQESSSSKKISRKEKDQLREQKRKKMAKKQLRMKELEEQREGEKNRWLDFFNNSKNLKGVTKKSIFASPETLNGRVGVGTCGIGDKPMTSFKQDKVVYKK
The following text describes a protein:
Function:
Clavin has the same substrate specificity as alpha-sarcin. It is specific for purines in both single- and double-stranded RNA. Its toxic action on eukaryotic cells is the result of cleavage of a single phosphodiester bond in the 60S subunit of ribosomes.
Subcellular Localization:
Secreted.
Sequence:
MVAIKNLVLVALTAVTALAMPSPLEERAATWTCMNEQKNPKTNKYENKRLLYNQNNAESNAHHAPLSDGKTGSSYPHWFTNGYDGDGKILKGRTPIKWGNSDCDRPPKHSKNGDGKNDHYLLEFPTFPDGHQYNFDSKKPKEDPGPARVIYTYPNKVFCGIVAHTRENQGDLKLCSH
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MVSRNLFDFLRFRQFYQFQTISASSLYGTNRAQYCQSKQGYVKAWDASPLPSKWIRSYCTSAKFLHCRHVRLFSAVSGKGSGNEQQQNAPTPQLLSKLFPQTAVEGTENEQQQEKHRKEEEAEKESSWKRMKFGFVFFGFSVSAFCVYTVWVFGAPDRDAEGNIIVDEFMELPTFQQYFRRMWKSMTYYQKMIQEPSREKLLPDPLKYPYVQPPYTLVLEMKDVLVHPDWTYQTGWRFKKRPGVDKFLETLAANYEIVVFTADQGMTVFPILDALDPRGYIMYRLVRDATHFVDGHHVKNLDNLNRDLSKVIVVDWDPNSTKLHPENTLNIPRWTGNDDDAGLFDLMAMLVTIATSEVEDVRDVMTYYKSFENPLVKFRENQRLLAEQMAEREHEEKQRNLPAVQRWRPSFLGGGR
The following text describes a protein:
Function:
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Sequence:
MPPKLLIVAGESSGELYGSLLASYLKEDFELIGLGGKHMSRAGIKLIGEVTHSFGVLEVVSQLRKIKKNMDVAIKALKDVQGVILIDFPDFNLRLAKKAKQSGKKVLYYVSPQIWAWRKGRLNIIKRVVDYMAVVLPFEEEIYKKAGIPAQFVGHPIFEAMIEELKSDSEDFIIQNKKLLKDKFGIKQDNIITLMPGSRPSEIKMKMPLMLSLINYFDRQKTHFIIPKAPNVEFNEETLKKLTSFGNVTIFNEQSYTALAMSDAAVITSGTSTLQATLLKVPMIVIYRVNPFSYIIGKMFIKGVKHIALPNVIADFMNVGDTRVTEFIQKIDVVKIVENINLLLHDTDYRGKIINFLDNIRRYFINKKASENVAEICKQLF
The following text describes a protein:
Function:
Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate). Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLFWAAHLLLSLQLVYCWAFSCQRTESSPGFSLPGDFLLAGLFSLHGDCLQVRHRPLVTSCDRPDSFNGHGYHLFQAMRFTVEEINNSSALLPNITLGYELYDVCSESANVYATLRVLALQGPRHIEIQKDLRNHSSKVVAFIGPDNTDHAVTTAALLGPFLMPLVSYEASSVVLSAKRKFPSFLRTVPSDRHQVEVMVQLLQSFGWVWISLIGSYGDYGQLGVQALEELAVPRGICVAFKDIVPFSARVGDPRMQSMMQHLAQARTTVVVVFSNRHLARVFFRSVVLANLTGKVWVASEDWAISTYITSVTGIQGIGTVLGVAVQQRQVPGLKEFEESYVRAVTAAPSACPEGSWCSTNQLCRECHTFTTRNMPTLGAFSMSAAYRVYEAVYAVAHGLHQLLGCTSEICSRGPVYPWQLLQQIYKVNFLLHENTVAFDDNGDTLGYYDIIAWDWNGPEWTFEIIGSASLSPVHLDINKTKIQWHGKNNQVPVSVCTTDCLAGHHRVVVGSHHCCFECVPCEAGTFLNMSELHICQPCGTEEWAPKESTTCFPRTVEFLAWHEPISLVLIAANTLLLLLLVGTAGLFAWHFHTPVVRSAGGRLCFLMLGSLVAGSCSFYSFFGEPTVPACLLRQPLFSLGFAIFLSCLTIRSFQLVIIFKFSTKVPTFYRTWAQNHGAGLFVIVSSTVHLLICLTWLVMWTPRPTREYQRFPHLVILECTEVNSVGFLLAFTHNILLSISTFVCSYLGKELPENYNEAKCVTFSLLLNFVSWIAFFTMASIYQGSYLPAVNVLAGLTTLSGGFSGYFLPKCYVILCRPELNNTEHFQASIQDYTRRCGTT
The following text describes a protein:
Function:
Nucleotide-sugar transporter that transports UDP-rhamnose or UDP-galactose and UMP in a strict counter-exchange mode.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MAPVSKADKKAAVDAAAWMFNVVTSVGIIIVNKALMATYGYSFATTLTGLHFATTTLMTLVLRCLGYIQPSHLPFTELLRFILFANFSIVGMNVSLMWNSVGFYQIAKLSMIPVSCLLEMVFDKIRYSRDTKLSIGLVLVGVGVCTVTDVSVNTKGFVAAFVAVWSTALQQYYVHYLQRKYSLNSFNLLGHTAPAQAATLLVVGPFLDYWLTEKRVDMYDYNLVSVLFITLSCTIAIGTNLSQFICIGRFTAVSFQVLGHMKTILVLIMGFFFFGREGLNLHVVVGMIIAVLGMIWYGNASSKPGGKERRNYSLPTTRQQKLGAASDSDDNEDKA
The following text describes a protein:
Function:
Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
Sequence:
MRPRVQTAAAWPRVCIESVTPSVDNGRFPVKRTVGDRICVEADAFCDGHDRIAVAVLWRPADAKTWASAPMRALGNDRWRAEFPLERIGTYEFRVEGWRDVFATLHADLEKKRAASTVLPVDVQEAVAVVQAAHARSEGALATQLQDILTRIGAQSEPLQQLAIVLEPDTAQAMALADDKPFRSEYPVTFRVESERRAAHFSSWYELFPRSQSGDGQRHGTFDDVIGRLAHIRAMNFDVLYMPPIHPIGAKNRKGRNNAVTAQDGEPGSPYAIGAADGGHTEVHAELGGLEGFRRLIQAARAHGLEVALDFAIQCAPDHPWLQEHKDWFTWRADGSIPYAENPPKKYQDIVNVDFYASGAVPDLWNTLRDAVLFWVNEGVTLFRVDNPHTKPFPFWEWLIADVRGRRPDVVFLSEAFTRPKMMYRLAKCGFSQSYTYFTWRNHKHELREYIEELNDGVPRECFRPHFFVNTPDINPLFLQTSGRNGHLIRAALATTLSGLWGMYQGFELCEATPLAPGKEEYLDSEKYQLRAWPERAPGDIVDEITRFNQLRRMHPELQSHLGTRFYQAHNDQVLYFGKFLDAGYLSRSRSMVLVAINLDPQAGQDAEVEIPLWELGLPDHASVAVEDLWDGHRFTWHGKTQHIRLEATRPFALWRIRAGEVA
The following text describes a protein:
Function:
Bidirectional lipid inositolphosphotransferase capable of converting phosphatidylinositol (PI) and ceramide to inositol-phosphorylceramide (IPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoinositol acceptors. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target (By similarity).
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MISYPFFSLSPPGLVPPPMAVPPVEMYSGSFWNRMRKPLPLRTQVIRFTVVFVIVSFILAVALQITHERMPDPKVTKPLPDLGFELLTKISFLSVVTDVLIAFLSSLSFFTLWKLYLLHRHCVGSGEPELPCNIPGVSRFFLSVWLCKENCRIELRNVHTIAWIRFITSYALLLLFRSLVIVMTSMPTPVDKCQNPPKIENPVKNVILTVLTAGGGSIHCGDLMYSGHTVILTLHLMFHWIYGAMVHWSFRPVVTVVAIFGYYCIVASRSHYTDDVLVAIYLTIATFIAVGHNADGAPWQLQLFIRWLPCCGANSREVTEDSQPVMVAFKSEAVDELRERDDSAGLSCEVSTNEV
The following text describes a protein:
Function:
Adapter protein that links cell surface receptor tyrosine phosphorylation to downstream signaling pathways and effectors, many of which are involved in regulation of the actin cytoskeleton. Recruited by Dscam1/Down syndrome cell adhesion molecule homolog and InR/insulin-like receptor. Recruits Pak to membranes, probably when dock/dreadlocks is associated with activated receptors. Required for guidance and targeting of photoreceptor (R cell) axon projections but not for axon outgrowth, differentiation or target induction in the developing eye. As part of a signaling pathway that involves the lbm/late bloomer protein, involved in synapse formation of the RP3 motorneuron at the muscle 7/6 cleft, probably by stimulating axon defasciculation from other SNb neurons.
Miscellaneous:
MISCELLANEOUS: Dreadlocks is named for the distinctive appearance of defective photoreceptor cell (R cell) axon projection pattern caused by excessive bundling of axons in loss of function mutants.
Subcellular Localization:
Perikaryon. Cell projection, axon. Cell projection, growth cone. Note=Highest concentration localized to the growth cones of neuronal cells.
Domain:
Possesses 3 SH3 domains, which bind polyproline motifs, and 1 SH2 domain that binds phosphotyrosine. The SH2 and SH3 domains are cooperatively involved in the binding of the cytoplasmic domains of Dscam1 and InR. SH3 domain 1 preferentially binds Dscam1 PXXP motif 1. SH3 domain 2 preferentially binds Dscam1 polyproline tract. SH3 domain 3 preferentially binds Dscam1 PXXP motif 2. Interaction of the SH2 domain with Dscam1 requires Dscam1 to be phosphorylated. InR can interact with either the SH3 domains (all 3 domains required) or the SH2 domain. Only SH3 domain 2 binding activity is essential, but not sufficient, for R cell projection targeting. SH3 domain 1, SH3 domain 2 and the SH2 binding activities contribute to R cell targeting but have redundant functions. SH3 domain 2 and the SH2 domain are both essential for targeting and patterning of inner optic ganglion neurons. SH3 domain 2 is necessary and sufficient for binding to Pak.
Sequence:
MLEHPQRFVRNIPDSSASSQQYPQQQQHPPQLPQHQNLNLNQNQNLNQNQIYQYRPQVPVPVPGSPAHHQRHSSLSQQQQLHHHRTLSTASSCSAQHKSVTFGQPALDCGGNGSGSANGSGSGNSSSGSAAGNAGTQSMAGNMKHGKSQDDVCYVVAKYDYAAQGAQELDLRKNERYLLLDDSKHWWRVQNSRNQSGYVPSNYVKKEKPSLFDSIKKKVKKGSGSKTLPNCSPSRQVESPTMSRRLPPDPAEAIGTAVVKYNYQAQQPDELSLTKGTRILILEKSNDGWWRGQSGNSVGWFPSNYTTEDCDNDGEIHTYAMAENVLDIVVALYSFTSNNDQELSFEKGDRLEIVDRPASDPDWYKARNNQGQVGLVPRNYLQELNDYLATPYRNASASAGNGNGGGSNGGAGGGGGNDSMERRNEGNKPAAQSSGQPIERPNLAGKSWYYGAITRSQCDTVLNGHGHDGDFLIRDSETNMGDYSVSLKAPGRNKHFRVHVEQNMYCIGQRKFHSLDQLVDHYQRAPIYTNKQGEKLYLVRSLPKANGT
The following text describes a protein:
Function:
Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
Subcellular Localization:
Cytoplasm.
Sequence:
MMVEAKVPLKLTLFGEHAVVYDRPAIAMTISESLKVKVSENDKFLIISPSLNIKGVKLDLNEMKIESDEAKKVLRYVFEVLNYFEMKKPVKIEINSTVEPSVGLGTSAAVIVGTVAAYSKYLGIDLSRDEIAKISHNIELKVQGIASRMDTYTETYGGLIYFPAGGKGFEKIDTNFELTAGYIRRSMSTADVLWRVRTLKESNKEVFENILDVIGEITNRAKSLIVEQNFEELGLLMYVNHGLLFSLGITSPEADEIVSRAKQLGIKGCKISGGGAGGSIICIKSVEAEVLLRSYNARIVNSTLTKDGVIFSIL
The following text describes a protein:
Function:
Involved in plastid protein homeostasis.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MEVAAATATSFTTLRARTSAIIPSSTRNLRSKPRFSSSSSLRASLSNGFLSPYTGGSISSDLCGAKLRAESLNPLNFSSSKPKRGVVTMVIPFSKGSAHEQPPPDLASYLFKNRIVYLGMSLVPSVTELILAEFLYLQYEDEEKPIYLYINSTGTTKNGEKLGYDTEAFAIYDVMGYVKPPIFTLCVGNAWGEAALLLTAGAKGNRSALPSSTIMIKQPIARFQGQATDVEIARKEIKHIKTEMVKLYSKHIGKSPEQIEADMKRPKYFSPTEAVEYGIIDKVVYNERGSQDRGVVSDLKKAQLI
The following text describes a protein:
Function:
Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90. Dephosphorylation positively regulates the Hsp90 chaperone machinery.
Subcellular Localization:
Nucleus.
Sequence:
MNFNRLAVDRRKESTLLERQDLARKPPTPKNQHKMSSSSSSIDQSTQSPTGSQPPSLDSSNSSSPPGDSRAPLGMLSIDLEPGSAYDPSLDGTSVASDVSNGVRPTDKSQLSEETIAEALRLKSEANKRFTASQYQEALDLYTLSINLNPFDATVWCNRSAVRLKREEHGLAIMDTSKAIELDPKYVKAYFRRATAQLSIMKPQLAIKDFKKCMSLDPGNAAAKVQLDATTKLVRRLDFEKAIASEDEEATSKRIQKLISEGACELDSSYAGPMLEKTGNGWKPSLKFIEEMLEWFKAGKTLPKRWIYEIILGCYEILKKEASLTEYTIPKGETCDVIGDTHGQFFDVLHLLSLTGLPSETHALVFNGDFVDRGSWSTEVVLTVFALKWYMPHKVFLNRGNHETADMNKVYGFEGETKKKYSELCYKLFEEVFCALPLCCLVTASQQPESTLVSKIPAKPFFDPQGRKRFFIVHGGLFSKDEVTFDELRKIPRMVKKQPGSEGLMMECLWTDPQDAPGRGPSKRGVGLGFGPDITENWCRHSGVTAVIRSHEVRDAGYSIEHDGRCITVFSAPNYVDQVGNQGGFVRINEHGTLEFTSYKHQPHPNIKPMAYAGGFMGLGGMI