lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transmembrane protein that binds to and facilitates the assembly of lysosomal proton-transporting V-type ATPase (v-ATPase), resulting in enhanced lysosomal acidification and trafficking. By bringing the v-ATPase accessory protein ATP6AP2 and the v-ATPase subunit ATP6V0D1 together, allows v-ATPase complex formation and activation. TMEM9-controlled vesicular acidification induces hyperactivation of Wnt/beta-catenin signaling, involved in development, tissue homeostasis and tissue regeneration, through lysosomal degradation of adenomatous polyposis coli/APC. In the liver, involved in hepatic regeneration.
Subcellular Localization:
Lysosome membrane; Single-pass type I membrane protein. Late endosome membrane; Single-pass type I membrane protein. Endosome, multivesicular body membrane; Single-pass type I membrane protein.
Domain:
The transmembrane domain (TMD) is essential for the interaction with ATP6AP2.
Sequence:
MKLLSLVAVVGCLLVPPAEANKSSEDIRCKCICPPYRNISGHIYNQNVSQKDCNCLHVVEPMPVPGHDVEAYCLLCECRYEERSTTTIKVIIVIYLSVVGALLLYMAFLMLVDPLIRKPDAYTEQLHNEEENEDARSMAAAAASLGGPRANTVLERVEGAQQRWKLQVQEQRKTVFDRHKMLS
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
MAFPRSRASTVSSYASTPTLSSYPSSNISTPSSNISNPSPSAAAKRATKIFTGSSNPSSFATDAISSTGIRLIVPTGGSAGGPKFIEGKRLQQHQDVVESSSFPIEAVITTGVRLTGVAIGHNPELAATGDHIVAMIRVHDALADLLLVLPKNIFPFMMQNVTPFVDELCPTRGASLSARYGNTLRGLTKSIRTGLQVLKVMILNYTSEAVPQGGGIHEITKYLLSYIMSLLEHRTSLRIILSDRQEGTVAMETLQDIVATLVSHLETMLEKESFRYQDAGLKQLFLVNNANFVLHQVKGSEIKYLLGDDWVLQHREQLKDNISRFVDISWESVMYSFHVKTSKIPIFSSLPTLKIFNLEFERIYWTQKMWTVENPLLRSDMRKSVSQKLVQAYRSYLEDHQNKVAKLVKYTPEDLEELLSELFEG
The following text describes a protein:
Function:
Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA (Potential). Has a preference for replication forks over 5' flap structures or Holliday junctions and shows much lower activity toward 3' flap structures (By similarity). Required for proper crossover distribution through inhibition of crossover formation at the central region of chromosomes (By similarity).
Subcellular Localization:
Nucleus.
Domain:
Both the N- and C-terminal regions are required for interaction with him-18.
Sequence:
METFILSSDSDDDCPPPPKRRSIEGVPKSFDGDKKMRFSFDVTRDIILEDSEAPCSSNNIFTPSFRRDSNKTLLKTPVSLRRRSRSMNCMTPIVDTINEPPINQVCSAFVQKEIQLDDDDDDEKESSTEHADDDLNLRALLSPEKKKRKEKVDKRRPFGVEEVQNEFYGVYCLISRSERQCYKNRCYIGYTVDPNRRIMQHNGGRFKGGAKKTDSRGPWDMVCVVHGFPNHVAALRFEWAWQNPAVSKSLKEKQLKKERKETPFAYQLRIACELMNSEAFSRFALTFRWLNTKEELPFPISCTPPNHVKLRYGKVKKEMSLVPAKSADYVAMGECRLCGKDIEKLWGLVRCISQSCHSHFHSKCLAEHGLKNKNEYADQIYPLKSNCPICGHFYLWGDVVREQRRIIKVSTKCAEEFRNKVVRKDLPHREISSRLRLKK
The following text describes a protein:
Function:
Required for nicotinamide riboside transport across the inner membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLITTQLSKRFYATLALSCVFLTITNILVKGSFINLLAGLSGVLYAFFAGERQTICFVFGLVYNLSYAYVAYQWKLNADVILCLFLYMPVTIYGLFAWKKTEQHEGVIKAQKLSKNWRFILILGVGVLTCVSALFFKEIKTNFLWAESFNFVIFIIAFILQVLRYIENYALVTLGNIVSIIVWFCIFQISTESLVQLFTTILYLFIGLYYFNRWNKSCKQ
The following text describes a protein:
Function:
Oxidizes L-pipecolate and L-proline (6,7% of the activity for L-pipecolate).
Subcellular Localization:
Secreted. Cytoplasm. Nucleus.
Sequence:
MVKNTSVIIVGAGVFGLSAALELTKRGGYTIKILDRAPPPVIDGSSVDANRIIRSDYADAVYCSMGIDALEEWRTNPLFKEQFYGSGLMFVGRDNVEYRDMSLENLTKMGVSAAKFQTTEELRKLFPKWIGELNDGEAGYANFSSGWANAEQSVKSVVNYLAHAGVSFISGPEGTVEELITEENVVKGVRTTTGAYMAEKLIFATGAWTASLLPNDHTRFLATGQPVAYIKLTPEEYIRFLTNPVYLDFDTGFYIFPPTPDGYLKFARHGYGFTRMQNLKSGKVESVPPKKPLVSPILPKEAELDLRRNLQRTYGEEISQRPFYKTRICYYTDTADAEFVFDYHPDYENLFVCTGGSGHGFKFFPILGKYSIGCMFRELEEPLLKKWRWKKENLEFAALDHSRAGPSRQELS
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; Peripheral membrane protein; Matrix side.
Sequence:
MCQSSPASSPTRAFVERNYKELKTLNPKLPILIRECSGVEPQLWSRYDLGVEKGIKLEGLLEAQIFKALEDLVNI
The following text describes a protein:
Function:
Proposed subunit of cytochrome c oxidase (COX, complex IV), which is the terminal component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. May play a role in the assembly of respiratory supercomplexes.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein. Mitochondrion inner membrane.
Sequence:
MSTDTGVSLPSYEEDQGSKLIRKAKEAPFVPVGIAGFAAIVAYGLYKLKSRGNTKMSIHLIHMRVAAQGFVVGAMTVGMGYSMYREFWAKPKP
The following text describes a protein:
Function:
Transcription regulator. Does not seem to be essential for embryonic development and postnatal survival (By similarity).
Subcellular Localization:
Nucleus.
Domain:
The Prospero-type homeodomain and the adjacent Prospero domain act as a single structural unit, the Homeo-Prospero domain.
Sequence:
MDPNSILLSPQPQICSHLAEACTEGERSSSPPELDRDSPFPWSQVPSSSPTDPEWFGDEHIQAKRARVETIVRGMCLSPNPLVPGNAQAGVSPRCPKKARERKRKQNLPTPQGLLMPAPAWDQGNRKGGPRVREQLHLLKQQLRHLQEHILQAAKPRDTAQGPGGCGTGKGPLSAKQGNGCGPRPWVVDGDHQQGTSKDLSGAEKHQESEKPSFLPSGAPASLEILRKELTRAVSQAVDSVLQKVLLDPPGHLTQLGRSFQGQVAEGRSEPSPPVGGACKDPLALAALPRRVQLQAGVPVGNLSLAKRLDSPRYPIPPRMTPKPCQDPPANFPLTAPSHIQENQILSQLLGHRYNNGHWSSSPPQDSSSQRHPSSEPALRPWRTTKPQPLVLSQQQCPLPFTSAHLESLPLLPSVKMEQRGLHAVMEALPFSLLHIQEGLNPGHLKKAKLMFFFTRYPSSNLLKVYFPDVQFNRCITSQMIKWFSNFREFYYIQMEKSARQAISDGVTNPKMLVVLRNSELFQALNMHYNKGNDFEVPDCFLEIASLTLQEFFRAVSAGRDSDPSWKKPIYKIISKLDSDIPEIFKSSSYPQ
The following text describes a protein:
Function:
Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Sequence:
EALGPVMSQHTGIDQIGRKEGAIGVFTAGKLTRSSVYHQAVVLALSPFHNAIYR
The following text describes a protein:
Function:
Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates.
Subcellular Localization:
Mitochondrion. Peroxisome matrix.
Sequence:
MAGLAGRFARRWFSGLLGSPLQVPALGLHVRGPAMLASQKDFNNAVSQVKLLKEDPGNEVKLKLYALYKQATEGPCNVPKPGMLDFINKTKWDAWNALGSLSKEAARQNYVDLVSRLSASSESPSPEAPAADRKQPESDSLVVTSEDGITTIRLNRPAKKNALTTQMYHDIIAALQAASKDESAITVLTGSGDYYCSGNDLTNFTHLPAGGLEEMARSAAALLRDFVNCFIDFPKPLVAVVNGPAVGISVTILGLFDVVYATDRASFHTPFSHLGQSPEGCSSYTFPKIMGSSKAAEMLLFGKKLTAQEACAQGLVTEVFPDGTFQKEVWARLKAYSKLPPNAMRISKQIIRNREKEKLHAVNAEESSVLRERWQSDECMNAIASFLSRKAKL
The following text describes a protein:
Function:
As a homodimer binds DNA via the E-box sequence 5'-CACGTG-3'. Represses lag-2 transcription during embryogenesis via Notch signaling, in an unc-37-dependent manner. Also represses tbx-37 independent of Notch signaling. In the intestine, plays a role in probiotic-mediated protection against infections by pathogens such as S.enterica. This is most likely by positively regulating the expression of genes such as bar-1 upon exposure to probiotic bacteria such as the E.faecium.
Subcellular Localization:
Nucleus.
Sequence:
MSSSPTSSSSGSPSSHGHRSETEKQRRDDTNDLLNEFKKIVQKSESEKLSKEEVLFRIVKLLSGIQLHHESFSTSPGPIRSIKKIKSDREQVRRNKRVAAYRELRKFIALNNLSSSEEIDKMENLKVLEIIFEVIRGKSITCTVPCLPFPILPFLPVFPVYSPLVFNSYNQFSLYPPHMPTVQIPIVPSSSFEIDALEIEENEKDIDIVG
The following text describes a protein:
Function:
Peptidyl-alpha-hydroxylglycine alpha-amidating lyase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Mediates the dismutation of the unstable peptidyl(2-hydroxyglycine) intermediate to glyoxylate and the corresponding desglycine peptide amide. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
Subcellular Localization:
Secreted.
Sequence:
MSRLLFVALLAISLGYVASSSSNHLPAGLAMDLGPGVNLNERFFDQVRALIKRRLQEKGLAKPEQPELAMPLTDDDAVALQNQRSYDNVPLPAASVPTPVLVENWPTEQHSFGQVTAVAVDPQGSPVVFHRAERYWDVNTFNESNIYYLIEYGPIKENTIYVLDAKTGAIKSGWGSNMFYMPHGLTIDLHGNYWITDVAMHQAFKFKPFSNKPLLTIGKRFRPGSSVKHLCKPTSIAVATTGEFFIADGYCNSRILKFNAAGKLLRTIPQPPEFLSLQVPHAITLLEHLDLLCIADRENMRVVCPKAGLISSHGEGEPAATIQEPDLGRVFGVASFGDIVFAVNGPTSMLPVRGFTIDPRSETIIGHWGEFKNPHSMAVSVNGSALYVTEIGTNHQTNRVWKYVLA
The following text describes a protein:
Function:
Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development. Interacts with splicing-related factors via the intrinsically disordered region and regulates alternative splicing of target pre-mRNA species. May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery. May be involved in ATXN1 mutant-induced cell death. The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit. Involved in the assembly of cytoplasmic stress granule, possibly by participating in the transport of neuronal RNA granules. Also acts as an innate immune sensor of infection by retroviruses, by detecting the presence of reverse-transcribed DNA in the cytosol. Directly binds retroviral reverse-transcribed DNA in the cytosol and interacts with CGAS, leading to activate the cGAS-STING signaling pathway, triggering type-I interferon production.
Subcellular Localization:
Nucleus. Nucleus speckle. Cytoplasmic granule. Note=Colocalizes with SRSF2 in nuclear speckles (By similarity). Colocalized with POU3F2. Colocalized with ATXN1 in nuclear inclusion bodies. Localizes to cytoplasmic stress granules (By similarity).
Domain:
The WW domain may play a role as a transcriptional activator directly or via association with the transcription machinery. The WW domain mediates interaction with WBP11, ATN1, SF3B1 and the C-terminal domain of the RNA polymerase II large subunit; Except for the WW domain, the protein is intrinsically disordered.
Sequence:
MPLPVALQTRLAKRGILKHLEPEPEEEIIAEDYDDDPVDYEATRLEGLPPSWYKVFDPSCGLPYYWNVDTDLVSWLSPHDPNSVVTKSAKKLRSSNADAEEKLDRSHEKSDRGHEKSDRGHEKSDRSHEKSERNHEKSDRDRERGYDKVDRERERDRDRDRGYDKVDREESKERRHHRREELAPYPKSKKAASRKDEELDPMDPSSYSDAPRGTWSTGLPKRNEAKTGADTTAAGPLFQQRPYPSPGAVLRANAEASRTKQQD
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MITMGKSLALIPLYPSKNSLFKKVYSVFVIVFITIWTLIANFYRISYYKTFVPTKLINNILFEIVSYSLTVATILNAILYGKNKWYVVLDFLKNKEQKYVCYFAIANAFYWVIVLYAISVWVDFEGNDYFKKFSDDVVLFYNHFYICCFIYIFTKEVKNAYKSLNMMLKLPKINKIQDLQNRVASLKNTIDSFNELFGLPFVCIIFTTGVTVVDFLDDILKNSYGYSRTQHLRIVAANLITIISVLIPTVGMILSCQQVYGSATVLLNTAYNLRRGLVGRERQEVTSFINTLLNHFPNFTAANFFRIDKSVVFRVLGVVTTYLIVVVQFNASSDT
The following text describes a protein:
Function:
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Localization:
Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MSQNNPLSVCVADNLINYDIQNESFRLGNVSVEGDKYICVKENVNENTQVVVINLHNKNSTRKHMKAESVIIHPNDPILALKGTIKNMNTIFLQVFNIETKEKICSLNLNEYMNYWKWINNDTIAIVCEKNVYHWNIDIHNTKKNKDNNDNNNNNNNNNNNNNNNNYFNTLTKVFEKAQIFIDNNSQILYYSTDKDMKWCILCGISTQDQGKSIDGYMQLYSCEKKLHQTIEGFIGCFGSFVFDNLDMKPLFCFVEKKKNSTISRLHLMDIYTNKTETTIPYKIVKEINLINENLNDFPIYISLNTLQGVIYIVTKCSYVYVFDEGTLSLIVKEKISEDNIFICCDSKNGEGIYAVNKKGIIFYITINYFHLINHLKLSNLEFKDKIIKNLCVKYGYPGCDYISAYKKCINDMDFKKASKIICLMKNTKIFEEHSNNIAESILIMNRKNIDIRIIPPLRTQQVLNSFKSFKNTSGQLSPLLLYFSVLLEYDKLNTYESIELVKPVVLQKKKEYLEKWIKDDKLTCSEELGDLVKVLDLRLALNIYLRCSSHNKILSTYCLLNMFNNVLSYINNFKQINFDYVGIFITIVNYEFPQGNADNKDSAFVGDFNSGSKNETMDFFNDGAASISNDQNNSINKLNKGHINEVAIQYIKFLCENNISFDINKIIDYLLSKKKLQEATSILLDYLKENKAEHKNLQTKLFEFNLYNNVQVAETLFQMDIFTYYDKNKIAYLCEEKGLYQRALENYTNINDIKRVITKSTCFQKGGNNNNTTTTTTTTSNMGDGHFDMNNVSKGKISIEWIKNYFSTLSDSVCEELLFDFMKGSKINMEVVISICVQYYDKIGIKKIINKFEENKNYEGIFYFVSNILNDLPNLIVKGNNNDNLSNNSLSTYNNMNDEDASILLTSDICSTPQYSYETANLKLEDVHYIMFKYIEACVKINNIQELDRICKDKNAKYNPEQIKNFLKDCKLSDPRPLIYVCDIHNYIEELAEYLYKNSLLKYIEVYVIKVNPNNAHKVIGVLLDLDASEDFLLNLLNNIKNISNIGNLIEIAEKRNRLKLLLPWLESRANEGYENIELHNALAKIYIDLNKDPENFLKNNNFYDKKMIGKYCEDLDPHLAYTAYERSNGECDEELIYITSKNGLFKLQARYLISRQSIELWKVVLDETNKYRKNVIDQVIGSTLIESNNADEITVTVKAFIEKKLSSELIELLEKIVLHNSEFSDNKNLQNLLILTAIKSDSKKVMEYINRLDNFSGPQIAAVAYEYKLREEAFVIYKKFNCYTSAISVLLDKILYNKNQKNKNFHEFSSHDSTVPYYSNNNNKDNIFGNKSDNENDEYLKQFTQNNSYREKYGSYYNNNDISNSNNNNIHLHPEFNNEDKFSSDTLHNYEDIDSTESTCDLSNYEDDLNRAIEFAQKCNNNDVWFILGKAQLKLNKIIDSIDSFVKSNNPEAYKEVIEKCKENNFYEHLITYLNTLREQNSLKDVLVDSELLYAYAKLKKTNEMNKFINTTNSANLQLIGDRLYKEEEYEVAKILYSNIPNNQKLTACYLKLKEYALAIEAAKKAKSLKTWKEVNFICVKYKQLKYAHTAGLQLIMHADHLDEIIKIYEKKKYINELMNLLENGLNNERAHVGIYTELGILYAKYKPEKLMEFIRNYTNKMNTRKLIDVCENEYLLKEAVYLYISYDEYNLAVDTIIKHSPTAYTADTFMQVIHKVTNSDIIHKVIDFYIEEHPLNLYNLLKILENKIDNNRLVQTLKKSNNLPLIQKYLEDIQAQNITAVNETLNEIYLQNDDYISLRNSIDEYDNFNQTNLLNKLENHKLPEMRRIAALLYKKNKKYKEAINLSKKEKQYKDAIEIARVSKNNVYIEDLINYFIESKNKEAFCACLIVCYDLLKPDYILEIVWTSGFKDQAMLYFIQIISDYTNQIEHMKKQIEDMEKEKKMNKSAPNDYSAMNNQFNYSLNNNLSIMPPQNNFMSSNSFDKYDMFNNNTHF
The following text describes a protein:
Function:
Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the epimerization of UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (UDP-alpha-D-GlcNAc3NAcA) to UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid (UDP-alpha-D-ManNAc3NAcA). Exhibits high specificity towards the substrate as UDP-alpha-D-GlcNAc, UDP-alpha-D-GlcNAcA (UDP-2-acetamido-2-deoxy-alpha-D-glucuronic acid) and UDP-alpha-D-GlcNAc3NAc (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucose) cannot act as substrates.
Sequence:
MKILTIIGARPQFIKASVVSKAIIEQQTLSEIIVHTGQHFDANMSEIFFEQLGIPKPDYQLDIHGGTHGQMTGRMLMEIEDVILKEKPHRVLVYGDTNSTLAGALAASKLHVPIAHIEAGLRSFNMRMPEEINRILTDQVSDILFCPTRVAIDNLKNEGFERKAAKIVNVGDVMQDSALFFAQRATSPIGLASQDGFILATLHRAENTDDPVRLTSIVEALNEIQINVAPVVLPLHPRTRGVIERLGLKLEVQVIDPVGYLEMIWLLQRSGLVLTDSGGVQKEAFFFGKPCVTMRDQTEWVELVTCGANVLVGAARDMIVESARTSLGKTIQDDGQLYGGGQASSRIAEYLAKL
The following text describes a protein:
Function:
Catalyzes the epoxidation of physiological unsaturated fatty acids in vitro. Can use laurate, oleate, linoleate, linolenate and vernolate as substrate.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MFPLISFSPTSLDFTFFAIIISGFVFIITRWNSNSKKRLNLPPGPPGWPVVGNLFQFARSGKPFFEYAEDLKKTYGPIFTLRMGTRTMIILSDATLVHEALIQRGALFASRPAENPTRTIFSCNKFTVNAAKYGPVWRSLRRNMVQNMLSSTRLKEFGKLRQSAMDKLIERIKSEARDNDGLIWVLKNARFAAFCILLEMCFGIEMDEETIEKMDEILKTVLMTVDPRIDDYLPILAPFFSKERKRALEVRREQVDYVVGVIERRRRAIQNPGSDKTASSFSYLDTLFDLKIEGRKTTPSNEELVTLCSEFLNGGTDTTGTAIEWGIAQLIANPEIQSRLYDEIKSTVGDDRRVDEKDVDKMVFLQAFVKELLRKHPPTYFSLTHAVMETTTLAGYDIPAGVNVEVYLPGISEDPRIWNNPKKFDPDRFMLGKEDADITGISGVKMIPFGVGRRICPGLAMATIHVHLMLARMVQEFEWCAHPPGSEIDFAGKLEFTVVMKNPLRAMVKPRI
The following text describes a protein:
Function:
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Sequence:
MSRAGLEVLIRRVDPDVPLPAYAQPGDAGADLRTTVERELAPGERAVLPTGVSVALPEGYAAFVHPRSGLAARCGVALVNAPGTIDAGYRGEIKVIVVNLDPRESVRFERFDRIAQLVVQQVERVRFRQVAELPGSARAEGGFGSTGGHAGLDPASGTSGQVAEGGPTGGNRYASVVSDREGQ
The following text describes a protein:
Function:
May play an important role in maintaining centrosome integrity during mitosis.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Note=Localizes at spindle poles and/or centrosomes in both mitotic and interphase cells. Spindle pole localization is more pronounced during mitosis. Centrosomal localization culminates at prophase.
Sequence:
MSATTACWPAFTVLGEARGDQVDWSRLYRDTGLVKMSRKPRASSPFSNNHPSTPKRFPRQPRREKGPVKEVPGTKGSP
The following text describes a protein:
Function:
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
Miscellaneous:
MISCELLANEOUS: Present with 91800 molecules/cell in log phase SD medium.
Sequence:
MDAYSTRPLTLSHGSLEHVLLVPTASFFIASQLQEQFNKILPEPTEGFAADDEPTTPAELVGKFLGYVSSLVEPSKVGQFDQVLNLCLTEFENCYLEGNDIHALAAKLLQENDTTLVKTKELIKNYITARIMAKRPFDKKSNSALFRAVGEGNAQLVAIFGGQGNTDDYFEELRDLYQTYHVLVGDLIKFSAETLSELIRTTLDAEKVFTQGLNILEWLENPSNTPDKDYLLSIPISCPLIGVIQLAHYVVTAKLLGFTPGELRSYLKGATGHSQGLVTAVAIAETDSWESFFVSVRKAITVLFFIGVRCYEAYPNTSLPPSILEDSLENNEGVPSPMLSISNLTQEQVQDYVNKTNSHLPAGKQVEISLVNGAKNLVVSGPPQSLYGLNLTLRKAKAPSGLDQSRIPFSERKLKFSNRFLPVASPFHSHLLVPASDLINKDLVKNNVSFNAKDIQIPVYDTFDGSDLRVLSGSISERIVDCIIRLPVKWETTTQFKATHILDFGPGGASGLGVLTHRNKDGTGVRVIVAGTLDINPDDDYGFKQEIFDVTSNGLKKNPNWLEEYHPKLIKNKSGKIFVETKFSKLIGRPPLLVPGMTPCTVSPDFVAATTNAGYTIELAGGGYFSAAGMTAAIDSVVSQIEKGSTFGINLIYVNPFMLQWGIPLIKELRSKGYPIQFLTIGAGVPSLEVASEYIETLGLKYLGLKPGSIDAISQVINIAKAHPNFPIALQWTGGRGGGHHSFEDAHTPMLQMYSKIRRHPNIMLIFGSGFGSADDTYPYLTGEWSTKFDYPPMPFDGFLFGSRVMIAKEVKTSPDAKKCIAACTGVPDDKWEQTYKKPTGGIVTVRSEMGEPIHKIATRGVMLWKEFDETIFNLPKNKLVPTLEAKRDYIISRLNADFQKPWFATVNGQARDLATMTYEEVAKRLVELMFIRSTNSWFDVTWRTFTGDFLRRVEERFTKSKTLSLIQSYSLLDKPDEAIEKVFNAYPAAREQFLNAQDIDHFLSMCQNPMQKPVPFVPVLDRRFEIFFKKDSLWQSEHLEAVVDQDVQRTCILHGPVAAQFTKVIDEPIKSIMDGIHDGHIKKLLHQYYGDDESKIPAVEYFGGESPVDVQSQVDSSSVSEDSAVFKATSSTDEESWFKALAGSEINWRHASFLCSFITQDKMFVSNPIRKVFKPSQGMVVEISNGNTSSKTVVTLSEPVQGELKPTVILKLLKENIIQMEMIENRTMDGKPVSLPLLYNFNPDNGFAPISEVMEDRNQRIKEMYWKLWIDEPFNLDFDPRDVIKGKDFEITAKEVYDFTHAVGNNCEDFVSRPDRTMLAPMDFAIVVGWRAIIKAIFPNTVDGDLLKLVHLSNGYKMIPGAKPLQVGDVVSTTAVIESVVNQPTGKIVDVVGTLSRNGKPVMEVTSSFFYRGNYTDFENTFQKTVEPVYQMHIKTSKDIAVLRSKEWFQLDDEDFDLLNKTLTFETETEVTFKNANIFSSVKCFGPIKVELPTKETVEIGIVDYEAGASHGNPVVDFLKRNGSTLEQKVNLENPIPIAVLDSYTPSTNEPYARVSGDLNPIHVSRHFASYANLPGTITHGMFSSASVRALIENWAADSVSSRVRGYTCQFVDMVLPNTALKTSIQHVGMINGRKLIKFETRNEDDVVVLTGEAEIEQPVTTFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNHFKDTYGFSILDIVINNPVNLTIHFGGEKGKRIRENYSAMIFETIVDGKLKTEKIFKEINEHSTSYTFRSEKGLLSATQFTQPALTLMEKAAFEDLKSKGLIPADATFAGHSLGEYAALASLADVMSIESLVEVVFYRGMTMQVAVPRDELGRSNYGMIAINPGRVAASFSQEALQYVVERVGKRTGWLVEIVNYNVENQQYVAAGDLRALDTVTNVLNFIKLQKIDIIELQKSLSLEEVEGHLFEIIDEASKKSAVKPRPLKLERGFACIPLVGISVPFHSTYLMNGVKPFKSFLKKNIIKENVKVARLAGKYIPNLTAKPFQVTKEYFQDVYDLTGSEPIKEIIDNWEKYEQS
The following text describes a protein:
Function:
Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides.
Sequence:
MDLLERLGLGGRRVLILHHDDLGLTHAQNGAYQALGLPTGSVMVPGAWASGVKGEDLGVHLVLTSEWPAPRMRPLTEGESLRDEAGYFPESLEALWRKARAEEVERELKAQIQAAAKLFSPTHLDAHQGAVLRPDLAEVYLRLAEAYRLVPLVPESLEGLGVPPPFLPELERLLYETPFPQVRFLDPYGLPPEERLGFYLDLAHLPPGLYYLVHHSALPTPEGRALPDWPTREADYFALSHPEVRRVLAEFHPLTWRAVREALF
The following text describes a protein:
Function:
Binds to and releases the BluR repressor from its bound DNA target in a blue light-dependent (470 nm) fashion. A shift to low temperature also triggers a BluF-mediated relief of repression by BluR, suggesting BluF may serve as a thermometer. Blue light may act to increase the affinity of BluF for BluR, allowing it to be released from its operator. The protein has a reversible photocycle, and undergoes structural changes, probably in the EAL domain, in response to light.
Domain:
The joining helix is required for stability of the light-adapted state; Contains a defective C-terminal cyclic-di-GMP phosphodiesterase EAL domain, which lacks key amino acids required for phosphodiesterase activity. Restoration of consensus amino acids in the degenerate EAL domain does not restore phosphodiesterase activity and reduces ability to antagonize BluR.
Sequence:
MLTTLIYRSHIRDDEPVKKIEEMVSIANRRNMQSDVTGILLFNGSHFFQLLEGPEEQVKMIYRAICQDPRHYNIVELLCDYAPARRFGKAGMELFDLRLHERDDVLQAVFDKGTSKFQLTYDDRALQFFRTFVLATEQSTYFEIPAEDSWLFIADGSDKELDSCALSPTINDHFAFHPIVDPLSRRIIAFEAIVQKNEDSPSAIAVGQRKDGEIYTADLKSKALAFTMAHALELGDKMISINLLPMTLVNEPDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFQPDRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKAKLNGIPSIAWPEKK
The following text describes a protein:
Function:
Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Required for cell division and expansion and is involved in proper organization of the embryo.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MLLDMDLGVLLPSLQSVYVLVFYFVYLAVAGEILPGKVIRGVLLSDGSQLRYRCNGLLALILLVAILGICAKLGIVSPLVVADRGLELLSATFIFCVLVTLALYVTGRSSSNKGSSLKPHVSGNLVHDWWFGIQLNPQFMSIDLKFFFVRAGMMGWLLINLSILAKSVQDGSLSQSMILYQIFCALYILDYFVHEEYMTSTWDIIAERLGFMLVFGDLLWIPFTFSIQGWWLLHNKVELTVPAIVVNCLVFLIGYMVFRGANKQKHIFKKNPKTPIWGKPPVVVGGKLLVSGYWGIARHCNYLGDLMLALSFSLPCGISSPVPYFYPIYLLILLIWRERRDEVRCAEKYKEIWAEYLRLVPWRILPYVY
The following text describes a protein:
Function:
Probable transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MEEITSQEAAESPRVQFQSLESQSECLSPELRFLRDTEMEQGYTDAPPVPQVPALPHEGSPGDQAAALLTARYQEFVTFEDVAVHLTREEWGCLDPVQRELYREVMLENYGNVVSLGFPISKPDGISQREQDLQVFDLETQNREGVRNDCSDGETREENKLLIPKRKISEEVHSYKVRVGKFKQDIAQVPETREAYKSEDRLERLQEILRKFLFLEREFRQITISKKTFSNEKNTEPEKSFSLDSTLDTDQRVLRIQTIDDSKYDMNFNQNPAVGEQEPINLTENFQNTDYKESLMDLSHLNKWESMPTTDRSYKCDTCGKTFHQASALTRHQRIHTREKPYKCKECEKSFSQSSSLSRHKRIHTREKSYRCEASDKSCDASDKSCSQSSDVLQHKKVHAKAKSYKCGTCERVFSRSVHLTQHQRTHKDTACKCTVCGSDFCHTSYLVEHQRLHHQEKSYEYDECGLAYVKQQGIRFREKPYSCNECGKDFRLNSHLVQHQRIHTGEKLHECNERGKAFSQTSCLSQHHKMHRKEKSYEYNNYEESFSHNSDLTLQQEVPIRERVFDCDAWEENFSQRAHLIPHERAHTKEKPYECNELGETFSQVQASFNM
The following text describes a protein:
Function:
Intermedin/ADM2 is a peptide hormone that plays a role as physiological regulator of gastrointestinal and cardiovascular bioactivities mediated by the CALCRL-RAMPs receptor complexes. Activates the cAMP-dependent pathway through interaction with CALCRL-RAMP3 receptor complex.
Subcellular Localization:
Secreted.
Sequence:
MAQLLMVTVTLGCISLLYLLPGTLSGSLGKGLRHSRPREPPAKIPSSNLQPGHPSLQPVVWKSRRHAPQPQGRGNRALAMVHLPQGGGSRHPGPQRPTGSRRPHAQLLRVGCVLGTCQVQNLSHRLWQLVRPAGRRDSAPVDPSSPHSYG