lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Receptor for CM101, a polysaccharide produced by group B Streptococcus with antipathoangiogenic properties.
Subcellular Localization:
Basolateral cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle, secretory vesicle membrane; Multi-pass membrane protein. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane. Lysosome membrane.
Sequence:
MSLPNGYSINSPPSESGEDEEPLIKNNPGKFAIFLFIYHVISDNNYQRRRSPLLLDFNEAPICCSARLNLAILMFLGFSVVYGLRVNLSVAMVAMVNTTDPDATKNSSVIHACPLPSGAENGSQTFQQPYPWDSETQGWLLGAFFFGYLCTQIPGGYLAGHYGGSIFLGLGVLGTAVLTLFTPLAAKWGSYWLFALRALEGFGEGVTFPAMMAMWARWAPPLERSRLTTLSGSGSSFGAFLALPLTGYICEQLGWPAVFYICGGAGCFWAVLWFAFVSDDPRTHRRISDEERDYIINSIGPQVKHLFSGTGHGWTLPLLSMMLSVPLWAIILTQMSANWAFYTLLTSLPTYMSDILHFDLQSNGFLSALPYLGSLVVSLLSAVAADILIERKVFSLVLPAVFLVAVNYAGCDHILTVTFFTLSSSLGGTSAPGVYINQIDIAPRYAGFLLGITNTFGTIPGVLAPITKISVFWVAAGINLGGAIIYLLLGTADIQPWANPDEEGVRQQKRRGESIS
The following text describes a protein:
Function:
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the aspoquinolone mycotoxins. Within the pathway, asqF performs FAD-dependent dehydrogenation of the dimethylallyl quinolone peniprequinolone to yield the conjugated aryl diene yaequinolone E (By similarity). The first step of the pathway is catalyzed by the nonribosomal peptide synthetase asqK that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin. 4'-methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase asqJ. AsqJ also converts its first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI. 4'-methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B. The prenyltransferase asqH1 then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase asqF to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase asqH2 to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain. The FAD-dependent monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin. Finally, after dehydratation of the epoxide at C3 by asqC, the quinolone epoxide rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring system in aspoquinolone (Probable).
Sequence:
MALFRLSAAIVVIFLYIWSPSQRIQCRCRSFERCWPSQQDWSALNNSISGHLVNPRPVAYVCHDPDFDHDACEHVRYMANNSLWRASMPGALQNTVWESSLVSTQTCLPFSAREQPCNQGRIPLYAAVVESKKEVQTAVRFARKYNLRLVIRNTGHDGAGSSSGPESFQIFTHRLNSILYHSNFCPGGSHSKYQTCAGPAVSIGAGVMFRDLYARGAERGFVVTGGDSGTVGAAGGFIQGGGVPAFMGYTWGLAVDNVLEFEVVVATGQLVIANADENADLFWALRGGGGGSFGIVVRVTMRTYPDLPTLKGELTVSGNRHDPSFWTEDIAGLLNALRAFNHLDAPGVFRLIQTSAKGSISAVLEVYLLNRTLAEDLTRMMGPILGTSRRKYNISPITVGKISSFANPNEPTITEFFGSTILSRNFFESPNGPLVMAKRMAAINLDPGDGLLTSNLGGRINNENSDLPLHPAWRSSAHLVSLVVNVDTSLRARERAMVRLTDELMPMLYAIDSSQWVSYSNMGNPNEPDFKERYWGMRNYRRLVSIKKKWDPKDLFIARVGVRSDGWDSEGMCRT
The following text describes a protein:
Function:
Transcription factor. Plays a role in embryogenesis and later development, perhaps acting redundantly with forkhead protein fkh-2.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MTELNSSLCQLNWLIAKGGIGDVNGPEMSLVPEKQPILEVASAPQIAPGVRRKIYEGPDKPPYSYSQLIRFAIEDSVDKKCTLAEIYSYISQSFQFYRENRNPSWKNSIRHNLSLNKQFNRIEKNDGDRRGWWVCVEPPAKKPRILKGDPVRVNPIYEHLYNNKQQEVHEVIYSPVPEQVYLPQNDEEIVIQETELTEQEIMELNLFESYDLNSSFRDVYNQIFEKPKSPNEKKQAAQIDWLKISLEAAGLDYHDEQDLREIDTVKLKDYVYNGFPSECDSDASTPRTDFSRHSSSDSCVSNSLPVHGEESDDETDWDTLI
The following text describes a protein:
Function:
Transcription regulator involved in mid-term, stationary-phase viability under nitrogen starvation. Might control expression of the salvage pathways or in some other way repress the recycling of nucleobases to nucleic acids and enhance their use as general nitrogen sources during nitrogen-limited growth.
Miscellaneous:
MISCELLANEOUS: Its activity might be modulated by a sensory iron-sulfur cluster, by reversible dithiol-disulfide formation, or by both mechanisms. It is not an oxygen-responsive regulator.
Subcellular Localization:
Cytoplasm.
Sequence:
MSESAFKDCFLTDVSADTRLFHFLARDYIVQEGQQPSWLFYLTRGRARLYATLANGRVSLIDFFAAPCFIGEIELIDKDHEPRAVQAIEECWCLALPMKHYRPLLLNDTLFLRKLCVTLSHKNYRNIVSLTQNQSFPLVNRLAAFILLSQEGDLYHEKHTQAAEYLGVSYRHLLYVLAQFIHDGLLIKSKKGYLIKNRKQLSGLALEMDPENKFSGMMQ
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:
MNILKESSKRITFQLRHQKLFIQKKVLVLDLDETLVHLNSRKMKIFNMKLFLNILKVRPYLNQFLLEASKDYEIFIFIAGYEDYCQEVLGFIDKKKQLLTILQEEAVTLQMGFVIKIYYQSIGLWKIQYSLIIIQMLLQSTRIMDYSNDDDCLLKLLLFLKYMAKKIDVRPVEQYLRNYEDKIGTTVFSEAKKSIQLEQEEPDEDTLSEGKVVKRDQEVTDLDIKNKKSQTQQEIANKVKIHTLSDLQLFDCL
The following text describes a protein:
Function:
The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).
Miscellaneous:
MISCELLANEOUS: Present with 3510 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion.
Sequence:
MLRTTRLWTTRMPTVSKLFLRNSSGNALNKNKLPFLYSSQGPQAVRYTSQHEWIAVHQDKTAFVGITKYATDALGDATYVELPEVGTEIAQGESLGSIESVKSASEIYQPADGTVEEINTNLEENPGVVNEDPMGDGWLVKMKLGEGVNVEQVEGLMSLEQYEKTLVHDD
The following text describes a protein:
Function:
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Protects the cells against high-temperatures and aids in the restoration of enzyme activity of thermally denaturated proteins. Contributes to tolerance and adaptation to host-generated stresses. Has strong immunomodulatory potential and modifies the cytokine profile of the host towards the proinflammatory axis.
Miscellaneous:
MISCELLANEOUS: Expression in M.smegmatis enhances its survival within macrophages, adaptation to oxidative stress and biofilm formation.
Subcellular Localization:
Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.
Domain:
Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence:
MKSTVEQLSPTRVRINVEVPFAELEPDFQRAYKELAKQVRLPGFRPGKAPAKLLEARIGREAMLDQIVNDALPSRYGQAVAESDVQPLGRPNIEVTKKEYGQDLQFTAEVDIRPKISPPDLSALTVSVDPIEIGEDDVDAELQSLRTRFGTLTAVDRPVAVGDVVSIDLSATVDGEDIPNAAAEGLSHEVGSGRLIAGLDDAVVGLSADESRVFTAKLAAGEHAGQEAQVTVTVRSVKERELPEPDDEFAQLASEFDSIDELRASLSDQVRQAKRAQQAEQIRNATIDALLEQVDVPLPESYVQAQFDSVLHSALSGLNHDEARFNELLVEQGSSRAAFDAEARTASEKDVKRQLLLDALADELQVQVGQDDLTERLVTTSRQYGIEPQQLFGYLQERNQLPTMFADVRRELAIRAAVEAATVTDSDGNTIDTSEFFGKRVSAGEAEEAEPADEGAARAASDEATT
The following text describes a protein:
Function:
Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.
Sequence:
MAWLAIVCLLAATTALCVRMAALAPGVYGPAVCGGRSGGGRGPPRHVMIFLGSGGHTGEMLRLLEVYGAALVAGATVRVGYTDEASAERGRQSAALRAARGVEYVPLLKAREVGAGAGAAVRSTVRAAAQAFSAVRRARRALHTGPHVVVLNGPGTSVVVLFWLRVLDLLSLRRTRVVYVESLARTESLSLSGRLAYPFADEFVVQWPDLAQRYRRARWFGALV
The following text describes a protein:
Function:
Transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MSNTETNTVDEDDVCESYKMRETTKKRKLTPIQLCLLEESFEEDKRLEPDRKLWLAEKLGLQPTQVAVWFQNRRARFKTRQLELDCDSLKASYAKLKTDRDILFRQNQALENKVALLKEKLQFQEKLETQSMEAEKLGEEGSSVKSDNTQYTEEEEGLGSNQYSFPELAALGFYYDPTMSASNLGL
The following text describes a protein:
Function:
Catalyzes the release of fatty acids from lysophospholipids.
Subcellular Localization:
Secreted.
Sequence:
MKLSSFGLFLALQLLPALGLPSRIDEVDVSDPELIGLLKPDNVDKPANSIPLSKRSTSPSYAPYTVACPSGSLLRPASDGLSTGEQEFVDKRVSKVNSALESFISKTGLKIDTKSVLNDTDGPRLGIAISGGGFPAMLTGAGAINAFDARNGNTTSLGGILQSSMYLTGLSGGSWLVGSVAVNNFANITFLHDDVWNLDHSLFAPYDDAFENFYIYQEWFEQVLQKKNAGFNVSITDLWGRALALKLVNPLTGGANTTFSSVTNETWFQDGEFPFPIIIADNVIEGETVIPLNDTVFEFTPIEFGTWDTGVESFIPMEYTGTHLINGIPLNESCVRNFDNAGFLMGTSSNVFSGILPATNASLTASNNTFNNAVLSFLEMLAEDQLDVGLYPNPYQGYGNASNTTTTNPLEPYPIIELIDGGSDSEGIPFWPLLHPQRDVDVIFAIDGGYQSATSGWPDGSSLVSTYERVLATNSSGVRGFPYIPDTNTFLALGLNTHPTFFGCDGRNTTAGNHTVNDDTPPLVVYFPNYPWTMYANVTTYTVQLEDTLSSGMIENAAVAATQNNSDSFAVCVACALVQRSLERKNMSTPSQCASCFNQYCWNGTIASTTVTTYAPTVLSAKI
The following text describes a protein:
Function:
Mitochondrial transporter required for glutathione import into mitochondria.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MLSNSVNNNNNNNNINNSNSNNNDSNIHKNVKKLMVASIFGGIMSSLIVTPLDVVKTRLQTQNTGSHINQKHVFKGTLDAFKKIYKNEGPLTFWRGVTPSLLMTIPSATIYFTSYEYLKEYLYQFNDTEAYNIYTVPLVAGTLARIFSASVTSPFELLRTNSQGIVLQNAYKNTVAMAASSSTATIGTIPLSSEQRFNSFKLYRDIVNNVGIKGLWRGLGPTLVRDVPFSAIYWAGYEVLKNKLMKSQIDPNFSRNSKSPFFINFIAGATSGTLAAVLTTPIDVIKTRIQMSAQQTLSPSLTPQQQLDFIKKNNSSIYHLKQILSQEGWKGLTKGLVPRVAKVSPACAIMISTFEYIKQSHIADDN
The following text describes a protein:
Function:
Involved in capsid formation and genome binding. Shortly after infection, interaction between incoming particle-associated Gag proteins and host dynein allows centrosomal targeting of the viral genome (associated to Gag), prior to nucleus translocation and integration into host genome (By similarity).
Miscellaneous:
MISCELLANEOUS: Foamy viruses are distinct from other retroviruses in many respects. Their protease is active as an uncleaved Pro-Pol protein. Mature particles do not include the usual processed retroviral structural protein (MA, CA and NC), but instead contain two large Gag proteins. Their functional nucleic acid appears to be either RNA or dsDNA (up to 20% of extracellular particles), because they probably proceed either to an early (before integration) or late reverse transcription (after assembly). Foamy viruses have the ability to retrotranspose intracellularly with high efficiency. They bud predominantly into the endoplasmic reticulum (ER) and occasionally at the plasma membrane. Budding requires the presence of Env proteins. Most viral particles probably remain within the infected cell.
Subcellular Localization:
[Gag protein]: Virion. Host nucleus. Host cytoplasm. Note=Nuclear at initial phase, cytoplasmic at assembly. Shortly after infection, Gag protein is targeted to centrosomes. It is then actively transported into the nucleus thanks to its nuclear localization signal. In the late phases of infection, Gag proteins assemble in the cytoplasm to form the virion's capsids (By similarity); [p3]: Virion.
Domain:
Gag protein contains 3 glycine-arginine motifs (GR-boxes) necessary for RNA packaging, the first of which has nucleic acid binding properties in vitro; Late-budding 'domains' (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. Nucleocapsid protein p14 contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 (By similarity).
Sequence:
MASGSNVEEYELDVEALVVILRDRNIGRNPLHGEIIGLRLTEGWWGQLERFQMVRLILQDEDNEPLQRPRHEIIPRAVNPHTMFVLSGPLAELQLAFQDLDLPEGPLRFGPLANGHYVEGDPYSRSYRPVTMAETAQMTRDELEDTLNTQSEIEIQMINLLELYEVETRALRRQLAERSSIGQGGISPGASHSRPPVSSFSGLPSLPAIPGIHTRAPSPPRATSTPGNIPRSLGDDNMPSSSFAGPSQPRVSFHPGNPFAEAEGHRPRSQSRERRRDIPSAPVISAPVPSAPPMIQYIPVPPPPPVGAVIPIQHIRSVTGEPPRNPREIPIWLGRNAPAIDGVFPTTTPDLRCRIINALLGGNLGLSLTPGDCITWDSAVATLFIRTYGQYPLHQLGNVLKGIADQEGVATAYTLGMMLSGQNYQLVSGIIRGYLPGQAVVTAMQQRLDQEIDDQTRAETFIQHLNAVYEILGLNARGQSIRASVTPQPRPSRGRGRGQSAPEPSQGPVNSGRGRQCPAPGQNDRGSNIQNQGQENSSQGGYNLRSRTYQPQRYGGGRGRRWNENTNNSETRPTEQSPQTPRPIQAGSGVRGNQSQTYKPAAGRGGRGNQNRNQRSSGAGDSRAVNTVTQSATSSTDESSSTTTAAPSGGQGN
The following text describes a protein:
Function:
Receptor for retinoic acid that acts as a transcription factor. Forms homo- or heterodimers with retinoic acid receptors (RARs) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription. The high affinity ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression (By similarity). On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation (By similarity). Serves as a common heterodimeric partner for a number of nuclear receptors, such as RARA, RARB and PPARA. The RXRA/RARB heterodimer can act as a transcriptional repressor or transcriptional activator, depending on the RARE DNA element context (By similarity). The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes (By similarity). Together with RARA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (By similarity). Acts as an enhancer of RARA binding to RARE DNA element (By similarity). May facilitate the nuclear import of heterodimerization partners such as VDR and NR4A1 (By similarity). Promotes myelin debris phagocytosis and remyelination by macrophages. Plays a role in the attenuation of the innate immune system in response to viral infections, possibly by negatively regulating the transcription of antiviral genes such as type I IFN genes. Involved in the regulation of calcium signaling by repressing ITPR2 gene expression, thereby controlling cellular senescence (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm. Mitochondrion. Note=Localization to the nucleus is enhanced by vitamin D3 (By similarity). Nuclear localization may be enhanced by the interaction with heterodimerization partner VDR (By similarity). Translocation to the mitochondrion upon interaction with NR4A1 (By similarity). Increased nuclear localization upon pulsatile shear stress (By similarity).
Domain:
Composed of three domains: a modulating N-terminal or AF1 domain, a DNA-binding domain and a C-terminal ligand-binding or AF2 domain.
Sequence:
MDTKHFLPLDFSTQVNSSSLNSPTGRGSMAVPSLHPSLGPGIGSPLGSPGQLHSPISTLSSPINGMGPPFSVISSPMGPHSMSVPTTPTLGFGTGSPQLNSPMNPVSSTEDIKPPLGLNGVLKVPAHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVEKILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQAT
The following text describes a protein:
Function:
Probable component of a transcriptional corepressor complex involved in branching control. Regulates cotyledon expansion and lateral root growth, but not germination or hypocotyl elongation. Promotes auxin transport and PIN1 accumulation in the stem and represses BRC1/TCP18 expression in axillary buds.
Subcellular Localization:
Nucleus.
Domain:
Contains 1 EAR motif required for the interaction with TPR2.
Sequence:
MPTPVTTARECLTEEAARALDDAVVVARRRSHAQTTSLHAVSALLAMPSSILREVCVSRAARSVPYSSRLQFRALELCVGVSLDRLPSSKSPATEEDPPVSNSLMAAIKRSQANQRRHPESYHLQQIHASNNGGGGCQTTVLKVELKYFILSILDDPIVNRVFGEAGFRSSEIKLDVLHPPVTQLSSRFSRGRCPPLFLCNLPNSDPNREFPFSGSSGFDENSRRIGEVLGRKDKKNPLLIGNCANEALKTFTDSINSGKLGFLQMDISGLSLISIEKEISEILADGSKNEEEIRMKVDDLGRTVEQSGSKSGIVLNLGELKVLTSEANAALEILVSKLSDLLKHESKQLSFIGCVSSNETYTKLIDRFPTIEKDWDLHVLPITASTKPSTQGVYPKSSLMGSFVPFGGFFSSTSNFRVPLSSTVNQTLSRCHLCNEKYLQEVAAVLKAGSSLSLADKCSEKLAPWLRAIETKEDKGITGSSKALDDANTSASQTAALQKKWDNICQSIHHTPAFPKLGFQSVSPQFPVQTEKSVRTPTSYLETPKLLNPPISKPKPMEDLTASVTNRTVSLPLSCVTTDFGLGVIYASKNQESKTTREKPMLVTLNSSLEHTYQKDFKSLREILSRKVAWQTEAVNAISQIICGCKTDSTRRNQASGIWLALLGPDKVGKKKVAMTLSEVFFGGKVNYICVDFGAEHCSLDDKFRGKTVVDYVTGELSRKPHSVVLLENVEKAEFPDQMRLSEAVSTGKIRDLHGRVISMKNVIVVVTSGIAKDNATDHVIKPVKFPEEQVLSARSWKLQIKLGDATKFGVNKRKYELETAQRAVKVQRSYLDLNLPVNETEFSPDHEAEDRDAWFDEFIEKVDGKVTFKPVDFDELAKNIQEKIGSHFERCFGSETHLELDKEVILQILAASWSSLSSGEEEGRTIVDQWMQTVLARSFAEAKQKYGSNPMLGVKLVASSSGLASGVELPAKVDVIW
The following text describes a protein:
Function:
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate. Chitosan is a component of the spore wall.
Subcellular Localization:
Prospore.
Sequence:
MKSSLLKKALVLACASGRFAAAMPSQNEYEVDAEMTPFPAWLTELTGLSQWPDADPPYIPIESIDLSKVPDYKPYREGECHLNPPESCSFDCYKCLAIDDVHTCPRLSQTFDDGPSEATLELLGHLNHKTTFFNLGYNIVRNPAVYRQVMAAGHLIGTHTWSHPFLPSLTNEQVVAQLQWSIWAMNATGNHLPRWFRPPYGGIDNRIRAIARQFGLTTVLWDRDTFDWMLQSSEFSRTEQQILDDVTEWMRTGTGLILEHDGHERTARMGIQVNDMIGPNQMTVAECAGGVDYLQSLPWFSRNSHLSSEEAQ
The following text describes a protein:
Function:
May be required for pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MANRTVKDANSIHGTNPQYLVEKIIRTRIYESKYWKEECFGLTAELVVDKAMELKYVGGVYGGNIKPTPFLCLTLKMLQIQPEKDIIVEFIKNEDFKYVRLLGALYMRLTGSSVDCYKYLEPLYNDYRKIKNQNRNGEFELMHVDEYIDELLHSERVCDIILPRLQKRQVLEEAELLDTRVSALEEDLDEVETSEEEEEEEEEKPERGQSPEPHRRSYRDVDRPRRSPSPRYRRSRSPRRRSRSPKRRSPSPRRERHRSKSPRRHRSRSRERRHRSKSPGHHRSHRHRSHSKSPERSKKSHKKSRRGNE
The following text describes a protein:
Function:
Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex. Regulates trichome branch positioning and expansion.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MPITRYQIRNEYSLADPELYKAADKDDPEALLEGVAMAGLVGVLRQLGDLAEFAAEIFHDLHEEVLATAARGHGLMIRVQQLEAEVPPIEKALLSQTNHSLFLFNTGVDWHPNLQMDQNLVSRGDLPRFVMDSYEECRGPPRLFLLDKFDVAGAGACLKRFSDPSFFKIKLTSSESNKVEIQREKKVRKVKRKGSRWRNGETQEAFPASDSKLHQLFSEENNQTENNVPGYRMKLKKRQLNAFPFDSTTGKSYMERFVESLSPKHKIVCESSLTSANLKTTSRDASALGSDIHEISTENPDKNILQQRKTSIVVSPSKQEKVLEPSMEELHEDAVEGLKKSPEQIPNNEVEKIPSTFYKPHNQGESTENQKESAVNVERKLEASGDGYQSDGNTSEVENYMDALATMESEIETDTESKTKNDRGFVNIERQGVYSDTNKEELELQAQFLDSHSGDESSVSDDGNISFEKGGSNFSNSDTLSSCAETAPSDGDIAAKVYPSIETCLDKPEDVSSKKLNGDGFATKSSDDMIPGGCCIKELKDPSHRPEFGQTSSKFSITESTTHFQLSSDISLNEFHLQGQESVEISSVSVKSCTGGSSSIMEDDGKILSVDLSCPISASDFSSQMKDDSLLKGPMKTQPEELDGVKDDFLGTVSAKSQHLEVLDGGALDRSSDALPQLYSISNLAPEKEESGTDFEEVPPTEYPEDVSSENFGSPHSVVLPTVQVHGLEEQNLEACSGTTQAELFPPTNAGGLEDVNPDNKVVETDIIVLSTERNSRYCEDGSIESSSLPHVVILPTKEHLEGLTGGLEACECFTAAEHPCSTPEHMPTSVSAGDVDDVKPDTDRDILLPIGVNSESLTPEFNIRRTNEFAEDNVSGRTNEVPPRELTCEENCEHSEVKMSSNNMEVLSNASDIMLKNEPKVDVPGSINEFPTFDLDEEKNDTEHSELKTPSNKQEVPSDISHVEVTDESKPDMVHMNPCDFMGTSLSLEISSICKVPDSPKPVLMAETHLQLDEKVTETVNAEADDYNDASAHPYLIGSPSFGQIKLQEEYLFNGNSELSKLEMSEAHTPEHILPTDDQKEVNQLELSTENLNEQPKLESHDSSSSKLLQSSYDSLELHDPPTSELLENIHDCSLQFEHAPSHLSHLHLSDGLWVPKSSDETNQEWESKSTYQTDFSENAKDAVSSPTHLLQESGFPSEQVLELQADKPNIESCHDDEESSKLSDLQCEQMRPPDHIDQNGRFTASESSWVASQQCEAMLSPKPDSQSFGISVRDMDQFPSFDILPGATHQKLLEQQPTGPAIDLPVLDPNALQAELEMPPLPPLPPIQWRMGKLQNGSLTSERAMVQSSLNPFLPLLSATSDEKAKQGLSTFERETTPPTNSLSLPSACEDEKPQHDSETFGGKILNSSLNPFLPQPPVMVDDENSEHCFQTCVGEMPNLNPFFPSPPPEDEKPQHSTLASGEETMQPSLNQFTSLQSTIKDMNSRHAFMSLQGESVEPLSLLAPKPNIEDEMLQQSSLSPERGITQHLDLSVLPMTVQAEKPPHPSLSSEGEVMWPMGTFEQLPNVEDGRANGKIQIKQPRPRDPLIEAVASHDKSTLRKVEEWIRPLVGPRKDERDSLLEQIRAKSFNLKPVVTTRPIIQRSKTNLNVVAILEKANAMRQALVGSDEDDGDSWSDS
The following text describes a protein:
Function:
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSVLRAVLVQDMARALLLAAAAFVLTLIIGGWWVRFARRHKLGKRIRPDGPQSHLVKVGTPTMGGIMIVSTVLILTILFNLVDRWSMLLPLGVMVSFAVLGAIDDWLSLTGSRSKTHGFTVRFKFWIMMAVAFVASLALYLPQPYGLEHEGLVQIPFVGEVNIGLWFIPIAVLIIVFISNAVNITDGLDSLAGWNLTLAFGAYGVITFLAEPRLTNLMAFCFTVVGACAAFLWYNAYPAQVFMGDLGALALGATLAVVALQSQQWLLLPVIGIVFVVEALSTMIQTGYFKWTKWRYGEGRRIFKMAPLHHHFELLGWSQPQVTQRFVLIGTVAAMVGISLALIFGPPATGLQVDQPGIIVIEGDGSR
The following text describes a protein:
Function:
Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSETVDSTEVKSPSYDLSKFQLKRILTNNSVRKSISLLGTFPDLGTDDAIVVFEKNAYRESDVATASSEESPKKPSYFTADLKVDTEFINNIYGSFQVVPTQDLCSVKSTVIYPATEKHIEKYSVSQKYLIRETPDLYQRITLPYLTSSQFSLEWVYNILEHKQETERIVYEDRDPKTGFILLPDLKWDGRNVETLYLLGIVHKRDIKSLRDLNESHLDLLRNVRQASKDAIAKLYGINPNQLRMYFHYQPSFYHLHVHINPVRNDAPGIWCEKSHMLDTVINNLELMPDYYQRATLPFVLYEGNKLLDLYEQELPIRALTVSSDDKELPDSDSLNVAPPEGFSDEEPEERQCKRIKLGSPEPKEAESAVQACA
The following text describes a protein:
Function:
Required for meiosis I progression during spermatogenesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MHPGRTTGKGPSTHTQIDQQPPRLLIVHIALPSWADICTNLCEALQNFFSLACSLMGPSRMSLFSLYMVQDQHECILPFVQVKGNFARLQTCISELRMLQREGCFRSQGASLRLAVEDGLQQFKQYSRHVTTRAALTYTSLEITILTSQPGKEVVKQLEEGLKDTDLARVRRFQVVEVTKGILEHVDSASPVEDTSNDESSILGTDIDLQTIDNDIVSMEIFFKAWLHNSGTDQEQIHLLLSSQCFSNISRPRDNPMCLKCDLQERLLCPSLLAGTADGSLRMDDPKGDFITLYQMASQSSASHYKLQVIKALKSSGLCESLTYGLPFILRPTSCWQLDWDELETNQQHFHALCHSLLKREWLLLAKGEPPGPGHSQRIPASTFYVIMPSHSLTLLVKAVATRELMLPSTFPLLPEDPHDDSLKNVESMLDSLELEPTYNPLHVQSHLYSHLSSIYAKPQGRLHPHWESRAPRKHPCKTGQLQTNRARATVAPLPMTPVPGRASKMPAASKSSSDAFFLPSEWEKDPSRP
The following text describes a protein:
Function:
Catalyzes the incorporation of an ammonium ion into alpha-ketoglutarate to form L-glutamate, the major route of assimilation of ammonia into an organic form in yeast.
Miscellaneous:
MISCELLANEOUS: Present with 77500 molecules/cell in log phase SD medium.
Sequence:
MSEPEFQQAYEEVVSSLEDSTLFEQHPEYRKVLPIVSVPERIIQFRVTWENDKGEQEVAQGYRVQYNSAKGPYKGGLRFHPSVNLSILKFLGFEQIFKNSLTGLDMGGGKGGLCVDLKGRSNNEIRRICYAFMRELSRHIGQDTDVPAGDIGVGGREIGYLFGAYRSYKNSWEGVLTGKGLNWGGSLIRPEATGYGLVYYTQAMIDYATNGKESFEGKRVTISGSGNVAQYAALKVIELGGTVVSLSDSKGCIISETGITSEQVADISSAKVNFKSLEQIVNEYSTFSENKVQYIAGARPWTHVQKVDIALPCATQNEVSGEEAKALVAQGVKFIAEGSNMGSTPEAIAVFETARSTATGPSEAVWYGPPKAANLGGVAVSGLEMAQNSQRITWTSERVDQELKRIMINCFNECIDYAKKYTKDGKVLPSLVKGANIASFIKVSDAMFDQGDVF
The following text describes a protein:
Function:
May function as a transcription factor. May play an important role in erythroid maturation and lymphoid proliferation.
Subcellular Localization:
Nucleus.
Sequence:
MAALSPTFATSTQDSTCLQDSEFPVSSKDHSCPQNLDLFVCSGLEPHTPSVGSQESVTFQDVAVDFTEKEWPLLDSSQRKLYKDVMLENYSNLTSLGYQVGKPSLISHLEQEEEPRTEERGAHQGACADWETPSKTKWSLLMEDIFGKETPSGVTMERAGLGEKSTEYAHLFEVFGMDPHLTQPMGRHAGKRPYHRRDYGVAFKGRPHLTQHMSMYDGRKMHECHQCQKAFTTSASLTRHRRIHTGEKPYECSDCGKAFNDPSALRSHARTHLKEKPFDCSQCGNAFRTLSALKIHMRVHTGERPYKCDQCGKAYGRSCHLIAHKRTHTGERPYECHDCGKAFQHPSHLKEHVRNHTGEKPYACTQCGKAFRWKSNFNLHKKNHMVEKTYECKECGKSFGDLVSRRKHMRIHIVKKPVECRQCGKTFRNQSILKTHMNSHTGEKPYGCDLCGKAFSASSNLTAHRKIHTQERRYECAACGKVFGDYLSRRRHMSVHLVKKRVECRQCGKAFRNQSTLKTHMRSHTGEKPYECDHCGKAFSIGSNLNVHRRIHTGEKPYECLVCGKAFSDHSSLRSHVKTHRGEKLFVSSVWKRLQ