lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional.
Miscellaneous:
MISCELLANEOUS: Due to the fact that PBP-1c can neither substitute for PBP-1a or PBP-1b, nor rescue a PBP-1a/PBP-1b double mutant, it is possible that PBP-1c has its own distinct function. Moreover it does not bind to most of the beta-lactams known to bind to other binding proteins, suggesting that the penicillin-binding domain must be different from those present in PBP-1a and PBP-1b. It may function as a transglycosylase only.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein.
Sequence:
MPRLLTKRGCWITLAAAPFLLFLAAWGADKLWPLPLHEVNPARVVVAQDGTPLWRFADADGIWRYPVTIEDVSPRYLEALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVARLLDPHPKTFGGKIRQLWRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYSEAAMLAVLPQAPSRLRPDRWPERAEAARNKVLERMAVQGVWSREQVKESREEPIWLAPRQMPQLAPLFSRMMLGKSKSDKITTTLDAGLQRRLEELAQNWKGRLPPRSSLAMIVVDHTDMRVRGWVGSVDLNDDSRFGHVDMVNSIRSPGSVLKPFVYGLALDEGLIHPASLLQDVPRRTGDYRPGNFDSGFHGPISMSEALVRSLNLPAVQVLEAYGPKRFAAKLRNVGLPLYLPNGAAPNLSLILGGAGAKLEDMAAAYTAFARHGKAGKLRLQPDDPLLERPLMSSGAAWIIRRIMADEAQPLPDSALPRVAPLAWKTGTSYGYRDAWAIGVNARYVIGIWTGRPDGTPVVGQFGFASAVPLLNQVNNILLSRSANLPEDPRPNSVTRGVICWPGGQSLPEGDGNCRRRLATWLLDGSQPPTLLLPEQEGINGIRFPIWLDENGKRVAADCPQARQEMINVWPLPLEPWLPASERRAVRLPPASTSCPPYGHDAQLPLQLTGVRDGAIIKRLPGAAEATLPLQSSGGAGERWWFLNGEPLTERGRNVTLHLTDKGDYQLLVMDDVGQIATVKFVMQ
The following text describes a protein:
Function:
Catalyzes the conversion of ribulose 5-phosphate (Ru5P) to 1-deoxy-D-xylulose 5-phosphate (DXP), providing a direct route from pentoses to terpenes. May play a role in biosynthesis of DXP under conditions of thiamine starvation.
Miscellaneous:
MISCELLANEOUS: Overexpression supports cell viability in the absence of the essential dxs-encoded 1-deoxy-D-xylulose-5-phosphate synthase. Overexpression confers resistance to the 4-amino-2-methyl 5-hydroxymethylpyrimidine (HMP) analogs bacimethrin and 4-amino-2-trifluoromethyl 5-hydroxymethylpyrimidine (CF(3)-HMP).
Sequence:
MQYNPLGKTDLRVSRLCLGCMTFGEPDRGNHAWTLPEESSRPIIKRALEGGINFFDTANSYSDGSSEEIVGRALRDFARREDVVVATKVFHRVGDLPEGLSRAQILRSIDDSLRRLGMDYVDILQIHRWDYNTPIEETLEALNDVVKAGKARYIGASSMHASQFAQALELQKQHGWAQFVSMQDHYNLIYREEEREMLPLCYQEGVAVIPWSPLARGRLTRPWGETTARLVSDEVGKNLYKESDENDAQIAERLTGVSEELGATRAQVALAWLLSKPGIAAPIIGTSREEQLDELLNAVDITLKPEQIAELETPYKPHPVVGFK
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Sequence:
MTVTLDHVTRTVDGVAHIRDVSLTLESGTLNVLLGPTLSGKTSIMRLLAGLDKPTTGKVLVNGKDVTGVDVRQRSVAMVYQQFINYPSFTVYENIASPLRVQGKPREEIEARVAEAAKLLRLEPFLKRTPLQLSGGQQQRTAMARALVKGADLVLLDEPLANLDYKLREELRAELPRIFEASGAIFVYATTEPTEALLLGGNTVCMWEGQALQIGETPSVYRRPQTLRVAQVFSDPPLNLVGIEKKNGSVQYAGGIAAPASGLYSALADGAYRVGFRAHQLALANGETDRHAFHATVTVTEITGSESFVHLTRDGSNWVAVLHGVHEFEPGQTIDAVLDPNDVFVFDAADRLVAAPNS
The following text describes a protein:
Function:
GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state (By similarity). Trans-acting factor necessary for meiotic distortion. Distortion is only seen in individuals that carry the RanGAP tandem duplication and express a RanGAP truncated protein. Binding of truncated RanGAP product to the Responder(RSP) locus initiates events that lead to sperm dysfunction. During oogenesis, plays a role in the biogenesis of annulate lamellae containing nuclear pore complex components.
Subcellular Localization:
Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Association to cytoplasmic side of the nuclear pore complex is promoted by Nup214. Co-localizes with Nup358/RanBP2 to annulate lamellae.
Sequence:
MSTFNFASMAAQLGQEQGISFENKVLSWNTAADVQDVVDALNKQTTVHYLNLDGNTLGVEAAKAIGEGLKRHPEFRKALWKNMFTGRLISEIPEALKHLGAALIVAGAKLTVLDLSDNALGPNGMRGLEELLRSPVCYSLQELLLCNCGLGPEGGSMLSRALIDLHANANKAGFPLQLRVFIGSRNRLEDAGATEMATAFQTLKTFEEIVLEQNSIYIEGVEALAESFKHNPHLRVLNMNDNTLKSEGAEKIAEALPFLPLLREMSFGDCLIKTNGAYHFGEALERGNERLEVIDLGFNEINSDGGLVLVNAMGNKPKLRILNLDGNSFGEEGSEKIISEMSKLPTAAALQPFQHQEEEDLEDEYQADKQDADYEEEEEVHEHANDTTEEADEDSEGDEDDEEDEGDEEYSNVAEETAYVTTNAYTTKLFNDTTNSMASETFAVANKTISQKCTPEKFCLSQKPCSQEDFDSLDMDNKLEALQSIVNQFTGDNHLLLLVFTTLKCAHLSQSSKAALDLAVSLYQATFDYAIKTKQETRVLNYVLMQLRLLPCKEVFHSDYDVKNCRFALREALKQPTFANDNIKNSFKTFLEGAES
The following text describes a protein:
Function:
May operate as a cation/H(+) antiporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MVDVTMNNNTISFPIFCQSIQQSHPVGIFNGGNPLAHSFSLIMFNLILNTLITRSLQVLLKPLKQPVIISQIIGGMIVGPSFLGQSRWFQRHMMTESTQFIMRNLGVMGFMFFLFMYGVRMDPTLLRKSGKLHVSTAFISITIPMVTAFVVALCMRKNMDKEMALIPSLGSISGYLGITAFPVLYHILKEFNLLNSDMGRSALSIALIGDSFGMLCIMAFEASSQGETKMINTLWYMISFVGLMAFLMFCVRPAMIWINNNTPEGHPVQQSFVVAIFLGALVMGFLTDMFGIAIANGPVFLGLVIPDGPRVGATIVQKTETIMADILLPFSFIMVGSYTDFYAMSASGWSSLEPLIVMVITGYVLKFFSTWIVLHFWRMPLREGLTLSLTLSLRGHIELILFVHWMDKNILHIPDFTLLVLMTTILTATFAPLINILYDPTKPYMVNQRRTIQHNPPDEELRIVLCILDTETINGFIRLLDISNPNSSSPLSISVVRLAELVARANPLFLDHEKQRVPPNYQWTNTINALTQHQQHKGMLMKLHFFTAVTPKQTMFRDICELALEQEASLIILPFKSSSDVHNHSVNSQVLNTAPCSVAIFVDKGLPDINNIGSSSTSFRRSQYRFAVLFLGGGDAREALVYADRMVANQDVSLTVIRFLSRNFKGYNEIEKKLDDGIVTWFWVKNEINQRVVYREVLVSNGEETIEEIQAMNDGAFDLLIVGRKHGINPILLTGLSEWSESDELGLIGDYVSSADFFGSASVLVVQQQILRG
The following text describes a protein:
Function:
High-affinity S-methylmethionine (SMM) permease, required for utilization of S-methylmethionine as a sulfur source.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Endoplasmic reticulum.
Sequence:
MDEFESTKLSKVQFSTSVLSTPSNEGNNLIHRFKNSFKRNDSPAIQEGLLYSELSEEEKIQWDLANQPYKKVLDQRHLTMIAIGGTLGTGLFIGLGESLASGPASLLIGFLLVGASMLCVVQCGAELSCQYPVSGSYALHASRFIDPSVGFSIGINYLLMWLISYPSELVGCSLTISYWAPSVNPAAWVAIAFVLSMLLNLFGARGFAESEFYMSIFKIVALFIFIIIGIVLIAGGGPDSTGYIGTKYWHDPGSFAVPVFKNLCNTFVSAAYSFSGTEMVVLTSTEARSVSSVSRAAKGTFWRIIIFYIVTVIIIGCLVPYNDPRLISGSSSEDITASPFVIALSNTGAMGTRVSHFMNAVILIAVFSVCNSCVYASSRLIQGLATAGQLPKICAYMDRNGRPLVGMAICGAFGLLGFLVVSKNQGTVFTWLFALCSISFFTTWFCICFCQVRFRMAMKAQGRSKDDIIYRSTLGIYGGIFGCILNVLLVIGEIYVSAAPVGSPSSAANFFEYCMSIPIMIAVYIGHRIYRRDWRHWYIKRMDIDLDSGHSLEDFEATKLERDEDKKYVSSKPLYYRIYRFFC
The following text describes a protein:
Function:
This enzyme has both lysozyme (acetylmuramidase) and diacetylmuramidase activities.
Subcellular Localization:
Secreted.
Sequence:
MVFHCLIFPFLLLSFLSIPAQSFSLNTSDLYTHECHGLTAGRTLLQARSGVPGMDVSSYQGNVDWPSAYNNVARFAYIKGTEGTGYPNPYFSQQYVGSYRAGFIRGAYHFGRPDISNGATQAMYFLTNGGRWSSDGQTLPGALDIEYNPSCGNSCNPLQTCYNLGKPEMRKWIQDFVNTSKQGTGVYPVIYSTADWYNTCVGTYGDFSSVCPFWLACYCPMVTTYPYNWKVYTFWQYADSGTFPGDQNVFNGPYSLLQKLAKG
The following text describes a protein:
Function:
Self-assembles to form a helical, filamentous nucleocapsid (Probable). Together with capsid protein 2, wraps arounds the DNA and maintains it in an A-form (Probable). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable).
Subcellular Localization:
Virion.
Sequence:
MSVEVYRQKIEKGGYSAAYEATRRYEREEIEVLSWSSRWESAWSKFGEAVKALGKIEGAPRALVIAKVQEALAYMSKPLPNMKLAMAAAVQAVRACEQLPGMNRERCLDAVAGALGVAKDWIRREMTGGGGGGGGGGGGGGGAVV
The following text describes a protein:
Function:
Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MVALFLTIAFSSIVAGFSKVMEVTQPVFTVVKSQGAANFQCGFTNTEDASKLRITLLKQEGNESVQICALSFPLEEGSLFKTNEDGIQCQIHPGRESVNITLWGLKATDAGLYVCQMEWIYPPPYYSVLGSGTQLFLLERDACPAVYPYFWISVMIASGLLGYSILITIYMKTKVLRKSMYFTPGIYEKIIPM
The following text describes a protein:
Function:
Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.
Sequence:
MVSGSKAGVSPHREIEVMRQSIDDHLAGLLPETDSQDIVSLAMREGVMAPGKRIRPLLMLLAARDLRYQGSMPTLLDLACAVELTHTASLMLDDMPCMDNAELRRGQPTTHKKFGESVAILASVGLLSKAFGLIAATGDLPGERRAQAVNELSTAVGVQGLVLGQFRDLNDAALDRTPDAILSTNHLKTGILFSAMLQIVAIASASSPSTRETLHAFALDFGQAFQLLDDLRDDHPETGKDRNKDAGKSTLVNRLGADAARQKLREHIDSADKHLTFACPQGGAIRQFMHLWFGHHLADWSPVMKIA
The following text describes a protein:
Function:
Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
Subcellular Localization:
Periplasm.
Sequence:
MKKLLCAVLLSPLLYSNAVLADDAKQLRETLTGTESLKADFKQTVTDVNKKVIQSGAGVFALAHPNQFYWHLTAPDESKIVADGKDLWIYNPFAEEVVIMDFTQAITASPIALLVHRDDATWSQYAVTKKQDCYEIKPKATDAGISAVNVCFNKGTLNKFNVLDDKGNLSQFDLSNQHSISTGDKALFKFVLPDNVDVDDQRIKTQ
The following text describes a protein:
Function:
Involved in DNA mismatch repair (MMR), correcting insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLbeta heterodimer, which probably forms a ternary complex with the MutSbeta heterodimer that initially recognizes the DNA mismatches. This complex is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in promoting meiotic crossing-over and is involved in maintaining the genetic stability of simple sequence repeats by correction of frameshift intermediates.
Subcellular Localization:
Nucleus.
Sequence:
MIDDSSLTAEMEEEESPATTIVPREPPKIQRLEESVVNRIAAGEVIQRPVSAVKELVENSLDADSSSISVVVKDGGLKLIQVSDDGHGIRREDLPILCERHTTSKLTKFEDLFSLSSMGFRGEALASMTYVAHVTVTTITKGQIHGYRVSYRDGVMEHEPKACAAVKGTQIMVENLFYNMIARRKTLQNSADDYGKIVDLLSRMAIHYNNVSFSCRKHGAVKADVHSVVSPSRLDSIRSVYGVSVAKNLMKVEVSSCDSSGCTFDMEGFISNSNYVAKKTILVLFINDRLVECSALKRAIEIVYAATLPKASKPFVYMSINLPREHVDINIHPTKKEVSLLNQEIIIEMIQSEVEVKLRNANDTRTFQEQKVEYIQSTLTSQKSDSPVSQKPSGQKTQKVPVNKMVRTDSSDPAGRLHAFLQPKPQSLPDKVSSLSVVRSSVRQRRNPKETADLSSVQELIAGVDSCCHPGMLETVRNCTYVGMADDVFALVQYNTHLYLANVVNLSKELMYQQTLRRFAHFNAIQLSDPAPLSELILLALKEEDLDPGNDTKDDLKERIAEMNTELLKEKAEMLEEYFSVHIDSSANLSRLPVILDQYTPDMDRVPEFLLCLGNDVEWEDEKSCFQGVSAAIGNFYAMHPPLLPNPSGDGIQFYSKRGESSQEKSDLEGNVDMEDNLDQDLLSDAENAWAQREWSIQHVLFPSMRLFLKPPASMASNGTFVKVASLEKLYKIFERC
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MLYELVGIASVTPAHAAAKQAVTQIGRMIIGNRGVVRLIECWRFKPLPQIMKAQQKSYVVGDYFYMKFDCSPGAQGEIMRAVQADPRLIRTFCVKLNEKSSKTLI
The following text describes a protein:
Function:
General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. Binds single-stranded DNA (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSSSSSSEDELEKKVTKEQKKKETKSKKRQSEAVEEEKQEVKKAKNEEEVSGRLKDSDGNEMFEIGNLRYATVSKFKGKEYVNIREYYIDRDSQKMMPSRKGISLSKAQWANLKDLIPEIDKKF
The following text describes a protein:
Function:
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
Sequence:
MPRAHDDNWDLASSVGATATMVAAGRALATKDPRGLINDPFAEPLVRAVGLDFFTKLIDGELDIATTGNLSPGRAQAMIDGIAVRTKYFDDYFRTATDGGVRQVVILAAGLDARAYRLPWPAGTVVYEIDQPQVIDFKTTTLAGIGAKPTAIRRTVYIDLRADWPAALQAAGLDSTAPTAWLAEGMLIYLPPDPRTGCSTTAPNSVLRAARSLPNLSRALWISTQAGYEKWRIRFASTAWTSTWRRWCIPANAATSSTTCAPRAGTLRAQCGPTYSGAMVCPFPPHTTTIRSAKSSSSAVV
The following text describes a protein:
Function:
Binds tetrapyrroles and promotes the photooxidative degradation of protoporphyrin IX. Can bind the benzodiazepine receptor agonist PK-11195 (in vitro); this interferes with photooxidative tetrapyrrole degradation. May play a role in the transmembrane transport of tetrapyrroles and similar compounds (By similarity).
Subcellular Localization:
Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MNKQILTLALCIGLCLAVGFAGSTFTPKPASWYYTTLVKPSWNPPDWLFPPVWTILFIMMGTALAKVLGTGWKKNEVNVGVVLFAIQLMLNLGWSASFFGMQSPLAGLVDIVLLWIFIVLTMLAFARVSKPASLLLVPYLCWVSFASYLNFTILQLNP
The following text describes a protein:
Function:
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Sequence:
MSSHKQEPLEENVDQLTQFRERCAEHVTEFKAILDECNDRVNSRSETEETCHQEMADYVHHLDHCAMPKAFASLK
The following text describes a protein:
Function:
Enhances the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic reticulum by displacing ATP2A1/SERCA1 inhibitors, thereby acting as a key regulator of skeletal muscle activity. Also enhances the activity of the ATP2A2/SERCA2 ATPase (By similarity). Does not directly stimulate SERCA pump activity. Binds preferentially to the phosphorylated E1 and E2 conformational forms of ATP2A2 which predominate at high Ca(2+) concentrations during the systolic phase of the cardiac cycle. Competes with ATP2A2 inhibitor phospholamban (PLN) for binding to ATP2A2 and displaces PLN (By similarity). Can activate ATP2A2 directly in the absence of PLN (By similarity). Also enhances sarcoplasmic reticulum Ca(2+) uptake and myocyte contractility by displacing the SERCA inhibitory peptides sarcolipin (SLN) and myoregulin (MRLN).
Subcellular Localization:
Sarcoplasmic reticulum membrane; Single-pass membrane protein.
Domain:
The transmembrane domain is sufficient to compete with phospholamban (PLN) for binding to ATP2A2.
Sequence:
MAEKESTSPHLIVPILLLVGWIVGCIIVIYIVFF
The following text describes a protein:
Function:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. 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. In the lumen of the endoplasmic reticulum, adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MMDALRVLLETSTFNEVLRGLAISILLAKLTQSTTSSSKSQGSTFITASGFILIYFFARSWLALVNHYAPEPYLDEVFHIPQAQTYCEGRYHEWDNKITTPPGLYLLSVGWHKLVRLVECTPSSLRSNNLVATLLIALIALSCRRRIEAQTAVGIEKSAVSFYAYHTAINIALFPVIFFFSGLYYTDVASTLVMLVAYWNHLNRVASHSEKPGFLNGLWTVVLGVAALFMRQTNVFWVVVYMGGLEAAHVVKGLKPKPVSKNDTPDFVLENIRDSFGFWLRRYAVGDVHDPPVDMAWPDDWALCLLSIGIAALCNPLRVLRQVWPHITIMGLFAGFVAWNGGVVLGDKSNHIATIHLPQMLYIWPFFAFFSAPLLIPRVLSTLADLITHARTPTPSHTTTKDPGRSSWRFTKPSITSKKSSTTKPPQRSGPTPASSSSSSSSFSPDTNSSGRGFRFILDLVLSRKLYYPFYLLATILLSAAIIHYNTIIHPFTLADNRHYMFYIFRYTILRSSLVRLALVAAYTLSRWLIWKRLEGNNPPLRDLAGETGLKITKNKLGWRDEFSASPFVTQDFYGPKTIKTDEQKNIKDKQKEVEEEEEEEEKEDWLIGGAYTTLSLSSTQPSPATSSPPTSTVLLWLLTTTLSLVTAPLVEPRYFILPWVFYRLLVPAMPVSSSLVSSSSSSSFASSTTESGNGDGNDAATAARQQQNGNGKRGLLWNIIRRTDAALALETVWFLAINIGTMYMFLFKPFYWKTASGEMLDGGRLQRFMW
The following text describes a protein:
Function:
Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase (By similarity).
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MAMETCFRAWALHAPAGSKDRLLVGNLVLPSKRALAPLSVGRVATRRPRHVCQSKNAVDEVVVADEKNWDGLVMACETPVLVEFWAPWCGPCRMIAPVIDELAKDYAGKITCCKVNTDDSPNVASTYGIRSIPTVLIFKGGEKKESVIGAVPKSTLTTLIDKYIGSS
The following text describes a protein:
Function:
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE
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.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MPLVRVEVRNVYGLGKTELHRDVDREDPKAVLNGVAVSGLVGILRQLGDLTEFATEIFHGIQEEVILTSSRSNKLKMRLKQIETTVPSIQKAVLEQPNHIQFAYTGGLEWHPRIPNVQDYFVYDDLPQFIMAPYDDCRDPPRLQLLDKFDINGPGSCLKRYTDPTHFKRSSRASKHPVIKKKKSLPRSRDVSRVASMANQSDRKTLTSLSFSGRTSSSKTASTVETESKSDLQDHRSCSFDSRSGGEKLKGVYTPSRFTPGPRTIASVLSESESESEDATDDSPSQDLTPRGSSCVSWREKAEIVEADTLKLETDEAPEVMETNAELESGLKEHRVVETVQDITPRVVEMDSEDETESEEDDFVDALYTIDSESDNDQEVQKQISNEITEEEFDNYVCEKETENVSNSFGLEDEAMCAAASELHLSSPVSKPDEMIHQDPWEDLDMSNGTTHSYSNGFSNPLYDTNGVQEHQESEDESSCDNEEGTQLWTNGNLLGLKPSKPEIEEETIKETDAEALQEQPLREAHKADFDWFTSSPQLDHMKISFTPSETLPSSELKLKLPDEYTFSSFQLVPETGGGTSLPDSDSDKDTFCRTSSYVSDNSDNQSVSISEQQSDDERKSQQELYDDSFHRINTEASSLSAPSSQFETSNGYLAGKISYLQNPAEPLPPPLPPLQWMVSKVPSGRFEDNNKQSFKDTLTRALEQRSSLSTVKKEESNNVTAYDPKPDNNKQSFKETLTRALEQRSYLSTVKKEEPNNIITYDPKPDNNKQSFKDTLTRALEQRSSLSMIKKEESNSVIAYDTKPENNVRDYKQSHGNVKETEAGDFLHQIRTKQFTLRRVVTTKASSSEATMNTNFSVILEKANSIRQAVANDDGDGESDTWSDSDT
The following text describes a protein:
Function:
Competitive inhibitor of the HD-ZIPIII transcription factors in shoot apical meristem (SAM) development. Acts by forming non-functional heterodimers. Part of a negative feedback loop. Essential for proper functioning of stem cells in the SAM.
Sequence:
MQREHKTHNKLSFIYITPLYISPINQTRLTYLSSSFLLSSSSKMCLSSSETFSDTPTRLVLYLKTQSHVRIPRLSRRRRMWREEKKMEMINLKLYVENQNIIRENEKLKKKALLLHQENKTLFSLLQTKKLSSVHK
The following text describes a protein:
Function:
Transcription factor involved in male gametophyte development.
Subcellular Localization:
Nucleus.
Sequence:
MIPNDDDDANSMKNYPLNDDDANSMKNYPLNDDDANSMENYPLRSIPTELSHTCSLIPPSLPNPSEAAADMSFNSELNQIMARPCDMLPANGGAVGHNPFLEPGFNCPETTDWIPSPLPHIYFPSGSPNLIMEDGVIDEIHKQSDLPLWYDDLITTDEDPLMSSILGDLLLDTNFNSASKVQQPSMQSQIQQPQAVLQQPSSCVELRPLDRTVSSNSNNNSNSNNAAAAAKGRMRWTPELHEVFVDAVNQLGGSNEATPKGVLKHMKVEGLTIFHVKSHLQKYRTAKYIPVPSEGSPEARLTPLEQITSDDTKRGIDITETLRIQMEHQKKLHEQLESLRTMQLRIEEQGKALLMMIEKQNMGFGGPEQGEKTSAKTPENGSEESESPRPKRPRNEE
The following text describes a protein:
Function:
Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex.
Subcellular Localization:
Nucleus. Chromosome, centromere. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex.
Sequence:
MDSYSAPESTPSASSRPEDYFIGATPLQKRLESVRKQSSFILTPPRRKIPQCSQLQEDVDPQKVAFLLHKQWTLYSLTPLYKFSYSNLKEYSRLLNAFIVAEKQKGLAVEVGEDFNIKVIFSTLLGMKGTQRDPEAFLVQIVSKSQLPSENREGKVLWTGWFCCVFGDSLLETVSEDFTCLPLFLANGAESNTAIIGTWFQKTFDCYFSPLAINAFNLSWMAAMWTACKMDHYVATTEFLWSVPCSPQSLDISFAIHPEDAKALWDSVHKTPGEVTQEEVDLFMDCLYSHFHRHFKIHLSATRLVRVSTSVASAHTDGKIKILCHKYLIGVLAYLTELAIFQIE
The following text describes a protein:
Function:
Plant type III polyketide synthases (PKSs) that catalyzes the condensation of malonyl-CoA units with various CoA ester starter molecules to generate a diverse array of natural products including long-chain alkyl alpha-pyrones. Accepts up to C(20) chain-length fatty acyl CoAs as starter substrates, and carries out sequential condensations with malonyl-CoA to produce triketide and tetraketide alpha-pyrones, potential sporopollenin precursors. Favorite substrates for are midchain- and v-hydroxylated fatty acyl-CoAs (e.g. 12-hydroxyoctadecanoyl-CoA and 16-hydroxyhexadecanoyl-CoA). Required for pollen development and sporopollenin biosynthesis, the major constituent of exine in the outer pollen wall. In vitro, can use 4-coumaroyl-coenzyme A as substrate to produce bis-noryangonin and fatty acyl-coenzyme A as substrate to produce medium-chain alkyl pyrones. May play a role in both the synthesis of pollen fatty acids and phenolics found in exine.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MGSIDAAVLGSEKKSNPGKATILALGKAFPHQLVMQEYLVDGYFKTTKCDDPELKQKLTRLCKTTTVKTRYVVMSEEILKKYPELAIEGGSTVTQRLDICNDAVTEMAVEASRACIKNWGRSISDITHVVYVSSSEARLPGGDLYLAKGLGLSPDTHRVLLYFVGCSGGVAGLRVAKDIAENNPGSRVLLATSETTIIGFKPPSVDRPYDLVGVALFGDGAGAMIIGSDPDPICEKPLFELHTAIQNFLPETEKTIDGRLTEQGINFKLSRELPQIIEDNVENFCKKLIGKAGLAHKNYNQMFWAVHPGGPAILNRIEKRLNLSPEKLSPSRRALMDYGNASSNSIVYVLEYMLEESKKVRNMNEEENEWGLILAFGPGVTFEGIIARNLDV
The following text describes a protein:
Function:
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Sequence:
MKPLKGCPVAKDVRVAIVGSCFNSPIADRLVAGAQETFFDFGGDPSSLTIVRVPGAFEIPCAIKKLLSTSGQFHAVVACGVLIQGETSHYEHIADSVAAGVSRLSLDFCLPITFSVITAPNMEAAWERAGIKGPNLGASGMKTALEMASLFSLIGKE
The following text describes a protein:
Function:
Binds to WNT proteins and inhibits their activities. May be involved in mesoderm segmentation.
Subcellular Localization:
Secreted.
Sequence:
MERRNRQQQQDKDDLSLWIDQQQVKMFSGFPMEIYIAAEGRVLSYILDPNFEKYLPVIPSEVGYVNFTWKSGEHKKYYYHFDRLQSFNEDILQPPTVSVEIRGRVPRKPKVFSVLLPCSGNSSGVASFSIGLLIESHKGKPLPGTPLRLRLRKECAERGPDPECDKKCANGGWCNHEKICQCLEGYMGQHCRTALCYPQCMNGGSCTSPGMCSCPSGFQGRHCEGGICKDKCLNGGKCIQKDTCDCPKGFYGLRCEFTKCVIPCLNGGRCKGVNKCRCSPGFKGDHCEVTPPGRLAQRHLCQRPCRHGTCVGQNRCLCHEGWHGKLCHRSMTNEC