lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum. Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway. Binds cholesterol via its SSD domain.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MTLTERLREKISQAFYNHGLLCASYPIPIILFTGLCILACCCPLLKLPLPGTGPVEFTTPVKDYSPPPVAPDHKPGEPSERPEWYVGAPVAYIQQIFVKSSVSPWHKNLLAVDVFRSPLSRAFQLVEEIRNHVLRDSSGTRGLEEVCLQVTDLLPGLRKLRNLLPEHGCLLLSPGNFWQNDRERFHADPDIIGTIHQHEPKTLQTSATLKDLLFGVPGKYSGVSLYTRKRMVSYTITLVFQRYHAKFLGSLRARLMLLHPSPNCSLRAESLVHVHFKEEIGIAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRMELADLNKRLPSEACLPPAKPVGRPARFERQLAVRPSTPHTITLQPSSFRNLRLPKRLRVIYFLARTRLAQRLIMAGTVVWIGILVYTDPAGLRTYLAAQVTEQSPLGEGALTPMPVPGGVLPASHPDPAFSIFPPDGPKLPENQTLPGEPPEPGGPAEGAHDSLVPEVTWGPEDEELWRKLSFRHWPTLFSYYNITLAKRYISLLPVIPVTLRLNPREALEGRHPQDGRSAWPQRRPGPGGLWEAGPRAPGVAPAHGDVTLYKVAALGLAAGMVLVLLLLCLYRVLCPRNYGQPGSGPGRRRRGELPCDDYGYAPPETEIVPLVLRGHLMDIECLASDGMLLVSCCLAGHVCVWDAQTGDCLTRIPRPGRQRRDSGVGIAFEAQESWERLSDSGKGGPEEPGDSPPLRHRPRGPPPPALFGDQPDLTCLIDTNFSAQPRLSEPTQPEPRHRAGCSRARDGPGYDFSRLVQRVYQEDGLAPSCTPPLRPPSPGPGPPLTPEDEGPPEKGSPCLAWAPSADGSIWSLELQGSLIVVGRSSGRLEVWDAIEGTLRCSSEEVSSGITALVFLDKRIVAARLNGSLDFFSLETHSVLSPLQFRGTPGRSSSPTSPVYSSSDTVSCRLTHTVPCAHQKPITALKAAAGRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTVYIDQTMVLASGGQDGAICLWDVLTGSRVSHMFAHRGDVTSLTCTTSCVISSGLDDLISIWDRSTGIKLYSIQQDLGCGASLGVISDNLLVTGGQGCVSFWDLNYGDLLQTVYLGKNSEAQPTRQILVLDNAAIVCNFGSELSLVYVPSVLEKLD
The following text describes a protein:
Function:
Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MAKTSKLCLGKWRLWITSLLFCVTAADVRYSVPEETKTKFVIGNLSKDLNLDYNGLRFRKARLDYQGDRRYCEIDLDSGDLFVSERIDREMLCGTASPCIMHFEFILENPLELHNIALEVQDVNDNPPVFPKGSIKLEISEGAPTGSKLQLTRARDLDVGINSVQTYILSQNKHFVLDTKSSKDRYVDIVLKNSLDRETRGEHSLILSAVDGGNPPNSGTVVIEVVVIDMNDNAPLFSQPLYNARLSENSALGTSVIKITATDEDEGANGEIKYYINHLSDNTKQLFKIDENYGEISVIGQLDHEKASSYEVEVQAEDGGGQTGHCKVVIEIDDVNDNAPVISVKSLKNKIPENTTPGTEIAVINVKDQDSGENSRISCSISPNLPFQLQPYIKSYFILTTSSSLDREQIDNYNVTIIATDGGIPPLFSNISLNIQVSDVNDNSPRFELHSYFIYISENKQAGTSVCSVSANDPDWRQNGTVLYSLVPSEVNGVPMSSFLSINGDTGVIHTVRSFDYEQFRNFSVKVVARDNGSPPLSSNVTVKVFITDENDNSPQILYPVPDGKSLMTEMVPKATLSGSLVSKVIAVDADSGQNAWLSYQILKSTDPGLFTIGLHSGEIKTQRDISESDNMKQNLVISVKDNGQPSLSTTCVVNLLISDNLSEVPELKDMSYEDNNSKLTSYLIIALVSVCAFFLTFIIMMLAVKFCHRRKPRLLFDGAVAVPSAYLPPNYADVDGAGTLRSSYNYDAYLTTGSRTSDFKFVSSYNENTLPAGGILDKSEIDFNMLRLSDVGECTEQKPPNTDWRFPPNQRPGPSGAGARPEEAGAGAGVMAGTGPWPNPPTEAEQLQAMMAAANASEATATLGPRYNLQYGPDYRQNVYIPGSTATLTANPQQQVLQQALPPPQALPPTEVPKAAQTPASKKKPTKKDKK
The following text describes a protein:
Function:
Implicated in secretion, nuclear segregation and in maintenance of cell size.
Miscellaneous:
MISCELLANEOUS: Present with 33400 molecules/cell in log phase SD medium.
Domain:
Three regions of the protein are predicted to form a coiled-coil. It may adopt a rod-shaped rather than a globular configuration.
Sequence:
MSSQQHKFKRPDVSVRDKKLDTLNVQLKKIDTEIGLIRKQIDQHQVNDTTQQERKKLQDKNKEIIKIQADLKTRRSNIHDSIKQLDAQIKRKNNQIEEKLGKKAKFSSTAEAKQRINEIEESIASGDLSLVQEKLLVKEMQSLNKLIKDLVNIEPIRKSVDADKAKINQLKEELNGLNPKDVSNQFEENQQKLNDIHSKTQGVYDKRQTLFNKRAALYKKRDELYSQIRQIRADFDNEFKSFRAKLDKERLKREEEQRLSKLLEQKDVDMGKLQEKLTHAKIPAFTYEIGAIENSLLVLDPTYVKPKKNILPDLSSNALETKPARKVVADDLVLVTPKKDDFVNVAPSKSKKYKKKNQQKNTENEQPASIFNKVDGKFTLEPTLIATLAELDVTVPINSDDVKITVEQLKKKHEELLSKQEEQTKQNIESVEKEIEKLNLDYSNKEQQVKKELEEKRLKEQEESEKDKEN
The following text describes a protein:
Function:
Histone methyltransferase that specifically mono- and di-methylates 'Lys-4' of histone H3 in vitro. Does not tri-methylate 'Lys-4' of histone H3 in vitro. Promotes spermatid development and fertility by positively regulating the transcription of spermatocyte-specific genes in primary spermatocytes. Together with spr-5, required for transgenerational fertility.
Subcellular Localization:
Nucleus. Note=In males and hermaphrodites, localizes to foci in the nucleus of spermatocytes, which express the mono- and di-methyl states of 'Lys-4' of histone H3. These foci are stable nuclear structures with slow diffusion and liquid-like properties. In turn, these foci co-localize with the transcription start sites for major sperm proteins.
Sequence:
MNIKHNYISYFQMNGIQIPGISNPEAIIPITGEKKSYKLVLDFNDGAISIIEARYLDSKLHREIQDLSDNDVTILGTEISDGAYDENLDIHCDKCNKFYRPYCRLHPLFKIPDRVLKRDESSNLSFSQQTLPILFRIEESKLPNAGLGVIAEVFIPVGMVFGPYKGRRCQKKTDFYKDGYAWLIKSGDKRFYIDGSDAERSNWLRYINSPRFEDEQNMLAFQTNGKIFYRVIKPIRINQELLVWYGSSYGNEFVESENGNKYKKPAKNPFICVGAQR
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:
MKTTNKLPPRNTGTQLNYANQNLSIFQNQKPINLRRYTTGAEEMRRHQNSYGSQKRNESNEIQKQTKGKCQHNTADKQFTENGRQQHVSSLSDSQSQQPPLVMIKCQAKPQFENFKNHANAKNHNFITQQQRNEKPHSFKQIAQVNSKHLSNCNELIKFQVYYVGDLQNAILNQNAKNSEMFREHIVVSFTYIPLIQKSEIDIQQIEDKKLNIPLARNKKYNKTIIFDMDETLMHCNEDENDKCQFKIPIEFEDGERIVAGINIRNFAKEIIQKLSDVCEVMVFTASQDIYANQVINILDPHNNLGKRIFRDNCISLDDNHLIKHLGILNRDLRNVVIIDNSSCSFAHHLENGIPIISFYNDEKDNQLIKLYRYLCQYILPAEDVRPIILAHFKQDKLIQYETVEEAVKQLYF
The following text describes a protein:
Function:
Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at one or more of its N-terminal cysteine residues, which is required for its proper membrane localization (By similarity).
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Domain:
The DHHC domain is required for palmitoyltransferase activity.
Sequence:
MQCRKCCFACEKWCFIGAKAFLPLVVNFLIIWACWVHAWLVCWEPQLFESDTTFWRVYGVAGVAIGIMCNVLYLKVCKVGPGSPTDIDNFSVPLVEYQNACSAEGQHLTPPREMANSVCAKENGGLRFCTKCIGWKPDRSHHCSNYKRCVLKFDHYCPWFATAIGFHNHKYFVLFLWYVTILCFFCLGSTGFVFYNHILEIGAMRGPDGNTDYVGAISVNVMILMVLALVFAIAVGTFATFSLYLVFNNQSTVEFLESTQYRSAVPTAAYRYTFAPTSKTVGNVFDVGWKRNFQLVMGDKWWMWLLPIQPSEAARGNGTQFPLNKQVLQKIREAAAKEVQIRDQNQAYIKQQRQQQQKRTQYDLPQHLQPPPQEHYEYDDEAQDSGDDIPLINMVNKNNTK
The following text describes a protein:
Function:
Needed for flagellar regrowth and assembly.
Sequence:
MNDVVTRWLAPDLHMAPALPEAEFDEPAVYEPVLRPPTLEEIQAIEDAAQQEGFARGHAEGFAQGQSEVRRLTAQIDGILDNFTRPLARLENEVVGALGELAVRIAGSLVGRAYQAEPQLLADLVQEAIDAVGSAGREVEVRLHPDDITALLPHLATSSTTRVAPDLTLSRGDLRVHAESVRVDGTLDARLRAALETVMRKSGAGL
The following text describes a protein:
Function:
Divalent metal cation transporter which exports Zn(2+), Cd(2+) and possibly Fe(2+). May be involved in zinc and iron detoxification by efflux. In vitro, can also bind, but probably not transport, Hg(2+), Co(2+), Ni(2+), Mn(2+), Ca(2+) and Mg(2+).
Miscellaneous:
MISCELLANEOUS: Asp-49 and Asp-157 are required for both metal binding and transport process. Asp-49 is a selective binding residue for Zn(2+), Cd(2+) and Fe(2+). Asp-157 is a highly specific coordination residue for Zn(2+) and Cd(2+), but not for Hg(2+) and Fe(2+).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
The two transmembrane domains of the dimer swing out to yield a Y-shaped structure. In each protomer, the cytoplasmic domain adopts a metallochaperone-like protein fold. Each protomer contains three zinc-binding sites: a tetrahedral active Zn(2+) binding site for zinc transport, which is located toward the center of the transmembrane domain, and two cytoplasmic Zn(2+) binding sites that may serve as zinc sensors and regulate activity.
Sequence:
MNQSYGRLVSRAAIAATAMASLLLLIKIFAWWYTGSVSILAALVDSLVDIGASLTNLLVVRYSLQPADDNHSFGHGKAESLAALAQSMFISGSALFLFLTGIQHLISPTPMTDPGVGVIVTIVALICTIILVSFQRWVVRRTQSQAVRADMLHYQSDVMMNGAILLALGLSWYGWHRADALFALGIGIYILYSALRMGYEAVQSLLDRALPDEERQEIIDIVTSWPGVSGAHDLRTRQSGPTRFIQIHLEMEDSLPLVQAHMVADQVEQAILRRFPGSDVIIHQDPCSVVPREGKRSMLS
The following text describes a protein:
Function:
Transcription factor involved in abiotic stress responses. May play a regulatory role in tolerance to salt, cold, and drought stresses. Transcriptional activator that binds specifically to a mitosis-specific activator cis-element 5'-(T/C)C(T/C)AACGG(T/C)(T/C)A-3', found in promoters of cyclin genes such as CYCB1-1 and KNOLLE (AC Q84R43). Positively regulates a subset of G2/M phase-specific genes, including CYCB1-1, CYCB2-1, CYCB2-2, and CDC20.1 in response to cold treatment.
Miscellaneous:
MISCELLANEOUS: Plants over-expressing MYB3R-2 show increased tolerance to freezing. Plants over-expressing MYB3R-2 show retarded growth, increased tolerance to cold, drought and salt stresses, and have decreased sensitivity to seed germination inhibition by abscisic acid (ABA) or salt.
Subcellular Localization:
Nucleus.
Sequence:
MGAMAMVEQEGCVENRQPLAASSSSVSDGSSYGGGGGGLAQMSPPVSSSANSISGLRRTSGPIRRAKGGWTPEEDETLRKAVEAYKGRNWKKIAECFPYRTEVQCLHRWQKVLNPELIKGPWTQEEDDQIIDLVKKYGPTKWSVIAKALPGRIGKQCRERWHNHLNPEIRKDAWTTEEEQALINAHRIYGNKWAEIAKVLPGRTDNSIKNHWNSSLRKKQDMYNTSNNMVVPKLLVHDKFKDKPKLMAMEGHLDLNKAPIINSKDQPGTAHRSNCSGFLSRSSLPTAQPLTSREASVVDGSAVTLVAQALESDSVRGKGLEIDSVHEKGLEVNSAPDHTGNSWTIQLEAAPSKGEAELSLKNEARSLGPLCYQIPNMEDVVPVSSSLFSDHLTGNHTSEHCGDDILSPAGCTTPPPTKGKLTSQLSVDSILKSAANSFPGTPSILKRRKRDKSTPVSASEMKISGSNTDRFYTPMGMEPATATPESFKTTSFLSLGSLDGSVKSFDVSPQYRARSKRMALTKTVEKQLDFSSDGLDTCGSEILNSSCNNSQSTLSITEAPKLKEKEHAVQLENLTKNFAHTTNLDVT
The following text describes a protein:
Function:
Binds specifically to the plant telomeric double-stranded DNA sequences. At least 2 repeats of telomeric sequences are required for binding. Induces DNA bending.
Subcellular Localization:
Nucleus.
Domain:
The Myb-extension domain (509-540) is necessary and sufficient for telomere binding.
Sequence:
MVSHKVLEFGDDGYKLPAQARAPRSLRKKRIYEKKIPGDDKMCAIDLLATVAGSLLLESKSPVNACLVVQNTVKNEYPADENPVKAVPYSESPSLFDNGKCGFSSVITNPNHLLVGDKVGKEVEGFSSLGVSGDVKPDVVASIGSNSSTEVGACGNGSPNESRDDVNLFSRNDDDENFSGYIRTRMTRPVPRIGDRRIRKILASRHWKGGSKNNTDAKPWYCSKRSYYLHHHQRSYPIKKRKYFDSVYDSNSDDYRLQGKTHKGSRTISSMKSRNASFVSRDHHVKLRIKSFRVPELFVEIPETATVGSLKRMVMEAVTTILGDGLRVGLMVQGKKVRDDGKTLLQTGISEENNHLDSLGFSLEPSLETTPQPLLSSYLSDHACDDVTLCHDNALDSSHEPEPSPADSFGKLGTSDHSRALIPVASAAMLAPRPPNRKFKRTEQQLAAQRRIRRPFSVTEVEALVQAVEKLGTGRWRDVKVRAFEDADHRTYVDLKDKWKTLVHTARISPQQRRGEPVPQELLDRVLKAHAYWSQHLMHQLQTEPPSTQVEAL
The following text describes a protein:
Function:
Has a role in meiosis.
Subcellular Localization:
Cytoplasm.
Sequence:
MTNPEQLKRILSHEVLLKIEMSKNGIVEYANPAFFELIGYEGDLFQCSFYEYLQSDDEHLMKKATDNLFRKSISVAHVFAFLRCNPIRSPNYYIQQAKAPFEGKTYIRMLFRGILVDSLYGKDTRVLWAGKYLYPQRSVINEMDFILFNTLGIGAFILHDHLLGIIKYNYIHVPPPSGKLCSLCEDNLPEWYFEVHSDFCLVWNDLVRRVFAVQQLINCKKLEIEDIVNKLPTGSNHMVEETFLSLPVITVFNGKKNRKQRFRIRSWRSSLNFLVKELDKSIKNFAYLEHRTFLTISNSAAKDMKREIYEKSLVNWEYDFLVPSKIQDYFYDVHSLLLKNLSSKIKLCNHILMYQATFNEVKNFLQTYSLNMLSIEMENIEGSLYFGNAQLSNLICVNQYLSEQRPVFFNRLLALGNVENNNSIYDDIQKRTERISTIKRHKKYFEIGERLTEKDLIVSKTFKTTRIDYFKAVKGSIEDLDVRPLKNRQKFVNKFYASIVHFLTESMQFPSHNDRRFGDNTPHSLDEFILLKEINRGAYGRVYLAKKRSSGKYFALKMIPKSSLDSLKKIKGLLLEKRNMHIQRYGPNTVKLYYAFDSGDYLCLVMDYFNGGDCETLIQKLGPLPEQWVCQYAAELLNAIELLHQDGIIHHDIKPANMLVDETGHIRLTDFGLSENVEEKKEVYKLTKRMSFEQKHGNLYEQLQPKKFEFVRYVRNYRGNIDELEKAESPQQNSDYANDSVQHLLDFDINNMDETAIHMLMNQLEKKENRTFIKKDISGTPNYMAPEILMGVDTQMGDIWAMGCVIFEMLTGTRPFEANTVKAIWARIERNDIGWTKRVKESCSKEAVDLITKLMDPDCNKRLGSNGYQEIKKHPFFRTIKWDNLNSGPGPFVPQTENVEDLTYFEKNISGSDNINKNNCQTSATLILNGIFAFHPPPKATPADSGTETSNSAAFSASEEETTNLTDQKRKDLFSLITKAFKGIDLKALNYNNKATLLRMYDEVDFPKNQQRNKEKFRIQKRPNKKYRYHLF
The following text describes a protein:
Function:
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within keratan-like structures on N-linked glycans and within mucin-associated glycans that can ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X and in lymphocyte homing to Peyer patches. Has no activity toward O-linked sugars. Its substrate specificity may be influenced by its subcellular location. Sulfates GlcNAc residues at terminal, non-reducing ends of oligosaccharide chains.
Subcellular Localization:
Golgi apparatus, trans-Golgi network membrane; Single-pass type II membrane protein.
Sequence:
MSRSPPRALPPGASARLLPAAPAAAPRALLPPWPRRPGRRWPASPLGMKVFRRKALVLCAGYALLLVLTMLNLLDYKWHKEPLQQCSPDGPLGAAAGTGGGGWGRPGPPPAAPPRAHTRLDPRIPYRPPAAAVGAAPAAAAGAAAPPGNGTRGTGGGGDKRQLVYVFTTWRSGSSFFGELFNQNPEVFFLYEPVWHVWQKLYPGDAVSLQGAARDMLSALYRCDLSVFQLYSPAGSGGRNLTTLGIFGAATNKVVCSSPLCPAYRKEVVGLVDDRVCKKCPPQRLARFEEECRKYRTLVIKGVRVFDVAVLAPLLRDPALDLKVIHLVRDPRAVASSRIRSRHGLIRESLQVVRSRDPRAHRMPFLEAAGHKLGAKKEGVGGPADYHALGAMEVICNSMAKTLQTALQPPDWLQGHYLVVRYEDLVGDPVKTLRRVYDFVGLLVSPEMEQFALNMTSGSGSSSKPFVVSARNATQAANAWRTALTFQQIKQVEEFCYQPMAVLGYERVNSPEEVKDLSKTLLRKPRL
The following text describes a protein:
Function:
The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.
Subcellular Localization:
Secreted.
Domain:
The N- and C-terminal barrels adopt an identical fold despite having only 13% of conserved residues; The N-terminal region may be exposed to the interior of the granule, whereas the C-terminal portion may be embedded in the membrane. During phagocytosis and degranulation, proteases may be released and activated and cleave BPI at the junction of the N- and C-terminal portions of the molecule, providing controlled release of the N-terminal antibacterial fragment when bacteria are ingested.
Sequence:
MMARLYGVVVVLLLLAEVAMFGEGASNPGLVARITRKGLKYVHEHVAAALQKELSAIEVPDFLGSFQVGWFGRVSYESNGILNGTFGLSVDGISISVSLNLGKDPSGRPTASVAHCDSSIDGIDINISGPLSRIQNFFHGIMEIYFKNILEQKICEMVRMSTTSRLEPYLRTLPVTSMIDQVAGIDYSLVGAPQVTSQCLDTPFKGEFFGRSWHSPVPFDAPPIRLPQEHDRMIYFAVSDFVFNTASRVYHQAGHMKFIIQNEHLKSLTKLANNESAKKWRKQYSNSSCQTSKSTSLTATVSCFASSFLLLLLQIPLDSSIALNTNSFRALIPQLAKLYPNMQLEFETSPESAPFLMFTPGNVTLLPVIDIQTFALPPNSSDRKPLFQLRVRTSISATIGVTSSRIIASLTSVSRLTLELKHSNVGFVNVQSMETILNYYAFHILYPSLNGKKSCCCWPRATLEFSPFHSIDGSLIRKVGPLSLLAGVLATHDPGPHGVHALLGRQTCNRQ
The following text describes a protein:
Function:
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Sequence:
MRNGWNDSSKMKRFAFLGITSLFMTMALCAEADEGSSASRKTEEIHRGSKLMITKTAVSIICSSTDYKQECIASLETVKSPDPRNLIRAAFDLAIISIRSGINRGMTDIESRADADVRTRDALNSCWELMDFAIDDLLKTRDTFKGFLFTRLSDFIDDLLVWLSGSVTYQQTCIDGFEGIDSIAAEIMEMVMRKGQHLTSNGLAIASNLDALLKIFRIPIPFLRPGSGGLGIFRSDSPEEQPLDSPEGSPQMGDSSDNQQLDSSEVSPQMGDSSENQRLDSSKDSPPQNLNGPKKRPLDSSENQPMDSYENQPLDSSENQSLDSSKYSPHNLDPSKNQQPDLSESRPSDSYTTQHLDSSRNLPLDSSENTRQKLHSSESRPMDPLRALNPFGKLEDRHLSEEGGFPRWVTTHSRRLLAARGRRIRANVVVAKDGSGKCKTIKQALAMVPMKNRRKFVIYIKQGVYKEKIEVTKKMKNVMFVGDGPTKTIITGNVAFLPDRIGTYRTSTVAVNGDYFMAKDIGFENTAGAARHQAVALRVSADFAVFFNCHMNGYQDTLYVHTHRQFYRDCRISGTIDFVFGDAKAVFQNCEFVIRRPMDNQQCIVTAQGRKDRRETTGIVIHNSRITGDATYRPVKAKNRAFLGRPWKEYSRTIIMNTNIDDVIDPEGWLKWNETFALKTLFYSEYRNRGRGSGQARRVRWRGIRRISARQARGFAPGEFLRGNAWITKRRIPYNAY
The following text describes a protein:
Function:
Transcriptional activator of a number of genes encoding proteasomal subunits. Binds to the DNA sequence 5'-GAAGGCAAAA-3', enriched in regions upstream of proteasome genes.
Subcellular Localization:
Nucleus.
Sequence:
MTSLAILPQLKRTITDIMDEELYQSPSSPNSMTSFPSGTGNLMSNTNHNTFNQSNNTPFNMNYNHISNRNSINSSPNLSATTFNNANNLGNVLNIPDSFLEQLASQDYIDHLKSQQQQEQAFENPDDIYVQDVHENQVNPFNDYGNPDSFIRAQEQQSQLPQPQQPISQQDKQRPQSQQQQATKAPLPQAFPTRRRRKITLLNDIGGSSTRKKHFDEDYLLYNPDISPGHIVTDCSLDSSLVIPPNSNELFLTESESPEFANDIIPGYENDYLFLDDDDEQIEEDVSDDEGDNYFQVDEDFDDYLMNNNGYDGYPTFNNYESSGNNTDIINNNNNIVDETISDANSNSELEVVFDQPKEVSPSAISPASPDSDDMMIDVEDETEIADATAAKEEINKKHSKSGKKESKSQKENQLTTTTKSKKHSHGISGAEITLNNPNHQCNLINPSTGEPCNKQFSRPYDLIRHQDTIHASMKKIFRCVICEGRLNGGPGNGKEKTFSRGDALSRHIKIKHGLVGQDALDLINEAKENVEYIPV
The following text describes a protein:
Function:
Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process.
Subcellular Localization:
Nucleus.
Sequence:
MSQQEEQLPTQPEDLANFMDQIFSQMESKFTDMAQQVLKRIDEMSSKINELESSIDTLMQQAEQDK
The following text describes a protein:
Function:
Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity).
Subcellular Localization:
Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=Associated with the plasma membrane of basal skin keratinocytes. Translocates into the nucleus of differentiating suprabasal keratinocytes (By similarity).
Domain:
The EGFR-binding region prevents binding of a cyclin-like activator to the EGFR kinase domain, and thereby keeps EGFR in an inactive conformation. Also maintains EGFR in an inactive conformation by preventing formation of an asymmetric homodimer (By similarity).
Sequence:
MSTAGVAAQDIRVPLKTGFLHNGQALGNMKTCWGSRNEFEKNFLNIDPITMAYNLNSPAPEHLTTLGCASPSAPGSGHFFAERGPSPKSSLPPLVIPPSESSGQREEDQVLCGFKKLSVNGVCASTPPLTPIQSCSSPFPCAAPCDRSSRPLPPLPISEDPSLDEADCEVEFLTSADTDFLLEDCVPSDFKYDVPGRRSFRGCGQINYAYFDSPTVSVADLSCASDQNRVVPDPNPPPPQSHRRLRRSHSGPAGSFNKPAIRISSCTHRASPSSDEDKPEIPPRVPIPPRPAKPDYRRWSAEVTSNTYSDEDRPPKVPPREPLSRSNSRTPSPKSLPSYLNGVMPPTQSFAPDPKYVSSKALQRQSSEGSAKAPCILPIIENGKKVSSTHYYLLPERPPYLDKYEKYFREAEEANPSTQIQPLPAACGMVSATDKLASRMKMDVGGHGKRKHLSYVVSP
The following text describes a protein:
Function:
Required for the biosynthesis and the transport across the inner membrane of sulfolipid-1 (SL-1), which is a major cell wall lipid of pathogenic mycobacteria. Could also transport SL1278 (2-palmitoyl-3-(C43)-phthioceranyl-alpha, alpha'-D-trehalose-2'-sulfate), which is the precursor of SL-1. Required for virulence.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MCDVLMQPVRTPRPSTNLRSKPLRPTGDGGVFPRLGRLIVRRPWVVIAFWVALAGLLAPTVPSLDAISQRHPVAILPSDAPVLVSTRQMTAAFREAGLQSVAVVVLSDAKGLGAADERSYKELVDALRRDTRDVVMLQDFVTTPPLRELMTSKDNQAWILPVGLPGDLGSTQSKQAYARVADIVEHQVAGSTLTANLTGPAATVADLNLTGQRDRSRIEFAITILLLVILLIIYGNPITMVLPLITIGMSVVVAQRLVAIAGLAGLGIANQSIIFMSGMMVGAGTDYAVFLISRYHDYLRQGADSDQAVKKALTSIGKVIAASAATVAITFLGMVFTQLGILKTVGPMLGISVAVVFFAAVTLLPALMVLTGRRGWIAPRRDLTRRFWRSSGVHIVRRPKTHLLASALVLVILAGCAGLARYNYDDRKTLPASVESSIGYAALDKHFPSNLIIPEYLFIQSSTDLRTPKALADLEQMVQRVSQVPGVAMVRGITRPAGRSLEQARTSWQAGEVGSKLDEGSKQIAVHTGDIDKLAGGANLMASKLGDVRAQVNRAISTVGGLIDALAYLQDLLGGNRVLGELEGAEKLIGSMRALGDTIDADASFVANNTEWASPVLGALDSSPMCTADPACASARTELQRLVTARDDGTLAKISELARQLQATRAVQTLAATVSGLRGALATVIRAMGSLGMSSPGGVRSKINLVNKGVNDLADGSRQLAEGVQLLVDQVKKMGFGLGEASAFLLAMKDTATTPAMAGFYIPPELLSYATGESVKAETMPSEYRDLLGGLNVDQLKKVAAAFISPDGHSIRYLIQTDLNPFSTAAMDQIDAITAAARGAQPNTALADAKVSVVGLPVVLKDTRDYSDHDLRLIIAMTVCIVLLILIVLLRAIVAPLYLIGSVIVSYLAALGIGVIVFQFLLGQEMHWSIPGLTFVILVAVGADYNMLLISRLREEAVLGVRSGVIRTVASTGGVITAAGLIMAASMYGLVFASLGSVVQGAFVLGTGLLLDTFLVRTVTVPAIAVLVGQANWWLPSSWRPATWWPLGRRRGRAQRTKRKPLLPKEEEEQSPPDDDDLIGLWLHDGLRL
The following text describes a protein:
Function:
Involved in delta-9 desaturation of fatty acids (Probable). Plays a role in the production of very-long-chain monounsaturated fatty acids (VLCMUFAs) in seed lipids and in membrane phospholipids and sphingolipids. Acts as C-16:0 desaturase for monogalactosyl diacylglycerol (MGDG) and phosphatidylglycerol (PG). Is an essential component for cold adaptation. Is essential to adjust the acyl composition of organelle membrane lipid composition in response to cold stress.
Miscellaneous:
MISCELLANEOUS: Substrate specificity shifts from delta-9 to delta-7 desaturation when the protein is retargeted to the chloroplast.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Sequence:
MSVTSTVEENHQKNPSTPAAVEEKKKRRWVFWDRRWRRLDYVKFSASFTVHSLALLAPFYFTWSALWVTFLFYTIGGLGITVSYHRNLAHRSFKVPKWLEYLLAYCALLAIQGDPIDWVSTHRYHHQFTDSERDPHSPKEGFWFSHLLWIYDSAYLVSKCGRRANVEDLKRQWFYRFLQKTVLFHILGLGFFLFYLGGMSFVTWGMGVGAALEVHVTCLINSLCHIWGTRTWKTNDTSRNVWWLSVFSFGESWHNNHHAFESSARQGLEWWQIDISWYIVRFFEIIGLATDVKVPTEAQRRRMAIVR
The following text describes a protein:
Function:
Membrane-associated protein that warps the membrane surface to access and bind aromatic isoprenes with high specificity, including ubiquinone (CoQ) isoprene intermediates and presents them directly to Coq7, therefore facilitating the Coq7-mediated hydroxylase step. Participates in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular Localization:
Mitochondrion.
Sequence:
MNNNNNNDNDNNNDNNEILFWKVFKNVVIRNLIFKVMSEQVIEYDDMKKYYVGNRVKFSNMTLALISKNKLWTILKDKLISNQYIRIDKKGLSSFFENCNEDLDTIKLLYKFKKEEINSIIDPINQSIENENELALKYFINYIDEETGMKLPITLDSIQNGFYKHINTISMLDVLYKELRNKLNNNKNNKNNNKIDIIKVFNRLIVKNEWELLSYIFDNCLDVFIKPNELNYKEKLGYGLFTLTYKGSDEFRTKCFKSGFIEVKSTIPIYYILNNYTQFSYQDCLFLLKINHYYNNNNKKISTKQVNDLIEEMVEKEGLKYKENIEFEKIKFIKYKIAKEYDKNIFYKAYFDEFDDRISKETTTDLSTIAEYTFSSFSINGLNCLIENSFKFPKHHYVMCNLSKIEEIKGRIVQFFKIYFENDNHLNIGFSSWKPVSELIFSYQYPFEIINELLDVFPDSHLPFIIEKLNDFTVKCPSTTVKIIQKVSERIPGVMYLKRENYFKALEFYFEIYTEQQVDDLKFFEKKFFINVSSDQESISTSTLKAINNYYSVLSLSLESMEAIKRCLINYPNAEKAVICKKLYIGSLNNLDIEKIKQFIEIIGIQDINSPIFCQFHTNFNFKKLTNITQVENILNNLNQLQFPTIKINPKLTCIFFESLFDSFSFKELIENCPSFKLIDFNSFPNESLELVITNLIKSKQYESILFILNQLSSNSRLCIKYETEPNYLFEFKSGEININFNFENPNLIIQVLNEIIKKINIQESSNFIVFQILFNELVKCKNINFDQINLFLEICKSNKIQLIIGFYHIIYYFNIKNFKLSNYLTSLYLPKKTTSFSMVNKYNCGINFDFGQFPLDVIEKLSTSQLLKKLVILSKPRDFFKNNIDYLFKINEDKLALISMERYLKNTTNKDSVPSHFIKLLFKSHWFSNISNVIYVLENIKFLHKNSILERATLKKRLDIMNLILTLYDTKETKIK
The following text describes a protein:
Function:
Stabilizing factor of the core iron-sulfur cluster (ISC) assembly complex that regulates the stability and cysteine desulfurase activity of Nfs1 and participates in the [2Fe-2S] clusters assembly on the scaffolding protein IscU.
Subcellular Localization:
Mitochondrion.
Sequence:
MSTRRQAITLYRNLLRESEKLPSYNFRMYAARKIRDTFRANRSTRDFAEIDRQMAEGQQNLELIRRQVIIGHLYSADKLVIENKKTLKPSDD