lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the first dolichyl beta-D-mannosyl phosphate derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-dolichol to produce Man(6)GlcNAc(2)-PP-dolichol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MILIKNKVALKLLQLANDRKYSMTVCGVLLALEAVFLVAIIHKVPYTEIDWKAYMEQAALILGGEYDYSKIVGGTGPMVYPGGHARIFTALYDVTSGGENIRLAQYIYAAVYLGTQFFAFTVYLLADAPPYLFPLLCLSKRLHSIYVLRLFNDVFGTFAMTFCVFTLQNQMWLLSGLWMSLAIGIKMNFMLYLPAFLLITLQGMSRNGLLVVFALSIVGIQVFLALPFCNPSPDHIWSYLAGAFDLSRAFMWKWTVNWRFVGQKVFENRKFHGILLWTHLTALIGFACTIWNAPSGYQNPFEMFFTNPPPAPRGLTAAQRAEWDRIRQEASGNEVQFDVQQKRSKREQKRMQEQEEEIKKQQLAQQEGREKPPLFYSRTQFSTLVTQEYVFVTMATCNLIGVLFARSLHYQFYSWFYWTMPFLLYRATYAISPLSPMQSTLRYEGRLSKTEIRIFFTDIIGFVFIFGTWALQEYAWNVYPSTFWSSIIAVSCIAITIIGVYVSECRYPSANNTEAPTSNELQKYLAKVEKENEARAKN
The following text describes a protein:
Function:
May play a role in ciliary/flagellar motility by regulating the assembly and the activity of axonemal inner dynein arm.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MAFKARSSRFSVKMVEDTGGSQDLINNSFSSFIEEKSKESKKNKGNVTISDRSSNPFHISRDMDYFLLREQEQNQAIAEREQKKILRVHQKMTYASKVSAKHTSLRRELQLEDEMEQQLLNAEAKEMNCFRENNDWKLAMTRERKREPETLNDYMEKRRSMFLLQYALAMKRNEIQRLEMLATREENRLERAEKFLEKDASLFDEFLRENDRNSVQAMRMAEKETKIKTEKIVEIRELTAQITSIKSEISKFEDTLKHYKIYKEFLYKLSPKEWLDEQQEKHLAFKRAKESSELTRNNSTAILFGDKGSGSKSKTAFLWKEVPGLKKVTKTGRLVKALSSSIQSLPQVGQLTQLSPHSELDSRLSSTMFPSQDDTDSDGEELALYFTEPQQLLDVFTKLEEENLSLIQNTQEMEETLDELNVTLKNTQIRMDKEVNLLKQWIASMMISISKEEESAAELELKARVFHFGEYQGDQQDTMLESLNHKVLEVYRKCVGMQQEANLGTVQMLTVVERQLDELLENLERVPQVKIEQAEKAKERERRMRLREEKAMMQKQLQEERLQRARARAQAKIKKKRGRKLISRSHPPVIKVKEVREQTLINKDKEEMLFFFT
The following text describes a protein:
Function:
Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module. Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins. It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states. Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex. Binds directly to HSC70 and HSP70 and regulates their ATPase activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNNPQIQQLPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIRSRTPSASNDDQQE
The following text describes a protein:
Function:
Binds to F-actin and may modulate the chemotactic response during early development and contribute to the maintenance of the strength of the actin cytoskeleton.
Subcellular Localization:
Cell projection, pseudopodium. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton.
Sequence:
MSNLGKCTRCQKTVYSQEGFIAVKVPFHRSCFKCEVCNWQLVLTNYKSINGKVYCANHYPVGGLSVTPEKTHTTSDDLVMKNALNAPRVETVNEQLRGGNEKPQTSTDDLVTKNALNAPKSNLVNNQVRGTSDSAPLTSADDLVTRNALKAPKSDLVNNQVRGTSEMGPQAGIDIVTANALKAPKLETMSGYQKSVQN
The following text describes a protein:
Function:
Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MARTVTYVQFALALALFMFALVQFELWNLKSSNVGQASVGRKLKAQIRLPDSKLTPEPNKLKALEKEAPIAAVVVVACNRPDYLERTIQGILKFHTSSSKFPLFISQDGTNAEVKAVAQKYAHFEHFQHIESQPPQMEAGHPQSWLSYYRIADHYKYVFTRIFEERKFQRIIILEDDMEVAVDFFDYFEALAPILDRDESLYAVSSWNDNGQKQFVHDPEAVYRSDFFPGLGWMMPRRMWAELGPKWPKAFWDDWMRLKDVRNGRQTIFPEICRNYNFGEHGSSLGQYFEQYLRPIRLNTEPVDWSQKDLTYLERDRYPAFFERLTSAATVIPADRAGAAAAAEAGDVLVEYDGESEPAFKDVARHFGIFEDWKDGVPRTAFQGAVTFRLGGPRRVIIAPRKSS
The following text describes a protein:
Function:
Lipid transfer protein required for autophagosome completion and peroxisome degradation. Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion. ATG2 binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, using basic residues in its N-terminal region (NR) and to the expanding edge of the IM through its C-terminal region. The latter binding is assisted by an ATG18-PtdIns3P interaction. ATG2 then extracts phospholipids from the membrane source using its NR and transfers them to ATG9 to the IM through its predicted beta-sheet-rich structure for membrane expansion.
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MFSLPSFLTTFSFTLPSLPSISLPANIQRRFLSYVLKRTLGRFVSHQALDAERIQAQVSEGWVEIENLEIECSEINNYIPPPLPLSLTSGTINKLTAKLPFPNLWSDPLQVSLDTLTLDFTLSSPSPLSRGRAATRPEHHDLAESVTSAADDFLHHELDAYEEKELEGSIRQSLILSQTDPFISDVPGGFPLGSPGEISPGRPLPANMESTTVLAGMVERILARLEFRVEKIKIRLVIEDEEDVVELTVGRIRYADESEAQTNDDGKSTTRAIRISNISLDIVPSQRKPPSLVIPQRQSLEPSVSSSTSTASTSSGNDYSDMFMSQAVVDLRQSLLTPEQISEPANEQTVHESNMFYSALSQPNESEPGASTGIKRSGISQNPKLADEIEEERSRSETPTPETKPQPSGIPVLSFGQEDVVLHMRTTRPLISAGHQTSFNDNKPTVEMNITIGTITTVLLPSHLKLFISALQTLQALCQKDDVPAAKDKPAQSTSPQTRLTATTKLKAFYVSLVYDLSAETSLNLHSTMASHLTRPTNPIPYPHLRFRLDTLVASYQSPGHSNPSRPAFTRPTPNMSTANLRRKSSGHARFGSLPSNLTVNVGDISLFEWMGEGMIAPVILFDPGLKHQYDLPSAPPHKGQAGFPECECRDWREEKKTGSEKAWRVRPRGRGILKGGARATTEDEGPVVHVRQDLGSDSAAVINLQSLHVFVDLSLIERLLPLLRSVTPLIHPPEPTPAWLQSVPSQSISEEITPESIISSLSAPPPTARGKKMKADIRCDLVRLSVRCPAPPPEPAERQIGDGRQLRSGIVFVDVHGLKSRFMDTSRTGTRPASSEVANVEFEQTLIFFASVSQHYAYPFLIFAPLSPEPGEEDIPLLPSISLSSFPQASSLPASSIAKTTLVTCKMPAIRASVHHPTVTGLQYFADDVTRWLDVAFADGSAKPRDELKMIGSRFFGGSKGSEASSEIDEPYDVEEVAAGMKVEIEISEIDMGLYVPRLDASGERVFSFKANDLGVRMETHPEENETALELSIMDLDFSDVSSTPLRILGRTTPFTLTSHQAPVVYLRFVSSTDLRTTLKESNISVALSHFTFAVHKEIAWLHEIAQFAKPPKGVFENLSPTDLTRLSINLSSASFLLVPPNLPGSIVILVREVEGKTEIPKGATDSVLEVGMSGLGALAVEGESGPLEVSSDLADVWKKAGYAQLAEVMVLELRLMRELVAAGEVSLDITQAQFKVTACADSLATFAEIATDFGRLFPNKKEEHVKLPSMGQSINVFDSLDENAFNLLPEIVSHSDTDMIEDDLPHNLDYLDHATRISKHYPSMDRTTGENLRAWHTPEEGLEEGEWENGESGETIRAFGGEIEEEEGYWEGLPILNDVYSADQKPGKIHIRVLDASLKIFLHDGYDWPRTRKAIEDEVRAVRRRLERIRQLLASGQKADESIENATSSVLFNSIYIGLEQKGEMGLSTMGMGKMDEKALMAAIDEELDGMETESGSSWQTLPAGVGAGPSAVHQAHKKTRLKGKRLVRSKKAQIEITLSGIKTDVDLYPTEESTSSRVHFTAKEMEILDHIKTSTWKKFLTEMKADNRGNIRETDADMLRIELVGVRLKEDEEELRLRAKILPLRLHVDQDALDFLKRFFSFKAPPMTSARPLAQHTTSSTPDLYFQHVEIFPIQLKLDYKPKRVDFRALREGKTIELMNFFHFEGAEMTLRHITLSGITGLERLGTTLQDLWTPDVKANQLADVISGVSPIRSMVNVGSGVADLILLPIEQYRKDGRIAKGVQRGTNSFVKSTALEVMKLGARLATGTQVILERAEGVLGGKSGEDVVGQVQGLSTNAFGVDSGMLEGGSSSEDEQEAISRYADQPESMKEGVQAAYKSLSKNVNAAAQTILAVPMEVYERSGDDGPLKAVIRAVPIAVLKPMIGTTEAVSKTLLGMRNSLDPSARRELDDKYK
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
METFAVNIFSFPSAQINSFVTFLLFLVVCFLFFQESNQKEHLASSAIEKTMSGQKDTLIGESQDEDSGSPFPAAAQSRGPEGTTKYFGNCPVVKEEPEEAPAQQWETQWQEYLSSVDDSASLPEAPHFPQEPAPWDDTPAFLASFEQVAKAYQWPEEEWAGRLLPTLKGEAELAFSSLEDEEREDYWKVKAAILRGDTLNQEKSRQCFRRFCYQQADGPRGTYNQLQEFCRQWLKAERNSKEQILELLILEQFLTVLPAEIQGWVKKHHLESGAQAVSLAEDFLLQQGLPLVKEERTIESQGEGSVILSELEESLSDAGPRPQLCRVSEMEEDTDFSDTDLLADGEDEENHLQEYPEHRRTHSGEHPYRCSDCGEGFLSRLSLEAHQRVHMGQKASLSPPEVTVYICGECGETFNSTLDLNAHERIHAGQKSCTCKECGESFSQMLDLREHQRTHSGFKTSGSGENNLWASSHKNHRDIHSGNTNTLTLREETRTKKKTLSCPRCGEVCTCTWKLRWQLKNKSSLNVSRTRRNSYKCSKCQKCFASEITLSIHQCIYIGEKRKQLNTPLRREIVPKRKDFANQSLRKEKPYRCTDCGESFLWAVSLKRHRKKAHKGKKSVPVLEKVPGIQGKRYACQECGESFERQGLLKIHQCVRAKKKPYSCAICGDRFQWGVSLYRHRKEVHKWKTFPQHLQTVPGRKEKIHTCKKCGKNFNRPWRLMAHRCNPVAENPHPSPEHGQTLPQNISGAGTKCFSCPVCKKKFARENHLNAHQHIHTGEEPYQCGSCGERFMWRPSFYSHRRKVHKGIARLTRATPCVKGKCTVCGKSSMWEATFEKLTKNHRRENPTFSHKKKGTRLQGDPNTCKVCGKTFSDRSYVAKHQRIHTGNQPYQCSDCELTFRWRTSFINHRKIHKHHKPSKLIQKLSGTEKTSMKSYKCSHCGESFLGLAALDLHQMTDHIGKKLVPLLERIPNTQYVMAFKTGKRSHKQTEGLMQKPTQKDSKSYACSQCGKSFAYPSSLWRHQYVHLPVKLFQCHLCGKKFMLKEYLAKHMKRHAGLQ
The following text describes a protein:
Function:
Acts as a component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery (By similarity). Required for yeast cell adherence to silicone substrate, but nor required not required for buccal epithelial cell adherence or virulence in mouse systemic infection.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSNRKLQKEIDIIFKKIQEGLQDFDYHYERYESIQNTEDDSDNQREKEKLANDLKKEIKKLQKFREQIKHWLQNDTVHTLGPVGTSYESKLAENKSLIEDSMETYKLVEKQSKLKTFSNQSIMMTFMDSTNGDDDDDDDDSDDDELFSGSDEDEEDEYSDLPEDAVNAIHFFKDSILQLREQTHKLDHEYEKLAAKKLRKNNLATIEAKKEKIQSTIGNNKFHQKKLKKLLRQLTSGVVTEFNLIWLLKDDLNKYLESNGDYEFTRETELYDDIFNQIAAVEEDYSEIHEDNHDHSHSHLEKTSTANGTHHESATTTATAAKNSSVTTRTSPSPILTKANGHIKELSVESGSPTTSRSKLSKIHTNTSQSSTHSNTSSSTHAQAPRQSPELTSPAIVKTLRPATAPSKPVGTLKWSAAAAAAIPDVQEKPELVETESNGSSVHKTVSKDQYEEKINYQSPAPTQQQQQPQTSVESKTLSTTQSLASSITDNINLDKYKEVIKNSNLTKTELGLFSDMNLARVPPGIQDLVISFASKRNNDNFKVLVDSTEFNQFALPLHKPYLPEIVQPSYYSQYTSTSFKHPTPLVKFQSYWNQVRANFGFQKLMDEIKSLTLQNNADNLPIIAELTFVLFYGFYYGVTPAENLIAESYLFELGWKPYKNQSEDGSNNLSTGSISLSDINGSKSKSNRSSNYYFWFKRVKLISRGEDMGQPSNIEFGDYQVFDLSFWEIFVKYGFKFDYNFCQMEPSKTLF
The following text describes a protein:
Function:
Acts as a transcriptional repressor.
Subcellular Localization:
Nucleus.
Sequence:
MSSAAVAASRRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRIEFVIETARQLKRAHGFQEGRSPGPVGKPGKDMQSINHAEPGSRPPQPLDRYPLTSDRPPRLGAEYQRQANGIPVPNGFPKPDEPPELNRQSPNPRRTGAIPPNLVPLVNGSMPPVHALNGRSVQMGIPPGALAEHVGKRADDMKDKHRADSMSDPSDGHKRVDEWTQKGKTVREMMTLQTLDSRFKKEHAALPHRMSYESSSGALKTDRGKHSRGIKRKTSPEPDGEGIAVKLNGEGQPWLPSPSEVLKMPSAALPGFAAAPPSTISPHSRTTPPEAATAVQNSQSPMAALILAADNAGTGSPKDAGNQVHSTTTSAAGRRNSGSPQSPSAGQRRPALGATGTAHIPGMDPQAGHPHSIPDSSVPPSSVPLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRESIKQQGATGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDP
The following text describes a protein:
Function:
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
Subcellular Localization:
Cytoplasm.
Sequence:
MNNILSEEVLNVTDFTTSRQLTLWKREDLQSPQLDDVAEEVPVALVYNGISHVVMMASPKDLTHFAMGFSLSEGIIDSPREIYGMDVVPSCNGLEVQIDLSSRRFMGLKARRRALAGRTGCGVCGVEQLNDIGKPVQPLPFSQTFNLGNLDRALKHLNDFQPTGKLTGCTHAAAWVMPSGELAGGHEDVGRHVALDKLLGRRATEGEEWRQGAALVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAERCNLTLVGFCKPGRATIYTHPQRLIAD
The following text describes a protein:
Function:
Metalloprotease.
Subcellular Localization:
Secreted.
Sequence:
MRFLFLSWTLFIGSYGVELPKIPKLTDLINPFQQFKLRDILGAITALETPDIGSDPPGISYPKHEYTDRLSSISDINRSKRDLLFQGDIHLSFEHLSNIVREQLDHPRRKRTAFRNAQYPSTIWLPYVPYELHTSLSPKSRSSLIAAISFWEKNTCVNFKKRTNEEVYLLMSAEEEGCWSTVGRDEAQKAQILNIGEGCEMFGITSHELAHALGLFHEQSRYDRNNYVQIIKSRIAQKNFYDFAIVGMRNMETYGQKYDIGSVMHYRPTEFSIDGGNTIIAKDINMQNTMGQFRGPSFLDVAKINRHYNCETNCKYKIKCVNGGYQHPRNCNVCVCPPGYGGKDCTGIETSNPAKCNGILVAGETQRKFTINIKPKYLVNGVRKCNYHITAPPGKRIVVIVDSVIGNCVQGCYEEGVELKMYDDKTVTGARFCCKLQKPQTLVSQGNTVPVMVVAGKAQAFVQLRYATVDHPQNRSPKDGNATSSGFNPLFLEKYLDDSIDSEAIRREYLIQSDNIGQEDFETLVRREFVDENSVEI
The following text describes a protein:
Function:
Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity).
Subcellular Localization:
Cell junction, adherens junction. Cell membrane. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Nucleus. Nucleus matrix. Note=Colocalized with PXN at focal adhesions during myogenic differentiation. Colocalizes with the Ten-1 ICD form of TENM1 in the nucleus (By similarity). Colocalizes with actin stress fibers. Also detected at the plasma membrane and in neuronal intranuclear inclusions.
Sequence:
LNRDDDSDLHSPRYSFSEDTKCDDGWFVGTSRRTK
The following text describes a protein:
Function:
Not essential for growth. Inhibits early G-protein signaling events following pheromone stimulation. May help create heterodimerizable beta-tubulin by facilitating the efficient transfer of nascent beta-tubulin polypeptides to the folding apparatus.
Miscellaneous:
MISCELLANEOUS: Present with 2250 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MEDKLDRYYTNVLSNAEKDKHTTVDSDDKSSGEENLDELLNELDRELDEDHEFLSAYRSERLQQISDHLKQVKKNVEDDGYGRLQCIDNEADAIQICTKTTMVVIHFELETFGKCQYMNEKLENLAKRYLTTRFIKVNVQTCPFLVNKLNIKVLPFVVGYKNGLEKVRYVGFSKLGNDPNGFDIRRLEQSLAHSGVIEDTFEIRKHSSVNTERFASTNHDRSESDSDLDI
The following text describes a protein:
Function:
Secreted effector that effector that induces cell death when expressed in host plants. Induces the expression of defense response genes in tomato.
Subcellular Localization:
Secreted. Host nucleus.
Domain:
The CRN proteins have modular architectures that include a signal peptide, a conserved N-terminus, and highly diverse C-terminal domains. The conserved CRN N-terminus harbors a distinct LXLFLAK motif, which is followed by the conserved DWL domain. A highly conserved HVLVXXP motif marks the end of the CRN N-terminal domains and forms a junction where diverse C-terminal domains are fused. The conserved CRN N-terminus mediates the translocation into the plant host cells.
Sequence:
MVKLVCAIVGVAGSAFPVDTDASQLVGDLKKAIKAENAMTFTGDAKDLQLFLAKQPVDDESGKEVVPVYRPSAEEMKEESFKWLPDEHRAALKLVEGESDDYIHALTAGEPILGSKTLTTWFYTKNNMELPSSEQIHVLVVVPDGAGGSASDTSRMDRLFDKVDKVYEHTVLSKRTRYVHSEMNSAKGNILLNDLKIRISPVDTVKFAGGVPTPAKEFKWKSDRTEEQQKEPYREYVVANIGDVLTNNKLCVVGVEKGVNILTVEVPGRDIVLAGRTDMIVLSDIAQKFPHYLPHLPGVRMLIEVKKVVTTASEFQALSELIALDIIATESVMALLTNLTNHWQFFWVSRKSDDRVIIETTTLIAPGEAFAVIRTLLDQSPSAGAEVSLPCFEKPVKRQKLSQLLPSISEASGSSGIRESIERYYDIASMLGPDLEMARAVASQVARSIPTLSYFS
The following text describes a protein:
Function:
Coenzyme A transferase which is involved in short-chain fatty acid degradation and catalyzes the activation of short-chain fatty acids to their respective CoA thiolesters. During acetoacetate degradation, catalyzes the transfer of CoA from acetyl-CoA to acetoacetate by a mechanism involving a covalent enzyme-CoA compound as a reaction intermediate. Utilizes a variety of short chain acyl-CoA and carboxylic acid substrates but exhibits maximal activity with normal and 3-keto substrates.
Subcellular Localization:
Cytoplasm. Note=Membrane associated.
Sequence:
MKTKLMTLQDATGFFRDGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVRKVIASHIGTNPETGRRMISGEMDVVLVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEGKQTLTLDGKTWLLERPLRADLALIRAHRCDTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQESK
The following text describes a protein:
Function:
Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MGSFDRPRKRIQLWKKALIHFALCFVMGFFTGFAPASTASIFSRRIGSSDRPTKPVPALEKLADPGIANRSIMAEIPVGESPEPHLDRQLIIITTTRSDDRLQEAFLRRLACTLKLVPPPLLWIVVQARAAAPVTAEMLRKTGVMYRHLTFEKNFTDPAAEADHQRNVALNHVEYHRLAGVVHFADASNVYDLEFFEEIRQIKVFGTWPLATASANRRRVVVDGPVCSSSKVVGWLFKDSSNDKATVRSPMTDADMKGKSLQIDISAFAFNSTILWDPERWGRPTSVPDTSQDSMKFVQKVIREDDIKLKGIPADCSKIMLWHPYRPRVIPLPFQNPR
The following text describes a protein:
Function:
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of desulfo-glucosinolates (dsGSs), the final step in the biosynthesis of the glucosinolate core structure. Substrate preference is desulfo-benzyl glucosinolate > desulfo-6-methylthiohexyl glucosinolate. Increased specific activity with increasing chain length of desulfo-glucosinolate derived from methionine. Preferred substrate is desulfo-8-methylthiooctyl glucosinolate.
Subcellular Localization:
Cytoplasm.
Sequence:
MESKTINDVVVSESNHELASSSPSEFEKNQKHYQEIIATLPHKDGWRPKDPFVEYGGHWWLQPLLEGLLHAQKFFKARPNDFFVCSYPKTGTTWLKALTFAIANRSKFDVSTNPLLKRNPHEFVPYIEIDFPFFPSVDVLKDEGNTLFSTHIPYDLLPESVVKSGCKIVYIWRDPKDTFVSMWTFAHKERSQQGPVVSIEEAFDKYCQGLSAYGPYLDHVLGYWKAYQANPDQILFLKYETMRADPLPYVKRLAEFMGYGFTKEEEEGNVVEKVVKLCSFETLKNLEANKGEKDREDRPAVYANSAYFRKGKVGDWQNYLTPEMVARIDGLMEEKFKGTGFLSSKS
The following text describes a protein:
Function:
Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core. Within the SPT complex, SPTSSA stimulates the catalytic activity and plays a role in substrate specificity, which depends upon the overall complex composition. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. Independently of its action as a SPT component, may be involved in MBOAT7 localization to mitochondria-associated membranes, a membrane bridge between the endoplasmic reticulum and mitochondria, may hence affect MBOAT7-catalyzed incorporation of arachidonic acid into phosphatidylinositol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MKVSCEDINGPRSSLSRAWNHMSWLYYQYLLVTALYMLEPWERTIFNSMLVSIVGMALYTGYIFMPQHILAILHYFEIVQ
The following text describes a protein:
Function:
Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells. Activity is inhibited by mannose, glucose, maltose and sucrose. Also involved in cell-substrate adhesion, haploid invasive growth and diploid pseudohyphae formation.
Subcellular Localization:
Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor.
Domain:
The number of the intragenic tandem repeats varies between different S.cerevisiae strains. There is a linear correlation between protein size and the extend of adhesion: the more repeats, the stronger the adhesion properties and the greater the fraction of flocculating cells (By similarity).
Sequence:
MPVAARYIFLTGLFLLSVANVALGTTEACLPAGEKKNGMTINFYQYSLKDSSTYSNPSYMAYGYADAEKLGSVSGQTKLSIDYSIPCNGASDTCACSDDDATEYSASQVVPVKRGVKLCSDNTTLSSKTEKRENDDCDQGAAYWSSDLFGFYTTPTNVTVEMTGYFLPPKTGTYTFGFATVDDSAILSVGGNVAFECCKQEQPPITSTDFTINGIKPWNADAPTDIKGSTYMYAGYYYPIKIVYSNAVSWGTLPVSVVLPDGTEVNDDFEGYVFSFDDNATQAHCSVPNPAEHARTCVSSATSSWSSSEVCTECTETESTSYVTPYVTSSSWSSSEVCTECTETESTSTSTPYVTSSSSSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTSTPYVTSSSWSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTSTPYVTSSSSSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTSTPYVTSSSWSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTSTPYATSSTGTATSFTASTSNTMTSLVQTDTTVSFSLSSTVSEHTNAPTSSVESNASTFISSNKGSVKSYVTSSIHSITPMYPSNQTVTSSSVVSTPITSESSESSASVTILPSTITSEFKPSTMKTKVVSISSSPTNLITSYDTTSKDSTVGSSTSSVSLISSISLPSSYSASSEQIFHSSIVSSNGQALTSFSSTKVSSSESSESHRTSPTTSSESGIKSSGVEIESTSTSSFSFHETSTASTSVQISSQFVTPSSPISTVAPRSTGLNSQTESTNSSKETMSSENSASVMPSSSATSPKTGKVTSDETSSGFSRDRTTVYRMTSETPSTNEQTTLITVSSCESNSCSNTVSSAVVSTATTTINGITTEYTTWCPLSATELTTVSKLESEEKTTLITVTSCESGVCSETASPAIVSTATATVNDVVTVYSTWSPQATNKLAVSSDIENSASKASFVSEAAETKSISRNNNFVPTSGTTSIETHTTTTSNASENSDNVSASEAVSSKSVTNPVLISVSQQPRGTPASSMIGSSTASLEMSSYLGIANHLLTNSGISIFIASLLLAIV
The following text describes a protein:
Function:
Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular Localization:
Membrane; Single-pass type I membrane protein. Secreted, extracellular space, extracellular matrix, basement membrane.
Sequence:
MALISAWPLVFPILLFSRCFSSSTASSAGGVFLFDIEGSSAVSTQEATVIRGQQQSVATGSWVPFAEECQEGFYRTSSGKCSPCNCNGNANRCLDGSGICVDCQRNTTGEHCEQCPDGFVGDVVGGAPTFCQPCPCPLPEAANFAVSCYRKNGNVRCVCKENYAGPNCERCAPGYYGNPLLIGSTCKKCDCSGNSDPNLIFEDCDEVTGQCRNCLHHTTGFKCEQCAPGYYGDAIFAKNCTACNCGGRMCDSRTGECLADSPLVSTGTDCPTISCDKCIWDLTDDIRLAVLAIDESKSTLLSISTGVAAQKRLHDLNLTTTHLQAAMSKKKDHSTLWTIQVDDAVDDMNDLLREAENLDDQGNQASSKGLLVQKETMETNNRATQLVQKLSNMRDNIQEISSKMKYYAIQQELSPEEIAQKLSVAEEMLKEIKRRKPFTNERQLADEEEHAAEDLLQRVEEFHERYNDTRSLFSDVVEQLSEHNMKLSDLEEALGQALDYVIQTEALNKENTANLQEHEKQHEKLKEQADEVNSIVLSATAILAEPQKISSELSEVIKNVSGFYAEIDGAKKELQEKIANLSLFDDELEEKAMQHAHNLRRLADELDRNLHGVDTNGLVQRAINASNVYENIAGYIEEANKAALLALNTTNRVNDAAVGIDTQIIYHRGKSEELLRRAMELQQTAAYSNDLTIADTSRHVNGTAARMHAVQSKLMRAITKMQSAELGLEARERLEQAKQKTAEAVSTTVTVTQATTPMDENVRLWSQNLQDFQHDSAAYDSAVHSAGDAVKKLTEVFPQLLDKLRKVEQKAPANNISSSIQRIRDLIAQTRSVASKVQVSMMFGGESAVEVNPKINVEELKSFTSMSLYIKLQKDNPQLAASPDRFILYLGNKNVKNYMGLAIKNDNLVYTYNLGDQDVEIPLDSKPVSTWPSYFSIIKIERIGRHGKMFLTIPSLSSTSEEKFIKTGESLGPSSLLNLEPENTVFYIGGAPPDFKLPPSLDLPGFIGCLELATLNDDVISLYNFKHAYNIDTTTSPPCARNKLAFTQSRAVSYFFDGSGYAVARNIERRGRFSQVTRFDIEVRTPSDNGLILLMVNGSMFFSLEMHNGFLYLRYDFGFSTGPALLEDSMKKAQINDAKFHEISIIYHNSKKMILVVDRRHIKSIDNERTAMPFTDIYIGGAPAEVLQSSISSHLAGIIGFKGCMKGFQFQKKDFNLLEEPGTLGISYGCPEDSLISRKAYFNGESFIASSQKVSLLSEFEGGFNFRTLQPNGLLFYYSEGSDVLSISMDRGAVVLNASGIKIQSPDRNYNDGKTHFIVTSVTPERYELSVDDKKQSKKNPVKDRAGKSPDSIKKFYFGGSPLKTQQANFTGCISNAYFTRLDREVEVEDFQRYSEKVQTSFYGCPVESPPVALLHKKGRNSSKAKGNRNKKVGRDKDKASQPSTGLKKLYQEVNMQKDPQCHLPMNPKATEHAYQFGGTANSRQEFDHLPKDFSERAQFSISLKTHSSHGMIFYVSDQKETNFMTLFVAHGRLIFMFNAGHQKIRIKSQEKYNDGLWHNVIFIRGKNIGRLIIDGLRVLEETFNVNANTWQVTEPLYIGGVAPGKAVKNIQINSVYSFSGCLSNLQLNGRSITSASQTFSVTPCFEGPSEAGTYFSSEGGYVVLDESFSLGLKFEVVFEIRPRSSSGILLHGHSVNGEYLNMHMRNGQVTVKLNNGIRDFSTSVTLKQSLCDGRWHRIAVIRDANVVQLDVDSEVNHVVGPLNPKATDHREPVFIGGVPESLLTSSLTTRNSFIGCIRNFMIDEKTVSFSKAALVSGAVSINTCPAA
The following text describes a protein:
Function:
Catalyzes the synthesis of activated sulfate.
Sequence:
MGKSEIFCMKPFVLWMTGLPCSGKTTIVKDLQKDIPNLAMLDGDELREWFSPKDFSKAGRDEHNKKVAHLAKLLLKHGVPSAVSLVSPYLENRENARTIVDAGDQFAECYVKCSLEECEKRDVKGMYAKARKGEIKGFTGIDDPYEAPEKADLIVDTENESLGDSANKVKEFLKSRNLL
The following text describes a protein:
Function:
FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins.
Subcellular Localization:
Mitochondrion intermembrane space.
Sequence:
MKAIDKMTDNPPQEGLSGRKIIYDEDGKPCRSCNTLLDFQYVTGKISNGLKNLSSNGKLAGTGALTGEASELMPGSRTYRKVDPPDVEQLGRSSWTLLHSVAASYPAQPTDQQKGEMKQFLNIFSHIYPCNWCAKDFEKYIRENAPQVESREELGRWMCEAHNKVNKKLRKPKFDCNFWEKRWKDGWDE