lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability.
Subcellular Localization:
Nucleus.
Sequence:
MNTPGFVNRAKAWLQSAWHIQVPFHWLEACINWIQQDNAGTVLTQAEINKQVLEQWLLTDLRDLEQPILPRGISEAAKVEINGFYCLQIDSLLDVSQPAYSQIQKLKGKDFTNENVTAVTQVSQKPWEAKPLRMLMLQLTDGVQQLQGMEYQPIPDLHANLSPGSKILLQGKIVCRLGVLLLTPLNVKVIGGEVEGLVEEFSQERVLSRVLGETENAVQRPSSQDREMPNVDEGFENLTSPSGEELLASIETVDQLAMSNVVGHDSGYGSRSEVSSVLTRNSTLQSYHSGLSVPESQTTQMVPERASEEVLELDDADFDDIPVDDLDDVIYLEDSPPEFETPSTEQSFLCNQMTMSGNSNINSRNVPSTLNLTNNMVEVPENVSGERIVSIRPQIRTMTNDGNSIEVPELLEGSLTVPVEMSKLRSVCESSAIPSHSASGVNIKPVVKCQSFENWQLGSAVHYESCEEEESVPLQTDVNFQPEMKVDLNSCPFSYLSVLLGEKTAIVKVVKVKAFIVTLLGSLSSSSGSWHIKVKISDGTDYLDVDLSNEVLVSLIGFTVEETKKMKKDPDQRKRVTAGLQKCQQELIDLCCIMTIEYDPCNSKAVLLGLQDVTLEDYNNLEKRLQN
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Subcellular Localization:
Membrane. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Sequence:
MSIEIDWLSLTPSIAEKLTERLNGLLANLSTPDFLGPLRIQSIDFGDIAPEVEIVDIRDVSRGFRIADGESHPSSSPECSSAPTIKPDEDGHSQPSLQIHLRLTYDGNLRLRFSTALVLNHPAAEFMSLPLRATVVGVGFDAEIILAIEGDRSKFHLSLLEPPHSELPLYEDSVENGGKRNSSIGARILPHLFVETEVGNADRHVLRNVGKVERFLTETIRSLICEEFLYPTFQTFEWD
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:
MEDVENMDVDMDDLFGDGAGLSLPSRPPPSKELHQRIDELRGSGCCQGIAWSKWGSIASIAPNGNGLELRNLRCHPTDGTWGLSKPTLIPQLTNNLDGGPLKHLSWSPTGSELAVIDSAGRHGPAVKEASGFRYDASQAPILGPSHPIPSKSAFLYVTSNGSLRLLWQQGNNKWFESHTELESIVSSDDLITHAAICAERTPSLLIALATGSKQLRIIRAGIDWGMPQTQEKVNQMTLSLNASLRIKPLTVTSWMHDVPGDTLNPSHLESSMVQLSHLKFLSPCIDSKNHMTPPIVMAVRSYLPGPTSHYNQEVYSTVDRWEFRERNQQPVHSAFEHLSSRKGTDGPQSTKPVYTAQLKKLESFTVNKIVVAMQTIYIGRVICFAYSDSSVDYRDRITMNETFNDGDLDRVSHLSQIGFSYTEDEPCLQVVLSPSTCSLAQITNDGKVKWKQLDYHLGEIGSSMEDPRYAAMITALSTSCSTSVMIFINYDDIIATAHSFAKTKDNLAYDWLNELAKILKITVDYSEEAHYDVLIRNTTIQLCLSIQNSLGFRGDFNPRKFAGKFSWLVLQLRNIVVLVTMAANMKVPGPTHDKTSTPLDDPEVISALAGSVRWVLDLMAWIIDTLLDLPSSLPGELSLTDPAKLSLPDLLAHLHTQNNVTLHLLLSSPTRGFLTAICRRLQHLDYVARKAIATNTNAQNQPGGQGQQSISPALRSSYVQIAQLTSNCIVRIKTFETLLSSLTLSVKSAYASHKPPLPVNNSSGPSRNGLEMKMLFGGEIPTAFKPVIIDLFKGVQDNKKSNESNTAPDNAGTGHLSAVRLEIEPSDLWFADFTMLEVEEEEECVARRKNSGLTMDCFRKTWLSNPPPSSSKSSSTKNASSSAAAVSGDNHLAPIPGFAAFGLATPGTAGNGNANANANANANAVTTMTKRWRRCARCAAVMEDVLSQRPTLQWLVMQQRRCFCSGYWDTLQQGEMAA
The following text describes a protein:
Function:
Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Mediates Notch-induced ubiquitination and degradation of substrates including TCF3/E2A and JAK2. Required during embryonic heart development for complete heart looping (By similarity). Required for cardiomyocyte differentiation. Specifically promotes the ubiquitination of SMAD9 and targets it for proteasomal degradation, leading to avoid excessive accumulation of SMAD9. Plays a role in the regulation of NK-cell migration by modulating protein levels of filamin A/FLNA via regulation of its ubiquitination and proteasome degradation (By similarity); [Isoform 1]: Involved in myogenic differentiation and targets filamin FLNB for proteasomal degradation but not filamin FLNA. Also targets DES for proteasomal degradation (By similarity). Acts as a negative regulator of skeletal muscle mass (By similarity); [Isoform 2]: Targets filamins FLNA and FLNB for proteasomal degradation. This leads to enhanced adhesion of hematopoietic cells to fibronectin. Required for FLNA degradation in immature cardiomyocytes which is necessary for actin cytoskeleton remodeling, leading to proper organization of myofibrils and function of mature cardiomyocytes (By similarity). Required for degradation of FLNA and FLNB in immature dendritic cells (DC) which enhances immature DC migration by promoting DC podosome formation and DC-mediated degradation of the extracellular matrix (By similarity). Does not promote proteasomal degradation of tyrosine-protein kinases JAK1 or JAK2 in hematopoietic cells.
Subcellular Localization:
Cytoplasm, cytoskeleton, stress fiber; [Isoform 1]: Cytoplasm, myofibril, sarcomere, Z line. Note=Localizes to the Z line in cardiomyocytes.
Domain:
The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes; [Isoform 2]: Both the N-terminus and ANK repeats 1 to 10 are necessary for interaction with filamins; [Isoform 1]: The UIM domain is required for monoubiquitination.
Sequence:
MATQISTRGSQCTIGQEEYSLYSSLSEDELVQMAIEQSLADKTRGPTTAEATASACTNRQPAHFYPWTRSTAPPESSPARAPMGLFQGVMQKYSSSLFKTSQLAPADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRSGVSPLHLAAERNHDEVLEALLSARFDVNTPLAPERARLYEDRRSSALYFAVVNNNVYATELLLQHGADPNRDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFAMKCLSLLKFLMDLGCDGEPCFSCLYGNGPHPPAPQPSSRFNDAPAADKEPSVVQFCEFVSAPEVSRWAGPIIDVLLDYVGNVQLCSRLKEHIDSFEDWAVIKEKAEPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ
The following text describes a protein:
Function:
May be a specific regulator of miRNA biogenesis. Binds to microRNAs MIR7-1, MIR16-2 and MIR29A hairpins recognizing the 3'-ATA(A/T)-5' motif in the apical loop.
Subcellular Localization:
Nucleus.
Sequence:
MSNVSEERRKRQQNIKEGLQFIQSPLSYPGTQEQYAVYLRALVRNLFNEGNDVYREHDWNNSISQYTEALNIADYAKSEEILIPKEIIEKLYINRIACYSNMGFHDKVLEDCNIVLSLNASNCKALYRKSKALSDLGRYKKAYDAVAKCSLAVPQDEHVIKLTQELAQKLGFKIRKAYVRAELSLKSVPGDGATKALNHSVEDIEPDLLTPRQEAVPVVSLPAPSFSHEVGSELASVPVMPLTSILPLQVEESALPSAVLANGGKMPFTMPEAFLDDGDMVLGDELDDLLDSAPETNETVMPSALVRGPLQTASVSPSMPFSASLLGTLPIGARYAPPPSFSEFYPPLTSSLEDFCSSLNSFSMSESKRDLSTSTSREGTPLNNSNSSLLLMNGPGSLFASENFLGISSQPRNDFGNFFGSAVTKPSSSVTPRHPLEGTHELRQACQICFVKSGPKLMDFTYHANIDHKCKKDILIGRIKNVEDKSWKKIRPRPTKTNYEGPYYICKDVAAEEECRYSGHCTFAYCQEEIDVWTLERKGAFSREAFFGGNGKINLTVFKLLQEHLGEFIFLCEKCFDHKPRMISKRNKDNSTACSHPVTKHEFEDNKCLVHILRETTVKYSKIRSFHGQCQLDLCRHEVRYGCLREDECFYAHSLVELKVWIMQNETGISHDAIAQESKRYWQNLEANVPGAQVLGNQIMPGFLNMKIKFVCAQCLRNGQVIEPDKNRKYCSAKARHSWTKDRRAMRVMSIERKKWMNIRPLPTKKQMPLQFDLCNHIASGKKCQYVGNCSFAHSPEEREVWTYMKENGIQDMEQFYELWLKSQKNEKSEDIASQSNKENGKQIHMPTDYAEVTVDFHCWMCGKNCNSEKQWQGHISSEKHKEKVFHTEDDQYCWQHRFPTGYFSICDRYMNGTCPEGNSCKFAHGNAELHEWEERRDALKMKLNKARKDHLIGPNDNDFGKYSFLFKDLN
The following text describes a protein:
Function:
Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici; Promotes hydrogen peroxide H(2)O(2) production and cell death.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MRSRVTGTYFLALQFFLSFNFNIARVSPLSFKLNFTESNNNALAAIQFQDDAFYNKAIRLTKDELNNDITYSVGRAVYTDPVPLWDSATGQLADFTTRFTFMIAATDRSNSTGEGLAFFLSPYPSVIPNSSTDGFLGLFSNSNGQNDPSNELVAVEFDSHKNTWDPDDNHVGIDIHSIVSVANRTWISSINDGRIANAWVTYQASSMNLSVFLTYLDNPQHSGNSSLSYSVDLRKYLPDKVAIGFSAATGRSVELHQILYWEFDSTDLQLMKTEKTRSILAISLGTSISVVVCSMGLVWYLLHFRSRRSKKEREKKLDYNVSIDCEFEKGRGPRRFRYNELVGATKNFVLERKLGEGGFGAVYQGFLKDQNLDVAIKRVAKGSTQGRKEYISEVKIISQLRHRNLVQLEGWCHERGEFLLVYEFMPNRSLDTHLYDNSNLLTWPLRFKVTIGVASALLYLHEEWEQCVVHRDVKPSNVMLDSAFNAKLGDFGLARLVDHDRASQTTVLAGTMGYMAPECVTTGKASKESDVYSFGILALEIACGRRPVVLKEEDNKIRLVQWVWDLYGRNEILNAVDGRLDGAFEEREVLCLMVVGLWCAHPDYNLRPSIRQVISVLKFEAPLPSLPAKMPVAMYFAPPISLCRFSYTSSDGTLKEQELERSNGYGKTNSSSATNASSSPPSVRLPEAGY
The following text describes a protein:
Function:
L-Ala--D-Glu endopeptidase involved in production of single L-alanine side chains from tetrapeptides in the spore cortex peptidoglycan. Therefore, is required for the endospore cortex maturation.
Miscellaneous:
MISCELLANEOUS: The presence of single L-alanine residues in the spore cortex increases the spores ability to be resistant to heat.
Sequence:
MKVLLSALLLLLFAFEPSASGKKLSDPVLSKRMELYHKIEAVTQIPWYALAAVDQYEENVRSNRKDLPEKAGIISIYIPDDIWSGPENPNPKDDAPLSIKVFDGIGMDGDGDGKAEVSNDEDILYTFSQYLLSYGTDEDNIRIGLWNYYRRDQTVGIISEFMKLFKAYGHIDLGEHAFPLPIRTDYSYRSTWGDARGFGGRRIHEGTDIFAHYGLPVKSTCYGVVEMKGWNRFGGWRIGIRDINNTYHYFAHLNGFAKGIKTGQIVEPGQVIGSVGSSGYGPPGTAGKFPPHLHYGMYKDNGRTEWSFDPYPHLRAWERYEYQKKK
The following text describes a protein:
Function:
Participates in bacterial attachment to several surfaces, including various extracellular matrix (ECM) components and a hydrophobic abiotic surface. Involved in adhesion to host epithelial cells and is required for full virulence in mice. Also implicated in the resistance to porcine serum.
Subcellular Localization:
Cell surface. Cell outer membrane. Note=The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface (By similarity). Localizes at the new cell pole generated after cell division.
Domain:
The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface.
Sequence:
MKLPPVFVFELVENQGLANIALIRPRVIAPDNNLRPGGIVSGIAGLLTLGQENRNLISENRQVINNNTTAIGQNSDRIDANAKGVADNRAAIGQNSGRIDANAKGVADNKAAIGRNSGRIDANAKGVADNKTAIGRNSGRIDTNAKGVADNRAAISQNRGRINANAAGVASNRAAIRQNSAAISALGQRVDGLQGQINSARKEARAGAANAAALSGLRYDNRPGKVSIATGVGGFKGSTALAAGIGYTSKNENARYNVSVAYNEAGTSWNAGASFTLN
The following text describes a protein:
Function:
Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
Sequence:
MTAAQADLQIDRPRVADGAALWRIARDSEVLDLNSSYSYLLWCRDFAATSAVVRDGHGVPVGFITGYVRPDSPDTLLVWQVAVDGTYRGRGLAATLVDGLADRVARERGITILETTISPDNTASQRLFTSFAERRGARLEREVLFDTAVFPDGPHEPEVLYRIGPLSAGG
The following text describes a protein:
Function:
Male-specific histone demethylase that catalyzes trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3. Has relatively low lysine demethylase activity.
Subcellular Localization:
Nucleus.
Sequence:
MKSCGVSLTTAAVAFGDEAKKMAAGKASREGEEEPLSLTVEEREALGDMDSRLFGFVRLHEDGARTKTLLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAKEIHLRLGLMFKVNTDYKSSLKHFQLALIDCNPCTLSSAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLPAQVKATVLQQLGWMHHNMDLVGDKATKESYAIPYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFVSYRQSIDRSEASADTWCSIGVLYQQQNQPIDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAARSKRCSNTSTLAARIKFLQNGSDNWNGGQSLSHHPVQQVYSLCLTPQKLQHLEQLRANRDNLNPAQKHQLEQLESQFVLMQQMRHKEVAQVRTTGIHNGAIADSSLPTNSVSNRQPHAALTRVSSVSQPGVRPACVEKLLSNGAFSAGCIPCGTSKILGSTDTILLGSNCIAGSESNGNVPYLQQNTHTLPHSHTDLNSSTEEPWRKQLSNSTQGLHKSQSSCLSGPNEEQPLFSTGSAQYHQATSTGIKKSNEHLTLPSNSVPQGDADSHLSSHTATSGGQQGIMFTKESKPSKNRSLVPETSRHTGDPSNGCADVKGLSNHVHQLIADAVSSPNHGDSPNLLIADNPQLSALLIGKANGNVGTGTCDKVNNIHPAVHTKTDHSVASSPSSAISTATPSPKSTEQRSINSVTSLNSPHSGLHTVNGEGLGNSQSSTKVDLPLVSHRSTSQIIPSMSVSICPSSTEVLKACRNPGKNGLSNSCILLDKCPPPRPPTSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPKNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHIVEVRTQLLQPADENWDPTGTKKIWRCESNRSHTTIAKYAQYQASSFQESLRAGMQWCDLSSLQPPPPGFKRFSHLSLPNSWNYRHLPSCPTNFCIFVETGFHHVGQAHLELLTSGGLLASASQSAGITGVSHHAR
The following text describes a protein:
Function:
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Subcellular Localization:
Nucleus. Mitochondrion.
Sequence:
MSTSAYFRPVTRSQAAQSGSKFADLKARAQALQTTRSRGGKSTPTAQGGPSSSADPTGPSQKKTAQKRVKREHTKIEYEAEAEGDAKGSSSSAKPRTTHSIKKERWEPERWREQLENIKRMRAARDAPVDSMGCQTCPDKNAAPEVKRYHALISLMLSSQTKDQMTSAAMKRLIDHGLTVDNILKTSDQKLGELIYPVGFWKTKVKYIKNTTQMXKDQYGGDIPATVAEMXQVPGVGPKMAYLTMDVGWGKVEGICVDTHVHRISNRLGWLKKPTKVPEDTRMALEEWLPREHWSELNWLLVGFGQQTCLPVGAKCSGCLNKEICPFGKSQLRYSKNKKSPKK
The following text describes a protein:
Function:
Subunit b, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Part of the complex F(0) domain. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MAALRALQPLRSAAQAGPVSVLASRGLKISTPQQSALLESKTGKTGAAVLGFGLAAYLASKEILILHSETVVVASIAAVTYGLMSKAGKDIASGLDERAQAIQEGLEKGRVARIAAIEKEIAQQEQLKASVSNLQEIYDVNRELASATRELAYRTELHAARDNALANLKDMVAIEQSQRQAEQNEIANWIEAEVLKALEGKEEALMKQSIADLEDLAKAQA
The following text describes a protein:
Function:
Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Note=Imported into the mitochondria via the mitochondrial mia40-erv1 machinery.
Domain:
The twin Cx9C motifs are involved in the recognition by the mitochondrial mia40-erv1 disulfide relay system and the subsequent transfer of disulfide bonds by dithiol/disulfide exchange reactions to the newly imported protein.
Sequence:
MNKSPIEEEFDLRKQHQKLLKKNCQKEIEDFVKCATGRTFSVTWKCRSENKTMKDCLTKAADEISEWQIRSEYNKAKQESFIGKQDEKK
The following text describes a protein:
Function:
Involved in regulation of circadian rhythm, and in the control of the photoperiodic flowering. Acts as a suppressor of flowering under short-day (SD) and long-day (LD) conditions. Activates Hd1/CONSTANS gene.
Subcellular Localization:
Nucleus.
Sequence:
MSASNEKWIDGLQFSSLFWPPPQDSQQKQAQILAYVEYFGQFTADSEQFPEDIAQLIQSCYPSKEKRLVDEVLATFVLHHPEHGHAVVHPILSRIIDGTLSYDRNGFPFMSFISLFSHTSEKEYSEQWALACGEILRVLTHYNRPIFKVDHQHSEAECSSTSDQASSCESMEKRANGSPRNEPDRKPLRPLSPWITDILLAAPLGIRSDYFRWCGGVMGKYAAGGELKPPTTAYSRGSGKHPQLMPSTPRWAVANGAGVILSVCDEEVARYETANLTAAAVPALLLPPPTTPLDEHLVAGLPPLEPYARLFHRYYAIATPSATQRLLFGLLEAPPSWAPDALDAAVQLVELLRAAEDYDSGMRLPKNWMHLHFLRAIGTAMSMRAGIAADTSAALLFRILSQPTLLFPPLRHAEGVELHHEPLGGYVSSYKRQLEVPASEATIDATAQGIASMLCAHGPDVEWRICTIWEAAYGLLPLSSSAVDLPEIVVAAPLQPPTLSWSLYLPLLKVFEYLPRGSPSEACLMRIFVATVEAILRRTFPSETSEQSRKPRSQSKNLAVAELRTMIHSLFVESCASMDLASRLLFVVLTVCVSHQALPGGSKRPTGSDNHSSEEVTNDSRLTNGRNRCKKRQGPVATFDSYVLAAVCALSCELQLFPFISKNGNHSNLKDSIKIVIPGKTTGISNELHNSISSAILHTRRILGILEALFSLKPSSVGTSWSYSSNEIVAAAMVAAHVSELFRRSRPCLNALSALKQCKWDAEISTRASSLYHLIDLHGKTVTSIVNKAEPLEAHLTLTPVKKDEPPIEEKNINSSDGGALEKKDASRSHRKNGFARPLLKCAEDVILNGDVASTSGKAIASLQVEASDLANFLTMDRNGGYRGSQTLLRSVLSEKQELCFSVVSLLWQKLIASPEMQMSAESTSAHQGWRKVVDALCDIVSASPTKASAAIVLQAEKDLQPWIARDDEQGQKMWRVNQRIVKLIAELMRNHDSPEALVILASASDLLLRATDGMLVDGEACTLPQLELLEVTARAVHLIVEWGDSGVSVADGLSNLLKCRLSTTIRCLSHPSAHVRALSMSVLRDILNSGQINSSKLIQGEHRNGIQSPTYQCLAASIINWQADVERCIEWEAHSRRATGLTLAFLTAAAKELGCPLTC
The following text describes a protein:
Function:
Transcriptional activator of the nitrous-oxide reductase gene NosZ.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MRALRFSAGSWRCVFAWMLLLVGLAAQGAELSELERLRIAQVFPAVERIGDPEGDYGVRRLSKGEETLGYAFQTLSVTDIPAYSGKPINLQVILDPQAVIRDAYVLEHHEPILLIGIPEEKLHAFSARYDGVRADQRVVVGRSSDPQAVTVDAVSGATVTVMVVNEIVMRAAHTVAVALGLIEDRGNVRPKPAQVRQQPAATASWSELLGNGAIRRLQLSRGQIDDAFKGSEAEGIGEADAAHRDEPFIDLYSALLNPPAVGRSLLGDNQYRELMASLKPGEYAFVVLGDGEYSFKGSGYVRGGIFDRVQLRQFGDIISFRDLDYQRLSDVYAEGMPEFREMAIFVARASQRFDPGSPWTLELLVRRQTGPVAGVFTSFELACQTPEEYLERPQPTAEELAALEEAARPLWLRVWYQKSFQVGVLCTALVLLLAILFLQDRLVRRPRLMQRLRTGYLAFTLVYLGWYSLGQLSVVNVLTFVHALFEGFRWELFLSDPLLFILWTFTAASLLLWGRGVFCGWLCPFGALQELLNELARKLRVPQFQVPFAVHERLWAIKYIILLVLFGLSLESLALAEQAAEVEPFKTAITLGFDRQWWFVAYAVALLVVNLFTRKVYCRYLCPLGAALAIPAKARLFDWLKRRAECGRPCQLCARECEIQAIHPDGRIEANECHYCLDCQMTYHDQDKCPPLVNKRKKRAKSAPADNARIPAENL
The following text describes a protein:
Function:
Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to ethyl acetate, pentyl acetate, methyl caproate, anisole, heptanal, 2-heptanone, r-carvone, nonanoic acid, and pyrazines.
Miscellaneous:
MISCELLANEOUS: The atypical heteromeric and topological design of the odorant receptors appears to be an insect-specific solution for odor recognition, making the OR/Orco complex an attractive target for the development of highly selective insect repellents to disrupt olfactory-mediated host-seeking behaviors of insect disease vectors. Odor-evoked OR currents are independent of known G-protein-coupled second messenger pathways.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MQDQLDHELERIDKLPKLGLLWVEYSAYALGVNIAPRKRSSKYCRLTRILVLIVNLSIIYSLVAFIMENYMISFETYVEAVLLTFQLSVGVVKMFHFQNKVESCSQLVFSTETGEVLKSLGLFQLDLPRKKELLSSVSLILLNNWMIIDRQVMFFFKIVCMPVLYYCVRPYFQYIFDCYIKDKDTCEMTLTYPAIVPYLQLGNYEFPSYVIRFFLLQSGPLWCFFAVFGFNSLFVVLTRYESGLIKVLRFLVQNSTSDILVPKDQRVKYLQCCVRLFARISSHHNQIENLFKYIILVQCSVSSILICMLLYKISTVLEVGWVWMGMIMVYFVTIALEITLYNVSAQKVESQSELLFHDWYNCSWYNESREFKFMIKMMLLFSRRTFVLSVGGFTSLSHKFLVQVFRLSANFFLLLRNMNNK
The following text describes a protein:
Function:
Cysteine protease that cleaves specifically after arginine or lysine residues. May play a role in apoptosis.
Subcellular Localization:
Recycling endosome. Note=Localizes to RAB11-positive recycling endosomes.
Sequence:
MDLLLGVLSSGILQNALPFVAGVGRVKRPKRVKLEEAFREAHLCRPVIPYRAPTPYTGGRVKALFVGINYTGTRNKLSGCVNDVRQMLGTLQRIQFPISECCILVDDMRFPNFTALPTRENIIKHMAWLVHDVRPGDVLFFHYSGHGTETKAERDSEELYDQCLVPLDYQVQGAILDDDLFELLVKGLPAGVRMTAVFDCCHSASLLDLPFAFVGNNNFYSGGRHEMRKVRANNFSMGDVVVFSGCDDSGTSADVSNVSSFGSGLVASGGAATQALTWALVNTSQLSYADIFIRTREILRQKGYKQVPQLSSSKPVDLYKPFSLFGPITVNTSLIHYVPQQYLQPWGPPQPYYPPPQPQQPYYPPPQPQQPYYPSSQLPTQYNNLAPTAGIPLMTSSSEVPPGQYPQALSGDQNGGVPPQYPSDQSTYYSSAQYLSGVGKPL
The following text describes a protein:
Function:
Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually, LchA2 exhibits activity towards B.subtilis L1 (IC(50)=30 uM), Rhodococcus sp. SS2 (IC(50)=16.6 uM), M.luteus B1314 (IC(50)=2.6 uM), B.megaterium VKM41 (IC(50)=2 uM), S.aureus 209p (IC(50)=20 uM), B.pumilus 2001, B.globigii I, B.amyloliquefaciens I, M.smegmatis 1171 and M.phlei 1291. However, when combined with LchA1, it displays much stronger activity against B.subtilis L1 (IC(50)=0.64 uM), Rhodococcus sp. SS2 (IC(50)=0.64 uM), M.luteus B1314 (IC(50)=0.09 uM), B.megaterium VKM41 (IC(50)=0.12 uM) and S.aureus 209p (IC(50)=0.64 uM). The activity of the combined LchA1 and LchA2 peptides is strongest at a molar ratio of 1. Even when applied at 17-fold concentration of the highest IC(50) values for Gram-positive bacteria, neither the individual nor the combined peptides display activity against Gram-negative bacteria P.aeruginosa PAO1, P.putida I-97 or E.coli C600.
Subcellular Localization:
Secreted.
Sequence:
MKTMKNSAAREAFKGANHPAGMVSEEELKALVGGNDVNPETTPATTSSWTCITAGVTVSASLCPTTKCTSRC
The following text describes a protein:
Function:
Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Responsible for energy coupling to the transport system.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MEQSVANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRVRQFLDGIADGPVPFRYPAGDYHADLLPGS
The following text describes a protein:
Function:
Controls phase transition from the vegetative to the reproductive state. Involved in the maintenance of the shoot apical meristem (SAM) thus preventing inflorescence meristem (IM) formation and subsequent inflorescence stem development during flowering. Regulates leaf and organ morphology.
Miscellaneous:
MISCELLANEOUS: Transcribed by RNA polymerase III (pol III).
Subcellular Localization:
Nucleus.
Sequence:
MNVDIDTETGSSFSITIDFGETVLQIKEKIEKSQGIPVSKQILYLDGKALEDDLHKIDYMILFESLLLRISPDADPNQSNEQTEQSKQIDDKKQEFCGIQDSSESKKLTRVMARRVHNVYSSLPAYSLDELLGPKYSATVTVGGRTNQVVQTTEQASTSGTAKEVLRDSDSPVEKKIKTNPMKFTVHVKPYQEDTKMIQVEVNADDNVEELRKELVKMQERGELNLPHEAFHLVSSELPLIETKSFKWNRVADGDTIELIREK