lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in double-strand break repair via non-homologous end joining (NHEJ); the repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Has a role in meiosis.
Subcellular Localization:
Nucleus.
Sequence:
MSWVQLRGHRFHFIQASFDAESNEAVQVIHITDLVRVWSCTCSRNQIVNQAESERCPIDPFQTFETLVDVLAEVLVNVSSESRIQLRGSNDEGSLKIFCTSKIAKDIFLEWNWTLWLTPPETIAKMVWFPLINHHLFESETDTSPGSLMSIIRDQKSLLNDKTWFKEALNERSSSSNPSTPRKRSAFADIISPKRPRTRYDFV
The following text describes a protein:
Function:
Catalyzes three sequential steps of tetrahydrofolate biosynthesis.
Sequence:
MDKIIIKDLLIQAVIGVNPGERIIKQNIIISVTAYKDLSKCGSSDNVIDTVSYSSLSKSICSYSESSHHYTLEALATGVAKICCLGFGIERVKVLVQKPGAIKLAKWPGVQIERTLDYFKSNSFVEIPSKLINNNKNSNNSNAGNNIVYLAFGSNLGDKFQNILNSFKRLEKQCFIQSTSFMYESSPQYYREQDSFYNCACKVSTDLKPHDLLKFIKQIENDMGRVETFRNGPRVIDIDIIYYNGLIIKTDDLEIPHPLMWERDFVLLPLSDIAPNFIHPTLHITTNRMKLNLPNGGNIHNIPPPPTATTTCNNIIEKVIRIGNLNYNWNDKTFIMGILNVTPDSFVDGGKFNTLEKSIQQATALIEQGADIIDIGGQSTYPGAQQISIEEEINRVVPTIKKIREVLGNDIPLSIDTLHHQVAKEAILAGCNIINDVSGEFRVPIILNHSQPTTQYLQQKQNEQYLNNSNDSNSNSSINTNGEDNNNNNNNNNNNNNNNNNNNNNNNNNDDNDNDNRSKIKQKIDLSSPKIETCTKLGLFRWQIILDPGLGFYKTYEQSIEILQRGKELMGLGFPVLIGPSRKGFIANTIANAEKDKSLPPPSPKSERRLWGTIACCCIGSMWGANIIRIHDIPEIRDAMLISDSVNKPQRRYQIQK
The following text describes a protein:
Function:
The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating dsDNA into templates for DNA synthesis. A processive ATP-dependent 5'-3' DNA helicase it has DNA-dependent ATPase activity.
Sequence:
MEFENLKKIPHSLEAERALIGGIFYNQDLFDEIRDIVNAGDFYKIEHSSIYAAIEKVYSENKGIDGILIEEEIKKSNSKNKDEILEILSDILDEITSSYNLLEYANLIKEKAMLRRLGNVGAEITQLAYNDVRVAEEIIDEAEAKVLNLSKNILKNNIVDMKTAGVAEIMRMERVSENRGKTLGIPTGFIDLDKMTSGLNNSDLIILAARPAMGKTAFALNLALNAGKEKKNVLVFSLEMPVQQLYQRLLSIESGISQNKLKNAYLEEQDWEKLTIATGILSNSNIFVADLPHTNVLEIRSYARKMKSQKQLDLIIIDYLQLINGSGRGGSEFNRQQEISDISRALKGLARELDVPVIALSQLSRAVESRVDKRPMLSDLRESGAIEQDADIVAFLYREEYYIPDTENKGITELIIGKHRNGATGTVKLNFLSEFTKFTNYTDQVK
The following text describes a protein:
Function:
Exhibits holdase chaperone activity involved in the stabilization of POR proteins against photooxidative stress in chloroplasts. Required for chloroplast development.
Subcellular Localization:
Plastid, chloroplast envelope. Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Sequence:
MATTLISKLTLSSAFLGQQFSSRGNSMRSAPAGLFLRGPRCAATDTPYGGNIPQFPRVNVWDPYKRLGISRDASEEEVWSSRNFLLNQYYNHERSAESIEAAFEKILMASFINRKKTKINLKTRLKKKVEESPPWVQNLLSFVELPPPVIILRRLFLFGFMACWSVMNSTEAGPAFQVAISFGACVYFLNDKTKSLGRAALIGFGALVAGWFCGSLLVPMIPPNLLHPTWSLELLTSLFIYVSLFLGCTFLK
The following text describes a protein:
Function:
The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspC is involved in transcription regulation.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MAGINLNKKLWRIPQQGMVRGVCAGIANYFDVPVKLVRILVVLSIFFGLALFTLVAYIILSFALDPMPDNMAFGEQLPSSSELLDEVDRELAASETRLREMERYVTSDTFTLRSRFRQL
The following text describes a protein:
Function:
Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MDLKMRFSMCLLFLYGTFVLKMCIVLANHGKTPNCSKHQLVGGAIGGVLELNSRIGREQTIAMEMAVHDFCRTTNDTCSCPVLRVKDSQGSSAHSYYKESATMSSFVQISHDVKIHMQCIAAIVGHFSWRKVTPIYEDQSTFSASPGLLTLLSDALQVVDSTIERPLVFPPLHSLPNPSSYIIKELKKLRMKENRIFILLKSSPRSCILLFKKAKQLGMMEKGYVWIISDDISSLLDSVDQSVILNMQGVVGFKTHFAETGKHFTNFKVQFRKRFRNKYPNEEYLNPSINALRAYDATSVVVKAIQVSNGSSSSMNLSHSIIHTKLNGVSGDISFKDGKLAQLPTFCIINVIGRSYREIEFWSPAFGFLNDKLGTGEASLNLIYWPGGTQRIPMGRVLRNEEKPLKIGVPARGAFRQFVNVSYDPDKNETYVTGFSIQVFEAAVKKLNYSLSYVFIPYNGTYDDLVAEVHNKTLDAAVGDTEIMADRYEYAEFSQPYLDSGLVIVVPMKPNIMKERFIFFYAFTRKLWIILLAMTIGTVSVVWFNEHTHGNSEFVATSVFEYASKMLWFAVAVLSFAHRELITNNLSRLVLATWFCVNVIVAACFTATLSSIITISKLQPALDLQRSHVGCNRNSFIVPYLVNVLNIKAEKIRQINSIDDYDGAFKRGEIAAAFFVAPHANVFLAKYCHGYEKIGHTYKLGGFGFMFRKGSPLVEDISKAVLKVTQSGEVDTLQENMLRSFSNCSGSAEDQSRGSTGLDLGLFTGLFIISGSISAFVFFTALARVVINHWESIQTSLKLITRRIGNWWTMLLHIIIIDRKLSVGLTPNQAVP
The following text describes a protein:
Function:
Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes. Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity. Recognizes and binds poly-ADP-ribose chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting its activity.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MTIVQVKHVVSCTSEDTLHKADNLLKGDSYKKWTGGSEGEKQVSVILQLDKASNIHSIDVGNESSAFVEILGGHSSSDSDDLYQVILVTSSFMSPVESRNNTNMNRVRMFGPESLSKAVADKKFDRIKIVCTQPFNKRCKYGLSFIKLHGPPGAGDQQEGTSGQPTLGKFRLKEESKSSLSVGSFFKGRDTESTQKPLTGAAAVRAASSIPPSQQASSSSSTSSPKQPSQSSTKRRLSDADKKEGENSHKRPAVEPKREEPRRKESVPNKSKESKPQPATGEAFGKLMKKVVFVMSGFQHPLRGELRKKATEMGAKYQADWGPGATHLICAFANTPKYNQVKGKGKIVKKEWILDSYRKRTLLPWIRYKLSSGRDSSSDESESEEEEEMEEEEVVTPVKPSSSKSPQPKTPTPKKPADVDEYSGSTDEEGNDTEPMSGGSSGDDTEDEIRKAQAKPKAQTKTSPKGGSPCKKGQSSSPGEIPDLPDFFSSKRFFLFGKFDKEERRQVNRFIIAFNGLIENYMDESVNYVITNSNWDNNFEEALSENSSITFVRPRWLYACNEKLKMVPYQPYIVVPAN
The following text describes a protein:
Function:
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs. Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1). Also has 5'-3' exonuclease activity.
Miscellaneous:
MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSTEQDAVLGLAKDLEGINLLTVPNLERGHQSKLCKEKTTSDSSSSRKPSQQRDNYRKRRPKLICIPYTSFLHTGMHNFLTKPPRDIFHESKEVALFTNGRAYTILRKDLIPNLKESIAELYESSLLEAKKRKVPYLGHDLFANIDEFVPMTISELDSVSPCFSYIENWILDNPGKDFKIGKKFTVVTTRHHIVDLTMHLFNRRNRQTSLIVTYMGAGLLSFCRNVKKDSQMSKEGIYSNDPNMKKICYSGFEFENWVTENSKVADLTGSKCPIFSLVESKLSEEIGLLIRCEMDAFNPVSETNTELKCFAPLSMHNSNHRRKLLKTWVQTGLLPNSDIMIGLRDSHSGQLLDIQWYSRDLLCKKFNHPGLPTNKKELNYNAQIAVEWCHYCIEAICKLVEANISDYSSTKPESFEIGIDTNNAIVITKLKTTPRNVELFGM
The following text describes a protein:
Function:
Non-catalytic component of the proteasome.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MASFLTGGTVVAVAHKDGVLMAADTVLNYGSTRRTDNYERIIPVGTHTLIGFTGDEADFKDSLYTLKSMHREARCHGTPPPSTREIHGFLATRNYSSRLEMDPIYNGYIIGGCEPGESPYIGVVDLRGTQFTASFFATGMGRHYALPVLREGWKPGISKDEAVALLLESLKTLAFNDAAAGSSFIICEATSDGTHIGPVQTLDLDWSSAAYKDSAVN
The following text describes a protein:
Function:
Glycerophosphocholine acyltransferase (GPCAT) that utilizes acyl-CoA to acylate glycero-3-phosphocholine (GPC), forming lysophosphatidylcholine (LPC). Shows broad acyl specificities with a preference for 16:0-CoA, polyunsaturated acyl-CoA, and the hydroxylated ricinoleoyl-CoA. Also catalyzes the acylation of glycero-3-phosphoethanolamine (GPE) with acyl-CoA. In addition to acyl-CoA, GPCAT efficiently utilizes LPC and lysophosphatidylethanolamine (LPE) as acyl donors in the acylation of GPC. Contributes to the maintenance of phosphatidylcholine (PC) homeostasis and might also have specific functions in acyl editing of PC, such as transferring acyl groups modified at the sn-2 position of PC to the sn-1.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSNNEDPINEFVSNGDSFEKVKQRLKDRSKKVAQTKEILSKQANQTKEILSKQAVKIAKQAEEHESFINKVTHLLGVLGFGGFCFLLGARPQDIPYVYCLFFFIFVPLRWIYYRFKKWHYFLLDFCYYANTIFLVDLLLYPKDEKLFMVCFSFAEGPLAWALIVWRCSLVFSSVDKIVSVLIHLLPGLVFFTIRWWNPATFEAMHPEGTSGRASWPYVEDKSFLFTWLFLVPLVAYFLWQLLYFLIVNVLRRQRLLRDPEVMTSYRELSKKAQKANNVWWRLSGLLGDQNRMLMYILLQALFTVATTALTVPIFLSYELHAVFQILKVSAAVWNGGSFLLDVMPRQVILKEKKKSELQPAHIQQYHSEPKQDQSPNSMEIRMKTIHSAEEQ
The following text describes a protein:
Function:
Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Preferentially utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) as substrate: shows a higher activity towards an acyl-CoA substrate with a double bond at the delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z) positions.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
Each protomer consists of 9 transmembrane segments, which enclose a cytosolic tunnel and a transmembrane tunnel that converge at the predicted catalytic site: acyl-CoA enters the active site through the cytosolic tunnel, whereas cholesterol enters from the side through the transmembrane tunnel.
Sequence:
MVGEETSLRNRLSRSAENPEQDEAQKNLLDTHRNGHITMKQLIAKKRQLAAEAEELKPLFLKEVGCHFDDFVTNLIDKSASLDNGGCALTTFSILEEMKNNHRAKDLRAPPEQGKIFISRRSLLDELFEVDHIRTIYHMFIALLIIFILSTLVVDYIDEGRLVLEFSLLAYAFGQFPIVIWTWWAMFLSTLAIPYFLFQRWAHGYSKSSHPLIYSLIHGAFFLVFQLGILGFIPTYVVLAYTLPPASRFILILEQIRLVMKAHSYVRENVPRVLSAAKEKSSTVPVPTVNQYLYFLFAPTLIYRDSYPRTPTVRWGYVAMQFLQVFGCLFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVFNSILPGVLMLFLSFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTWNVVVHDWLYYYVYKDLLWFFSKRFRPAAMLAVFALSAVVHEYALAVCLSYFYPVLFVLFMFFGMAFNFIVNDSRKRPVWNIMVRASLFLGHGVILCFYSQEWYARQRCPLKNPTFLDYVRPRTWTCRYVF
The following text describes a protein:
Function:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Sequence:
MNTLTAGAKAPLFTLQDQQGNTVSLQECLTRGPVLVYFYPKASTPGCTVQACGLRDSKAELDSHSVTALGISPDPVAKLAKFAEKQSLNFTLLSDEDHSVADAFGVWGEKKFMGKIYDGIHRLSFLINTDGTIAHVFDKFKTSDHHQVVLAQIAGQ
The following text describes a protein:
Function:
Synthesis and degradation of fructose 2,6-bisphosphate.
Sequence:
MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMRVRKQCALAALRDVKSYLTKEGGQIAVFDATNTTRERRHMILNFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRINCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEYNLQGKIGGDSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVSTHRERSEAVKIQHFASVVRPSSYTELDFQSVESAKQDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEERVASTSAALPSCLPPEVPTQLPGQPLLGKACLRSVCHIFSKFSPY
The following text describes a protein:
Function:
The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs), including taf-4 (By similarity). Essential for early embryonic development, probably acting via activating transcription initiation by RNA polymerase II, as part of the TFIID complex. In early embryos, but not oocytes, remains, presumably inactive, in the cytoplasm as a result of binding to oma-1. Upon degradation of oma-1, taf-4 is released and bound by taf-12, and the taf-4/12 heterodimer translocates to the nucleus and transcriptional repression is relieved. Involved in lifespan extension in a manner dependent upon mitochondrial function. Plays a role in modulating polyribosome formation.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Localization is ubiquitous in one-cell and early two-cell embryos, then enriched in nucleus in all subsequent embryo stages. Localization to the nucleus is prevented by interaction with oma-1 and is sequestered in the cytoplasm, following fertilization, and thus allows for transcriptional suppression in early embryos, but not in oocytes. Localized to the nucleus in a taf-12-dependent manner.
Domain:
The histone-fold domain mediates hetero-dimer protein-protein interactions.
Sequence:
MSLPRFRLVQGKAIGERSTPGVSTPEPAPPQIKQEVDYQDAHQMAPEPVEAPQAQNHQMQPPRQPIQQQMQHFQSPSPMAPQGPPGTPQNSAAAAAAASDDKNVTKCVRFLKTLINLSNNDDPEMPDKAARVKELIRGVIYLETTAEEFTRNLQQVLKSQAQPHLLPFLQNTLPALRNAVRNGTASVEGVNPPPGYVFNNGRTPGPPQPPPPQQQSQQQPPLEMRQIPNPNQIPPQMVQGGPHMVSVGARPMIRPMGPGGPSPMGLQGPVRGPMGHQMVQMHPPPPPQQIQQQHPAPPVEMEVEENLQPTAAATATRQYPEGSLKSSILKPDEVLNRITKRMMSSCSVEEEALVAISDAVESHLRELITLMAGVAEHRVESLRIPENYVAIDDVKRQLRFLEDLDRQEEELRESREKESLIRMSKNKNSGKETIEKAKEMQRQDAEAKRNRDANAAAIAALSSNKTVKNKWENTGAATTAPRPRTVRVTTRDLHLLVNQDSRFTGTFIREKMSYGGPAVDTTI
The following text describes a protein:
Function:
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization.
Subcellular Localization:
Membrane; Single-pass membrane protein. Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
Sequence:
MTQSNPNEQNVELNRTSLYWGLLLIFVLAVLFSNYFFN
The following text describes a protein:
Function:
Histone H3-H4 chaperone that plays a role in maintenance of chromatin structure during RNA polymerase II transcription elongation.
Subcellular Localization:
Nucleus.
Sequence:
MDFVESEAEESEGEYEEGTVPNTKKFTEDDDEEEEEENPEDQDEQGNLRGFINDEDDEEDMEEDDEGGSESGGSDEEVGHKKRKHTFDDRLEDDDFDLIEENLGVKVKRQKFRRVRKMSDDEDEEEEDFGKEEHEKEAIAEEIFQDGEDEERRDVLDQPGAGPEDEDEDDDEESDIDDFIVDDDGQPLKKPKWRKKLPGYTDAALQEAQEIFGVDFDYNEFEKYDEDDEEMEEYDYEDDEGDAATRVRPKKTAKKRVSRRSIFEIYEPSELESSHLTDQDNEIRTTDMPERFQLRTISVKSAEDDELEEEAEWIYRNAFATPTISLQETNDYLERGQVGSNFNRKGPSTIQKIREALNFMRNQHFEVPFIAFYRKEYVEPELNINDLWRVWQWDEKWTQLKLRKQNLIRLFEKMQAYQYEQISSDPDKPLADGIRALDTVDMERLKDVKSMDELKDVYNHFLLYYGRDIPKMQNAAKSSQKKMKRIPEEGEEGADAGEQEEESSKGPELKQASRRDMYSICQIAGLDGLAKKFGLTPEQFGENLRDSYQRHETEQFPAEPLELAKDYTCSQFTTPEAVLEGARYMVALQIAREPLVRQVLRQTFQERAKVNIIPTKKGKKEIDEAHFAYAFKYLKNKPVKELRDDLFLKMCIAEEEQLLTIEICIDMKDVEGYGDQTYFEEIKQFYYRDEFSHQVQEWNRQRTLAIERALKQFLYPQMAKELKNKLVLEAKDFVIKSCSRKLYNWLKVASYRPDTQVEEDDDFMEENQGKGIRVLGMAYSSARDHPVFCSLINGEGEVTDFLRLPYFTKRKNAWREDERERKARDMETLKKFLISKKPHVVAIASENRDAQMMVEDVKRVVQELEQGQQMSAIGVEMVDNELAVLYMNSKKSETDFRDYPPVLRQAVSIARRIQDPLIEFAQVCSTDDDILCLKLHPLQEHVVKEELLNSLYCEFINRVNEVGVDVNRAIAHPYTQALIQYVCGLGPRKGAHLLKILKQNNTRLENRTQLVTMCHMGPKVFINCAGFVKIDTNSLGDSTDSYIEVLDGSRVHPETYEWARKMAVDALEYDESAEDANPAGALEEILENPERLKDLDLDAFAEELERQGYGDKHITLYDIRAELSCRYKDLRTTYRSPNPEEVFNMLTRETPETFYIGKLITCNVTGIAHRRPQGETYDQAIRNDETGLWQCPFCQQDNFPELSEVWNHFDSGSCPGQAIGVKTRLDNSVTGFIPTKFISDKAVKRPEERVKVGMTVHCRIMKINIEKFSVDLTCRTSDLMDKNNEWKLPKDTYYDFDTESADHKQEEEFKKKQQRTTYIKRVIAHPSFHNINFKQAEKMMETMDQGDVIIRPSSKGENHLTVTWKVCEGIYQHVDVREEGKENAFSLGSTLWINNEEFEDLDEIIARFVQPMASFARDLINHKYFQDCNNGEKKKLEELLIKTKKEKPTFIPYYISACKELPGKFLLGYQPRAKPRVEYVTVTPEGFRYRGQIFPTVNGLFRWFKDHYQDPVPGITPSSSSRTRTPASVNATPANINLADLTRAVNALPQNMTSQMFNAIAAVTGQHGQNPNATPAQWASSQYGYGGGSGGGSSAYHVFATPAQQPVATPLMTPSYSYATPSQPITTPQYHQLPPSATPTPAPTPQSSHSQSSSHSQSSSRHRQQSKSNNHTAIDWGKMAEQWLQEKEAERRKQKQRVTPRPSPSPMIESTPMSVAGDATPLLDEMDR
The following text describes a protein:
Function:
Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues (By similarity); PEX, the C-terminal non-catalytic fragment of MMP2, possesses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrin alpha-v/beta-3 on the surface of blood vessels (By similarity); [Isoform 2]: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: Induced by oxidative stress.
Subcellular Localization:
[Isoform 1]: Secreted, extracellular space, extracellular matrix. Membrane. Nucleus. Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes (By similarity); [Isoform 2]: Cytoplasm. Mitochondrion.
Domain:
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Sequence:
MEARVAWGALAGPLRVLCVLCCLLGRAIAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARALKVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGREYSSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRNDGKVWCATTTNYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSHDDIKGIQELYGPSPDADTDTGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPDVQQVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADSWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC
The following text describes a protein:
Function:
Catalytic component of the mitochondrial inner membrane peptidase (IMP) complex. IMP catalyzes the removal of signal peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. The two catalytic IMP subunits seem to have non-overlapping substrate specificities. IMP1 substrates include nuclear encoded CYB2, mitochondrially encoded COX2, NADH-cytochrome b5 reductase and GUT2.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MTVGTLPIWSKTFSYAIRSLCFLHIIHMYAYEFTETRGESMLPTLSATNDYVHVLKNFQNGRGIKMGDCIVALKPTDPNHRICKRVTGMPGDLVLVDPSTIVNYVGDVLVDEERFGTYIKVPEGHVWVTGDNLSHSLDSRTYNALPMGLIMGKIVAANNFDKPFWDGSIRNIWGFKWINNTFLDVQAKSN
The following text describes a protein:
Function:
Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
Sequence:
MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKHSERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS
The following text describes a protein:
Function:
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Subcellular Localization:
Nucleus.
Sequence:
MYDLKIYSSYIVAAIKDKIVFFSTDGAVLHTITVEQKAPVKDTDAGNEPNGNQTQPTPANVVTFEYCPTAKVLAVSLSDKTWRRYQLREEDGGKLCSAPLGEDITTARTIVSMKFVPKHGVLFGTDKSDCFEFGALDKTSEPQPKWILGHMSQILALAVSDDERFIVTSDRDEKIKVSSYPDCHNIECFCLGHTEYVGGIEIIPSEKLISVSGDRTLRLWDVTEGKELSKLSLKEPALDFTVQKVAEGCGMLCAVRSYVQNMVEVALVSYDKPDASELYDPLTIDESLIILNAGLSASLRLMLLTMEKESKRVRMLVYEFCAEKRAFKACDDHPFVKNFEDQFKDVTIEQVRDYSTLFKHTIDNLTEYFERKKIKMESKKSK
The following text describes a protein:
Function:
Ligand for members of the frizzled family of seven transmembrane receptors.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MDVFTKFVRHLLLLVVLLVNVPIFQAIIWSPASNVLLAGSKRHITYIDSVSAGIQNAVKECQFQFKWDKWNCPEVSVFTNTQANVRCVHSSHRVCGVMYSLTKNCSQGAFDDCGCDKRRNGNSGGEGWTWGGCSDNVRFGERMASDIMDDAESSQGAISVMTLHNNEAGRKAVKQTLQRTCKCHGVSGSCSLQTCWNHVANFRVIGDEIKRKYFQAVRVDFVRGKLIDGNSAEDRFPQAVVSASHNRRDLVFLDQSPDYCRANLTIGVTGTAGRECMVREDVTEVSSSSSLTKDSTSPSSFRWVKQSCSRLCRSCGMVIRKTQVIITSSCNCNFVWCCQVKCDTCRRTVTRRTCQPVG
The following text describes a protein:
Function:
Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Sequence:
MPFEFENLGMGIVLIKPKVFPDKRGFFLEVFKSEDFTKAEIPNIVQTNMSFSFKGVVRGLHYQITPKEQGKLVFVPKGKILDVALDLRKSSPTFGKYVKVELNDENHYILWIPPGFAHGFQALEDSIVVYFLTHNEYSKSDERCVNYSYVDWPIKEFIISDKDSQCPPLEKADVFN
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Sequence:
MFRNVISRAKVTQIGSIRSIHTPAKLSRESKYAQNGLEGLYSKNGFNTAWTDYQRFLVSKLTDLTVDTPLQSRSPFDILRFTAADRDQAATFNFASQAFNNHFFFEALAEKPVAQTTAPTDYLRSRLEDKFESMERARENFLATADEMTGNGWVFLYEGGDKNMYISAHHNAGSPFSFQRFQHQEFNFPASEEVKRDQQNIEAAVRKGLKESILPLLAVNVWQQAYVDDYGVNGKYNYLENYWECINWDVVNARLFVGAQ
The following text describes a protein:
Function:
Required for regulating the establishment of planar cell polarity in the wing. Forms a complex with Bdbt which likely functions in the regulation of planar polarity by promoting the activity of Dco during planar polarity establishment. Within the complex, probably functions to stabilize Bdbt, while Bdbt directly promotes Dco activity in regulating phosphorylation of core proteins such as dsh, and asymmetric localization.
Subcellular Localization:
Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MGDYDSDDEKSQVEKLRHAKVPRGMFVSGWDDDADELIEEDKNPQSSIERMILWAVNENRISEVREILKLDADTVNAKDNDGYTPLHRAAYNNFVDMAKLLLQYHANPNARTELGWTPLHSACKWNNADCAHLLLQFGADVNAESDGKQTPLHITATVSNCRNTATVLLLDRYIQPRKENNSEELASVIARRTGMSFPIFESGEEAYDCETGLID
The following text describes a protein:
Function:
Plays a role in promoting resistance to bacterial pathogens such as P.aeruginosa by inhibiting bacterial intestinal colonization; (Microbial infection) Promotes infection by microsporidian pathogens such as N.parisii in the early larval stages of development. Involved in ensuring the proper orientation and location of the spore proteins of N.parisii during intestinal cell invasion.
Subcellular Localization:
Secreted.
Sequence:
MRLLFFFSILYTASLCCQLKDFLPCVMQLSAQKVDFNMNPIEVIFNITTEAKLMHTCRTYSRILPCFDQKMVQCGKPSEKTQLERGKRLHSYLCAPFSLQRQKIFLRRSKCIQDVLAEPQSSVCNRNDTVFADKLQSCREMCTRPDCVSKIELSEVSTCTYINIGKKCTAEAAQFFAQMQQVLTNKEYPMQCQYDLRKKPESELKKGLPIESLVAQTTSSTTYVTVHPPALPSVIDGVVTRTSLPIMRRTDPNSKFKPRPTTSQSNGPVIKTVIVDERGAPMNQPTSTQKPKVVHKFLPNPYTTKNPNTLKNDIIRTTRTIIPVVDKHTYVPWNYKVDAVQVSTLTSALAPVKPTETVISSPPVAFNFKLPAEQTSTQPFRVEINWHDDEVKQEPTKAPGVFVSPWYLKTPSHIPPEIEFATPTPLISSPLEAVSPILSQLKSNSLNFTELGNQANNYFSAALSAFAETKKEMAHNDPWRTIIDAVAPTIHKFSPDVIPRIREEINRIQPHQQKN