lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Plant specific protein that enhances G-box-binding factor (GBF) DNA binding activity. May function as a nuclear chaperone or lever and regulate the multimeric state of GBFs. May contribute to bZIP-mediated gene regulation. Is able to refold denatured rhodanese in vitro. Reduces DNA-binding activity of BZIP16, BZIP68 and GBF1 under non-reducing conditions through direct physical interaction. Acts as a negative co-regulator in red and blue light-mediated hypocotyl elongation. Functions to promote hypocotyl elongation during the early stages of seedling development by regulating the repression effect by BZIP16 and the activation effect by BZIP68 and GBF1 on LHCB2.4 expression. Enhances transcriptional activity of LBD18 in the EXP14 promoter. May act as a transcriptional coactivator of LBD18.
Subcellular Localization:
Nucleus.
Sequence:
MSRISGDGGSRVSIPADLLQTIQNIREVTGKQHSDEDIFSVFKECFSDPHETTQKLLYLDTFHEVRSKRERKKENLVPNTQGRGRTGRKNFASSYTDASNGRSAAFKKQSGANHIIGGSGTASSAPNNARNDTKPSSIMAPNPISLPSGISNQKIQDAIISPVDKVDTEEQPLSKATSSSKDVVEPDKSKESSVSVAVSDSVVENDTQYAVVETFQIPQQSERVIKSEVAASKCKNESLLKSDVGERPHVTFPVHIQVAKMLENGLTFGSFDSNFVREASSDKFTIGCDDSNIESSHGTAASARKDISTFSQDKNHEISNSAAQNELTLQPDQTVLPEEGSEGDKVKNEVLPITDTHQAAKCDAPPISYPDQYSLAAAQQAMHLYRQQYSLNYFPYGPYFPPYYMPQPYIHQYLSPNGFQQQSYLPPGDDAPAPPGAELPLTHIKPGSDIGNSPPTTIPFSYTSYAFNHIPSAATINATHKEEKKENMYTTGPLSLANLQASPMYNLSLQGQPIAFPTMQAGIRGLYQQTQPILAPLSISARTEPIGPSHVTNQQPQAARTNLGNNY
The following text describes a protein:
Function:
Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.
Subcellular Localization:
Cytoplasm. Dynein axonemal particle.
Sequence:
MASGREKLEDLNMTQDELQRFEKAFKSEEFRKLFAEYAEEISDPENRKRYEAEITAMERERGTDVTFINPEPHYVIKTSLDGEKKCFINICANEHIERPTSQPCVQGEGPSRRMGQTWSVPHSLTPGREDLDKDKQRCMVYDVVFHQETLQKAAADKRFKQMVHDIAFSALERQFQVKLDKTNIKIPKMKYKGNPTATVMRKPSSDGPQATPDNDDDPIKFPYPYSPSSENTETAKQTQSPSKSKEEKEPEKKQDFTVPKYTIKHRSEFDIQNFREAPDAAPSTRPKELVVDIDFPLLKSAAKLELDIFEKQLRVESKKPAYKLDISLPYPVDENKGGAKFDKSKRRLTVTLVVKPAPEADLPFTAGRTEDKQLVEEVTEVQVGEKAEENHIQDGENIIPTGVSEVEPDSRSGNPAAAQTEEIGSGPASDVGVETATDTANTSDKDIFVEEDELQSSSTSLDLPPDSATPVSTAPVRATPAPPTCPDYTFRQDEDSMTIVIHVPNIIEKSISKTYSTSSYIISVQFQAAGTAGLQYYQLFVVLLDGNTVVRGRTSMDVSPHNAVLLLHKDDSCKGLWASFKAGVDIMNLEEKQFLTEASVEAAVQAVVSEGQAEAADTIGVKVTEASEDKLAIELTKTTGVQKQEMGEKPTPTGVTVDEDNLSSQTSSGKSSIKERVSEMIEAGKKGEGLDSDDDDDSGNALGTEAVPEKSVSGNGVESPAETVQDGENVLLKDNDTDVPTGKTKRRRRKKKGKTQGQSQDSNAGGKTGPGTSGEEGGLLEVKEEEERKTDTSSKPAISNQSTNVSQSKKGASTQDTIGFDKTIINTGRERKNSGKKSVTFSDKVEIHKLDEKNGKSKKKQKSKKDNQNAQKVANGHGKTEGEPTTADFGEAIVSEAGTVTGVSNTESMSVSESEDKLAGQDEVGDGDVKKEGSDPAKKKPKPQAVDALTIRDVKTGEEEVVTEHRAECAVQFTNKVMFELD
The following text describes a protein:
Function:
E2-dependent E3 ubiquitin-protein ligase that functions as a RIGI coreceptor in the sensing of viral RNAs in cell cytoplasm and the activation of the antiviral innate immune response. Together with the UBE2D3, UBE2N and UB2V1 E2 ligases, catalyzes the 'Lys-63'-linked polyubiquitination of RIGI oligomerized on viral RNAs, an essential step in the activation of the RIG-I signaling pathway. Through a ubiquitin-independent parallel mechanism, which consists in bridging RIGI filaments forming on longer viral RNAs, further activates the RIG-I signaling pathway. This second mechanism that synergizes with the ubiquitin-dependent one would thereby allow an RNA length-dependent regulation of the RIG-I signaling pathway (Probable). Associated with the E2 ligase UBE2N, also constitutively synthesizes unanchored 'Lys-63'-linked polyubiquitin chains that may also activate the RIG-I signaling pathway.
Subcellular Localization:
Cytoplasm. Cytoplasm, Stress granule.
Domain:
The B30.2/SPRY domain mediates the interaction with the substrate RIGI; The coiled-coil domains mediate homodimerization and the bridging of viral RNA-associated RIGI filaments.
Sequence:
MAGLGLGSAVPVWLAEDDLGCIICQGLLDWPATLPCGHSFCRHCLEALWGARDARRWACPTCRQGAAQQPHLRKNTLLQDLADKYRRAAREIQAGSDPAHCPCPGSSSLSSAAARPRRRPELQRVAVEKSITEVAQELTELVEHLVDIVRSLQNQRPLSESGPDNELSILGKAFSSGVDLSMASPKLVTSDTAAGKIRDILHDLEEIQEKLQESVTWKEAPEAQMQGELLEAPSSSSCPLPDQSHPALRRASRFAQWAIHPTFNLKSLSCSLEVSKDSRTVTVSHRPQPYRWSCERFSTSQVLCSQALSSGKHYWEVDTRNCSHWAVGVASWEMSRDQVLGRTMDSCCVEWKGTSQLSAWHMVKETVLGSDRPGVVGIWLNLEEGKLAFYSVDNQEKLLYECTISASSPLYPAFWLYGLHPGNYLIIKQVKV
The following text describes a protein:
Function:
Catalyzes the trans-addition of the three molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl diphosphate.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MEAQNIFLYLLIVFLSLHFVFTTLKGRLSPANTRRLIRLLHIPIKSPVAAAIFARKDTREFLDSSIKLVNEEDDFGFSFDFKPYMISKAETINRALDEAIPLIEPLNIHKAMRYAILAGGKRVRPILCLAACELVGGEERLAIQAACAVEMIHTMSLIKDDLPCMDNDDLRRGKPTTHKVFGESVAILSGGALLALAFEHLTEADVSSKKMVRAVKELAKSIGTKGLVAGQAKDLSSEGLEQNDVGLEDLEYIHVHKTGSLLEASAVIGAVIGGGTEKEIEKVRNFARCIGLLFQVVDDILDETKSSEELGKTAGKDKVAGKLTYPKVIGVEKSKEFVEKLKRDAREHLQGFDSDKVKPLIALTNFIANRNH
The following text describes a protein:
Function:
A dominant-negative regulator of endogenous whiB2 expression. Low level expression in liquid culture in M.smegmatis leads to elongated and highly branched cells, with multiple nucleoids, similar to the effects seen in deletion experiments for whiB2 in M.smegmatis, as well as loss of acid-fastness. High level expression is lethal. Represses expression of endogenous whiB2. The apo-form binds to the whiB2 promoter found in M.tuberculosis. M.smegmatis cells expressing this protein will not grow on plates. Low level expression in M.smegmatis leads to superinfection exclusion, possibly via modification to the cell wall.
Subcellular Localization:
Host cytoplasm.
Sequence:
MHMHMGGDPSAICAQTDPELWFPDKGQSTRDAKRMCMRCPLLDECRALALRDPHLVGVWGGLSAQERRRIRKGASA
The following text describes a protein:
Function:
Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues.
Subcellular Localization:
Secreted, cell wall. Secreted, extracellular space, apoplast.
Sequence:
MEFRISGCVQSVMLLLCLSMVAAAASQSIADRFYPWTDNVKYPSSSRMQLTLDQRYAAGAVSKKSWTYGEWSVCMKLPAGNSAGTVTTFYMMSPQGDAHCEYDMEFLGNSTGQPYLLHTNVFVGGQGGREEQTYLGFDPTADFHCYKIRWSKDLVAFFVDDVVVRIFRNLEDKVAGFQYCKFKALGMHVSIWDGSSWATQGGRVPINWNSAPFVATYENFQMSGCEVNSIDKNAPVGCQSHPSATGIPVTRDQVLQMQARKASMMKYDYCTDKARYKVTPPECPFNNVYM
The following text describes a protein:
Function:
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Sequence:
MNTLKKNGEFQNIYNLGNKYFGNYSLIFFNKNKLEYSRFGFIASKKVGKAFCRNRIKRLFREYIRLNINKINDNYDIIIVAKKKFGENIEDLKYKDIEKDLNRVFKNSKII
The following text describes a protein:
Function:
Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting.
Miscellaneous:
MISCELLANEOUS: Present with 8528 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MVVLNPNNWHWVDKNTLPWSKDYLNGKLTSLSTVSSDGKSKIELTQVSSITGDSNVSQRKGKPICYFDLQLSMNVKVTNLDTNKDDEDDDGILADGKLEIPEFMHDESDIPILSQGFDAFDGLVRSEFVPKVVETLLKYQDDLIKEHSKDIQV
The following text describes a protein:
Function:
[CLE33p]: Signaling peptide involved in the regulation of root colonization by arbuscular mycorrhizal (AM) fungi. Moves from root to shoot to function with the receptor kinase SUNN, in a signaling pathway that repress strigolactone biosynthetic genes and strigolactone content in the roots, and consequently reduces the promotion of further colonization by AM fungi.
Miscellaneous:
MISCELLANEOUS: Roots of plants overexpressing CLE33 exhibit normal growth, but reduced levels of colonization by arbuscular mycorrhizal (AM) fungi.
Subcellular Localization:
[CLE33p]: Secreted, extracellular space.
Sequence:
MASWRMLCFVLLFTSILICHDARPLPSSLSSSNGSPAFVESVKQVVKEIMRRKQLLGTQYSTNRLSPSGPDPHHH
The following text describes a protein:
Function:
Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MAVNVYSTSVTIENLSRHDMLAWVNDSLQLTYTKIEQLCSGAAYCQFMEMLFPGCILLKKVKFQAKLEHEFIHNFKVLQAAFKRMNVDKIIPVERLVKGKFQDNFEFVQWFKKFFDANYDGKEYDPIQARQGQDVAPPPNPGEHFSHKPKRTGPSGPQRTSPTVPKNMPTPQRVTTTIRKNPTHARNGGSDAEITELNQQLMELKLTVDGLEKERDFYFSKLRDIELICQDHEAESSPVISRIIDILYATEDGFAPPEDDEIDEQSHLDQDEY
The following text describes a protein:
Function:
Cleaves A-5'-PPP-5'A to yield AMP and ADP. Can cleave all dinucleoside polyphosphates, provided the phosphate chain contains at least 3 phosphates and that 1 of the 2 bases composing the nucleotide is a purine. Is most effective on dinucleoside triphosphates. Negatively regulates intracellular dinucleoside polyphosphate levels, which elevate following heat shock.
Sequence:
MSQAVYFSHFLVTNQVFYRTRYSYALVNLKPLVPGHVLIAPLRPTCVRLRDLTPEEHSDYFQTLQVVHQFIQAEFKAAALNIAIQDGPEAGQTVPHLHTHLIPRYADNNIGDAIYDHLDRWSFEDQLADWQRRRAAYCGDEAARRELAKPDDVRKPRTADDMTAEARALSAGLQSFLADHPALAPK
The following text describes a protein:
Function:
Calcium-regulated non-lysosomal thiol-protease.
Subcellular Localization:
Nucleus.
Sequence:
MKSVIPWPYTHTHTHTHTHTHTQCYSLVLHTRTHTHTHTHTHTHSLTPACASRVASNSRRARCHMRTSRDYALLSPAQSREPWRSRARRHSPGQAPPPHVLSRARLLPPHLRRNARGPGCACAVEPVGGAGECGCLDGGRPRGRRVSQRAPARKAGSRPSAAEDKLGRSLHGVRGSASRRCCGRRKAWCVGPSLPPGLPPRVRGSGAMDATALERDAVQFARLAVQRDQEGRYSEAVFYYKEAAQALIYAEMAGSSLEHIQEKINEYLERVQALHSAVQSKSADPLKSKHQLDLERAHFLVTQAFDEDEKGNVEDAIELYTEAVDLCLKTSYETADKTLQNKLKQLARQALDRAEALSEPLTKPLCKIKSTNNKPKPPPTRAHFPLGTSPFLERPQPFISPQSCDAQGQRYTAEEIEVLRTTSKINGIEYVPFMSIDLRERFAYPVPFCDRWGKLPLSPKQKATFSKWVRPEDLTNNPTMIYTVSSFSIKQTIVSDCSFVASLAISAAYERRFNKKLITSIIYPQNKDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHKGELLCSYSNNKSELWVSLIEKAYMKVMGGYDFPGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYQRFHKGDVLITASTGMMTEAEGEKWGLVPTHAYAVLDIREFKGLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQKYLNFDPRTAQKIDNGIFWISWDDLCQYYDVIYLSWNPGLFKESTCIHSTWDAKQGPVKDAYSLANNPQYKLEVQCPQGGAAVWVLLSRHITDKDDFANNREFITMVVYKTDGKKVYYPGDPPPYIDGIRINSPHYLTKIKLTTPGTHTFTLVVSQYEKQNTIHYTVRVYSACSFTFSKIPSPYTLSKQINGKWSGQSAGGCGNFQETHKNNPIYQFHIEKTGPLLIELRGPRQYSVGFEVVTVSMVGDPGPHGFQRKSSGDYRCGFCYLELENIPAGIYNIIPSTFLPKQEGPFFLDFNSIIPIKTTQLQ
The following text describes a protein:
Function:
Binds double-stranded RNA. May be involved in RNA-mediated silencing.
Sequence:
MYKNQLQELAQRSCFNLPSYTCIREGPDHAPRFKASVNFNGEIFESPTYCSTLRQAEHAAAEVSLNVLSSRVPSKSLTAKILDETGIYKNLLQETAHRAGLDLPMYTSVRSGSCHFPGFSCTVELAGMTFTGESAKTKKQAEKNAAIAAWSSLKKMSSLDSQDEEKEQEAVARVLSRFKPKEVRRRETTNQWRRRTSQQDSNKDLLIERLRWINLLTNQASSSSSTSTPNQHKNSSFISLIPPPPPPKSSKILPFIQQYKDRSSQEAKTETATEMINSKAKVNETSTRLSKQMPFSDMNRYNFVGGCSVNPYSLAPAVQMRSVIPVFAAPPPKPNPNLNPSSLSSSVNEFTSSNNSCSVLNTPGLGGQEKKNLTREMIKLGSESRILDQTHDS
The following text describes a protein:
Function:
Antimicrobial peptide. Has activity against the Gram-positive bacterium S.aureus (MIC=6 uM) and the Gram-negative bacterium E.coli (MIC=3 uM). Lacks hemolytic activity against human erythrocytes.
Subcellular Localization:
Secreted.
Sequence:
MFTLKKSLLLLFFIGVIKLSLCEEERNADDDERRDDPDEMDVEVENRSAVGRHGRRFGLRKHRKH
The following text describes a protein:
Function:
GPI inositol-deacylase that catalyzes the remove of the acyl chain linked to the 2-OH position of inositol ring from the GPI-anchored protein (GPI-AP) in the endoplasmic reticulum. Initiates the post-attachment remodeling phase of GPI-AP biogenesis and participates in endoplasmic reticulum (ER)-to-Golgi transport of GPI-anchored protein.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MRLVVYAFFAFALGLLLVGLRELLFGFEENRCSMTYMFEYPEYRRVQLPRRVARQYPSYGLYLYGEGAYAQETRGLKLTGAPVLFLPGNAGSYKQARSLGSVALRKAENLERQIHLNVFTIDFNEELVALYGGSLRRQTQFLHESIKAILRLYKDRPDPPTSVVLVGHSMGGVVARALFTLARFHPRLVSLIITQASPHQAPVLSLDPYILEFYSTVRQGWNKRAEDLRNVTVLSVGGGNLDFQVLSGLTALSCPIDDLNKISVVATAVPRTWLSTDHISIVWCKELVLATVRAFFDLIEPETGQFTESPEERLSVLNYHFFRHPVLPPGEVQGASVTFSAPPEAWKEVNTLRLFYSAPKEAQVKYFLFGLSSRRKAYSHFYCRSNNMEMTSWLYGCTQMSGSMCVQAVDLSSDTELLPAYKTVAVKISKLMSVSHLIIDASNPSGAQFVVECELQREESLTVSVQVPHLLSFGLTVTDVSINSSGLLHTLQLQDFHQVYQAFRITIMSHCKTNKDRLPSVYRVSVPWFREDSFAMSSTPSVSEIFSMLHSSRPDNTSSAMLQLHTAPNCQYKVSIRTSFPKVLGQILRFCGPLLPVYCALALLLMIRVQLSSVRRSGRPVELQEAMSKSLEIHKLELPVLLLMLLLRQSWFQDVWTSLGLPGVDALPLNTVEDLSHEKASVQEWPRLVSPLLCVFGAAIAFWGSTVLRMSVCFLSFIVAPLHRPSVSRDCGTFGLHTQIVLMVSLGVLGSLTCGSLALMLCCLLHLYRVLRLQMTERSLSHMLNLAPQKASHNTENGFNGNDHHSNGKECNGSALLSESVLQDVRDDLQLHLSVSTVLTLTMMLCAPSLIHWKHNLRYWLHLDPDPCWPHTVPLLISSVMLINCNTNSLLRSKLMLNLTLRLLLLLCVGLLAFCPLHIYRVTHFLSAALSLLVCSCYF
The following text describes a protein:
Function:
Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSEYQFPKESMGTTLLAIQCTDGVVMASDSRTSSGSFIPNRATNKITEIQPKIFAARCGNAADTQFLARAVKNYLNALNITRENTDDSTILVASNVIRSLIVRYRQYLSAGVIVGGWDSAGPQVYSIEVSGMAIKKKIASNGSGSTYIQAYIDQNYREDMTMEEATKFAIAAVTGAIIRDGSSGGVVNIVQINADGAKRMTVRPAQQPFNYDIVKG
The following text describes a protein:
Function:
Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
Sequence:
MHVAVRHLVQILQFLPMKTKQSIRSGRVSLSSISLMGPEKIGADHEWTTLDLSSDAVKLLVEHDYEGDGKFRYANPGDFLRWALRPPGYYQSWHIGIRVKKSLVACLFGVPARIIVRDNEAVKVAAVRFLCVQKDFRSKGLVPIMIKEMIRRVNLKDIWQGAFCTDLLVATPVTTIRQWIRMLNPANVSKFLGEAMSIKDATKLYELPNAPVTPGFRKMVQSDVHAVTELLRVYLLEFEVAAEFHPETHVVTDCCSFYTISFTVGGRKNNKFDIFHAKDVMDNKTFFEQLKFEEVGAQNHFYLFNQRLRTGLQPSQLGLTLF
The following text describes a protein:
Function:
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Sequence:
MDEHFIKIHKWLYPVSWIYGAVVTVRNKLFDWGFLRSKSFGVPVICIGNLSVGGTGKTPHTEYLIKLLRDNYHVAVLSRGYKRHSRGYVLATPQSTARSIGDEPYQMHTKFPSVTLAVDENRCHGIEQLLSIKEPSIEVVLLDDAFQHRYVKPGLSILLTDYHRLFCDDTLLPAGRLRESVNGKNRAQIVIVTKCPQDIKPIDYNIITKRLNLYPYQQLYFSSFRYGNLQPVFPSANSEIDSTVNELPLSALTNTDILLVTGIASPAPILEELKMYTDQIDSLSFDDHHHFSHRDIQQIKERFGKLKGEHKLIVTTEKDATRLIHHPVLSEELKPFIYALPIEIEILQNQQDKFNQHIIGYVRENTRNSSFSERENAHQS
The following text describes a protein:
Function:
Suppresses cannabinoid receptor CNR1-mediated tonic inhibition of voltage-gated calcium channels.
Sequence:
MASARTEERAFKTSLSLTRSEDSSPVFFKVDGERFKETRTLKLQVDSKYKVVLEFRPPQTLAEAAISGGSLKAELKKIDENCSVYEGLFSTQGMPSSKSKDRAYIVLSLKFNTGHEMNVQVQSKLYSVKDNTHVTWGACLKSLDFECKMRDGQSFVSIQKTTFR
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 (By similarity).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Domain:
In NdvA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Sequence:
MSIFSLYTRVLELLGKEARLGWLLAFANLLLAASQFAEPVLFGRIVDVLSGKSVAGSSSAWPFLAAWVAFGLFTIACSALVALQADRLSHRQRQAVLTDYFEHILQLPLTFHSGTHSGRLMKVMLNGTDALWRLWLGFFREHFAAILSVVVLLPLSLYLNWRLAILLFVLCIVFTALTTFVVRRTFGMQMAVEEHYSELSARASDALGNVALVQSFVRVESEVQGLRSVANQLLEAQMPVLSWWALVTVITRASTTITVLAIFTLGIALHDQGLTSVGEIVMFVSFATLLIQKLEQVVSFINNVFMEAPRLREFFNVLDAVPAVHDRPDAIDAGRLSGLVEFNDVTFSYDGKRPAVEDLSFTALPGQTVALVGPTGAGKSTAIALLHRAFDPQSGFIRIDGMDVRGVTLTSLRRNIGVVFQEALLFNRSIAENLRVGKPDATEAEMRKAAERAQALEFIERSGGFETNAGERGRMLSGGERQRLSIARALLKDPPILILDEATSALDAVTEVKVNAALDEVMRGRTTFVIAHRLATIRNATRILVFENGRVTESGTFDELVAKGGHFAELARAQFMVQEQSRANTRASVTAAETIATAAKSP
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MALWSATKFVAKGGVLGGAVYLTTKNGIWGENPDTGIRAIKQFSKSVDGTLGGEYMGKVTQLPQLNATEKWNKAVSYSIDCVADSPAIAAKAYKTIKDKII
The following text describes a protein:
Function:
Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation.
Subcellular Localization:
Secreted.
Sequence:
MMKTKSEVLIFFFTLVLLLSMASSVILREDGFAPPKPSPTTHEKASTKGDRDGVECKNSDSEEECLVKKTVAAHTDYIYTQDLNLSP
The following text describes a protein:
Function:
Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle.
Subcellular Localization:
Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Golgi apparatus, trans-Golgi network.
Sequence:
MEPRSMEYFSAQVQQKDVGGRLQVGQKLLLYLSAPGAIPDLEKDLGRLGETVDALTGWVGSSNYRVSLMGLEILSAFVDRLSTRFKSYVVMVIVALIDRMGDAKDKVRDEAQTLILKLMDQVAPPMYIWEQLASGFKHKNFRSREGVCLCLIETLNIFGTQPLALSKLVPHLCILFEDSNSKVRDAAVLAMVEIYRHVGERVRVDLYKRGIPPARLEMIFAKFDEVQNSGGMILSVCKDKSFDDEESVDGNRPSSAASAFKVPAPKTSGNPVNSARKPGSAGGPKVGGASKEGGAGAVDEDDFIKAFTDVPTVQIYSSRELEETLNKIREILSDDKHDWDQRANALKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLSTVLGNKFDHGAEAIVPTLFNLVPNSAKVMATSGCAAIRFIIRHTHVPRLIPLITSNCTSKSVPVRRRSFEFLDLLLQEWQTHSLERHAAVLVETIKKGIHDADAEARVEARKTYMGLRNHFPGEAETLYNSLEPSYQKSLQTYLKSSGSVASLPQSDRSSSSSQESLNRPFSSKWSTANPSTVAGRVSTGSSKASSLPGSLQRSRSDIDVNAAAGAKAHHAAGQSVRSGRLGAGALNPGSYASLEDTSDKMDGATSEDGRVRAKLSAPLAGMGNAKTDSRGRSRTKMVSQSQRSSSPDKNEGSQSANTIGAGSRSGSPGRVLTTTALSTVSSGVQRVLINSASAPKRSKIPRSQGCSREASPSRLSVARSSRIPRPSVSQGCSREASRESSRDTSPVRSFQPLASRHHSRSTGALYAPDVYGASGPGFGISQSSRLSSSVSAMRVLNTGSDVEEAVADALLLGDIRTKKKPARRRYESYGMHSDDDANSDASSACSERSYSSRNGSIPTYMRQTEDVAEVLNRCASSNWSERKEGLLGLQNLLKNQRTLSRVELKRLCEIFTRMFADPHGKVFSMFLETLVDFIQVHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRESFPNDLQFNILMRFTVDQTQTPSLKVKVAILKYIETLAKQMDPGDFINSSETRLAVSRVITWTTEPKSSDVRKAAQSVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLRNTGNGTQGSMGSPLTRPTPRSPANWSSPLTSPTNTSQNTLSPSAFDYDTENMNSEDIYSSLRGVTEAIQNFSFRSQEDMNEPLKRDSKKDDGDSMCGGPGMPDPRAGGDATDSSQTALDNKASLLHSMPAHSSPRARDYNPYNYSDSISSFNKSALKEAMFDDDADQFPDDLSLDHSDLVAELLKELSNHNERVEERKIALYELMKLTQEESFSVWDEHFKTILLLLLETLGDKEPTIRALALKVLREILRHQPARFKNYAELTVMKTLEAHKDPHKEVVRSAEEAASVLATSISPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERVSKETLNLLLPEIMPGLIQGYDNSESSVRKACVFCLVAVHAVIGDELKPHLSQLTGSKMKLLNLYIKRAQTGSGGADPTTDVPGQS
The following text describes a protein:
Function:
Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.
Domain:
The C-terminal part (437-563) is required for the association with the endoplasmic reticulum lumen membrane.
Sequence:
MRLRTAIATLCLTAFTSATSNNSYIATDQTQNAFNDTHFCKVDRNDHVSPSCNVTFNELNAINENIRDDLSALLKSDFFKYFRLDLYKQCSFWDANDGLCLNRACSVDVVEDWDTLPEYWQPEILGSFNNDTMKEADDSDDECKFLDQLCQTSKKPVDIEDTINYCDVNDFNGKNAVLIDLTANPERFTGYGGKQAGQIWSTIYQDNCFTIGETGESLAKDAFYRLVSGFHASIGTHLSKEYLNTKTGKWEPNLDLFMARIGNFPDRVTNMYFNYAVVAKALWKIQPYLPEFSFCDLVNKEIKNKMDNVISQLDTKIFNEDLVFANDLSLTLKDEFRSRFKNVTKIMDCVQCDRCRLWGKIQTTGYATALKILFEINDADEFTKQHIVGKLTKYELIALLQTFGRLSESIESVNMFEKMYGKRLNGSENRLSSFFQNNFFNILKEAGKSIRYTIENINSTKEGKKKTNNSQSHVFDDLKMPKAEIVPRPSNGTVNKWKKAWNTEVNNVLEAFRFIYRSYLDLPRNIWELSLMKVYKFWNKFIGVADYVSEETREPISYKLDIQ
The following text describes a protein:
Function:
Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.
Sequence:
LTMSSTTRVSFKSSTRSSGARGGVSSSLGVGSLGGLGISSGMSRLSLGGGLGGLRGGAVSLGAGAAGLGLGGVGLGAAGLGIGGGLSLGGAGLGYGGGLSLGGGGLGYGGGLGFGAPGLAFASGGGGGGFAASPAFAMGRTIAAAGLSTGSALAAGPSLGPVTPQLLSRAAEKHTLSSLNDRFSQYMGKVRVLQQENASLEAQLSQFTGGAVIEPDSSSTADHEAQLKDYRTTLENLTLETIKLEIELDNIRGTAHEMKAKFDFEQGVKFQLEADIAAMKRDIETASDLRIDLDAKYQSLNNELDFISKTHEEELAGLQAKLGTTTADTSVSMIEVDTVKSFDISSALNKMRAEYEKSVQQHREEAEAYYKLKMDEIQTVTVKNTEAISTVKVEITASRKELQALNLELQGLISTNLALEQSLAEAQAQSSVGVAEYQAQIASLESSIEVAKADLHKQILAYQELLDVKLALDVEIATYKKLLEGDDFKISDSGSFSESYSFTVIDGGIQKKELRTEETESSIIS
The following text describes a protein:
Function:
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Miscellaneous:
MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MASSTFFSDWNQMLKPRVTSLVLATIIPGLYLASEQSPSGFLIAITLFGTFLMSSASFIFNQVIEKDRDAKMKRTSNRPIPSGRISVVQATLVGIAMMGSSFYVLAVYVNLLTALCAFAALISYVFLYTIFLKPRTTQNIVIGGVAGCVGPLIGYAAIGNSLPVQAWSLFMMIFLWTPAHFWALAIFLKEEYSDADFPMLPVVKGIHQTTKSIFFYTILYSIACVSFYFLESSMGFLYLIVSLIVCIWMGILSYQLIQNPEPQSARKFFFFSILHLFIINITIVVDHLI
The following text describes a protein:
Function:
Dynein-attachment factor required for cilia motility.
Subcellular Localization:
Cell projection, cilium, flagellum. Cytoplasm.
Sequence:
MAKKTAGQLTSIDHGAFDTAALQKELAQALEDDRLYKLTDNMKKRAIHTAANYDEFKNLVACADLKPISQKELRDFSRAERQTNLSFKKKKSRKKPESERRFQPAASTLDAPPATAVDFCRNWTRYLKTTDAKFRYLQITTPERLAEMFKSDIDSDLMAEIVQVLVASWRQKSSDMNPEEPRPATFALSVMEAFAQTARFSLILDFLDDQQTEMVRELFNLVESTVDLHEQDQKVLANLKTKFRLG