lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of genome stability.
Subcellular Localization:
Cytoplasm.
Sequence:
MRLAAESSLVFFVSHFYFERFFSFVMVAYTLDTLFASDIDSATLFYSEGCGPIRLVALSAQMRRLVRLGPIRVAKACVEVRPMAPTKEFFEEGRQLQHIEAAGVGDFPDSERSGDTFVNPFTGRLTPTWGRVAKELFSLGFEHSIVNPFRLVWNPTKAALVSDAALQPFRTSTVTWRRNLAALLSRRDAADAVGEEIHRLYNEITSAYLPPKLDTMHDPRLSTMTMTPDQQNVIRCALRGYSMFIGGSAGTGKTVLLKAIHRKLTEMGLRVAMTATTGVASVQLGGCTFHLAFGVPIKGEEGTRKRWDSNAFRAVDVVIIDEVSLLDAELFETFEEEARMARLQQSPFGGLQVIACGDFLQLAMMDVSIGGPCYQSHAFRHLIPVCLVTSMRQAQGDPFCELLGQLRVGKFDKKAFKALDRPVSGDANNVTYIFPRRCDAQRLNDEKLCELRSEEMIFAPQRGPLQLVGNFTPAGLVDWGRKKDFPKREKIITVLSEEIKRITGVDIVDHNIVVMPAGGEKNAVLIRLRHSEDRNVLICKNGGSKEHGASNEGGAEESHWRAILEATAGRLKGKLHQIYNQDPHNFIPPSVSLMLADASLHPNAELISPLRLKLGCRVMINRNLSRTVSNGSVGIVEAFAAPNLDLFPRRHETSPKAFHTWSLERNGFQRLPIVRLLSGEVVQLPPLSVMIGGTPSTYFYGHELFVLPLQLGYGFTVHKVQGLTLEGTVVLDCKKFFECPHLVYVACSRVRSMDQLIVRNVRSDMIIVRQSALDFTNALRDASVMSSLDPPDGCTRASWVRRLSPLLVGLTD
The following text describes a protein:
Function:
Mediates sugar transport across membranes.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
RERRRKFILLSHSMDLLQLFGIWVSCMQISLLALPLSLVNQWRLRGSSHGFSVIQLLIPIPIQICWLRYGYLTVDMLMITTNVILLATSIAYLFIFIYYLPDKSTIVKEVSIMCAVIILLMIYVSIHPHNEQANIMGKIAPLVQNTRIMGAAHQLKDIIDKKTTEFLPYQMPFVMCAFISQNALYSFLAEKSPVVWASIPGLFFNFTFLIMYIVYPPKTWRVPIIGTGKKITAGEKKE
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent formation of L-aspartate 4-semialdehyde (L-ASA) by the reductive dephosphorylation of 4-phospho-L-aspartate. Mediates the second step in the biosynthesis of amino acids that derive from aspartate (the aspartate family of amino acids), including methioinine and threonine, the latter of which is a precursor to isoleucine.
Sequence:
MDKESWKAQSRTVGVLGATGTVGQRFIVLLSKHPNFKLIQLGASSRSAGKAYSNIVRWKQAVPIPDIVKDLVVQECNPEHFMDCDIIFSGLDADVAGEIESAFRAKDLPVFSNAKNYRRDPLCPLIVPLVNTEHLGIVEHQRKTHVDPLTKLPSPLKKGFIVTNANCSTTGLVVPLKALESSFGPIDKVVVTTLQAISGGGYPGVPSLDILDNVVPFISGEEDKIEWECLKILGTLDHSTHPTSIILRSEQSTDRSLTEVQKTSTGSMKISATTTRVPVLDGHTATVSLSFKNQPPPSPEDCVRALRAYRSEPQTFNCPSAPTHSIFVHDEEDRPQPRLDRYFQDGAGVSVGRVRKCQVLDIKFIVLSNNVSIGAATSSIMNAELAVAKNVV
The following text describes a protein:
Function:
Nuclear transport receptor that mediates nuclear import of proteins, such as histones, proteasome and actin. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates the import of pre-assembled proteasomes into the nucleus; AKIRIN2 acts as a molecular bridge between IPO9 and the proteasome complex (By similarity). Mediates the nuclear import of histones H2A, H2B, H4 and H4. In addition to nuclear import, also acts as a chaperone for histones by preventing inappropriate non-nucleosomal interactions (By similarity). Mediates the nuclear import of actin.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAAAAAAGAASGLPGPVAQGLKEALVDTLTGILSPVQEVRAAAEEQIKVLEVTEEFGVHLAELTVDPQGALAIRQLASVILKQYVETHWCAQSEKFRPPETTERAKIVIRELLPNGLRESISKVRSSVAYAVSAIAHWDWPEAWPQLFNLLMEMLVSGDLNAVHGAMRVLTEFTREVTDTQMPLVAPVILPEMYKIFTMAEVYGIRTRSRAVEIFTTCAHMICNMEELEKGAAKVLIFPVVQQFTEAFVQALQMPDGPTSDSGFKMEVLKAVTALVKNFPKHMVSSMQQILPIVWNTLTESAAFYVRTEVNYTEEVEDPVDSDGEVLGFENLVFSIFEFVHALLENSKFKSTVKKALPELIYYIILYMQITEEQIKVWTANPQQFVEDEDDDTFSYTVRIAAQDLLLAVATDFQNESAVALATAATRHLQEAEQTKASGTEHWWKIHEACMLALGSVKSIITDSVKNGRIHFDMHGFLTNVILADLNLSASPFLLGRALWAASRFTVAMSPELIQQFLQATVSGLHETQPPSVRISAVRAIWGYCDQLKVSESTHVLQPFLPSILDGLIHLAAQFSSEVLNLVMETLCIVCTVDPEFTASVENKICPFTIAIFLKYSNDPVVASLAQDIFKELSQIEACQGPMQMRLIPTLVSIMQAPADKIPAGLCATAIDILTTVVRNTKPPLSQLLICQAFPAVAQCTLHTDDNATMQNGGECLRAYVSVTLEQVAQWHDEQGHNGLWYVMQVVSQLLDPRTSEFTAAFVGRLVSTLISKAGRELGENLDQILRAILSKMQQAETLSVMQSLIMVFAHLVHTQLEPLLEFLCSLPGPTGKPALEFVMAEWTSRQHLFYGQYEGKVSSVALCKLLQHGINADDKRLQDIRVKGEEIYSMDEGIRTRSKSAKNPERWTNIPLLVKILKLIINELSNVMEANAARQATPAEWNQDDSNDMWEDQEEEEEEEEDGLAGQLLSDILATSKYEEDYYEDDEEDDPDALKDPLYQIDLQAYLTDFLCQFAQQPCYIMFSCHLNDNERRVLQTIGI
The following text describes a protein:
Function:
Pore-forming component of the membrane attack complex (MAC), a multiprotein complex activated by the complement cascade, which inserts into a target cell membrane and forms a pore, leading to target cell membrane rupture and cell lysis. The MAC is initiated by proteolytic cleavage of C5 into complement C5b in response to the classical, alternative, lectin and GZMK complement pathways. The complement pathways consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. Constitutes the pore-forming subunit of the MAC complex: during MAC assembly, C9 associates with the C5b8 intermediate complex, and polymerizes to complete the pore.
Subcellular Localization:
Membrane; Single-pass type I membrane protein. Secreted. Target cell membrane; Multi-pass membrane protein.
Sequence:
MMLPWGRGTAGPRAWRGTRKPRLLFLLLLLLLSLFLVQAADLAGSREPQFVWKAGPWGRCTGGCGGGGTQTRTVRCFHVDGRTSPQAHCLDEDKPEEERGCFRACTWHREFFEWEVAEWDACQLVPRVPTTDPGHRAIGTQEQTCTTAQPGLQRRPIRCVQKQNRTQVLVDICEQLAPRPPGEQACLMPCPRGCVVSEFSSWSACGPRCGASVQHRIRTLLVPPLFGGEACPSLSDVRGCESPAACTLGEPDVTTSLSAGPWSPCRPPPRRELASSRRTLLDFSSNRNERSPIRRQSYRAAQRLPGPRPPEIGYQTRQVRCVRSDGQSAPLSLCLPGSSLSTMRSCALPEDCETTDWSPWSLCSKTCQSEDHSPGLRSRRRRVRRVAVEAGRDCPALLETEACNLGGDTLQPCPRFSWKTSEWKGCQPGLLLESQNSRQRAGAVALCGGGLQIREVFCVQEGPETSALVFGGEGSRPVERKLCPGPAPSAIQLCYVPCSVDCMLSTWSTWGSCLPETCRDPQGKKGFRMRQRHVVIEVVGPTGRCPHLVEASLCEEPACHRWKVEAAHCVPEHGTCGPGQRKQRAECRDAQGEVVAPQLCPSPPPDEWTACTVPCDSDCVLSEWTQWTPCPQACVGKSGEGMQSRTRAVLAPPGDGGKPCPSGHALHQLRPCSDHPCTRFYWEASSWGPCLDAVGTTSLNSTIGWNGEATCGVGVQTRKVSCVNSHIGPVASKRCPDALRPETLQPCLLPCRRDCVVTPFSEWTPCPSSCRPGNGPRARQSRYRVIVEEAAPGGRDCPDTLFEERECDAAQPCPNFRWKTHPWSPCILVPEVVRQAALGSGEACGQGLQSRAVTCEAEAAQPVEMEECLRGPDPMPPLLQPCLLPCRDDCTFTPWSRFTPCSANCTSTRTRRRTLTGRSRKRERCLDGETYPLQETEPCPCHAFRAQPYGDWSDCILSDSVHEQQPRLGPVGGRAHGCGEGLRLRALACLDALGRLVALEHCGGSGYVEEACTIPCPFDCRLSDWSIWGPCSARCGVGVRTRSRWLKEKPHNGGRPCPTLDLRNQVHETMPCFDECHRYSWAAGPWSPCEIPGDPTALLCGEGLQTRKVRCVRTVGESGGEMVDRTLCDQTEIPAGAQRCIRFCPSQCVLSHWEPWSPCPQPCDPRTTQRRTRHVLRPALSGGTCAGDVQLRPCVLNENCFQHQYNLTEWSTCQLSGNTACGHGVQTRLLSCVRSDGAIVATGFCEELGLTKPSPLSSRCLVECVVDCRLSPWSSWSQCSQSCGLTGHMSRTRQVVLQPQGEGRPCPPRLSQIKPCPVKPCYAWLVGGWSPCTVEGGDCGEGLQSRTLTCVVHNASLTPSAPPVEEVLCARIPLPESPLQRLCSVPCPGDCHLAEWTSWSACELTCLDGRSFGATGHQSRSRASITQALNNRVSCPEQVLETRPCTGGKCFHYEWKSSLWRNNERAVWCQRSDGMNVTGGCSPQSRPVAVRHCHPDCRKPFSYCTQNGVCGCKPGYTEILRSNGFLDYCLKVSSSGDRKADVKTSTAKNKPVNSKIRDIFRTWSLHPVDADGRVKLWVYGISAGGILLVLLLTFLSYLVCKKPSQHQSPAPQQKPLTLAYDGDVDM
The following text describes a protein:
Function:
Background potassium channel. Rectification is dependent on external potassium concentration. Acts as an outwardly rectifying channel but as external potassium levels increase, this is reversed.
Miscellaneous:
MISCELLANEOUS: Inhibited by barium.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSPNRWILLLIFYISYLMFGAAIYYHIEHGEEKISRAEQRKAQIAINEYLLEELGDKNTTTQDEILQRISDYCDKPVTLPPTYDDTPYTWTFYHAFFFAFTVCSTVGYGNISPTTFAGRMIMIAYSVIGIPVNGILFAGLGEYFGRTFEAIYRRYKKYKMSTDMHYVPPQLGLITTVVIALIPGIALFLLLPSWVFTYFENWPYSISLYYSYVTTTTIGFGDYVPTFGANQPKEFGGWFVVYQIFVIVWFIFSLGYLVMIMTFITRGLQSKKLAYLEQQLSSNLKATQNRIWSGVTKDVGYLRRMLNELYILKVKPVYTDVDIAYTLPRSNSCPDLSMYRVEPAPIPSRKRAFSVCADMVAAQREAGMVHANSDTELSKLDREKTFETAEAYRQTTDLLAKVVNALATVKPPPAEQEDAALYGGYHGFSDSQILASEWSFSTVNEFTSPRRPRARACSDFNLEAPRWQSERPLRSSHNEWTWSGDNQQIQEAFNQRYKGQQRANGAANSTMVHLEPDALEEQLKKQSPGAGRVKKFSMPDGLRRLFPFQKKRPSQDLERKLSVVSVPEGVISQQARSPLDYYSNTVTAASSQSYLRNGRGPPPPFESNGSLASGGGGLTNMGFQMEDGATPPSALGGGAYQRKAAAGKRRRESIYTQNQAPSARRGSMYPPTAHALAQMQMRRGSLATSGSGSAAMAAVAARRGSLFPATASASSLTSAPRRSSIFSVTSEKDMNVLEQTTIADLIRALEVVHTHAVLDEQQQAAAAGGAAGGGGISRGSRKQRKMGNAGLEPPQLPPILSLFAGDQTRTLQAAAANRLYARRSTIVGISPTGGAATAPAARSLLEPPPSYTERAANQSQITAGPSNAPTVQSKFRRRFSVRPTALQIPPGQAPPPGASLMEQSSQTALQRRLSLRPSPLARELSPTSPPGGSGSALPAGAIDESGGTSAQRLLPLPAGTRPSTSSTHSPLSRIVQISQAQRKSSMPSAAATGSSGAPAEK
The following text describes a protein:
Function:
Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Increases AURKB activity. Inhibits apoptosis induced by TGFB1. Overexpression induces swelling of mitochondria and reduces mitochondrial membrane potential.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Membrane; Single-pass type I membrane protein. Mitochondrion.
Sequence:
MPAGAGRHSLPQRSHLCWLLCALTLQLCRAEAPVRAEKLSVSTSNLPCWLVEEFVVAEECAPCSSFRAKTTPECGSTGYVEKITCSSSKRNEFKSCRSALMEQHLFWKFEGAVVGVALVFACLVIVRQRQLDRKALEKVRKQIESI
The following text describes a protein:
Function:
Regulates mitochondrial small subunit maturation by controlling 15S rRNA 5'-end processing. Localizes to the 5' precursor of the 15S rRNA in a position that is subsequently occupied by mS47 in the mature yeast mtSSU. Uses structure and sequence-specific RNA recognition, binding to a single-stranded region of the precursor and specifically recognizing bases -6 to -1. The exchange of Ccm1 for mS47 is coupled to the irreversible removal of precursor rRNA that is accompanied by conformational changes of the mitoribosomal proteins uS5m and mS26. These conformational changes signal completion of 5'-end rRNA processing through protection of the mature 5'-end of the 15S rRNA and stabilization of mS47. The removal of the 5' precursor together with the dissociation of Ccm1 may be catalyzed by the 5'-3' exoribonuclease Pet127. Involved in the specific removal of group I introns in mitochondrial encoded transcripts.
Sequence:
MKVSSRFEGSICGTIFLHRPSWNWSAIAASATAIAATSSVSQTTASIQLGDQGSGRRRQVATAGLGPVQQRRCFHGSWSSQSGGLVDGVARRPIGGSTGCPLLTTPSLRVTPTSLSGTNSRRALDSNFFRYSVSAPQKRSHTAAAAAAAAPVPDPVAAAAPEPSADQKPADSVFSAPSALHDDLSTESHSGANPQSQELPESHSAKLGHLTKEELLELVDPYHDLDGTVEDYLKFIRDPYMHNYAPADRPRFTFVQNEDDYEYPGPDEVVGLDEFGQHTLSDLRFAVLVRLRTPHKVDLDTIYDLYQQLPEPRMPYINGRLRHQLLKALGQPQRRNSKSMLRYFAVIADVRNCSMPLTAGEWNCAISFASRYVGTVTETQAQSAMRLWREMEVDAGIKATEVTFNILFDVASKAGNFTLAEMIYQEMVSRGHYFNRYHHVSLIHFFGLKRETGGLRAAFREMVEAGEMIDTVVLNAVISGLLRSGEEAAAERIYARMVASIAKWSEVSFPTRSYASDRAITQALKMMARVAKKAPELQHSFQEMVPMHPNLRTYSILVKYYGVRCGDLSRVAKYIDDMKLFDIPVHGSIFKVLFRAFDRHGGYATSAWSARRLESIYSALLEAIDAGRTLIHDSAPPPVDEAAFTDDQAQETQFHEPVQVQQDHIQEEHLPDIYDDEAELPFEEEEYQQKKEWGVDRPGIEIKTWLAIWVLRAFMRCTNGDRVVEVYDQLRARWELSDKDELFMADFLSSLLINGSRRGKW
The following text describes a protein:
Function:
Required for high affinity copper (probably reduced Cu I) transport into the cell.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSLSKMSMSGMSGMGMGSSSNSSAATCRMSMLWNWYIHDSCFLAKSWHINTGNKFAGSIIGIFFFAVAIEGLSLVQRMFDRWIVAHSNGKTLSGPLRIFFPSSTVHVTVWQQLIRAAMYSSFYLSATILMLIVMSFNGYAILFGFVGAWIGFFLFASDTYGTPSTGTGCCESR
The following text describes a protein:
Function:
Probable ligand of the IGFLR1 cell membrane receptor.
Subcellular Localization:
Secreted.
Sequence:
MKIRNACAVLIEVLLFILEGVTGARKISTFSGPGSWPCNPKCDGRTYNPSEECCVHDTILPFKRINLCGPSCTYRPCFELCCPESYSPKKKFIVKLKVHGERSHCSSSPISRNCKSNKIFHGEDIEDNQLSLRKKSGDQP
The following text describes a protein:
Function:
ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombination during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork. FANCM-MHF also promotes non-crossover recombination in meiotic cells.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MSDDSFSSDEDWDELDTQVVDKIENEYHNNTIGLNGYSVDEYFDANDSNRYRLQHELDESAAQQWVYPINVSFRDYQFNIVQKALFENVLVALPTGLGKTFIAAVVMMNYLRWFPKSYIVFMAPTKPLVTQQMEACYKITGIPKSQTAELSGHVPVTTRNQYYQSRNVFFVTPQTILNDIKHGICDRTRISCLVIDEAHRSTGNYAYVEVVHLLSLSNKNFRILALSATPGNKLEAIQNVIDSLHISRIEIRTENSIDISQYVQKKEVDFFPVDLSAEITDIRDRFSSILEPMLQKLNKGNYYRIQNAKDITSFTVVQAKQAFLAMSGQNFPANQKWDILNTFDALATFAYPLNLLLNHGIRPFYQKLREVEEECFVGRSGYKKRIINHENYRPLMDDIEILLRDQSFVGHPKLEHLERIVTEYFEKEQTKDTRIMIFVEIRSSAEEILRFLGKFYPNVRPAIFIGQSAVRKAAGMSQKLQNETVKQFQKGEVNTLIATSIGEEGLDIGEVDMIICYDASASPIRMLQRMGRTGRKRKGYIYMLLTRGKEEAKWERAKDAYRTLQDNIVSGRGLSLSEKSYRILPEKFRPVCDKRVIEIPKENEEVVVAPKKVQLRTKIKKKFFMPENALNGFITASALGKPKRALAKSEESPFEICPVTYSIEQEKKLEKYKRVCLRGLDIHRNRRLSQLSVTGRIPHSLATKSIHSFLKHLNTIDSQKAQEWRREINNQFQVSNINSTDRDTKQPKMHDFRQPLHPNPMTTLKRKGQHNSFSYDKSTLFYDNNNNLEEDLPDVNISISSRNEEASKTKPFDDRQQRLQQLVEKRKRMKGMLI
The following text describes a protein:
Function:
Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP-mannose.
Subcellular Localization:
Cytoplasm.
Sequence:
MTASKISDVSFVTDFVSKYQKGMEMSYTLDGNSRVSEFNQKMSSVSILLFHRDLEQFLLVRQFRPAIFTASISNSPENHGKEFDKIDWSSYDSETGYTIELCAGLIDKEGLSPREIASEEVAEECGYRVDPDDLIHVITFVVGAHQSGSAQHLYYAEIDESMKISEGGGNVHEGEVITKVYYPVNVAREIARPAIGTHAEVKGPPGVLFAFQWWFLVLDPKKKGLIATPPTGYQWQPHNVKTISNVKFNTDFDKKKYGYNPKRMIFTINGITRNWDLALCPNTATCILVDMVKKELIFLQKLRAPVFVGKNRFLKENIGKPLDEIDFSNSDPKIAYTLELVVNRVPDFDDPRKFARISVKQLGYDLPEDSFKLQAKCIPGIGQSGDTQSIFAVDVSKARLCEKEEDEDIEELRVSFADLPSLYRQHNIGPPTTYYAIGFALDQLLERDTL
The following text describes a protein:
Function:
Potential calcium sensor.
Sequence:
APTPPRSDFSGRSTQFRPPPWSPSPPPDLDMSDATTAPAVAAGAGDPAVDAAAHKPVAPSPETTRRGGSSVVAAISQAAQQQQQQQSRLDDDQLAELREIFRSFDRNADGSLTQLELGSLLRSLGLTPSADQLDALITRADTNSNGLVEFSEFVALVAPDLLADSSPYSEDQLRRLFAIFDRDGNGFITAAELAHSMARLGHALTVKELTGMIKEADTDGDGRINFQEFSRAITAAAFDNIFS
The following text describes a protein:
Function:
May be involved in neurite outgrowth.
Sequence:
MATSRSPLPSPSPQESLATACHAHLHLRCQPLSRSSSSLLGPRPADAQDGPGSRTELRKSTSSTVCQGSLGQGELQGTLRADLPPSAGISPERRVGEEAEEPAGMADHDPPEVWSPGAWGTRGLGVYGKSSKEENVAPEGAMQRSHSDLTHADRTPGSIPAKEASASCSALGTLSGALGCHAGRWCGGLMGQENRNRFVPMTLPAGPNASTGRVAGGPAPPSATGYSDPGPLLSPVPGARLSRNSCLYSLVFPQGGGAYGTLPDAPRPVPVLPIHRPAATPCPAGAVVKVGDTYPAYCHPLPIPAVQLVSQLGGPGRDGSGPSCWHGPPPLESPSFPQLVTSVSEPGLGIGQLATCCGSAGEWPVSGHGSSRARVAPWEIPACPASGGSQPETGPATRTKDVWTMTSLGDLSPRCQDAEVQTAPLPACKSVGTSPRAEGDALPHVFPEVNLEPGPADAKSPVRDVRWDNEGMTWEVYGASVDPEVLGLAIQKHLEIQIEQFQLEPSEGAPSGLKDAPTKEAKRRPFRTVIHSLSRPSCCARSSTTLE
The following text describes a protein:
Function:
Receptor for the netrin NTN4 that promotes neuronal cell survival. Plays a role in cell-cell adhesion and cell guidance. Receptor for netrin involved in cell migration (By similarity). Plays a role in the regulation of neuronal cell migration in the developing brain via its interaction with FLRT2. Plays a role in axon guidance by mediating axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. May play a role in apoptosis in response to DNA damage. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). Mediates cell-cell adhesion via its interaction with FLRT3 on an adjacent cell.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MGTGAADGSRGARRWLPWLGLFFWAAGAAAARGADGSEILPDSIPSAPGTLPHFIEEPEDAYIIKSNPIALRCKARPAMQIFFKCNGEWVHQNEHVSEESLDESSGLKVREVFINVTRQQVEDFHGPEDYWCQCVAWSHLGTSKSRKASVRIAYLRKNFEQDPQGREVPIEGMIVLHCRPPEGVPAAEVEWLKNEEPIDSEQDENIDTRADHNLIIRQARLSDSGNYTCMAANIVAKRRSLSATVVVYVNGGWSSWTEWSACNVRCGRGWQKRSRTCTNPAPLNGGAFCEGMSVQKITCTALCPVDGSWEVWSEWSVCSPECEHLRIRECTAPPPRNGGKFCEGLSQESENCTDGLCILDKKPLHEIKPQRWSRRGIENASDIALYSGLGAAVVAVAVLVIGVTLYRRSHSDYGVDVIDSSALTGGFQTFNFKTVRQGNSLLLNPAMQPDLTVSRTYSGPICLQDPLDKELMTESSLFNPLSDIKVKVQSSFMVSLGVSERAEYHGKNHSGTFPHGNNRGFSTIHPRNKTPYIQNLSSLPTRTELRTTGVFGHLGGRLVMPNTGVSLLIPHGAIPEENSWEIYMSINQGEPSLQSDGSEVLLSPEVTCGPPDMLVTTPFALTIPHCADVSSEHWNIHLKKRTQQGKWEEVMSVEDESTSCYCLLDPFACHVLLDSFGTYALTGEPITDCAVKQLKVAVFGCMSCNSLDYNLRVYCVDNTPCAFQEVISDERHQGGQLLEEPKLLHFKGNTFSLQVSVLDIPPFLWRIKPFTACQEVPFSRVWSSNRQPLHCAFSLERYTPTTTQLSCKICIRQLKGHEQILQVQTSILESERETITFFAQEDSTFPAQTGPKAFKIPYSIRQRICATFDTPNAKGKDWQMLAQKNSINRNLSYFATQSSPSAVILNLWEARHQQDGDLDSLACALEEIGRTHTKLSNITEPQIDDADFNYSRQNGL
The following text describes a protein:
Function:
Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.
Sequence:
MAFEQRIEAAMAAAIARGQGSEAPSKLATALDYAVTPGGARIRPTLLLSVATACGDDRPALSDAAAVALELIHCASLVHDDLPCFDDAEIRRGKPTVHRAYSEPLAILTGDSLIVMGFEVLARAAADQPQRALQLVTALAVRTGMPMGICAGQGWESESQINLSAYHRAKTGALFIAATQMGAIAAGYEAEPWEELGARIGEAFQVADDLRDALCDAETLGKPAGQDEIHARPNAVREYGVEGAAKRLKDILGGAIASIPSCPGEAMLAEMVRRYAEKIVPAQVAARV
The following text describes a protein:
Function:
Catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, which can be subsequently metabolized to cholesterol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Sequence:
MATNQSISIFSSASLAVEYVDSLLPENPLQEPFKNAWNYMLNNYTKFQIATWGSLIVHEALYFFFCLPGFLFQFIPYMKKYKIQKDKPETWENQWKCFKVLLFNHFCIQFPLICGTYYFTEYFSIPYDWETMPRWYIALARCFGCAVIEDTWHYFLHRLLHHKRIYKYIHKIHHEFQAPFGMEAEYAHPLETLILGTGFFIGIMLLCDHVILLWAWVTVRLIETIDVHSGYDIPLNPLHLIPFYAGSRHHDFHHMNFIGNYASTFTWWDRIFGTDAQYNAYNEKRKKAEKKTE
The following text describes a protein:
Function:
May be involved in neurite outgrowth.
Sequence:
MDFLSERERVVCNQMTTTDNPAIHPLCPVHLERSERARVQERKEVKEAGAVWAEGKETRGGSGRNFTMEEEQRPTSEIYLPSISLGSVDAETVDDHELPIISLSKSSTEMVSGPPQRTELAWYRQNLRKSVSSAACTQRPVSLGGPATGVFEHEQGSICSGNSTPETVIWHGGTAGSWSVMEDSPRRTPTQDLFLGQNQVHSGVKCVPHSPSTNRDLRIKGLVCKEGCCRFCGPAENLTGCSCCRVACQMSSSGLNNSYTPQGVNTEDHVQSNCESHHLTACHRSTCSGHMMNTACLRNPCSVIPCPGHFISRPPCTGSPCAGQRSLLHSGLLGFPPLVSSVSETRLDSRSTVHCCGSELRGQNSSCLRLDRKGQTTLNRTVKDATTMTSDHQLKDAGVQTISNSLVSSLSHVFPEISLRADPTSEAHLTTEHMCHRTPVKEVEWDAEGMTWEVYGAAVDPEELGLAIQKHLELQIKETAAAAAAAAQTEDSTDNISNLALQSRPRKKSEGIIRTLRSSACCSNPSTVGD
The following text describes a protein:
Function:
Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantiomer.
Sequence:
MDSQILKFWPIIPSKNLIFNSKKAVPIRGLSNTRFRVAAAGSVQKSEEEWRAILSPDQFRILRQKGTETQGSGEYNKFFGVGTYLCAGCGTPLYRSATKFNSPCGWPSFYEGLPGAINRNPDPDGIRMEITCAACGGHLGHVFKGEWFRTPTNERHCVNSISLKFKPPQFS
The following text describes a protein:
Function:
Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins; (Microbial infection) Acts as a receptor for CdiA-EC93, the contact-dependent growth inhibition (CDI) effector of E.coli strain EC93; antibodies against extracellular epitopes decrease CDI. Its role in CDI is independent of the other Bam complex components. Is not the receptor for CdiA from E.coli strain 536 / UPEC, which does not have the same mode of toxicity as CdiA from strain EC93; the decreased expression of bamA101 in some experiments decreases the level of outer membrane proteins in general. Susceptibility to CdiA-EC93 is dependent on E.coli BamA; replacing BamA with the gene from S.typhimurium LT2, E.cloacae ATCC 13047 or D.dadantii 3937 renders cells resistant to CdiA-EC93. Cells with BamA from another bacteria no longer form CdiA-EC93-induced aggregates with EC93 cells. A chimera in which E.cloacae extracellular loops 6 and 7 are replaced with loops 6 and 7 from E.coli is susceptible to CdiA-EC93 and to CdiA-CT from strain 536 / UPEC.
Subcellular Localization:
Cell outer membrane.
Domain:
Contains 5 N-terminal periplasmic polypeptide transport-associated (POTRA) domains which interact with other subunits of the complex, may recruit substrates from the periplasm into the outer membrane and also act as a chaperone. The C-terminal region forms a discontinuous 16-stranded beta-barrel transmembrane region. The central pore is ellipsoid, and probably closed by extracellular loop 6, perhaps with the aid of other loops.
Sequence:
MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGDTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTIADIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAEIQQINIVGNHAFTTDELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYVTVNITEGDQYKLSGVEVSGNLAGHSAEIEQLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSMPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDAVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYAVGINGTKNDYQTYAELSVTNPYFTVDGVSLGGRLFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNSLRAGLGYVHNSLSNMQPQVAMWRYLYSMGEHPSTSDQDNSFKTDDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVTLDTATYVPIDDDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYFPHQASNYDPDYDYECATQDGAKDLCKSDDAVGGNAMAVASLEFITPTPFISDKYANSVRTSFFWDMGTVWDTNWDSSQYSGYPDYSDPSNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW
The following text describes a protein:
Function:
Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.
Sequence:
MPEPTKKIVSAFSKKPKSQTAEIGARVIFEAETEKPGVKVKWQRESKDILPSHKYTISAEDNKHSLTINNIIQEDAVGYAVIAGMSKVKFELKIKESEVKGVEKAKSPDPAAVEHKPEESKPEESKPEPKEPPPAPTENSAPESTGPPSDGVAPEALPESHQPDTRQDLTGLFTEKPHSGEVNVGENIIFIARVCGESLLKKPTVKWFKGKWMDLASKSGKHLQLKEHYDRNTKVYTFEMHIIAAKANFAGAYRCEVSSRDKFDSCNFDLIVHEARTTEGFDIRTAFRRTSTDAGDDSGELDFSALLKKRDSFVKTGQRAVHVSTEPDVDVWDILQKAPPSEYEKIAFQYGITDLRGMLKRLKKMKKEEKKSAAFLKKLDPAYQVEKGHKIKLEIEVANPDAEVKWLKNGQEIHPTGSKYIFESVGNKRFLTINNCSLSDDAAYMCVVGDEKTVTELFVKEPPVLIVRNLEDQMAMKGDRVEFECEVSEEGAQVKWEKDGVELTRDESFKYRFKKDGCKHVLIINDVTKEDCGHYRVKTNGGQSLAELMVQEKQLEVYQSIADLTVKAKDQAVFKCEVSDENVKGIWYKNGVEVKPDARTLITHIGRIHKLTIDDVKPEDEGDYTFVPEGFAFNLSAKLNFLEVKIDFVPRQDPPKIHLDCMGRTAESTILVVAGNKLRLDVPITGDPAPTVIWTKGEKVLTDSDGRVHVESTKGHCIFTIEGAERQDEGVYSVIVRNPAGEDTADINVKVVDVPDPPEAPRILSVGEDSCVVQWDAPRFDGGQPVIGYVLERKKKKSYRWMRLNFDPYKETTFEAKKMIEGVPYEMRVYAVNAIGMSRPSAASQPFVPVAPTSEPIGLCVDDISDTTISLKWRTPERIGSAELEGYGVEYCKEGSDEWIPAFSGLTERTSVIIRDLPTGEKMQFRVRAYNMAGPSAPATLQQAVTIREIMQRPKIWLPRNLRQTLIKKVGETINLVIPFQGKPRPQVSWTKNDEPLDPKSVSIRNSDTDTILFIRRSERKDSGKYDVQVQIENVEDKASVNIQIVDVPGPPQNLKVMDVWGFNVALEWKPPKDNGNCDITGYNIQKADKKTMEWYTVFEQYRRTNCVVSDLIMGNEYVFRVYAANMVGLSPEPCLSKDSAYIQKTGIVYKPPSYKDHDFSEAPKFTHPLKSRSVIAGYNATLSCSVRGIPKPKITWYKNKMDITNEAKYRMFSNQGVLTLEIRKPCPFDGGVYMCKAVNDSGEDLVECKLEVRLPQVTKEDIKK
The following text describes a protein:
Function:
Plays a role in nuclear egress of nucleocapsids and intranuclear microvesicle formation.
Subcellular Localization:
Virion. Host cytoplasm. Host nucleus. Note=Localizes predominantly in the host intranuclear rim, site of several morphogenetic processes associated with occlusion-derived virions (ODV).
Sequence:
MSNLMKNFFTELVKSTTFTTKVSVVKTTLSNWLCEQVYPDKDFSLKLKRVVNMFLNNEIENNKIYKLVETVDSSNKLSRRQVDFLIHALLNNVSVTFTLHRFVDDNVLTQDELSFLANFLVTKMDEAYQLPAY