lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular Localization:
Nucleus.
Domain:
The F-box is necessary for the interaction with ASK proteins.
Sequence:
MDSGSAVDIISTLSDFLLVLIISNLSFKEALSTSRLSTRWRHICRETRNISFREDEIVTFADDSVARYYQRAALVAYMVGWVNNFTGGVVESFELRLSNSYAFEEGVTTLIEFAVSKNVKHLFLDLSEPRWVTNNDAAQLEPGLIKLPESFYKITSLVTLKLFGCRFEPSRLAKPGMVKTMFFRWIRLEMLSALIAKTPLLEILNIKNCWEIGLDAITGYNDRLMKLVFKYCSFSAQQTTLDVPNIQIFKYFGKVYRFEFASANKLMEEAYLDYREESRYNVSAGAIISGFLYSMLSAKTFTICPYVLQLIQECEDPVRLKAPMETRQLVLKTNFEPNEFVGIRFMLNSSPYLETLSFQMVGPRPIEEMVPQIDPEAYWGQNTSHECLKKTLKKVEVWSFYGGTHELRVLEYLIRYGRMLERVDLYQPIGLDDIQLLPIRAAADRVGEFEARSENLVVTFY
The following text describes a protein:
Function:
Catalyzes the attachment of serine to tRNA(Ser) (By similarity).
Miscellaneous:
MISCELLANEOUS: Present with 405 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion matrix.
Domain:
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Sequence:
MIIRRLFSISNRSFFLKKPQFDVKKIIEMIPQYQTSIQNRELIEADSIIRSLQLLGERYQNIKEIDKVIADIQIQRKSIEAQIKKDKTKITEYSAALKALKEQYNDQNSKSSELKKKILETCKSLPNTLDPTVPLDAPQIEQWINPLKTHKTSEAQAHVDIMLKKNMLDLQTASNVTGMSWYYLLNDGARLEQALVAYALKKANENGFSSCVPPSITKKELIDACGFNPRDMNNERQIYALQDTNLGLVATAEIPLAGLGANKVLELNSGECSKKLVGVSRCYRAEAGARGKDTKGLYRVHEFTKVELFCWSKPETSAKVLEEIKQFQISVVEELGIPAKVLNMPSNDLGNPAFKKYDIEAWMPGRGKFGEISSASNCTDFQSRRLNTKYRDDNTGKLEYVHTLNGTAMAIPRVIVALVENFYDPSTGKISVPECLREFMNGQRYI
The following text describes a protein:
Function:
Is able to catalyze the biosynthesis of dTMP using dUMP, tetrahydrofolate and formaldehyde in vitro, i.e. a reaction equivalent to that catalyzed by bacterial thymidylate synthases (EC 2.1.1.45). However, M.jannaschii like most methanogenic Archaea lacks folates, thus the physiological cosubstrate is unknown but is likely one of the non-methylated methanopterin biosynthetic intermediates.
Sequence:
MVLNINSFYKNCRGEFMRAVFIYHKNNQRMEKFYKNLLNEPDFCRICDDCYNCRGNWTFKNNVKNIVIEEVYEEFVDNPYDYLPELPEGDICIAQLHEDLLYELPLLLKEKGYKALIVPSETPHDLSLALRRDLKRVCSNYNIEFENPKPFCSLEKKEGNEYINKFIDYFKIGKPELEIEVENGLIKDVKVKISAPCGETYYIAKRLKGKAIDDLKEEIANAHHNYPCLASMEMDKELGDTILHKAGYIAFEVVEKALKK
The following text describes a protein:
Function:
Truncated and inactivated form of SRK, the female specificity determinant of self-incompatibility when active. Most A.thaliana cultivars contain such an inactive form and thus, are self-fertiles.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Domain:
The protein kinase domain is predicted to be catalytically inactive.
Sequence:
MRGELPNKHHSYTFFVFLFFFLILFPDLSISVNTLSATESLTISSNKTIVSPGGVFELGFFRILGDSWYLGIWYKKISQRTYVWVANRDTPLSNPIGILKISNANLVILDNSDTHVWSTNLTGAVRSSVVAELLDNGNFVLRGSKINESDEFLWQSFDFPTDTLLPQMKLGRDHKRGLNRFVTSWKSSFDPSSGSFMFKLETLGLPEFFGFTSFLEVYRSGPWDGLRFSGILEMQQWDDIIYNFTENREEVAYTFRVTDHNSYSRLTINTVGRLEGFTWEPTQQEWNMFWFMPKDTCDLYGICGPYAYCDMSTSPTCNCIKGFQPLSPQDWASGDVTGRCRRKTQLTCGEDRFFRLMNMKIPATTAAIVDKRIGLKECEEKCKTHCNCTAYANSDIRNGGSGCIIWIGEFRDIRNYAADGQDLFVRLAAAEFGERRTIRGKIIGLIIGISLMLVLSFIIYCFWKKKQKRARATAAPIGYRDRIQELIITNGVVMSSGRRLLGEEEDLELPLTEFETVVMATENFSDSNILGRGGFGIVYKGRLLDG
The following text describes a protein:
Function:
A beta-galactoside alpha2-3 sialyltransferase primarily involved in terminal sialylation of ganglio and globo series glycolipids. Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through an alpha2-3 linkage. Sialylates GM1/GM1a, GA1/asialo-GM1 and GD1b gangliosides to form GD1a, GM1b and GT1b, respectively. Together with ST3GAL3, primarily responsible for biosynthesis of brain GD1a and GT1b that function as ligands for myelin-associated glycoprotein MAG on axons, regulating MAG expression and axonal myelin stability and regeneration. Via GT1b regulates TLR2 signaling in spinal cord microglia in response to nerve injury. Responsible for the sialylation of the pluripotent stem cell- and cancer stem cell-associated antigen SSEA3, forming SSEA4. Sialylates with low efficiency asialofetuin, presumably onto O-glycosidically linked Galbeta-(1->3)-GalNAc-O-Ser.
Subcellular Localization:
Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted.
Sequence:
MKCSLRVWFLSVAFLLVFIMSLLFTYSHHSMATLPYLDSGALDGTHRVKLVPGYAGLQRLSKERLSGKSCACRRCMGDAGASDWFDSHFDGNISPVWTRENMDLPPDVQRWWMMLQPQFKSHNTNEVLEKLFQIVPGENPYRFRDPHQCRRCAVVGNSGNLRGSGYGQDVDGHNFIMRMNQAPTVGFEQDVGSRTTHHFMYPESAKNLPANVSFVLVPFKALDLLWIASALSTGQIRFTYAPVKSFLRVDKEKVQIYNPAFFKYIHDRWTEHHGRYPSTGMLVLFFALHVCDEVNVYGFGADSRGNWHHYWENNRYAGEFRKTGVHDADFEAHIIDMLAKASKIEVYRGN
The following text describes a protein:
Function:
Acyl-CoA-independent ceramide synthase that catalyzes the conversion of dihydroceramide and also phytoceramide to dihydrosphingosine or phytosphingosine. Prefers dihydroceramide. Very low reverse hydrolysis activity, catalyzing synthesis of dihydroceramide from fatty acid and dihydrosphingosine. Is not responsible for the breakdown of unsaturated ceramide. May play a role in heat stress response.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MLFSWPYPEAPIEGYWGKPTSLIDWCEENYVVSPYIAEWSNTITNSIFLMTAFYSTYSAWRNKLETRYILIGMGFSLVGIGSWLFHMTLQYRYQLLDELPMLYATIIPSWSIFAETQEILIKDEKKRKESSFRIQMVISFIMCGIVTILTWIYVVVQKPAIFQVLYGILTLLVVVLSGWLTYYHVHDSFAKKNLFITMVMGMIPFVIGFICWQLDIHLCSFWIYIRRTYLALPLGVLLELHAWWHLLTGTGVYIFVVYLQYLRILTHGNPNDFLFIWRWGFFPELVRKGLPIGTSYSLEYLGPIVNTQVDDETKKNN
The following text describes a protein:
Function:
Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MATALPPRLQPVRGNETLREHYQYVGKLAGRLKEASEGSTLTTVLFLVICSFIVLENLMVLIAIWKNNKFHNRMYFFIGNLALCDLLAGIAYKVNILMSGKKTFSLSPTVWFLREGSMFVALGASTCSLLAIAIERHLTMIKMRPYDANKRHRVFLLIGMCWLIAFTLGALPILGWNCLHNLPDCSTILPLYSKKYIAFCISIFTAILVTIVILYARIYFLVKSSSRKVANHNNSERSMALLRTVVIVVSVFIACWSPLFILFLIDVACRVQACPILFKAQWFIVLAVLNSAMNPVIYTLASKEMRRAFFRLVCNCLVRGRGARASPIQPALDPSRSKSSSSNNSSHSPKVKEDLPHTAPSSCIMDKNAALQNGIFCN
The following text describes a protein:
Function:
Acyltransferase which is required to remodel newly synthesized phospholipid cardiolipin, a key component of the mitochondrial inner membrane. Required for the initiation of mitophagy. Required to ensure progression of spermatocytes through meiosis.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Mitochondrion outer membrane; Peripheral membrane protein; Intermembrane side.
Sequence:
MNHLTVYNKEVLYELIENRGPATPLITVSNHQSCMDDPHLWGILKLRHIWNLKLMRWTPAAADICFTKELHSHFFSLGKCVPVCRGDGVYQKGMDFILEKLNHGDWVHIFPEGKVNMSSEFLRFKWGIGRLIAECHLNPIILPLWHVGMNDVLPNSPPYFPRFGQKITVLIGKPFSTLPVLERLRAENKSAECR
The following text describes a protein:
Function:
RNA-binding component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Sequence:
SLHKTFRIKRFLAKKQKQNRPIPQWIRMKTGNKIRYNSKRRHWRRTKLGL
The following text describes a protein:
Function:
Forms a fork protection complex (FPC) with CSM3 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSDYESGSDIDNYYEADEFDDFIEYSDNEVEQEKSKPTPGQIEVEEIEEPEEDRIRTLTTTLKPNETQAQKLLKAHISVLVSALGGPDHTSDIQPPPYKLGHDALACLKDIKRWIRAVDEKKNNYEVALACAESGLVTNDLIVIMCQWEDKMQKKEIIKNKTTTEKTMLACLELLVLLTWPVEFGKDLSESQKLLYSEIKKVHVSYKKQILMFNNGQLLKAAIRLVLPTIAKSRIDREPRDNQILKLVLYLIRNLLAIEPANLSISNKSRKGASVTASDLPLGVTQDDISINNVLSVFKKNKVLMLLLTISGSLGTEFDRDMFGEICLESIYLIIKGLSASEVLVKKNLGSTPVAAPSQNTVPDAINASQPLQPVTTTVGMQLQDLLATESKKKKIQTQNIASRHGRFGSLLSIRSADSNSFVVSGQEALINTDSSLAKLDKSKKWKDRTYFKYDSDEYVNTSTPVYLNLTGQDILYNFVEQFLSGGCFNNLIECMGSRLTSQTDLNMVDELTLASYFFTISWFLSYQRERIGLDSENKELNYGSVGAALSEVNFILIIGYFRDSFSVKKWNSLHVAMICFKELLQISNSVFGKEITNQTGEGDEISQHEIDRELAEGIIRKLFSFNDFLSIIVQIPQTAAKHSPDYLRVSVSVVHILLKAFETFANEDVHLYIQSKRKQSKRNRKRVNNLDKSTEDRLRDVIYASDEELDQSSAKEITQERKLDFKKTEARFFHQAIVSTYINYLSRYEDLSNQEIKTCLSYFHRLFVVRKDFTGLYRLDFMQLLQKLRNYLQRGSSLRLQVEEFIYYFMKKFKTAFERFPMPIEVLFPRFEDNECKVYLATGEVYEKEETTSTSRSPRLAKDLEFVRDFGLDDQIKILVSQLHVQEKQSLLKWLIQELERIINDRILNSDSIAELNASNQQRRLFINNGYLRFLLRIIGFDLPYTMEEVPELATTVDMEHLTKVTELIKKWDSSQPVIFEDDKVPSYFVRTREAGYDEDQYNENDQEYDFNDDSIAFETEANPNSNRNHVSELDHLEELERQLSSNGSRVNSKERNGTKGKARKKSKEKKRPEPKKVRGLKRRRIPKDLLDDDDSQHVVKSAEFVHDSDDESDDEKDKAFFEREEKMRNLLNDMGGIATSEQLKEIQKVWKNLETGGNNKVASTVAKAVKEVGLFVEESDNDDEVEEESRNSAPVNEEADRTIFESGEVDTQQDLSDNTSNTSDMESETETTKRSFVEDPEEISHVQPKRKRLVISDDEEE
The following text describes a protein:
Function:
Hydrolyzes glycosphingolipids; exhibits broad substrate specificity including monosialodihexosylganglioside (GM3), monosialotetrahexosylganglioside (GM1), fucosyl-GM1, lactosylceramide, globotriosylceramide, globotetraosylceramide, ganglioside GD1a, and ganglioside GD1b. No activity towards glucosylceramide and galactosylceramide.
Subcellular Localization:
Secreted. Membrane; Lipid-anchor.
Sequence:
MRKTVVAFAAAIAACSAVLSSTTTSAAPPATPITTLQADGTHLVDGYGRTVLLHGVNNVDKDAPYLPAGETLTPQDIDILVRHGFNTVRLGTSFDALMPQRGQIDEAYLDRLTGVVDALTARGMHVLLDNHQDGLSKAWGGNGFPEWAIESRPREWEPNPGFPLYYLMPSLNAGWDEVWGNTHGALDHLGTALGALAERVEGKPGVMGIELLNEPWPGSRFLSCFPNGCPDFDRTYQAAMQKLTDAVRAQNPTIPVYWEPNVTWNQMMPSNLFAPPVTPALTTADVVFAPHDYCIPSQLAIYLGLPQALRGLCVPQQDLTWSNIDAITERANVPTVITEFGDGDPTVLKNTLARADERFIGWQYWHFGAGNATDPFLGEVGRQLVRTYPQATAGEPGRMIFDADNGDFAYRFTPRAATRPTEIFVSDLHYPDGYAVQVDGGQVTSAPGARIVTVVADGSGPVTVKINRPGSAGAEVPDGPIETSSSGSSGSS
The following text describes a protein:
Function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
SIQDIEVFIGLEKKISSQLHQYLIKKEENLQKMEAILASVRYQQEHQIVKYEDQPRYPIAAYTLLKRFIHDWSSITKLMTHQLGQDFIRNLRRRETILPTVVDWDYTIKSILRLQTTYNLTAKDLADGKIQGTKDLGIQLNWFDCTMIANAANEERGFGNAYDWAKLALKLSENATDMTNDVRKEIIRSLSTNAFQIGRTKEAIGYIQELLKLEEATNVLKNGPNHFQDYVKRLGRADSTRRLAENTEFGNLCRGNVKEVNYILCSILLANKTLKCYYSNQSPLLYLAPIPVEEISLDPFIVIYYDIINDHQIETIKKISPSKSNKSPNHAMLCSGIKSEATQVSIFCCSTWLEDAYDPVVEKISRLTQELTHLDVNYAEDLQVANYGIGGHYVPHYDSTIIAPEDPLQRLATMMFYLSNVEIGGATIFPRLGVAVRPQKGSALFWINLKRNGLTNRQTLHAACPVVIGSKWIANKWIITSGQEFRYPCSLHSDE
The following text describes a protein:
Function:
Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism.
Domain:
Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Sequence:
MTRQLEKPNAPLLCGSITDSFAYLTIKDRMPVILTKILDQFARMQYKGLDGKTVHFSPDQLAQLKEITFDISELKYNMVRDRPLTPISSHSPSDWTESAVASLTADSNVWNAAMEELGDALACTWFQAPWLFVECYMYRALRQIITARNAWTDFDVFAQDKQTSLIGSIQSILQLSTTLGTKTNGIDSDLMRELIQTDLSLLVHAKHDDLHKLQVSGKNQLAAVCNNIIVNDIDRVIGKIQSVHTGDVVFVLDNAGFELFADLCMADHLTLSTDCRIVFQVKQYGWFVSDTTISDFHQTLDVCQTQAEIHGCAILMEAVSRWRLWLKNGRWILEQDPFWTTPFPFWRMPDKACVLLQTLSDAKFIFFKGDLNYRKMVHDASWPTTTTLEEAIGPLAKTQIAPFVLLRTCKSDTIVGLVEGQAEKLTEIDANWMVNGKFGVIQYHE
The following text describes a protein:
Function:
Required for ciliogenesis.
Subcellular Localization:
Cell projection, cilium. Vacuole membrane; Multi-pass membrane protein.
Sequence:
MKLTLRRYSWVLLFQFALLGVDLFCNAFGPSLARNRLQTAIILFVTQDALIIAEYLLFTLALHSTCVYQVGASHIILRNCKLFMASITIYFLLSASQHFWIIYQYRQPPEEDGHHWPLGLIALSVAQRIMSVFYYYSSKSTALTMADPRFKEEHLDWIADQLGDK
The following text describes a protein:
Function:
Mediates the transbilayer movement of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (lipid III) from the inner to the outer leaflet of the cytoplasmic membrane during the assembly of enterobacterial common antigen (ECA).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MSLAKASLWTAVSTLVKIGAGLLVVKLLAVSFGPAGVGQAGNFRQMITVLGVLAGAGIFNGVTKLVAQHHDNPAQLRTVVGTSSAMVLGFSTLLALVFLLAAAPISQGLFGHTDYQGLVRLVALVQMGIAWANLLLALMKGFRDASGNALSLIVGSFLGVAAWYLCYRVGGYEGALLGLALVPALVVVPAGIILIKRGTVPLRYLKPSWDNGLAGQLSKFTLMALITSVTMPVAYVMMRNQLAAHYSWSDVGIWQGVSSISDAYLQFITASFSVYLLPTLSRLTEKQDITREVVKALKFVLPAVAAASFTVWLLRDFAIWLLFSAKFTAMRDLFAWQLVGDVLKVGAYVFGYLVIAKASLRFYILAEISQFILLTAFAHWLIPAHGALGAAQAYMATYIVYFSLCCGVFLLWRRRA
The following text describes a protein:
Function:
Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of glycosphingolipids forming gangliosides (important molecules involved in the regulation of multiple cellular processes, including cell proliferation and differentiation, apoptosis, embryogenesis, development, and oncogenesis). Mainly involved in the biosynthesis of ganglioside GM3 but can also use different glycolipids as substrate acceptors such as D-galactosylceramide (GalCer), asialo-GM2 (GA2) and asialo-GM1 (GA1), although less preferentially than beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer (LacCer).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MVTLNHLSVEDPDDGSPLLPVAAETPTLTPVSHRQRVIPKMESRDFFLSRKANLASSLLVLMGCYLVILIPAYFPMDKMTADSDDHQYPKDLVLLNHSASLLSHPCQPHWCLNHLKPLSFSKRLLDIPVFVQQGRPAEWALGPPLGLHGSEEHLALTLASMPEPGLPPSLKTKDSCRRCVVVGNGGVLQGSHLGPHIDQYDVIIRMNNAPVVGFERDVGSRTTIRLMYPEGAPHSANEYRKTSMIALVVFKSLDLDWLTSVITKKPLSFWSKMWFWREVVDDIPLSPESFKILHPEIIHKTGQVLQKYTLKQGNMNPTLGASALVMAMQLCDQVSLAGFGYNMQHPEARLHYYEAIRMDAMKAQVVHDVSAEKLFLRDLVAAGAVTDLTGAL
The following text describes a protein:
Function:
May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Domain:
The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes.
Sequence:
MSKSTKLCGKTSCPRSNIFCNLLDKIVKRPSLQFLGQWGYHCYEPRIYRSLAKILRYVDLDGFDALLTDYIAFVEKSGYRFEVSFNLDFTEICVNTILYWVFARKGNPDFVELLLKKTKDYVQDRSCNLALIWRTFTPVYCPSPLSGITPLFYVAQTRQSNIFKILLQYGILEREKNPINIVLTIVLYPSRVRVMVDRELADIHEDAKTCLVLCSRVLSVISVKEIKTQLSLGRHPIISNWFDYIPSTRYKDPCELLHLCRLTIRNQLLTNNMLPDGIFSLLIPARLQNYLNLEI
The following text describes a protein:
Function:
Cargo protein of a type 1 encapsulin nanocompartment. Has both general peroxidase activity and dye-decolorizing activity. Can catalyze the oxidation of both protoporphyrinogen IX and coproporphyrinogen III to their corresponding porphyrins. Also efficiently decolorizes the dyes alizarin red and Cibacron blue F3GA (By similarity). This cargo-loaded encapsulin nanocompartment is probably involved in protection against oxidative damage (By similarity).
Subcellular Localization:
Encapsulin nanocompartment.
Domain:
The C-terminus (at least 10 residues, not detailed in paper) targets the protein to the nanocompartment.
Sequence:
MTEAFPNGKTPQHVLGPPAPAAVFLVLTVRSGAEAEAKDFLGDIAGVVRSVGFRAREDHLSCVTGIGAELWDRMFDAPRPAGLHPFIEQRGDVHTAPSTPGDLLFHIRARRMDLCFELARQLVGELGDAVSVVDEVHGFRYFDERDIMGFVDGTENPEDQEAVDSVFTPTGGDDPASSTYVIVQKYTHDMAAWEALSVEDQEAAFGRHKLSDMEFPDEDKAPNSHLILNTIEDEDGTEHKIVRDNMVFGSVESGEFGTYFIGYAADVSVTEQMLENMFIGNPRGTYDRILDFSTAQTGGLFFVPSQDFLDDPDGELAAAEPSDAQNDDPASASARIEETDPPNPASADDPAPADDSLGIGSLRRRDQ
The following text describes a protein:
Function:
Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease.
Subcellular Localization:
Secreted.
Sequence:
MQRLGATLLCLLLAAAVPTAPAPAPTATSAPVKPGPALSYPQEEATLNEMFREVEELMEDTQHKLRSAVKEMEAEEAAAKASSEVNLANLPPSYHNETNTDTKVGNNTIHVHREIHKITNDQTGQMVFSETVITSVGDEEGRRSHECIIDEDCGPSKYCQFASFQYTCQPCRGQRMLCTRDSECCGDQLCVWGHCTKMATRGSNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPASRLLDLITWELEPDGALDRCPCASGLLCQPHSHSLVYVCKPTFVGSRDQDGEILLPREAPDEYEVGSFMEEVRQELEDLERSLTEEMALGEPAAAAATLLGGEEI
The following text describes a protein:
Function:
Together with zig-8, required postembryonically to maintain the position of ASI and ASH head neuron cell bodies and ventral nerve cord axons of PVQ, PVP and HSN neurons by preventing their displacement that could occur during body growth and movement. May act by reducing L1CAM-like protein sax-7 (long isoform) adhesion.
Subcellular Localization:
Secreted.
Sequence:
MPSPLNHHLSCFVLSVILLGSHVSTSKIPIAPQSVCEGLIEPSVLSIDKPLENIKANRGDSLVLRCAFYASPQPTIVWYHRGKRVDSHPAAHFETLLSATNLGQSVVESALRIDCLDERTAGEYFCEATSPCTQPVVTSSTVTINKAPKSITGTCKSIRQPLESPPIVSDFTLSRIELPGGVAQLACRVRGVPTPKTKWFKIEEDESLSTIDGQPNYMHLSNGDLLIVGDEETISESFRCVASNPLGSVHQDASVIYMMA
The following text describes a protein:
Function:
Bifunctional glycosyltransferase that can produce both C- and O-glycosidated flavonoids. Converts 2-hydroxynaringenin to isovitexin. Converts eriodictyol to orientin and isoorientin. Converts naringenin and eriodictyol to naringenin 7-O-glucoside and eriodictyol 7-O-glucoside, respectively.
Sequence:
MAANGGDHTSARPHVVLLPSAGMGHLVPFARLAVALSEGHGCNVSVAAVQPTVSSAESRLLDALFVAAAPAVRRLDFRLAPFDESEFPGADPFFLRFEATRRSAPLLGPLLDAAEASALVTDIVLASVALPVARERGVPCYVLFTSSAAMLSLCAYFPAYLDAHAAAGSVGVGVGNVDIPGVFRIPKSSVPQALHDPDHLFTQQFVANGRCLVACDGILVNTFDAFEPDAVTALRQGSITVSGGFPPVFTVGPMLPVRFQAEETADYMRWLSAQPPRSVVYVSFGSRKAIPRDQLRELAAGLEASGKRFLWVVKSTIVDRDDTADLGGLLGDGFLERVQGRAFVTMGWVEQEEILQHGSVGLFISHCGWNSLTEAAAFGVPVLAWPRFGDQRVNAALVARSGLGAWEEGWTWDGEEGLTTRKEVAKKIKGMMGYDAVAEKAAKVGDAAAAAIAKCGTSYQSLEEFVQRCRDAERK
The following text describes a protein:
Function:
Flippase that catalyzes the transport of undecaprenyl phosphate (UndP) across the cytoplasmic membrane, from the external side to the cytoplasmic side. Is involved in UndP recycling during peptidoglycan synthesis.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGSLISEILTWLTNMGYAGIAIGLMIEIIPSEIVLAYGGYMVSEGTIGFIGAIIAGVIGGTIAQIFIYWIGRYGGRPFLDKYGKYLLIKKHHIDMSENWFQKYGAGVVFSARFIPVVRHAISIPAGIARMPFLKFVVLTVLAIIPWSILFVYLGIQLGSQWDDVENIAGTYTTPIMILAVVVIALYFVIKKRTAIFKR
The following text describes a protein:
Function:
Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for CATSPER1 stability before intraflagellar transport and/or incorporation of the CatSper complex channel into the flagellar membrane.
Subcellular Localization:
Cell projection, cilium, flagellum membrane; Single-pass type I membrane protein. Note=Specifically located in the principal piece of sperm tail.
Sequence:
MLVLMLVVATTFRLCPLVKARPLCRIRTLRTGKVFPVEEKIQGDRLYFSSGKTHLIKHPCKKNLALYLGRQIFLTKDTFESSLIPFSIPTSMQVGTPEVTSAHFAGSVLLLVVNQKVYVYDYEANFWTASTGIQHPVSHVSGDNCCYSGNSFCMDISNSVFAYLRGDQVSQANIYFSNSRGYRFQKYTQERRAELVGTFGGIFSFHSLSQVGLLLVDEQMAMFSYSDHPLNRSFGLPFDYDRALDILIAPGQKGILIFWSEKNLLVSRNSGQLVESVQVREGQRILYNSIVKANVTIHSVAANENELAVLTEENNLYYGSLGIQSSSLIKFADQNIWSQEAVLMFTDVGMLEILTPLRDVLFPAFDFQKCRLNIQALLMDPQLQAGVCKVELLQGEFENKMYTIDMNSQLELTALMIPRPGMLPVPLVSVSNPHSLGLQAVICEDGYTYDGNTKHRLNISLKQQHHWGRADPNFTSSIKRPTISTITLDIANKEISCVDLKPLTALISVGCDLEKKIVIQNELSACYHGVLDPVALQDNYSYIIEREAYDPNFQGQQAKKDLEVHYPYEKLGCPLLAYYDIPWKPVVELWREGKFQEVVEAEYVLLEMNGLFTYTYSLTASTAGCSAQPQNWTTITKMAGDTAPFSWDRENYISCHDPNYHEPLRWPDVPYQILGGQTENKVVFDQRNGIYIFFISIVDPSYSYCRLETTFSVYVYGAFPLSIFPPEITIVLLTAATLLSIWLAYMIPQLLHTEQGLEGNGFWVRLYQRCRKSCACLWGRC
The following text describes a protein:
Function:
Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
Sequence:
MCGIFAYMNYRVPKTRKEIFETLIRGLQRLEYRGYDSAGVAIDGNNHEVKERHIHLVKKRGKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPNAVNSHPQRSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPVLYPTCNIENVKNICKTRMKRLDSSTCLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSATDDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLDEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Probably involved in the tetrapyrrole synthesis required for the chlorophyll biosynthesis.
Miscellaneous:
MISCELLANEOUS: During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA (By similarity).
Subcellular Localization:
Plastid, chloroplast membrane.
Domain:
The N-terminus (65-92) is required for heme inhibition, but not for activity.
Sequence:
MAVSSAFVGCPKLETLLNHHNLSPSSSSSSSVSQTPLGLNGVRVLPKNNRTRRGLIQKARCELSASSDSASNAASISALEQLKNSAADRYTKERSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPVSEICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTETNIASGAVSVSSAAVELALMKLPQSSNVSARMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGIEIIYRPLDEMLACASEADVVFTSTASETPLFLKEHVENLPQASPEVGGLRHFVDISVPRNVGSCVGEVETARVYNVDDLKEVVAANKEDRMRKAMEAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGDDINKKTTRAVDDLSRGIVNRFLHGPMQHLRCDGSDSRTLSETLENMHALNRMYGLEKDILEEKLKAMAEQQQK
The following text describes a protein:
Function:
Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MTSTPQESSNLKRQLENSEDSSSPNKKSKTETTTENQSSWESDFNSLPVELLQTETNGTSPAPAPATPIDTTNVSNSKERDQDTSKLNDAIAAAGVDIQQEEEILLQQQLNRKSAEGMASNLKSVIRSSKSPPFLHNYHLAAFIDKVAKQNGIQQNFLMDGEMLELISAACETWLSNLATKTIILSRHRRRGIPVINKKSGSSSVPRSEISKELRSLALKQKEMEEKRVNKRVMLGLEKSTKDASKNDENGESKAGAEETLHRAANATAAMMTMNPGRKKYSWMTSSATAGGGSDFGKSSGGSSKDSGKHQSPIISVRGDNGLRFREIRSGNSIIMKDLLGAIEDEKMGTRNAVIKGYAKLKD