lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Sequence:
MHDCEDTCSYYLSEARESDGGFQHGGSEDSASDGSNDSDHDGDKDDGGGGDGNDEPRDDPYFRASGDMDEASRVTLSAALLSDLETSHTSPTPHAAQETQSKSSDCCVCGTHAMYTCPGCARRTCSMICVRVHKEDFKCTGMRDVAAKVPLSEFTDRQLQRDYHFLENCRRAIDNIERCFPRTSWRYNYKALPPPLHALREAARRRGVICQIMSEGMRKRDENTSRLDRKTNTIVWRCEFEFSSADDGAEVTTISTDWGSERHRLGDILKYCWATNPPLLCYHINRRYNRVSKYVGESATKTAKGVEGEVPGETDPTQHDRAAAPLETAVDACSAAAPPTGADVLPTAEVTRVASDEGEGDVPPPTVAAVESEAAASREGRPLRAPAEVLPLRAYEVVLPMPPIEPVTSREAQQQAFVQAFLTREKYVILSKAERLGNNARYFLLNPYDTLNENLRRLFFVSEFPVFVVVHASQLHRFSLVTEEDKEAIRSSFRSKKTYEPRERPPMRKRSEMKPEELERLSRVPCRRFLQCRCPNAEECPYWHCTPNEIPVCRTFLRFGECDKGTRCSFRHDADAVRIARKRQRDGLAEDGNPMRGRGMGRGRGFGRLRDGARGRGGMGGGFYPPRRRTE
The following text describes a protein:
Function:
Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating demethylation of dimethylsulfoniopropionate (DMSP) to methyl-mercaptopropionate (MMPA). The intracellular concentration of DMSP is estimated to be 70 mM.
Miscellaneous:
MISCELLANEOUS: DMSP is used as an intracellular osmolyte, predator deterrent and antioxidant.
Sequence:
MASIFPSRRVRRTPFSAGVEAAGVKGYTVYNHMLLPTVFDSLQADCAHLKEHVQVWDVACERQVSIQGPDALRLMKLISPRDMDRMADDQCYYVPTVDHRGGMLNDPVAVKLAADHYWLSLADGDLLQFGLGIAIARGFDVEIVEPDVSPLAVQGPRADDLMARVFGEAVRDIRFFRYKRLAFQGVELVVARSGWSKQGGFEIYVEGSELGMPLWNALFAAGADLNVRAGCPNNIERVESGLLSYGNDMTRENTPYECGLGKFCNSPEDYIGKAALAEQAKNGPARQIRALVIGGEIPPCQDAWPLLADGRQVGQVGSAIHSPEFGVNVAIGMVDRSHWAPGTGMEVETPDGMRPVTVREGFWR
The following text describes a protein:
Function:
Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MASVETLLWVGVWMSAFSITTADDNSVPKAENVRWMSLDFTTVLTWTAKPSSYSFTVQYATDGDDWTESPDCIRISDTKCDLTEHLIPYDMNYIADIQTEHLEADYDVENLPHTYSPKFNPFSESNISAVEFSVTQLNETTVCVNITDPLTAIHQKNQQLSIRDILKKDLKYKISYYKSGNTRKRDFESPTSTAEISGLDPGQSYCFMVAAYIPSRAKANQNGALSLEQCTEGDGGILQELSVGAWVGVVFLIITVIIVLVTVIALCCRNPNRNKSLQSTQLSAPV
The following text describes a protein:
Function:
Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes (By similarity). When secreted, interacts with NK cell-activating receptor NCR3/NKp30 acting as an inhibitory ligand which antagonizes NK cell attack (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Secreted. Note=Secreted by a non-classical secretory pathway and associates with the cell surface. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion.
Sequence:
MADSFSLNDALSGSGNPNPQGWPGPWGNQPAGAGGYPGASYPGAYPGQAPPGGYPGQAPPGGYPGQAPPGGYPGQAPPGGYPGQAPPGGYPGQAPPGGYPGQAPPGTYPGPTAPAYPGPTAPGTQPGQPSGPGAYPPPGQPSAPGAYPAAGPFGIPAGPLTVPYDLPLPGGVKPRMLITILGTVRPSANRLALDFKRGNDVAFHFNPRFNEDNKRVIVCNTKLDNIWGKEERQAAFPFESGKPFKIQVLVESDHFKVAVNDAHLLQYNHRMKNLPEISKLGISGDIDLTSASYAMI
The following text describes a protein:
Function:
Histone lysine methyltransferase that specifically mono-, di-, and trimethylates 'Lys-37' of histone H3 to regulate sporulation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MRIPVIRSPLEIRDTERKGRGVFALEPIPAQTCIEISPVLMFSKEEYEQHGQYTVLNEYTYVWSEGKQGLALGLGSMFNHDRHPNVYWKKDNRNNYISYYTLREIKTNEELCISYGDHLWFEDEASSASRISPNEENEDFPLQNISL
The following text describes a protein:
Function:
Stimulates the cysteine desulfurase activity of CsdA. Contains a cysteine residue (Cys-61) that acts to accept sulfur liberated via the desulfurase activity of CsdA. May be able to transfer sulfur to TcdA/CsdL. Seems to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct(6)A37) in tRNAs that read codons beginning with adenine. Does not appear to participate in Fe/S biogenesis.
Sequence:
MTNPQFAGHPFGTTVTAETLRNTFAPLTQWEDKYRQLIMLGKQLPALPDELKAQAKEIAGCENRVWLGYTVAENGKMHFFGDSEGRIVRGLLAVLLTAVEGKTAAELQAQSPLALFDELGLRAQLSASRSQGLNALSEAIIAATKQV
The following text describes a protein:
Function:
As a component of the decapping complex, involved in the degradation of mRNAs. Promotes P-body formation. Translational repressor.
Subcellular Localization:
Cytoplasm, P-body.
Sequence:
MASESASRSSTTSADSYIGSLISLTSKSEIRYEGVLYNINTQESSIGLENVRSFGTEGRKKDGPQVPPGDKIYKYILFRGSDIKDLQVKSSPPVQPMPPINIDPAIIQSHFARPISTSTSLPPAVSGSMTDISSHSAQLGLHGSSFQGGLPLYQPGGNIASWGATPPPSSANGGGLAMPMYWQGYYGPPNGLPHLHQQSLLRPPPGLPMPSSLQLPMPSSLQLPMQYPNFNVSLPSGSSNLPEVPSPLPPASSNSMNLSSSSLAPSTLPPVPSVTLASETLVNSVPNKAPPSSGLPTIALGSSMPSLAPLAMSSADINAILPPISNKPSAIPGPILSYQASLQSTSSIVGTSNTIRAEAPAPSLVTPGQLLQSVPSAVASSQTLQTVHKDVEVDQVSSSSSESIVPVLAEGQPPLLPLPVPSRTSQKPNGTPFQYRQGYRGRDRGRGSGSSHPVTKFSEDFDFIAMNEKFKKDEVWGHLGKSNKSNSREGDGEVSDEDDTLDDEDAQLSKFEVTQSVYKKDDFFDSLSCNSLNHELQNGRSRFSEQMKIDTETFGDFTRYRGGRGGRGSGRGGRFRGGYYGRGYNHVGRGRGPGIFGRSP
The following text describes a protein:
Function:
Required for cytoplasmic partitioning and asymmetric cell division in early embryogenesis. Phosphorylates and restricts the asymmetry effectors mex-5 and mex-6 to the anterior cytoplasm of the zygote and maintains these phosphorylations until fertilization. Phosphorylates and regulates aak-2 in response to oxidative stress. May also play a role in motility, behavioral response, regulation of lifespan and dauer formation through this pathway (By similarity).
Subcellular Localization:
Cytoplasm, cell cortex.
Sequence:
MEGPSSSSVPTASDAPSKYLLPSDSDDGIATSSAANVGARNHVTNTEKMEKEKKPSPMVLNVDPDYDYDEEDGGSCEEDQRGPPAPISREIVDGAIARRSRDRQISPGVKMSIGNYDDMEDDDEEAETPEEQKQRFLASMKRIRNQPQEAFDPPEDTEAMREFINRQVNDAMMFNRDNHIDYSPVNKPKEAKIIEGYLWGGIIGTGSYGKVKEVIDIYTITRRAAKIMKYEKLRKIPNGWDNIRSEMSILRRLNHRNIVKLIEVFNLPEKGKVYMIFEYCIGSVQNLIDMEPAHRLSIGESHAIFLELCHGLNYLHSKRVSHKDIKPGNLLLSIDMTVKICDFGVAEQICLFQSDGRCTKVNGTPKFQPPECVYGNHEYFDGYKVDMWSAGVTLYNMVSGKYPFEQQVLLRLYESIGTNPVEMPTNVELSKDLQDIIKRLLDKDFNTRPNISDVMQHPWFQTGFPEDQGLGRIMERMRTGDRPFTMYPSLQAMYDGAGSEVILDEDGNELVLPPPDLVKRGLKFFLELKILENLPGTLSLSSFPGFQTLEKRPGDGPPPSSDSGVVAAPDSASGDPLRRPSSRSMPTSAPPRPPSGAVEVVEAVAAPEAVVEDPVVEEAPAQQQEAPDRRRRGKRSLFSCIFRSRTDSS
The following text describes a protein:
Function:
Involved in the trafficking of vacuolar proteins. Functions probably as a sorting receptor for protein trafficking to the protein storage vacuole (PSV) by binding the C-terminal vacuolar sorting determinant (VSD) of vacuolar-sorted proteins.
Subcellular Localization:
Prevacuolar compartment membrane. Protein storage vacuole membrane. Golgi apparatus membrane; Single-pass type I membrane protein. Note=Localizes mainly to the prevacuolar compartment of the protein storage vacuole, but a minor portion also localizes to the Golgi complex.
Sequence:
MRLVVSSCLLVAAPFLSSLLRVSLATVVLNSISASFADLPAKFDGSVTKNGICGALYVADPLDGCSPLLHAAASNWTQHRTTKFALIIRGECSFEDKLLNAQNSGFQAVIVYDNIDNEDLIVMKVNPQDITVDAVFVSNVAGEILRKYARGRDGECCLNPPDRGSAWTVLAISFFSLLLIVTFLLIAFFAPRHWTQWRGRHTRTIRLDAKLVHTLPCFTFTDSAHHKAGETCAICLEDYRFGESLRLLPCQHAFHLNCIDSWLTKWGTSCPVCKHDIRTETMSSEVHKRESPRTDTSTSRFAFAQSSQSR
The following text describes a protein:
Function:
Increases viral DNA accumulation. Enhances infectivity and symptom expression.
Sequence:
MDSRTGELITAPQAENGVFIWEINNPLYFKITEHSQRPFLMNHDIISIQIRFNHNIRKVMGIHKCFLNFRIWTTLQPQTGHFLRVFRYEVLKYLDSLGVISINNVIRAVDHVLYDVLENTINVTETHDIKYKFY
The following text describes a protein:
Function:
Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGLLELFITACMPVLNMLLVTGVGSFLATDSAGILGKEARKHLNYVVFYVFNPALIATYLAKTIIMESLAKLWFMPVNVFFTFIFGLILGWIVIKVTGAPLKLRGLILGCCSAGNLGNIFLIIIPALCKEKGSPFGTPDVCQTYGLAYSSLSLAIGAVFLWTGAYNIIRANSNVTEGDGSSPITQTKVLVSGGTRCADSEDNRDRVDECTLPLISNRTKTKVPLMERAKGFISSVSGAIDLRKLFAP
The following text describes a protein:
Function:
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MDIQRSILIVALAVVSYLLVLQWNKDYGQPELPAASASMNTTQGLPDTPSASGTSSDVPTAQSSAAGSEAADKPVAVSDKLIQVKTDVLDLAIDPRGGDIVQLGLLQYPRRLDRPDVPFPLFDNGRERTYLAQSGLTGADGPDASSAGRPLFRSAQSSYQLADGQNELVVDLSFSHDGVNYIKRFTFHRGLKADCSDKEKAQKKIECINENAYQVGVSYLIDNQSGKTWSGNLFAQLKRDGSADPSSTTATGVSTYLGAAVWTPDSPYKKISTKDMDKEQFKESVQGGWVAWLQHYFVTAWVPTKGEQHQVMTRKDGQGNYIVGFTGPTLSVPAGSKVETDLTLYAGPKLQKHLKELSPGLELTVDYGFLWFIAQPIFWLLQHIHSLIGNWGWSIIALTVLIKLAFFPLSAASYRSMARMRAVSPKMQAIKEQHGDDRQKMSQAMMELYKKEKINPLGGCLPILVQMPVFLSLYWVLLESVEMRQAPWLGWITDLSVKDPFFILPIVMGGTMLIQQMLNPTPPDPMQAKVMKLMPIIFTFFFLWFPAGLVLYWVVNNCLSIAQQWYITRKIEAAAKTA
The following text describes a protein:
Function:
Isomerase that catalyzes the condensation of two molecules of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) into the phenazine ring system. The final product is not yet known.
Sequence:
MHRYVVIDAFASEPLQGNPVAVFFDCDDLSGERMQRMAREMNLSESTFVLRPQQDGDARIRIFTPVNELPFAGHPLLGTAIALGAETDKDRLFLETRMGTVPFALERQDGKVVACSMQQPIPTWEHFSRPAELLAALGLKGSTFPIEVYRNGPRHVFVGLESVAALSALHPDHRALCDFPDLAVNCFAGAGRHWRSRMFSPAYGVVEDAATGSAAGPLAIHLARHRQIPYGQQIEILQGVEIGRPSRMYARAEGAGERVSAVEVSGNGAAFAEGRAYL
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in tRNAs. Probably not able to catalyze formation of N(1)-methyladenine at position 9 (m1A9) in tRNAs.
Sequence:
MDCEWEGRPQRAGSRASQDPEGLPEARDDGLSESFLLLQMDVEYDPQEKRRPANSAAWSSKNVQRKQRHWERIVSSKKSKRKQERERRKIKRAEDLGNGTCPQHSKRFLKALTKEKLLEAKHSGPRLCVDLSMTQHMSKKELSRLAGQIRRLYGSNKKASRPFWIYLTGFSTDSPLYEECLRMNDGFSAYVLDVTEEDCFSLFPLETLVYLTPDSEHPLEDIDLSTVYIIGGLVDESIQKKVTFQKAQEYSVKTARLPIQEHMIRCQNEKNFHSEILAINQVFDILSAYLETRDWPEALKKGVSPGKGYILQNSVE
The following text describes a protein:
Function:
Involved in spore wall assembly. May be a component of the mitochondrial RNase MRP (MtMRP), a ribonucleoprotein endoribonuclease involved in the cleaving RNA transcripts to generate primers for DNA replication in mitochondria. Causes growth arrest when highly overexpressed.
Miscellaneous:
MISCELLANEOUS: Present with 8640 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion.
Sequence:
MGKLIKLITTLTVLVSLLQYCCEFNSGSISCERTQTLCHYTNPRVWNTYFSRNCELYKNKVSPGFDIVARKYDTAVKPVIDDATVKVNKVAIQPAFKVIHSQCKKWNCGKYYQLVRSPMVKTRRFFFAKYNAFVKPNLDKFFTAEFRSHLKERILKYKNIGHYYFTITSRCIKSKYDFIVGNTEEKLMGKFKNKDTHGIHGSVTREPSSEDMVLTVSTMESDEEELTTTSTQTVVETITLDQEEASAVANHAHDDEASTDVEGSTDVNVNEQALLQEDFDMWSETILQKTQDVIQLFEKDVSKYINGKLVEEANHFKAKFQSLDDKSKKFFSKISLAINDIECVEGIDSETGKKIFFDKSGSTEISQYITRELVREYFNETRSTLDELTNAMEKDLSEITDEIEKKVNAIREENVEVFEEWGDIIVNEWSKRMAYVDVINAHMGADDDTTLDEEKAKSSVNWKKFLKGKKQIIESRDKLAHHSADLSRVNAFRQKVQKKILSFTQESGEFLYILRSKANLQFQERERKERERKEREKAAAEEFQRQQELLRQQEEEDEEDVSYTSTSTITTTITMTL
The following text describes a protein:
Function:
Together with KTI11; associates with the elongator complex and is required for tRNA Wobble base modifications mediated by the elongator complex. Association with the elongator complex is mediated via interaction with KTI11. The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). Together with KTI11; also required for diphthamide biosynthesis; diphthamide is a post-translational modification of histidine which occurs in elongation factor 2. May participate in regulatory interactions between microtubules and the cell cycle.
Subcellular Localization:
Cytoplasm.
Sequence:
MSCVYAFGSNGQRQLGLGHDEDMDTPQRSVPGDDGAIVRKIACGGNHSVMLTNDGNLVGCGDNRRGELDSAQALRQVHDWRPVEVPAPVVDVACGWDTTVIVDADGRVWQRGGGCYEFTQQHVPLNSNDERIAVYGCFQNFVVVQGTRVYGWGSNTKCQLQEPKSRSLKEPVLVYDTGSVAVDYVAMGKDFMVIVDEGGRIVHASGRLPTGFELKQQQKRHNLVVLCMWTSIHLWNARLNTVESFGRGTHSQLFPQERLDFPIVGVATGSEHGILTTANQEGKSHCYNVYCWGWGEHGNCGPQKGSQPGLQLVGQYSGKPRVFGGCATTWIVL
The following text describes a protein:
Function:
May function in cell morphology by maintaining the integrity of the circumferential actin ring and controlling lamellipod formation. Involved in the regulation eye, tooth, brain and craniofacial development.
Subcellular Localization:
[Isoform 1]: Apical cell membrane; Peripheral membrane protein. Cell projection, lamellipodium. Cell junction, tight junction. Cell junction, focal adhesion. Note=Colocalizes with the tight junction protein TJP1 in epithelial cells. Localizes to the leading edge of lamellipodia in motile cells; [Isoform 3]: Cytoplasm.
Sequence:
MPFAKRIVEPQWLCRQRRPAPGPAVDASGGSAEPPPPLQPPGRRDLDEVEAPGPEEPARAVPAPSGLPPPPPPLPAPADQTQPPHGEASVAGEESTAGIPEAAPAAGEASSAAAAAAVLLMLDLCAVSNAALARVLRQLSDVARHACSLFQELESDIQLTHRRVWALQGKLGGVQRVLSTLDPKQEAVPVSNLDIESKLSVYYRAPWHQQRNIFLPATRPPCVEELHRHARQSLQALRREHRSRSDRREQRAAAPLSIAAPPLPAYPPAHSQRRREFKDRHFLTFNSTRSPSPTECCHMTPWSRKSHPPEDEDTDVMLGQRPKNPIHNIPSTLDKQTNWSKALPLPTPEEKMKQDAQVISSCIIPINVTGVGFDREASIRCSLVHSQSVLQRRRKLRRRKTISGIPRRVQQEIDSDESPVARERNVIVHTNPDPSNTVNRISGTRDSECQTEDILIAAPSRRRIRAQRGQSIAASLSHSAGNISALADKGDTMFTPAVSSRTRSRSLPREGNRGGDAEPKVGAKPSAYEEGESFVGDHERTPNDFSEAPSSPSAQDHQPTLGLACSQHLHSPQHKLSERGRSRLSRMAADSGSCDISSNSDTFGSPIHCISTAGVLLSSHMDQKDDHQSSSGNWSGSSSTCPSQTSETIPPAASPPLTGSSHCDSELSLNTAPHANEDASVFVTEQYNDHLDKVRGHRANSFTSTVADLLDDPNNSNTSDSEWNYLHHHHDASCRQDFSPERPKADSLGCPSFTSMATYDSFLEKSPSDKADTSSHFSVDTEGYYTSMHFDCGLKGNKSYVCHYAALGPENGQGVGASPGLPDCAWQDYLDHKRQGRPSISFRKPKAKPTPPKRSSSLRKSDGNADISEKKEPKISSGQHLPHSSREMKLPLDFANTPSRMENANLPTKQEPSWINQSEQGIKEPQLDASDIPPFKDEVAESTHYADLWLLNDLKTNDPYRSLSNSSTATGTTVIECIKSPESSESQTSQSESRATTPSLPSVDNEFKLASPEKLAGLASPSSGYSSQSETPTSSFPTAFFSGPLSPGGSKRKPKVPERKSSLQQPSLKDGTISLSKDLELPIIPPTHLDLSALHNVLNKPFHHRHPLHVFTHNKQNTVGETLRSNPPPSLAITPTILKSVNLRSINKSEEVKQKEENNTDLPYLEESTLTTAALSPSKIRPHTANKSVSRQYSTEDTILSFLDSSAVEMGPDKLHLEKNSTFDVKNRCDPETITSAGSSLLDSNVTKDQVRTETEPIPENTPTKNCAFPTEGFQRVSAARPNDLDGKIIQYGPGPDETLEQVQKAPSAGLEEVAQPESVDVITSQSDSPTRATDVSNQFKHQFVMSRHHDKVPGTISYESEITSVNSFPEKCSKQENIASGISAKSASDNSKAEETQGNVDEASLKESSPSDDSIISPLSEDSQAEAEGVFVSPNKPRTTEDLFAVIHRSKRKVLGRKDSGDMSVRSKSRAPLSSSSSSASSITSPSSNVTTPNSQRSPGLIYRNAKKSNTSNEEFKLLLLKKGSRSDSSYRMSATEILKSPILPKPPGELTAESPQSTDDAHQGSQGAEALSPLSPCSPRVNAEGFSSKSFATSASARVGRSRAPPAASSSRYSVRCRLYNTPMQAISEGETENSDGSPHDDRSSQSST
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 using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MFRSVLRLAQVSTRFNQIVSAKVVPKQAVSFTPLSVKKYSSSAVAVTDEEHTAAWISFFERKDLDYVIFKIGFMNLYQEDSVPEPAIVQAALYACRRINNLPLAMRVLEMVKNKCDDRQDIYDYIVQELRPSLDDLGLKTVEEYGLDQVLD
The following text describes a protein:
Function:
Orphan receptor.
Miscellaneous:
MISCELLANEOUS: Most adhesion GPCRs undergo autoproteolysis at the GPS domain. ADGRF2 is not autoproteolyzed at the GPS motif because of the lack of a consensus catalytic triad sequence within GPS region of the GAIN-B domain.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MGLTAYGNRRVQPGELPFGANLTLIHTRAQPVICSKLLLTKRVSPISFFLSKFQNSWGEDGWVQLDQLPSPNAVSSDQVHCSAGCTHRKCGWAASKSKEKVPARPHGVCDGVCTDYSQCTQPCPPDTQGNMGFSCRQKTWHKITDTCQTLNALNIFEEDSRLVQPFEDNIKISVYTGKSETITDMLLQKCPTDLSCVIRNIQQSPWIPGNIAVIVQLLHNISTAIWTGVDEAKMQSYSTIANHILNSKSISNWTFIPDRNSSYILLHSVNSFARRLFIDKHPVDISDVFIHTMGTTISGDNIGKNFTFSMRINDTSNEVTGRVLISRDELRKVPSPSQVISIAFPTIGAILEASLLENVTVNGLVLSAILPKELKRISLIFEKISKSEERRTQCVGWHSVENRWDQQACKMIQENSQQAVCKCRPSKLFTSFSILMSPHILESLILTYITYVGLGISICSLILCLSIEVLVWSQVTKTEITYLRHVCIVNIAATLLMADVWFIVASFLSGPITHHKGCVAATFFVHFFYLSVFFWMLAKALLILYGIMIVFHTLPKSVLVASLFSVGYGCPLAIAAITVAATEPGKGYLRPEICWLNWDMTKALLAFVIPALAIVVVNLITVTLVIVKTQRAAIGNSMFQEVRAIVRISKNIAILTPLLGLTWGFGVATVIDDRSLAFHIIFSLLNAFQVSPDASDQVQSERIHEDVL
The following text describes a protein:
Function:
Required for peroxisome biogenesis. Necessary for the developmental elimination of obsolete peroxisome matrix proteins. May be involved in the ubiquitination of PEX5, targeting it for recycling. Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Subcellular Localization:
Peroxisome membrane; Peripheral membrane protein.
Sequence:
MQASRARLFKEYKEVQREKVADPDIQLICDDTNIFKWTALIKGPSETPYEGGVFQLAFSVPEPYPLQPPQVRFLTKIFHPNVHFKTGEICLDILKNAWSPAWTLQSVCRAIIALMAHPEPDSPLNCDSGNLLRSGDVRGFNSMAQMYTRLAAMPKKG
The following text describes a protein:
Function:
May be involved in environmental stress response.
Sequence:
MVNETEALPCEGGCGLYGTRVNNNLCSLCYKKSVLQHSPALRFEPETEQSQCCPPTNSPAVEEEPVKKRRCGICKRKVGMLGFKCRCGHMFCGSHRYPEEHSCPFDYKQSGRLALATQLPLIRADKLQRF
The following text describes a protein:
Function:
Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MADKPDMGEIASFDKAKLKKTETQEKNTLLTKETIEQEKRSEIS
The following text describes a protein:
Function:
With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MSWIREGELTIIERFCANIIKAGPMPKHVAFIMDGNRRYAQKCHVERQQGHSQGFDKLAQTLRWCLNLGIREVTVYAFSIENFKRSKEEVDGLMDLARQKFSRLLEEQENLKKHGVCIRVLGDLPLLPLDVQELIAQAVMATRNYNKCFLNVCFAYTSRHEISNAVREMAWGVEQGLLEPSDVSESLLDKCLYTSNSPDPDLLIRTSGEVRLSDFLLWQTSHSCLVFQSVLWPEYSFWNLCEAILRFQMNYNALQKARDSYMEERKQQQMERDQAYVTKKLQQEGFASHGDSRRRRTLLQKCTAMREERIQGFLQALEHKRADFFERLCTVSA
The following text describes a protein:
Function:
Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MGKIKEINDDEDKYNIAILHPDLGIGGAERLIVDVALGLKSCGHKIDVYTSRHDPTRCFRETANGDLNVKVCGDYFPRHFLNRFMVICAIIRNLLAAIHIIFFSKKHLSPLFKWFTKSKVLFYCHFPDKLLTSRNSTIKRLYRVPIDLFEEWTTSCADEILVNSNFTSSIFKKSFTHIKKSPNVLYPCLNTVEFDKTKQSSDFSNQTKYNNKPISLENKEFFLSINRYERKKDLKLALDSFSVVYSNNPNKDIYLVFAGGYDTGLKENVEHLEELKEKTKEYGLEDRVFFLCSINEGQKQWLLLNCCCLVYTPSFEHFGITPLEGMYASKPVIAVNNGGPLETVVDSKTGFLCPPDQKDFSEAFQKIISDPLHSKKMGFAGKQRVNEKFSFKPFANNLNTISNNLMIN
The following text describes a protein:
Function:
Involved in the fatty acid remodeling steps of GPI-anchor maturation where the unsaturated acyl chain at sn-2 of inositol phosphate is replaced by a saturated stearoyl chain. May catalyze the first step of the fatty acid remodeling, by removing the unsaturated acyl chain at sn-2 of inositol phosphate, generating a lyso-GPI intermediate. The fatty acid remodeling steps is critical for the integration of GPI-APs into lipid rafts; Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MAWRTARLLLLAGAAALASGSQGDREPVYRDCLLQCEERNCSGGALKHFRSHQPIYMSLAGWTCRDDCKYECMWVTVGLYLQEGHKVPQFHGKWPFSRFLCFQEPASAVASFLNGLASLVMLCRYRASVPASSPMYPTCVAFAWVSLNAWFWSTVFHTRDTDLTEVSASHSLLCLGQPRRSPGEVGQRRLFLLRTHSVSGSPEHLPYAGHFRSKLDYFCASTVILHSVYLCCVRTVGLQRPAVASAFRALLLLMLTAHVSYLSLVHFDYGYNLAANVAMGLVNAAWWLAWCLRNRRRLPHVRKCMVVVLLLQALSLLELLDFPPLFWVLDAHAIWHISTIPVHVLFFSFLEDDSLYLLKESEAKFKLA
The following text describes a protein:
Function:
Possesses 5'->3' exoribonuclease activity. Required for the processing of nuclear mRNA and rRNA precursors. May promote the termination of transcription by RNA polymerase II (By similarity). Essential for vegetative cell growth and chromosome segregation.
Subcellular Localization:
Nucleus.
Sequence:
MGVPALFRLLSRKFAKVITPVIEAPTEKLPDGTEIEPDLSLPNPNGVECDNLYLDMNGIVHPCSHPEDRPAPETEDEMMVAVFEYTDRILAMVRPRQLLFIAIDGVAPRAKMNQQRSRRFRSSREAALKEEELQAFIEEAKQQGIPIDENATKKKSWDSNCITPGTPFMDTLAKSLRYYIINKLNSDPCWRNVRFILSDASVPGEGEHKIMEFIRSQRVKPEYDPNTHHVVYGLDADLIMLGLATHEPHFRVLREDVFFQQGSTKKTKEERLGIKRLDDVSETNKVPVKKPFIWLNVSILREYLEVELYVPNLPFPFDLERAIDDWVFFIFFVGNDFLPHLPSLDIRDGAVERLTEIWRASLPHMGGYLTLDGSVNLARAEVILSAVGNQEDDIFKRLKQQEDRRNENYRRRQQRESNQESESYVDNVVIQRSVETQSTEVVTSSKSTSVDTKPPKKTQKIDAPAPVDLVNLSEKTSNRSLGATNRELINNRAANRLGLSREAAAVSSVNKLAASALKAQLVSNETLQNVPLEDSIASSSAYEDTDSIESSTPVVHPIDTKVSNVGQKRKAPDSTEENENTDTVRLYEPGYRERYYEQKFHISPDEPEKIREAVKHYVHGLCWVLLYYYQGCPSWTWYYPYHYAPFAADFKDLASIDVKFELNQPFKPYEQLLGVLPAASKNNLPEKLQTLMTDENSEIIDFYPENFTIDLNGKKFEWQGVALLPFIDENRLLNAVSKIYPQLTEEESKRNEDGSTLLFISEHHPMFSELVKQLYSKKRQGKPLKLSGKMAHGLFGKVNTNDSVIPNVSVQCPIDVTSADALQKYGSIDDNQSISLVFEVPKSHFVHKSMLLRGVKMPNRVLTPEDINQVRAERSFSSRRNNGNSYRGGHQSYGVRRSYQSQSYSSRQSYTGVTNGFANGGVQPPWSGNGNFPRSNASYNSRGGHEGYGGRSRGGGYSNGPPAGNHYSSNRGKGYGYQRESYNNNNRNGYY
The following text describes a protein:
Function:
Inhibits cell division by binding directly to FtsW to prevent the final constriction of the FtsZ ring.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MIRVARESFALVSVIGFVWMMCTVANLVA