lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MPACTSIAVTGQPQSCTSAAALTVPLRPQLLRSKMLGLTGNACTSPHLHPLREASTHLLGDTQQRARHRCCPTTHDATLSHHRKEALSTKAIDDINHSLLNNTAYGVLSGKRGCRPRRSSSGACRSSSLALLDTAEAALTRPDRCSSAPAKEAVASTVATLPSLSPMKVKAVADSASVSPGVTSTTAVAEVLPMSLCASNTPRRLSDALRCDLGQSSDSDCSIASPRMALSLYATEEELPVCIDPEGVQCCPLIDPECEEGVVTDAQINLSPFLNWKFVPYLSSQAKGQVRPTVVLDMDETLLHTSVMPMPDADAEIDALCPSDEAQGTGTSMTSGRYKLFVKYRPHLERFLLFCLDHFEVVIFTASKALYAQTVLRQLQKDFPSINIRLDGSSASGSAPASQRVGDEARVIELLHRDHCTPTNVGYAKDLHLLGRDLRRTILVDNNNVCGVFQPYNSVHVRDFARRRCAERVPEQQRMRVTQLCQLKGTAPASAMTAVEDADTSHLLGNLECTTSTYDWLDREDTVLLRLCAAGGLLHRLSQCENVPSFMQRTVCFSRRAHLSRLVRGSVSSGIRPFPGEG
The following text describes a protein:
Function:
Subunit e, 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 (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (By similarity).
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MVPPVQVSPLIKLGRYSALFLGVAYGAKRYNYLKPRAEEERRIAAEEKKKQDELKRIERELAEAQEDSILK
The following text describes a protein:
Function:
CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
Sequence:
MDRESNAKHSVLELMLLDASAEPMDLPLSLLEDITNGFSHDQQIGSGGFAVLYKGILGKVTIAVKKLSKTFDNHEKQFHEEVSCLMKAKHKNIVRFLGYCSDTRGKMVAFEGKLVMADVRQRLLCFEYLPRGSLDKYIAGSSYVLQWKESYQIIKEICEGLHYLHVERRIVHLDLKPTNILLDCNMVPKIADFGLSRRFCEKQSQILTAEVKGTLGYMAPEFVNNGQITFKSDIYSLGIIITEILTRQRGYRDVEDVLDIWRNRLQESQREIHLEQVRVCTEIAKECSDYNPANRPAIQDIINRLDETESVGGSIETRGSTLSVAQEEKDPSEQHQWTPKVPGEASDEDCRMEVGTILMKRYEIGRLIAQGDLAKVYYAQNLTSEQDVAIKMIDKDKVSSVELMVRIKREMTLMNLLGHPNVLKLVEVMASKSKLYFVLEYPKGGDLSTKIVTGGLHEDAARKYFRQLISAVEYCHSQGVYHRNLNLENILLDENGNLKISDFGLSVLPGSREDGLFHYPCGTPAYVAPEVLSWRGYAGAKVDIWSCGVILFVLVAGYLPFQGTDATDLFNKISLGKYECPSWISVKLKDILCKILDLDPSTRASVSSIKASAWYRNHIEVKACKGEATTSETTECSMLSKGKTKCSNSVGNQAPSSFTHSNAVGVISLSVKFYLSNLSEKKYGLWENKFTARLPAETLFARINELAEQLKLKVKKKENGILKLVASEEGMGRLELDAEVFELAPSFLLVEIKITNGDKEYELQMKVKDAVRLIFKDMVWAWQDDSHSQQPQFTLFR
The following text describes a protein:
Function:
Able to bind (1->3)-beta-D-glucans (laminarin). Probably involved in cell-to-cell trafficking regulation.
Miscellaneous:
MISCELLANEOUS: Overexpression of PDCB1 results in callose accumulation and decreased plasmodesmal molecular diffusion.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor. Cell junction, plasmodesma.
Sequence:
MAALVLSLLLLSLAGHSSASWCVCKTGLSDTVLQATLDYACGNGADCNPTKPKQSCFNPDNVRSHCNYAVNSFFQKKGQSPGSCNFDGTATPTNSDPSYTGCAFPTSASGSSGSTTVTPGTTNPKGSPTTTTLPGSGTNSPYSGNPTNGVFGGNSTGGTTGTGINPDYTTDSSAFALKNSSKLFICLLLIASSGFCSFLML
The following text describes a protein:
Function:
Catalyzes the attachment of tryptophan to tRNA(Trp) in a two-step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of tRNA(Trp).
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MAASLRDVGKMALPMWRRAAVLLYRAGRGRRGLQESVKERGNKDVEPRVFSGIQPTGIPHLGNYLGALQSWVHLQEQYNTVLYSIADLHSITVPQDPSTLRASILDMAACLLACGINPAKSCIFQQSQVAEHAELAWILNCLTSMPRLRHLPQWKVKCQTQKNEGSAGLFTYPVLQAADILLYKSTHVPVGDDQVQHLELTQDTARLFNRIYGDFFPIPRGIMGTSKKIYSLRDPSSKMSKSDPQKLATVRLTDSPEEIVLKFRKAVTDFTSEVTYDPERRPGVSSLVAIHSAVTGLGTDIIVQQSRGMDTAQYKLTVADAVIQKLCPIREEMQRLQREQGYLREVLYQGAQRAKEMAAPVYDSVARLVGFR
The following text describes a protein:
Function:
Component of the U1 small nuclear ribonucleoprotein complex (U1 snRNP) involved in the initiation of meiotic recombination. Involved in the formation of DSBs at recombination hot-spots through meiosis-specific splicing of REC107 pre-mRNA. Collaborates with MER1 to promote splicing of essential meiotic mRNAs REC10, AMA1, MER3, HFM1, SPO22 and PCH2. NAM8 interacts with the pre-mRNA downstream of the 5' splice site, in a region of non-conserved sequence and is required for efficient splicing of uncapped RNA precursor.
Miscellaneous:
MISCELLANEOUS: Present with 1480 molecules/cell in log phase SD medium.
Domain:
The RNA binding domains RRM2 and RRM3 are required for NAM8 meiotic function. Within the U1 snRNP complex, the RRM2 domain of NAM8 is positioned to bind to the intronic region immediately down-stream of nucleotide +13.
Sequence:
MSYKQTTYYPSRGNLVRNDSSPYTNTISSETNNSSTSVLSLQGASNVSLGTTGNQLYMGDLDPTWDKNTVRQIWASLGEANINVRMMWNNTLNNGSRSSMGPKNNQGYCFVDFPSSTHAANALLKNGMLIPNFPNKKLKLNWATSSYSNSNNSLNNVKSGNNCSIFVGDLAPNVTESQLFELFINRYASTSHAKIVHDQVTGMSKGYGFVKFTNSDEQQLALSEMQGVFLNGRAIKVGPTSGQQQHVSGNNDYNRSSSSLNNENVDSRFLSKGQSFLSNGNNNMGFKRNHMSQFIYPVQQQPSLNHFTDPNNTTVFIGGLSSLVTEDELRAYFQPFGTIVYVKIPVGKCCGFVQYVDRLSAEAAIAGMQGFPIANSRVRLSWGRSAKQTALLQQAMLSNSLQVQQQQPGLQQPNYGYIPSSTCEAPVLPDNNVSSTMLPGCQILNYSNPYANANGLGSNNFSFYSNNNATNTQATSLLADTSSMDLSGTGGQQVIMQGSEAVVNSTNAMLNRLEQGSNGFMFA
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSNCLFNNLRNCIAVHLDRNEDKFNLLIYMIRKLYAVANGECQIESQDSPMNQEILLGGHMYSMVLKEKLELWLSRVKNLILKYMAKTNDEKLENAIVRAANNGTNIPNQLEYFLATGNLVARADLGLMQVAGYVLVADRLNFMRFVSHFRSVHRGSFFTEMRTTAVRKLLPEAWGFLCPVHTPDGAPCGLLNHLAASCKVVTKMSDTTKLVSTLYELGMLSLSDPLIEYSSAHVVILDGKIVGYIQKEIGKEIADKLRYLKINNMDMVDPSTEIALVHDGISGLYNGLYLFTSPARMIRPVTNLRLQKQEMIGTFEQVFMDICITAEEAYAEVTTHQELSPCSMLSALARLTPFSDFNQSPRNMYQCQMGKQTMGTPIQSFKYRSDNKLYRIQGYDMEDAMILNKSSVERGFAHATIYKSEVINLNSKTADGLEIFGQTPGTTDSDNIDLDGLPKIGSILNSGDPYYCTLNLSTSQCVVHYYRGQEQGIVDDVKLLGSDSGRKPLQRICVKFRIERNPIIGDKFSSRHGQKGVCSQLWPIENMPFTESGMTPDILFNPHGFPSRMTIGMMIESMAGKSASLHGLCHDATPFQFSEKVSAVDYFGKYLEKAGYNYFGTERMYDGMSGEEFEANIFIGTVYYQRLRHMISDKFQVRTTGPIDSLTRQPVQGRKRAGGVRFGEMERDALISHGTSFLLQDRLLNCSDKSVAHVCKKCGSVLGITTDVNKNEADIFREFSRKVYRCTTCDSTQEVTKMYLPYVYLYLVTEFAALNIKAVIEVE
The following text describes a protein:
Function:
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Sequence:
MRYLIKNGTIIDPANRVATIGDILVANGKVERLYDLADLHTDREPLAPDVEVINARGCVVAPGFTDLHTHLRQPGEEHKETIASVSAAAAVGGFTTLCARPTTRPTPDHAAAIRQLRELADQYARVRIDLIGALTMGNEGQVLSEMRELAEAGCIAFSDGGRTIANTALLRHALAYAAALKLPVMVSCQDPYLAAGGVAHEGAVSIRLGLPAIPAAAEEAIVARDIALAEATGAHLHISRVSTAGSVALIRAARARGVHVTAEVTPHHLTLSDRWLLGWLEERNEIETGRPGAHPDLSLPSWLNPALLPPYDSSTRVDPPLRSIEHVEALVEGLRDGVIDAIATDHAPHALVDRDCEYGIAPPGISGLETALALTLTLVHRGEMDIVNLIAKLTEGPAQVLNRSPANLRPGATADIVIFDPERSWVVDPDHFASRGRNTPLRGQRLKGQVMLTMAAGKIIFRREDFGRQAQAAPQPSRLEGILGAE
The following text describes a protein:
Function:
Protease that catalyzes two essential functions in the smo-1 pathway: processing of full-length smo-1 to their mature forms and deconjugation of smo-1 from targeted proteins (By similarity). May deconjugate smo-1 from the cadherin protein hmr-1 and plays a role in its recruitment to and the maintenance of adherens junctions. Required for epidermal morphogenesis during embryonic development.
Subcellular Localization:
Nucleus. Cytoplasm, cytosol.
Sequence:
MSDSTQMEANAAINEIKKRTRKLDQSLQMRFCADQFFIGNHCTKLASGKSIIISQNSKNRICLRFFMAADPLVGYTGRDFGIAFNQIDHISLKDEQQENPAVLICTLNLSSYTKMCKLQTGLKDVVEKPFLYNKSLARNLTFILKPWNDDPDTFVKISYNDEHREYVHSYDYDVAKSLMFKEVQAVWEQSLKEQLQRRHQTGRVYLTSQLSEMTPREWVQFLADQKLSKIVCHNGSIQYARVEDNPHGRKHTAVATNGFDHRGTRVLNSFGKAHASLATQEKSYAKKRKLTEQSLKLIYRNDRSVWLEGSCAKNLKMPKINSEPNMGEFMGWPDMDNAMTHPTSNFENEDVMKSTKQPNDFVSFEQLQAPPPVLQRQNGAIYSTQSVAFTHISGNDGVEDLTEKISHLGEEAYNIDMANALHAFSDNWHYEIHPNTVHNASFEQLHIGDGNSSIGTIGFNPLEPYPQSSFPQSNNWQQAHGDFTFPQVSFPNTQQGSCLPSTPTAALPPTRPVVEKIPPDTQLFTFPPSGSCTTGMDPVVLLVKDIKTLDRKEFLNDSVMAFMLNYIAFMLSSELMKSVHMCNTFLFVNLTRLLPPLCFSKRRPIEPEHIKIVKDNCPRVLRWTRKFDVLAKDYIIIPINEDLHWLVIAVINPSGAIVDMSNEEASRAAPKCYIVFFDPLSGLDPSKKNHMCHCIKIYLAQLYENTKAPGMKFASKNPTIYDEERVVVTRAENTPIQDNFYDCGLYVLHFIEGLFCYPNRPVNVNDFPNFDWSKFFPEANKMCDLMRDKVYNLILQQADKPARSRLAKFERENKCGLSREGALRKARRHSAVNERRTKRHRDYYARHYSLSPPHRNVMNDDPTFMNPRGLAEMPITRLVRRLRIPEDNFPIAY
The following text describes a protein:
Function:
Mediates the uptake of pyruvate into mitochondria.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
GEGSEGGNCRKARVVLLLDRCRWGWWRGSCCPPQPGRLGCHWDTAEAVAAAAAAAAVAAGVSSHGRGSGAESGRLCPEQGFPGLFDEHFWGPVANWGLPIAAFNDMKKSPEIISGRMTFALCCYSLAFMRFAYKVQPRNWLLFACHATNEVAQIIQGGRLVKYNLSKKTSA
The following text describes a protein:
Function:
V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. Involved in vesicular transport from the late endosomes to the trans-Golgi network. Along with VAMP7, involved in an non-conventional RAB1-dependent traffic route to the cell surface used by KCNIP1 and KCND2. May be concerned with increased secretion of cytokines associated with cellular senescence.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type IV membrane protein.
Sequence:
MSSDFEGYEQDFAVLTAEITSKIARVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDAGNSSENQRAHLLDNTERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDREKIQRARDRLRDADANLGKSSRILTGMLRRIIQNRILLVILGIIVVIAILTAIAFFVKGH
The following text describes a protein:
Function:
Key structural component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells and can generate more than 100 centrioles. Probably sufficient for the specification and formation of the deuterosome inner core.
Subcellular Localization:
Cytoplasm. Note=Localizes to the deuterosome.
Sequence:
MFTNIHSIARNSSCENELEELMHQIDIMVSHRKVEWEKHVKVLEQKLEAQDRELTEARNLVDEKNHEIGILCKKLEGVDTAQHEMAQNYERQLQALKFQLCKLKKSYEKLHFHQEKHQKNENAAQERSRCELQWLTQKIEEFKARSREWEKQRVFYQDQLKSLDEQRKTLAEKCQLFQKESLSYQEQLSSQKQLQSEAITNNQSEMRRLRCLLDTSQETIRSDGVIIENLKSTVKEITLSRDSLKDENQQLLQELRRCQKQSQNMEAQLYKAKLELQSCNDLLRVPALEERQAQKETANLANQKTAQGEEASFQVTDPRMNYMTSEPEHKSFNLSKSEKYQAENDLHGTEAKNSDLERLRKDIGDLTAKLNQKDVTIATVSRKVSRLERELELKGAQNRQTSMPLSQKDVIAELESEMPQIHAVNKAPQTDSGEVDPWISIKCGEHDKPQKHRSFHGENNSLKPTNYADTRNHSVGSEWESEKSLCPWNTPTLGSATDDDCDLVDNENEWLSLYNSTLYPGLDLPPISYACDQLKDSTNSSLAGSSLISAAEKFLLEETRRASDFEKILNSHIEEMKRNSESTVSRYQSHGQSRHI
The following text describes a protein:
Function:
Part of the anaerobic respiratory chain of trimethylamine-N-oxide reductase TorA. Acts by transferring electrons from the membranous menaquinones to TorA. This transfer probably involves an electron transfer pathway from menaquinones to the N-terminal domain of TorC, then from the N-terminus to the C-terminus, and finally to TorA. TorC apocytochrome negatively autoregulates the torCAD operon probably by inhibiting the TorS kinase activity.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein.
Sequence:
MRKLWNALRRPSARWSVLALVAIGIVIGIALIVLPHVGIKVTSTTEFCVSCHSMQPVYEEYKQSVHFQNASGVRAECHDCHIPPDIPGMVKRKLEASNDIYQTFIAHSIDTPEKFEAKRAELAEREWARMKENNSATCRSCHNYDAMDHAKQHPEAARQMKVAAKDNQSCIDCHKGIAHQLPDMSSGFRKQFDELRASANDSGDTLYSIDIKPIYAAKGDKEASGSLLPASEVKVLKRDGDWLQIEITGWTESAGRQRVLTQFPGKRIFVASIRGDVQQQVKTLEKTTVADTNTEWSKLQATAWMKKGDMVNDIKPIWAYADSLYNGTCNQCHGAPEIAHFDANGWIGTLNGMIGFTSLDKREERTLLKYLQMNASDTAGKAHGDKKEEK
The following text describes a protein:
Function:
Induces expression of IL6, CXCL8/IL8, and CSF2/GM-CSF from endothelial cells.
Subcellular Localization:
Secreted.
Sequence:
MLVAGFLLALPPSWAAGAPRAGRRPARPRGCADRPEELLEQLYGRLAAGVLSAFHHTLQLGPREQARNASCPAGGRPADRRFRPPTNLRSVSPWAYRISYDPARYPRYLPEAYCLCRGCLTGLFGEEDVRFRSAPVYMPTVVLRRTPACAGGRSVYTEAYVTIPVGCTCVPEPEKDADSINSSIDKQGAKLLLGPNDAPAGP
The following text describes a protein:
Function:
Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSAPVVLALMSICFLSFGYLGVPVPFSLMAGVFIGAILSDVSLAAIIQKIFDGVDSEALLAIPFFLLVGELMSSANVVVRIANLSVSLVGHIRGGLSQVVVVFSMFFSEMSGSTTADVAVMSRALGGPMKREGYEPAFIAAIIASASTIAALVPPSITAVVYGAVGNVSIAGLFMAGVVPGLMIGIGLMIYCYFFGPSGLRKPRAPLRQVVFAAGDAALPLMIPVILLGGILTGWFTPTEAGVVAVAWIVLVVIPALNRGHFTKIPYDFCLAGLIFSLPLITIGAANAFGWMLAYLRGASYIAELITSIAGHDPHLIMLLMVLLFTVVGDFIEPVPTIIIFMPLVNTLTEAGDINAVHMGVVLIATLAFGLITPPYGLVLLMASKFVGISFAKALRAALPIYVVFLATIAFAIYFPSVVLWLPRHVLPESVGCFKSPAGTGYICPQ
The following text describes a protein:
Function:
Permease involved in lysine uptake. In addition, functions as a lysine sensor that mediates the lysine-dependent regulation of the transcriptional activator CadC. In the absence of lysine, or at low lysine concentrations, LysP inhibits CadC by an interaction with the transmembrane domain of CadC. In the presence of lysine, LysP loses its ability to interact with and inhibit CadC, and acts as a lysine permease.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MVSETKTTEAPGLRRELKARHLTMIAIGGSIGTGLFVASGATISQAGPGGALLSYMLIGLMVYFLMTSLGELAAYMPVSGSFATYGQNYVEEGFGFALGWNYWYNWAVTIAVDLVAAQLVMSWWFPDTPGWIWSALFLGVIFLLNYISVRGFGEAEYWFSLIKVTTVIVFIIVGVLMIIGIFKGAQPAGWSNWTIGEAPFAGGFAAMIGVAMIVGFSFQGTELIGIAAGESEDPAKNIPRAVRQVFWRILLFYVFAILIISLIIPYTDPSLLRNDVKDISVSPFTLVFQHAGLLSAAAVMNAVILTAVLSAGNSGMYASTRMLYTLACDGKAPRIFAKLSRGGVPRNALYATTVIAGLCFLTSMFGNQTVYLWLLNTSGMTGFIAWLGIAISHYRFRRGYVLQGHDINDLPYRSGFFPLGPIFAFILCLIITLGQNYEAFLKDTIDWGGVAATYIGIPLFLIIWFGYKLIKGTHFVRYSEMKFPQNDKK
The following text describes a protein:
Function:
CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
Sequence:
MNQYHIYEAIGRGKHSTVYKGRKKKSIEYYAIKSVEKAQKTRVLQEVRTLHSLDHHNVLKFYAWYETSAHLWLVLEYCVGGDLLTLLRQDTRLPEESIHDFARDLVQALQFLHSKGVIYCDLKPSNILLDENGRLKLCDFGLARRLGDISKSSVQQLPQAKRGTPCYMAPELFQEGGVHSFGSDLWALGCVMYECFSGRPPFVSNSFTQLVNSILTDSPPPLRGNPTSEFQNLVGRLLVKDPAKRLQWAELREHPFWRTKIQTVPLPPQPALANFLRMAQKSGSPRSDSAASRNALPDITPSPDKRSLRDKSSKLSDSSAGKRGASQTACLGDGRSEDAGSVENAPSSEADRARRMSGAAASASPLKGEPARANGVVNVLRLSKIVKSNLQKEGQGESYRQHVPNAPAANDSDVTIENHDQELDFAEVNENDVDDDEEEAATCPSATAVPSEESKAEEQVPSLVQTAQPEGEKPEDLTVCQVAQPINQDPEDDHSGPKPEQVEAKKHDAARSEVAATPPGVGVPRKLQRQTSDVRDLKKNSSLPSSQAAGEPAKASLTLSQALWHPSDLSVRPIMISRRVEKTPDTAFDVRTLPVDPLQFSDFVKLSSEMVESFVNRIMTSIQGSSSLNDKLNTLRYVESLCSNIDAANILINGPLMSLLVKTLRTSKLPTLRVQVAFVMGLLIRHATLIEDDLAGSGIIAVLTETLRDKQEKVRRCAMATLGELLFYIATQSEGSPRSGVTNESGSKDGRSSSVWQVSSTTIALVASILRKGEDDVTQHYALKTIENISSQGWDWASRFTSREVINNLCHTFKSSGKPEAVRASAGSCLVRLVRFSPTTIPSVLEKVTFKDLVVVLARGSAKEQQVSLNLLNMALVGCSVINNMSKYLLALLEEKTLVPSLMALLEQGLEVLRGKAFVCAGLLCKVNRRWLPSLCNAKLMPVIERSAKEKDPYVQQCVETLVQTIISIVPDILDSISLDILQLSSAKRPSSTSSRGQPRSSIPLFPVVLHLFNSPTLRSRLVNEQVIKQLVGALKQVETLSFQGHDEFQSTLLQIIEVLSQQSSVVLKYPDTFIAQVLPSLSQLYKSNTDGDMRFLCFKIFFDILMLYLEDISTSDGESPSSQNPATESRPTCMTHIEPIIGKYFLPLYPKLVDDEDPIPMYAHKLLVMLLDHKCIKIVDILQLKLVSQFFEFLSDDLSTINLHNVRLCLFLASAPEVDSKSLSALRVVGRIGSLLEFVHAKGMEDFLDPVLSVCKFFLIRNAGSSGGKSGDGLIQDIEELCRHSGIFVELCGSHDRISETSAECLVLTVKASPTAASSGVLANLSKVAQVLESCVERHDSASLQRRLLFVVSTIFKEQRMASGSSLPVPKIAHSDFIALENIVIRLRRSSAPQVAEAAVSAAFELHHLPRNS
The following text describes a protein:
Function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. NDUFA4 is required for complex IV maintenance.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLATVMKQLKSHPALIPLFIFIGGGATMSMLYLGRLALKNPDCSWDRKNNPEPWNKLGPNDQYKLFSVNMDYSKLKKDRPDF
The following text describes a protein:
Function:
Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.
Miscellaneous:
MISCELLANEOUS: Dictyostelium myosin-2 has no K(2)EDTA ATPase activity, perhaps correlated with the absence of a Cys at the SH-1 position (688).
Subcellular Localization:
Cytoplasm, cell cortex. Note=Highest concentration in the posterior cell cortex.
Domain:
Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2); The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.
Sequence:
MNPIHDRTSDYHKYLKVKQGDSDLFKLTVSDKRYIWYNPDPKERDSYECGEIVSETSDSFTFKTVDGQDRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDGRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFRAGQLARIEEAREQRISEIIKAIQAATRGWIARKVYKQAREHTVAARIIQQNLRAYIDFKSWPWWKLFSKARPLLKRRNFEKEIKEKEREILELKSNLTDSTTQKDKLEKSLKDTESNVLDLQRQLKAEKETLKAMYDSKDALEAQKRELEIRVEDMESELDEKKLALENLQNQKRSVEEKVRDLEEELQEEQKLRNTLEKLKKKYEEELEEMKRVNDGQSDTISRLEKIKDELQKEVEELTESFSEESKDKGVLEKTRVRLQSELDDLTVRLDSETKDKSELLRQKKKLEEELKQVQEALAAETAAKLAQEAANKKLQGEYTELNEKFNSEVTARSNVEKSKKTLESQLVAVNNELDEEKKNRDALEKKKKALDAMLEEMKDQLESTGGEKKSLYDLKVKQESDMEALRNQISELQSTIAKLEKIKSTLEGEVARLQGELEAEQLAKSNVEKQKKKVELDLEDKSAQLAEETAAKQALDKLKKKLEQELSEVQTQLSEANNKNVNSDSTNKHLETSFNNLKLELEAEQKAKQALEKKRLGLESELKHVNEQLEEEKKQKESNEKRKVDLEKEVSELKDQIEEEVASKKAVTEAKNKKESELDEIKRQYADVVSSRDKSVEQLKTLQAKNEELRNTAEEAEGQLDRAERSKKKAEFDLEEAVKNLEEETAKKVKAEKAMKKAETDYRSTKSELDDAKNVSSEQYVQIKRLNEELSELRSVLEEADERCNSAIKAKKTAESALESLKDEIDAANNAKAKAERKSKELEVRVAELEESLEDKSGTVNVEFIRKKDAEIDDLRARLDRETESRIKSDEDKKNTRKQFADLEAKVEEAQREVVTIDRLKKKLESDIIDLSTQLDTETKSRIKIEKSKKKLEQTLAERRAAEEGSSKAADEEIRKQVWQEVDELRAQLDSERAALNASEKKIKSLVAEVDEVKEQLEDEILAKDKLVKAKRALEVELEEVRDQLEEEEDSRSELEDSKRRLTTEVEDIKKKYDAEVEQNTKLDEAKKKLTDDVDTLKKQLEDEKKKLNESERAKKRLESENEDFLAKLDAEVKNRSRAEKDRKKYEKDLKDTKYKLNDEAATKTQTEIGAAKLEDQIDELRSKLEQEQAKATQADKSKKTLEGEIDNLRAQIEDEGKIKMRLEKEKRALEGELEELRETVEEAEDSKSEAEQSKRLVELELEDARRNLQKEIDAKEIAEDAKSNLQREIVEAKGRLEEESIARTNSDRSRKRLEAEIDALTAQVDAEQKAKNQQIKENKKIETELKEYRKKFGESEKTKTKEFLVVEKLETDYKRAKKEAADEQQQRLTVENDLRKHLSEISLLKDAIDKLQRDHDKTKRELETETASKIEMQRKMADFFGGFKA
The following text describes a protein:
Function:
Chitosanase catalyzing the endo-type cleavage of chitosan, the deacylated form of chitin. Chitosanase may be crucial in the degradation of the deacetylated portion of chitin in the fungal cell wall. Chitoolisaccharides produced by the hydrolysis of partially N-acetylated chitosan are known to have many biological activities, including antibacterial activity, immune-enhancing effects, and elicitor activity. The chitosans with higher degrees of deacetylation were shown to be the better substrates. Chitodimer, chitotrimer, and chitotetramer are the major products but monoacetyl chitodimer, monoacetyl chitotrimer, and monoacetyl chitotetramer are also produced.
Subcellular Localization:
Secreted.
Sequence:
MRLSEILTVALVTGATAYNLPNNLKQIYDKHKGKCSKVLAKGFTNGDASQGKSFSYCGDIPGAIFISSSKGYTNMDIDCDGANNSAGKCANDPSGQGETAFKSDVKKFGISDLDANIHPYVVFGNEDHSPKFKPQSHGMQPLSVMAVVCNGQLHYGIWGDTNGGVSTGEASISLADLCFPNEHLDGNHGHDPNDVLFIGFTSKDAVPGATAKWKAKNAKEFEDSIKSIGDKLVAGLKA
The following text describes a protein:
Function:
Thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act together with BSN. May recruit liprin-alpha proteins to the CAZ.
Subcellular Localization:
Cytoplasm. Synapse. Presynaptic active zone. Cytoplasm, cytoskeleton. Note=Localized to the active zone of presynaptic density. Colocalizes with RIMS1 and BSN in early stages of synapse formation.
Sequence:
MYGSARTISNPEGSPSRSPRLPRSPRLGHRRTSSGGGGGTGKTLSMENIQSLNAAYATSGPMYLSDHEGVASTTYPKGTMTLGRATNRAVYGGRVTAMGSSPNIASAGLSHTDVLSYTDQHGGLGGSSHHHHHQVPSMLRQVRDSTMLDLQAQLKELQRENDLLRKELDIKDSKLGSSMNSIKTFWSPELKKERVLRKEEAARMSVLKEQMRVSHEENQHLQLTIQALQDELRTQRDLNHLLQQESGNRGAEHFTIELTEENFRRLQAEHDRQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLPSKSLEDDNERTRRMAEAESQVSHLEVILDQKEKENIHLREELHRRSQLQPEPAKTKALQTVIEMKDTKIASLERNIRDLEDEIQMLKANGVLNTEDREEEIKQIEVYKSHSKFMKTKNDQLKQELSKKESELLALQTKLETLSNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKGTLAGEIRDMKDMLEVKERKINVLQKKIENLQEQLRDKDKQLTNLKDRVKSLQTDSSNTDTALATLEEALSEKERIIERLKEQRERDDRERLEEIESFRKENKDLKEKVNALQAELTEKESSLIDLKEHASSLASAGLKRDSKLKSLEIAIEQKKEECNKLEAQLKKAHNIEDDSRMNPEFADRLKQLDKEASYYRDECGKAQAEVDRLLEILKEVENEKNDKDKKIAELESLTLRHMKDQNKKVANLKHNQQLEKKKNAQLLEEVRRREFSMVDNSQHLQIEELMNALEKTRQELDATKARLASTQQSLAEKEAHLANLRMERRKQLEEILEMKQEALLAAISEKDANIALLELSASKKKKTQEEVMALKREKDRLVHQLKQQTQNRMKLMADNYDDDHHHYHHHHHHHHHRSPGRSQHSNHRPSPDQDDEEGIWA
The following text describes a protein:
Function:
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MYECVECGYKTDCLFRKLSTEVIKLSHCENCKQPVDKYIEYDNILTGIDATLHKTQAYRHLIHNSNIKSTMKLWLVYLLCDVYVAWQSLKKMSCDDADEPYSEGVFSMLFLLAVVDWLWYVVVLFLLITLFTDVSTKDHYLRTLVLSSFGKLLSLPALIWTTMHENIYFILIQIFILTSNITALKGPPF