lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the hydrolysis of endogenous amidated lipids like anandamide (AEA or N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine) and eicosapentaneoyl ethanolamide (EPEA or (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl) ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules. EPEA promotes dauer formation and may constitute a signal of high nutrient availability. Breakdown of EPEA may promote lifespan extension when nutrient availability is high. Facilitates axon regeneration after injury by degradating inhibitory compounds such as AEA. FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity).
Sequence:
MIFYLVLLVLGAIAFYVHFSNNRKKLIERLEIVAQRRRDDLSKNVEQARKAADKLDTQRRDWIGSLDFEQLRDELQRGHVTCVEAIRAYFHKAILAHEKTNAVTCFILDAERQAEELDEQAKLPYYVKPPLFGVPLSLKECLKVKGYDTTRGFVQDAYHPATEDSIQVEHYKKLGLIPFCQTNVPQSLLSYNCSNPLFGTTTNPYDSTRTCGGSSGGEGALIGAGGSLIGIGTDVGGSVRIPCHFTGTAGIKPSKMRFAHRGGGASVPGKPLIDANDGPMAKDVKTNVEFLRNVWGDIDFQSDRDPYCPPVHWNESVYSSEKKLRVGYYIDDGWFTPTPALQRAVLESKKHLEAAGHTVIPFYPPRLPSVMQLYFRAVCLDGGQYVLNKLLKDIIEPTIRFQVTLWMVPVWIQRILSYPVSLVFPRMGMLMQSLTRDTFELREAYADIEAYREEFVGLMMKDNLDVILCPASIMPAPQHDIPSKVVSGVSYTCLYNLLDFGAGVVPVTAVSKSDEEKLINEYPETDKWYQITKKATLGAVGMPIGVQVAAPPYREEAVLRTMREIEIAVTGK
The following text describes a protein:
Function:
Negatively regulates proliferation of neuronal precursor cells, thereby controlling the timing of postembryonic neurogenesis.
Subcellular Localization:
Secreted.
Sequence:
MASAMRGEKCERSRIRELVLILSLITMAGDSRATPFDPSFFIEGVQSEVVNPFNRTILNRFNLTEEQILSIQNRSNPNMRDDSAQSSNQQYLQQVATQRLNDIFKRVQKAISNEPNGSASKEKAGFPICNAETTNPEDWSLGNNVTLQFASSVFISNNDDRLSSALLRLYKTNPGQTREHNPGQASTQPISTENPGNTAPNCAEQPPVGPQIRVTVSIVHQQRKKQRKKRTCNTAMLSSSSTGWVEIDVKCALAYWEQQHRQQLRQQQPLQPQLTASVVGILMIEVHDDEENLLRPGLYFAPPTCDQADIAVPWSVYRTEPFKSHLASWTLPRKPRLDIFFNGSNSMKNSYNTPKSRAFIESTTSNSPTIDNQLDESGEYESQQRVHAPLVHHRRHHHNHQQPESESESAQLEAEIEAEELMSSASNSEQQMEPISNHHRHRTGHHHPHHQLHQHHHHHHRHTKHHRIPAHKQE
The following text describes a protein:
Function:
Forms chloride channels.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane.
Sequence:
MTVIYSADVATAGCGFLKLLLRWRGSIYKLLKVDFFLYVMTFYSLALIYRFVLTSDQQTIFYFIAEHCHVFNSSTALAFVLGFFINLVMQRWNSLVGSIPSPDRMAMFVTANIRGHDDKVRLMRRTIMRYLCLSYLITLSSISPVVKKKFPKFKNMVEAGFMLENELQVIENIDSRDNKYFVPIAWCTTLLARARLEGKIKDESALKTLIDEVNDFRGKLGGLFTFDWAPLPLVYTQVVTIAVYSYFIPALICKQFRYGPGNFLIYQDWFPIFTFLEYFFYVGWLKVGESFINPFGKDDDDVDFTTLIDRNLRVSYLVVDDMHSEHPELIKDQYWETTFSQTPGQEHTSGPNNMSYLGSALDVQLKESGKHRSIDGNKQEKSWWRKGSKASSGTDRQNSANSDKDAQNVKLSSKKKQKSSIDSSTEDGKLSKNRDCDNRRR
The following text describes a protein:
Function:
Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis.
Subcellular Localization:
Chromosome, centromere, kinetochore. Nucleus.
Sequence:
MDGRVGLRASRRAAPTPRVAVRSSPRQRARVREQEPVVSAMSGSGLGKENKAGSSTPLRHRPNAFSELDNATPRVMLRKIIQNQPQVSPLALQTVQLEETEDARPEPPSQRTSSTVELQLPDLVPEDASVTTFRMTRKRKKLSISEFERAADKRLPQNQAHSTLDSTLVRSLRMSVGSVMAPDTVEKRGLLRRPQNHKAIDIAAFEGGVEQNMLQIKAQDYLVDLQTSSMTGTTTIRTDAEVVLNNTELFVEPQLGEQNLLAVEPQLSDSKTSAQRSNTSYPAHEKARLEGLVSRVSTDERRTLRFSEKDLITDHEHVDGITQKTPAKEGEDEQDHSQQNDPMEQFSESEEMAGTTEHHADAEYSEHSEKKLSRKAVSQLTAAQDAGVEMEMTPSEGGVAEGTEHQDSPKAELQMAGSPGGHSPASYSLKKSGAKPLKEAVEQTGEIERGTITGVLDAAEEEATDDESDIEDHESEEISMKTPMFVHAAAYRPHPVLSPPHPVKSASPELPPQPVRAKPVPKSSGAAQRKTREPEIASSLIKQIFSHYVKTPVTRDAYKIVEKCSERYFKQISSDLEAYSQHAGRKTVEMADVELLMRRQGLVTDKMPLHVLVERHLPLEYRKLLIPIAVSGNKVIPCK
The following text describes a protein:
Function:
May be an activator protein for the gylABX operon.
Sequence:
MSQTVDRALSILPLLAEGPADLGRVADRLGVHKSTALRLLRTLHDHGFVYRQSDQRYRLGARLISLAQEAMENLDVREIAHPHLVRLNEQVGHTVHLAVHEEDEVLYIDKVESRYPVRMYSRIGKPVAITVAAVAKLLLADLPEDERRAVAEQLDYPMYTARSTPNADGFLKELAKVREQGWATDLGGHEESINCVAAPIRGADGRVVAAMSVSAPNVVVTADELLTLLPLVRRTADAISGEYSGRTPVKEVTA
The following text describes a protein:
Function:
Transcription factor involved in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' (By similarity). Important regulator of DSG1 in the context of hair anchorage and epidermal differentiation, participates in the maintenance of the skin barrier. There is no genetic interaction with GRHL3, nor functional cooperativity due to diverse target gene selectivity during epithelia development (By similarity). May play a role in regulating glucose homeostasis and insulin signaling (By similarity).
Miscellaneous:
MISCELLANEOUS: GRHL genes (GRHL1, GRHL2 and GRHL3) show a paradoxical lack of redundancy despite their extensive sequence identity in the DNA-binding and protein dimerization domains and the fact that the core consensus DNA binding sites are identical. They have related but remarkably different functions during embryogenesis because of their differential spatiotemporal expression patterns during development.
Subcellular Localization:
Nucleus.
Sequence:
MTQEYDNKRPVLVLQNEALYPQRRSYTSEDEAWKSFLENPLTAATKAMMSINGDEDSAAALGLLYDYYKVPRERRSSTAKPEVEHPEPDHSKRNSIPIVTEQPLISAGENRVQVLKNVPFNIVLPHGNQLGIDKRGHLTVPDTTVTVSIATMPTHSIKTETQPHGFTVGIPPAVYHPEPTERVVVFDRNLSTDQFSSGAQAPNAQRRTPDSTFSETFKEGVQEVFFPSDLSLRMPGMNSEDYVFDSVSGNNFEYTLEASKSLRQKPGDSTMTYLNKGQFYPITLKEVSSNEGIHHPISKVRSVTMVVFAEDKSREDQLRHWKYWHSRQHTAKQRCIDIADYKESFNTISNIEEIAYNAISFTWDINDEAKVFISVNCLSTDFSSQKGVKGLPLNIQIDTYSYNNRSNKPVHRAYCQIKVFCDKGAERKIRDEERKQSKRKVSDVKVPLLPSHKRMDITVFKPFIDLDTQPVLFIPDVHFASLQRGTHVLPIASEELEGEGSVLKRGPYSTEDDFAVPPSAKLARIEEPKRVLLYVRKESEEVFDALMLKTPSLKGLMEAISDKYDVPHDKIGKIFKKCKKGILVNMDDNIVKHYSNEDTFQLQIEEAGGSYKLTLIEI
The following text describes a protein:
Function:
Acts as a component of the histone chaperone complex chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto DNA during replication and repair. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. Plays a role in the maintenance of heterochromatin.
Subcellular Localization:
Nucleus. Note=Localizes to replicating chromatin.
Domain:
The region N-terminal to the PCNA-interaction protein motif (PIP box) also contributes to binding of pcn1/PCNA.
Sequence:
MNSESVDSDVAASTSNKGNELCSSSTDITSLSVSSPNESVIHSSHSASEADEYVCKLSYEGNRKKRIYNGSAEAGKEKKLQKQRAQEERIRQKEAERLKREKERQQREQEKKLREQEKIAAKKMKELEKLEKERIRLQEQQRRKEERDQKLREKEEAQRLRQEQILNKERQQLKLNNFFTKGVEKRIAPNENFVADKTDELNEFEKEFRPFFIKHQMSLSKYPSPNESDSFLDEVLSTSKSYPLKLNDIFTPSDAVSSANSLGVSNRNSENEVRQLMSAYQDPSVSKPQEILSCLSQIPIKFIFFYQDVRPPYFGSYTKTHSHGSNVLLNPWLEDEDIDYTYDSEAEWVADEEDDGEDLESEDEEVDNSDDIVEDGDNAFVDDEDDDKDSVNASNTHRSSGPLEVIVEGPVWDSKFLPDFNCLSLIEPISSFSASTYLQIDPKEDLWASQDTAPASSGMTIGPTSSLSDDLQVRFPSEDIPKFIEYVRNSHDNKVFLIENLRHMFPYVTKNIISETLGKVAVRKGKSVSDGWIIKENFASLLSS
The following text describes a protein:
Function:
Involved in RNA editing event in chloroplasts. Required for the editing of a single site in rpl23 transcript.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MISSLAAITGGPSTFRRDPDSNTLRLSRRKTLISVLRSCKNIAHVPSIHAKIIRTFHDQDAFVVFELIRVCSTLDSVDYAYDVFSYVSNPNVYLYTAMIDGFVSSGRSADGVSLYHRMIHNSVLPDNYVITSVLKACDLKVCREIHAQVLKLGFGSSRSVGLKMMEIYGKSGELVNAKKMFDEMPDRDHVAATVMINCYSECGFIKEALELFQDVKIKDTVCWTAMIDGLVRNKEMNKALELFREMQMENVSANEFTAVCVLSACSDLGALELGRWVHSFVENQRMELSNFVGNALINMYSRCGDINEARRVFRVMRDKDVISYNTMISGLAMHGASVEAINEFRDMVNRGFRPNQVTLVALLNACSHGGLLDIGLEVFNSMKRVFNVEPQIEHYGCIVDLLGRVGRLEEAYRFIENIPIEPDHIMLGTLLSACKIHGNMELGEKIAKRLFESENPDSGTYVLLSNLYASSGKWKESTEIRESMRDSGIEKEPGCSTIEVDNQIHEFLVGDIAHPHKEAIYQRLQELNRILRFKENQIDIIMGF
The following text describes a protein:
Function:
May act as a morphogenetic regulator of cell adhesion. Participates in the early events that lead to differentiation.
Subcellular Localization:
Nucleus.
Sequence:
MNTIVFNKLGGAVLFEDRGTPDRERGSRTFSGFLDNPHTGPEVGIPDGPPLKDNLSLRHRRTGARQNGGKVRHKRQALQDMARPLKQWLYKHRDNPYPTKTEKILLALGSQMTLVQVSNWFANARRRLKNTVRQPDLSWALRIKLYNKYVQGNAERLSVSSDGDSCSEDGENPPRNHMNEEGYSTPAHHTVIKGESSAIKAGGRPESRAAEDYVSPPKYKSSLLNRYLNDSLRHVMATSTAMMGKTRRRNHSGSFSSNEFEEELVSPSSSETEGTFVYRTDTPDIGSTKGDSAANRRGPSKDDTYWKEINAAMALTNLAQGKDEVQGTTSCIIQKSSHIAEVKTVKLPLVQRF
The following text describes a protein:
Function:
DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPS and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks. In complex with CENPS, CENPT and CENPW (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPS, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own.
Subcellular Localization:
Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore. Note=Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPX being less stably bound at the kinetochore than CENPS.
Sequence:
MEGNSGFRKELVSRLLHLHFRDCKTKVSGDALQLMAEFLRIFVLEAAVRGVWQAQAEDLDVVEVDQLEKVLPQLLLDF
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MVKKHTSIAIAPPAPRLLANDLPTDRDLTAAQKDTLWDFTDGGAKIWKEPQDEPSKLTSNLKRLWIERGDFSQLTIESIEKQKAKPVSELEVPKSNEDDAAENQASKRSETITVDELWEMRMQMAHQLLVMSGELSTGLDLLNTLLAPLAPDAVDTTSLPLPPGGIAPMTHSLDHLSPQPEPITLINSSVSLMRKRKAAQNASCLLKRAASELGREAKRSQNEWDTLLKLREAGWNMRPKGAKPGVDMSLMGRGAERAAKEIGIAYATTEAAEALRASSFASLEPLNLDDHESTQISLKLPPRPRRRLAITLALPNQPIERFSPWERHNLEEIDILPFGEDLELARAEVLEEEIFGEISKEAQSSATYRTSTSDRSVVVKGFWEDAEISFEMLESHEETHTTTEMSSKCRLISALIRLLMVSIYRSRRSCAIGIMTANTQPSQPKILEPVLGLTVFFIYTYNLHNLFSQAVSDLKPTKLEVEAELDPILESASGMVNLICGRSNTSPQKLEVGGIAALRIMGRRLVTFTITCPVVISFWLKDEPMRIGPDQLYSVLINGINQSIIGLLIEMIDNKTLVTRKAPTGLVCQSMNHSIFLAPKFRFGTGLTIEVGNYFASNKTLSEDESMAKNLEQALLPSLGNYLGQVGLAEWVESLKEFLLT
The following text describes a protein:
Function:
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Miscellaneous:
MISCELLANEOUS: Present with 721 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSQIAQEMTVSLRNARTQLDMVNQQLAYLDRQEKLAELTKKELESYPTDKVWRSCGKSFILQDKSKYVNDLSHDETVLLDQRKTLKIKKNYLETTVEKTIDNLKALMKN
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N3 position of a uridine in 28S rRNA. Required for association of the centrosomes with the poles of the bipolar mitotic spindle during metaphase. Also involved in chromosome alignment. May promote centrosome maturation probably by recruiting A-kinase anchor protein AKAP9 to centrosomes in early mitosis. Binds specifically to miRNA MIR145 hairpin, regulates MIR145 expression at a postranscriptional level.
Subcellular Localization:
Cytoplasm.
Sequence:
MADEPSEKKNKPNTLSNKEGEERKNWKKWKEQKKEEKRRRKETKLIQQLEKQKLKKEEENQQQVKQEEKESKGRLYTVSVALPGSVMDNAQSPELRTYLAGQIARACAVFCVDEVVIFDELGEDAKSVEGEFKGVGKKGQSCVQLARILQYLECPQYLRKFFFPKHQDLQFAGLLNPLDSPHHMRIDEEAEFREGVVLDRPVKAGKGSFVNCGMRKEVQIDKQLKTGLRVTVQLNESQNKDGRVYKGVVVAPHIPRTEAGLYWGYSVRLASCLSAVFSECPYKEGYDLTIGTSEKGQNTDHVTLPAFRHMLVVFGGLQGLEASVDADENLTISDPSVLFDLYLNTCPAQGSRTIRTEEALLISLSGLRQKIASTFPDPPTG
The following text describes a protein:
Function:
Acts as a transcription regulator that binds target promoter DNA and bends the DNA. Binds to the sequences 5'-AACAAT-'3 or 5'-AACAAAG-3'. Modulates transcriptional regulation via WNT3A. Inhibits Wnt signaling. Promotes degradation of activated CTNNB1. Plays a key role in the regulation of embryonic development. Required for normal development of the definitive gut endoderm. Required for normal looping of the embryonic heart tube. Plays an important role in embryonic and postnatal vascular development, including development of arteries. Plays an important role in postnatal angiogenesis, where it is functionally redundant with SOX18. Required for the generation and maintenance of fetal hematopoietic stem cells, and for fetal hematopoiesis. Probable transcriptional activator in the premeiotic germ cells; [Isoform 2]: Has no DNA-binding activity, and does not function as transcriptional activator.
Subcellular Localization:
Nucleus.
Domain:
The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Sequence:
MSSPDAGYASDDQSQPRSAQPAVMAGLGPCPWAESLSPLGDVKVKGEVVASSGAPAGTSGRAKAESRIRRPMNAFMVWAKDERKRLAQQNPDLHNAELSKMLGKSWKALTLAEKRPFVEEAERLRVQHMQDHPNYKYRPRRRKQVKRMKRVEGGFLHALVEPQAGALGPEGGRVAMDGLGLPFPEPGYPAGPPLMSPHMGPHYRDCQGLGAPALDGYPLPTPDTSPLDGVEQDPAFFAAPLPGDCPAAGTYTYAPVSDYAVSVEPPAGPMRVGPDPSGPAMPGILAPPSALHLYYGAMGSPAASAGRGFHAQPQQPLQPQAPPPPPQQQHPAHGPGQPSPPPEALPCRDGTESNQPTELLGEVDRTEFEQYLPFVYKPEMGLPYQGHDCGVNLSDSHGAISSVVSDASSAVYYCNYPDI
The following text describes a protein:
Function:
Intramembrane glycolipid transporter that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. RFT1 could mediate the translocation of the cytosolically oriented intermediate DolPP-GlcNAc2Man5, produced by ALG11, into the ER lumen where dolichol-linked oligosaccharides assembly continues. However, the intramembrane lipid transporter activity could not be confirmed in vitro.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MISFISNQLLVRSLDPSLFGIWSVRLALVQETIVFWARDGIRKAAPRSQNPHKFAILPFLIGLIVSPIIVYISLKSAPEVEGYTLAVIMTAMSSVMELIGEMWAVPQLAVMDGSTTAKVSGPAFLVRSISSIVLSKLFYKQEGEPLPLMLCFGASNIIFGLLVIFGFYFRCGKPKIEFPTRNEYNAIKPFAFQTILQWLFSQGERIVLIASNTPEQIGVYGFVSDISSLIARLVFAPIEAAVFSMCASSAPLQFDMYSLIVRIVVYIGLCAAAFGPLLAPVVLQTVYSKSWSGDDSKSAMSWFLRIMPFMAFNGVTEAFSNARLSEKSLMYYNILLAIVSSIYFGLIFYFSKIFGTQGAIMANGVNMILRSIMAITVISREFKNFFSLFPNIIQLIAFGSLIYFQNSIRILYVLIFAPFYGLMILFFERHSIKKLWNSLKSKKRD
The following text describes a protein:
Function:
Sesquiterpene alcohol synthase that catalyzes the formation of (1S,6S,7R)-sesquipiperitol, a terpene intermediate in murgantiol biosynthesis, a male-released aggregation pheromone.
Domain:
The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Sequence:
MVSIAAKSLPKLSGAVFGQFSRRKQLIQRHWLDTRTDQYYDVLRRIVVPECKNIASDVPEYPERIEKLLYYTNPAFSDAWNFTTELIYRTVADESHQTEENITKMYLIRATMDLLFTMSAVLDDISDRSEFRKGKKGWHMICQGGESTALYDGTQMGLFPLYLLKQYFKNDPGYSRLLETVVMTYIKLTIGQTIDVLGQFKKSPSMAEYKRINYYKAGQFVAAGSELAVIHAGITSQDLIDKTVEIFTIAGQIIQTWDDFNDYYSSSEQNGKLSCDFMNAGTTWVSAKAMEVFTPSQAVKFMECYGSDDQSKMKTVQELYDEIDMPKLYTEYVLENYNRCETLIKELPHDRLREACSSYMEWLVVRETPDEDSEHKVALCLNISG
The following text describes a protein:
Function:
Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 initiates activation of G proteins G(i)/G(o) and beta-arrestin pathways inducing cellular responses via second messenger pathways such as intracellular calcium mobilization, phosphorylation of MAP kinases MAPK1/MAPK3 (ERK1/2), TYRO3, MAPK14/P38MAPK and PI3K leading to multifunctional effects, like, reduction of immune responses, enhancing of adipogenesis and angionesis. Resolvin E1 down-regulates cytokine production in macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-kappa-B. Positively regulates adipogenesis and adipocyte metabolism.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MEDLEETLFEDFENYSYALEYYSPETDSEEKAPLGAIHWVSLVLCCLAFVLGIPGNATVIWFTGFKWKKTVTTLWFLNLAIADFIFLLFLPLYISYVAMNFHWPFGIWLCKANSFIAQLNMFASVFFLMVISLDRYIYLIHPVLSHRYRTLRNSLIVIIVVWLLASLMGGPALYFRDTLELNNHTLCYNNFHEHDVDLRLLRHHVLTWVKVIVGYLLPLLTMSICYLCLIFKVKKRSILISSKHFWTILAVVMAFLICWTPYHLFSIWELTIHHNSYFHQVLQASIPLSTGLAFLNSCLNPILYVLISKKFQARFRASVAEILKYTLWEVSCSGTLSEQLRNSETKNLSLLETAQ
The following text describes a protein:
Function:
Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Catalyzes the hydrolysis of several naturally occurring membrane-associated lipids. Hydrolyzes lysophospholipids and monoacylglycerols, preferring the 1-acyl to the 2-acyl isomer. Does not catalyze hydrolysis of di- or triacylglycerols or fatty acid amides.
Miscellaneous:
MISCELLANEOUS: Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type III membrane protein.
Sequence:
MEAPLQTGMMGTSSHGLATNSSGAKVAERDGFQDVLAPGEGSAGRICGAQPVPFVPQVLGVMIGAGVAVVVTAVLILLVVRRLRVPKTPAPDGPRYRFRKRDKVLFYGRKIMRKVSQSTSSLVDTSVSATSRPRMRKKLKMLNIAKKILRIQKETPTLQRKEPPPAVLEADLTEGDLANSHLPSEVLYMLKNVRVLGHFEKPLFLELCRHMVFQRLGQGDYVFRPGQPDASIYVVQDGLLELCLPGPDGKECVVKEVVPGDSVNSLLSILDVITGHQHPQRTVSARAARDSTVLRLPVEAFSAVFTKYPESLVRVVQIIMVRLQRVTFLALHNYLGLTNELFSHEIQPLRLFPSPGLPTRTSPVRGSKRMVSTSATDEPRETPGRPPDPTGAPLPGPTGDPVKPTSLETPSAPLLSRCVSMPGDISGLQGGPRSDFDMAYERGRISVSLQEEASGGSLAAPARTPTQEPREQPAGACEYSYCEDESATGGCPFGPYQGRQTSSIFEAAKQELAKLMRIEDPSLLNSRVLLHHAKAGTIIARQGDQDVSLHFVLWGCLHVYQRMIDKAEDVCLFVAQPGELVGQLAVLTGEPLIFTLRAQRDCTFLRISKSDFYEIMRAQPSVVLSAAHTVAARMSPFVRQMDFAIDWTAVEAGRALYRQGDRSDCTYIVLNGRLRSVIQRGSGKKELVGEYGRGDLIGVVEALTRQPRATTVHAVRDTELAKLPEGTLGHIKRRYPQVVTRLIHLLSQKILGNLQQLQGPFPAGSGLGVPPHSELTNPASNLATVAILPVCAEVPMVAFTLELQHALQAIGPTLLLNSDIIRARLGASALDSIQEFRLSGWLAQQEDAHRIVLYQTDASLTPWTVRCLRQADCILIVGLGDQEPTLGQLEQMLENTAVRALKQLVLLHREEGAGPTRTVEWLNMRSWCSGHLHLRCPRRLFSRRSPAKLHELYEKVFSRRADRHSDFSRLARVLTGNTIALVLGGGGARGCSHIGVLKALEEAGVPVDLVGGTSIGSFIGALYAEERSASRTKQRAREWAKSMTSVLEPVLDLTYPVTSMFTGSAFNRSIHRVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSLWRYVRASMTLSGYLPPLCDPKDGHLLMDGGYINNLPADIARSMGAKTVIAIDVGSQDETDLSTYGDSLSGWWLLWKRLNPWADKVKVPDMAEIQSRLAYVSCVRQLEVVKSSSYCEYLRPPIDCFKTMDFGKFDQIYDVGYQYGKAVFGGWSRGNVIEKMLTDRRSTDLNESRRADVLAFPSSGFTDLAEIVSRIEPPTSYVSDGCADGEESDCLTEYEEDAGPDCSRDEGGSPEGASPSTASEMEEEKSILRQRRCLPQEPPGSATDA
The following text describes a protein:
Function:
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular Localization:
Nucleus.
Sequence:
MAPIEIPRGQASYKKREGIITLTPDKTALIWSPLPGTGPPVISLSVSNITNLQQTPKTNPKVVLRVVEKPKAPGADPAAYPFQFTHATEARNEADAIKDLLSQIIAELRGDDPSLPKPAKSGPNGAGASAAMAMASAVNSKHLPFRWFEDDMLKADVELQQSLMKKDKALAHIYNDAKLSKPDSLSDASFNSQFWATRISLLRAYAIELNQKKGSYNVLSTIKPRTENGELKLNINHEQVQLIFQQHPLVKRIYNENVPKLTESEFWSRFFLSRLSKKLRGERITDNDNTDPLFDKYLEADNTMAVPAKITATSVPPIINIEGNEENQGGFRGGNLKDVEMRPRANIPIIKTLNSLSEKIMANVAPTDVDPSAASYSKDGIADALSKQLALQDLRGDAEAQLIRLSVKDTSTFFTGNQPSLTDQEAADARLYATQVPSDVLFEVQADMDTLDSDGRGGIDLHRSIGVDPDSDDEGNNSLDSKSGPKPQHVGSRAALRFAQNQILESMKSARSHLTTTTTHGGSHTTTTNASEERPMSLPTDIAHRATLTCATTAEFLKQFWTVFNNSSNSSPEKQQELAYLADSLVRSKQRIEALADEAEKRRQEIMEKRKREIREYYQKTGRKAKWVPVGGGRDAVWAAFEGVVGGLERAVAVWEMVKSGRI
The following text describes a protein:
Function:
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MQDQVDGMELETLYQRYCIRLKHALFLSCLTVAVVTSAGLLVTTCVLQELEISLLPIVTMSVLTFSLFCILFASQFPFILESETWALVSSLFITTIVTTSMLLLGQRHAPLPLFALLLAIHTMLPLSRAVALALASIVTLAYMALSIVDRVNDDKHPYYLQLIPEGVLLVAASCTGLYYRHMTEGAHRRTFVGTRTCIESRVKLECEKEQQEQLLLSVIPAYIAAEVKRSIMLKMADACNEHSNRSFHEMYVQRHNNVSILYADIVNFTPLSEQLSASDLVKTLNELFGRFDQIAQDNQCMRIKILGDCYYCVSGLPVSRPNHAYNCVNMGLQMIEAIRFVREATGFNVDMRIGIHTGNVLCGVLGLRKWQFDVWSDDVTLANHMESGGIAGRVHITRATLHQLGDRFEVEPGDGMNRESYLADHKIETFLIVPPKKPETEAQNGNARGPLATIAERHNSIGTEGGIYGMATPSGPPTRSRPSSKMTKYVECWGADKPFANIAESTLAKNIELTTLAMIESNLLPDRSTCLECKKCWHSEDLHPALLWFRNRKQESEYRSQPDPEFRCYIAFATSIFLAMCIMQIATIPRTVVLYGTLAPTLVVLTVFVYLCWLDGCCGPRPPSDTPTDEPGACSPPGEVVTGSRCLRLAIFLVSVTLISACAVVTLVDYNPEPLPATMRELQAEKNGSVIDNRTLSTLINEFDAEIYSMEPTYLYSSALALAAISVFLRMGFILKLGLMVASVILHIFVYSYLDFFRDYHNDKFFAIPFELKSALVLAIVVIFFHILDRQIEFTSRTDYLWKAKLKVEQEEVETMRGINKILLENILPAHVAEHFLASRDTQELYHERYSCIAVMFASIPNYKEFYDESDVNKQGLECLRLLNEIICEFDKLLLKPKFSCIEKIKTIGSTYMLASGLRPGAEENSKEASRKEEHIIIALVDFAVSLMTSLDQINRDAFQRFKLRVGLNHGPVIAGVVGAQKPQYDIWGNTVNVASRMDSCGIMGKIQVTEETAKILMNAGYQCECRGVTYVKGKGNLTTYFVKTPFDDK
The following text describes a protein:
Function:
Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter.
Subcellular Localization:
Secreted, extracellular space.
Sequence:
MGVIKFGILFFFCFLLEPTCDASNPIPSVHDNQVCELCDKYLTLAIDYLQNEDNQNAFVEALHMTCSQIPPLQKQADRYTQRFFTQVSLLKPHHICKSLNLCQPPLHSQGNCDACHDTVSQLLPKLKDPQTKLKIIRLLLKECKSLNNYQDKCKKMVFEYGPLMLADLENFLEKKDVCSILGVCPTHSFYVLPAALADS