lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
With Ku probably forms a non-homologous end joining (NHEJ) repair enzyme, which repairs dsDNA breaks (DSB) with reduced fidelity. Acts as a DNA ligase on singly nicked dsDNA, fills dsDNA gaps (3- or 4- nucleotide gaps, prefers a 5'-phosphate at the gap distal end, prefers dNTPs over rNTPs) , has DNA-directed DNA polymerase activity (templated primer extension) and DNA-directed RNA polymerase activity , adds 1 or 2 non-templated rNTP (or less well dNTP) to ssDNA or blunt-end dsDNA (primer extension). Has 3' resection activity, removing 3'-rNMPs from DNA using its 3'-ribonuclease and 3'-phosphatase activities sequentially. Resection requires a 2'-OH in the penultimate nucleoside position (i.e. a ribo- not deoxyribonucleoside) , although the 3'-phosphatase activity does not, and its specific activity is 16-fold higher on a DNA substrate. On appropriate substrates will extend a DNA primer to the end of the template strand and then incorporate a non-templated nucleotide; The preference of the polymerase domain for rNTPs over dNTPs may be advantageous in quiescent cells where the dNTP pool may be limiting.
Miscellaneous:
MISCELLANEOUS: LigD has variable architecture; domain order can be permutated, domains can be independently encoded, while some bacteria lack the 3'-phosphoesterase domain entirely.
Domain:
The N-terminal 3'-phosphoesterase domain (PE) has 3'-ribonuclease and 3'-phosphatase activities; The central ATP-dependent ligase domain (Lig) functions as an independent domain; The C-terminal polymerase/primase domain (Pol) adds up to 4 rNTPs in a DNA template-directed fashion.
Sequence:
MPSSKPLAEYARKRDFRQTPEPSGRKPRKDSTGLLRYCVQKHDASRLHYDFRLELDGTLKSWAVPKGPCLDPAVKRLAVQVEDHPLDYADFEGSIPQGHYGAGDVIVWDRGAWTPLDDPREGLEKGHLSFALDGEKLSGRWHLIRTNLRGKQSQWFLVKAKDGEARSLDRFDVLKERPDSVLSERTLLPRHGEAATPAARPARRGKSGGKTPMPEWIAPELASLVEQPPRGEWAYELKLDGYRLMSRIEDGHVRLLTRNGHDWTERLPHLEKALAGLGLQRSWLDGELVVLDEEGRPDFQALQNAFEEGRGENILYVLFDLPYHEGEDLRDVALEERRARLEALLEGRDEDPLRFSATLAEDPRDLLASACKLGLEGVIGKRLGSAYRSRRSNDWIKLKCQLRQEFVIVGYTEPKGSRRHIGALLLGLYSPDEERRLRYAGKVGSGFTAASLKKVRERLEPLAVRSSPLAKVPPARETGSVQWVRPQQLCEVSYAQMTRGGIIRQAVFHGLREDKPAREVTGERPAGPPPLRGARKASAGASRAATAGVRISHPQRLIDPSIQASKLELAEFHARYADLLLRDLRERPVSLVRGPDGIGGELFFQKHAARLKIPGIVQLDPALDPGHPPLLQIRSAEALVGAVQMGSIEFHTWNASLANLERPDRFVLDLDPDPALPWKRMLEATQLSLTLLDELGLRAFLKTSGGKGMHLLVPLERRHGWDEVKDFAQAISQHLARLMPERFSAVSGPRNRVGKIFVDYLRNSRGASTVAAYSVRAREGLPVSVPVFREELDSLQGANQWNLRSLPQRLDELAGDDPWADYAGTRQRISAAMRRQLGRG
The following text describes a protein:
Function:
This protein binds preferentially and cooperatively to single-stranded DNA (ssDNS). Involved in mitochondrial DNA replication. Stimulates PIF1 helicase activity.
Miscellaneous:
MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion.
Sequence:
MFLRTQARFFHATTKKMDFSKMSIVGRIGSEFTEHTSANNNRYLKYSIASQPRRDGQTNWYNITVFNEPQINFLTEYVRKGALVYVEADAANYVFERDDGSKGTTLSLVQKDINLLKNGKKLEDAEGQENAASSE
The following text describes a protein:
Function:
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Sequence:
MATESSEGEEDVKLTGGNQVLVVEDDLREMGKKAAWSVSSCKPGNGVSALRDDNLETYWQSDGVQPHLVNIQFQKKVKLQLVVLYVDFKLDESYTPSKISIRAGDGFHNLKEIKTVELVKPTGWVYLLLSGNDPKDTFVNTFMLQIAVLSNHLNGRDTHVRQIKIYGPRPNPIPHQPFQFTSREFITYSIIR
The following text describes a protein:
Function:
Member of the two-component regulatory system DctS/DctR. Probably activates DctR by phosphorylation (By similarity). Essential for expression of dctP.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNKKKLSIRWKITILSYILVIFSFLIGGIVLIGNIQHTEERELKKRLMNTARTVSEMTEVKEALARKKQTEAVRHAVEEIRMINEADYIVVMDMNHIRYTHPVSTSIGKKSEGADEEAAFAEHIYFSEAKGEIGTAVRAFYPVKDQDLNQIGVVLVGKTLPGIADILLHLKRDIAFIVVLTLGFGLAGSFLLARHIKKQMFQLEPHEIVRMYEERTATFHSMNEGVIAIDNRLVITIFNEKAKQIFEVQGDLIGKVIWEVLKDSRLPEIVERNKAVYNEEIRVSGKVIMSSRIPIVMKKKVIGAVAIFQDRTEAAKMAEELTGVRNFVEALRVQNHEHMNKLHTIAGLIQLGKSEKALQLAFQASTEQENVTEFLHRSIQNDAAAGLLLSKIRRGRELGIAVHIDENSSLQQFPEHVDQHDIVVLLGNLIENAFGSFETVQSEDKRIDISIEQTDDILAILIEDNGCGIEPTHMPRLYDKGFTVNKTGGTGYGLYLVKQIIDKGSGTIEVDSHAGQGTSFSIVFPMKGEEAQHGS
The following text describes a protein:
Function:
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum.
Sequence:
MADDQLEGSIKNILEQKSLKWVFVGGKGGVGKTTCSCSLAAQLSKVRGRVLLISTDPAHNISDAFCQKFTKTPTLVEGFTNLFAMEIDSNPSGEGVEMANIEEMLQNAAQNEGGSGNGFAMGKDFLQQFAGGLPGIDEAMSFGEMIKLIDSLDFDVVVFDTAPTGHTLRLLQFPTLLEKVFTKILSLQGMFGPMLNQFGGMFGMGGGSMNEMIEKMTTTLESVKKMNGQFKDPNCTTFVCVCIAEFLSLYETERLIQELTKQGIDTHNIIVNQLLFPDTDESGKITCRKCGSRQAIQSKYLSEIDELYEDFHVVKLPLLESEVRGGPEILKFSERMVHPEKNTNQ
The following text describes a protein:
Function:
Microtubule inner protein involved in the attachment of outer dynein arms (ODAs) to dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. Functions at the initial step of left-right asymmetry specification of the visceral organs.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MGAGILRVIIMDSENYVETHPSDDNEAMKTSDVYKVDKNLPKRFNNPDCFQGYSTKINHPFYQTSSQIYGSKRPTVHEMPTTFNGSYRKFSEHMLKSGMFRDNGFNTSIEKSKITGHDTIPMFQDRINFNYAYDSGNGPKN
The following text describes a protein:
Function:
Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Sequence:
MIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARLVGAKLDLDEDSILLLQMIPLRGCIDDRIPTDPTMYRFYEMLQVYGTTLKALVHEKFGDGIISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPF
The following text describes a protein:
Function:
Component of the volatile terpenes biosynthesis pathways. Converts mainly geranyllinalool to trimethyltridecatetraene (TMTT).
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MSAAVALAVILAVYVVLRYISSPRGRSKPLNLPPGPRGWPVIGSLGALAGALPPHRALAALAARHGPLMHLRLGSYHAVVASSADTARLVLKVHDLAFADRPRTAAGEVASYGYLGIVHTPYGAYWRMARKLCATELFSARRVDSFERVRAQEMRALARGLFECAGRGAVAVREHVAGATLRNILRMAVGEKWSGCYGSPEGEAFRRTLDEAFAVTGAVSNVGEWVPWLGWLDLQGCVRRMKRLRAQYDRFFEQILDDHDHKKTRRERGRPGAGDSAADDDLVDVLLRLVEEDEDRPETTEASRLTRDGVKAFVQDIVAGGTESSAVTIEWAMSELLRRPDALRAATAELDRVIGHGRWVTERDLPDLPYIDAVVKETMRLHPVGPLLVPHHAREHTVVAGYDVPAGARVLVNVWAIARDPASWPDAPDAFRPERFLNGSSGASVDVRGAHFELLPFGAGRRMCPAHGLAMKLVTAGVANLVHGFAWRLPDGMAPEDVSMEELFGLSTRRKVPLVAVAEPRLPAHLYTNVTPPQQVAGSTIANLSTRPEYKLVF
The following text describes a protein:
Function:
RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs. Acts as a scaffold protein that connects deadenylation and decapping machinery. Required for cytoplasmic mRNA processing body (P-body) assembly.
Subcellular Localization:
Cytoplasm, P-body. Nucleus. Nucleus, PML body. Nucleus speckle. Note=Predominantly cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Enriched in splicing speckles. Localization to nuclear foci and speckles requires active transcription. Excluded from the nucleolus.
Domain:
The region C, also named Pat-C, is required for RNA-binding and mediates the binding with the Lsm-containing SMN-Sm protein complex and the decapping machinery. It folds into an alpha-alpha superhelix, exposing conserved and basic residues on one side of the domain.
Sequence:
MFRYESLEDCPLDEDEDAFQGLGEEDEEIDQFNDDTFGSGAVDDDWQEAHERLAELEEKLPVAADEQTGNGERDEMDLLGDHEENLAERLSKMVIENELEDPAIMRAVQTRPVLQPQPGSLNSSIWDGSEVLRRIRGPLLAQEMPTVSVLEYALPQRPLQGPEDDRDLSERALPRRSTSPIIGSPPVRAVPIGTPPKQMAVPSFNQQILCPKPVHVRPPMPPRYPAPYGERISPNQLCSVPNSSLLGHPFPPNVPPVLSPLQRAQLLGGAQLQPGRMSPSQFARVPGFVGSPLAAMNPKLLQGRVGQMLPPAPSFRAFFSAPPPATPPPQQHPPGPGPHLQNLRPQAPMFRADTTHLHPQHRRLLHQRQLQSRNQHRNLNGTGDRGGHQSSHQDHLRKDPYANLMLQREKDWVSKIQMMQLQSTDPYLDDFYYQNYFEKLEKLSAAEEIQGDGPKKERTKLITPQVAKLEHAYQPVQFEGSLGKLTVSSVNNPRKMIDAVVTSRSEDDETKEKQVRDKRRKTLVIIEKTYSLLLDVEDYERRYLLSLEEERPALMDERKHKICSMYDNLRGKLPGQERPSDDHFVQIMCIRKGKRMVARILPFLSTEQAADILMATARNLPFLIKKDAQDEVLPCLLSPFSLLLYHLPSVTVTSLLQQLMNLPQSASAPAPSNSHLTAVLQNKFGLSLLLILLSRGEDLQSSDPAIESTQNNQWTEVMFMATRELLRIPQAALAKPISIPTNLVSLFSRYVDRQKLNLLETKLQLVQGIR
The following text describes a protein:
Function:
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Subcellular Localization:
Nucleus.
Sequence:
MPLIASEGGVGSGQSSFQPWLEAVSAVTSAPHGSHQQQASSARGDTAIRLRNEARLHFEALSSGIRSDASTITATNTSSTSPPTPLKPSLSTVAQDISKASTSTPNGALALLVSILGPSISSNKSIPSHQKLVARVRALSCLLGALEGTSSLTHGVRQAVGRFLVELCRPDCRDDDIDEEDDAGGVANQIEMDTSGRHDYVDATNLTADEVTRHLQAMEKARLQQQHVPNKAPNSSSSVSNNDVRDTAMSCLKALLQSRLEMFPTQQSKSPQKDASSPRTEAMAVIRQSMELRMELAMAGVRYRCDAGTDNGDANAINPGAGYEMDLDTGIEEGLSQLPRIKRSLCFNLLEGALDGLKEDTVLWDKLQSQSKEGGTCVLPSSLLKSMAAFASLTSSCLHGETDPRCLLQLLRLLNKGQQVVLPLFREDESTTKSISGMDLGRGGRDIFPSIEIFDAVAPYYPVHFTPPKNDPHGITRVMLHDALMAVLCEKGVNYETCEAVVDCGTESGDEIENMITLASRMMLERLDPPKASDYDPPTESNVDDKVDALRDLSTMFLPSDSKPAQQYSVNITRVPSAFLLEMSSSLARVHEEAVSSDNDDQKPLASAVRTFSSALAFSLEPSANDTTRLWEAFVVSVTDRLSPTLASAPQGMHGRASTAYLASLAAGSGLATLNKVLSECMPRFLSLLSTLDDDIKGDVIDTGRRKKNRDEEKMSAAMRGIAALMSSCRVATDCWKRDNNGVQVHPHPLSTYTSCIVQRIAGVLGSSAGNHDEGSLSLAAIGALESFFTSVDLSTLTDEEMDSLDIISSVVSSVVLEDIEERMDVDVNRNDTVWKTACARTLGAMIAIGMTQDDGSRLNASAKSLLPQCVTAATTTSSKSTTGVRQRYDWIVLAKACANGTERVSKQIVSELLSGIISWLIENQENSEVSLQLECFPAMVLSYLIRYGGSNVDAAFHCMVPPNTTPLDIVNALCKPLDGRNTDNGMNEEQMVVTRQLPVGMSHLQLPVSRAKEEETANAIIERAYSILPHLIPAYECPSSASSCESLVQLVDQILPPLSEWDEVKLCITFPLMTSILNSSNDVWNMLNDVTIEGLTSMVTYLAEFSISSDHETRSRSAAASSLFSILIHCKEDEGCNSIQALLENKVCSDLVDAASSLTQDLTAILTPRASCVPLESSARLSSFSRVEDTLNFVGLLGSAAACKGGTYSRTADAIAAFLVEMSCTGNAQVPFAETAIHLAAPTHDGQKQPILDPSSHAYVLPAAAFGSMLSVHNGGPFWRQRMTHKTLPILLKALQAQAQSQNPPALGTLAVVCHMLCCLPAKLLGESNVRQMIPTLIAGLVYFSKNLQALTQSESISCKTSDVLSIILAALLKLLSISPEDLMHRIHCLKLSKFIGIIIPSLLLLCTSTGSEKYIPKQLLALQCLETVANLPTPRNAVLREKDQVVAVLSAVVDHPAFIVRQAVVQVRNACSFSPSLPTMTPLPTIHAVCLLSLLVVSSANAAWSSRDDKEDDFSPRQQGEIVFVSPSGALDSTPSLTYDTNDNVVKVDKFSANTFYGDSLNFRGREIRNAALVDCNLEGLKQLTVESLALSSQSSTPGKNGHGLAIIDNDGAVLSTQHMRWDEKTKELKVFSLSSFSKSLAIESDVDMKTNTLRNVNIEAKTTLRDLFFKDGYIENSVLHNVTATELNLGDVSIDALSISAFNNKQQVGSLLLVGDDGAVEISPTIRQEHDGRLLIDDEVSLTKTLDLNNQDVLNANVKSGSIDGPINVSVDFVKAKGITLTGIQYDKTVLSDGLAVIGLDGELKMSPIDVLGDGSLGDINVRGTIDFAPAFSDSKDLGKIANAHIVGGTIDSVEKLSVLGEAELGAGLHVAGETYIDGALTVSGSVLGSGPYVDVSDGRYKRNVVKIDSKDALGKILLLEGVSYELDLSEVGKHERLGRGGVLTSDNQERQLGFIAQDVEKVFPELVYNDASDFKGLQYARLAPVLVEGLKQLTMENQTFFINVYNS
The following text describes a protein:
Function:
Involved in transport of proteins into the mitochondrion. Essential for embryonic development.
Subcellular Localization:
Mitochondrion outer membrane.
Sequence:
MAAPMELYCWKGDWGLPSVDPDCLTVLTYAKFSGAPLKVHKITNPWRSPSGRLPALKTSDDGVLFQPSRIITHLRKQKYNADYDLSARQGADTLAFISLLEEKLLPALIHSFWVEGKNYVEHTRKWYAESIPFPLNFFLPNQMHKRNMERLKLIRGESWREEDEEMEGRVSMLINNPCAAQNRGGASVIHIGSSSHLLLHTEGTPISYMSPHYPPVCAPQLYTDAHECLSLLSQRLANNNFFFGDSPASLDAYVFSHLAPILNAKLPNNKLQQHLSSLPNLCRYCTSIITVYFPWEQESGPRVAPKPPSAETQDTEDDPHKRRNQVLSVLAGLLAMVGYAVLSGIVSIQRVAPDHALEQGITMEDNEEEEE
The following text describes a protein:
Function:
Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing.
Sequence:
MDPPSVRSKITEIEGDLFHAPDGAALIHACNCQGSWGKGIAKAFKDKYPAAFAIYRSHCQNLLSSPRYMFEPDLQSEESHARSSRDVRLPEGTALIIPPQKRDSEANGKKHWIICLFTSRGFGRAVSPPDVIVRNTELAVADMTRQLAELQTDQSSREESVGELWSCRFNAGLFGVPWERSRRVLEDAGLEVTVVRPHGG
The following text describes a protein:
Function:
Component of the gamma-tubulin ring complex (gTuRC) which mediates microtubule nucleation.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center.
Sequence:
MDEHQSGDLVKELVLRLVPADSGGALRFAHRLLSSRLAPAVFPDEHALAESVKRRLAASGRPDDTLAFADLHSKLSARSRPASLWPLLYLLDSLSPHRRGAAACLPDLPTAAPPRHAPRAPGTPAGGAALVSKDPDNIREIALREYTELVLDETEVSEATLVRDVLYACQGIDGRYVRYDKASDTYDLPAGVRVPGSTRTLVRKLCEVGWLFRKVRGFVSDNVSRLPSHAATEVGTVAQAFCSALQEELSDYYKLLAVLESYSLHPIPTPGSDSGVSGNYLSLRCLVVWLAEPAVKMRLMAVLVDGCRGLRGGGMAGVIHGHAQHGDPMVQDFMGRLLRRVCSPLFEMVRSWVLEGELEDVFGEFFIVGQPVKAESLWREGYLIQSDMLPSFISPVLAQRILRTGKSINFLRVCCDDNGWAEAATEAAAYVGTTTSRGGLGYGQIDALEALVVEAAKRIDQRLMDVIHKRYRFKDHCLAIKRYLLLGQGDFVQYLMDVVGPELSEPANRISSFHLAGLLETAIRASDAQYDDRDILDRIRVKMMDHGDGDRGWDVFSLEYDARVPLDTVFTASVMKMYLKIFNFLWKLKHVDHSLTGVWKTMKPNCIVSSPFYKEGTNIRAQFVSVLRKCQVLFNEMNHFVTNFQYYIMFEVLEVSWARFSEEMDAAKDLDDLLMGHDKYLTSIVEKSLLGERSLGILRNLFALFDIILQFRSHADRWFERIYELQLRGKSKLKTKSKETGSWLEGGRKAMIQLAGELFRKMGEDLDSIAKDYTASLDSFISQLPLQKHVDLKFLLFRLDFTEYYSRVSSNK
The following text describes a protein:
Function:
Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
Sequence:
MTGIIHSLLDTDLYKFTMLQVVLHQFPQTHSLYEFRCRNASTVYPLADIREDLEAELDALCQLRFTHDELGYLRSLRFIKSDFVDYLELFQLQRRFVEIGTDDKDRLNIRIEGPMIQAMFFEIFILAIVNELYFRRLETPAVIEEGERRLQAKAARLKEIAAAQNPDEPPFLISDFGTRRRYKLAWQEHVIRTLLEAAPGIVRGTSNVFLAKKLGITPIGTMAHEFLQAFQALDVRLRNFQKAALESWVHEYRGDLGVALTDVVGMDAFLRDFDLYFAKLFDGLRHDSGDPYVWGDKAYAHYQKLKIDSRTKMLTFSDGLDIERSWALHQYFKDRFKTGFGIGTNLTNDMGHTPLNIVLKLVECNGQSVAKLSDSPGKTMTNNSTFLAYLRQVFDVPEPETP
The following text describes a protein:
Function:
The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization; Transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity.
Subcellular Localization:
Cell membrane, sarcolemma. Cell membrane; Single-pass type I membrane protein. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Postsynaptic cell membrane. Secreted, extracellular space.
Sequence:
MTASANQQLACKSHDSQHQPQECCHPQNLDSAKQSSMAVLWPSLLVDLFCTYSPRRRGSISESRLTYTGTLLAVLVVCLLNFSAVGASKHESNDVITWLETYPVSPVTDATVKSNVPVSVLWGVPDLNVVVGRLLQFTIPPDAFKGDIAKYKVSAAGGGKLPSWVQWVGEDRTLICTPSESDVGLLYITVTAIGKPNNTSDPPSQASDVFSINVVPETAPESTAAPALVSYLGNVENSVVCLPGEPFTMVTVIVDADPDKLYPKDKLKLLSGMKAHMKVPLDFLKLLPMGNKRILDASAFMAGPGNVKQAKTEGMLLSWTVGCGSDTSNLRGVNRVEETAKSGEMARDLGYDVIGWHVTSPKPHLSKRMKRQLQLRPTPTPVPVIPVIPEVPESSAIPPTRVIPTQASPIFTVGRTATLEPTPAPSKVVPTDTKVSLTASPKGTRTKPTMSASMMQTPTMLPPRPTRIDIVTSTVAPSRSELVTPTPVFTVPVTPTQVTQPVTTPDKTSERTTTPKTTKPEETTTPKKETTPEKETTPEAPTFPKTPQVPTEPNTPPELINHIDRVTVYQGEVLRFTIPMDTFFDVEDGNTRKLKLVFMNIDGLIMPKNSWVRFNDTSQELYGLPMGEHVGTGEYLMAALDSAGAVARDAFEIQVLPRTKQFNHKFSVRIDYDFDKFKYDVNKQLLLMEKLAKLYGESDTSSITVQEFKAGSVIYSWSNNTLPYYPCPSEEITQLRAKLMKNGEINPELIEALKPEFIVTKVSVAPAGPCDKGYGTDKPIGPSIDESNSRVTSDDDKWLHIVLPAVICAAILLLLGLIIFLLYRRRRKGKLSKEDKHTFVNKGIPIIFADELEDTKPTTSSTPVIMKDEKPPLPPPEYPKVPLPDMPPGVDPPHTPDDEFSTPPYQPPPPFSTPQGSRGTRPVIAPPYRSPPPYVPP
The following text describes a protein:
Function:
Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Required for the coactivation of estrogen responsive promoters by SWI/SNF complexes and the SRC/p160 family of histone acetyltransferases (HATs). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells (By similarity).
Subcellular Localization:
Nucleus.
Domain:
The HMG domain is essential for CD4 silencing and CD8 activation; mutation of this domain blocks thymus development.
Sequence:
MSKRPSYAPPPTPAPATASSGITIPKPPKPPDKPLMPYMRYSRKVWDQVKASNPDLKLWEIGKIIGGMWRDLTDEEKQEYLNEYEAEKIEYNESMKAYHNSPAYLAYINAKSRAEAALEEESRQRQSRMEKGEPYMSIQPAEDPDDYDDGFSMKHTATARFQRNHRLISEILSESVVPDVRSVVTTARMQVLKRQVQSLMVHQRKLEAELLQIEERHQEKKRKFLESTDSFNNELKRLCGLKVEVDMEKIAAEIAQAEEQARKRQEEREKEAAEQAERSQGSIAPEEEQVANKAEEKKDEENIPMETEETHLEDTAENQQNGEEGTSTPEDKESGQEGVDSMEVEGTSDSNTGSESNSATVEEPPTDPVPEDEKKE
The following text describes a protein:
Function:
Catalyzes the addition of a mannose residue from GDP-D-mannose to the position 6 of the alpha-1,6-linked mannose residue of the triacyl phosphatidylinositol dimannoside (Ac3PIM2) to generate triacyl phosphatidylinositol trimannoside (Ac3PIM3).
Sequence:
MRVVQVANFYGPRSGGLRTAVDRLGAEYCASGHEVFLIVPGARTERHLLRTGVVRITLPAKHIPYTGGYRAVMPGAVRTVLETLRPDALEVSDRLTLRSLGRWGREHGVTTVMISHERLDRFAGQLLPRRAAQKFADFANARTAANYDTVVCTTGFAREEFDRIGATNTVTVPLGVDLKTFHPRRRCARVRQHWATPTQILLVHCGRLSVEKHADRSIDALAALCDAGVDARLVIAGEGPLRARLERKATGLPIDFTGFISDRHAVAGLLASADVALAPGPHETFGLAALESLACGTPAVVSRTSALTEIITADSGACADNRPEAIAHAVRTIVSRPERHRRRCARRRAEIFTWQRAAASMLATLGAMAVSTRCGDTQDTA
The following text describes a protein:
Function:
Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals. Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP). Promotes cleavage of serine/threonine-protein phosphatase PGAM5 in damaged mitochondria in response to loss of mitochondrial membrane potential. Mediates differential cleavage of PINK1 and PGAM5 depending on the health status of mitochondria, disassociating from PINK1 and associating with PGAM5 in response to mitochondrial membrane potential loss. Required for processing of CLPB into a form with higher protein disaggregase activity by removing an autoinhibitory N-terminal peptide. Promotes processing of DIABLO/SMAC in the mitochondrion which is required for DIABLO apoptotic activity. Also required for cleavage of STARD7 and TTC19. Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein; [P-beta]: Nucleus. Note=Translocated into the nucleus by an unknown mechanism.
Sequence:
MALYSWVQRGWRCGQTWAPLLGGGYRELSATQARQLLGRRFNLLLQQKCGFRKAPRKVEPRRSDTGSSGEAYKRSALIPPLEETVFYPSPYPVRTLLKPFFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQKEGNLRKEINKWWNSLSDGQRTVTGIIAANALVFCLWRVPSLHRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSTSIVNILGQEQFVAVYLSAGVISNFVSYVCKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPVFTFTAGNALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYITYGHELIWKNREPLVKIWHEIRTNGPKKGGGSK
The following text describes a protein:
Function:
The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein (By similarity). The carboxylated form binds strongly to apatite and calcium (By similarity).
Subcellular Localization:
Secreted.
Sequence:
AVPAGTLSPLQMESLREVCEVNVACDEMADTAGIVAAYTXFYGPVP
The following text describes a protein:
Function:
Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Can also transport L-cysteine. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Plays an important role in L-glutamate and L-aspartate reabsorption in renal tubuli. Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate. Contributes to glutathione biosynthesis and protection against oxidative stress via its role in L-glutamate and L-cysteine transport. Negatively regulated by ARL6IP5.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein. Early endosome membrane. Late endosome membrane. Membrane; Multi-pass membrane protein. Recycling endosome membrane. Synapse, synaptosome.
Sequence:
MRKKPRKGCDCKRFMQNNWLLIATVLSVVLGIGIGVLVREYSNFSNLDKFYFAFPGEILMRMLKLIILPLIISSMITGVAALDSNVSGKIGLRAVVYYFSTTVIAVILGIVLVVSIKPGVSQEADEIDRVGSTPEVSTVDAMLDLIRNMFPENLVQACFQQYKTKREELKLPGTLERGSMTEEPVTMMMTTAISKNETKEYKIVGMYTDGINVLGLIVFCLVFGIVIGKMGEKGQVLVDFFNALNDATMKIVQIIMWYMPLGILFLIAGKIIEVENWDIFRKLGLYMATVLSGLAIHSIVILPLIYLIVVRKNPFRFAMGMAQALLTALMISSSSATLPVTFRCAEENNHVDKRITRFVLPVGATINMDGTALYEAVAAVFIAQLNDLDLDIGQIITISVTATAASIGAAGVPQAGLVTMVIVLSAVGLPAKDVTLIVAVDWLLDRFRTMVNVLGDAFGTGIVEKLSKRELEQMSSASEVNIVNPFALEPTMLDNEEAESKKSYINGGFAIDKTDTISFTQTSQF
The following text describes a protein:
Function:
Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA). May play a role in the uptake of fatty acids by trapping them metabolically as CoA esters. May also play an important role in the channeling of fatty acids into triacylglycerol (TAG) for use by Mycobacterium during its dormancy.
Miscellaneous:
MISCELLANEOUS: Stimulates fatty acid uptake in E.coli cells.
Sequence:
MSDYYGGAHTTVRLIDLATRMPRVLADTPVIVRGAMTGLLARPNSKASIGTVFQDRAARYGDRVFLKFGDQQLTYRDANATANRYAAVLAARGVGPGDVVGIMLRNSPSTVLAMLATVKCGAIAGMLNYHQRGEVLAHSLGLLDAKVLIAESDLVSAVAECGASRGRVAGDVLTVEDVERFATTAPATNPASASAVQAKDTAFYIFTSGTTGFPKASVMTHHRWLRALAVFGGMGLRLKGSDTLYSCLPLYHNNALTVAVSSVINSGATLALGKSFSASRFWDEVIANRATAFVYIGEICRYLLNQPAKPTDRAHQVRVICGNGLRPEIWDEFTTRFGVARVCEFYAASEGNSAFINIFNVPRTAGVSPMPLAFVEYDLDTGDPLRDASGRVRRVPDGEPGLLLSRVNRLQPFDGYTDPVASEKKLVRNAFRDGDCWFNTGDVMSPQGMGHAAFVDRLGDTFRWKGENVATTQVEAALASDQTVEECTVYGVQIPRTGGRAGMAAITLRAGAEFDGQALARTVYGHLPGYALPLFVRVVGSLAHTTTFKSRKVELRNQAYGADIEDPLYVLAGPDEGYVPYYAEYPEEVSLGRRPQG