entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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O55134
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PCD12_MOUSE
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Protocadherin-12 (Vascular cadherin-2) (Vascular endothelial cadherin-2) (VE-cad-2) (VE-cadherin-2) [Cleaved into: Protocadherin-12, secreted form]
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MMLLLPFLLGLLGPGSYLFISGDCQEVATVMVKFQVTEEVPSGTVIGKLSQELRVEERRGKAGDAFQILQLPQALPVQMNSEDGLLSTSSRLDREKLCRQEDPCLVSFDVLATGASALIHVEIQVLDINDHQPQFPKDEQELEISESASLHTRIPLDRALDQDTGPNSLYSYSLSPSEHFALDVIVGPDETKHAELVVVKELDRELHSYFDLVLTAYDNGNPPKSGISVVKVNVLDSNDNSPVFAESSLALEIPEDTVPGTLLINLTATDPDQGPNGEVEFFFGKHVSPEVMNTFGIDAKTGQIILRQALDYEKNPAYEVDVQARDLGPNSIPGHCKVLIKVLDVNDNAPSILITWASQTSLVSEDLPRDSFIALVSANDLDSGNNGLVHCWLNQELGHFRLKRTNGNTYMLLTNATLDREQWPIYTLTVFAQDQGPQPLSAEKELQIQVSDVNDNAPVFEKSRYEVSTWENNPPSLHLITLKAHDADLGSNGKVSYRIKDSPVSHLVIIDFETGEVTAQRSLDYEQMAGFEFQVIAEDRGQPQLASSISVWVSLLDANDNAPEVIQPVLSEGKATLSVLVNASTGHLLLPIENPSGMDPAGTGIPPKATHSPWSFLLLTIVARDADSGANGELFYSIQSGNDAHLFFLSPSLGQLFINVTNASSLIGSQWDLGIVVEDQGSPSLQTQVSLKVVFVTSVDHLRDSAHEPGVLSTPALALICLAVLLAIFGLLLALFVSICRTERKDNRAYNCREAESSYRHQPKRPQKHIQKADIHLVPVLRAHENETDEVRPSHKDTSKETLMEAGWDSCLQAPFHLTPTLYRTLRNQGNQGELAESQEVLQDTFNFLFNHPRQRNASRENLNLPESPPAVRQPLLRPLKVPGSPIARATGDQDKEEAPQSPPASSATLRRQRNFNGKVSPRGESGPHQILRSLVRLSVAAFAERNPVEEPAGDSPPVQQISQLLSLLHQGQFQPKPNHRGNKYLAKPGGSSRGTIPDTEGLVGLKPSGQAEPDLEEGPPSPEEDLSVKRLLEEELSSLLDPNTGLALDKLSPPDPAWMARLSLPLTTNYRDNLSSPDATTSEEPRTFQTFGKTVGPGPELSPTGTRLASTFVSEMSSLLEMLLGQHTVPVEAASAALRRLSVCGRTLSLDLATSGASASEAQGRKKAAESRLGCGRNL
|
Cellular adhesion molecule that may play an important role in cell-cell interactions at interendothelial junctions. Acts as a regulator of cell migration, probably via increasing cell-cell adhesion (By similarity). Promotes homotypic calcium-dependent aggregation and adhesion and clusters at intercellular junctions. Unable to bind to catenins, weakly associates with the cytoskeleton.
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O55135
|
IF6_MOUSE
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Eukaryotic translation initiation factor 6 (eIF-6) (B4 integrin interactor) (CAB) (p27(BBP))
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MAVRASFENNCEVGCFAKLTNAYCLVAIGGSENFYSVFEGELSDAIPVVHASIAGCRIIGRMCVGNRHGLLVPNNTTDQELQHIRNSLPDSVQIRRVEERLSALGNVTTCNDYVALVHPDLDRETEEILADVLKVEVFRQTVADQVLVGSYCVFSNQGGLVHPKTSIEDQDELSSLLQVPLVAGTVNRGSEVIAAGMVVNDWCAFCGLDTTSTELSVVESVFKLNEAKPSTIATSMRDSLIDSLT
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Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Behaves as a stimulatory translation initiation factor downstream insulin/growth factors. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by a RACK1 (RACK1)-dependent protein kinase C activity. In tissues responsive to insulin, controls fatty acid synthesis and glycolysis by exerting translational control of adipogenic transcription factors such as CEBPB, CEBPD and ATF4 that have G/C rich or uORF in their 5'UTR. Required for ROS-dependent megakaryocyte maturation and platelets formation, controls the expression of mitochondrial respiratory chain genes involved in reactive oxygen species (ROS) synthesis. Involved in miRNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC (By similarity). Modulates cell cycle progression and global translation of pre-B cells, its activation seems to be rate-limiting in tumorigenesis and tumor growth. {ECO:0000255|HAMAP-Rule:MF_03132, ECO:0000269|PubMed:18784653, ECO:0000269|PubMed:21665150, ECO:0000269|PubMed:26383020, ECO:0000269|PubMed:26391622}.
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O55137
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ACOT1_MOUSE
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Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.-) (CTE-I) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2)
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MEATLNLEPSGRSCWDEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFWRLVKRDVQTPFVVELEVLDGHEPDGGQRLAHAVHERHFLAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKNMETMHMEYFEEAVNYLRSHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTISYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVDKKSFIPVERSDTTFLFLVGQDDHNWKSEFYADEISKRLQAHGKEKPQIICYPAAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHAMAQLDAWQQLQTFFHKQLGSECLHVSPKI
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Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20).
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O55142
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RL35A_MOUSE
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Large ribosomal subunit protein eL33 (60S ribosomal protein L35a)
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MSGRLWCKAIFAGYKRGLRNQREHTALLKIEGVYARDETEFYLGKRCAYVYKAKNNTVTPGGKPNKTRVIWGKVTRAHGNSGMVRAKFRSNLPAKAIGHRIRVMLYPSRI
|
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Required for the proliferation and viability of hematopoietic cells (By similarity).
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O55143
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AT2A2_MOUSE
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Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2+)-ATPase 2) (EC 7.2.2.10) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase)
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MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDKVEGDTCSLNEFSITGSTYAPIGEVQKDDKPVKCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTPGVKQKIMSVIREWGSGSDTLRCLALATHDNPLKREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELSPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKSEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFDGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNLTQWLMVLKISLPVILMDETLKFVARNYLEQPGKECVQPATKSSCSLSACTDGISWPFVLLIMPLVVWVYSTDTNFSDMFWS
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This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation. Also modulates ER contacts with lipid droplets, mitochondria and endosomes (By similarity). In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis. [Isoform 2]: Involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca(2+) signaling cascades that promote osteoclast differentiation and activation.
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O55145
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X3CL1_RAT
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Fractalkine (C-X3-C motif chemokine 1) (CX3C membrane-anchored chemokine) (Neurotactin) (Small-inducible cytokine D1) [Cleaved into: Processed fractalkine]
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MAPSQLAWLLRLAAFFHLCTLLAGQHLGMTKCNITCHKMTSPIPVTLLIHYQLNQESCGKRAIILETRQHRHFCADPKEKWVQDAMKHLDHQTAALTRNGGKFEKRVDNVTPRITSATRGLSPTALAKPESATVEDLTLEPTAISQEARRPMGTSQEPPAAVTGSSPSTSKAQDAGLAAKPQSTGISEVAAVSTTIWPSSAVYQSGSSLWAEEKATESPPTIALSTQASTTSSPKQNVGSEGQPPWVQEQDSTPEKSPGPEETNPVHTDIFQDRGPGSTVHPSVAPTSSEKTPSPELVASGSQAPKVEEPIHATADPQKLSVFITPVPDSQAATRRQAVGLLAFLGLLFCLGVAMFAYQSLQGCPRKMAGEMVEGLRYVPRSCGSNSYVLVPV
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Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1. The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis. Regulates leukocyte adhesion and migration processes at the endothelium. Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner. In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins. In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1. [Processed fractalkine]: The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils.
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O55156
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CLIP2_RAT
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CAP-Gly domain-containing linker protein 2 (Cytoplasmic linker protein 115) (CLIP-115) (Cytoplasmic linker protein 2)
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MQKPSGLKPPGRGGKHSSPVGRPSIGSASSSVVASASGSKEGSPLHKQASGPSSAGATTTVSEKPGPKAAEVGDDFLGDFVVGERVWVNGVKPGVVQYLGETQFAPGQWAGVVLDDPVGKNDGAVGGLRYFECPALQGIFTRPSKLTRQPAAEGSGSDGHSVESLTAQNLSLHSGTATPPLTGRVIPLRESVLNSSVKTGNESGSNLSDSGSVKRGDKDLHLGDRVLVGGTKTGVVRYVGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCPPKFGLFAPIHKVIRIGFPSTSPAKAKKTKRMAMGVSALTHSPSSSSISSVSSVASSVGGRPSRSGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHICEVEKEIALLKAQHEQYVAEAEEKLQRARLLVENVRKEKVDLSNQLEEERRKVEDLQFRVEEESITKGDLETQTQLEHARIGELEQSLLLEKAQAERLLRELADNRLTTVAEKSRVLQLEEELSLRRGEIEELQHCLLQSGPPPADHPEAAETLRLRERLLSASKEHQRDSTLLQDKYEHMLKTYQTEVDKLRAANEKYAQEVADLKAKVQQATTENMGLMDNWKSKLDSLASDHQKSLEDLKATLNSGPGAQQKEIGELKALVEGIKMEHQLELGNLQAKHDLETAMHGKEKEGLRQKLQEAQEELAGLQQHWRAQLEEQAAAPAELQEAQDQCRDAQLRVQELEGLDVEYRGQAQAIEFLKEQISLAEKKMLDYEMLQRAEAQSRQEAERLREKLLVAENRLQAVESLCSAQHSHVIESNDLSEEKIRMKETVEGLQDKLNKRDKEVAALTSQMDMLRAQVSALENKCKSGEKKIDSLLKEKRRLEAELEAVSRKTHDASGQLVHISQELLRKERSLNELRVLLLEANRHSPGPERDLSREVHKAEWRIKEQKLKDDIRGLREKLTGLDKEKSLSEQKRYSLIDPASAPELLRLQHQLVSTEGCLRDALDQAQQVERLVEALRGCSDRTQTISNSGSANGIHQPDKAHKQEDKH
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Seems to link microtubules to dendritic lamellar body (DLB), a membranous organelle predominantly present in bulbous dendritic appendages of neurons linked by dendrodendritic gap junctions. May operate in the control of brain-specific organelle translocations.
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O55159
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EPCAM_RAT
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Epithelial cell adhesion molecule (Ep-CAM) (Epithelial glycoprotein 314) (EGP314) (Protein D5.7A) (Tumor-associated calcium signal transducer 1) (CD antigen CD326)
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MAPPKALAFGLLLAVVTATLAAAQKDCVCNNYKLTSRCYENENGECQCTSYGTQNTVICSKLASKCLVMKAEMTHSKSGRRMKPEGAIQNNDGLYDPECDEQGLFKAKQCNGTATCWCVNTAGVRRTDKDTEITCSERVRTYWIIIELKHKERAQPYNFESLHTALQDTFASRYMLNPKFIKSIMYENNVITIDLMQNSSQKTQDDVDIADVAYYFEKDVKGESLFHSSKSMDLRVNGELLDLDPGQTLIYYVDEKAPEFSMQGLTAGIIAVIVVVVLAVIAGIVVLVISTRKRSAKYEKAEIKEMGEIHRELNA
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May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E (By similarity).
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O55162
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LYPD3_RAT
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Ly6/PLAUR domain-containing protein 3 (GPI-anchored metastasis-associated protein C4.4A)
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MDAARRGDTQPVMWTTRWLLLLPLLLCEGAQALECYSCVQKADDGCSPHKMKTVKCGPGVDVCTEAVGAVESIHGQFSVAVRGCGSGIPGKNDRGLDLHGLLAFIQLQQCTEDRCNAKLNLTLRGLNPAGNESAYEHNGAECYSCMGLSREKCQGAMPPVVNCYNASGRVYKGCFDGNVTLTAANVTVSLPVRGCVQDEACTRDGVTGPGFTLSGSCCQGPRCNSDLRNKTYFSPRIPPLVLLPPPTTPAPSTRTQNSSSTTSTTAPTTATTTIKPTTVQASHTSSTHETEHEVIQEEGSHLSGGATGHQDRSNMGKFPEKGGAQIPSKGGSDALGSWLSAILLTVVAGAML
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Supports cell migration. May be involved in tumor progression.
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O55164
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MPDZ_RAT
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Multiple PDZ domain protein (Multi-PDZ domain protein 1)
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MLETIDKNRALQAAERLQSKLKERGDVANEDKLSLLKSVLQSPLFSQILSLQTSLQQLKDQVNVATLATANADHAHTPQFSSAIISNLQSESLLLSPSNGNLEAISGPGAPPAMDGKPACEELDQLIKSMAQGRHVEIFELLKPPCGGLGFSVVGLRSENRGELGIFVQEIQEGSVAHRDGRLKETDQILAINGQVLDQTITHQQAISILQKAKDTIQLVIARGSLPHISSPRISRSPSAASTVSAHSNPTHWQHVETIELVNDGSGLGFGIIGGKATGVIVKTILPGGVADQHGRLCSGDHILKIGDTDLAGMSSEQVAQVLRQCGNRVKLMIARGAVEETPAPSSLGITLSSSTSTSEMRVDASTQKNEESETFDVELTKNVQGLGITIAGYIGDKKLEPSGIFVKSITKSSAVELDGRIQIGDQIVAVDGTNLQGFTNQQAVEVLRHTGQTVRLTLMRKGASQEAEITSREDTAKDVDLPAENYEKDEESLSLKRSTSILPIEEEGYPLLSTELEETEDVQQEAALLTKWQRIMGINYEIVVAHVSKFSENSGLGISLEATVGHHFIRSVLPEGPVGHSGKLFSGDELLEVNGINLLGENHQDVVNILKELPIDVTMVCCRRTVPPTALSEVDSLDIHDLELTEKPHIDLGEFIGSSETEDPMLAMSDVDQNAEEIQTPLAMWEAGIQAIELEKGSRGLGFSILDYQDPIDPANTVIVIRSLVPGGIAEKDGRLFPGDRLMFVNDINLENSTLEEAVEALKGAPSGMVRIGVAKPLPLSPEEGYVSAKEDTFLCSPHTCKEMGLSDKALFRADLALIDTPDAESVAESRFESQFSPDNDSVYSTQASVLSLHDGACSDGMNYGPSLPSSPPKDVTNSSDLVLGLHLSLEELYTQNLLQRQHAGSPPTDMSPAATSGFTVSDYTPANAVEQKYECANTVAWTPSQLPSGLSTTELAPALPAVAPKYLTEQSSLVSDAESVTLQSMSQEAFERTVTIAKGSSSLGMTVSANKDGLGVIVRSIIHGGAISRDGRIAVGDCILSINEESTISLTNAQARAMLRRHSLIGPDIKITYVPAEHLEEFRVSFGQQAGGIMALDIFSSYTGRDIPELPEREEGEGEESELQNAAYSSWSQPRRVELWREPSKSLGISIVGGRGMGSRLSNGEVMRGIFIKHVLEDSPAGKNGTLKPGDRIVEVDGMDLRDASHEQAVEAIRKAGSPVVFMVQSIVNRPRKSPLPSLPHSLYPKCSFSSTNPFAESLQLTSDKAPSQSESESEKATLCSVPSSSPSVFSEMSSDYAQPSATTVAEDEDKEDEFGYSWKNIQERYGTLTGQLHMIELEKGHSGLGLSLAGNKDRTRMSVFIVGIDPTGAAGRDGRLQIADELLEINGQILYGRSHQNASSIIKCAPSKVKIIFIRNADAVNQMAVCPGSAADPLPSTSESPQNKEVEPSITTSASAVDLSSLTNVYHLELPKDQGGLGIAICEEDTLNGVTIKSLTERGGAAKDGRLKPGDRILAVDDELVAGCPIEKFISLLKTAKTTVKLTVGAENPGCQAVPSAAVTASGERKDSSQTPAVPAPDLEPIPSTSRSSTPAIFASDPATCPIIPGCETTIEISKGQTGLGLSIVGGSDTLLGAIIIHEVYEEGAACKDGRLWAGDQILEVNGIDLRKATHDEAINVLRQTPQRVRLTLYRDEAPYKEEDVCDTFTVELQKRPGKGLGLSIVGKRNDTGVFVSDIVKGGIADADGRLMQGDQILMVNGEDVRNATQEAVAALLKCSLGTVTLEVGRIKAAPFHSERRPSQSSQVSESSLSSFSLPRSGIHTSESSESSAKKNALASEIQGLRTVEIKKGPADALGLSIAGGVGSPLGDVPIFIAMMHPNGVAAQTQKLRVGDRIVTICGTSTDGMTHTQAVNLMKNASGSIEVQVVAGGDVSVVTGHQQELANPCLAFTGLTSSTIFPDDLGPPQSKTITLDRGPDGLGFSIVGGYGSPHGDLPIYVKTVFAKGAAAEDGRLKRGDQIIAVNGQSLEGVTHEEAVAILKRTKGTVTLMVLS
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Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses. Promotes clustering of HT2RC at the cell surface.
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O55165
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KIF3C_RAT
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Kinesin-like protein KIF3C
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MASKTKASEALKVVARCRPLSRKEEAAGHEQILTMDVKLGQVTLRNPRAAPGELPKTFTFDAVYDASSKQADLYDETVRPLIDSVLQGFNGTVFAYGQTGTGKTYTMQGTWVEPELRGVIPNAFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKEPGKRLELKENPETGVYIKDLSSFVTKNVKEIEHVMNLGNQARAVGSTHMNEVSSRSHAIFVITVECSERGSDGQDHIRVGKLNLVDLAGSERQNKAGPNTPGGPATQSTAGGGGGGGGTSGSGSSGERPKEASKINLSLSALGNVIAALAGNRSTHIPYRDSKLTRLLQDSLGGNAKTIMVATLGPASHSYDESLSTLRFANRAKNIKNKPRVNEDPKDTLLREFQEEIARLKAQLEKKGMLGKRPRRKSSRRKKAVSAPAGYPEGAVIEAWVAEEEDDNNNNHRPPQPTLEAALEKNMENYLQEQKERLEEEKAAIQDDRSLVSEEKQKLLEEKEKMLEDLKREQQATELLAAKYKAMESKLLIGGRNIMDHTNEQQKMLELKRQEIAEQKRREREMQQEMLLRDEETMELRGTYSSLQQEVEVKTKKLKKLYAKLQAVKAEIQDQHEEYIRVRQDLEEAQNEQTRELKLKYLIIENFIPPEEKNKIMNRLFLDCEEEQWKFQPLVPAGVNNSQMKKRPTSAVGYKRPISQYARVAMAMGSHPRYRAENIMFLELDVSPPAIFEMEFSHDQEQDPRVLHMERLMRLDSFLERPSTSKVRKSRSWCQSPQRPPPPSTVHASMASAPLHPATVVDHD
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Microtubule-based anterograde translocator for membranous organelles.
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O55166
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VPS52_RAT
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Vacuolar protein sorting-associated protein 52 homolog (SAC2 suppressor of actin mutations 2-like protein)
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MAAAATMAAAARELVLRAGASDMEEEEGPLGAGSGLQEPLQLGELDITSDEFILDEVDVHIQANLEDELVKEALKTGVDLRHYSKQVELELQQIEQKSIRDYIQESENIASLHNQITACDAVLERMEQMLGAFQSDLSSISCEIRTLQEQSGAMNIRLRNRQAVRGKLGELVDGLVVPSALVTAILEAPVTEPRFLEQLQELDAKAAAVREQEARGTAACADVRGVLDRLRVKAVTKIREFILQKIYSFRKPMTNYQIPQTALLKYRFFYQFLLGNERATAKEVRDEYVETLSKIYLSYYRSYVGRLMKVQYEEVAEKDDLMGVEDTAKKGFFSKPSLRSRNTIFTLGTRGAVISPAELEAPILVPHTAQRGEQRYPFEALFRSQHYALLDNSCREYLFICEFFVVSGPAAHDLFHAVMGRTLSMTLKHLESYLADCYDAIAVFLCIHIVLRFRNIAAKRDVPALDRYWEQVLALLWPRFELILEMNVQSVRSTDPQRLGGLDTRPHYITRRYAEFSSALVSINQTIPNERTLQLLGQLQVEVENFVLRVAAEFSSRKEQLVFLINNYDMMLGVLMERAADDSKEVESFQQLLNARTQEFIEELLSPPFGGLVAFVKEAEALIERGQAERLRGEEARVTQLIRGFGSSWKASVESLSQDVMRSFTNFRNGTSIIQGALTQLIQLYHRFHRVLSQPQLRALPARAELINIHHLMVELKKHKPNF
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Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD. Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane.
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O55170
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SOX10_RAT
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Transcription factor SOX-10
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MAEEQDLSEVELSPVGSEEPRCLSPSSAPSLGPDGGGGGSGLRASPGPGELGKVKKEQQDGEADDDKFPVCIREAVSQVLSGYDWTLVPMPVRVNGASKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESDKRPFIEEAERLRMQHKKDHPDYKYQPRRRKNGKAAQGEAECPGGETDQGGAAAIQAHYKSAHLDHRHPEEGSPMSDGNPEHPSGQSHGPPTPPTTPKTELQSGKADPKRDGRSLGEGGKPHIDFGNVDIGEISHEVMSNMETFDVTELDQYLPPNGHPGHVGSYSAAGYGLSSALAVASGHSAWISKPPGVALPTVSPPAVDAKAQVKTETTGPQGPPHYTDQPSTSQIAYTSLSLPHYGSAFPSISRPQFDYSDHQPSGPYYGHAGQASGLYSAFSYMGPSQRPLYTAISDPSPSGPQSHSPTHWEQPVYTTLSRP
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Transcription factor that plays a central role in developing and mature glia (By similarity). Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (By similarity). Once induced, MYRF cooperates with SOX10 to implement the myelination program (By similarity). Transcriptional activator of MITF, acting synergistically with PAX3 (By similarity). Transcriptional activator of MBP, via binding to the gene promoter.
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O55171
|
ACOT2_RAT
|
Acyl-coenzyme A thioesterase 2, mitochondrial (Acyl-CoA thioesterase 2) (EC 3.1.2.2) (ARTISt/p43) (Acyl coenzyme A thioester hydrolase) (MTE-I) (Very-long-chain acyl-CoA thioesterase)
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MVASSFAVLRASRLCQWGWKSWTQLSGPPPLSTGGRTTFARTNATLSLEPGSRSCWDEPLSITVRGLAPEQPVTLRAALRDEKGALFRAHARYRADAGGELDLARAPALGGSFTGLEPMGLIWAMEPERPLWRLVKRDVQKPYVVELEVLDGHEPDGGQRLAQAVHERHFMAPGVRRVPVRDGRVRATLFLPPEPGPFPEIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKTMETMRIEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTVCYKDETIPPVSLLRDKVKMTKDGLLDVVEALQSPLVDKKSFIPVERSDTTFLFLVGQDDHNWKSEFYAREASKRLQAHGKEKPQIICYPEAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLSGKS
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Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (By similarity). Displays higher activity toward long chain acyl CoAs (C14-C20). The enzyme is involved in enhancing the hepatic fatty acid oxidation in mitochondria (By similarity).
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O55173
|
PDPK1_RAT
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3-phosphoinositide-dependent protein kinase 1 (EC 2.7.11.1) (Protein kinase B kinase) (PkB kinase)
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MARTTSQLYDAVPIQSSVVLCSCPSPSMVRSQTEPSSSPGIPSGVSRQGSTMDGTTAEARPSTNPLQQHPAQLPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPDSKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESITWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSAVDASLPQRSGSNIEQYIHDLDTNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQQYQSSPDAAVQ
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Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages (By similarity). {ECO:0000250, ECO:0000269|PubMed:11781095}.
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O55174
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ZNT4_RAT
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Probable proton-coupled zinc antiporter SLC30A4 (Dri 27 protein) (Solute carrier family 30 member 4) (Zinc transporter 4) (ZnT-4)
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MAGPGAWKRLKSLLRKDDAPLFLNDTSAFDFLDEVSDEGLSRFNKLRVVVADDDSEAPERPVNGAHPALQADDDSLLDQELPLTNSQLSLKMDPCDNCSKRRELLKQRKVKTRLTIAAVLYLLFMIGELVGGYMANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTRRFTFGFHRLEVLSAMISVMLVYVLMGFLLYEAMQRTIHMNYEINGDVMLITAAVGVAVNVIMGFLLNQSGHHHSHAHSHSLPSNSPSMVSSGHSHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYIFSLLVAFTTLRIIWDTVVIILEGVPSHLNVDYIKESLMKIEDVYSVEDLNIWSLTSGKATAIVHMQLIPGSSSKWEEVQSKAKHLLLNTFGMYKCTVQLQSYRQEATRTCANCQSSST
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Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment (By similarity). Controls zinc deposition in milk (By similarity).
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O55176
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PJA1_MOUSE
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E3 ubiquitin-protein ligase Praja-1 (Praja1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase Praja-1)
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MSHQERIASQRRTTAEVPMHRSTANQSKRSRSPFASTRRRWDDSESSGASLAVESEDYSRYPPREYRASGSRRGLAYGHIDTVVARDSEEEGAGPVDRLPVRGKAGKFKDDPEKGARSSRFTSVNHDAKEECGKVESPPAARCSARRAELSKQNGSSASQISSAEGRAAAKGNNSLERERQNLPARPSRAPVSICGGGENTPKSAEEPVVRPKVRNVATPNCMKPKVFFDTDDDDDVPHSTSRWRDAADAEEAHAEGLARRGRGEAASSSEPRYAEDQDARSEQAKADKVPRRRRTMADPDFWAYTDDYYRYYEEDSDSDKEWMAALRRKYRSREQPQSSSGESWELLPGKEELERQQAGAGSLASAGSNGSGYPEEVQDPSLQEEEQASLEEGEIPWLRYNENESSSEGDNESTHELIQPGMFMLDGNNNLEDDSSVSEDLEVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDALPEILVTEDHGAVGQEMCCPICCSEYVKGEVATELPCHHYFHKPCVSIWLQKSGTCPVCRCMFPPPL
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Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome. May be involved in protein sorting.
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O55183
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STC1_MOUSE
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Stanniocalcin-1 (STC-1)
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MLQNSAVILALVISAAAAHEAEQNDSVSPRKSRVAAQNSAEVVRCLNSALQVGCGAFACLENSTCDTDGMYDICKSFLYSAAKFDTQGKAFVKESLKCIANGITSKVFLAIRRCSTFQRMIAEVQEDCYSKLNVCSIAKRNPEAITEVIQLPNHFSNRYYNRLVRSLLECDEDTVSTIRDSLMEKIGPNMASLFHILQTDHCAQTHPRADFNRRRTNEPQKLKVLLRNLRGEGDSPSHIKRTSQESA
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Stimulates renal phosphate reabsorption, and could therefore prevent hypercalcemia.
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O55186
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CD59A_MOUSE
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CD59A glycoprotein (MAC-inhibitory protein) (MAC-IP) (Membrane attack complex inhibition factor) (MACIF) (Protectin) (CD antigen CD59)
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MRAQRGLILLLLLLAVFCSTAVSLTCYHCFQPVVSSCNMNSTCSPDQDSCLYAVAGMQVYQRCWKQSDCHGEIIMDQLEETKLKFRCCQFNLCNKSDGSLGKTPLLGTSVLVAILNLCFLSHL
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Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (By similarity).
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O55187
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CBX4_MOUSE
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E3 SUMO-protein ligase CBX4 (EC 2.3.2.-) (Chromobox protein homolog 4) (E3 SUMO-protein transferase CBX4) (Polycomb 2 homolog) (Pc2) (mPc2)
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MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSADNRAKLELGTQGKGQGHQYELNSKKHHQYQPHSKERSGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGTKSHPPDKWAHGAAAKGYLGAVKPLGGGAGAPGKGSEKGPPNGMTPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEAAEGEARSPSHKKRAAEERHPQGDRTFKKAAGASEEKKAEVPCKRREEEALVSGDAQPQDLGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARSSHPPAHHHHHHHHHHHHHTVGLNLSHARKRCLSETHGEREPCKKRLTARSISTPTCLGGSPVSEHPANVSPTAASLPQPEVILLDSDLDEPIDLRCVKMRSDAGEPPSTLQVKPEAPAVAAVVAPAPASEKPPAEAQEEPVEPLSEFKPFFGNIIITDVTANCLTVTFKEYVTV
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E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (By similarity). PcG PRC1 complex acts via chromatin remodeling and modification of histones it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (By similarity). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3). Plays a role in the lineage differentiation of the germ layers in embryonic development.
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O55188
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DMP1_MOUSE
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Dentin matrix acidic phosphoprotein 1 (DMP-1) (Dentin matrix protein 1) (AG1)
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MKTVILLVFLWGLSCALPVARYHNTESESSEERTGDLAGSPPPPTNSESSEESQASPEGQANSDHTDSSESGEELGYDRGQYRPAGGLSKSTGTGADKEDDEDDSGDDTFGDEDNDLGPEEGQWGGPSKLDSDEDSTDTTQSSEDSTSQENSAQDTPSDSKDHDSEDEADSRPEAGDSTQDSESEEQRVGGGSEGESSHGDGSEFDDEGMQSDDPESTRSDRGHARMSSAGIRSEESKGDHEPTSTQDSDDSQSVEFSSRKSFRRSHVSEEDYRGELTDSNSRETQSDSTEDTASKEESRSESQEDTAESQSQEDSPEGQDPSSESSEEAGEPSQESSSESQEGVTSESRGDNPDNTSQAGDQEDSESSEEDSLNTFSSSESQSTEEQADSESNESLSLSEESQESAQDGDSSSQEGLQSQSASTESRSQESQSEQDSRSEEDSDSQDSSRSKEESNSTGSASSSEEDIRPKNMEADSRKLIVDAYHNKPIGDQDDNDCQDGY
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May have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite (By similarity).
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O55192
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SC6A2_MOUSE
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Sodium-dependent noradrenaline transporter (Norepinephrine transporter) (NET) (Solute carrier family 6 member 2)
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MLLARMNPQVQPELGGADPLPEQPLRPCKTADLLVVKERNGVQCLLASQDSDAQPRETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQYNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFASFTLNLPWTNCGHSWNSPNCTDPKLLNASVLGDHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLMVVIVVLYFSLWKGVKTSGKVVWITATLPYFVLFVLLVHGVTLPGASNGINAYLHIDFYRLKEATVWIDAATQIFFSLGAGFGVLIAFASYNKFDNNCYRDALLTSTINCVTSFISGFAIFSILGYMAHEHKVNIEDVATEGAGLVFILYPEAISTLSGSTFWAVLFFLMLLALGLDSSMGGMEAVITGLADDFQVLKRHRKLFTCVVTISTFLLALFCITKGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSNDIQQMMGFKPGLYWRLCWKFVSPAFLLFVVVVSIINFKPLTYDDYTYPPWANWVGWGIALSSMILVPAYVIYKFLSIRGSLWERVAYGITPENEHHLVAQRDVRQFQLRHWLAI
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Mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline). Can also mediate sodium- and chloride-dependent transport of dopamine (By similarity).
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O55193
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CCR2_RAT
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C-C chemokine receptor type 2 (C-C CKR-2) (CC-CKR-2) (CCR-2) (CCR2) (CD antigen CD192)
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MEDSNMLPQFIHGILSTSHSLFPRSIQELDEGATTPYDYDDGEPCHKTSVKQIGAWILPPLYSLVFIFGFVGNMLVIIILISCKKLKSMTDIYLFNLAISDLLFLLTLPFWAHYAANEWVFGNIMCKLFTGLYHIGYFGGIFFIILLTIDRYLAIVHAVFALKARTVTFGVITSVVTWVVAVFASLPGIIFTKSEQEDDQHTCGPYFPTIWKNFQTIMRNILSLILPLLVMVICYSGILHTLFRCRNEKKRHRAVRLIFAIMIVYFLFWTPYNIVLFLTTFQEFLGMSNCVVDMHLDQAMQVTETLGMTHCCVNPIIYAFVGEKFRRYLSIFFRKHIAKNLCKQCPVFYRETADRVSSTFTPSTGEQEVSVGL
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Key functional receptor for CCL2 but can also bind CCL7 and CCL12 (By similarity). Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (By similarity). Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B (By similarity). Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation (By similarity). Facilitates the export of mature thymocytes by enhancing directional movement of thymocytes to sphingosine-1-phosphate stimulation and up-regulation of S1P1R expression signals through the JAK-STAT pathway to regulate FOXO1 activity leading to an increased expression of S1P1R (By similarity). Plays an important role in mediating peripheral nerve injury-induced neuropathic pain (By similarity). Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (By similarity). Mediates the recruitment of macrophages and monocytes to the injury site following brain injury (By similarity).
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O55197
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C3AR_RAT
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C3a anaphylatoxin chemotactic receptor (C3AR) (C3a-R)
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MESFTADTNSTDLHSRPLFKPQDIASMVILSLTCLLGLPGNGLVLWVAGVKMKRTVNTVWFLHLTLADFLCCLSLPFSVAHLILRGHWPYGLFLCKLIPSVIILNMFASVFLLTAISLDRCLMVHKPIWCQNHRSVRTAFAVCGCVWVVTFVMCIPVFVYRDLLVVDDYSVCGYNFDSSRAYDYWDYMYNSHLPEINPPDNSTGHVDDRTAPSSSVPARDLWTATTALQSQTFHTSPEDPFSQDSASQQPHYGGKPPTVLIATIPGGFPVEDHKSNTLNTGAFLSAHTEPSLTASSSPLYAHDFPDDYFDQLMYGNHAWTPQVAITISRLVVGFLVPFFIMITCYSLIVFRMRKTNLTKSRNKTLRVAVAVVTVFFVCWIPYHIVGILLVITDQESALREVVLPWDHMSIALASANSCFNPFLYALLGKDFRKKARQSVKGILEAAFSEELTHSTSCTQDKAPSKRNHMSTDV
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Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production.
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O55201
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SPT5H_MOUSE
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Transcription elongation factor SPT5 (DRB sensitivity-inducing factor large subunit) (DSIF large subunit)
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MSDSEDSNFSEEEDSERSSEAEEAEVEEDQRSAAGSEKEEEPEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQWEDGAEDILEKEEIEASNIDNVVLDEDRSGARRLQNLWRDQREEELGEYYMKKYAKSSVGETVYGGSDELSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEVANLKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLKMIPRIDYDRIKARMSLKDWFAKRKKFKRPPQRLFDAEKIRSLGGDVASDGDFLIFEGNRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTESTGKEREHNFQPGDNVEVCEGELINLQGKVLSVDGNKITIMPKHEDLKDMLEFPAQELRKYFKMGDHVKVIAGRFEGDTGLIVRVEENFVILFSDLTMHELKVLPRDLQLCSETASGVDVGGQHEWGELVQLDPRTVGVIVRLERETFQVLNMHGKVVTVRHQAVTQKKDNRFAVALDSDQNNIHVKDIVKVIDGPHSGREGEIRHLYRSFAFLHCKKLVENGGMFVCKARHLVLAGGSKPRDVTNLTVGGFTPMSPRISSPMHPSAEGQHGGFGSPGGMSRGRGRRDNELIGQTVRISQGPYKGYIGVVKDATESTARVELHSTCQTISVDRQRLTTVDSQRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSRAEEEYEYAFDDEPTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSGIEQNSSDWVTTDIQVKVRDTYLDTQIVGQTGVIRSVTGGMCSVYLKDSEKVVSISSEHLEPITPTKNNKVKVILGEDREATGVLLSIDGEDGIIRMDLEDQQIKILNLRFLGKLLEA
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Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (By similarity).
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O55203
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LDB2_MOUSE
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LIM domain-binding protein 2 (LDB-2) (Carboxyl-terminal LIM domain-binding protein 1) (CLIM-1) (LIM domain-binding factor CLIM1)
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MSSTPHDPFYSSPFGPFYRRHTPYMVQPEYRIYEMNKRLQSRTEDSDNLWWDAFATEFFEDDATLTLSFCLEDGPKRYTIGRTLIPRYFSTVFEGGVTDLYYILKHSKESYHNSSITVDCDQCAMVTQHGKPMFTKVCTEGRLILEFTFDDLMRIKTWHFTIRQYRELVPRSILAMHAQDPQVLDQLSKNITRMGLTNFTLNYLRLCVILEPMQELMSRHKTYNLSPRDCLKTCLFQKWQRMVAPPAEPTRQPTTKRRKRKNSTSSTSNSSAGNTTNSAGSKKKTPAASLSLATQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQYDAANGMDDEEDFNNSPALGNNSPWNSKPPATQETKSENAPPQASQ
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Transcription cofactor. Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors.
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O55207
|
SYNJ2_RAT
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Synaptojanin-2 (EC 3.1.3.36) (Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 2)
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MALSKGLRLLARLDPTGPSSVLLEARGRGDCLLFEAGAVATLAPEEKEVIKGLYGKPTDAYGCLGELSLKSGGVPLSFLVLVTGCTSVGRIPDAEIYKITGTEFYPLQEEAKEEDRLPALKKILSSGVFYFAWPNDGACFDLTIRAQKQGDDCSEWGTSFFWNQLLHVPLRQHQVNCHDWLLKVICGVVTIRTVYASHKQAKACLISRISCERAGARFLTRGVNDDGHVSNFVETEQAIYMDDGVSSFVQIRGSVPLFWEQPGLQVGSHHLRLHRGLEANAPAFERHMVLLKEQYGQQVVVNLLGSRGGEEVLNRAFKKLLWASCHAGDTPMINFDFHQFAKGRKLEKLENLLRPQLKLHWDDFGVFAKGENVSPRFQKGTLRMNCLDCLDRTNTVQCFIALEVLHLQLESLGLNSKPITDRFVESFKAMWSLNGHGLSKVFTGSRALEGKAKVGKLKDGARSMSRTIQSNFFDGVKQEAIKLLLVGDVYNEESTDKGRMLLDNTALLGLGSNKQNSLSGMLDGKATPRILKAMTERQSEFTNFKRIQIAMGTWNVNGGKQFRSNLLGTTELTDWLLDAPQLSGAVDSQDDGGPADIFAVGFEEMVELSAGNIVNASTTNRKMWGEQLQKAISRSHRYILLTSAQLVGVCLYIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVGIRFQFHSTSFCFICSHLTAGQSQVKERNEDYREITHKLSFPSGRNIFSHDYVFWCGDFNYRIDLTYEEVFYFVKRQDWKKLMEFDQLQLQKSSGKIFKDFHEGTINFGPTYKYDVGSAAYDTSDKCRTPAWTDRVLWWRKKHPYDKTAGELNLLDSDLDGDANIRHTWSPGTLKYYGRAELQASDHRPVLAIVEVEVQEVDVGARERVFQEVSSVQGPLDATVIVNLQSPTLEERNEFPEDLRTELMQTLGNYGTIILVRINQGQMLVTFADSHSALSVLDVDGMKVKGRAVKIRPKTKDWLEGLREELIRKRDSMAPVSPTANSCLLEENFDFTSLDYESEGDVLEDDEDYLADEFGQPVVSDSELGGDDSSDTMSASTPASKSPALAKKKQHPTYKDDADLMTLKLELEVAGNFRHRSPSRSLSVPNRPRPPHPPQRPPPPTGLMVKKSASDASISSGTHGQYSILQTAKLLPGAPQQPPKARTGISKPYNVKQIKTTNAQEAEAAIRCLLEAGGGVPESAPGATPLRNQGSSKPEASLGPPVLPRRPVPRVPTMKKPTLRRTGKPMLPEEQCEQQPVHFTMASQEMNLETPPPITAPIPPVPKPRTFQPGRGVERRPSGGKPEPDDAPPVTGAVELSSPEAPEAPSLAPKVPPRRKKSAPAAFHLQVLQSNSQLLQGLTCSSSSPSPPKPDTPLLYPQMALGTSSAISPETDGPRVTEPEAASFHGDYPDPFWSLLHHPKLLNNNTWLSKSSEPLDLGSRTPERTHTDSAQVNASVVERGLPPDHGGKDFSHWMAASNKDKRTTLGV
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Inositol 5-phosphatase which may be involved in distinct membrane trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis (By similarity).
|
O55208
|
FIGLA_MOUSE
|
Factor in the germline alpha (FIGalpha) (Transcription factor FIGa)
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MDTAPASPEPFLVTPQAEVLEELIQAQMGPLPRLAAICRLKRLPSGGYSTTDDLHLVLERRRVANAKERERIKNLNRGFAKLKALVPFLPQSRKPSKVDILKGATEYIQILGCVLEEAKVSEKQSPEEQTHSGRPSDPHVSSTRELLGNATQPTSCASGLKKEEEGPWAYAGHSEPLYSYHQSTVPETRSYFTH
|
Germ-line specific transcription factor implicated in postnatal oocyte-specific gene expression. Plays a key regulatory role in the expression of multiple oocyte-specific genes, including those that initiate folliculogenesis and those that encode the zona pellucida (ZP1, ZP2 and ZP3) required for fertilization and early embryonic survival. Essential for oocytes to survive and form primordial follicles. The persistence of FIGLA in adult females suggests that it may regulate additional pathways that are essential for normal ovarian development. Binds to the E-box (5'-CANNTG-3') of the ZPs (ZP1, ZP2, ZP3) promoters.
|
O55222
|
ILK_MOUSE
|
Integrin-linked protein kinase (EC 2.7.11.1) (59 kDa serine/threonine-protein kinase) (Beta-integrin-linked kinase) (ILK-1) (ILK-2) (p59ILK)
|
MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLAKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQAPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK
|
Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Regulates cell motility by forming a complex with PARVB. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.
|
O55225
|
OTOG_MOUSE
|
Otogelin
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MGARMPRRCLLLLSCFCLLRVESTAEVQHQASALTWKISAELQQEPAPEPSHTYQEMSLAVEDVTTVMEGQEAEALAASAMSSWERRLHRAKCAPSYLFSCFNGGECVHPALCDCRRFNATGPRCQLVYNVGPERDSICRTWGQHHVETFDGLYYYFSGKGSYTLVGHHEPEGQSFSIQVHNDPQCGSAHYTCPRSVSLFLSGEREICLAKEVTHGGVRVQLPQVVGGVQLQQLAGYVIARHPSAFTLAWDGISAIYIKMSPEFLGWTHGLCGNNNADPQDDLVTSYGKVTDDVGEFVHSWQEQVPNSPPGPVTTSLPRPPCLQQSPASMQGVYERCEVLLRPPFDTCHAYVSPLPFAASCTSDLCQSGGDEATWCRALMEYARACAQAGRPLQGWRTQLSQCTVHCKEKAFIYNECIACCPASCQSRASCVDSEITCVDGCYCPNGLIFEDGGCMSPAECPCEFHGTLHPPGSVVTEDCNACTCTAGKWVCSSSVCPAECSVTGDIHFTTFDGRRYTFPATCQYILAKSRSSGTFTVTLQNAPCGLNQDGACVQSVSVILHQDPRRQVTLTQAGDVLLFDQYKITPPYSDDAFEIRRLSSVFLRVRTNVGVRILYDREGLRLYLQVDQRWVEDTVGLCGTFNGNTQDDFLSPVGVPESTPQLFGNSWKTLSACVPLVPGSLLDPCDVHLQAASYALQSCSVLTGELFAPCSAYLSPIPYFEQCRRDACRCGQPCLCATLAHYARLCRRHGLPVDFRAHLPACALSCEATKEYSPCVTLCAPTCQDLASPDVCGANGGGNFSREECVEGCTCPPDTFLDTQADLCVPRNQCSCHFQGVDYPPGDSDIPSLGHCHCKDGVMSCDSRAPAAACPAGQVFVNCSELHPDPELSRERTCEQQLLNLSVPARGPCLSGCACPQGLLRHGDACFPPEECPCTWKGKEYFPGDQVVSSCHTCVCQRGSFQCTLHPCASTCTAYGDRHYRTFDGLPYDFVGACKVHLVKSTSELSFSVMVEDVNCYGSGVICRKSISINVGSSLIIFDDDSGDPSPESFLDEKQAVHIWRAGFFTLVHFPREHITLLWDQRTTVHVQAGPQWQGQLVGLCGNFDLKTINEMRTPENLELTNPQEFGSSWAAVECPDTPDPRDTCVLNPLREPFARKECGILLSEVFETCHPVVDVTWFYSNCLTDTCGCSRGGDCECFCASVAAYAHQCCQHGVVIDWRTPRICPYDCDFFNKALGKGPYQLSSVAAGGTLVATKAVDSDIALVRAEDLAPGDISSFLLTAALYKAKAHDPDVVSLEAADRPNFFLHTTANGSIGLAKWQRDEAFHQHASFSLHRGTWQAGLVALESLAKPGSFLHSSGLELALRAYEHTEVFRGGALFRLLDAKPLGAAYPTCEWRYDACASPCFQTCRDPRATSCQDVPRVEGCVPVCPTPKVLDEVTQRCVYLEDCVEPAPRGPTETLGNETLVPGQVPPTTSAEQQLPQGLPGASAYSPAPVPVAPPTSAPNPPMAATEGQAPSPGSTQPTLQTPLGLTTSNFPAGHTEATAREEGAASLLTTSHPPGFSSSLPSSLQMPTSGIVSGATETTKVTITFTGSPNTTVASRSPPIPRFPLMTKAVTVPSHDSFPVKTTPLQPSWLWSLSSRPMTSLGATSWPPTSPGSHLSTAVTKVANKTMTSLSVLAQSTSSSSQPLAAVTTAHRAPASPLVTKGLEVVSATEKGEAGHSQLTELPVSPPPSPAPIDLPHPAQHTTTAPGPSALSPGILAAGSPSTGAHRPGATALASLEPTRPPHLLSGLPLDTSLPLAKVGTSAPVATPGSKGYIPTPPPQHQATTLATAMTVSPLTQSLSLTVPLMSAVEEQAHSPSPKPPQGTGMAPDQMLGATLPSFGASSVIAGVPPTVSAAPRKSTTQRAAILSKKVSPPTLISDSVQGGFTELTPIVSHTVTPLATEAEGPRAGTVPLVPTTYSLSRVSARTASREGPLVLLPQLAEAYGTPAGLQPQEDLVRQATTEQSGRSAPAKSIAEESMEAEVNTSATCVPIAEQDCVRHICLEGQLIRVNQTQHCPQGAVRPRCGVLGLAVRVGGDRCCPQWECACRCSIFPDLSFVTFDGSHAALFKEAIYVLSQSPDETISVHVLDCKSANLGHLNWPPFCLVILNVTHLAHHVSIDRFNRKVTVDSQVVWPPMSRYGFRIEDTGHMYIVRTPSHIQIQWLHSSGLMILEASKVSKTQGHGLCGICDGDAANDLTLKDGSVLGEAEDPAPFLDSWQVPSSLTSEGQTRFRPDSCATADCSPCLRMVSNRTFSACHSFVSPESFCELWIRDTKYVQQPCVALTVYVAMCHKFHVCIEWRGSDYCPFLCSSDSTYQACVAACEPPDTCQDGILGPLDPEQCQVLGEGCVCTEGTILHRRHSALCIPEDKCACTDSTGVPRALGETWNSSLSGCCQQQCQAPDTIIPVDLDCPGPRPESCPRFGEVILLQPTEDPCCLGSVCVCNQTLCEGLAPTCRPGHSLITHFQEDSCCPSYSCECDPGLCEAEQVPTCREDQILIEGRLGDSCCTSYFCGCGECSDPMPECQEGEALTVHRNTTELCCPLYQCVCENFRCPQVQCGMGTSLVEVWSPDRCCPYKSCECDCDTIPVPRCHLWEKSQLDEEFMHSVENVCGCAKYECVKAPVCLSRELGVMQPGQTVVELSADGVCHTSRCTDVLDPLTNFYQINITSVLCDMHCEANQEYDHPRDLAACCGSCRNVSCLFTFPNGTTSLFLPGASWIADCARHHCGSTPLGAVLVRSPISCPPFNETECAKVGGSVVPSLEGCCRACKEDGRSCKKVTIRMTIRKNDCRSNTPVNLVSCDGRCPSASIYNHNINTYARFCKCCREVGLQRRSVQLFCATNATWVPYTVQEPTDCACQWS
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Glycoprotein specific to acellular membranes of the inner ear. May be required for the anchoring of the otoconial membranes and cupulae to the underlying neuroepithelia in the vestibule. May be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. May play a role in mechanotransduction processes.
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O55229
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CHKB_MOUSE
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Choline/ethanolamine kinase (Choline kinase beta) (CK) (CKB) (EC 2.7.1.32) (Ethanolamine kinase) (EK) (EC 2.7.1.82) (choline/ethanolamine kinase beta) (CKEKB)
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MAADGTGVVGGGAVGGGLPKDGLQDAKCPEPIPNRRRASSLSRDAQRRAYQWCREYLGGAWRRARPEELSVCPVSGGLSNLLFRCSLPNHVPSVGGEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYLPSRPLKTQELRDPVLSGAIATRMARFHGMEMPFTKEPRWLFGTMERYLKQIQDLPSTSLPQMNLVEMYSLKDEMNSLRKLLDDTPSPVVFCHNDIQEGNILLLSEPDSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEEWPFYKARPTDYPTREQQLHFIRHYLAEVQKGEILSEEEQKKREEELLLEISRYSLASHFFWGLWSTLQASMSTIEFGYLEYAQSRFQFYFQQKGQLTSSPSS
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Has a key role in phospholipid metabolism, and catalyzes the first step of phosphatidylethanolamine and phosphatidylcholine biosynthesis.
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O55230
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RA51D_MOUSE
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DNA repair protein RAD51 homolog 4 (R51H3) (RAD51 homolog D) (RAD51-like protein 3)
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MGMLRAGLCPGLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLSYKALVALRRVLLAQFSAFPLNGADLYEELKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKQASALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLGGQQREGLALMMQLARELKILARDLGVAVVVTNHLTRDWDGRRFKPALGRSWSFVPSTRILLDVTEGAGTLGSSQRTVCLTKSPRQPTGLQEMIDIGTLGTEEQSPELPGKQT
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Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM (By similarity).
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O55232
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OREX_RAT
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Hypocretin neuropeptide precursor (Hypocretin) (Hcrt) (Orexin precursor) (Prepro-orexin) (Preprohypocretin) [Cleaved into: Orexin-A (Hypocretin-1) (Hcrt1); Orexin-B (Hypocretin-2) (Hcrt2)]
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MNLPSTKVPWAAVTLLLLLLLPPALLSLGVDAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRPGPPGLQGRLQRLLQANGNHAAGILTMGRRAGAELEPYPCPGRRCPTATATALAPRGGSRV
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Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. A modulation effect on luteinizing hormone-releasing hormone (LHRH) secretion also suggests a more minor contribution to the regulation of reproductive function.
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O55233
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CER1_MOUSE
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Cerberus (Cerberus-like protein) (Cer-l) (Cerberus-related protein)
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MHLLLVQLLVLLPLGKADLCVDGCQSQGSLSFPLLERGRRDLHVANHEEAEDKPDLFVAVPHLMGTSLAGEGQRQRGKMLSRLGRFWKKPETEFYPPRDVESDHVSSGMQAVTQPADGRKVERSPLQEEAKRFWHRFMFRKGPAFQGVILPIKSHEVHWETCRTVPFNQTIAHEDCQKVVVQNNLCFGKCSSIRFPGEGADAHSFCSHCSPTKFTTVHLMLNCTSPTPVVKMVMQVEECQCMVKTERGEERLLLAGSQGSFIPGLPASKTNP
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Cytokine that may play a role in anterior neural induction and somite formation during embryogenesis in part, through a BMP-inhibitory mechanism. Can regulate Nodal signaling during gastrulation as well as the formation and patterning of the primitive streak.
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O55234
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PSB5_MOUSE
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Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain epsilon chain) (Multicatalytic endopeptidase complex epsilon chain) (Proteasome chain 6) (Proteasome epsilon chain) (Proteasome subunit X)
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MALASVLQRPMPVNQHGFFGLGGGADLLDLGPGSPGDGLSLAAPSWGVPEEPRIEMLHGTTTLAFKFLHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGTAFSVGSGSVYAYGVMDRGYSYDLKVEEAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHDKYSSVSVP
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Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity.
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O55236
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MCE1_MOUSE
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mRNA-capping enzyme (HCE) (MCE1) [Includes: mRNA 5'-triphosphate monophosphatase (EC 3.6.1.74) (mRNA 5'-phosphatase); mRNA guanylyltransferase (EC 2.7.7.50) (GTP--RNA guanylyltransferase) (GTase)]
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MAYNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMSLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERSPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDIEEAPPPPVLPDWCFEDEDEEDEDEDGKKDSEPGSSASFSKRRKERLKLGAIFLEGITVKGVTQVTTQPKLGEVQQKCHQFCGWEGSGFPGAQPVSMDKQNIRLLEQKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLEFPFRKDLRMHLSNTLLDGEMIIDKVNGQAVPRYLIYDIIKFNAQPVGDCDFNIRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRPKQFFDINISRKLLEGNFAKEVSHEMDGLIFQPIGKYKPGRCDDILKWKPPSLNSVDFRLKITRMGGEGLLPQNVGLLYVGGYERPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRIDKSFPNAYNTAMAVCNSISNPVTKEMLFEFIDRCAAAAQGQKRKYPLDPDTELMPPPPPKRLHRPT
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Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate.
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O55237
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CD70_MOUSE
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CD70 antigen (CD27 ligand) (CD27-L) (Tumor necrosis factor ligand superfamily member 7) (CD antigen CD70)
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MPEEGRPCPWVRWSGTAFQRQWPWLLLVVFITVFCCWFHCSGLLSKQQQRLLEHPEPHTAELQLNLTVPRKDPTLRWGAGPALGRSFTHGPELEEGHLRIHQDGLYRLHIQVTLANCSSPGSTLQHRATLAVGICSPAAHGISLLRGRFGQDCTVALQRLTYLVHGDVLCTNLTLPLLPSRNADETFFGVQWICP
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Cytokine which is the ligand for CD27. The CD70-CD27 pathway plays an important role in the generation and maintenance of T cell immunity, in particular during antiviral responses. Upon CD27 binding, induces the proliferation of costimulated T-cells and enhances the generation of cytolytic T-cells.
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O55239
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NNMT_MOUSE
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Nicotinamide N-methyltransferase (EC 2.1.1.1)
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MESGFTSKDTYLSHFNPRDYLEKYYSFGSRHCAENEILRHLLKNLFKIFCLGAVKGELLIDIGSGPTIYQLLSACESFTEIIVSDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLEGNRMKGPEKEEKLRRAIKQVLKCDVTQSQPLGGVSLPPADCLLSTLCLDAACPDLPAYRTALRNLGSLLKPGGFLVMVDALKSSYYMIGEQKFSSLPLGWETVRDAVEEAGYTIEQFEVISQNYSSTTSNNEGLFSLVGRKPGRSE
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Catalyzes the N-methylation of nicotinamide using the universal methyl donor S-adenosyl-L-methionine to form N1-methylnicotinamide and S-adenosyl-L-homocysteine, a predominant nicotinamide/vitamin B3 clearance pathway. Plays a central role in regulating cellular methylation potential, by consuming S-adenosyl-L-methionine and limiting its availability for other methyltransferases (By similarity). Actively mediates genome-wide epigenetic and transcriptional changes through hypomethylation of repressive chromatin marks, such as H3K27me3. In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state (By similarity). Acts as a metabolic regulator primarily on white adipose tissue energy expenditure as well as hepatic gluconeogenesis and cholesterol biosynthesis. In white adipocytes, regulates polyamine flux by consuming S-adenosyl-L-methionine which provides for propylamine group in polyamine biosynthesis, whereas by consuming nicotinamide controls NAD(+) levels through the salvage pathway. Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase. Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification (By similarity).
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O55240
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RDH5_MOUSE
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Retinol dehydrogenase 5 (EC 1.1.1.209) (EC 1.1.1.315) (EC 1.1.1.53) (11-cis retinol dehydrogenase) (11-cis RDH) (11-cis RoDH) (9-cis retinol dehydrogenase) (Cis-retinol dehydrogenase)
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MWLPLLLGALLWAVLWLLRDRQSLPASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKACWARLPPAIQAHYGEAFLDTYLRVQRRIMNLICDPELTKVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLTWILPRPAQSVS
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Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner. Has no activity towards all-trans retinal (By similarity). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE). Also recognizes steroids (androsterone, androstanediol) as its substrates (By similarity).
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O55241
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OREX_MOUSE
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Hypocretin neuropeptide precursor (Hypocretin) (Hcrt) (Orexin precursor) (Prepro-orexin) (Preprohypocretin) [Cleaved into: Orexin-A (Hypocretin-1) (Hcrt1); Orexin-B (Hypocretin-2) (Hcrt2)]
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MNFPSTKVPWAAVTLLLLLLLPPALLSLGVDAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRPGPPGLQGRLQRLLQANGNHAAGILTMGRRAGAELEPHPCSGRGCPTVTTTALAPRGGSGV
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Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested.
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O55242
|
SGMR1_MOUSE
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Sigma non-opioid intracellular receptor 1 (Sigma 1-type opioid receptor) (Sigma1-receptor) (Sigma1R)
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MPWAAGRRWAWITLILTIIAVLIQAAWLWLGTQNFVFSREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCILHASLSEYVLLFGTALGSHGHSGRYWAEISDTIISGTFHQWKEGTTKSEVFYPGETVVHGPGEATALEWGPNTWMVEYGRGVIPSTLFFALADTFFSTQDYLTLFYTLRAYARGLRLELTTYLFGQDS
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Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration. Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112.
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O55528
|
L_SENDO
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RNA-directed RNA polymerase L (Protein L) (Large structural protein) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); GTP phosphohydrolase (EC 3.6.1.-); GDP polyribonucleotidyltransferase (EC 2.7.7.88) (PRNTase); mRNA cap methyltransferase (EC 2.1.1.375) (mRNA (guanine-N(7)-)-methyltransferase) (G-N7-MTase) (mRNA (nucleoside-2'-O-)-methyltransferase) (N1-2'-O-MTase)]
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MDGQESTQNPSDILYPECHLNSPIVRGKIAQLHVLLDVNQPYILKDDSIINITKHKIRNGGLSLRQIKIRSLGKALQRTIKDLDRYTFEPYPTYSQELLRLDIPEICDKIRSVFAVSDRLTKELSNGFQDLWLNIFKQLGNIEGREGYDPLQDISTIPEITERYSRNKWYRPFLTWFSIKYDMRWMQKTRPGGPLDTSNSHNLLECKSYTLVTYGDLVMILNKSTLTGYILTPELVLMYCDVVEGRWNMSAAGQLDKRSTGITSKGEELWELVDSLFSSLGEEIYNVIALLEPLSLALIQLSDPVIPLRGAFMRHVLTELQTVLTSKDVYTDPEADAIVESLLAIFHGTSIDEKAEIFSFFRTFGHPSLEAVTAADKVRAHMYAQKAIKLKTLHECHAVFCTIIINGYRERHGGQWPPCDFPDHVCLELRNAQGSNTAISYECAVDNYTSFIGFKFRKFIEPQLDEDLTIYMKDKALSPRKEAWDSVYPDSNLYYKVPESEETRRLIEVFINDENFNPEDIIDYVESGDWLKDEKFNISYSLKEKEIKQEGRLFAKMTYKMRAVQVLAETLLAKGIGELFSENGMVKGEIDLLKRLTTLSVSGVPRTDSVYNNPRSSEKRNESMKKRNSKGYWDEKKRSRHEFKATDSSTDGYETLSCFLTTDLKKYCLNWRFESTALFGQRCNEIFGFKTFFNWMHPVLEKCTIYVGDPYCPVADRMHRQLQDHADSGIFIHNPRGGIEGYCQKLWTLISISAIHLAAVRVGVRVSAMVQGDNQAIAVTSRVPVAQTYKQKKNHVYEEITRYFGALRHVMFDIGHELKLNETIISSKMFVYSKRIYYDGKILPQCLKALTRCVFWSETLVDENRSACSNISTSIAKAIENGYSPILGYCIALYKTCQQVCISLGMTINPTISPTVRDQYFKGKNWLRCAVLIPANVGGFNYMSTSRCFVRNIGDPAVAALADLKRFIRADLLDKQVLYRVMNQEPGDSSFLDWASDPYSCNLPHSQSITTIIKNITARSVLQESPNPLLSGLFTETSGEEDLNLASFLMDRKVILPRVAHEILSNSLTGVREAIAGMLDTTKSLVRASVKRGGLSYGILRRLVNYDLLQYETLTRTLRKPVKDNIEYEYMCSVELAVGLRQKMWIHLTYGRPIHGLETPDPLELLRGTFIEGSEVCKLCRSEGADPIYTWFYLPDNIDLDTLTNGSPAIRIPYFGSATDERSEAQLGYVRNLSKPAKAAIRIAMVYTWAYGTDEISWMEAALIAQTRANLSLENLKLLTPVSTSTNLSHRLKDTATQMKFSSATLVRASRFITISNDNMALKEAGESKDTNLVYQQIMLTGLSLFEFNMRYKKGSLEKPLILHLHLNNGCCIMESPQEANIPPRSTLDLEITQENNKLIYDPDPLRDVDLELFSKVRDVVHTVDMTYWSDDEVIRATSICTAMTIADTMSQLDRDNLKEMIALVNDDDVNSLITEFMVIDVPLFCSTFGGILVNQFAYSLYGLNIRGREEIWGHVVRILKDTSHAVLKVLSNALSHPKIFKRFWNAGVVEPVYGPNLSNQDKTLLALSVCEYSVDLFMHDWQGGVPLEVFICDNDPDVADMRRSSFLARHLAYLCSLAEISRDGPRLESMNSLERLETLKSYLELTFLDDPVLRYSQLTGLVIKVFPSTLTYIRKSSIKVLRTRGIGVPEVLEDWDPEADNALLDGIAAEIQQNIPLGHQTRAPFWGLRVSKSQVLRLRGYEEITRGEVGRSGVGLTLPFDGRYLSHQLRLFGVNSTSCLKALELTYLLSPLVDKDKDRLFLGEGAGAMLSCYDATLGPCINYYNSGVYSCDVNGQRELNIYPAEVALVGKKLNNVTSLGQRVKVLFNGNPGSTWIGNDECEALIWNELQNNSIGLVHCDMEGGDHKDDQVVLHEHYSVIRIAYLVGDRDVVLISKIAPRLGTDWTRQLSLYLRYWDEVNLVVLKTSNPASTEMYLLSRHPKSDIIEDSKTVLASLHPLSKEDSIKIEKWILIEKAKAHEWVTRELREGSSSSGMLRPYHQALQTFGFEPNLYKLSRDFLSTMNIADTHNCMTAFNRVLKDTIFEWARITESDKRLKLTGKYDLYPVRDSGKLKTISRRLVLSWVSLSMSTRLVTGSFPDQKFEARLQLGIVSLSSREIRNLRVITKTILDRFENTIHSITYRFLTKEVKILMKILGAVKMFGARQNEYTTVVDDGSLDDIEPYDSL
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RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene. RNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated.
|
O56075
|
POLG_PEMVM
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Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
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MASITFGNACTVVFGQVRKEEVTAGPVAVNLNEGTRMVVVPTAAQMATPTPSVSIKIINRWSNKAVSSYERQVEDVFANFFAKKERSDELLTRYYGKVVQKGNKLMVKRAPLHVARVLEKQRLQDIEDEKAFLQYRDAGVHVAGSVKFTDTRSRGQTVSFRTEHYKPTGKIVQKKKAQKQRANADVDHLIDEVMKICSADCKQVEFISMGKRRLTAKFKLFGKSVIPCIHLAHEQGRRLRRELDPRIHEQVIAHLVTGRKVRELIKDDMVTYGWSGAILNKNLFKRTPFRWDEVVIRGRLYGKLVDARSKLSECSKDKIHQYSSFEAQFWKGWKNKFDTLHPHNKDHICEPTINNEKCGEIVATIFQAIHPVIKVSCSTCRERLTKASNEELNEYLATNLACHKATFDDMRQQHATVNTVLNKIEQTSLANPNLKDSMEIVRLLQNLNQTQARQLMKVNNTLLKGNVATSEEFSDATTQLLEVTRWYAKHLSLVDEGSISSFRNKATSKSLINPSLLCDNQLDRNGNFVWGERGRHSKRFFENFFEEVVPGGGYKKYQIRNSPNCTRKLAIGNLIVPMSLERARNALIGESVERLPVTEACVSRVNGAFMHVASCVTSDNGSAHFSPLYSPTKRHLVVGTTGDSKYIDLPATESDKMYVAKEGYCYINIFLAMLVNVNEDSAKDFTKMIRDTIVPMLGTWPSMMDVATACYILTVFHPETKSAELPRILVDHTNKTMHVIDSFGSISTGYHILKAGTVSQLIHFASNELVSEMKHYVVGGEAPHARRMRMEKALIQGIFKPKQLVYLIEEDPYILMMSLVSPTLLINLFNVGGLEVAMKHWIKKEMNIGLIFSMLSSLAQKVSRADLVNEQITMIDANAAQFIETLAGIDVENPMRNELVSALTMMLARSDVDSTLNKTGFTGFSDTLLEMREKIIGDELNKVWSELSWWEKFSSIIFSRRARKHIMAPLPNTKLHAIDDRYAISCTWLHGKIKARFNGAKSATLEVCKKVTSILKRNTVDSILYICRKCYSDIFYFVNVMLISSMILSVIYTMHKMVIESRAHKQAMVIMKMREDELVVKQMYDQYCKLANETPTKEEFFQYVCKMNKELGERIAPEFEEGSLVVYQAKTETELGLEKVVAYLALIAMIFDGERSDAVFRALSKLKTVFGTLGETVRYQSLDEIESVADEKKMTIDFELEGSEASSSTVMSAKFSDWWYKQLETNRVVPHYRIGGEFVEFTRKTAAEVVNNMRASNASEFLVRGAVGSGKSTGLPHLLAQKGRVLLLEPTRPLAENVCKQLRQAPFQQNPTLRMRGLTTFGSSNIVIMTSGFALHYYANNPTKLQEYDFVMIDESHTMDASAMAFYCLVREYNFQGKIIKVSATPPGKECEFKTQFDVALLIEEDLSFQQFAQSQGQGGNADMTKHGDNILVYVASYNDVDQLAELLIRGNHFVTKVDGRTMKMGSTEIVSKGTASKKHYIIATNIIENGVTLDVDVVVDFGQKVVAELDGDSRCMRYRKVAVSYGERIQRLGRVGRVKKGTALRIGHTEHGISEIPASISTEAAFLCFAYGLPVITHNVTVSILANCTVQQARTMMLFELSPFFLADLVKYNGSMHPEVHKLLKPYKLRDSEIELCKLAIPNSSIGRWLSVHEYAKLGIKIHAVDSVRIPFAGRGIPDKLYSELWHIIQEHKHEAGFGRLTSASASTIAYTLSTDPEAIPRTIALLDNLIAEEMQKKAHFEALNSTLCSQRFTLKNIVDTVRQRYMKDHSKHNIEVLQSARSQILEFNSATHDFKKVASLLGYGFLDTVQYQSKNELSKRLGLKGRWNKSLVTNDLLVCGMVLFGGVWMVWEYAKSAMNEPVRYQGKRQNQKLKFRDARDRKVGREVYGDDGTIEHFFGEAYTKKGKSKGNHTVKGMGRKTRRFIHMYGFDPTEYSFVRFVDPLTGYAIDENITCDISLVQDEVAEVRKQFINEDEISAQSIAENPGIIAYYMSRNADKALKIDLTPHNPLAVGRGGSSIAGFPEREYELRQTGKPLEVKKSEVPPVSKDVVATEGKSMCRGLRNYNPIATSICKLVNESDGHSETIHGIGFGPVIITNSHLFRRNNGTLQIQTHHGVFRVKNSTQLQVSHMAKKDMIIIKMPCDVPPFPSKLRFRQPEQGEKAVLVGSLFQQKSITSSVSESTMVMPVNDSGYWRHWVSTKDGDCGLPLVSTVDGAILGLHGLTSTKSDRNYFVPFDEQFERDILANLEKLDWKRHWLHSSDLIAWGGMSLKENHPHDCFRTSKLVTDLLGLTKDSVEYQSGQDKWVLAGLENNLKAVAQSESQLVTKHVVKGQCMYFQEYLATHSTAEKFFKPLMGAYQPSKLNKEAFTKDLYKYQNEIIVGEVDKDAFDNAVEAVIYLLDDLGFGECAYVTDEEAILDSLNMKAAVGALYKGKKKEYFESLSEPEKHHIVQASCERLFYGEMGVWNGSLKAELRPKEKVALNKTRTFTAAPIDTLLGGKCCVDDFNNRFYSLNIEGPWTVGMTKFYGGWDKLMRKLPDGWRYCHADGSQFDSSLTPFLLNAVLAVRLMFMEDWWVGEQMLRNFYTEIIYTPILTPDGTIVKKFKGNNSGQPSTVVDNTLMVMIAMFYGMKKLNWTDEQIKERIVFFAXGDDLIIAVQPEHEGILDTLQRSLGELGLKYDFSERCDDRQELWFMSHQGHLVDGMYIPKLEQERIVSILEWDRSTVIEHRAEAICAAMIEAWGYPELLKQIRLFYAWILDHDMFKSLVAEGKLPYIAETALRKLYTDADATDVELEEYILRFTEVDEDEDHNDEVRYQSGENKSKVEVDAAAAKLKEKEKEKHKKTEEGTSEGTSQTKEPDVDTGSQGIVYVPKLAKITKKMRMPMVGGQVILHIPHLLDYKPEQVDLSNTRSSQQQFTAWYNGLKEAYEITDDTSMSVLMNGLMVWCIENGTSPNINGNWTMMDGHEQNEYPLKPVIENAKPTFRQIMHHFSDAAEAYIEMRNAEKPYMPRYGLQRNLRDFSYARIAFDFYEITSRTSAKAREIHMQMKAAALNNVAIKTFGLDGNVGTQDEDTERHTANDVNRNMHSLLGMRQM
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[Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. [Viral genome-linked protein]: Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (By similarity). Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA directly binds EIF4E and is a template for transcription (By similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation (By similarity). [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication. [Capsid protein]: Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
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O56129
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CAPSD_PCV2
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Capsid protein
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MTYPRRRYRRRRHRPRSHLGQILRRRPWLVHPRHRYRWRRKNGIFNTRLSRTFGYTVKATTVRTPSWAVDMMRFNIDDFVPPGGGTNKISIPFEYYRIRKVKVEFWPCSPITQGDRGVGSTAVILDDNFVTKATALTYDPYVNYSSRHTIPQPFSYHSRYFTPKPVLDSTIDYFQPNNKRTQLWLRLQTSRNVDHVGLGTAFENSIYDQDYNIRVTMYVQFREFNLKDPPLKP
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Self-assembles to form the virion icosahedral capsid with a T=1 symmetry. This very small capsid (17 - 22 nm in diameter) allows the virus to be very stable in the environment and resistant to some disinfectants, including detergents. Essential for the initial attachment to heparan sulfate moieties and chondroitin sulfate B of the host cell surface proteoglycans. After attachment, the virus is internalized in a clathrin-, caveolae- and dynamin-independent, actin and Rho-GTPase-mediated pathway and traffics to the nucleus. The capsid protein binds and transports the viral genome and Rep across the nuclear envelope (By similarity). {ECO:0000250, ECO:0000269|PubMed:10950986, ECO:0000269|PubMed:16537616, ECO:0000269|PubMed:18952130}.
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O56861
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ENV_FFV
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Envelope glycoprotein gp130 (Env polyprotein) [Cleaved into: Leader peptide (LP) (Env leader protein) (Elp) (gp18LP); Surface protein (SU) (Glycoprotein 80) (gp80); Transmembrane protein (TM) (Glycoprotein 48) (gp48)]
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MEQEHVMTLKEWMEWNAHKQLQKLQSTHPELHVDIPEDIPLVPEKVPLKMRMRYRCYTLCATSTRIMFWILFFLLCFSIVTLSTIISILRYQWKEAITHPGPVLSWQVTNSHVTMGGNTSSSSRRRRDIQYHKLPVEVNISGIPQGLFFAPQPKPIFHKERTLGLSQVILIDSDTITQGHIKQQKAYLVSTINEEMEQLQKTVLPFDLPIKDPLTQKEYIEKRCFQKYGHCYVIAFNGNKVWPSQDLIQDQCPLPPRFGNNLKYRNHTIWKYYIPLPFKVSSNWTRVESYGNIRIGSFKVPDEFRQNATHGIFCSDALYSNWYPRDLPSSVQQSFAQAYITKVLMKRKKQPTLRDIAFPKELSPVGSGMLFRPINPYDICNMPRAVLLLNKTYYTFSLWEGDCGYYQHNLTLHPACKNFNRTRQDHPYACRFWRNKYDSESVQCYNNDMCYYRPLYDGTENTEDWGWLAYTDSFPSPICIEEKRIWKKNYTLSSVLAECVNQAMEYGIDEVLSKLDLIFGNLTHQSADEAFIPVNNFTWPRYEKQNKQQKTSCERKKGRRQRRSVSTENLRRIQEAGLGLANAITTVAKISDLNDQKLAKGVHLLRDHVVTLMEANLDDIVSLGEGIQIEHIHNHLTSLKLLTLENRIDWRFINDSWIQEELGVSDNIMKVIRKTARCIPYNVKQTRNLNTSTAWEIYLYYEIIIPTTIYTQNWNIKNLGHLVRNAGYLSKVWIQQPFEVLNQECGTNIYLHMEECVDQDYIICEEVMELPPCGNGTGSDCPVLTKPLTDEYLEIEPLKNGSYLVLSSTTDCGIPAYVPVVITVNDTISCFDKEFKRPLKQELKVTKYAPSVPQLELRVPRLTSLIAKIKGIQIEITSSWETIKEQVARAKAELLRLDLHEGDYPEWLQLLGEATKDVWPTISNFVSGIGNFIKDTAGGIFGTAFSFLGYVKPVLLGFVIIFCIILIIKIIGWLQNTRKKDQ
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The surface protein (SU) attaches the virus to the host cell by binding to the cell receptor. This interaction triggers the refolding of transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). The leader peptide is a component of released, infectious virions and is required for particle budding.
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O57209
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MCEL_VACCA
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mRNA-capping enzyme catalytic subunit (Virus termination factor large subunit) (VTF large subunit) (mRNA-capping enzyme 97 kDa subunit) (mRNA-capping enzyme D1 subunit) (mRNA-capping enzyme large subunit) [Includes: Polynucleotide 5'-triphosphatase (EC 3.6.1.74) (mRNA 5'-triphosphatase) (TPase); mRNA guanylyltransferase (EC 2.7.7.50) (GTP--RNA guanylyltransferase) (GTase); mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56) (mRNA cap methyltransferase)]
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MDANIVSSSTIATYIDALAKNASELEQRSTAYEINNELELVFIKPPLITLTNVVNISTIQESFIRFTVTNKEGVKIRTKIPLSKVHGLDVKNVQLVDAIDNIVWEKKSLVTENRLHKECLLRLSTEERHIFLDYKKYGSSIRLELVNLIQAKTKNFTIDFKLKYFLGSGAQSKSSLLHAINHPKSRPNTSLEIEFTPRDNEKVPYDELIKELTTLSRHIFMASPENVILSPPINAPIKTFMLPKQDIVGLDLENLYAVTKTDGIPITIRVTSKGLYCYFTHLGYIIRYPVKRIIDSEVVVFGEAVKDKNWTVYLIKLIEPVNAINDRLEESKYVESKLVDICDRIVFKSKKYEGPFTTTSEVVDMLSTYLPKQPEGVILFYSKGPKSNIDFKIKKENTIDQTANVVFRYMSSEPIIFGESSIFVEYKKFSNDKGFPKEYGSGKIVLYNGVNYLNNIYCLEYINTHNEVGIKSVVVPIKFIAEFLVNGEILKPRIDKTMKYINSEDYYGNQHNIIVEHLRDQSIKIGDIFNEDKLSDVGHQYANNDKFRLNPEVSYFTNKRTRGPLGILSNYVKTLLISMYCSKTFLDDSNKRKVLAIDFGNGADLEKYFYGEIALLVATDPDADAIARGNERYNKLNSGIKTKYYKFDYIQETIRSDTFVSSVREVFYFGKFNIIDWQFAIHYSFHPRHYATVMNNLSELTASGGKVLITTMDGDKLSKLTDKKTFIIHKNLPSSENYMSVEKIADDRIVVYNPSTMSTPMTEYIIKKNDIVRVFNEYGFVLVDNVDFATIIERSKKFINGASTMEDRPSTKNFFELNRGAIKCEGLDVEDLLSYYVVYVFSKR
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Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) methyltransferase. Heterodimeric mRNA capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to the first transcribed nucleotide (cap 0 structure), whereas the methyltransferase OPG102 is responsible for a second methylation at the 2'-O position of the ribose (cap 1 structure). Also involved in early viral gene transcription termination and intermediate viral gene transcription initiation. Early gene transcription termination requires the termination factor VTF, the DNA-dependent ATPase NPH-I/OPG123 and the RAP94/OPG109 subunit of the viral RNA polymerase, as well as the presence of a specific termination motif. Binds, together with RAP94/OPG109, to the termination motif 5'-UUUUUNU-3' in the nascent early mRNA.
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O57311
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ZIC3_XENLA
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Zinc finger protein ZIC 3 (XZic3) (XlZic3) (Zinc finger protein Zic3-A) (Zinc finger protein of the cerebellum 3)
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MTMLLDGGPQFPTLGVGGFGTARHHEMSNRDAGMGLNPFTEPSHAAAFKLSPASHDLSSSQSSAFTPQASGYASSLGHHAGQVPSYGGAAFNSTRDFLFRNRNSGIADSSSAGSQHGLFANHGPPGIGEPPGHLIFPGLHEQSSSHTSSNGHVVNGQMHLGLRGDIFGRPDPYRAVPSPRTDHYAAAQFHNYNHMNMSMNVAAHHGQGAFFRYMRQPIKQELSCKWLEESTMNHPQKTCDRTFSSMHELVTHMTMEHVGGPEQNNHICYWEECPRGGKSFKAKYKLVNHIRVHTGEKPFPCPFPGCGKIFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYICKVCDKSYTHPSSLRKHMKVHESQGSDSSPAASSGYESATPPAMVSANSEEPSKNSSATHQTNNNSHNTGLLPPNFNEWYV
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Probably acts as a transcriptional activator. May bind to the minimal GLI-consensus sequence 5'-GGGTGGTC-3'. Can determine the ectodermal cell fate and promote the earliest step of neural and neural crest development. Involved in establishing left-right asymmetry in the embryo.
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O57314
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DHB12_ANAPL
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Very-long-chain 3-oxoacyl-CoA reductase (EC 1.1.1.330) (17-beta-hydroxysteroid dehydrogenase 12) (17-beta-HSD 12) (3-ketoacyl-CoA reductase) (KAR) (Estradiol 17-beta-dehydrogenase 12) (EC 1.1.1.62)
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MLPAAGLLWWVGALGALYAAVRGALGLLGALRVWGIGAGRAALGPGLGAWAVVTGATDGIGKAYAKELAKRGMKVALISRSKEKLDQVAGEITEQYGVETKVIVADFGEREDIYDRIRAGLEGLEIGVLVNNVGISYSYPEYFIDVPDLDKTIDKMININIMSVCKMTRLVLPGMLERSKGVILNISSAAGMYPTPLLTLYSASKAFVDYFSRGLHAEYKSKGIIVQSVMPYYVATKMSKISKPSFDKPTPETYVRAAIGTVGLQSQTNGCLPHAFMGWVFSILPTSTVMNLLMKTNKQIRARFLKKKMKEK
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Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation.
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O57321
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EAA1_AMBTI
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Excitatory amino acid transporter 1 (SEAAT1) (Sodium-dependent glutamate/aspartate transporter) (GLAST)
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MTKSNGEDPRAGSRMERFQQGVRQRTLLAKKKVQNITKDDVKGFLKRNGFVLFTVIAVVVGSILGFSVRSYHMTFRELKYFSFPGELLMRMLQMLVLPLIVSSLVTGMAALDSKASGKMGLRAVVYYMTTTVIAVFIGIVIVIIVHPGKGTKEHMHREGKIEPVTAADAFLDLIRNMFPPNMVEACFKQFKTSYEKKIFKVTMPANETAVMTSVLNNVSEAMETLTKMREEMIPVPGAVNGVNALGLVVFSMCFGLVIGNMKEQGKALKDFFDSLNEAIMRLVAVIMWYAPIGILFLIAGKIAEMEDMGVVGGQLGMYTVTVIIGLLIHAVIVLPLLYFAVTRKNPWVFIGGILQALITALGTSSSSATLPITFKCLEENNKVDKRVTRFVLPVGATINMDGTALYEALAAIFIAQVNNYDLNFGQILTISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWFLDRLRTTTNVLGDSLGAGIVEHLSRHELQSGDAEMGNSVIEENEMKKPYQLVSQENELEKPIDSETKM
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Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (By similarity).
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O57341
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FGF8A_DANRE
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Fibroblast growth factor 8 (FGF-8)
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MRLIPSRLSYLFLHLFAFCYYAQVTIQSPPNFTQHVSEQSKVTDRVSRRLIRTYQLYSRTSGKHVQVLANKKINAMAEDGDVHAKLIVETDTFGSRVRIKGAETGFYICMNRRGKLIGKKNGLGKDCIFTEIVLENNYTALQNVKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPKGHQIAEHRPFDFINYPFNRRTKRTRYSGER
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Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration (By similarity). Required for Kupffer's vesicle ciliogenesis.
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O57342
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MAFA_COTJA
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Transcription factor MafA (V-maf musculoaponeurotic fibrosarcoma oncogene homolog A)
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MASELAMTAELPTSPLAIEYVNDFDLMKFEVKKEPAEAERLCHRLPAGSLSSTPLSTPCSSVPSSPSFCAPSPGGQPSAGPTAAPLGSKPQLEELYWMSGYQHHLNPEALNLTPEDAVEALIGAPHHHHHHHQSYESFRPQPFGGEELPPAAHHHNAHHHHHHHHLRLEERFSDDQLVSMSVRELNRQLRGFSKEEVIRLKQKRRTLKNRGYAQSCRYKRVQQRHILENEKCQLQSQVEQLKQEVSRLAKERDLYKEKYEKLAARGFPRETSPPAAPKTTAADFFM
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Transcription factor involved in transcription regulation during lens development, including that of crystallin genes. Binds to CRE-type MARE 5'-TGCTGACGTCAGCA-3' and TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequences.
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O57383
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DPOLB_XENLA
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DNA polymerase beta (EC 2.7.7.7) (5'-deoxyribose-phosphate lyase) (5'-dRP lyase) (EC 4.2.99.-) (AP lyase) (EC 4.2.99.18)
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MSKRKAPQESPNEGITDFLVELANYERNVNRAIHKYNAYRKAASVIAKYPTKIKSGTEAKKLDGVGAKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPAAARKFFDEGIKTLDDLRNNEHKLNHHQKIGLKHFDDFEKRIPRKEMLQMQEIILDKVNNLDPEYIATVCGSFRRGAESSGDMDILLTHPDFTSESAKQPRLLHQVVQCLEDCNFITDTLVKGDTKFMGVCQLPCESDQDYPYRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRTHALEKGFTLNEYTLRPLGVTGIAGEPLPIDSEKDIFDYIQWKYREPKDRSE
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Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase) through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase.
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O57385
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PA2H_DEIAC
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Basic phospholipase A2 homolog acutohaemolysin (svPLA2 homolog) (Dac-K49)
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MRALWIVAVLLVGVEGSLFELGKMIWQETGKNPVKNYGLYGCNCGVGGRGEPLDATDRCCFVHKCCYKKLTDCDSKKDRYSYKWKNKAIVCGKNQPCMQEMCECDKAFAICLRENLDTYNKSFRYHLKPSCKKTSEQC
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Snake venom phospholipase A2 homolog that lacks enzymatic activity. Is myotoxic (By similarity). Has a strong indirect hemolytic activity and anticoagulant activity. A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer (By similarity). This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane-disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers (By similarity). The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups (By similarity). Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues (By similarity). This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death (By similarity).
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O57413
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VM2T3_PROMU
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Zinc metalloproteinase/disintegrin [Cleaved into: Snake venom metalloproteinase TM-3 (SVMP) (EC 3.4.24.-) (Atrolysin e) (Fibrinlysin) (Trimutase); Disintegrin trimucrin]
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MIEVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVSALPKGAVQPKYEDAMQYEFKVNGEAVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIHNDADSTASISACDGLKGYFKLQGETYPIEPLELSDSEAHAVFKYENVEKEDEAPKMCGVTQNWESDESIKKASQLYLTPEQQRFPQRYIKLAIVVDHGMYTKYSSNFKKIRKRVHQMVSNINEMCRPLNIAITLALLDVWSEKDFITVQADAPTTAGLFGDWRERVLLKKKNHDHAQLLTDTNFARNTIGWAYVGRMCDEKYSVAVVKDHSSKVFMVAVTMTHELGHNLGMEHDDKDKCKCDTCIMSAVISDKQSKLFSDCSKDYYQTFLTNDNPQCILNAPLRTDTVSTPVSGNEFLEAGEECDCGSPENPCCDAATCKLRPGAQCAEGLCCDQCRFKKKRTICRRARGDNPDDRCTGQSADCPRNGLYG
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[Snake venom metalloproteinase TM-3]: Potent fibrinogenolytic protease which cleaves mainly the Aalpha chain of fibrinogen (FGA) and slightly the Bbeta (FGB) and the gamma (FGG) chains. May possess hemorrhagic activity. Compared to other SVMP, the substrate-binding pocket is relatively shallow. Is less susceptible to tripeptide inhibitors than TM-1 (AC U3KRG1) and TM-2. [Disintegrin trimucrin]: Inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3).
|
O57437
|
DAZLA_XENLA
|
Deleted in azoospermia-like-A (DAZ-like protein A) (xDazl-A)
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MSGKEESSNYAATAEEEAVNQGFVLPEGEIMPNTVFVGGIDITMDEIEIRDFFTRFGNVKEVKIITDRTGVSKGYGFISFSDEVDVQKIVKSQISFHGKKLKLGPAIRKICTYVQPRPVVLSHPTPFHHAWNNQNADSYIQHSPIVSPITQYVQACPYPSSPPMAIQQIPVGCQQPGYFQVSPQWPADQRSYMFPTPAFTFNYHCCDMDPNGGEPIPREYPIDQTVSASGANPQKRYVEMSTQTIVSCLFDPANKFHSFVSQEDYLKDNRVHHLRRRESVIKRVSK
|
RNA-binding protein that is required for primordial germ cell (PGC) differentiation and indirectly necessary for the migration of PGCs through the endoderm. May promote meiotic cell division during spermatogenesis. Shows a preference for G- and U-rich RNAs and probably binds the 3'-UTR of target mRNAs. Stimulates the initiation of translation of mRNAs through the recruitment of poly(A)-binding proteins (PABPs).
|
O57460
|
TLL1_DANRE
|
Dorsal-ventral patterning tolloid-like protein 1 (EC 3.4.24.-) (Mini fin protein)
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MDYLYSALTSKMNWIALLLAGLTFCCKVSVHSCLDYDDSYDYYEEEKTETIDYKDPCKAAVFWGDIALDDEDLKMFHIDGTIDLKQQTHGRQGHTSGGLGEHVPTKKRGSLYLLLDRIRRLGFESWPVNSSKDVSSIKTGIRRVNSARNVKSRVPRAATSRAEKIWPGGVIPYVIGGNFTGSQRAMLKQAMRHWEKQTCVTFIEKTDEESYIVFTYRPCGCCSYVGRRGNGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRDNIQPGQEYNFIKMEPGDVNSLGEPYDFDSIMHYARNTFSRGMFLDTILPSRDENGVRPAIGQRTRLSKGDISQAKKLYRCPACGETLQDSVGNFSSPGYPNGYPSYTHCVWRISVTPGEKIVLNFTTMDLYKSSLCWYDYIEVRDGYWRKAPLLGRFCGDKIPEVLVSTDSRMWIEFRSSSNWVGKGFAAVYEAICGGEISKDSGQIQSPNYPDDYRPSKECVWRITVSEGYSVGLSFQVFEIERHDSCAYDYLEVRDGLSENSPLIGRFCGYDKPEDIRSTSNNLWMKFVSDGTVNKAGFAANFFKEEDECLKPDNGGCEQRCVNTLGSFKCACDPGYELAPDKKSCEAACGGLLTKLNGTITTPGWPKEYPPNKNCVWQVVAPTQYRISMQFEAFELEGNEVCKYDYVEVRSGLSSDSKLHGKYCGTEVPEVITSQYNNMRIEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQHECINTIGSYVCQCRNGFILHENKHDCKEAECEHKIHSTTGTISSPNWPDKYPSRKECTWDITATPGHRVKISFNEFEIEQHQECAYDHLEAFDGDSDKTPILSRLCGNKIPEPLISTGNKMYLRFISDASVQRKGFQATHSTECGGRLKAEARQKNLYSHAQFGDNNYPGHTDCEWLIVAESGYGIELTFTTFEVEEEADCGYDYIELYDGYDTGAHKIGRFCGSGPREELYSAGDAVLIHFHSDDTISKKGFHIRYTSTKFQEALHTRK
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Required for patterning ventral tissues of the tail. May increase bone morphogenetic protein (BMP) activity at the end of gastrulation by proteolytic cleavage of chordin and release of BMP from inactive complexes.
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O57472
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CHRD_DANRE
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Chordin (Protein chordino)
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MMEGLLWILLSVIIASVHGSRLKTPALPIQPEREPMISKGLSGCSFGGRFYSLEDTWHPDLGEPFGVMHCVMCHCEPQRSRRGKVFGKVSCRNMKQDCPDPTCDDPVLLPGHCCKTCPKGDSGRKEVESLFDFFQEKDDDLHKSYNDRSYISSEDTSTRDSTTTDFVALLTGVTDSWLPSSSGVARARFTLSRTSLTFSITFQRINRPSLIAFLDTDGNTAFEFRVPQADNDMICGIWKNVPKPHMRQLEAEQLHVSMTTADNRKEELQGRIIKHRALFAETFSAILTSDEVHSGMGGIAMLTLSDTENNLHFILIMQGLVPPGSSKVPVRVKLQYRQHLLREIRANITADDSDFAEVLADLNSRELFWLSRGQLQISVQTEGQTLRHISGFISGRRSCDTLQSVLSSGAALTAGQTGGVGSAVFTLHPNGSLDYQLLVAGLSSAVLSVSIEMKPRRRNKRSVLYELSAVFTDQRAAGSCGRVEARHTHMLLQNELFINIATALQPDGELRGQIRLLPYNGLDARRNELPVPLAGVLVSPPVRTGAAGHAWVSVDPQCHLHYEIIVNGLSKSEDASISAHLHGLAEIGEMDDSSTNHKRLLTGFYGQQAQGVLKDISVELLRHLNEGTAYLQVSTKMNPRGEIRGRIHVPNHCESPAPRAEFLEEPEFEDLLFTREPTELRKDTHTHVHSCFFEGEQHTHGSQWTPQYNTCFTCTCQKKTVICDPVMCPTLSCTHTVQPEDQCCPICEEKKESKETAAVEKVEENPEGCYFEGDQKMHAPGTTWHPFVPPFGYIKCAVCTCKGSTGEVHCEKVTCPPLTCSRPIRRNPSDCCKECPPEETPPLEDEEMMQADGTRLCKFGKNYYQNSEHWHPSVPLVGEMKCITCWCDHGVTKCQRKQCPLLSCRNPIRTEGKCCPECIEDFMEKEEMAKMAEKKKSWRH
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Dorsalizing factor. Key developmental protein that dorsalizes early vertebrate embryonic tissues by binding to ventralizing TGF-beta family bone morphogenetic proteins (BMPs) and sequestering them in latent complexes (By similarity). {ECO:0000250, ECO:0000269|PubMed:9441687}.
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O57473
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WEE2B_XENLA
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Wee1-like protein kinase 2-B (EC 2.7.10.2) (Wee1-like protein kinase 1) (Xe-wee1)
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MRMAMSCGGRLVQRLDFSSSEEEDGLSNRINEAPQKGSPVSSWRTNNCPFPITPQRNERGLSPTQELSPSSDYSPDPSDKGVGGECPGTPLHYSTWKKLKLCDTPYTPKSLLYKTLPSPGSRVHCRGQRLLRFVAGTGAETEDPTLVNVNPFTPQSYRQTHFQPNGKRKERPEDDCSSDSQMKFTDKEHPAVFQSKRFVLRETNMESRYKTEFLEIEKIGAGEFGSVFKCVKRLDGCFYVIKRSKKPLAGSTDEQLALREVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYCNGGSLQDLIMENNKKGQFVPEQELKEILLQVSMGLKYIHGSGLVHMDIKPSNIFICRKQTEVGEDESDGEDDVASASVLYKIGDLGHVTSILNPQVEEGDSRFLANEILQEDYRQLPKADIFALGLTIALAAGAAPLPCNEDGWHHIRKGNLPHIPQPLTPAFLALLKLLVHPDPATRPPATSLAKNSVLRRCVGKAAELQKQLNVEKFKTAMLERELQAAKLAQDECLDLPPVSGFSCRGRKRLVGAKNARSLSFTCGGY
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Oocyte and early embryo-specific protein tyrosine kinase that phosphorylates and inhibits cdk1 and acts as a regulator of meiosis in oocytes. Required to ensure the meiotic cell cycle in oocytes by phosphorylating cdk1 at 'Tyr-15', leading to inhibit cdk1 activity and prevent meiosis.
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O57474
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CXA1_DANRE
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Gap junction alpha-1 protein (Connexin-43) (Cx43) (Short fin protein)
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MGDWSALGRLLDKVQAYSTAGGKVWLSVLFIFRILVLGTAVESAWGDEQSAFKCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSTPTLLYLAHVFYLMRKEEKLNRKEEELKAVQNDGGDVELHLKKIELKKFKHGLEEHGKVKMKGSLLRTYIFSIIFKSICEVVFLVIQWYLYGFSLSAVYTCERTPCPHRVDCFLSRPTEKTIFIIFMLVVSLFSLLLNIIELFYVLFKRIKDRVKSRQNTQFPTGTLSPTPKELSTTKYAYYNGCSSPTAPLSPMSPPGYKLATGERTNSCRNYNKQANEQNWANYSTEQNRLGQNGSTISNSHAQAFDYPDDTHEHKKLTPGHELQPLALIDARPCSRASSRMSSRARPDDLDV
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One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Plays an essential role in gap junction communication in the ventricles (By similarity).
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O57479
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G3P_COLLI
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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-)
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MVKVGVNGFGRIGRLVTRAAILSAKVQVVAINDPFIDLNYMVYMFKYDSTHGHFRGTVKAENGKLVINGNAITIFQERDPSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILAYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEYGYSNRVVDLMVHMASKE
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Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
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O57521
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HS90B_DANRE
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Heat shock protein HSP 90-beta
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MPEEMRQEEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELVSNASDALDKIRYESLTDPTKLDSGKDLKIDIIPNVQERTLTLIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVKVDHGEPIGRGTKVILHLKEDQTEYIEEKRVKEVVKKHSQFIGYPITLYVEKERDKEISDDEAEEEKAEKEEKEEEGEDKPKIEDVGSDDEEDTKDKDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDISNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFAELAEDKDNYKKFYDAFSKNLKLGIHEDSQNRKKLSELLRYQSSQSGDEMTSLTEYVSRMKENQKSIYYITGESKDQVAHSAFVERVCKRGFEVLYMTEPIDEYCVQQLKDFDGKSLVSVTKEGLELPEDEDEKKKMEEDKAKFENLCKLMKEILDKKVEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIMETLRQKAEADKNDKAVKDLVILLFETALLSSGFSLDDPQTHSNRIYRMIKLGLGIDEDEDVPVEEPSSAAAPEDIPPLEGDDDASRMEEVD
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Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (By similarity). Not required for myofibril formation in skeletal muscles.
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O57526
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IF23B_XENLA
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Insulin-like growth factor 2 mRNA-binding protein 3-B (IGF2 mRNA-binding protein 3-B) (IMP-3-B) (69 kDa RNA-binding protein B) (B3.65 protein B) (IGF-II mRNA-binding protein 3-B) (KH domain-containing transcription factor B3-B) (RNA-binding protein Vera-B) (Trans-acting factor B3-B) (VICKZ family member 3-B) (VLE-binding protein B) (Vg1 RNA-binding protein B) (Vg1 RBP-B) (Vg1 localization element binding protein B) (VgLE-binding and ER association protein B)
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MNKLYIGNLSENVSPPDLESLFKESKIPFTGQFLVKSGYAFVDCPDETWAMKAIDTLSGKVELHGKVIEVEHSVPKRQRSRKLQIRNIPPHLQWEVLDSLLAQYGTVENCEQVNTDSETAVVNVTYANKEHARQGLEKLNGYQLENYSLKVTYIPDEMATPQSPSQQLQQPQQQHPQGRRGFGQRGPARQGSPGAAARPKPQSEVPLRMLVPTQFVGAIIGKEGATIRNITKQTQSKIDIHRKENAGAAEKPITIHSTPEGCSAACKIIMEIMQKEAQDTKFTEEIPLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITISPLQDLTLYNPERTITVKGSIETCAKAEEEVMKKIRESYENDIAAMNLQAHLIPGLNLNALGLFPPSSSGMPPPSAGVSSPTTSASYPPFGQQPESETVHLFIPALAVGAIIGKQGQHIKQLSRFAGASIKIAPAEGPDAKLRMVIITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLEAHIKVPSYAAGRVIGKGGKTVNELQNLTSAEVVVPRDQTPDENDQVVVKITGHFYASQLAQRKIQEILAQVRRQQQQQQKTAQSGQPQPRRK
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RNA-binding protein that acts as a regulator of mRNA transport and localization. Binds to the RNA sequence motif 5'-UUCAC-3'. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Mediates the specific association of Vg1 RNA to microtubules. May regulate mRNA translation (By similarity). Binds specifically to the vegetal localization elements (VLE or VgLE) in the 3'-UTR of Vg1 and VegT mRNAs. Binds to the Vg1 and VegT mRNAs in both the nucleus and the cytoplasm. May regulate mRNA translation (By similarity). Acts as a transcription regulator. Binds to the 5'-[TA]GGTTACT-3' motif within element 3 of the TFIIIA gene promoter.
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O57539
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NCOA3_XENLA
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Nuclear receptor coactivator 3 (EC 2.3.1.48) (Retinoid X receptor-interacting coactivator xSRC-3)
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MSGLGENSLDPLASETRKRKPSSCDTPGPGLTCSGEKRRREQESKYIEELADLISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKASSNDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLYVVNREGSIVFVSENVTQYLQYKQEDLVNTSVYSILHEEDRKDFLKNLPKSTVNGVPWFSETPRQKSHTFNCRMLVKTSHDHLEDGSNLDARQRYETMQCFALSQPRAMIEEGEDLQSCMICVARRITTAERAFSANPESFITRHDLTGKVVNIDANSLRSSMRPGFEDTIRRCIQRFLFHSEGQPWTYKRHYQEAYVHGLSETPLYRFSLADGTMVTAQTKSKLFRNPVTNDPHGFVSTHFLQREQNGYRPNPNPMAQGIRPQMNPNLPNTMNSMPPQAMQQQNRNYGMGDPNSMAQMQGMRYKSPGNMAPVNQAPGVQQSPYQNNSNYGLNMNSPPHGSPGMNANQPNLMVSPRNRASPKMASNQFSPVPGMNSPMGSSGNAGGGSFSSSSLSALHAISEGVGSSLLSSLSSPGQKVENNSNMNMPQQGKICNQDCKSPSGLYCEQGQVESSVCQSSGREHLGEKDVKENIFEGSESQRSQAESKGHKKLLQLLTCFTEERGQSLMSSSSMDCKDSSNVTSPSGVSSSTSIGVSSTSNLHGSMLQEKHRILHKLLQNGNSPAEVAKITAEATGKDVFQETVSSAPCTEATVKREQLSPKKKENNALLRHLLDKDDWKDPLAKDIKPKVEHMDIKMGSCSSSNVPTSSQDKEVKIKTEPGEEVPGDLDNLDAILGDLAGSDFYSNSMSSRASDLGPKQPVFQDSPTLAMRSPDSMQGSRPPFNRAMSLDSRSSTPPVRNVNSFPMLPKQGMIGSPRMMDGQDNFGVMMGSGPNRSMNQHPGGDWAMQNSAVNRLEPPNVGSVGRPGPDYSSAMTRPAMGGNMPGLLTRSNSIPGSRPVMQQQQHILPMRPNDMAMSMGSNPYGQQAPSNPPGSWPDAIMMNQGRGGAQNRQLGRNSLDDLLCPPSTVEGQTDEIALLDQLHTLLSNTDATGLEEIDRALGIPDLVSQGQALEPQPDSYQPQGSPVMIDQKPPMYGQHYAGQGAAMSAGGFNNMQGQHPPFNTVMGQMNQQQGMHPLQGMHPRANLIRPRNNIPKQLRMQLQQRLQGQQFLNQNRQALEMKVDPMNPGGAGVMRPVMQTPVSQQGFLNAQMVAQKNRELISHQIRQHRMAMMMQQQQGQPQAFSPPPNVTASASMDNPLGGPPMPQAPPQQFSYPPNYGINQQTDPTFGRVSSPPNAMMSSRMAPSQNPHPQTTQMYPSPDMKGWPSGNMARPNSFPQQQYSHQTNPATYNMMHMNGNGNHMGQMNINSLPMSGMPMGPDQKYC
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Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as retinoids (RAR and RXR), thyroid hormone (TR) and orphan nuclear receptor (hepatocyte nuclear receptor 4 (HNF4) and constitutive androstane receptor (CAR)). Displays histone acetyltransferase activity.
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O57579
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AMPN_CHICK
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Aminopeptidase Ey (EC 3.4.11.20) (Aminopeptidase N)
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MAAGFFISKSVGIVGIVLALGAVATIIALSVVYAQEKNKSSGGSGGSDTTSTTTASTTTTSTTTASTTAAPNNPWNRWRLPTALKPESYEVTLQPFLTPDDNNMYIFKGNSSVVFLCEEATDLILIHSNKLNYTLQGGFHASLHAVNGSTPPTISNTWLETNTQYLVLQLAGPLQQGQHYRLFSIFTGELADDLAGFYRSEYTEGNVTKVVATTQMQAPDARKAFPCFDEPAMKAVFTVTMIHPSDHTAISNMPVHSTYQLQMDGQSWNVTQFDPTPRMSTYLLAFIVSQFDYVENNTGKVQIRIWGRPAAIAEGQGEYALEKTGPILSFFERHYNTAYPLPKSDQVGLPDFNAGAMENWGLVTYRENSLLYDNAYSSIGNKERVVTVIAHELAHQWFGNLVTLRWWNDLWLNEGFASYVEYLGADSAEPTWDIKDLMVLNELYTVMATDALTTSHPLTFREDEINTPAQISEVFDSIAYSKGASVLRMLSDFLTEDVFKEGLQSYLHDFSYNNTVYTDLWDHLQEAVNKNSVPLPDSIGAIMDRWTLQMGFPVVTVNTLTGSVQQSHFLLDSNSTVERPSVFNYTWIVPITWMTPSRTGDRYWLVDVSATNSDFSVGSSTWLLLNLNVSGYFRVNYNQENWDQLLQQLSNNHQAIPVINRAQIIDDAFNLARAQQVSVTLALNTTRFLSGETAYMPWQAALNNLQYFQLMFDRSEVFGAMTKYIQKQVTPLFEYYRTATNNWTAIPSALMDQYNEINAISTACSYGIAECQQLATALYQQWRQNVSNNPIAPNLRSAIYCSAVATGGEEVWDFIWERFLEAPVVSEADKLRTALTCSTETWILQRYLQYTIDPTKIRKQDATSTINSIASNVVGQPLAWDFIRSNWRTLFGQYGGGSFSFSRLISAVTQRFNTEFELKQLEQFKADNQDIGFGSGTRALEQALERTRTNINWVKENKEVVHAWFRAETASS
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Broad specificity aminopeptidase. Degrades a variety of peptides possessing various N-terminal amino acids including hydrophobic, basic and acidic amino acids. Preferentially hydrolyzes small peptides consisting of 4 or 5 amino acids. Hydrolyzes the N-terminal Xaa-Pro bonds in the chicken brain peptide Leu-Pro-Leu-Arg-PheNH2, the substance P fragment Arg-Pro-Lys-Pro and the bradykinin fragment Arg-Pro-Pro-Gly-Phe. Hydrolyzes the N-formylated peptides fMet-Leu-Phe, fMet-Ala-Gly-Ser-Glu and fMet-Nle-Leu-Phe-Nle-Tyr-Lys, but does not hydrolyze peptides with acetylation or pyroglutamic acid at N-terminus. Does not hydrolyze large peptides such as complete substance P, bradykinin or schistoFLRFamide.
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O57598
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ATOH7_CHICK
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Transcription factor ATOH7 (Atonal bHLH transcription factor 7) (Helix-loop-helix protein cATH-5) (cATH5) (Protein atonal homolog 5) (Protein atonal homolog 7)
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MKTCQSSHLDSGVESDIQCRSGSGCVVKCSTERMESAAKRRLAANARERRRMQGLNTAFDRLRKVVPQWGQDKKLSKYETLQMALSYIMALTRILAEAERYSTEREWINLHCEHFHPESYHHYTGQKVATDSDPYAQRIFSYHPEHFQIAN
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Transcription factor that binds to DNA at the consensus sequence 5'-CAG[GC]TG-3' (By similarity). Positively regulates the determination of retinal ganglion cell fate and formation of the optic nerve and retino-hypothalamic tract. Required for retinal circadian rhythm photoentrainment (By similarity). Plays a role in brainstem auditory signaling and binaural processing (By similarity). During retinal neurogenesis, activates its own transcription, as well as the transcription of CHRNB3 and BRN3.
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O57604
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PODXL_CHICK
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Podocalyxin (Podocalyxin-like protein 1) (PC) (PCLP-1) (Thrombomucin)
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MRAPLLLPLLPLLLFGVSSGNNDKTTHSTTVSPETTKQITTITVTTSQVQGSISASKPSSTAPTAVMSFTKAQEAATSSKQHDSSTSSIPPPSTSITPSIITTSPQGKTPSTPALTHTPDQNTKTTGRQDDTSHVSVASTSASQQVSSSASAAVPTTTSAVTSSATQQKVSPTDSSEILLKPSASPNSTQVTSPSRTPKGFLSTVTTSPHIADNGSTALNQLKSTVSSSEVPVSSFLDKDHSVSSSTSATNQHLSLSSHRPTSPVPKFECSTPHSGSVPSTSSKTSLSSPSSSTKNATVTTTMTTAKAAYTSQGDGSVTHKSGVTAQSPTSAPLPTPTLKDHMKSKSPDQTHSNVSPPNEVICEDQIGEVRPILNLKEEKTCDDWKKASNEAFFEVFCSGRRHAFNSTRDRCTVKLASSNHRRWAVHVIVHRVLDPAAVFEELKEKRNELEKLGITNVTYLNQEMEEEIKDQSSTPLIITIVTLAGSLLLIAAIYGCCHQRFSQKKSQQRLTEELQTMENGYHDNPTLEVMETGSEMQEKKVNLNGELGDSWIVPLDTIMKEDLEEEDTHL
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Involved in the regulation of both adhesion and cell morphology and cancer progression. Functions as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Involved in the formation of a preapical plasma membrane subdomain to set up initial epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells (By similarity). Induces the formation of apical actin-dependent microvilli. {ECO:0000250, ECO:0000269|PubMed:17311105}.
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O57672
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G3P_MELGA
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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-)
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AEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDKSLKIVSNALCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPFGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFHVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYSNRVV
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Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
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O57693
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GAPN_THETE
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NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.90) (Glyceraldehyde phosphate dehydrogenase (NAD(P))) (GAPN)
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MRAGLLEGVIKEKGGVPVYPSYLAGEWGGSGQEIEVKSPIDLATIAKVISPSREEVERTLDVLFKRGRWSARDMPGTERLAVLRKAADIIERNLDVFAEVLVMNAGKPKSAAVGEVKAAVDRLRLAELDLKKIGGDYIPGDWTYDTLETEGLVRREPLGVVAAITPFNYPLFDAVNKITYSFIYGNAVVVKPSISDPLPAAMAVKALLDAGFPPDAIALLNLPGKEAEKIVADDRVAAVSFTGSTEVGERVVKVGGVKQYVMELGGGDPAIVLEDADLDLAADKIARGIYSYAGQRCDAIKLVLAERPVYGKLVEEVAKRLSSLRVGDPRDPTVDVGPLISPSAVDEMMAAIEDAVEKGGRVLAGGRRLGPTYVQPTLVEAPADRVKDMVLYKREVFAPVASAVEVKDLDQAIELANGRPYGLDAAVFGRDVVKIRRAVRLLEVGAIYINDMPRHGIGYYPFGGRKKSGVFREGIGYAVEAVTAYKTIVFNYKGKGVWKYE
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Catalyzes the irreversible NAD(P)-dependent non-phosphorylating oxidation of glyceraldehyde-3-phosphate (GAP) to 3-phosphoglycerate (3PG). It is highly specific for D-GAP.
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O57712
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NSUN6_PYRHO
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tRNA (cytosine(72)-C(5))-methyltransferase (tRNA:m(5)C72 MTase) (EC 2.1.1.-) (PhNSun6)
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MAMNYLEAFPKELREYYKNLFGKEEANKIMKKLREPVEHYYIRVNTLKISREKLIGELKKEGLKPLRSPYLPEGLYFVREGPNFSDDFEPKLPVVVANKYAAESVYQGAMLYAPGVLKADKNIKEGDEVQIRDPKGLLVGIGIARMDYKEMTEATRGLAVEVTLPKFKLPSLSELKAFEKGYFYPQGLPSMVTARVLEPKEDDVIIDMAAAPGGKTTHIAQLLENKGEIIAIDKSKNRLRKMEENIKRLGVKNVKLVQMDARKLPDLGIKADKILLDAPCTALGVRPKLWEERTLKHIEATARYQRAFIWAAIKSLRRGGVLVYSTCTLSYEENEGNVKFMIRKGMKLEEQSIFIGSPGIGMNKVQRFYPHKHLTQGFFIAKLRKVKDI
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S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C5 position of cytosine 72 in several tRNAs. This modification appears to slightly promote the thermal stability of P.horikoshii tRNAs, but does not affect their amino acid accepting activity. Four elements in the acceptor stems of tRNAs are essential for substrate recognition by this enzyme: the target site C72, the 3'-CCA terminus, U73 or G73, and the second base pair C2:G71.
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O57767
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NADA_PYRHO
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Quinolinate synthase (QS) (EC 2.5.1.72)
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MDLVEEILRLKEERNAIILAHNYQLPEVQDIADFIGDSLELARRATRVDADVIVFAGVDFMAETAKILNPDKVVLIPSREATCAMANMLKVEHILEAKRKYPNAPVVLYVNSTAEAKAYADVTVTSANAVEVVKKLDSDVVIFGPDKNLAHYVAKMTGKKIIPVPSKGHCYVHQKFTLDDVERAKKLHPNAKLMIHPECIPEVQEKADIIASTGGMIKRACEWDEWVVFTEREMVYRLRKLYPQKKFYPAREDAFCIGMKAITLKNIYESLKDMKYKVEVPEEIARKARKAIERMLEMSK
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Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:15937336, ECO:0000269|PubMed:27224840}.
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O57878
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BARAC_PYRHO
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Broad substrate specificity amino-acid racemase (BAR) (EC 5.1.1.10)
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MVSMTKWDEIRKYTSKKIEKNLEIVKLDEKYIPRASGFKYYPMVIERSSGSRIWDKDGNEYIDFLTSAAVFNVGHTHPGVVKAVEEQIKKFFNYTMGYLYVEPPVRLAELLVEITPGNFEKKVTYGFSGSDAVDSSIKAARAYTKRVNIISFLHSYHGMTYGALSATGILDPKLKKLLHPMGNFHHVEFPDPYRNSWGIDGYEDPSELANRALDEIERKIKELNEDVAGIIIEPIQGDAGVVIPPEEFVRDLKKLTEEYGIVFIDEEVQTGMGRTGRWWGIEHFGVTPDLIVSAKALGGGMPISAVVGKAEIMDSVPVPFFVFTHIGHAVNASAAIATINVIKEEKLVERSEKLGEYMLKRLRELQETYPIIGDVRGKGLLIGVDIVKEGTREPDRSLAQKISWRAWEKGLIMITFGKHGNVLRIAPPLNIPQEDLDKGVEIIEESIKDAVEGKIPDEVLKFLRAW
|
Amino-acid racemase able to utilize a broad range of substrates. Can use Met, Leu, Phe, Ala, Ser, Ile, Val, Trp, Tyr and Thr. Is mostly active with Phe, Leu, Met and Tyr, followed by Ile, Thr and Trp. Has weaker activity with Val, Ser and Ala. Shows no activity toward Pro, Asp, Glu, Arg, His, Gln and Asn.
|
O58038
|
TTUA_PYRHO
|
tRNA-5-methyluridine(54) 2-sulfurtransferase (EC 2.8.1.-) (tRNA thiouridine synthetase TtuA)
|
MKCKFCSREAYIKIHYPKMYLCEEHFKEYFERKVSRTIERYKLLTKDERILVAVSGGKDSAVTAYVLKKLGYNIECLHINLGISGYSEKSEEYAKKQCKLIGAPLHIVRIKEILGYGIGEVKTRRPPCSYCGLTKRYIMNKFAYDNGFDAIATGHNLDDEASFLLNNILHWNTEYLAKGGPILPQQGKFIKKVKPLYEVTEREVVAYALAVGLEYIVEECPYARGATTLDMKGVLNELEEKRPGTKFNFVRGYLKKKKLFEPEIKEKEIKECKICRMPSSGDICAFCKFWGLKKEINFKVSSTDEEPFGP
|
Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is required for cell growth at high temperatures (By similarity). Can use free sulfide as sulfur source in vitro, which may be also the sulfur source in vivo.
|
O58308
|
NCPPR_PYRHO
|
NAD(P)H coenzyme A polysulfide/persulfide reductase (EC 1.8.1.-) (Coenzyme A disulfide reductase) (CoA-disulfide reductase) (CoADR) (EC 1.8.1.14) (Polysulfide reductase)
|
MGENMKKKVVIIGGGAAGMSAASRVKRLKPEWDVKVFEATEWVSHAPCGIPYVVEGLSTPDKLMYYPPEVFIKKRGIDLHLNAEVIEVDTGYVRVRENGGEKSYEWDYLVFANGASPQVPAIEGVNLKGVFTADLPPDALAIREYMEKYKVENVVIIGGGYIGIEMAEAFAAQGKNVTMIVRGERVLRRSFDKEVTDILEEKLKKHVNLRLQEITMKIEGEERVEKVVTDAGEYKAELVILATGIKPNIELAKQLGVRIGETGAIWTNEKMQTSVENVYAAGDVAETRHVITGRRVWVPLAPAGNKMGYVAGSNIAGKELHFPGVLGTAVTKFMDVEIGKTGLTEMEALKEGYDVRTAFIKASTRPHYYPGGREIWLKGVVDNETNRLLGVQVVGSDILPRIDTAAAMLMAGFTTKDAFFTDLAYAPPFAPVWDPLIVLARVLKF
|
Catalyzes the NAD(P)H-dependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides. The likely in vivo substrates are di-, poly-, and persulfide derivatives of coenzyme A, although polysulfide itself is also efficiently reduced. Shows coenzyme A disulfide reductase (CoADR) activity with both NADH and NADPH, with a preference for NADPH. May also play a role in the reduction of elemental sulfur.
|
O58328
|
GLKA_PYRHO
|
ADP-dependent glucose/glucosamine kinase (EC 2.7.1.-) (EC 2.7.1.147) (ADP-dependent glucokinase) (ADP-GK) (ADPGK) (Glucosamine kinase) (GlcN kinase)
|
MITMTNWESLYEKALDKVEASIRKVRGVLLAYNTNIDAIKYLKREDLEKRIEKVGKEEVLRYSEELPKEIETIPQLLGSILWSIKRGKAAELLVVSREVREYMRKWGWDELRMGGQVGIMANLLGGVYGIPVIAHVPQLSELQASLFLDGPIYVPTFERGELRLIHPREFRKGEEDCIHYIYEFPRNFKVLDFEAPRENRFIGAADDYNPILYVREEWIERFEEIAKRSELAIISGLHPLTQENHGKPIKLVREHLKILNDLGIRAHLEFAFTPDEVVRLEIVKLLKHFYSVGLNEVELASVVSVMGEKELAERIISKDPADPIAVIEGLLKLIKETGVKRIHFHTYGYYLALTREKGEHVRDALLFSALAAATKAMKGNIEKLSDIREGLAVPIGEQGLEVEKILEKEFSLRDGIGSIEDYQLTFIPTKVVKKPKSTVGIGDTISSSAFVSEFSLH
|
Catalyzes the ADP-dependent phosphorylation of D-glucose to D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000269|PubMed:29784881}.
|
O58389
|
TDH_PYRHO
|
L-threonine 3-dehydrogenase (L-ThrDH) (TDH) (EC 1.1.1.103) (L-threonine dehydrogenase)
|
MSEKMVAIMKTKPGYGAELVEVDVPKPGPGEVLIKVLATSICGTDLHIYEWNEWAQSRIKPPQIMGHEVAGEVVEIGPGVEGIEVGDYVSVETHIVCGKCYACRRGQYHVCQNTKIFGVDTDGVFAEYAVVPAQNIWKNPKSIPPEYATLQEPLGNAVDTVLAGPISGKSVLITGAGPLGLLGIAVAKASGAYPVIVSEPSDFRRELAKKVGADYVINPFEEDVVKEVMDITDGNGVDVFLEFSGAPKALEQGLQAVTPAGRVSLLGLYPGKVTIDFNNLIIFKALTIYGITGRHLWETWYTVSRLLQSGKLNLDPIITHKYKGFDKYEEAFELMRAGKTGKVVFMLK
|
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate. Is much less efficient when using NADP(+) instead of NAD(+). To a lesser extent, also catalyzes the oxidation of L-serine and DL-threo-3-phenylserine, but not that of L-allo-threonine, D-threonine and D-allo-threonine and many other L-amino acids.
|
O58440
|
NOB1_PYRHO
|
Endoribonuclease Nob1 (RNase Nob1) (EC 3.1.-.-) (Endonuclease VapC6) (Putative toxin VapC6)
|
MLRNLKKTLVLDSSVFIQGIDIEGYTTPSVVEEIKDRESKIFLESLISAGKVKIAEPSKESIDRIIQVAKETGEVNELSKADIEVLALAYELKGEIFSDDYNVQNIASLLGLRFRTLKRGIKKVIKWRYVCIGCGRKFSTLPPGGVCPDCGSKVKLIPRKR
|
Toxic component of a type II toxin-antitoxin (TA) system (Potential). Processes pre-16S-rRNA at its 3' end (the D-site) to yield the mature 3' end.
|
O58478
|
ASRAC_PYRHO
|
Alanine/serine racemase (ASR) (Ala/Ser racemase) (EC 5.1.1.-) (EC 5.1.1.1)
|
MPFLPFSYYPFSLEVILMEYPKIVVKPPGPRAKELIEREKKVLSTGIGVKLFPLVPKRGFGPFIEDVDGNVFIDFLAGAAAASTGYAHPKLVKAVKEQVELIQHSMIGYTHSERAIRVAEKLVEISPIENSKVIFGLSGSDAVDMAIKVSKFSTRRPWILAFIGAYHGQTLGATSVASFQVSQKRGYSPLMPNVFWIPYPNPFRNIWGINGYEEPDELINRVLDYLEYYVFSHVVPPDEVAALFAEPIQGDAGIVVPPENFFKELKKLLEEYGILLVMDEVQTGIGRTGKWFASEWFNVKPDMIIFGKGVASGMGLSGVIGRKEIMDITSGSALLTPAANPVISAAAEATLEIIEEENLLKNALEVGEFIMGRLKEIKERFEIIGDVRGKGLMIGVEIVKENGRPDPEMTGKICWRAFELGLILPSYGMFGNVIRITPPLVLTKEVAEKALEIIERAIKDTLTGKVERKVVTWH
|
Catalyzes the interconversion of L-alanine and D-alanine, and L-serine and D-serine. Has weak activity with valine and threonine.
|
O58523
|
TYW2_PYRHO
|
tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase (EC 2.5.1.114) (PhTYW2) (tRNA wyosine derivatives biosynthesis protein Taw2)
|
MRTQGIKPRIREILSKELPEELVKLLPKRWVRIGDVLLLPLRPELEPYKHRIAEVYAEVLGVKTVLRKGHIHGETRKPDYELLYGSDTVTVHVENGIKYKLDVAKIMFSPANVKERVRMAKVAKPDELVVDMFAGIGHLSLPIAVYGKAKVIAIEKDPYTFKFLVENIHLNKVEDRMSAYNMDNRDFPGENIADRILMGYVVRTHEFIPKALSIAKDGAIIHYHNTVPEKLMPREPFETFKRITKEYGYDVEKLNELKIKRYAPGVWHVVLDLRVFKS
|
S-adenosyl-L-methionine-dependent transferase that acts as a component of the wyosine derivatives biosynthesis pathway. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to 4-demethylwyosine (imG-14), forming 7-aminocarboxypropyl-demethylwyosine (wybutosine-86) at position 37 of tRNA(Phe). {ECO:0000255|HAMAP-Rule:MF_01922, ECO:0000269|PubMed:19717466}.
|
O58530
|
RGYR_PYRHO
|
Reverse gyrase [Cleaved into: Pho r-Gyr intein] [Includes: Helicase (EC 3.6.4.12); Topoisomerase (EC 5.6.2.2)]
|
MKAIYRGMCPNCRGAITDERLSNKNPCEGCLSEPILSEDYNELIVAVRNALKLRGTLKDWEELYRLNKEVSEIEELFEKSTGFKFWSAQRTWVKRIIRGKSFSIIAPTGMGKSTFGAFISIYFATKGKKSYIVVPTTPLVIQTVKKIESMLEKANVSVRLVYYHGNLRKKEKEEALEKIRNGDFDILITSSQFLATRFKELLKDKKFDLIFVDDVDAFLKASKNIDRSLIMLGFSEEIIGRAWEVIKLKKQLAKLLQNEKKNEEEIEKLNKEIEKIEDEIEEYKRRNKIGILIVASATGSAKGDRIKLYRELLGFEVGSGRSVLRNIVDTYLLPEKPIEEHVVELLRKLGKGGLIFVPIDKGIEYAEELTDYLKSQGFKVELVSAKNKKGLELFEKGEIDYLVGVATYYGTLVRGLDLPHLIRFAIFTGVPKFRFSMDLEQPTIYRVLGLMSEILEFLPEEKKSEGEKLYARLRRLIRNIPQYELMKIEEALAEGLELEGFHNHVLEVFKQSVEFLREVLKDEEVIKKIAENPFLSLKEIEGKLYIEIPDVRTYIQASGRTSRLFAGGITKGLSVIIVDDQKVFNGLIRQMRWRFVEFDIKKFEEVNLKEVLKEIDRDREKVKLVIEGKISEQVKDLVKSALMIVESPNKARTIASFFGQPSKRKIGDLTAYEVSIGDKMLTILASGGHMFDLVTNEGYHGVLILKNNGKPYFVPVYDTIKRCRDCGHQFVDWEQKGVCPRCGSRNVHDALENVKAMRELALEVDEILIGTDPDTEGEKIAWDIRNVLAPYAPNIKRIEFHEVTRPAILRAIREARDINEDRVNAQLVRRIEDRWIGFELSQKLWEVFENRNLSAGRVQTPVLGWIVQRYKEFTESETDFLGIILENGINVTIENAKGEVREVEVKDVIIEEKDVNPLPPYTTDTMLQDASRFLGFSATKTMQLAQDLFEAGLCVTPDTLVSLSDGRIIEIREAVENSEESLLGINGLKPKEAKALKFWEIDWDGPIKVIKLKNGHEIKATPDHGLLVMRDGKIGWVSAKNIREGDYVAFIYNLGHRGGKKYTLPQLLKELGISEYENSSSQELNNREQEMDSKQISIELDERFWYIFGVILGKGTLKGDKVVIFQKDVKPVIEEALPFVRIFESADHIGFSHLILAEVFRRLGVGEGKLHSLVFGLREEYINAMIAGYFDASGTFLRRAVLTSKRGDILRMLSVYLYQIGIVNNLRRDEHAGVWELIISDLEKFREKIYPYLRIKKSQFDKVYSISKNEGDFLPVASIFRKLKFRDGFKNRILDEEIPRDEVAKVLEYAEDSPEKEFLNSLVEARVTWVRVEKIEERHYTGKLYDFTTTTENFISNGIVSHNCTYHRTDSIHVSNTGIEVAKEYITQEIGEEYFTPRKWGEEGAHEAIRPTRPIDTGRLIQLIRDGIITIPKNLTRDHFRLYDLIFRRFMASQMKPAKILYEKAIISTPFKDVEVEGYIDVLYDGWSKIKSLPLRQIPKLEKGQRLRVKEVKQWRAPKVSLYTQGDVIALMKERGIGRPSTYAKIVQTLLQRGYVIETKGKKKLVPTEKGIKVYQYLITKYKDLVSEERTRQLEKIMDMVEEAKADYQDVLNELYEEIKRYVR
|
Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication (By similarity).
|
O58679
|
MFNA_PYRHO
|
L-aspartate/L-glutamate decarboxylase (ADC/GAD) (EC 4.1.1.11) (EC 4.1.1.15) (PhGAD)
|
MKFPRIGLPKEKVIELINEKTKKDLTFSSGKILGSMCTMPHDLAIEVYTKYIDRNLGDPGLHPGTRKIEEEVIEMISDLLHLEKGHGHIVSGGTEANILAVRAFRNLSDVEKPELILPKSAHFSFIKAGEMLGVKLVWAELNPDYTVDVRDVEAKISDNTIGIVGIAGTTGLGVVDDIPALSDLARDYGIPLHVDAAFGGFVIPFAKELGYELPDFDFKLKGVQSITIDPHKMGMAPIPAGGIVFRRKKYLKAISVLAPYLAGGKVWQATITGTRPGASVIAVWALIKHLGFEGYMRIVERAMKLSRWFAEEIKKINNAWLVREPMLNIVSFQTKNLKKVERELKSRGWGISAHRGYIRIVFMPHVTREMIEEFLKDLKEVLS
|
Catalyzes the decarboxylation of L-aspartate to produce beta-alanine, and the decarboxylation of L-glutamate to produce 4-aminobutanoate. Can also use cysteate and, to a lesser extent, cysteine sulfite (3-sulfino-L-alanine), but not L-tyrosine. Specific activities toward L-aspartate and cysteate are higher than toward L-glutamate.
|
O58801
|
NADK_PYRHO
|
NAD kinase (EC 2.7.1.23) (ATP-dependent NAD kinase) (Poly(P)-dependent NAD kinase) (PPNK)
|
MKFGIVARRDKEEALKLAYRVYDFLKVHGYEVVVDKETYEHFPHFKEGDVIPLDEFDVDFIVAIGGDGTILRIEHMTKKDIPILSINMGTLGFLTEVEPSDTFFALNRLIEGEYYIDERIKVRTYIDGENRVPDALNEVAILTGIPGKIIHMKYYVDGGLADEVRADGLVVSTPTGSTGYAMSAGGPFIDPRLDVILIAPLLPLPKTSVPMVIPGSSRIDIRMLTDREIILAIDGQYYEHLPPNVEITVVKSPRKTKFIRFTREIYPKYTIRIKERH
|
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP,UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus. NAD is the preferred substrate for the kinase, but NADH can also be used as phosphoryl acceptor. {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:16085824}.
|
O58832
|
DPH2_PYRHO
|
2-(3-amino-3-carboxypropyl)histidine synthase (EC 2.5.1.108) (Diphthamide biosynthesis protein Dph2) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase)
|
MLHEIPKSEILKELKRIGAKRVLIQSPEGLRREAEELAGFLEENNIEVFLHGEINYGACDPADREAKLVGCDALIHLGHSYMKLPLEVPTIFVPAFARVSVVEALKENIGEIKKLGRKIIVTTTAQHIHQLKEAKEFLESEGFEVSIGRGDSRISWPGQVLGCNYSVAKVRGEGILFIGSGIFHPLGLAVATRKKVLAIDPYTKAFSWIDPERFIRKRWAQIAKAMDAKKFGVIVSIKKGQLRLAEAKRIVKLLKKHGREARLIVMNDVNYHKLEGFPFEAYVVVACPRVPLDDYGAWRKPVLTPKEVEILLGLREEYEFDEILGGPRESDEPFGISIHSTR
|
Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).
|
O58843
|
ATGT_PYRHO
|
tRNA-guanine(15) transglycosylase (EC 2.4.2.48) (7-cyano-7-deazaguanine tRNA-ribosyltransferase) (Archaeal tRNA-guanine transglycosylase)
|
MSRGDKMLKFEIKARDGAGRIGKLEVNGKKIETPAIMPVVNPKQMVVEPKELEKMGFEIIITNSYIIYKDEELRRKALELGIHRMLDYNGIIEVDSGSFQLMKYGSIEVSNREIIEFQHRIGVDIGTFLDIPTPPDAPREQAVKELEITLSRAREAEEIKEIPMNATIQGSTYTDLRRYAARRLSSMNFEIHPIGGVVPLLESYRFRDVVDIVISSKMALRPDRPVHLFGAGHPIVFALAVAMGVDLFDSASYALYAKDDRYMTPEGTKRLDELDYFPCSCPVCSKYTPQELREMPKEERTRLLALHNLWVIKEEIKRVKQAIKEGELWRLVDERARSHPKLYSAYKRLLEHYTFLEEFEPITKKSALFKISNESLRWPVVRRAKERAKSINERFGELVEHPIFGRVSRYLSLTYPFAQSEAEDDFKIEKPTKEDAIKYVMAIAEYQFGEGASRAFDDAKVELSKTGMPRQVKVNGKRLATVRADDGLLTLGIEGAKRLHRVLPYPRMRVVVNKEAEPFARKGKDVFAKFVIFADPGIRPYDEVLVVNENDELLATGQALLSGREMIVFQYGRAVKVRKGVE
|
Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.
|
O58966
|
TDXH_PYRHO
|
Peroxiredoxin (EC 1.11.1.24) (Thioredoxin peroxidase) (Thioredoxin-dependent peroxiredoxin)
|
MVVIGEKFPEVEVKTTHGVIKLPDYFTKQGKWFILFSHPADFTPVCTTEFYGMQKRVEEFRKLGVEPIGLSVDQVFSHIKWIEWIKDNLSVEIDFPVIADDRGELAEKLGMIPSGATITARAVFVVDDKGIIRAIVYYPAEVGRDWDEILRLVKALKISTEKGVALPHKWPNNELIGDKVIVPPASTIEEKKQREEAKAKGEIECYDWWFCYKKLE
|
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. {ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:12944367, ECO:0000269|PubMed:15625325}.
|
O59010
|
GLT_PYRHO
|
Glutamate transporter homolog (Glt(Ph)) (Sodium-aspartate symporter Glt(Ph)) (Sodium-dependent aspartate transporter)
|
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYADAVKTYVKPFGDLFVRLLKMLVMPIVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQFQPKQAPPLVKILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSAETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVKVVGELAKVTAAVYVGLTLQILLVYFVLLKIYGIDPISFIKKAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYSFTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGAIMLAMVLESVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGELEKGVIA
|
Sodium-dependent, high-affinity amino acid transporter that mediates aspartate uptake (PubMed:17435767, PubMed:19380583, PubMed:17230192, Ref.11). Has only very low glutamate transport activity. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions, resulting in electrogenic transport (PubMed:17435767, PubMed:19380583, Ref.11). Na(+) binding enhances the affinity for aspartate (PubMed:19380583, Ref.11). Mediates Cl(-) flux that is not coupled to amino acid transport this avoids the accumulation of negative charges due to aspartate and Na(+) symport. In contrast to mammalian homologs, transport does not depend on pH or K(+) ions.
|
O59179
|
STOPP_PYRHO
|
Membrane-bound protease PH1510 (EC 3.4.21.-) (NfeD homolog) (Stomatin operon partner protein) (STOPP)
|
MRRILLSMIVLIFLASPILAKNIVYVAQIKGQITSYTYDQFDRYITIAEQDNAEAIIIELDTPGGRADAMMNIVQRIQQSKIPVIIYVYPPGASAASAGTYIALGSHLIAMAPGTSIGACRPILGYSQNGSIIEAPPKITNYFIAYIKSLAQESGRNATIAEEFITKDLSLTPEEALKYGVIEVVARDINELLKKSNGMKTKIPVNGRYVTLNFTNVEVRYLAPSFKDKLISYITDPNVAYLLLTLGIWALIIGFLTPGWHVPETVGAIMIILAIIGFGYFGYNSAGILLIIVAMLFFIAEALTPTFGLFTVAGLITFIIGGILLFGGGEEYLVRKEVFSQLRILIITVGAILAAFFAFGMAAVIRAHKKKARTGKEEMIGLIGTVVEELNPEGMIKVRGELWKARSKFNGKIEKGEKVRVVDMDGLTLIVVRERKEGGEK
|
Protease that cleaves its substrates preferentially near hydrophobic or aromatic amino acid residues. Can degrade casein and the stomatin homolog PH1511 (in vitro).
|
O59196
|
TET_PYRHO
|
Tetrahedral aminopeptidase (TET) (TET aminopeptidase) (EC 3.4.11.-) (Leucyl aminopeptidase) (PhTET2)
|
MEVRNMVDYELLKKVVEAPGVSGYEFLGIRDVVIEEIKDYVDEVKVDKLGNVIAHKKGEGPKVMIAAHMDQIGLMVTHIEKNGFLRVAPIGGVDPKTLIAQRFKVWIDKGKFIYGVGASVPPHIQKPEDRKKAPDWDQIFIDIGAESKEEAEDMGVKIGTVITWDGRLERLGKHRFVSIAFDDRIAVYTILEVAKQLKDAKADVYFVATVQEEVGLRGARTSAFGIEPDYGFAIDVTIAADIPGTPEHKQVTHLGKGTAIKIMDRSVICHPTIVRWLEELAKKHEIPYQLEILLGGGTDAGAIHLTKAGVPTGALSVPARYIHSNTEVVDERDVDATVELMTKALENIHELKI
|
Functions as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. However, can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. Has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity. Is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids.
|
O59245
|
RTCB_PYRHO
|
tRNA-splicing ligase RtcB (EC 6.5.1.8) (3'-phosphate/5'-hydroxy nucleic acid ligase) (tRNA ligase RtcB) [Cleaved into: Pho hyp2 intein (EC 3.1.-.-)]
|
MVVPLKRIDKIRWEIPKFDKRMRVPGRVYADEVLLEKMKNDRTLEQATNVAMLPGIYKYSIVMPDGHQGYGFPIGGVAAFDVKEGVISPGGIGYDINCLAPGTRVLTEHGYWLKIEEMPEKFKLQRLRVYNIEEGHNDFSKVVFVAEREVGSEEKAIRIVTESGKVIEGSEDHPVLTPEGYVYLRNVKEGDYILVYPFEGVPYEEKKGVILDESAFEGEDPQVVKFLRERNLIPLQWKDPKVGILARILGFALANGYISENDNLTFHGKEEVLREVRKDLEELGIEAIVAEEDKLKVTSREFAFLLEKLGMAHDSIPEWIIEGPLWIKRNFLAGLFGANGSIVEFKGDVPLPITLTHSRELLNDVSRILEGFKVRAKIKMGKNGSYQLVIEDEDSIRNFLGRINYEYDPEKKARGLIAYAYLKFKELMKGNLMTFEEFARDRGYEGGFVAEKVIEVKSVKPEYDKFYDIGVYHSAHNFIANGIVVHNCGVRLIRTNLTEKEVRPRIKQLVDTLFKNVPSGVGSQGRIKLHWTQIDDVLVDGAKWAVDNGYGWERDLERLEEGGRMEGADPEAVSQRAKQRGAPQLGSLGSGNHFLEVQVVDKIFDPEVAKAYGLFEGQVVVMVHTGSRGLGHQVASDYLRIMERAIRKYRIPWPDRELVSVPFQSEEGQRYFSAMKAAANFAWANRQMITHWVRESFQEVFKQDPEGDLGMDIVYDVAHNIGKVEEHEVDGKRVKVIVHRKGATRAFPPGHEAVPRLYRDVGQPVLIPGSMGTASYILAGTEGAMKETFGSTCHGAGRVLSRKAATRQYRGDRIRQELLNRGIYVRAASMRVVAEEAPGAYKNVDNVVKVVSEAGIAKLVARMRPIGVAKG
|
Essential for tRNA splicing and maturation (Probable). Acts by directly joining spliced tRNA halves to mature-sized tRNAs. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends.
|
O59248
|
RNP4_PYRHO
|
Ribonuclease P protein component 4 (RNase P component 4) (EC 3.1.26.5) (Rpp21)
|
MVDIVKRRDWEKKEKKKIAIERIDTLFTLAERVARYSPDLAKRYVELALEIQKKAKVKIPRKWKRRYCKRCHTFLIPGVNARVRLRTKRMPHVVITCLECGYIMRYPYLREVKQKRKKAT
|
Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Binds RNase P RNA. {ECO:0000255|HAMAP-Rule:MF_00757, ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16142906, ECO:0000269|PubMed:16574071, ECO:0000269|PubMed:16829535, ECO:0000269|PubMed:18929577}.
|
O59272
|
D89S1_PYRHO
|
Damage-control phosphatase PH1575 (EC 3.1.3.-) (Nucleotides phosphatase PH1575)
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MKVQYECLTCMANQCQRIVEMATQDMDIRRRAMILAAKLLAKEYNENAIPAIAGSLIFLELYKFLGNDDPFIEYKLKSEEMARKVADIIKRKLKLDFELAVKLAIIGNVIDFSVGFSPEDLEEEVEKMLKDKLYIDDSKELFEEVKRAENILYITDNVGEHYFDAILIEKIREISNAEVYIAGKEGPIINDATVEDLKRAGLEKLGKVISTGTRIVGVPLKLVSREFMEAFNKADVIIAKGQGNFETLSEINDSRIFFLLKAKCPAVARELKVPKGALVCMRNKFKL
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Metal-dependent phosphatase with probable damage-control functions. Shows phosphatase activity against p-nitrophenyl phosphate (pNPP), but natural substrates have not been identified yet. Low phosphatase activity against 8-oxo nucleotides suggests that it could hydrolyze oxidatively damaged purine nucleotides or their biosynthetic intermediates.
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O59425
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RNP1_PYRHO
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Ribonuclease P protein component 1 (RNase P component 1) (EC 3.1.26.5) (Rpp29)
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MRRNSKERKNRATRRSQGSYQEIIGRTWIFRGAHRGRVTRRNIIWHELIGLRVRIVGSTHPAFVGIEGYVIDETRNMLVIAGDRIWKVPKDVCIFEFEADDGTKIKIPGERLVGRPEMRLKKRWKKW
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Part of ribonuclease P (RNase P), a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Binds RNase P RNA.
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O59543
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RNP3_PYRHO
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Ribonuclease P protein component 3 (RNase P component 3) (EC 3.1.26.5) (Rpp30)
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MVGGGGVKFIEMDIRDKEAYELAKEWFDEVVVSIKFNEEVDKEKLREARKEYGKVAILLSNPKPSLVRDTVQKFKSYLIYVESNDLRVIRYSIEKGVDAIISPWVNRKDPGIDHVLAKLMVKKNVALGFSLRPLLYSNPYERANLLRFMMKAWKLVEKYKVRRFLTSSAQEKWDVRYPRDLISLGVVIGMEIPQAKASISMYPEIILKRLKY
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Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Not absolutely essential for activity in vitro, however it strongly stimulates activity. Binds RNase P RNA. {ECO:0000255|HAMAP-Rule:MF_00756, ECO:0000269|PubMed:12810070, ECO:0000269|PubMed:16574071, ECO:0000269|PubMed:16829535}.
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O59651
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KATG2_HALMA
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Catalase-peroxidase 2 (CP 2) (EC 1.11.1.21) (Peroxidase/catalase 2)
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MAETPNSDMSGATGGRSKRPKSNQDWWPSKLNLEILDQNARDVGPVEDDFDYAEEFQKLDLEAVKSDLEELMTSSQDWWPADYGHYGPLFIRMAWHSAGTYRTADGRGGAAGGRQRFAPINSWPDNANLDKARRLLLPIKQKYGQKISWADLMILAGNVAIESMGFKTFGYAGGREDAFEEDKAVNWGPEDEFETQERFDEPGEIQEGLGASVMGLIYVNPEGPDGNPDPEASAKNIRQTFDRMAMNDKETAALIAGGHTFGKVHGADDPEENLGPEPEAAPIEQQGLGWQNKNGNSKGGEMITSGIEGPWTQSPTEWDMGYINNLLDYEWEPEKGPGGAWQWAPKSEELKNSVPDAHDPDEKQTPMMLTTDIALKRDPDYREVMETFQENPMEFGMNFAKAWYKLTHRDMGPPERFLGPEVPDEEMIWQDPLPDADYDLIGDEEIAELKEEILDSDLSVSQLVKTAWASASTYRDSDKRGGANGARLRLEPQKNWEVNEPEQLETVLGTLENIQTEFNDSRSDGTQVSLADLIVLGGNAAVEQAAANAGYDVEIPFEPGRVDAGPEHTDAPSFDALKPKVDGVRNYIQDDITRPAEEVLVDNADLLNLTASELTALIGGMRSIGANYQDTDLGVFTDEPETLTNDFFVNLLDMGTEWEPAADSEHRYKGLDRDTGEVKWEATRIDLIFGSNDRLRAISEVYGSADAEKKLVHDFVDTWSKVMKLDRFDLE
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Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
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O59676
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PDP1_SCHPO
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PWWP domain-containing protein 1 (Set9-associated factor pdp1)
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MNNARTNAKRRRLSSKQGGLSISEGKESNIPSVVEESKDNLEQASADDRLNFGDRILVKAPGYPWWPALLLRRKETKDSLNTNSSFNVLYKVLFFPDFNFAWVKRNSVKPLLDSEIAKFLGSSKRKSKELIEAYEASKTPPDLKEESSTDEEMDSLSAAEEKPNFLQKRKYHWETSLDESDAESISSGSLMSITSISEMYGPTVASTSRSSTQLSDQRYPLSSNFDHRGEAKGKGKQPLKNPQERGRISPSSPLNDQTKALMQRLLFFRHKLQKAFLSPDHLIVEEDFYNASKYLNAISDIPFLNYELITSTKLAKVLKRIAFLEHLENDELYDIRQKCKNLLYSWAMFLPNEPSIKGM
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Necessary for DNA damage checkpoint activation. Required for the association of set9 with chromatin and subsequent methylation of H4K20. Associates with H4K20me1 to increase the concentration of set9 on chromatin to perform H4K20me3. H4K20me3 is mainly enriched at heterochromatin and is required for proper heterochromatin assembly.
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O59701
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CYSK_SCHPO
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Cysteine synthase 1 (CS 1) (EC 2.5.1.-) (EC 2.5.1.47) (O-acetylserine (thiol)-lyase 1) (OAS-TL 1) (O-acetylserine sulfhydrylase 1) (O-succinylserine sulfhydrylase)
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MATSGIQTKVPGIVSGFIGAIGRTPLIRLNTLSNETGCNILAKAEFQNPGGSVKDRAAYYVVRDAEKKGKLSRGGTIVEGTAGNTGIGLAHIARARGYKCVIYMPNTQSQAKIDTLKFLGAEVHPVPVAPFSNPLNYNHQARRHAESTPNASWTDQFDNVANLLSHYETTGPEIWDQTKGTVDGFTCSTGTGGTFAGVTKYLKEKSDGRVASFVADPPGSVLYSHIKTKGKHPDNKGSSFTEGIGQGRITGNVQPVYDLIDDAMKIPDEKSINMFFRLLDQEGLFLGGSSCLNVVAAVEMAKILGPGKTVVTILCDSGHKYATRLFSRSFLESKKLFDVIEPQYKKYIVLP
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Catalyzes the conversion of O-succinyl-L-serine into cysteine, the last step in the cysteine biosynthesis pathway. Can also use O-acetyl-L-serine.
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O59702
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CLR6_SCHPO
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Histone deacetylase clr6 (EC 3.5.1.98) (Cryptic loci regulator 6)
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MGFGKKKVSYFYDEDVGNYHYGPQHPMKPHRVRMVHNLVVNYNLYEKLNVITPVRATRNDMTRCHTDEYIEFLWRVTPDTMEKFQPHQLKFNVGDDCPVFDGLYEFCSISAGGSIGAAQELNSGNAEIAINWAGGLHHAKKREASGFCYVNDIALAALELLKYHQRVLYIDIDVHHGDGVEEFFYTTDRVMTCSFHKFGEYFPGTGHIKDTGIGTGKNYAVNVPLRDGIDDESYESVFKPVISHIMQWFRPEAVILQCGTDSLAGDRLGCFNLSMKGHSMCVDFVKSFNLPMICVGGGGYTVRNVARVWTYETGLLAGEELDENLPYNDYLQYYGPDYKLNVLSNNMENHNTRQYLDSITSEIIENLRNLSFAPSVQMHKTPGDFTFENAEKQNIAKEEIMDERV
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Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Has a role in chromatin assembly and chromosome segregation.
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O59703
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GGPPS_SCHPO
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Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (Sporulation-specific protein 9)
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MVNDFNEKNGIKKRLLDFFPVVLEGIREILESMQYFPEETEKLLYSIKRNTLGGKNNRGLAVLQSLTSLINRELEEAEFRDAALLGWLIEILQGCFLMADDIMDQSIKRRGLDCWYLVVGVRRAINESQLLEACIPLLIRKYFRNMPYYVDLLDTFREVTFLTELGQQEDLLSSRDGEASLRSFDLMKYDFIITYKTSFYSFYLPIKCALLLSRNSNQKAYDTTIKLSKLLGYYFQVQDDYLDCFGDYTVLGKVGMDIQDNKCTWLVCYAEKFASADQLNLLRAHYGKAGSENIAVIKQLYHELQIPELYHKFEDDMVDSISKEIDLIDESTGLKKCIFTKFFQLIYKRSR
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Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of ypt7 and rhb1. May be involved in vesicle trafficking and protein sorting. Required for forespore membrane formation.
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O59718
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NEM1_SCHPO
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Nuclear envelope morphology protein 1 (EC 3.1.3.16)
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MNSIARLSDEINKAILATPLDDDEADKEKLANARGRASSATLRHYNRRRSSYSASSLSSLSSKPTEKEVPTRNEKPKHANIMRVVVYWIRVFLKRIYTFFVHSARVFLYHFLNEEKEFTLASFFWGLCRFVFFPVLLSYKRREMLPPQPSVRRPRFYSSYSYPSSHQDPAYSSFKRHRSSNSYSSSSNGNHVRFQPSIAEEEISFNSFSNSLNSEEDVCVSPMKPKEVSLMGKANSNRSGHSHQPQSTQFSPPANDNISKLPSSFTIVNDPLKSPSSSRLRIRNITLCADKIPRPLLNSKLPRKTLVLDLDETLIHSVSRGSRTTSGQPIEVHVPGEHPILYYIHKRPHLDYFLSNVSQWFRLILFTASVQPYADPIIDYLERDKKIFAKRYYRQHCALVDSSFVKDISICNIHLSRIMIIDNSPASYNAHKENAIPIEGWISDPSDVDLLNLLSFLHALQYVHDVRDLLGLRLAK
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Catalytic component of the nem1-spo7 complex which acts as a phosphatase and may be required for proper nuclear membrane morphology.
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O59726
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FNX2_SCHPO
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Vacuolar membrane amino acid uptake transporter fnx2
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MSNPRTKSPNTNRGQGLRSERSALLNDSLSSLNGNSSYDSIKDSSKNNKDVAEVNEYPRRPESSVSVVSNSPHRQDAATTNTVSTVSVSKVLPALLLGVVLAALDNTIVASTYTKIGAEFGKFSQVSWTATAYMISCTAFQPLFGKFCDIYGRKKTLLAAYCVFGIGCFLCGTSRSLWQLVAARAIAGIGGGGMNSTVSILMSDIVPLKQRGTYQGIINVFFAIGSSLGGPVGGYFADQYTWRIGFLIQVPLIAIAFLCVYFTLNLPHHNHVSFMTRFRKIDLKGLILLIIGVTTMTCAFTLGGNVREWNDPVVISLLIASSISYLSFVYVEAFVAFEPLAPMDVLTERTCLSSYLCNFFHSVANFGWIYGMPLFFQSIKNEGAEKSGIRLIPMIIGSSLGSLLGGAVISLTGNYKKITVGSYFFGSVAALFMLRYGYSNFNWEYAVYPFSGGLGNGIAVTTTLVAIIHASPSAFQASAIATSYLFRSNGCVLGVSISSSIVQTVLGIKLRKSLDFDVDELLHHLRKDISYVHRLPEEIRQTVLDALLGSIHYSFLFVSFMFFCAFVCSMFIKNRNL
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MFS-type transporter involved in vacuolar amino acid uptake.
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O59734
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RUXF_SCHPO
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Small nuclear ribonucleoprotein F (snRNP-F) (Sm protein F) (Sm-F) (SmF)
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MSFVPVNPKPFLQGLIGKPVLVRLKWGQEYKGTLQSVDSYMNLQLLNAEELVDGVKTGDLGEILIRCNNVLWVGESTV
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Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity).
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