Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
D3Z8E6 | CAMP1_RAT | MVDAGGRSAAEGWRRMEAPPEGADLVPLDRYDAARAKIAANLQWICAKAYGLDNIPEDLRDPFYIDQYEQEHIKPPVIKLLLSSELYCRVCSLILKGDQAATLQGHQSVIQALSRKGIYVMESDDTPVTDADLSQAPIKMSGHMAMVDALMMAYTVEMISIEKVVASVKRFSTFSASKELPYDLEDAMVFWINKVNLKMREITEKEVKLKQQPLESPAHQKPGLEHAVMHCMLEPVDFARVVRYRREHLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHLNKCF... | null | null | cytoplasmic microtubule organization [GO:0031122]; cytoskeleton organization [GO:0007010]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; neuron projection development [GO:0031175]; regulation of cell morphogenesis [GO:0022604]; regulation of microt... | cytoplasm [GO:0005737]; microtubule [GO:0005874]; microtubule minus-end [GO:0036449] | calmodulin binding [GO:0005516]; microtubule binding [GO:0008017]; microtubule minus-end binding [GO:0051011]; spectrin binding [GO:0030507] | PF17095;PF11971;PF08683; | 3.10.20.360; | CAMSAP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5T5Y3}. Note=Associates with the minus-end of microtubules. In contrast to CAMSAP2 and CAMSAP3, does not form stretches of decorated microtubule minus-ends. {ECO:0000250|UniProtKB:Q5T5Y3}. | null | null | null | null | null | FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization (PubMed:19508979, PubMed:24117850). Specifically recognizes growing microtubule minus-ends and stabilizes microtubules (By similarity). Acts on free microtubul... | Rattus norvegicus (Rat) |
D3Z8K2 | CCD39_RAT | MSSEFLSELHWEDGFAIPVANQENKILEDQLAKLHKEKSNLQDQLRDYEDRINSMSSHLKNVNQEFLFTQSLYKARECEIESEEHFKAIAERELGRVKDEIQQLEKEMAIILERKNDKENAIFKATQKLDGLKCQMNWDQQALEAWLEESAHKDSDSLTLQKYSQQDNNKIRALTLKLEKLTMECNEKRKLLDNELTETLSAQLELDKAAQDFRKIHVERQELIQQWENTIEQMQRRDQEIDNCALALARIKQEAREKEGVVREKIKFLENEVGNNVEYERRISIAERKVSKCRMEYQRQEANRNQLKDELDTLKTTLNR... | null | null | axonemal dynein complex assembly [GO:0070286]; brain development [GO:0007420]; cerebrospinal fluid circulation [GO:0090660]; cilium movement [GO:0003341]; cilium-dependent cell motility [GO:0060285]; determination of digestive tract left/right asymmetry [GO:0071907]; determination of left/right symmetry [GO:0007368]; d... | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; cilium [GO:0005929]; cytosol [GO:0005829]; extracellular region [GO:0005576] | null | null | null | CCDC39 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UFE4}. Note=CCDC40 is required for localization to axonemes. {ECO:0000250|UniProtKB:Q9UFE4}. | null | null | null | null | null | FUNCTION: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Probably acts together with CCDC40 to form a molecular ruler that determines the 96 nanometer (nm)... | Rattus norvegicus (Rat) |
D3Z8L7 | RRAS_RAT | MSSGAASGTGRGRPRGGGPGPRDPPPGETHKLVVVGGGGVGKSALTIQFIQSYFVSDYDPTIEDSYTKICTVDGIPARLDILDTAGQEEFGAMREQYMRAGNGFLLVFAINDRQSFIEVSKLFTQILRVKDRDDFPIVLVGNKADLETQRQVLRSEASSFSASHHMTYFEASAKLRLNVDEAFEQLVRTVRKYQEQELPPSPPSAPRKKDGRCPCVLL | 3.6.5.- | null | cell migration [GO:0016477]; face morphogenesis [GO:0060325]; leukocyte differentiation [GO:0002521]; negative regulation of Schwann cell migration [GO:1900148]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell-matr... | plasma membrane [GO:0005886] | GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-containing complex binding [GO:0044877] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: S-palmitoylated by ZDHHC19, leading to increased association with membranes and with rafts/caveolae as well as enhanced cell viability. {ECO:0000250|UniProtKB:P10301}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P62070}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6207... | null | null | null | null | FUNCTION: Regulates the organization of the actin cytoskeleton. With OSPBL3, modulates integrin beta-1 (ITGB1) activity. {ECO:0000250|UniProtKB:P10301}. | Rattus norvegicus (Rat) |
D3Z902 | FBXW7_RAT | MNQELLSVGSKRRRTGGSLRGNASSSQVDEEQMNRVVEEDPQQQPRHQEEEHTARNGELVGADPRPGAQNDSQQGQVEENNNRFVSVDEDSSGNQEEQEEDEEHAGEQEEEEEEEEEEEEEEEMDQESDDFDQSDDSSREDEHTHNSNVTNCTSVVDLPINQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSDYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRIL... | null | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; lung development [GO:0030324]; negative regulation of gene expression [GO:0010629]; negative regulation of osteoclast development [GO:2001205]; Notch signaling pathway [GO:0007219]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation ... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; Parkin-FBXW7-Cul1 ubiquitin ligase complex [GO:1990452]; perinuclear region of cytoplasm [GO:0048471]; SCF ubiquitin ligase complex... | cyclin binding [GO:0030332]; identical protein binding [GO:0042802]; phosphothreonine residue binding [GO:0050816]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin binding [GO:0043130]; ubiquitin ligase-substrate adaptor activity [GO:1990756]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-prot... | PF12937;PF00400; | 1.20.1280.50;2.130.10.10; | null | PTM: Phosphorylation at Thr-211 promotes interaction with PIN1, leading to disrupt FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation. Phosphorylated by ATM at Ser-26 in response to DNA damage, promoting recruitment to DNA damage sites and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4. {... | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q969H0}. Chromosome {ECO:0000250|UniProtKB:Q969H0}. Note=Localizes to site of double-strand breaks following phosphorylation by ATM. {ECO:0000250|UniProtKB:Q969H0}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q969H0}. | null | null | FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter bri... | Rattus norvegicus (Rat) |
D3Z9H7 | NFAC4_RAT | MGAASCEDEELEFKLVFGEEKEAPPLGPGGPGEELDSEDAPPCCRLALGEPLPYGAAPIGIPRPPPPRPGMHSPPPRPAPSPGTWESQPPRSVRLGGPGGTAGGTGGGRVLECPSIRITSISPTPDPPTSLEDAPETWGDGSPRDYPPPEGFGGYREAGGQGGGAFFSPSPGSSSLSSWSFFSDASDEAALYAACDEVESELNEAASRFGLSSPLPSPRASPRPWTPEDPWSLYGPSSGGRAPEDSWLLLSAPGPIPASPRPASPCGKRRYSSSGTPSSASPALSRRGSLGEEGPEPPPPPPLPLVRDPSSSGPFDYVGA... | null | null | brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; branching involved in blood vessel morphogenesis [GO:0001569]; calcineurin-NFAT signaling cascade [GO:0033173]; cellular respiration [GO:0045333]; cellular response to lithium ion [GO:0071285]; cellular response to UV [GO:0034644]; dendrite morp... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; peroxisome proliferator activated receptor binding [GO:0042975]; RNA polymerase II cis-regula... | PF16179;PF00554; | 2.60.40.10;2.60.40.340; | null | PTM: Phosphorylated by NFATC-kinases; dephosphorylated by calcineurin/PPP3CA. Phosphorylated on Ser-168 and Ser-170 by MTOR, IRAK1, MAPK7/ERK5 and MAPK14/p38, on Ser-213 and Ser-217 by MAPK8 and MAPK9, and on Ser-289 and Ser-344 by RPS6KA3 (By similarity). Phosphorylated by GSK3B; this phosphorylation markedly increase... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K120}. Nucleus {ECO:0000250|UniProtKB:Q8K120}. Note=When hyperphosphorylated, localizes in the cytosol. When intracellular Ca(2+) levels increase, dephosphorylation by calcineurin/PPP3CA leads to translocation into the nucleus. MAPK7/ERK5 and MTOR regulate NFATC4... | null | null | null | null | null | FUNCTION: Ca(2+)-regulated transcription factor that is involved in several processes, including the development and function of the immune, cardiovascular, musculoskeletal, and nervous systems. Involved in T-cell activation, stimulating the transcription of cytokine genes, including that of IL2 and IL4 (PubMed:1237030... | Rattus norvegicus (Rat) |
D3Z9Z9 | SMRCD_RAT | MNLFNLDRFRFEKRSKIEEAPEAAPQPSQPGPSSPISLSAEEENAEGEVSRANTPDSDVTEKTEDSSVPEPPDNESKASLSCFQNQRTIQEYIDLSSDSEDVSPNCSSTVQEKKFSKDTVIIVSEPSEDEESHDLPSATRRNDISELEDLSELEDLKDAKLQTLKELFPQRSDSDLLKLIDSTSTMDGAIAAALLKFGDAGGGPRKRKLSSSSEAYEEDEANDDQSLKKPRGDRREESNESAEASSNWEKQESIVLKLQKEFPNFDKQELREVLKEHEWMYTEALESLKVFAEDQDVQCASQSEVTNGKEVARNQNYSKN... | 3.6.4.12 | null | chromatin remodeling [GO:0006338]; chromosome separation [GO:0051304]; DNA double-strand break processing [GO:0000729]; regulation of DNA recombination [GO:0000018] | heterochromatin [GO:0000792]; nuclear replication fork [GO:0043596]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; ubiquitin binding [GO:0043130] | PF00271;PF00176; | 3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Colocalizes with PCNA at replication forks during S phase. Recruited to double-strand breaks (DSBs) sites of DNA damage (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking D... | Rattus norvegicus (Rat) |
D3ZA12 | CHD6_RAT | MKMKIQKKEKQLSKLRALNHSPMSDASVNFDYKSPSPFDCSPDQGENIEEAANHCLPQKDFYTTEEEADTLFSRKLMSHNGMEDNGGRGTGVKKKRKKKEPGEQEGTKASKDREPKPKRKREPKEPKEPRRAKEPKRAKEPKEAKQKDGVKKPRKPREASGTKEGKEKRSCTDCGPRTKPKKASKDQGPTPVERKKKGKRKNETTVESLELDQSLPNPSLQSPEEPSESADSQKRRSGRQVKRRKYNEDLDFKVVDDDGETIAVLGAGRTSALSASTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEPPFDLELFYVK... | 3.6.4.12 | null | cell redox homeostasis [GO:0045454]; chromatin remodeling [GO:0006338]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468] | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; transcription coregulator b... | PF00385;PF00271;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8TD26}. Note=Enriched at sites of mRNA synthesis. {ECO:0000250|UniProtKB:Q8TD26}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q8TD26}; | null | null | null | null | FUNCTION: DNA-dependent ATPase that plays a role in chromatin remodeling. Regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. Activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2. ... | Rattus norvegicus (Rat) |
D3ZAA9 | MPP2_RAT | MPVAATNSESAMQQVLDNLGSLPNATGAAELDLIFLRGIMESPIVRSLAKAHERLEETKLEAVRDNNLELVQEILRDLAELAEQSSTAAELARILQEPHFQSLLETHDSVASKTYETPPPSPGLDPTFSNQPVPPDAVRMVGIRKTAGEHLGVTFRVEGGELVIARILHGGMVAQQGLLHVGDIIKEVNGQPVGSDPRALQELLRSASGSVILKILPSYQEPHLPRQVFVKCHFDYDPARDSLIPCKEAGLRFNAGDLLQIVNQDDANWWQACHVEGGSAGLIPSQLLEEKRKAFVKRDLELTPTSGTLCGSLSGKKKKR... | null | null | excitatory postsynaptic potential [GO:0060079]; long-term synaptic potentiation [GO:0060291]; maintenance of postsynaptic density structure [GO:0099562]; postsynapse organization [GO:0099173]; protein homooligomerization [GO:0051260] | cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendrite membrane [GO:0032590]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839];... | PDZ domain binding [GO:0030165]; structural constituent of postsynaptic density [GO:0098919]; transmembrane transporter binding [GO:0044325] | PF00625;PF02828;PF00595;PF07653; | 2.30.42.10;1.10.287.650;3.40.50.300;2.30.30.40; | MAGUK family | PTM: Phosphorylated by SRC. {ECO:0000250|UniProtKB:Q14168}. | SUBCELLULAR LOCATION: Cell projection, dendrite {ECO:0000250|UniProtKB:Q9WV34}. Postsynaptic density {ECO:0000269|PubMed:27756895}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14168}. Membrane {ECO:0000250|UniProtKB:Q14168}. Note=Prominently expressed in the postsynaptic densities of dendritic spines, is also detec... | null | null | null | null | null | FUNCTION: Postsynaptic MAGUK scaffold protein that links CADM1 cell adhesion molecules to core components of the postsynaptic density (PubMed:27756895). In CA1 pyramidal neurons, required for synaptic KCNN2-containing channel function and long-term potentiation expression (By similarity). Seems to negatively regulate S... | Rattus norvegicus (Rat) |
D3ZAR1 | ARH_RAT | MDALKSAGRALIRSPSLAKQSWAGGRHRKLPENWTDTRETLLEGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTAQMHDKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFKVAFEFWQVSKEEKEKREKANQEGGDVPGTRRDSTPSLKTSVATGNLLDLEELAKAPLSTVSANTKNMDDALRPQVLGNNSVVWELDDGLDEAFSRLAQSRTNPQVLDTGLTAQDIHYAQCLSPTDWDKPDSSGFDQDDVFSF | null | null | amyloid precursor protein metabolic process [GO:0042982]; cellular response to cytokine stimulus [GO:0071345]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle clearance [GO:0034383]; positive regulation of low-density lipoprotein particle clearance [GO:... | axon [GO:0030424]; basal plasma membrane [GO:0009925]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; early endosome [GO:0005769]; neurofilament [GO:0005883]; recycling endosome [GO:0055037] | amyloid-beta binding [GO:0001540]; AP-1 adaptor complex binding [GO:0035650]; AP-2 adaptor complex binding [GO:0035612]; clathrin adaptor activity [GO:0035615]; clathrin binding [GO:0030276]; low-density lipoprotein particle receptor binding [GO:0050750]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phos... | PF00640; | 2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8C142}. | null | null | null | null | null | FUNCTION: Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering ... | Rattus norvegicus (Rat) |
D3ZAW2 | PISD_RAT | MAVAGGRGCVRSLREGVLWRSSPCHCDYTATRHFLGALQKLPLQAWVRKVHTAPLRTLFLLRPVPILLAAGGGYAGYRQYEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGA... | 4.1.1.65 | COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03208}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03208}; | lipid droplet formation [GO:0140042]; mitochondrial protein catabolic process [GO:0035694]; phosphatidylethanolamine biosynthetic process [GO:0006646]; protein autoprocessing [GO:0016540]; regulation of mitochondrion organization [GO:0010821] | lipid droplet [GO:0005811]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | phosphatidylserine decarboxylase activity [GO:0004609] | PF02666; | null | Phosphatidylserine decarboxylase family, PSD-B subfamily, Eukaryotic type I sub-subfamily | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... | SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase beta chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}.; SUBCELLULAR ... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:2618245}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67 uM for phosphatidylserine {ECO:0000269|PubMed:2618245}; Vmax=77 nmol/h/mg enzyme {ECO:0000269|PubMed:2618245}; | PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis. {ECO:0000305|PubMed:2618245}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:2618245}; | null | FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity). {ECO:00... | Rattus norvegicus (Rat) |
D3ZAZ5 | BCAR3_RAT | MAAGKFASLPRHMPVNHQFPLASSMDLLSSKSPLAEHRTEAYPDVSIHGTLPRKKKGPPPIRSCDSASHMGTLPHSKSPRQSSPLTQDLILEKPLPDWKGDSFAFRDPYLLDPTLEYVKFSKERHIMDRTPERLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLWCLEERYGTSPGRGREGSFAEGRPDVVKRLSLTTGGIQARDHSLPRGNLLRNKDKSGSQPA... | null | null | endothelin receptor signaling pathway [GO:0086100]; epidermal growth factor receptor signaling pathway [GO:0007173]; insulin receptor signaling pathway [GO:0008286]; lens morphogenesis in camera-type eye [GO:0002089]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of GTPase activ... | cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; membrane [GO:0016020] | guanyl-nucleotide exchange factor activity [GO:0005085]; kinase binding [GO:0019900]; phosphotyrosine residue binding [GO:0001784] | PF00617;PF00017; | 1.10.840.10;3.30.505.10; | null | PTM: Phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:Q9QZK2}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QZK2}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9QZK2}. Note=Localization to focal adhesions depends on interaction with PTPRA. {ECO:0000250|UniProtKB:Q9QZK2}. | null | null | null | null | null | FUNCTION: Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (By similarity). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (PubMed:24216110). Promo... | Rattus norvegicus (Rat) |
D3ZB51 | TUTLB_RAT | MIWYVATLIASVISTRGLVAQVAHGLREEPEFVTARAGEGVVLRCDVIHPVTGQPPPYVVEWFKFGVPIPIFIKFGYYPPHVDPEYAGRASLHDKASLRLEQVRSEDQGWYECKVLMLDQQYDTFHNGSWVHLTINAPPTFTETPPQYIEAKEGGSITMTCTAFGNPKPIVTWLKEGTLLSASGKYQVSDGSLTVTSVSREDRGAYTCRAYSIQGEAVHTTHLLVQGPPFIVSPPENITVNISQDALLTCRAEAYPGNLTYTWYWQDENVYFQNDLKLRVRILIDGTLIIFRVKPEDAGKYTCVPSNSLGRSPSASAYLT... | null | null | homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; nervous system development [GO:0007399]; positive regulation of inhibitory postsynaptic potential [GO:0097151]; synaptic membrane adhesion [GO:0099560] | dendrite [GO:0030425]; GABA-ergic synapse [GO:0098982]; inhibitory synapse [GO:0060077]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; postsynaptic specialization of symmetric synapse [GO:0099629] | kinase binding [GO:0019900] | PF13895;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, Turtle family | PTM: N-glycosylated and sialylated. Not significantly O-glycosylated. {ECO:0000269|PubMed:23751499}. | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:23751499}; Single-pass membrane protein {ECO:0000255}. Postsynaptic density {ECO:0000269|PubMed:23751499}. | null | null | null | null | null | FUNCTION: Transmembrane protein which is abundantly expressed in interneurons, where it may regulate inhibitory synapse development (PubMed:23751499). May mediate homophilic cell adhesion (By similarity). {ECO:0000250|UniProtKB:E9PZ19, ECO:0000269|PubMed:23751499}. | Rattus norvegicus (Rat) |
D3ZB94 | GFRAL_RAT | MLVFIFLAVRLSSENESSSQTNDCAYFMRQCLTDTDGCKQSWRSMEDACLVSGDSCKINNPLPCNLSIQSLVEKHFQFKGCLCTDDLHCTVNKIFGKKCTNKTDSMKKDNKYKRNLTTPLYHDTGFKQMQSCLEVTEACVGDVVCNAQLALYLKACTANGNLCDVKHCQAAIRFFYQNMPFNTAQMLAFCDCAQSDIPCQQSKETLHSKPCALNVVPPPTCLSVIHTCRNDELCRTYYRTFQTECWPHVAGKCREDETCISMLGKQDLTCSGSDSCRAAYLGTFGTVLQVPCACRSITQGEEPLCMAFQHMLHSKSCFNY... | null | null | GDF15-GFRAL signaling pathway [GO:0160144]; glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; negative regulation of appetite [GO:0032099]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of neuron apoptotic process [GO:00... | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | glial cell-derived neurotrophic factor receptor activity [GO:0016167]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor activity [GO:0038023] | PF02351; | null | GDNFR family | PTM: Cleaved and inactivated by MMP14, inhibiting the GDF15-GFRAL aversive response. {ECO:0000250|UniProtKB:Q6UXV0}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:28846098}; Single-pass membrane protein {ECO:0000255}; Extracellular side {ECO:0000305|PubMed:28846098}. | null | null | null | null | null | FUNCTION: Brainstem-restricted receptor for GDF15 hormone, which triggers an aversive response, characterized by nausea, vomitting, and/or loss of appetite in response to various stresses (PubMed:28846098, PubMed:28846099, PubMed:31928886, PubMed:37060902). The aversive response is both required to reduce continuing ex... | Rattus norvegicus (Rat) |
D3ZBE5 | NEK7_RAT | MDEQPQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRASCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALDHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNICINPDPEKRPDIAYVYDVAKRMHACTASS | 2.7.11.34 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8TD19}; | cellular response to potassium ion [GO:0035865]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; protein phosphorylation [GO:0006468]; regulation of mitotic cell cycle ... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; spindle pole [GO:0000922] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molecular function activator activity [GO:0140677]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, NEK Ser/Thr protein kinase family, NIMA subfamily | PTM: Phosphorylation at Ser-195 required for its activation. {ECO:0000250|UniProtKB:Q8TDX7}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TDX7}. Cytoplasm {ECO:0000250|UniProtKB:Q8TDX7}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q8TDX7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TDX7}. Note=Present at centrosome throughout the cell ... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.34; Evidence={ECO:0000269|PubMed:11516946}; Physiolo... | null | null | null | null | FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression (PubMed:11516946). Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis (By similarity). Phosphorylates EML4 at 'Ser-146', promoting its dissociation from microtubules dur... | Rattus norvegicus (Rat) |
D3ZBN0 | H15_RAT | MSETAPAETTAPAPVEKSPAKKKTKKAGAAKRKATGPPVSELITKAVSASKERGGVSLPALKKALAAGGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKVASGEAKPKAKKTGAAKAKKPTGATPKKPKKTAGAKKTVKKTPKKAKKPAAAGVKKVTKSPKKAKAAAKPKKATKSPARPKAVKSKASKPKVTKPKAAKPKAAKVKKAVSKKK | null | null | chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; establishment of protein localization to chromatin [GO:0071169]; muscle organ development [GO:0007517]; negative regulation of DNA recombination [GO:0045910]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome ass... | chromatin [GO:0000785]; heterochromatin [GO:0000792]; nucleosome [GO:0000786]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; histone deacetylase binding [GO:0042826]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P16401}.; PTM: Citrullination at Arg-53 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P16401}. Chromosome {ECO:0000250|UniProtKB:P16401}. Note=Mainly localizes with heterochromatin (By similarity). Associates with actively transcribed chromatin and not heterochromatin (By similarity). {ECO:0000250|UniProtKB:P16401}. | null | null | null | null | null | FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin rem... | Rattus norvegicus (Rat) |
D3ZBP4 | MICA1_RAT | MASPTSTNPAHDHFETFVQAQLCQDVLSSFQGLCRALGVESGGGLPQYHKIKAQLNYWSAKSLWAKLDKRASQPAYQQGQACTNTKCLVVGAGPCGLRAAVELALLGARVVLVEKRTKFSRHNVLHLWPFTIHDLRALGAKKFYGRFCTGTLDHISIRQLQLLLLKVALLLGVEIHWGFTFTGLQPPPKKGSGWRARIQPSPPAQLASYEFDVLISAGGGKFVPEGFTIREMRGKLAIGITANFVNGRTVEETQVPEISGVARIYNQKFFQSLLKATGIDLENIVYYKDDTHYFVMTAKKQCLLRLGVLRQDLPETDQLL... | 1.14.13.225; 1.6.3.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q8TDZ2}; | actin filament depolymerization [GO:0030042]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein phosphorylation [GO:0001933]; regulation of regulated secretory pathway [GO:1903305]; sulfur oxidation [GO:0019417] | actin filament [GO:0005884]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; hippocampal mossy fiber expansion [GO:1990026]; intercellular bridge [GO:0045171]; midbody [GO:0030496] | actin binding [GO:0003779]; FAD binding [GO:0071949]; metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; NADPH oxidase H202-forming activity [GO:0106294]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular ... | PF12130;PF00307;PF01494;PF00412; | 1.10.418.10;2.10.110.10;3.50.50.60; | Mical family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TDZ2}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8TDZ2}. Endosome membrane {ECO:0000250|UniProtKB:Q8TDZ2}. Midbody {ECO:0000250|UniProtKB:Q8TDZ2}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-(R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044, ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:5834... | null | null | null | null | FUNCTION: Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Acts ... | Rattus norvegicus (Rat) |
D3ZCM3 | ABCG4_RAT | MAEKALEAVGCGLGPGAVAMAVALEDGAEPPVLTTHLKKVENHITEAQRFSHLPKRSAVDIEFVELSYSVREGPCWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAHGGRTVICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGEYGDL... | 7.6.2.- | null | cellular response to high density lipoprotein particle stimulus [GO:0071403]; cellular response to leukemia inhibitory factor [GO:1990830]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; positive regulation of cholesterol biosynthetic process [GO:0045542]; positive regulation of cholesterol effl... | cytoplasmic vesicle [GO:0031410]; endosome [GO:0005768]; endosome membrane [GO:0010008]; plasma membrane [GO:0005886] | ABC-type sterol transporter activity [GO:0034041]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF01061;PF19055;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCG family, Eye pigment precursor importer (TC 3.A.1.204) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H172}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q91WA9}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q91WA9}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) + phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q91WA9}; PhysiologicalDirection=left-to-right; Xr... | null | null | null | null | FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that may be involved in the cellular efflux of sterols, in particular cholesterol and desmosterol (a cholesterol precursor), to high-density lipoprotein (HDL) (By similarity). May play an important role in the removal of amyloid-beta peptides ... | Rattus norvegicus (Rat) |
D3ZD32 | CHD5_RAT | MRGPLGTEEELPRLFAEEMENEEEMSEEEDGGLEGFEDFFPAEPVSLPKKKPKKLKESKSKGKRKKKEGSNDELSENEEDLEEKSESEGSDYSPTKKKKKKLKEKKEKKAKRKKRDEDEEDNEDGGLKEPKSSGQLMAEWGLDDVDYLFSEDDYHTLTNYKAFSQFLRPLIAKKNPKIPMSKMMTVLGAKWREFSANNPFKGSSAAAAAAAVAAAVETVTIAPPLAISPQQVPQPLPVRKAKTKEGKGPGVRKKNKGAKDSKKKGRGKRVAGLKFRFGGISKRKKGSSSEEDEPEDSDLDNASIHSSSVRSECSAALGKK... | 3.6.4.12 | null | cerebral cortex neuron differentiation [GO:0021895]; chromatin remodeling [GO:0006338]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of signal transduction by p53 class mediator [GO:1901798]; regulation of ... | chromatin [GO:0000785]; heterochromatin [GO:0000792]; nucleus [GO:0005634]; NuRD complex [GO:0016581] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; H3K27me3 modified histone binding [GO:0061628]; helicase activity [GO:0004386]; histone binding [GO:0042393]; histone deacetylase binding [GO... | PF08074;PF06461;PF08073;PF00385;PF06465;PF00271;PF00628;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810;3.30.40.10; | SNF2/RAD54 helicase family | PTM: Methylated at Gln-1388 by N6AMT1. {ECO:0000250|UniProtKB:Q8TDI0}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21931736}. Chromosome {ECO:0000250|UniProtKB:A2A8L1}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chr... | Rattus norvegicus (Rat) |
D3ZDI6 | MYLIP_RAT | MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKESLLAGHLQCSPEQAVELSALLAQTKFGDYNQNTAQYSYEDLCEKELSSSTLNSIVGKHKELEGISQASAEYQVLQIVSAMENYGIEWHAVRDSEGQKLLIGVGPEGISICKEDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDTVTSAVMMQYSRDLKGHLASLFLNENINLGKKYVFDIKRTSK... | 2.3.2.27 | null | cholesterol homeostasis [GO:0042632]; negative regulation of low-density lipoprotein particle clearance [GO:0010989]; negative regulation of neuron projection development [GO:0010977]; nervous system development [GO:0007399]; positive regulation of protein catabolic process [GO:0045732]; protein destabilization [GO:003... | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; plasma membrane [GO:0005886] | cytoskeletal protein binding [GO:0008092]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF09380;PF00373;PF09379;PF13920; | 1.20.80.10;2.30.29.30;3.30.40.10; | null | PTM: Autoubiquitinated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WY64}. Cell membrane {ECO:0000250|UniProtKB:Q8WY64}; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteract... | Rattus norvegicus (Rat) |
D3ZDK2 | UB2D1_RAT | MALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIMGPPDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPDIAQIYKSDKEKYNRHAREWTQKYAM | 2.3.2.23; 2.3.2.24 | null | negative regulation of TORC1 signaling [GO:1904262]; positive regulation of protein polyubiquitination [GO:1902916]; positive regulation of protein ubiquitination [GO:0031398]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K48-linked ubiquitination [GO:0070936]; protein polyubi... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; ubiquitin ligase complex [GO:0000151] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P51668}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51668}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000250|UniProtKB:P51668, ECO:0000255|PROSITE-ProR... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates auto-ubiquitinat... | Rattus norvegicus (Rat) |
D3ZDK7 | PGP_RAT | MAEAEAGGDEVRCVRLSAERAKLLLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGPMGPEAGLEVFGTAYCSALYLRQRLAGVPDPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRYLQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTILTLTGVSSLEDVKSNQESDCMFKKKMVPDFYVDSIADLLPALQ... | 3.1.3.21; 3.1.3.48 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8CHP8}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHP8}; | glycerol biosynthetic process [GO:0006114]; glycerophospholipid metabolic process [GO:0006650]; negative regulation of gluconeogenesis [GO:0045721] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ADP phosphatase activity [GO:0043262]; glycerol-1-phosphatase activity [GO:0000121]; glycerol-3-phosphatase activity [GO:0043136]; magnesium ion binding [GO:0000287]; phosphoglycolate phosphatase activity [GO:0008967]; protein tyrosine phosphatase activity [GO:0004725] | PF13344;PF13242; | 3.40.50.1000; | HAD-like hydrolase superfamily, CbbY/CbbZ/Gph/YieH family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q8CHP8}; CATALYTIC ACTIVITY: Reac... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=47 nmol/min/mg enzyme with glycerol-3-phosphate as substrate {ECO:0000269|PubMed:26755581}; | null | null | null | FUNCTION: Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol (PubMed:26755581). Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism. Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-pr... | Rattus norvegicus (Rat) |
D3ZDM7 | OXDD_RAT | MDTVRIAVVGAGVIGLSTAACVSQLVPRCSVTVISDRFTPDTTSNVAAGMLIPPTYPDTPVPTLKRWFRETFQHLSEIARSAEAVDAGIHLVSGWQIFRSVPTEEVPFWADVVLGFREMTEAELKRFPQYEFGQAFTTLKCETSAYLPWLEKRIKGSGGLLLTRRIEDLWELQPSFDIVVNCSGLGSRRLVGDATVSPVRGQVLQAQAPWVKHFIRDGGGLTYVYPGTSYVTLGGSRQTGDWNLSPDAELSREIFSRCCALEPSLHRACDIKEKVGLRPSRPGVRLQKEILVRGEQRLPVVHNYGHGSGGISVHWGSALE... | 1.4.3.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:29292239, ECO:0000269|PubMed:32376478}; | aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; D-amino acid catabolic process [GO:0019478]; grooming behavior [GO:0007625]; hormone metabolic process [GO:0042445]; insemination [GO:0007320]; nervous system process [GO:0050877]; regulation of cell communication [GO:0010646] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | D-aspartate oxidase activity [GO:0008445]; FAD binding [GO:0071949] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:12209855, ECO:0000269|PubMed:1991137}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99489}. Note=Active in the peroxisomal matrix. {ECO:0000250|UniProtKB:Q99489}. | CATALYTIC ACTIVITY: Reaction=D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:12512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29990; EC=1.4.3.1; Evidence={ECO:0000269|PubMed:25747990, ECO:0000269|PubMed:29292239, ECO:0000269|PubMed:3... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.26 mM for D-aspartate (at 37 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:25747990}; Note=kcat is 31.1 sec(-1) with D-aspartate as substrate (at 37 degrees Celsius and at pH 8.3). {ECO:0000269|PubMed:25747990}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.3-12.5. {ECO:0000269|PubMed:29292239}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:29292239}; | FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids (PubMed:1991137, PubMed:25747990, PubMed:29292239, PubMed:32376478). Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors (By similarity). Protects the organism from the toxicity... | Rattus norvegicus (Rat) |
D3ZE55 | PCDH8_RAT | MSPVKRWGSPCLFPLQLFSLCWVLSVAQSKTVRYSTFEEDAPGTVIGTLAEDLHMKVSGDTSFRLMKQFNSSLLRVREGDGQLTVGDAGLDRERLCGQSPQCVLAFDVVSFSQEQFRLVHVEVEVRDVNDHAPRFPRAQIPVEVSESAPVGTRIPLEVPVDEDVGANGLQSVRLAEPHSPFRVELQTRADGAQCADLVLLQELDRESQASYSLELVAQDGGRPPRSATAALSVRVLDANDHSPAFPQGAVAEVELAEDAPVGSLLLDLDAADPDEGPNGDVVFTFGARTPPEARHLFRLDPRSGRLTLAGQVDYERQDTY... | null | null | cell adhesion [GO:0007155]; chemical synaptic transmission [GO:0007268]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; long-term memory [GO:0007616]; modulation of chemical synaptic transmission [GO:0050804]; morphogenesis of embryonic epithelium [GO:0016331]; regulation of synaptic memb... | dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202] | calcium ion binding [GO:0005509] | PF00028;PF08266; | 2.60.40.60; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000269|PubMed:10383464}. Presynaptic cell membrane {ECO:0000269|PubMed:10383464}. Postsynaptic cell membrane {ECO:0000269|PubMed:10383464}. Note=Also expressed in the cell bodies of neur... | null | null | null | null | null | FUNCTION: Calcium-dependent cell-adhesion protein. May play a role in activity-induced synaptic reorganization underlying long term memory. Could be involved in CDH2 internalization through TAOK2/p38 MAPK pathway. In hippocampal neurons, may play a role in the down-regulation of dendritic spines, maybe through its acti... | Rattus norvegicus (Rat) |
D3ZEF4 | CUL7_RAT | MVGELRYREFRVPLGPGLHAYPDELIRQRVGHNGHPEYQIRWLILRRGDDGDSSQVDCKAEHILLWMTDDEIYANCHKMLGEDGQVIRPSQESAEAGALDKSVLGEMETDVKSLIQRALRQLEECVGAVPPAPLLHTVHVLSAYASIEPLTGVFKDRRVLDLVMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLTEHPMSFEGVQLPQVPGRLLFSLVKRYLCVTFLLDRLNGNAEDQDAQNNFIPEELNAGRGRVELEFSMAMGTLISELVQAMRWDWASSRSESS... | null | null | epithelial to mesenchymal transition [GO:0001837]; Golgi organization [GO:0007030]; microtubule cytoskeleton organization [GO:0000226]; mitotic cytokinesis [GO:0000281]; placenta development [GO:0001890]; positive regulation of dendrite morphogenesis [GO:0050775]; protein ubiquitination [GO:0016567]; regulation of mito... | 3M complex [GO:1990393]; centrosome [GO:0005813]; Cul7-RING ubiquitin ligase complex [GO:0031467]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471] | ubiquitin protein ligase binding [GO:0031625] | PF03256;PF11515;PF00888; | 2.30.30.30;2.60.120.260;1.10.10.10; | Cullin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21572988}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21572988}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Note=During mitosis, localizes to the mitotic apparatus. CCDC8 is r... | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:21572988}. | null | null | FUNCTION: Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the le... | Rattus norvegicus (Rat) |
D3ZEH5 | SIDT2_RAT | MIAWRLPLCVLLVAAVESHLGALGPKNVSQKDAEFERTYADDVNSELVNIYTFNHTVTRNRTEGVRVSVNVLNKQKGAPLLFVVRQKEAVVSFQVPLILRGLYQRKYLYQKVERTLCQPPTKNESEIQFFYVDVSTLSPVNTTYQLRVNRVDNFVLRTGELFTFNTTAAQPQYFKYEFPDGVDSVIVKVTSKKAFPCSVISIQDVLCPVYDLDNNVAFIGMYQTMTKKAAITVQRKDFPSNSFYVVVVVKTEDQACGGSLPFYPFVEDEPVDQGHRQKTLSVLVSQAVTSEAYVGGMLFCLGIFLSFYLLTVLLACWENW... | null | null | cell morphogenesis [GO:0000902]; glucose homeostasis [GO:0042593]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; response to glucose [GO:0009749]; RNA catabolic process [GO:0006401]; RNA transport [GO:0050658]; type B pancreatic cell development [GO:0003323]; type B pan... | lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; plasma membrane [GO:0005886] | AP-1 adaptor complex binding [GO:0035650]; AP-2 adaptor complex binding [GO:0035612]; DNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; nucleic acid transmembrane transporter activity [GO:0051032]; RNA transmembrane transporter activity [GO:0051033] | PF13965; | null | SID1 family | PTM: Glycosylated. {ECO:0000269|PubMed:20965152}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8NBJ9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBJ9}. Cell membrane {ECO:0000250|UniProtKB:Q8NBJ9}. Note=Mainly localizes to lysosomes and only partly to the plasma membrane (By similarity). Lysosomal localization is required for SIDT2-mediat... | null | null | null | null | null | FUNCTION: Mediates the translocation of RNA and DNA across the lysosomal membrane during RNA and DNA autophagy (RDA), a process in which RNA or DNA is directly imported into lysosomes in an ATP-dependent manner, and degraded. Involved in the uptake of single-stranded oligonucleotides by living cells, a process called g... | Rattus norvegicus (Rat) |
D3ZEN0 | MILK2_RAT | MAAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFNALRKENIYENNKLAFQVAEEQLGIPALLDAEDMVALKIPDRLSILTYVSQYYNYFHGRSPIGGMAGMKRPSSDSTEELSGKKKVPSQPAKLSSPVPTQRLPLSPARTNPVVQRNEGVSERPSPKAAPGTVGSSVSSICGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSSTLHSGAYRATGEPGVFVCTHHSSEAVSVSPKLSNLASRQPGGGIADTRPIGVSQKVLETNGEATPLRARTAAWEHAGGNRAAKGFVQTELTPPATSRVH... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; bicellular tight junction assembly [GO:0070830]; endocytic recycling [GO:0032456]; neuron projection development [GO:0031175]; substrate adhesion-dependent cell spreading [GO:0034446] | actin filament bundle [GO:0032432]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | actin filament binding [GO:0051015]; actinin binding [GO:0042805]; filamin binding [GO:0031005]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267] | PF12130;PF00307;PF00412; | 1.10.418.10;2.10.110.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Recycling endosome {ECO:0000250}. Cell projection {ECO:0000269|PubMed:20008558}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. | null | null | null | null | null | FUNCTION: Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may ther... | Rattus norvegicus (Rat) |
D3ZER2 | BFSP2_RAT | MSERRVAMDLPSGSNASMPLQRHRVSSLRGTRSPSSLDSPPASRTSAVGSLVRAPGVYVGVAPSGGIGGLGARVTRRALGISSVFLQGLRSSGLATAPAPGPERNHATAEDLGGCLVEYMTKVHALEQVSQELETQLRAHLESKAKRSGGWDALRASWASSYQQVGEAVLENARLMLQMETIQAGADDFKERYENEQPFRKAAEEEVSSLYKVIDEANLTKTDLEHQIESLKEELGSLSRSYEEDVKVLYKQLAGSELEQTDVPMGTGLDDVLETIRVQWERDVEKNRAEAGAVLQAKQQTEVVHVSQTQEEKLAAALSV... | null | null | cell maturation [GO:0048469]; cytoskeleton organization [GO:0007010]; intermediate filament cytoskeleton organization [GO:0045104]; intermediate filament organization [GO:0045109]; lens fiber cell development [GO:0070307]; response to stimulus [GO:0050896]; visual perception [GO:0007601] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; intermediate filament [GO:0005882]; plasma membrane [GO:0005886] | structural constituent of eye lens [GO:0005212] | PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18449355}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q28177}; Cytoplasmic side {ECO:0000250|UniProtKB:Q28177}. Cytoplasm {ECO:0000269|PubMed:18449355}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q28177}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q... | null | null | null | null | null | FUNCTION: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Plays a role in maintenance of retinal lens optical clarity (By similarity). {ECO:0000250|UniProtKB:Q6NVD9}. | Rattus norvegicus (Rat) |
D3ZEY4 | DGKQ_RAT | MATAAESGARTWPGSGSPRLGSPAGSPVLGISGRARPGSGPERTGRAIGSVAPGHSFRKVTLTKPTFCHLCSDFIWGLAGFLCDVCNFMSHEKCLKQVKTPCTSIAPSLVRVPVAHCFGSLGLYKRKFCVVCRKSLEVPAFRCEVCELHVHPDCVPFACSDCRQCHQDGQHDYDTYHHHWREGNLPSGARCEVCRKTCGSSDVLAGVRCEWCGVQAHSVCSTALTPECTFGRLRSMVLPPSCVRLLSRNFSKMHCFRIPETMVLELGDGDDGLDGSAAVGTGREVSAATESTKQTLKIFDGNDSMRKNQFRLVTVSRLAR... | 2.7.1.107; 2.7.1.93 | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cAMP-mediated signaling [GO:0019933]; diacylglycerol metabolic process [GO:0046339]; G protein-coupled receptor signaling pathway [GO:0007186]; glycerolipid metabolic process [GO:0046486]; intracellular signal transduction [GO:00355... | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endosome [GO:0005768]; glutamatergic synapse [GO:0098978]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynapse [GO:0098793]; vesi... | ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; DNA-binding transcription factor binding [GO:0140297]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; phospholipase binding [GO:0043274]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297] | PF00130;PF00609;PF00781;PF00788; | 2.60.200.40;3.30.60.20; | Eukaryotic diacylglycerol kinase family | PTM: Phosphorylated by PRKCE and PRKCH in vitro. {ECO:0000250|UniProtKB:P52824}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52824}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6P5E8}. Cell membrane {ECO:0000250|UniProtKB:P52824}. Synapse {ECO:0000250|UniProtKB:Q6P5E8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P52824}. Nucleus {ECO:0000269|PubMed:15337525}. Nucleus speckle {ECO:000... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000269|PubMed:15337525}; PhysiologicalDirection=left-to-right... | null | PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000269|PubMed:15337525}. | null | null | FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:15337525). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targ... | Rattus norvegicus (Rat) |
D3ZF77 | AK1CA_RAT | MDLKHSRSVKLNDGNLMPVLGFGTFASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELILNKPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLLEDPVLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQMAFALDHPDYPF... | 1.1.1.-; 1.1.1.216 | null | steroid metabolic process [GO:0008202] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; aldo-keto reductase (NADP) activity [GO:0004033]; farnesol dehydrogenase activity [GO:0047886]; ketosteroid monooxygenase activity [GO:0047086]; steroid dehydrogenase activity [GO:0016229] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17574202, ECO:0000269|PubMed:21187079}. | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesol + NADP(+) = (2E,6E)-farnesal + H(+) + NADPH; Xref=Rhea:RHEA:14697, ChEBI:CHEBI:15378, ChEBI:CHEBI:15894, ChEBI:CHEBI:16619, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.216; Evidence={ECO:0000269|PubMed:17574202, ECO:0000269|PubMed:21187079}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for 4-nitrobenzaldehyde {ECO:0000269|PubMed:17574202}; KM=3.1 uM for benzaldehyde {ECO:0000269|PubMed:17574202}; KM=20 uM for pyridine-4-aldehyde {ECO:0000269|PubMed:17574202}; KM=25 uM for 2-phenyl-2-propenal {ECO:0000269|PubMed:17574202}; KM=2.4 uM for NAD... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.5 for the dehydrogenase activity. Optimum pH is 6 for the reductase activity. {ECO:0000269|PubMed:17574202}; | null | FUNCTION: Catalyzes the NADPH-dependent reduction of a variety of substrates including aromatic and aliphatic aldehydes, quinones, ketones, dicarbonyl compounds and 17-ketosteroids (PubMed:17574202). Catalyzes the NADP(+)-dependent oxidation of aromatic, alicyclic and aliphatic alcohols, and 17beta-hydroxysteroids (Pub... | Rattus norvegicus (Rat) |
D3ZF92 | TNR21_RAT | MGTSASSITALASCSRIAGQVGATMVAGSLLLLGFLSTITAQPEQKTLSLTGTYRHVDRTTGQVLTCDKCPAGTYVSEHCTNTSLRVCSSCPSGTFTRHENGIERCHDCSQPCPRPMIERLPCAALTDRECICPPGMYQSNGTCAPHTVCPVGWGVRKKGTENEDVRCKQCARGTFSDVPSSVMKCRAHTDCLGQNLMVVKQGTKETDNVCGVHLSSSSTTPSSPGIATFSHPEHTESHDVPSSTYEPQGMNSTDSNSTASVRTKVPSDIQEETVPDNTSSTSGKESTNRTLPNPPQLTHQQGPHHRHILKLLPSSMEAT... | null | null | adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; axonal fasciculation [GO:0007413]; B cell apoptotic process [GO:0001783]; cellular response to tumor necrosis factor [GO:0071356]; humoral immune response [GO:0006959]; myelination [GO:0042552]; negative regulation of B cell proliferation [GO:003088... | axon [GO:0030424]; plasma membrane [GO:0005886] | null | PF00531;PF00020; | 1.10.533.10;2.10.50.10; | null | PTM: Oxidized in response to reactive oxygen species (ROS), leading to endocytosis. {ECO:0000250|UniProtKB:O75509}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75509}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75509}. Note=Endocytosed following oxidation in response to reactive oxygen species (ROS). {ECO:0000250|UniProtKB:O75509}. | null | null | null | null | null | FUNCTION: Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B (By similarity). Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm (By similarity). Plays a role in neuronal apoptosis, including apoptosis in response to ... | Rattus norvegicus (Rat) |
D3ZFB6 | PRRT2_RAT | MAASSSEVSEMKGVEDSSNTHSEGPRHSEEGMGPVQVVAENLDQPEALQSGPDTTAAPVDSGPKAELAPETTETPVETPETVQATDLSVNPGEDSKTCPSPKEACQEPASRPEVNREATAEQGAEQQSAAPPEPTSEQALQLNTQSDPQPTSQPPPKPPLQAEPPTQENPTTEVLTESTGEKQENGAVVPLQAGDGEEGPAPQPHSPPSTKTPPANGAPPRVLQKLVEEDRIGRAHGGHPGSPRGSLSRHPSSQLAGPGVEGGEGTQKPRDYIILAILSCFCPMWPVNIVAFAYAVMSRNSLQQGDVDGAQRLGRVAKLL... | null | null | negative regulation of short-term synaptic potentiation [GO:1905513]; negative regulation of SNARE complex assembly [GO:0035544]; neuromuscular process controlling posture [GO:0050884]; regulation of calcium-dependent activation of synaptic vesicle fusion [GO:0150037]; synaptic vesicle fusion to presynaptic active zone... | axon terminus [GO:0043679]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynapse [GO:0098793]; presynaptic membrane [GO:0042734]; synaptic vesicle [GO:0008021]; synapt... | SH3 domain binding [GO:0017124]; syntaxin-1 binding [GO:0017075] | PF04505; | null | CD225/Dispanin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27172900}; Single-pass membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Presynaptic cell membrane {ECO:0000250|UniProtKB:E9PUL5}; Single-pass membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Synapse {ECO:0000250|UniProtKB:E9PUL5}. Cell projection, axon {ECO:000025... | null | null | null | null | null | FUNCTION: As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca(2+)-sensing. In the cerebellum, may inh... | Rattus norvegicus (Rat) |
D3ZFD0 | MY18A_RAT | MFNLMKKDKDKDGGRKEKKEKKEKKERMSAAELRSLEEMSMRRGFFNLNRSSKRESKTRLEISNPIPIKVASGSDLHLTDIDSDSNRGSIILDSGHLSTASSSDDLKGEEGSFRGSVLQRAAKFGSLAKQNSQMIVKRFSFSQRSRDESASETSTPSEHSAAPSPQVEVRTLEGQLMQHSGLGIPRPGPRSRVPELVTKRFPADLRLPALVPPPPPALRELELQRRPTGDFGFSLRRTTMLDRAPEGQAYRRVVHFAEPGAGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQPIPELSELSRSW... | null | null | actomyosin structure organization [GO:0031032]; asymmetric Golgi ribbon formation [GO:0090164]; canonical NF-kappaB signal transduction [GO:0007249]; cell migration [GO:0016477]; cellular response to type II interferon [GO:0071346]; Golgi organization [GO:0007030]; Golgi ribbon formation [GO:0090161]; Golgi vesicle bud... | actomyosin [GO:0042641]; brush border [GO:0005903]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; Golgi membrane [GO:0000139]; microtubule organizing center [GO:0005815]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; phagocytic vesicle [GO:0045335]; trans-Golgi network [GO:0005802] | actin filament binding [GO:0051015]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; cytoskeletal motor activity [GO:0003774] | PF00063;PF01576;PF00595; | 1.10.10.820;1.20.5.340;1.20.58.530;2.30.42.10;3.30.70.1590;3.40.850.10;1.20.120.720;4.10.270.10;1.20.5.1160; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q92614}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q92614}. Golgi outpost {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:31522887}. Note=Recruited to the Golgi apparatus by GOLPH3 (B... | null | null | null | null | null | FUNCTION: May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BP... | Rattus norvegicus (Rat) |
D3ZFJ3 | 3BP1_RAT | MMKRQLHRMRQLAHTGSSGRTPETAEFLGEDLLQVEQRLEPAKRAAHNVHKRLQACLQGQSGADMDKRVKKLPLMALSTAMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLNRLSEEELPAILKRKKSLQKLVSDWNTLKSRLSQAAKNSGSSQSLGGGSSSHTHMATANKVETLKEDEEELKRKVEQCKDEYLADLYHFSTKEDSYANYFTHLLEIQADYHRKSLTSLDTALAELRDNHSQADSSPLTTAAPFSRVYGVSLRTHLQDLGRDIALPIEACVLLLLSEGMQEEGLFRLAAGASVL... | null | null | actin filament organization [GO:0007015]; cell junction assembly [GO:0034329]; cell migration [GO:0016477]; establishment of epithelial cell apical/basal polarity [GO:0045198]; filopodium assembly [GO:0046847]; negative regulation of small GTPase mediated signal transduction [GO:0051058]; phagocytosis, engulfment [GO:0... | adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cell leading edge [GO:0031252]; cytosol [GO:0005829]; exocyst [GO:0000145]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; phagocytic cup [GO:0001891] | GTPase activator activity [GO:0005096]; semaphorin receptor binding [GO:0030215]; SH3 domain binding [GO:0017124] | PF03114;PF00620; | 1.20.1270.60;1.10.555.10; | null | null | SUBCELLULAR LOCATION: Cell projection {ECO:0000269|PubMed:21658605}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9Y3L3}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9Y3L3}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q9Y3L3}. Nucleus {ECO:0000250|UniProtKB:Q9Y3L3}. Cytoplasm, cytosol {... | null | null | null | null | null | FUNCTION: GTPase activating protein/GAP which specifically converts GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive GDP-bound form. By specifically inactivating RAC1 at the leading edge of migrating cells, it regulates the spatiotemporal organization of cell protrusions which is important for prop... | Rattus norvegicus (Rat) |
D3ZG27 | UBIA1_RAT | MAAVQAPGEKINIQAGETTQVGDTDQQRNDWPEEDRLPERSWRQKCASYVLALRPWSFSASLTPVALGSALAYRSQGVLDPRLLLGCAVAVLAVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDRILEPQDVVRFGVFLYTLGCVCAAYLYYLSTLKLEHLALIYFGGLSGSFLYTGGIGFKYVALGDLVILITFGPLAVMFAYAVQVGSLAIFPLVYAIPLALSTEAILHSNNTRDMESDREAGIVTLAILIGPTLSYILYNTLLFLPYLIFTILATHCSISLALPLLTSPMAFSLERQFRSQAFNKLPQRTAKLNLLLG... | 2.5.1.-; 2.5.1.39 | null | circulatory system development [GO:0072359]; endothelial cell development [GO:0001885]; menaquinone biosynthetic process [GO:0009234]; phylloquinone biosynthetic process [GO:0042372]; ubiquinone biosynthetic process [GO:0006744]; ubiquinone biosynthetic process via 3,4-dihydroxy-5-polyprenylbenzoate [GO:0032194]; vitam... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | 4-hydroxybenzoate decaprenyltransferase activity [GO:0002083]; antioxidant activity [GO:0016209]; prenyltransferase activity [GO:0004659] | PF01040; | 1.10.357.140; | UbiA prenyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000... | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + menadiol = diphosphate + menaquinol-4; Xref=Rhea:RHEA:74083, ChEBI:CHEBI:6746, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:193091; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74084; Evidence={EC... | null | PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000250|UniProtKB:Q9Y5Z9}.; PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000250|UniProtKB:Q9Y5Z9}. | null | null | FUNCTION: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquin... | Rattus norvegicus (Rat) |
D3ZG83 | M3K10_RAT | MEEEEGAAAREWGATPAGPVWTAVFDYEAVGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPAAPAAPTDLQLPQEIPFHELQLEEIIGVGGFGKVYRALWRGEEVAVKAARLDPERDPAVTAEQVRQEARLFGALQHPNIIALRGACLSPPNLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKL... | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | negative regulation of DNA-templated transcription [GO:0045892]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; positive regulation of JNK cascade [GO:0046330]; smoothened signaling pathway [GO:0007224] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; bHLH transcription factor binding [GO:0043425]; JUN kinase kinase kinase activity [GO:0004706]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transcription corepressor activity [GO:0003714] | PF07714;PF14604; | 2.30.30.40;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. {ECO:0000250}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Activates the JUN N-terminal pathway. {ECO:0000250}. | Rattus norvegicus (Rat) |
D3ZGB1 | NFAT5_RAT | MPSDFISLLSADLDLESPKSLYSRDSLKLHPSQNFHRAGLLEESVYDLLPKELQLPPPRETSAASMSQTSGGEAGSPPPAVVAADASSAPSSSMGGACSSFTTSSSPTIYSTSVTDSKAMQVESCSSAVGVSNRGVSEKQLTGNTVQQHPSTPKRHTVLYISPPPEDLLDNSRMSCQDEGCGLESEQSCSMWMEDSPSNFSNMSTSSYNDNTEVPRKSRKRNPKQRPGVKRRDCEESNMDIFDADSAKAPHYVLSQLTTDNKGNSKAGNGTLDSQKGTGVKKSPMLCGQYPVKSEGKELKIVVQPETQHRARYLTEGSRG... | null | null | calcineurin-NFAT signaling cascade [GO:0033173]; cellular response to cytokine stimulus [GO:0071345]; DNA damage response [GO:0006974]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of gene expression [GO:0010628]; positive regulation of leukocyte adhesion to vascular ... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequenc... | PF16179;PF00554; | 2.60.40.10;2.60.40.340; | null | PTM: Phosphorylated. Phosphorylated at Thr-152 by CDK5 in response to osmotic stress; this phosphorylation mediates its rapid nuclear localization. {ECO:0000250|UniProtKB:O94916}.; PTM: Poly-ADP-ribosylated by PARP1 in response to DNA damage, promoting recruitment to sites of R-loop-associated DNA damage. {ECO:0000250|... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23233732}. Cytoplasm {ECO:0000269|PubMed:23233732}. Chromosome {ECO:0000250|UniProtKB:O94916}. Note=Nuclear distribution increases under hypertonic conditions (By similarity). Recruited to sites of R-loop-associated DNA damage following poly-ADP-ribosylation by PARP1 (B... | null | null | null | null | null | FUNCTION: Transcription factor involved, among others, in the transcriptional regulation of osmoprotective and inflammatory genes (PubMed:23233732). Binds the DNA consensus sequence 5'-[ACT][AG]TGGAAA[CAT]A[TA][ATC][CA][ATG][GT][GAC][CG][CT]-3'. Mediates the transcriptional response to hypertonicity. Positively regulat... | Rattus norvegicus (Rat) |
D3ZGQ5 | NEK8_RAT | MEKYERIRVVGRGAFGIVHLCLRKADQKLVIIKQIPVEQMTKEERQAAQNECQVLKLLNHPNVIEYYENFLEDKALMIAMEYAPGGTLAEFIQKRCNSLLEEETILHFFVQILLALHHVHTHLILHRDLKTQNILLDKHRMVVKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMSGTFAPISDRYSPELRQLVLSLLSLEPAQRPPLSHIMAQPLCIRALLNIHTDVGSVRMRRAEKCLTPGTPMAPGSTGSRATSARCRGVPRGPVRPAIPPPLSSV... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | animal organ morphogenesis [GO:0009887]; determination of left/right symmetry [GO:0007368]; heart development [GO:0007507]; phosphorylation [GO:0016310]; regulation of hippo signaling [GO:0035330] | centrosome [GO:0005813]; ciliary base [GO:0097546]; ciliary inversin compartment [GO:0097543]; cilium [GO:0005929]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF00415; | 2.130.10.30;1.10.510.10; | Protein kinase superfamily, NEK Ser/Thr protein kinase family, NIMA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91ZR4}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91ZR4}. Cell projection, cilium {ECO:0000250|UniProtKB:Q91ZR4}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q86SG6}. Note=Predominantly cytoplasmic. Localizes to ... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Required for renal tubular integrity. May regulate local cytoskeletal structure in kidney tubule epithelial cells. May regulate ciliary biogenesis through targeting of proteins to the cilia. Plays a role in organogenesis and is involved in the regulation of the Hippo signaling pathway (By similarity). {ECO:00... | Rattus norvegicus (Rat) |
D3ZGS3 | OCRL_RAT | MEPRLPIGAQPLACLHMVAGLEMKGPLREPCVLTLARRNGQYELIIQLHGKEQHVQDIIPINSHFRCVQEAEETLLIDIASNSGCKIRVQGDWTRERHFEIPDEERCLKFLSEVLAAQEAQSQLLVPEQKDSSNWYQKLDTKDKPAYSGLLGFEDNFSSMNLDKKMNTQNPPTGIHREPPPPPSSNRMLPREKEALNKEQPKVTNTMRKLFAPNSQSGQREGLIKHILAKREKEYVNIQSFRFFVGTWNVNGQSPDSSLEPWLNCDPNPPDIYCIGFQELDLSTEAFFYFESVKEQEWAMAVERGLPSKAKYKKVQLVRL... | 3.1.3.36; 3.1.3.56; 3.1.3.86 | null | cilium assembly [GO:0060271]; in utero embryonic development [GO:0001701]; phosphatidylinositol dephosphorylation [GO:0046856]; signal transduction [GO:0007165] | clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; membrane [GO:0016020]; nucleus [GO:0005634]; phagocytic vesicle membrane [GO:0030670]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]... | GTPase activator activity [GO:0005096]; inositol phosphate phosphatase activity [GO:0052745]; inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity [GO:0052659]; inositol-1,4,5-trisphosphate 5-phosphatase activity [GO:0052658]; inositol-polyphosphate 5-phosphatase activity [GO:0004445]; phosphatidylinositol-3,4,5-t... | PF21310;PF16726;PF00620; | 2.30.29.110;3.60.10.10;2.60.40.10;1.10.555.10; | Inositol 1,4,5-trisphosphate 5-phosphatase type II family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q01968}. Early endosome membrane {ECO:0000250|UniProtKB:Q01968}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q01968}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q01968}. Cell projection, cilium... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000250|UniP... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of the 5-position phosphate of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol-3,4,5-bisphosphate (PtdIns(3,4,5)P3), with the greatest catalytic activity towards PtdIns(4,5)P2. Able also to hydrolyze the 5-phosphate of inositol 1,4,5-trisphosphate and of... | Rattus norvegicus (Rat) |
D3ZHA0 | FLNC_RAT | MMNNSNYSDASGLGLLDEADEMPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVQNAREAMQQADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPVRSKQLNPKKAIAYGPGIEPQGNTVLQPAHFTVQTVDAGVGEVLVYIEDPEG... | null | null | muscle cell development [GO:0055001]; sarcomere organization [GO:0045214] | costamere [GO:0043034]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; sarcolemma [GO:0042383]; sarcoplasm [GO:0016528]; Z disc [GO:0030018] | actin filament binding [GO:0051015]; ankyrin binding [GO:0030506]; cytoskeletal protein binding [GO:0008092] | PF00307;PF00630; | 1.10.418.10;2.60.40.10; | Filamin family | PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar... | null | null | null | null | null | FUNCTION: Muscle-specific filamin, which plays a central role in sarcomere assembly and organization. Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response ... | Rattus norvegicus (Rat) |
D3ZHH1 | DLL4_RAT | MTPGSRSACRWALLLLAVLWPQQRAAGSGIFQLRLQEFANERGMLANGRPCEPGCRTFFRICLKHYQATFSEGPCTFGNVSTPVLGTNSFVIRDKNSGSGRNPLQLPFNFTWPGTFSLNIQAWHTPGDDLRPETSPGNSLISQIIIQGSLAVGKNWKSDEQNNTLTRLRYSYRVVCSDNYYGDSCSRLCKKRDDHFGHYECQPDGSLSCLPGWTGKYCDQPICLSGCHEQNGYCSKPDECNCRPGWQGPLCNECIPHNGCRHGTCTIPWQCACDEGWGGLFCDQDLNYCTHHSPCKNGSTCSNSGPRGYTCTCLPGYTGE... | null | null | angiogenesis [GO:0001525]; aortic valve morphogenesis [GO:0003180]; blood vessel lumenization [GO:0072554]; blood vessel remodeling [GO:0001974]; branching involved in blood vessel morphogenesis [GO:0001569]; cardiac atrium morphogenesis [GO:0003209]; cardiac ventricle morphogenesis [GO:0003208]; cellular response to c... | plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; Notch binding [GO:0005112]; receptor ligand activity [GO:0048018] | PF01414;PF00008;PF12661;PF21795;PF07657; | 2.10.25.140;2.60.40.3510;2.10.25.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25700513}; Single-pass type I membrane protein {ECO:0000255|RuleBase:RU280815}. | null | null | null | null | null | FUNCTION: Involved in the Notch signaling pathway as Notch ligand. Activates NOTCH1 and NOTCH4 (PubMed:25700513). Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Essential for retinal progenitor proliferation. Required for suppressing rod fates in la... | Rattus norvegicus (Rat) |
D3ZHP7 | ULK3_RAT | MAGSGWGLPRLDGFILTERLGSGTYATVYKAYAKKATREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLKDFQWDNDNIYLIMEFCAGGDLSRFIHTRRILPEKVARVFMQQLASALQFLHERNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSPLYMAPEMVCRRQYDARVDLWSVGVILYEALFGQPPFASRSFSELEEKIRSNRVIELPLRPQLSLDCRDLLQRLLERDPSHRISFQDFFAHPWVDLEHMPSGESLAQATALVVEAVKKDQEGDAAAALSLYCKALDFFVPALHY... | 2.7.11.1 | null | autophagosome assembly [GO:0000045]; fibroblast activation [GO:0072537]; negative regulation of smoothened signaling pathway [GO:0045879]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of smoothened signaling pathway [GO:0045880]; protein autophosphorylation [GO:0046777]; regulation of autop... | autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF04212;PF00069; | 1.20.58.80;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily | PTM: Autophosphorylated. Autophosphorylation is blocked by interaction with SUFU (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to pre-autophagosomal structure during cellular senescence. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine protein kinase that acts as a regulator of Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative regulator of SHH signaling in the absence of SHH ligand: interacts with SUFU, thereby inactivating the protein kinase activity and preventing phosphorylation of GLI proteins (GLI1, GLI2... | Rattus norvegicus (Rat) |
D3ZHR2 | ABCD1_RAT | MPVLSTPSRPSRVTTLKRTAVVLALTAYGVHKIYPLVRQCLTPARGPQVPAGESTQEASGATTAKAGMNRVFLQRLLVLLRLLFPGVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFSWQLLQWLLIALPATFINSAIRYLEGQLALSFRSRLVAHAYGLYFSQQTYYRVSNMDGRLRNPDQSLTEDMVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAGTAWPSAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQHSYQDLASQINL... | 3.1.2.-; 7.6.2.- | null | fatty acid beta-oxidation [GO:0006635]; fatty acid elongation [GO:0030497]; fatty acid homeostasis [GO:0055089]; long-chain fatty acid catabolic process [GO:0042758]; long-chain fatty acid import into peroxisome [GO:0015910]; myelin maintenance [GO:0043217]; negative regulation of cytokine production involved in inflam... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; lysosomal membrane [GO:0005765]; mitochondrial membrane [GO:0031966]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | ABC-type fatty-acyl-CoA transporter activity [GO:0015607]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; enzyme binding [GO:0019899]; fatty acyl-CoA hydrolase activity [GO:0047617]; identical protein binding [GO:... | PF06472;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCD family, Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily | PTM: Tyrosine-phosphorylated. {ECO:0000269|PubMed:12176987}. | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33897}. Lysosome membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein {ECO:00002... | CATALYTIC ACTIVITY: Reaction=a very long-chain fatty acyl-CoA + H2O = a very long-chain fatty acid + CoA + H(+); Xref=Rhea:RHEA:67072, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950, ChEBI:CHEBI:138261; Evidence={ECO:0000250|UniProtKB:P33897}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | null | null | null | null | FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)-CoA from the cytosol to the peroxisome lumen (PubMed:12176987). Coupled to the ATP-dependent transporter activity has also a fatty acyl-CoA thioesterase activity (ACOT) and hydrol... | Rattus norvegicus (Rat) |
D3ZHS6 | BAP1_RAT | MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNSMFFAHQLIPNSCATHALLSVLLNCSNVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRVKYEARLHVLKGNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKPASSKSPFGLEAGRTPAASECTHTDGAEEVAGSC... | 3.4.19.12 | null | cell population proliferation [GO:0008283]; common myeloid progenitor cell proliferation [GO:0035726]; erythrocyte differentiation [GO:0030218]; erythrocyte maturation [GO:0043249]; gene expression [GO:0010467]; granulocyte differentiation [GO:0030851]; hematopoietic stem cell homeostasis [GO:0061484]; in utero embryon... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; PR-DUB complex [GO:0035517] | chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; cysteine-type deubiquitinase activity [GO:0004843]; histone H2A deubiquitinase activity [GO:0140950] | PF01088;PF18031; | 1.20.58.860;3.40.532.10; | Peptidase C12 family, BAP1 subfamily | PTM: Ubiquitinated: monoubiquitinated at multiple site of its nuclear localization signal (NLS) BY UBE2O, leading to cytoplasmic retention. Able to mediate autodeubiquitination via intramolecular interactions to couteract cytoplasmic retention. {ECO:0000250|UniProtKB:Q92560}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92560}. Nucleus {ECO:0000250|UniProtKB:Q92560}. Note=Mainly nuclear. Binds to chromatin. Localizes to the cytoplasm when monoubiquitinated by the E2/E3 hybrid ubiquitin-protein ligase UBE2O. {ECO:0000250|UniProtKB:Q92560}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q92560}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitina... | Rattus norvegicus (Rat) |
D3ZHV2 | MACF1_RAT | MSSSDEETLSERSCRSERSCRSERSYRSERSGSLSPCPPGDTLPWNLPLHEQKKRKSQDSVLDPAERAVVRVADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGESGDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAEDVDVPSPDEKSVITYVSSIYDAFPKVPEGGEGISATEVDSRWQEYQ... | null | null | cell migration [GO:0016477]; establishment or maintenance of cell polarity [GO:0007163]; Golgi to plasma membrane protein transport [GO:0043001]; intermediate filament cytoskeleton organization [GO:0045104]; mesoderm formation [GO:0001707]; positive regulation of axon extension [GO:0045773]; positive regulation of Wnt ... | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; intermediate filament [GO:0005882]; membrane [GO:0016020]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; ruffle membrane [GO:0032587] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; ATP hydrolysis activity [GO:0016887]; cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; microtubule binding [GO:0008017]; microtubule minus-end binding [GO:0051011]; structural molecule activity [GO:0005198] | PF00307;PF13499;PF02187;PF17902;PF00435;PF18373;PF21019;PF21020;PF21097; | 1.20.58.1060;1.20.58.60;1.10.418.10;1.10.238.10;3.30.920.20;2.30.30.40; | Plakin or cytolinker family | PTM: Phosphorylated on serine residues in the C-terminal tail by GSK3B. Phosphorylation inhibits microtubule-binding and this plays a critical role in bulge stem cell migration and skin wound repair. Wnt-signaling can repress phosphorylation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UPN3}. Cytoplasm {ECO:0000250|UniProtKB:Q9UPN3}. Golgi apparatus {ECO:0000250|UniProtKB:Q9UPN3}. Cell membrane {ECO:0000250|UniProtKB:Q9UPN3}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9UPN3}. Membrane {ECO:0000269|PubMed:16815997}. N... | null | null | null | null | null | FUNCTION: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). Acts as a positive regulator of Wnt receptor signaling pathway and is in... | Rattus norvegicus (Rat) |
D3ZI76 | GPAT2_RAT | METMLKSNPQMQQRNNHSGQETSLWSSGFGMKMEAITPFLGKYRPFMGRCCQTCTPKSWESLFHRSIMDLGFCNVILVKEENTRFRGWLVRRLCYFLWSLEQHIPTSSDASQMIMENTGVQNILLGKVPGAAGEGQAPDLVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVHKAAQEGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVLRVALDSRTCSPALRALLRKLGGLFLPPEANLSLDSSEGILARAVVRATVEQLLTSGQPLLIFLEEAPGYPGPRLSALGQAWLGLVVQAVQAGIV... | 2.3.1.15; 2.3.1.51 | null | CDP-diacylglycerol biosynthetic process [GO:0016024]; fatty acid metabolic process [GO:0006631]; glycerol-3-phosphate metabolic process [GO:0006072]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid biosynthetic process [GO:0008654]; piRNA processing [GO:0034587]; triglyceride biosynthetic process [GO:... | mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | 1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841]; glycerol-3-phosphate O-acyltransferase activity [GO:0004366]; sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity [GO:0102420] | PF01553;PF19277; | null | GPAT/DAPAT family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:22905194}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q14DK4}. | CATALYTIC ACTIVITY: Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287, ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15; Evidence={ECO:0000250|UniProtKB:Q14DK4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326; ... | null | PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. {ECO:0000250|UniProtKB:Q14DK4}. | null | null | FUNCTION: Transfers an acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate producing a lysophosphatidic acid (LPA), an essential step for the triacylglycerol (TAG) and glycerophospholipids. In vitro also transfers an acyl-group from acyl-ACP to the LPA producing a phosphatidic acid (PA). Prefers arach... | Rattus norvegicus (Rat) |
D3ZID8 | UBX2A_RAT | MKEVDNLDSIKEEWVCETGPPDNQPLNDNPQKDCEYFVDSLFEEAEKAGAKCLSPTEQKKQVDVNIKLWKNGFTVNDDFRSYSDGASQQFLNSIKKGELPSELQGVFDKDEVDVKVEDKKNEVCMSTKPVFQPFSGQGHRLGSATPRIVSKAKSIEVDNKSTLSAVSLNNLEPITRIQIWLANGERTVQRFNISHRVSHIKDFIEKYQGTQRSPPFALATALPFLRFLDETLTLEEADLQNAVIIQRLQKTAEPFRKL | null | null | autophagosome assembly [GO:0000045]; cellular response to leukemia inhibitory factor [GO:1990830]; Golgi organization [GO:0007030]; membrane fusion [GO:0061025]; negative regulation of ERAD pathway [GO:1904293]; negative regulation of proteolysis [GO:0045861]; nuclear membrane reassembly [GO:0031468]; positive regulati... | cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; perikaryon [GO:0043204] | acetylcholine receptor binding [GO:0033130]; ubiquitin binding [GO:0043130] | PF08059;PF00789; | 3.30.420.210; | null | PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q99KJ0}. | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:19474315}. Endoplasmic reticulum {ECO:0000269|PubMed:19474315}. Perikaryon {ECO:0000250|UniProtKB:Q99KJ0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99KJ0}. Nucleus {ECO:0000250|UniProtKB:P68543}. Cytoplasm {ECO:0000269|PubMed:19474315}. Note=Expressed a... | null | null | null | null | null | FUNCTION: Acts to repress the ubiquitination and subsequent endoplasmic reticulum-associated degradation of CHRNA3 by the STUB1-VCP-UBXN2A complex in cortical neurons (PubMed:26265139). Also acts to promote the translocation of CHRNA3 to the plasma membrane and subsequently increases plasma membrane acetylcholine-gated... | Rattus norvegicus (Rat) |
D3ZIE4 | FYB1_RAT | MDGKTDVKSLMAKFNTGSNPTEEVSTSSRPFKVAGQNSPSGIQSKKNLFDNQGNASPPAGPSNMSKFGTTKPPLAAKPTYEEKSEKEPKPPFLKPTGVSPRFGTQPNSVSRDPEVKVGFLKPVSPKPTSLTKEDSKPVILRPPGNKLHNLNQESDLKTLGPKPGSTPPVPENDLKPGFSKIAGAKSKFMPAPQDADSKPRFPRHTYGQKPSLSTEDAQEEESIPKNTPVQKGSPVQLGAKSRGSPFKPAKEDPEDKDHGTPSSPFAGVVLKPAASRGSPGLSKNSEEKKEERKTDIPKNIFLNKLNQEEPARFPKAPSKL... | null | null | integrin-mediated signaling pathway [GO:0007229]; protein localization to plasma membrane [GO:0072659]; T cell receptor signaling pathway [GO:0050852] | anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | lipid binding [GO:0008289]; protein-containing complex binding [GO:0044877] | PF14603;PF07653; | 2.30.30.40; | null | PTM: T-cell receptor ligation leads to increased tyrosine phosphorylation. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15117}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell junction {ECO:0000250|UniProtKB:O35601}. Note=Colocalizes with TMEM47 at cell-cell contacts in podocytes. {ECO:0000250|UniProtKB:O35601}. | null | null | null | null | null | FUNCTION: Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (By similarity). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degr... | Rattus norvegicus (Rat) |
D3ZJ25 | AAAT_RAT | MAVDPPKADPKGVVAVDPTANCGSGLKSREDQGAKAGGCCSSRDQVCRCLRANLLVLLTVAAAVAGVVLGLGVSAAGGAEALGHARFTAFAFPGELLLRLLEMIILPLVVCSLIGGAASLDPSALGRLGAWALLFFLVTTLLSSALGVALALALKPGAAFAAINSSVVDSSVHRAPTKEVLDSFLELLRNMFPSNLVSASAAFRIFATSYVSKDINTSGIHPCGACPQRSNATMDQPHCEMKMNILGLVVFAIVFGVALRKLGPEGELLIRFFNSFNDATMVLVSWIMWYAPIGILFLVAGKIVEMKDIRQLFIGLGKYI... | null | null | amino acid transmembrane transport [GO:0003333]; erythrocyte differentiation [GO:0030218]; glutamine secretion [GO:0010585]; glutamine transport [GO:0006868]; L-aspartate import across plasma membrane [GO:0140009]; L-glutamine import across plasma membrane [GO:1903803]; L-serine transport [GO:0015825]; neutral amino ac... | basal plasma membrane [GO:0009925]; melanosome [GO:0042470]; membrane [GO:0016020]; plasma membrane [GO:0005886] | antiporter activity [GO:0015297]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamine transmembrane transporter activity [GO:0015186]; L-serine transmembrane transporter activity [GO:0015194]; ligand-gated channel activity [GO:0022834]; metal ion binding [GO:0046872]; neutral L-amino acid transmemb... | PF00375; | 1.10.3860.10; | Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15758}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:Q15758}. | CATALYTIC ACTIVITY: Reaction=L-glutamine(out) + L-serine(in) + Na(+)(out) = L-glutamine(in) + L-serine(out) + Na(+)(in); Xref=Rhea:RHEA:70855, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + L-serine(out) + Na(+)(out) = L-g... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for Na(+) {ECO:0000269|PubMed:10698697}; KM=40 uM for thiocyanate (at -60 mV) {ECO:0000269|PubMed:10698697}; KM=90 uM for thiocyanate (at -20 mV) {ECO:0000269|PubMed:10698697}; | null | null | null | FUNCTION: Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (By similarity) (PubMed:10698697). The preferred substrate is the essential... | Rattus norvegicus (Rat) |
D3ZJ86 | SL9A6_RAT | MTSPKPWARSAGSCQTQRAVRTRKKECREEGESDTEKGPAASSASAQCSFPKRVSFFGWAGALDSSGGTTRAMDEEIVSEKQAEESHRQDSANLLIFILLLTLTILTIWLFKHRRARFLHETGLAMIYGLLVGLVLRYGIHVPSDVNNVTLSCEVQSSPTTLLVNVSGKFYEYTLKGEISSHELNNVQDNEMLRKVTFDPEVFFNILLPPIIFYAGYSLKRRHFFRNLGSILAYAFLGTAISCFVIGSIMYGCVTLMKVTGQLAGDFYFTDCLLFGAIVSATDPVTVLAIFHELQVDVELYALLFGESVLNDAVAIVLSS... | null | null | axon extension [GO:0048675]; brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; dendrite extension [GO:0097484]; dendritic spine development [GO:0060996]; establishment of cell polarity [GO:0030010]; glial cell activation [GO:0061900]; neuron projection morphogenesis [GO:0048812]; potassium ion ... | axon terminus [GO:0043679]; axonal spine [GO:0044308]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; glutamatergic synapse [GO:0098978]; late endosome [GO:0005770]; late endo... | identical protein binding [GO:0042802]; potassium:proton antiporter activity [GO:0015386]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | PTM: Ubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q92581}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q92581}. | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q92581}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q92581}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q92581}; Multi-pass membrane protein {ECO:0000250|UniPr... | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q92581}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence=... | null | null | null | null | FUNCTION: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A6 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Responsible for alkalizing and maintainin... | Rattus norvegicus (Rat) |
D3ZJ96 | UBP28_RAT | MTAELQQDDAAGAADGHGSSCQMLLNQLREITGIQDPSFLHEALKASNGDITQAVSLLTDQRVKEPSHDTAATEPSEVEESATSKDLLAKVIDLTHDNKDDLQAAIALSLLESPNIQTDSRDLNRIHEANSAETKRSKRKRCEVWGENHNPNNWRRVDGWPVGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSLPQNILENCRSHTEKRNIMFMQELQYLFALLLGSNRKFVDPSAALDLLKGAFRSSEEQQQDVSEFTHKLLDWLEDAFQLAVNVNSNPRTKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQ... | 3.4.19.12 | null | cell population proliferation [GO:0008283]; cellular response to UV [GO:0034644]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; protein deubiquitination [GO:0016... | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | cysteine-type deubiquitinase activity [GO:0004843]; deubiquitinase activity [GO:0101005] | PF00443; | 6.10.250.1720;3.90.70.10;1.10.8.10; | Peptidase C19 family, USP28 subfamily | PTM: Degraded upon nickel ion level or hypoxia exposure. {ECO:0000250}.; PTM: Phosphorylated upon DNA damage at Ser-67 and Ser-720, by ATM or ATR. Phosphorylated by PRKD1. {ECO:0000250|UniProtKB:Q96RU2}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; | null | null | null | null | FUNCTION: Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degra... | Rattus norvegicus (Rat) |
D3ZJP6 | MYO10_RAT | MDSFFPEGARVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITNQKVTAMHPLHEEGVDDMASLTELHGGSIMYNLFQRYKRNQIYTYIGSIIASVNPYQPIAGLYERATMEQYSRCHLGELPPHIFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSVISQHSLDLCLQEKSSSVEQAILQSSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLDQGEREEFYLSLPENYHYLNQSGCTEDKTISDQESFRQVIEAMEVMQFSK... | null | null | cytoskeleton-dependent intracellular transport [GO:0030705]; positive regulation of cell-cell adhesion [GO:0022409]; regulation of cell shape [GO:0008360]; regulation of filopodium assembly [GO:0051489] | cell cortex [GO:0005938]; cytosol [GO:0005829]; filopodium [GO:0030175]; filopodium membrane [GO:0031527]; filopodium tip [GO:0032433]; lamellipodium [GO:0030027]; myosin complex [GO:0016459]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; ruffle [GO:0001726] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; plus-end directed microfilament motor activity [GO:0060002]; spectrin binding [GO:0030507] | PF00373;PF00612;PF16735;PF00063;PF00784;PF00169;PF18597; | 1.10.10.820;1.20.5.170;1.20.5.190;1.20.58.530;1.20.80.10;6.20.240.20;3.40.850.10;1.20.120.720;1.25.40.530;2.30.29.30; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, filopodium tip {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, filopodium membrane {ECO:0000250}; Per... | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments ... | Rattus norvegicus (Rat) |
D3ZKB9 | TSH3_RAT | MAAYVSDELKAAALVEDDIEPEEQVADGEPSAKYMCPEKELSKACPSYQNSPAAEFSSHEMDSESHISETSDRMADFESSSIKNEEETKEVQVPLEDTTVSDSLEQMKAVYNNFLSNSYWSNLNLNLHQPSSENNGGGSSSSSSSSSSSCGSGSFDWHQSAMAKTLQQVSQNRMLPEPSLFSTVQLYRQSSKLYGSIFTGASKFRCKDCSAAYDTLVELTVHMNETGHYRDDNHETDNNNPKRWSKPRKRSLLEMEGKEDAQKVLKCMYCGHSFESLQDLSVHMIKTKHYQKVPLKEPVTPVAAKIIPAARKKPSLELEL... | null | null | in utero embryonic development [GO:0001701]; kidney morphogenesis [GO:0060993]; kidney smooth muscle cell differentiation [GO:0072195]; long-term synaptic potentiation [GO:0060291]; lung development [GO:0030324]; metanephros development [GO:0001656]; musculoskeletal movement [GO:0050881]; negative regulation of DNA-tem... | growth cone [GO:0030426]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872] | PF13912; | 3.30.160.60; | Teashirt C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:19343227}. Cell projection, growth cone {ECO:0000269|PubMed:19343227}. Note=Colocalizes with APBB1 in the nucleus (By similarity). Colocalizes with APBB1 in axonal growth cone. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcriptional regulator involved in developmental processes. Functions in association with APBB1, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. TSHZ3-mediated transcription repression involves the recruitment of histone deacetylases HDAC1 and HDAC2. Associates w... | Rattus norvegicus (Rat) |
D3ZKD3 | ALKB5_RAT | MAAASGYTDLREKLKSMTSRDNYKAGSREAAAAAAAAVAAAAAAAAAAEPYPVSGTTKRKYQEDSDPERSDYEEHQLQKEEEARKVKSGIRQIRLFSQDECSKIEARIDEVVSRAEKGLYNEHTVDRAPLRNKYFFGEGYTYGAQLQKRGPGQERLYPPGDVDEIPEWVHQLVIQKLVEHRVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVLSLPVRRGSVTVLSGYAADEITHCIRPQDIKERRAVIILRKTRLDAPRLETKSLSSSTLPPSYASDRLSGNTRDPA... | 1.14.11.53 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6P6C2}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6P6C2}; | cell differentiation [GO:0030154]; gamma-delta T cell proliferation [GO:0046630]; mRNA destabilization [GO:0061157]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; non-membrane-bounded organelle assembly [GO:0140694]; oxidative single-stranded RNA demethylation [GO:0035553]; regulation of mRNA sta... | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; paraspeckles [GO:0042382] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; metal ion binding [GO:0046872]; molecular condensate scaffold activity [GO:0140693]; mRNA N6-methyladenosine dioxygenase activity [GO:1990931]; oxidative RNA demethylase activity [GO:0035515] | PF13532; | 2.60.120.590; | AlkB family | PTM: Phosphorylated at Ser-88 and Ser-326 in response to reactive oxygen species (ROS), promoting sumoylation and inactivation. {ECO:0000250|UniProtKB:Q6P6C2}.; PTM: Acetylated by KAT8 at Lys-236, promoting interaction with PSPC1, thereby facilitating recognition of N(6)-methyladenosine (m6A) mRNA by ALKBH5. Deacetylat... | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q6P6C2}. Note=Promotes formation and localizes to paraspeckles, a nuclear membraneless organelle. {ECO:0000250|UniProtKB:Q6P6C2}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an N(6)-methyladenosine in mRNA + O2 = an adenosine in mRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:49520, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411, ... | null | null | null | null | FUNCTION: Dioxygenase that specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (By similarity). Demethylates RNA by oxidative demethylation, which requires molecular oxygen, alpha-ketoglutarate and iron (By similarity). Demethyl... | Rattus norvegicus (Rat) |
D3ZKX9 | LOXE3_RAT | MAVYRLCVTTGSYLKAGTLDNIYATLVGTCGESPKQKLDRVGRDFATGSVQKYKVRCASELGEILLLRLHKERFAFFCKDPWYCSRICVTTPDGSVVHFPCYQWIDGYCTVELRPGTARTICQDALPLLLDHRKRELQARQECYRWKIYAPGFPRMVDVSSFEEMESDKKFALTKTAPCADQDDNSGNRYLPGFPMKVDIPSLLHMEPNIRYSATKTASLIFNALPASLGMKIRGLLDRKGSWKRLDDIRNIFWCHKTFTSEYVTEHWCEDSFFGYQYLNGVNPIMLHCLSSLPSKLPVTNDMVAPLLGPGTCLQTELER... | 4.2.1.152; 5.4.4.7 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726}; | arachidonic acid metabolic process [GO:0019369]; ceramide biosynthetic process [GO:0046513]; establishment of skin barrier [GO:0061436]; fat cell differentiation [GO:0045444]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [G... | cytoplasm [GO:0005737] | hepoxilin A3 synthase activity [GO:0051120]; hydroperoxy icosatetraenoate dehydratase activity [GO:0106256]; hydroperoxy icosatetraenoate isomerase activity [GO:0106255]; intramolecular hydroxytransferase activity [GO:0050486]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on single donors with incorpo... | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. | CATALYTIC ACTIVITY: Reaction=a hydroperoxyeicosatetraenoate = a hydroxy-epoxy-eicosatetraenoate; Xref=Rhea:RHEA:55560, ChEBI:CHEBI:59720, ChEBI:CHEBI:137328; EC=5.4.4.7; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55561; Evidence={ECO:0000250|UniProtKB:Q9BYJ1}; CATALYTI... | null | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000250|UniProtKB:Q9BYJ1}.; PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000250|UniProtKB:Q9BYJ1}. | null | null | FUNCTION: Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxil... | Rattus norvegicus (Rat) |
D3ZLB7 | FOSB_RAT | MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPAVDPYDMPGTSYSTPGLSAYSTGGASGSGGPSTSTSTSGPVSARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSTSAKEDGFGWLLPPPPPPPLPFQSSRDAPPNLTASLFTHSEVQVLGDPFPVVSPSYTSSFVLTCPEVSAFAGSQRT... | null | null | behavioral response to cocaine [GO:0048148]; cellular response to calcium ion [GO:0071277]; cellular response to hormone stimulus [GO:0032870]; female pregnancy [GO:0007565]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response t... | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; RNA polymerase II cis-reg... | PF00170; | 1.20.5.170; | BZIP family, Fos subfamily | PTM: Phosphorylated; phosphorylation is induced by chronic electroconvulsive seizure (ECS) treatment. {ECO:0000269|PubMed:16687504}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P13346}. | null | null | null | null | null | FUNCTION: Heterodimerizes with proteins of the JUN family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing their transcriptional activity (By similarity). Exhibits transactivation activity in vitro (By similarity). As... | Rattus norvegicus (Rat) |
D3ZLH5 | PLXB3_RAT | MLTDFLQAPVMAPWSPFSLHLLLLFLLLLPLTRAHRFSVPNASFNHLVLAPDQGKLYVGAVNHLFQLSPELEMESVAITGPVIDSPDCVPFRDLAECPQAQLTDNANQLLLVSSRAQELVACGQVRQGVCEKRRLGDVTQVLYQAEDPGDGQFVAANTLGVTTVGLVVPLPGRDLLLVARGLAGKLSAGVPPLTVRQLAGPQPFSSEGLGRLVVGDFSDYNNSYVGAFSDAHSAYFVFRRRGARAQTEYRSYVARVCLGDVNLYSYVEVPLTCHGQGLIQAAFLAPDTLLGAFSAGTSQAQAALCAFPLADLDGSMEQAR... | null | null | cell chemotaxis [GO:0060326]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell migration [GO:0030336]; negative regulation of GTPase activity [GO:0034260]; negative regulation of lamellipodium assembly [GO:001059... | cell surface [GO:0009986]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116] | cell-cell adhesion mediator activity [GO:0098632]; protein domain specific binding [GO:0019904]; Rho GDP-dissociation inhibitor binding [GO:0051022]; semaphorin receptor activity [GO:0017154] | PF08337;PF20170;PF01437;PF01403;PF01833;PF18020;PF17960; | 2.60.40.10;2.130.10.10; | Plexin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ULL4}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9ULL4}. Note=Colocalizes with RIT2/RIN at the plasma membrane. {ECO:0000250|UniProtKB:Q9ULL4}. | null | null | null | null | null | FUNCTION: Receptor for SEMA5A that plays a role in axon guidance, invasive growth and cell migration. Stimulates neurite outgrowth and mediates Ca(2+)/Mg(2+)-dependent cell aggregation. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and c... | Rattus norvegicus (Rat) |
D3ZMK9 | PRAG1_RAT | MSACSDFVEHIWKPGSCKNCFCLRSDHQLTAGHPKARASSLPAGARLPARPEICRLEDEGVNGLAYSKPTIAVKPTMMTSETADLWTEASLSAEVPKVNWRRTPGKLLLQKQEDGPIVYLGSFRGMQKAAGPLACTDSNSRCPPAYTMVGLHNLEARVDRNTALQPVNFQEEKAGREELPSAQESFRQKLAAFTGMTSSCLKGPRPCTSPQPLRESLPSEDDSDQRCSPSGDSEGGEYCSILDCRPESRDAVHNTEGSGRRRGDCSPICWEQGTCTRPTEEEKQALNFPRECCGQGSTANPPHLGPKKPSLNSEAASSSD... | null | null | cell migration [GO:0016477]; negative regulation of neuron projection development [GO:0010977]; positive regulation of Rho protein signal transduction [GO:0035025]; regulation of cell motility [GO:2000145]; regulation of cell shape [GO:0008360]; regulation of Notch signaling pathway [GO:0008593] | cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; nucleus [GO:0005634] | identical protein binding [GO:0042802]; protein kinase activity [GO:0004672] | PF00069; | 1.10.510.10; | Protein kinase superfamily | PTM: Phosphorylated by CSK on Tyr-238, Tyr-343, and Tyr-391; Tyr-391 is a primary site of phosphorylation. {ECO:0000269|PubMed:27116701}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21873224, ECO:0000269|PubMed:27116701}. Nucleus {ECO:0000250|UniProtKB:Q571I4}. Cell junction, focal adhesion {ECO:0000269|PubMed:27116701}. Note=Colocalized with NOTCH1 in the nucleus. {ECO:0000250|UniProtKB:Q571I4}. | null | null | null | null | null | FUNCTION: Catalytically inactive protein kinase that acts as a scaffold protein (PubMed:29503074). Functions as an effector of the small GTPase RND2, which stimulates RhoA activity and inhibits NGF-induced neurite outgrowth (PubMed:16481321). Promotes Src family kinase (SFK) signallig by regulating the subcellular loca... | Rattus norvegicus (Rat) |
D3ZML2 | BRSK2_RAT | MTSTGKDGGGAQHAQYVGPYRLEKTLGKGQTGLVKLGIHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDERNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLL... | 2.7.11.1; 2.7.11.26 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | actin cytoskeleton organization [GO:0030036]; axonogenesis [GO:0007409]; cell division [GO:0051301]; DNA damage response [GO:0006974]; ERAD pathway [GO:0036503]; establishment of cell polarity [GO:0030010]; exocytosis [GO:0006887]; G2/M transition of mitotic cell cycle [GO:0000086]; intrinsic apoptotic signaling pathwa... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; distal axon [GO:0150034]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | ATP binding [GO:0005524]; ATPase binding [GO:0051117]; magnesium ion binding [GO:0000287]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321] | PF00069;PF21115; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily | PTM: May be phosphorylated at Thr-261 by PKA (By similarity). Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-175 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin (By si... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neuro... | Rattus norvegicus (Rat) |
D3ZMM8 | YLAT2_RAT | MEARELGSPTPTYHLLPKANQHTVKEDASSPSQGSPETMQLKKEISLLNGVSLVVGNMIGSGIFVSPKGVLKYTASYGLSLVVWAIGGLFSVVGALCYAELGTTITKSGASYAYILEAFGGFIAFIRLWVSLLIVEPTSQAIIAITFANYIIKPSFPTCDPPYVACRLLAAACVCLLTFVNCAYVKWGTRVQDTFTYAKVLALIAIIIMGLVKLCQGHTEHFQDAFKGSSWNVGDLSLALYSALFSYSGWDTLNFVTEEIKNPERNLPLAIGISMPIVTLIYILTNVAYYTVLNIQDVHKSDAVAVTFADQTFGMFSWTI... | null | null | amino acid transmembrane transport [GO:0003333]; glycine betaine transport [GO:0031460]; L-arginine transmembrane transport [GO:1903826]; leucine transport [GO:0015820]; neutral amino acid transport [GO:0015804]; nitric oxide biosynthetic process [GO:0006809]; ornithine transport [GO:0015822] | plasma membrane [GO:0005886] | arginine binding [GO:0034618]; basic amino acid transmembrane transporter activity [GO:0015174]; L-amino acid transmembrane transporter activity [GO:0015179]; L-arginine transmembrane transporter activity [GO:0061459]; L-lysine:L-arginine antiporter activity [GO:0106439] | PF13520; | 1.20.1740.10; | Amino acid-polyamine-organocation (APC) superfamily, L-type amino acid transporter (LAT) (TC 2.A.3.8) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92536}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=L-arginine(in) + L-lysine(out) = L-arginine(out) + L-lysine(in); Xref=Rhea:RHEA:70827, ChEBI:CHEBI:32551, ChEBI:CHEBI:32682; Evidence={ECO:0000250|UniProtKB:Q92536}; CATALYTIC ACTIVITY: Reaction=L-arginine(in) + L-leucine(out) + Na(+)(out) = L-arginine(out) + L-leucine(in) + Na(+)(in); Xref... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=55.82 uM for L-arginine {ECO:0000269|PubMed:22401943}; KM=71.06 uM for L-arginine (in astrocytes treated with ammonium chloride) {ECO:0000269|PubMed:22401943}; Vmax=1.301 nmol/min/mg enzyme toward L-arginine {ECO:0000269|PubMed:22401943}; Vmax=1.82 nmol/min/mg enzy... | null | null | null | FUNCTION: Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux routeby exporting cationic amino acids such as L-arginine from inside the cells in exchange with neutral amino acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and may participate in nitric oxide synthesis (... | Rattus norvegicus (Rat) |
D3ZMY7 | 5NTC_RAT | MMTSWSDRLQNAADVPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLNFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCDTGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGP... | 2.7.1.77; 3.1.3.5; 3.1.3.99 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:6260203}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P49902}; | adenosine metabolic process [GO:0046085]; allantoin metabolic process [GO:0000255]; amide catabolic process [GO:0043605]; dGMP catabolic process [GO:0046055]; dGMP metabolic process [GO:0046054]; GMP catabolic process [GO:0046038]; GMP catabolic process to guanine [GO:0006202]; GMP metabolic process [GO:0046037]; IMP c... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | 5'-nucleotidase activity [GO:0008253]; ATP binding [GO:0005524]; GMP 5'-nucleotidase activity [GO:0050484]; identical protein binding [GO:0042802]; IMP 5'-nucleotidase activity [GO:0050483]; metal ion binding [GO:0046872]; nucleoside phosphotransferase activity [GO:0050146]; ubiquitin protein ligase activity [GO:006163... | PF05761; | 3.40.50.1000; | 5'(3')-deoxyribonucleotidase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49902}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence={ECO:0000269|PubMed:6260203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485; Evidence={ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for IMP {ECO:0000269|PubMed:6260203}; KM=0.7 mM for dIMP {ECO:0000269|PubMed:6260203}; KM=0.7 mM for GMP {ECO:0000269|PubMed:6260203}; KM=1.1 mM for dGMP {ECO:0000269|PubMed:6260203}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:6260203}; | null | FUNCTION: Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates (PubMed:6260203). In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferab... | Rattus norvegicus (Rat) |
D3ZN95 | HCFC1_RAT | MASAVSPANLPAVLLQPRWKRVVGWSGPVPRPRHGHRAVAIKELIVVFGGGNEGIVDELHVYNTATNQWFIPAVRGDIPPGCAAYGFVCDGTRLLVFGGMVEYGKYSNDLYELQASRWEWKRLKAKTPKNGPPPCPRLGHSFSLVGNKCYLFGGLANDSEDPKNNIPRYLNDLYILELRPGSGVVAWDIPITYGVLPPPRESHTAVVYTEKDNKKSKLVIYGGMSGCRLGDLWTLDIETLTWNKPSLSGVAPLPRSLHSATTIGNKMYVFGGWVPLVMDDVKVATHEKEWKCTNTLACLNLDTMAWETILMDTLEDNIPR... | null | null | blastocyst hatching [GO:0001835]; cell cycle [GO:0007049]; cellular response to organic cyclic compound [GO:0071407]; chromatin remodeling [GO:0006338]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene ex... | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; histone acetyltransferase complex [GO:0000123]; histone methyltransferase complex [GO:0035097]; MLL1 complex [GO:0071339]; MLL1/2 complex [GO:0044665]; neuronal cell body [GO:0043025]; NSL complex [GO:0044545]; nuclear chromosome [GO:0000228]; nucleus [G... | chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription coacti... | PF01344;PF13415;PF13854; | 6.10.250.2590;2.60.40.10;2.120.10.80; | null | PTM: Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats. Further cleavage of the primary N- and C-terminal chains results in a 'trimming' and accumulation of the smaller chains. Cleavage is promoted by O-glycosylation. {ECO:0000250|UniProtKB:P51610}.; PTM: O-glycosylated. GlcNAcylation by... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51610}. Nucleus {ECO:0000250|UniProtKB:P51610}. Note=HCFC1R1 modulates its subcellular localization and overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm. Non-processed HCFC1 associates with chromatin. Colocalizes with CREB3 and CANX in the... | null | null | null | null | null | FUNCTION: Transcriptional coregulator (PubMed:24250814). Involved in control of the cell cycle (By similarity). Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300 (By similarity). Coactivator for EGR2 and GABP2 (By simila... | Rattus norvegicus (Rat) |
D3ZPG5 | UBP30_RAT | MLSSRAQAARTAADKALQRFLRTGAAVRYKVMKNWGVIGGIAAALAAGIYVIWGPITERKKRRKGLVPGLVNLGNTCFMNSLLQGLSACPAFVKWLEEFTTQYSRDQQGPHTHQCLSLTLLSLLKALSCQEVTEEEVLDASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRQPRVTHLFDVHSLEQQSEMAPRQVTCHTRGSPHPTTNPWKSQHPFHGRLSSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKGTQNGEKVEHQRTTFVKQLKLGKLPQC... | 3.4.19.12 | null | mitochondrial fusion [GO:0008053]; negative regulation of mitophagy [GO:1901525]; protein K11-linked deubiquitination [GO:0035871]; protein K6-linked deubiquitination [GO:0044313]; proteolysis [GO:0006508] | cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197] | PF00443; | 3.90.70.10; | Peptidase C19 family | PTM: Ubiquitinated by parkin (PRKN) at Lys-235 and Lys-289, leading to its degradation. {ECO:0000250|UniProtKB:Q70CQ3}. | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q70CQ3}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q70CQ3}; | null | null | null | null | FUNCTION: Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy (PubMed:... | Rattus norvegicus (Rat) |
D3ZPX4 | PLXA3_RAT | MHTVCLLPLLFFTIGGCLGSSRPFRTFVVTDTTLTHLAVHRVTGEVFVGAVNRVFKLASNLTELRAHVTGPIEDNARCYPPPSMRVCSHRLVPVDNVNKLLLIDYAARRLVACGSIWQGICQFLRLDDLFKLGEPHHRKEHYLSGAQEPDSMAGVIVEQGQGPSKLFVGTAVDGKSEYFPTLSSRKLIDDEDSGDMFSLVYQDEFVSSQIKIPSDTLSLYPAFDIYYIYGFVSASFVYFLTLQLDTQQTLLDTAGEKFFTSKIVRMCAGDSEFYSYVEFPIGCSWRGVEYRLVQSAHLAKPGLLLAQALGVPADEDVLFT... | null | null | axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; branchiomotor neuron axon guidance [GO:0021785]; facial nerve structural organization [GO:0021612]; gonadotrophin-releasing hormone neuronal migration to the hypothalamus [GO:0021828]; hippocampus development [GO:0021766]; negative chemo... | plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116] | semaphorin receptor activity [GO:0017154] | PF08337;PF20170;PF01437;PF01403;PF01833;PF18020;PF17960; | 2.60.40.10;2.130.10.10; | Plexin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance in the developing nervous system. Regulates the migration of sympathetic neurons, but not of neural crest precursors. Required for normal dendrite spine... | Rattus norvegicus (Rat) |
D3ZQF4 | FKBP6_RAT | MSVFSRLRNGIPPSRDDCQSPYERLSQRMLDISGDRGVLKDIIREGAGDPVTPDASVLVKYSGYLEHMDKPFDSNCFRKTPRLMKLGEDITLWGMELGLLSMRRGELARFLFKPTYAYGTLGCPPLIPPNATVLFEIELIDFLDSAESDKFCALSAEQQEQFPLQKVLKVAATEREFGNYLFRQNRFCDAKVRYKRALLLLHRRLAICEEQHLVEPAELLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYEQARDFLVRAQKEQPCNHDINNELKKLSSHYRDYVDREREMCHRMFAPCGS... | null | null | cell differentiation [GO:0030154]; meiotic cell cycle [GO:0051321]; piRNA processing [GO:0034587]; positive regulation of viral genome replication [GO:0045070]; protein folding [GO:0006457]; regulatory ncRNA-mediated gene silencing [GO:0031047]; siRNA-mediated retrotransposon silencing by heterochromatin formation [GO:... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; synaptonemal complex [GO:0000795] | Hsp90 protein binding [GO:0051879]; identical protein binding [GO:0042802] | PF00254; | 3.10.50.40;1.25.40.10; | FKBP6 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Does not localize to pi-bodies. Localizes to meiotic chromosome cores and regions of homologous chromosome synapsis (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Co-chaperone required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and P... | Rattus norvegicus (Rat) |
D3ZQF9 | LX12E_RAT | MGKYKILVVTGDSLLAGSTNLVQLWLVGEHAEADLGKQLRPLRGRKTELEIDVPLHLGRLLVVKLRKHKGLLDSDWFCKWITVQGPGIQGEAFFPCYSWVQGKETIYLPEGTALKVNDDTKNLFRKYREQELEDRRNVYRWGSWKEGLILPIAGSTERDLPRNQRFMEDKDLDFSLSLAKVLKDFAIKGTLDFVSRVQHLEDYQKVFPHSKTALAGRVRDSWKEDALFGYQFLNGANPMLLRRSKRLPARLVLPPGMEDLQTQLEKELKAGSLFEADFSLLDGVKPNVIIFKQQHVAAPLVMLKLQSDGRLLPMVIQLQP... | 1.13.11.-; 1.13.11.31 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726}; | arachidonic acid metabolic process [GO:0019369]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 15-lipoxygenase activity [GO:0050473]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:10428, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57444; EC=1.13.11.31; Evidence={ECO:0000269|PubMed:23382512}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10429; Evi... | null | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. | null | null | FUNCTION: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:23382512). Shows increasing catalytic activity within the series ... | Rattus norvegicus (Rat) |
D3ZQL6 | MILK1_RAT | MAGPRGALLAWCRRQCEGYRGVDIRDLSSSFRDGLAFCAILHRHRPDLLDFQSLSKENVFENNRLAFEVAEKELGIPALLDPNDMVSMSVPDCLSIMTYVSQYYNHFTSSGQAAASPPKPGKDPAAPSPTSTSPAVQPGEEAQGDDLSPDSLSEQGKPQPPSSACAACGQRVHLVQRYLAEGRLYHRHCFRCRQCSSTLVPGSYSSGPEEGTFVCAERCTRLGLGGRSGTRPLSLQKQQPAAAAEAKDGEDSDLSKSVVVVAAEADGLQASSEVQPHTLTKPPLPSKPQDLASPPVSRPTPAPRKASESSALTPPTPRPR... | null | null | actin cytoskeleton organization [GO:0030036]; cellular response to nerve growth factor stimulus [GO:1990090]; endocytic recycling [GO:0032456]; endocytosis [GO:0006897]; neuron projection development [GO:0031175]; plasma membrane tubulation [GO:0097320]; protein localization to endosome [GO:0036010]; protein targeting ... | cytoplasmic side of endosome membrane [GO:0010009]; endosome membrane [GO:0010008]; filamentous actin [GO:0031941]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; microtubule organizing center [GO:0005815]; recycling endosome membrane [GO:0055038] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphatidic acid binding [GO:0070300]; small GTPase binding [GO:0031267] | PF12130;PF00307;PF00412; | 1.10.418.10;2.10.110.10; | null | null | SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Late endosome membrane {ECO:0000250}. Note=Localization to late endosomes is actin-dependent. Association to tubular recycling endosomes is regulated by RAB35 and ARF6 (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediate... | Rattus norvegicus (Rat) |
D3ZQL7 | TPPP_RAT | MADSKAKPTKAANKTPPKSPGDPAKAAKRLSLESEGANEGAAAAPELSALEEAFRRFAVHGDTRATGKEMHGKNWSKLCKDCHVIDGKNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGRAPVISGVTKAVSSPTVSRLTDTSKFTGSHKERFDQSGKGKGKAGRVDLVDESGYVPGYKHAGTYDQKVQGGK | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O94811}; | astral microtubule organization [GO:0030953]; cell division [GO:0051301]; microtubule bundle formation [GO:0001578]; microtubule nucleation by microtubule organizing center [GO:0051418]; microtubule polymerization [GO:0046785]; myelin assembly [GO:0032288]; negative regulation of tubulin deacetylation [GO:1904428]; oli... | cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic Golgi apparatus [GO:0150051] | GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; microtubule nucleator activity [GO:0140490]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; tubulin binding [GO:0015631] | PF05517; | 1.10.238.10; | TPPP family | PTM: Phosphorylated by LIMK1 on serine residues; phosphorylation may alter the tubulin polymerization activity. Phosphorylation by LIMK2, but not LIMK1, regulates astral microtubule organization at early stage of mitosis. Phosphorylation by ROCK1 at Ser-31, Ser-106 and Ser-158 inhibits interaction with HDAC6, resulting... | SUBCELLULAR LOCATION: Golgi outpost {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:31522887}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O94811}. Nucleus {ECO:0000250|UniProtKB:O94811}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O94811}. Note=S... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:O94811}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:O9481... | null | null | null | null | FUNCTION: Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath (PubMed:19606501). Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtub... | Rattus norvegicus (Rat) |
D3ZR10 | DCDC2_RAT | MNGPSPRSSHLSQPVVKSVLVYRNGDPFFAGRRVVIHEKKVSSFDIFLKEVTGGVQAPFGAVRNIYTPRTGHRIRKLDQIESGGNYVAGGQEAFKKLNYLDIGEIKKRPMEAVNTEVKPVIHSKINVSARFRKALHEPCTIFLIANGDLISPASRLLIPRKALNQWDHVLQMVTEKITLRSGAVHRLYTLEGKLVESGAELENGQFYVAVGRDKFKRLPYSELLFDKSAMRRPYGQKASSLPPMVGSRKSKGSGNYRQSKSTIGSSDNSSPQPLKRKGKKDSNSEKPTKVKQSVKSKNSHQAIPDNDEGIFKAGAERSET... | null | null | cilium assembly [GO:0060271]; dendrite morphogenesis [GO:0048813]; intracellular signal transduction [GO:0035556]; neuron migration [GO:0001764]; neuronal action potential [GO:0019228]; positive regulation of smoothened signaling pathway [GO:0045880]; regulation of cilium assembly [GO:1902017]; regulation of Wnt signal... | axoneme [GO:0005930]; centriolar satellite [GO:0034451]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinocilium [GO:0060091]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; mitotic spindle [GO:0072686]; synapse [GO:0045202] | kinesin binding [GO:0019894] | PF03607; | 3.10.20.230; | null | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q9UHG0}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UHG0}. Cell projection, kinocilium {ECO:0000269|PubMed:25601850}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25601850}. Note=Localizes to the ciliary axoneme and to mitotic spi... | null | null | null | null | null | FUNCTION: Protein that plays a role in the inhibition of canonical Wnt signaling pathway (By similarity). May be involved in neuronal migration during development of the cerebral neocortex (PubMed:16278297). Involved in the control of ciliogenesis and ciliary length (By similarity). {ECO:0000250|UniProtKB:Q9UHG0, ECO:0... | Rattus norvegicus (Rat) |
D3ZRC4 | PLPL8_RAT | MSINLTLDIYIYFLNNARSFCGKQRSKQLNFLCSKQYWRMNHVNVHREFHTSKKSCKWNRSEAHCSKHWHSSSNHGVHIGIVKLSTSAPKGLTKVSIHMSRIKSTLNSVSKAIFGSQNEMVSRLAQFKPSSRIFRKVSDRGWLKHKNVKQAIESLKNYSDKSAEKNSFAEQKSYFADKEEGSDKHSLYHYAYRITTRFGESFYFLANHINSYFKNKEKMSQIKEDRQLQDKPCLEESKSISPSPDILTDRPDSGPPLNVEDKLSSSTQLPEALPVSTKQSIANFLSRPTEGVQALVGGYIGGLVPKLKSDPKSQPEEEEE... | 3.1.1.-; 3.1.1.5 | null | arachidonic acid metabolic process [GO:0019369]; arachidonic acid secretion [GO:0050482]; cardiolipin metabolic process [GO:0032048]; fatty acid metabolic process [GO:0006631]; intracellular signal transduction [GO:0035556]; linoleic acid metabolic process [GO:0043651]; lipid homeostasis [GO:0055088]; phosphatidylcholi... | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | calcium-independent phospholipase A2 activity [GO:0047499]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phospholipase A1 activity [GO:0008970] | PF01734; | 3.40.1090.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5XTS1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9NP80}. Microsome membrane {ECO:0000250|UniProtKB:Q5XTS1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9NP80}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9NP80}; Single-... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; Evidence={ECO:0000250|UniProtKB:Q9NP80}; PhysiologicalDirection=l... | null | PATHWAY: Phospholipid metabolism. {ECO:0000250|UniProtKB:Q9NP80}. | null | null | FUNCTION: Calcium-independent and membrane-bound phospholipase, that catalyzes the esterolytic cleavage of fatty acids from glycerophospholipids to yield free fatty acids and lysophospholipids, hence regulating membrane physical properties and the release of lipid second messengers and growth factors. Hydrolyzes phosph... | Rattus norvegicus (Rat) |
D3ZS74 | OMA1_RAT | MNFLYGLQSATRNQFLSGVNTLARRRTWTPPAGCPLASRLPAVNANWGLSTVSHCYSVILLPRNLHFCRTLKNKRSRCLSSAQSKEMGVLTYNWTVWGDASCSPNYAAIREVRSFHTSAPRQAAPVPLLMLILKPVQKLLAIIVGRGIRKWWQALPPDKKALFKDSVKRNKWRLLLGLSAFGLLFVVFYFTHLEVSPVTGRSKLLLVGKEHFRLLSDLEYEVWMEEFKNDLLPEEDPRYLTVKKVVYHLTQCNQDVPGVSEINWVVHVVHSPKVNAFVLPNGQVFVFTGLLNSVTDMHQLSFLLGHEIAHAVLGHAAEKA... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O75844}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75844}; | cristae formation [GO:0042407]; diet induced thermogenesis [GO:0002024]; energy homeostasis [GO:0097009]; glucose metabolic process [GO:0006006]; HRI-mediated signaling [GO:0140468]; integrated stress response signaling [GO:0140467]; lipid metabolic process [GO:0006629]; mitochondrial protein processing [GO:0034982]; m... | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | lipid binding [GO:0008289]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF01435; | 3.30.2010.10; | Peptidase M48 family | PTM: Autocatalytically cleaved in response to mitochondrial depolarization both at the N-terminus and C-terminus to generate the short active form (S-OMA1). Autocatalytic processing at the C-terminus takes place at residues 426-435. The S-OMA1 form is unstable (By similarity). OMA1 pre-processing by AFG3L2 may particip... | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9D8H7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D8H7}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.1 uM for OPA1 {ECO:0000269|PubMed:30926535}; | null | null | null | FUNCTION: Metalloprotease that is part of the quality control system in the inner membrane of mitochondria (PubMed:30926535). Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1 (PubMed:30926535). Involved in the fusion of the mito... | Rattus norvegicus (Rat) |
D3ZSI8 | PI51A_RAT | MASASSGPAAAGFSPLDSGVPAGTAASGIKRGTVSEGPYASLMPVKKIGHRSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHNMDHAQ... | 2.7.1.68 | null | actin cytoskeleton organization [GO:0030036]; cell chemotaxis [GO:0060326]; fibroblast migration [GO:0010761]; focal adhesion assembly [GO:0048041]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol phosphate biosynthetic process [GO:004685... | cytosol [GO:0005829]; lamellipodium [GO:0030027]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587] | 1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; ATP binding [GO:0005524]; kinase binding [GO:0019900] | PF01504; | 3.30.810.10;3.30.800.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P70182}. Cytoplasm {ECO:0000250|UniProtKB:P70182}. Nucleus {ECO:0000250|UniProtKB:Q99755}. Nucleus speckle {ECO:0000250|UniProtKB:Q99755}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q99755}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q99755}. Not... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; Evide... | null | null | null | null | FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesio... | Rattus norvegicus (Rat) |
D3ZSZ3 | NLK_RAT | MSLCGTRANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSN... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O54949}; | cellular response to osmotic stress [GO:0071470]; intracellular signal transduction [GO:0035556]; negative regulation of TORC1 signaling [GO:1904262]; negative regulation of Wnt signaling pathway [GO:0030178]; phosphorylation [GO:0016310]; protein stabilization [GO:0050821]; regulation of DNA-templated transcription [G... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; SH2 domain binding [GO:0042169]... | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme. {ECO:0000250|UniProtKB:O54949}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm {ECO:0000250|UniProtKB:O54949}. Note=Predominantly nuclear. A smaller fraction is cytoplasmic. {ECO:0000250|UniProtKB:O54949}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:O54949}; CATALYT... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. B... | Rattus norvegicus (Rat) |
D3ZTD8 | SEM5A_RAT | MKGACILAWLFSSLGVWRLARPETQDPAKCQRAEHPVVSYKEIGPWLREFRAENAVDFSRLTFDPGQKELVVGARNYLFRLQLEDLSLIQAVQWECDEATKKACYSKGKSKEECQNYIRVLLVGGDRLFTCGTNAFTPVCTIRSLSNLTEIHDQISGMARCPYSPQHNSTALLTASGELYAATAMDFPGRDPAIYRSLGTLPPLRTAQYNSKWLNEPNFVSSYDIGNFTYFFFRENAVEHDCGKTVFSRAARVCKNDIGGRFLLEDTWTTFMKARLNCSRPGEVPFYYNELQSTFFLPELDLIYGIFTTNVNSIAASAVC... | null | null | axon extension [GO:0048675]; axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:0002043]; branching involved in blood vessel morphogenesis [GO:0001569]; branching morphogenesis of an epithelial tube [GO:0048754]; cell chemota... | membrane [GO:0016020]; plasma membrane [GO:0005886] | axon guidance receptor activity [GO:0008046]; chemorepellent activity [GO:0045499]; chondroitin sulfate proteoglycan binding [GO:0035373]; heparan sulfate proteoglycan binding [GO:0043395]; semaphorin receptor binding [GO:0030215]; syndecan binding [GO:0045545] | PF01437;PF01403;PF00090; | 3.30.1680.10;2.20.100.10;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Bifunctional axonal guidance cue regulated by sulfated proteoglycans; attractive effects result from interactions with heparan sulfate proteoglycans (HSPGs), while the inhibitory effects depend on interactions with chondroitin sulfate proteoglycans (CSPGs). Ligand for receptor PLXNB3. In glioma cells, SEMA5A ... | Rattus norvegicus (Rat) |
D3ZTE0 | FA12_RAT | MTALLFLGSLLMSLDLTLSAPPWKSKEFKDGAGDPSVVLTVDGKLCHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYCLEPKKVKDHCSKHSPCHKGGTCVNTPNGPHCLCPEHLTGKHCQREKCFESQLLKFFHENEIWFRTGPGGVARCQCKGPQAVCKLLTSQVCRVNPCLNGGTCLLVEDHRLCHCPAGYAGPFCDLDLKATCYEDRGLSYRGQAKTTLSGAPCQRWASEATYRNMTETQALSWGLGHHAFCRNPDNDTRPWCYVWSGDRLSWDYCDLEQCQMPTLTSPVSPESHDMLKPRPPILQS... | 3.4.21.38 | null | blood coagulation [GO:0007596]; Factor XII activation [GO:0002542]; fibrinolysis [GO:0042730]; plasma kallikrein-kinin cascade [GO:0002353]; positive regulation of blood coagulation [GO:0030194]; positive regulation of fibrinolysis [GO:0051919]; positive regulation of plasminogen activation [GO:0010756]; protein autopr... | extracellular space [GO:0005615]; rough endoplasmic reticulum [GO:0005791] | calcium ion binding [GO:0005509]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF00008;PF00039;PF00040;PF00051;PF00089; | 2.10.10.10;2.10.25.10;2.40.20.10;2.40.10.10; | Peptidase S1 family | PTM: O- and N-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.; EC=3.4.21.38; | null | null | null | null | FUNCTION: Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-f... | Rattus norvegicus (Rat) |
D3ZTL1 | PO4F3_RAT | MMAMNAKQPFGMHPVLQEPKFSSLHSGSEAMRRVCLPAPQLQGNIFGSFDESLLARAEALAAVDIVSHGKNHPFKPDATYHTMSSVPCTSTSPTVPISHPAALTSHPHHPVHQGLEGDLLEHISPTLSVSGLGAPEHSVMPAQIHPHHLGAMGHLHQAMGMSHPHAVAPHSAMPACLSDVESDPRELEAFAERFKQRRIKLGVTQADVGAALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPVLQAWLEEAEAAYREKNSKPELFNGSERKRKRTSIAAPEKRSLEAYFAIQPRPSSEKIAAIAEKLDLKKNVVRV... | null | null | axon extension [GO:0048675]; inner ear auditory receptor cell differentiation [GO:0042491]; inner ear development [GO:0048839]; inner ear morphogenesis [GO:0042472]; inner ear receptor cell differentiation [GO:0060113]; neuromuscular process controlling balance [GO:0050885]; neuron apoptotic process [GO:0051402]; posit... | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-... | PF00046;PF00157; | 1.10.10.60;1.10.260.40; | POU transcription factor family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15319}. Cytoplasm {ECO:0000250|UniProtKB:Q15319}. Note=Preferentially localized in the nucleus. {ECO:0000250|UniProtKB:Q15319}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator. Acts by binding to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes. Involved in the auditory system development, required for terminal differentiation of hair cells in the inner ear. {ECO:0000250|UniProtKB:Q6395... | Rattus norvegicus (Rat) |
D3ZTT2 | LYPD6_RAT | MEPSPALAWLLLLSLVADCLKAAQSRDFTVKDIIYLHPSTTPYPGGFKCFTCEKAADNYECNRWAPDIYCPRDTRYCYTQHTMEVTGNSISVTKRCVPLEECLSTGCRDSEHEGYKICTSCCEGNICNLPLPRNDTDATFATTSPINQTNGHPHCVSVIVSCLWVWLGLTL | null | null | positive regulation of canonical Wnt signaling pathway [GO:0090263] | cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular region [GO:0005576]; membrane [GO:0016020]; membrane raft [GO:0045121]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202] | acetylcholine receptor inhibitor activity [GO:0030550]; acetylcholine receptor regulator activity [GO:0030548] | PF16975; | 2.10.60.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q86Y78}. Cytoplasm {ECO:0000250|UniProtKB:Q86Y78}. Cell membrane {ECO:0000269|PubMed:27344019}; Lipid-anchor, GPI-anchor {ECO:0000255}. Synapse, synaptosome {ECO:0000269|PubMed:27344019}. Membrane raft {ECO:0000250|UniProtKB:Q66IA6}. Cell projection, dendrite {ECO:0... | null | null | null | null | null | FUNCTION: Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain (PubMed:27344019). Inhibits nicotine-induced Ca(2+) influx through nAChRs (By similarity). In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner (By similarity). Acts as a positi... | Rattus norvegicus (Rat) |
D3ZTV3 | FLRT2_RAT | MGLQTAKWPSHGTFVLKFWLIMSLGLYSHVSKLLACPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQINNAGFPAELHNVQSVHTVYLYGNQLDEFPMNLPKNVRVLHLQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAFREAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVISDMAFQNLTSLERLIVDGNLLTNKGIADGTFSHLTKLKEFSIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFANLRKLERLDISNNQLRMLTQGVFDHLSNLKQLTARNNPWFCDCSIKW... | null | null | axon guidance [GO:0007411]; basement membrane organization [GO:0071711]; cell adhesion involved in heart morphogenesis [GO:0061343]; fibroblast growth factor receptor signaling pathway [GO:0008543]; heart morphogenesis [GO:0003007]; positive regulation of synapse assembly [GO:0051965]; regulation of neuron migration [G... | cell-cell junction [GO:0005911]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synapse [GO:0045202] | chemorepellent activity [GO:0045499]; fibroblast growth factor receptor binding [GO:0005104] | PF00041;PF13855;PF01463; | 2.60.40.10;3.80.10.10; | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BLU0}.; PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease. {ECO:0000250|UniProtKB:Q8BLU0}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BLU0}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BLU0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BLU0}. Synapse, synaptosome {ECO:0000269|PubMed:22405201}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8BLU0}. Secreted, extr... | null | null | null | null | null | FUNCTION: Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells. May play a role in the migration of cortical neurons during brain development via its intera... | Rattus norvegicus (Rat) |
D3ZU57 | RIOX1_RAT | MDELPNGNGAAPLKRGRGRRRRQPQPRGASVLALPLRPRKVRRHRKSAASRVAALRARALLSEDSDSNVESVRGKRERPAELPEASRSAEPRPVPVRPRPASATLPRRVEGRAALSRNLGKPAPLPGSHVDDPERPWDSPLQQVLAELNGIPSSRRRAARLFEWLLAPLPPDHFYRRLWEREAVLVRRQDHSYYEGLFSTSDLDWMLRYEDVHFGQHLDAARYIDGRRETLNPPGRALPAAAWSLYQAGCSLRLLCPQAFSPTVWQFLAVLQEQFGSMAGSNVYLTPPNSQGFAPHYDDIEAFVLQLEGRKLWRVYRPRD... | 1.14.11.27; 1.14.11.79 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q9JJF3}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9JJF3}; | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of osteoblast differentiation [GO:0045668] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; histone H3K36 demethylase activity [GO:0051864]; histone H3K36me/H3K36me2 demethylase activity [GO:0140680]; histone H3K4 demethylase activity [GO:0032453]; histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; iron ion binding [GO:0005506]; peptid... | PF08007;PF21233; | 3.90.930.40;2.60.120.650;1.10.10.1500; | ROX family, NO66 subfamily | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H6W3}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H6W3}. Note=Granular part of nucleoli. Nucleoplasm, nucleoplasmic foci, some of them associated with nucleoli. {ECO:0000250|UniProtKB:Q9H6W3}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29... | null | null | null | null | FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase (By similarity). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and... | Rattus norvegicus (Rat) |
D3ZUA0 | MTD2L_RAT | MATRARGLSLLRGRLGRGPARAPGVAERAWRGFGSSSRRHEAVIISGTEMAKQIRRELQQGVESWLALGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELIVKPKNVSQEELLDITDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTDGEHERPGGDATVTIAHRHTPREQLKAHTQLAEIIIVAAGIPGLITADMVREGATVIDVGINYVQDPVTGKTKLVGDVDFEAVKKKASFITPVPGGVGPM... | 1.5.1.15; 1.5.1.5; 3.5.4.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24733394}; | 10-formyltetrahydrofolate metabolic process [GO:0009256]; histidine biosynthetic process [GO:0000105]; methionine biosynthetic process [GO:0009086]; purine nucleotide biosynthetic process [GO:0006164]; tetrahydrofolate interconversion [GO:0035999] | mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NAD+) activity [GO:0004487]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488] | PF00763;PF02882; | 3.40.50.10860;3.40.50.720; | Tetrahydrofolate dehydrogenase/cyclohydrolase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21163947}; Peripheral membrane protein {ECO:0000269|PubMed:21163947}; Matrix side {ECO:0000269|PubMed:21163947}. | CATALYTIC ACTIVITY: [Isoform 1]: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000269|PubMed:21163947, ECO:0000269|PubMed:24733394}... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=147 uM for NAD(+) {ECO:0000269|PubMed:24733394}; KM=537 uM for NADP(+) {ECO:0000269|PubMed:24733394}; KM=40 uM for 5,10-methylenetetrahydrofolate (in presence of NAD(+)) {ECO:0000269|PubMed:24733394}; KM=42 uM for 5,10-methylenetetrahydrofolate (in presence of NADP... | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000269|PubMed:24733394}. | null | null | FUNCTION: [Isoform 1]: Bifunctional mitochondrial folate-interconverting enzyme that has both NAD/NADP-dependent methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities. {ECO:0000269|PubMed:21163947, ECO:0000269|PubMed:24733394}.; FUNCTION: [Isoform 2]: Has no NAD/NADP-dependent m... | Rattus norvegicus (Rat) |
D3ZUE1 | GA2L2_RAT | MSQHVGHGRKPRTPGPPVRSIRPFKSSEQYLEVMKEDLAEWLRDLYGLDIDAANFLRVLETGLVLCRHANTVTEAALAFLAEAPERVQKIPMPQVGVFCNGAAQPGTFQARDNISNFIQWCRKEMGIQEVLMFETEDLVLRKNVKSVVLCLLELGRRAWRFGVAAPSLVYLEEEIEEELRRDLDLPSPDPPPPVPPARRPCHFHNLDQMVQSLVSHCTCPVQFSMVKISDGKYRVGDSNTLIFIRILRSHVMVRVGGGWDTLGHYLDKHDPCRCTSLSHKPGSFLKPPGPPVQHEVKVQDGPSQPQPLMTISRSQSPLPP... | null | null | actin crosslink formation [GO:0051764]; microtubule bundle formation [GO:0001578]; negative regulation of microtubule depolymerization [GO:0007026]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; protein localization to microtubule plus-end [GO:1904825]; regulation of cilium beat freq... | actin filament [GO:0005884]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; microtubule plus-end [GO:0035371]; plasma membrane [GO:0005886]; stress fiber [GO:0001725] | actin filament binding [GO:0051015]; cytoskeletal anchor activity [GO:0008093]; G-protein alpha-subunit binding [GO:0001965]; microtubule binding [GO:0008017] | PF00307;PF02187; | 1.10.418.10;3.30.920.20; | GAS2 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23994616}. Cell membrane {ECO:0000269|PubMed:23994616}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q8NHY3}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8NHY3}. Note=Colocalizes with ADORA2A at neuronal processes (... | null | null | null | null | null | FUNCTION: Involved in the cross-linking of microtubules and microfilaments (By similarity). Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers (By similarity). Enhances ADORA2-mediated adenylyl... | Rattus norvegicus (Rat) |
D3ZUI5 | COBL_RAT | MKARAPPPPGKPAAQNVHSEQKLPHDATLGSQQSLVHLKEALHNSTLDITVVLPSGLEKQSVVSGSRAVMDLLVELCLQNHLNPSHHVLEIWSSETQQPLSFKPNTLIGSLNAHTVFLKEKVPEEKGKPGLTKAPEKSVRLVVNYLRTQKAVMRVSPEVPLQNILPVICAKCEVSPDHVVLLRDNIAGEELELSKSLNELGIKELYAWDNRREMLRKSSLGNDETDKEKKKFLGFFKVNKRSNSKAEHLGLSGADSDEDPSKSASGGDLNGCVTTPNSPSLHSRSLTLGPSLSLGNISGMSMKSDMKKRRAPPPPSPGLL... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament network formation [GO:0051639]; actin filament polymerization [GO:0030041]; collateral sprouting in absence of injury [GO:0048669]; digestive tract development [GO:0048565]; embryonic axis specification [GO:0000578]; floor plate development [GO:0033504]; live... | actin filament [GO:0005884]; axon [GO:0030424]; axonal growth cone [GO:0044295]; cell cortex [GO:0005938]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic growth cone [GO:0044294]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ... | actin monomer binding [GO:0003785] | PF09469;PF02205; | null | null | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, ruffle. Cytoplasm. Cytoplasm, cytosol. Note=Recruited to the cell membrane via interaction with PACSIN1. Colocalizes with the actin cytoskeleton. Detected throughout the neuron cell body, as wel... | null | null | null | null | null | FUNCTION: Plays an important role in the reorganization of the actin cytoskeleton. Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin de... | Rattus norvegicus (Rat) |
D3ZUM2 | SARM1_RAT | MVLTLLFSAYKLCRFFIMSGPRPGADRLTVPGPDRSGGTSPWWAAGGRGSREVSPGVGTEVQGALERSLPELQQALSELKQASAAQAVGAGLAEVFQLVEEAWLLPAVGREVAQGLCDAIRLDGGLDLLLRLLQAPELETRVQAARLLEQILVAENRDRVARIGLGVILNLSKEREPVELARSVAGILEHMFKHSEETCQRLVAAGGLDAVLYWCRRTDPALLRHCALALANCALHGGQTVQRCMVEKRAAEWLFPLAFSKEDELLRLHACLAVAVLATNKEVEREVEHSGTLALVEPLVASLDPGRFARCLVDASDTSQ... | 3.2.2.-; 3.2.2.6 | null | cell differentiation [GO:0030154]; innate immune response [GO:0045087]; NAD catabolic process [GO:0019677]; negative regulation of MyD88-independent toll-like receptor signaling pathway [GO:0034128]; nervous system development [GO:0007399]; nervous system process [GO:0050877]; protein localization to mitochondrion [GO:... | axon [GO:0030424]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991]; synapse [GO:0045202] | NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; signaling adaptor activity [GO:0035591] | PF07647;PF13676; | 1.25.10.10;3.40.50.10140;1.10.150.50; | SARM1 family | PTM: Phosphorylation at Ser-548 by JNK kinases (MAPK8, MAPK9 and /or MAPK10) enhance the NAD(+) hydrolase (NADase) activity (PubMed:32968873). Phosphorylation at Ser-548 and subsequent activation takes place in response to oxidative stress conditions and inhibits mitochondrial respiration (By similarity). Phosphorylati... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6SZW1}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PDS3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6PDS3}. Synapse {ECO:0000250|UniProtKB:Q6PDS3}. Mitochondrion {ECO:0000250|UniProtKB:Q6SZW1}. Note=Associated with microtubules. {ECO:0000250|UniProtKB:... | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000250|UniProtKB:Q6SZW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={... | null | null | null | null | FUNCTION: NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism. Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which inv... | Rattus norvegicus (Rat) |
D3ZUQ0 | RIPL1_RAT | MEEPLGSPPAALSALEKNVAELTVMDVYDIASLVGHEFERVIDQHGCEAIARLMPKVVRVLEILEVLVSRHHVAPELDELRLELDRLRVERMDRIEKERKHQKELELVEDVWRGEAQDLLSQIAQLQEENKQLMTNLNHKDVGFSEEELQKHEGMSERERQVMKRLKEVVDKQRDEIRAKDRELVLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSLRAELGKLRERLQGEHSQNGEEEEAEIPPQPDGEESISDAEKAALDLKDPNRPRFTLQELRDVLHERNELKSKVFLLQ... | null | null | cilium assembly [GO:0060271]; epithelial cell morphogenesis [GO:0003382]; nitric oxide mediated signal transduction [GO:0007263]; protein transport from ciliary membrane to plasma membrane [GO:1903445] | centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | dynein light intermediate chain binding [GO:0051959]; protein dimerization activity [GO:0046983]; small GTPase binding [GO:0031267] | PF09744;PF11461; | 1.20.58.1770;6.10.230.10; | RILPL family | PTM: S-nitrosylation is required for the interaction with GAPDH. {ECO:0000269|PubMed:19607794}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19607794}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:30398148}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:30398148}. | null | null | null | null | null | FUNCTION: Plays a role in the regulation of cell shape and polarity (By similarity). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). Neuroprotective protein, which acts by sequestring GAPDH in the cytosol and prevent the apoptotic function of GAPDH in the... | Rattus norvegicus (Rat) |
D3ZVK1 | MCM8_RAT | MSGAYRGRGFGRGRFQNWKRGRGGGNFSGRWRDRTDLSKAAGNHASEQASQPLLQQSTLDQFIPYKGWKLYFSEVYSNNSPLTEKIQAFEKFFTRHIDLYDKDEIERKGSILVDFKELTKDNEITNLIPDIENALRDAPEKTLACMGLAIHQVLTKDLERHAAELQAQEGLCNGGGTMVNVPHIYARVYNYEPLTHLKNIRATCYGKYISIRGTVVRVSNIKPLCTKMAFQCAACGEIQSFPLPDGKYNLPTKCPVPACRGRSFTPLRSSPLTVTMDWQLIKIQELMSDAQREAGRIPRTIECELVHDLVDSCVPGDTVT... | 3.6.4.12 | null | cell cycle [GO:0007049]; DNA damage response [GO:0006974]; DNA duplex unwinding [GO:0032508]; double-strand break repair via homologous recombination [GO:0000724]; female gamete generation [GO:0007292]; male gamete generation [GO:0048232]; protein localization to chromatin [GO:0071168]; protein stabilization [GO:005082... | chromosome [GO:0005694]; MCM complex [GO:0042555]; MCM8-MCM9 complex [GO:0097362]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; MutLbeta complex binding [GO:0032406]; MutSalpha complex binding [GO:0032407]; MutSbeta complex binding [GO:0032408]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activi... | PF00493;PF17855;PF17207; | 2.20.28.10;2.40.50.140;3.40.50.300; | MCM family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJA3}. Chromosome {ECO:0000250|UniProtKB:Q9UJA3}. Note=Localizes to nuclear foci. Localizes to double-stranded DNA breaks. Binds chromatin throughout the cell cycle. {ECO:0000250|UniProtKB:Q9UJA3}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q9UJA3}; | null | null | null | null | FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promot... | Rattus norvegicus (Rat) |
D3ZVM4 | LIN41_RAT | MASFPETDFQICLLCKEMCGSPAPLSSSSSASSSSSQTSTSSAGGGGPGAAARRLHVLPCLHAFCRPCLEAHRLPAPGGAGPAEALKLRCPVCDQKVVLAEAAGMDALPSSAFLLSNLLDAVVATADEPPPKNGRAGGGPGGAGGHSNHRHHAHHPAQRAAAPAPQPPPGPAASPGSLLLRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPAAASAAQQLGLGPPFAGAPFSILSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTLGRHGGHSFAYLQDALQDSRALTIQLLADAQ... | 2.3.2.27 | null | 3'-UTR-mediated mRNA destabilization [GO:0061158]; cellular response to organic substance [GO:0071310]; fibroblast growth factor receptor signaling pathway [GO:0008543]; G1/S transition of mitotic cell cycle [GO:0000082]; miRNA processing [GO:0035196]; miRNA-mediated gene silencing by inhibition of translation [GO:0035... | P-body [GO:0000932] | miRNA binding [GO:0035198]; translation repressor activity [GO:0030371]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF00630;PF01436;PF00643;PF00097; | 3.30.160.60;2.60.40.10;2.120.10.30;3.30.40.10; | TRIM/RBCC family | PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q1PSW8}. | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q2Q1W2}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (By similarity). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In additi... | Rattus norvegicus (Rat) |
D3ZVU1 | SPRTN_RAT | MDEDLVVALRLQEEWDVQAARRAAAREPLSLVDASWELVDPTPDLQALFLQFNDRFFWGQLEAVEVKWSVRMTLCAGICTYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINQLTGANITVYHTFHDEVDEYRRHWWRCNGPCQHKQPYYGYVKRATNRAPSAHDYWWADHQKTCGGTYIKIKEPENYAKKGRGKTKAGKQPTSAVENKDKLCRGEAQPLIPFSGKGYVLGDTSTCPSAGKLNTSHMVNDTKGLSGQDHSASGLKLDSNVEVKCEQNGLPNKKPHLVTPL... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040}; | DNA damage response [GO:0006974]; positive regulation of protein ubiquitination [GO:0031398]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]; response to UV [GO:0009411]; translesion synthesis [GO:0019985] | chromatin [GO:0000785]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; polyubiquitin modification-dependent protein binding [GO:0031593]; single-stranded DNA binding [GO:0003697]; ubiquitin bindi... | PF10263; | 3.30.160.60; | Spartan family | PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Monoubiquitinated; monoubiquitination promotes exclusion from chromatin. Deubiquitinated by VCPIP1: deubiquitination is required for sub... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:Q9H040}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress following deubiquitination. CHEK1 stimulates recruitment to chromatin. {ECO:0000250|UniProt... | null | null | null | null | null | FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication an... | Rattus norvegicus (Rat) |
D3ZVU9 | NAT8L_RAT | MHCGPPDMVCETKIVATEDHEALPGAKKDALLAAAGAMWPPLPAAPGPAAAPPPAAGPQPHGGTGGAGPPEGRGVCIREFRAAEQEAARRIFYDGILERIPNTAFRGLRQHPRTQLLYALLAALCFAVTRSLLLTCLVPAGLLALRYYYSRKVILAYLECALHTDMADIEQYYMKPPGSCFWVAVLDGNVVGIVAARAHEEDNTVELLRMSVDSRFRGKGIAKALGRRVLEFAMLHNYSAVVLGTTAVKVAAHKLYESLGFRHMGASDHYVLPGMTLSLAERLFFQVRYHRYRLQLREE | 2.3.1.17 | null | acetate metabolic process [GO:0006083]; aspartate metabolic process [GO:0006531]; positive regulation of dopamine uptake involved in synaptic transmission [GO:0051586] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | aspartate N-acetyltransferase activity [GO:0017188] | PF00583; | 3.40.630.30; | Camello family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F0}. Microsome membrane {ECO:0000269|PubMed:18621030}; Single-pass type I membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:18621030}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3U... | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-aspartate = CoA + H(+) + N-acetyl-L-aspartate; Xref=Rhea:RHEA:14165, ChEBI:CHEBI:15378, ChEBI:CHEBI:16953, ChEBI:CHEBI:29991, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.17; Evidence={ECO:0000269|PubMed:18621030}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14166;... | null | null | null | null | FUNCTION: Catalyzes the synthesis of N-acetylaspartate acid (NAA) from L-aspartate and acetyl-CoA (PubMed:18621030). Promotes dopamine uptake by regulating TNF-alpha expression (By similarity). Attenuates methamphetamine-induced inhibition of dopamine uptake (By similarity). {ECO:0000250|UniProtKB:Q3UGX3, ECO:0000250|U... | Rattus norvegicus (Rat) |
D3ZVV1 | KHDC3_RAT | MATLKTFRTLVQLKHKLGKAYEIVGEPRLPKWFHVEYLEDPKKMYVEPTLVEIMFGKDGEHIPHVECTLHVLIHVNVWGPEKQAEILIFGPPNFQKDVAQMLSNVAHFCRMKLMEKEALEAGVERRLMAASKATTQPTPVKVRDAATQVAPVQVRDAAIQPAPVKVRDAATQVAPVQVHEVATQPVPVQVRDAATQPVPVRVRDAATQPVPVRVRDAATQPVPVRVRDAATQPVPVRVRDAATEPVPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPVQVRDAATQPAPV... | null | null | actin filament organization [GO:0007015]; establishment of organelle localization [GO:0051656]; mitotic spindle assembly [GO:0090307]; mitotic spindle assembly checkpoint signaling [GO:0007094]; negative regulation of apoptotic process [GO:0043066]; positive regulation of dendrite development [GO:1900006]; positive reg... | apical cortex [GO:0045179]; cell cortex [GO:0005938]; centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; subcortical maternal complex [GO:0106333] | RNA binding [GO:0003723] | PF16005; | 3.30.1370.10; | KHDC1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9CWU5}. Nucleus {ECO:0000250|UniProtKB:Q9CWU5}. Mitochondrion {ECO:0000250|UniProtKB:Q9CWU5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9CWU5}. Chromosome {ECO:0000250|UniProtKB:Q587J8}. Note=Localized ... | null | null | null | null | null | FUNCTION: As part of the OOEP-KHDC3 scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart (By similarity). Regulates homologous recombination-mediated DNA r... | Rattus norvegicus (Rat) |
D3ZW55 | ITPA_RAT | MAASLVGKKIVFVTGNAKKLEEVIQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEAARQVQGPVLVEDTCLCFNALGGLPGPYIKWFLQKLKPEGLYQLLAGFEDKSAYALCTFALSTGDPSQPVLLFRGKTPGQIVMPRGSRDFGWDPCFQPDGYEQTYAEMPKAEKNTISHRFRALFKLQEYFGVTDGAGDH | 3.6.1.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03148}; | chromosome organization [GO:0051276]; deoxyribonucleoside triphosphate catabolic process [GO:0009204]; ITP catabolic process [GO:0006193]; nucleoside triphosphate catabolic process [GO:0009143] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | dITP diphosphatase activity [GO:0035870]; identical protein binding [GO:0042802]; ITP diphosphatase activity [GO:0036220]; metal ion binding [GO:0046872]; nucleoside triphosphate diphosphatase activity [GO:0047429]; nucleotide binding [GO:0000166]; XTP diphosphatase activity [GO:0036222] | PF01725; | 3.90.950.10; | HAM1 NTPase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03148}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03148}; PhysiologicalDirection=le... | null | null | null | null | FUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguis... | Rattus norvegicus (Rat) |
D3ZWK4 | LMBL1_RAT | MEGHSDMEIIRAVKGSATGEINVHLVARDSAGSHPHLPTTTFIIPTNAATLGLPSTALDVSYPREPVHVGAAERVAGSEPVTATILPQLSTGPGTNSTVRLLDWTGVSAPLAGSGMRFRINEYATQNMIEIERPRSPEQRHEGGTAGREADIQHPDVHKDPQEVIPQEPSVDAGSCKCQTCGPQQSIGLDVGSSGDRCPQPFQKRSVIVENSGCTVASELIKPMKKRKHKEYQSPSEESEPEAMKQGKGKDPDREPTPGTSENEEWSRSQLVSSEKKEGWSWESYLEEQKAVTAPVSLFQDSQAVTHNKNGFKLGMKLEG... | null | null | chromatin organization [GO:0006325]; hemopoiesis [GO:0030097]; heterochromatin formation [GO:0031507]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of megakaryocyte differentiation [GO:0045652]; regulation of mitotic nuclear division [GO:0007088] | chromatin [GO:0000785]; chromatin lock complex [GO:0061793]; condensed chromosome [GO:0000793]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; identical protein binding [GO:0042802]; methylated histone binding [GO:0035064]; nucleosome binding [GO:0031491]; SAM domain binding [GO:0032093]; zinc ion binding [GO:0008270] | PF02820;PF00536;PF01530; | 2.30.30.140;4.10.320.30;1.10.150.50; | null | PTM: Ubiquitinated in a VCP/p97-dependent way following DNA damage, leading to its removal from DNA damage sites, promoting accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited to DNA damage sites. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the nucleolus. Does not colocalize with the PcG protein BMI1, suggesting that these two proteins do not belong to the same complex (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor b... | Rattus norvegicus (Rat) |
D3ZYR1 | FCHO2_RAT | MVMAHFVENFWGEKNNGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQAIQNITQALQKSKENYNAKCVEQERLKKEGATPREIEKAAVKSKKATDTYKLYVEKYALTKADFEQKMTETAQKFQDIEETHLIHIKEIIGSLSNAIKEIHLQIGQVHEEFINNMANTTIESLIQKFAESKGTGKERPGLIEFEECDPASAVEGIKPRKRKTFALPGIIKKEKDAESVECPDADSLNIPDVDE... | null | null | clathrin coat assembly [GO:0048268]; clathrin-dependent endocytosis [GO:0072583]; membrane invagination [GO:0010324]; protein localization to plasma membrane [GO:0072659]; synaptic vesicle endocytosis [GO:0048488] | clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; presynaptic endocytic zone membrane [GO:0098835] | identical protein binding [GO:0042802]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786] | PF00611;PF10291; | 1.20.1270.60; | FCHO family | PTM: Ubiquitinated. Mainly undergoes monoubiquitination but also polyubiquitination (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2 (By similari... | null | null | null | null | null | FUNCTION: Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoin... | Rattus norvegicus (Rat) |
D3ZYW7 | FRDA_RAT | MWTFGRRAAAGLLPRTASRASAWVRNPRGRERIGTCGRRGLHVTANADAIRHSHLNLHYLGQILNIKKQSVCVVHLRNSGTLGNPSSLDETAYERLAEETLDALAEFFEDLADKPYTLKDYDVSFGDGVLTIKLGGDLGTYVINKQTPLLYLWFSGPCSGPKRYDWTGKNWVYSHDGVSLHELLARELTEALNTKLDLSSLAYSGKGT | 1.16.3.1 | null | [2Fe-2S] cluster assembly [GO:0044571]; [4Fe-4S] cluster assembly [GO:0044572]; adult walking behavior [GO:0007628]; aerobic respiration [GO:0009060]; cellular response to glucose starvation [GO:0042149]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; embryo development ... | cytosol [GO:0005829]; L-cysteine desulfurase complex [GO:1990221]; mitochondrial iron-sulfur cluster assembly complex [GO:0099128]; mitochondrion [GO:0005739] | 2 iron, 2 sulfur cluster binding [GO:0051537]; enzyme binding [GO:0019899]; ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; ferroxidase activity [GO:0004322]; iron chaperone activity [GO:0034986]; metallochaperone activity [GO:0016530] | PF01491; | 3.30.920.10; | Frataxin family | PTM: [Frataxin mature form]: Processed in two steps by mitochondrial processing peptidase (MPP). MPP first cleaves the precursor to intermediate form and subsequently converts the intermediate to yield frataxin mature form (frataxin(81-210)) which is the predominant form. The additional forms, frataxin(56-210) and frat... | SUBCELLULAR LOCATION: [Frataxin mature form]: Mitochondrion {ECO:0000250|UniProtKB:Q16595}.; SUBCELLULAR LOCATION: [Extramitochondrial frataxin]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q16595}. | CATALYTIC ACTIVITY: [Frataxin mature form]: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000250|UniProtKB:Q16595}; | null | null | null | null | FUNCTION: [Frataxin mature form]: Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly. Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thio... | Rattus norvegicus (Rat) |
D3ZZC3 | KLH22_RAT | MAEEQDFAQLCKLSTQPSHSHCVNNTYRSTQHSQALLRGLLALRDSGILFDVVLVVEGRHIEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIHGVSYNAMCQILHFIYTSELELSLSNVQETLVAACQLQIPEIIHFCCDFLMSWVDEENILDVYRLAELFDLNRLTQQLDTYILKNFVAFSRTDKYRQLPLEKVYSLLSSNRLEVSCETEVYEGALLYHYSMEQVQADQISLHEPPKLLETVRFPLMEAEVLQRLHDKLGPSPLRDTVASALMYHRNESLQPSLQGPHTELRSDFQCVVGFGGIHSTPSTILSDQAKY... | null | null | cell division [GO:0051301]; cellular response to amino acid stimulus [GO:0071230]; cellular response to leucine [GO:0071233]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint signaling [GO:0007094]; negative regulation of autophagy [GO:0010507]; negative regulation of type I interf... | centrosome [GO:0005813]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosome [GO:0005764]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; polar microtubule [GO:0005827] | 14-3-3 protein binding [GO:0071889]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF07707;PF00651;PF01344;PF13415;PF13964; | 1.25.40.420;2.120.10.80; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q53GT1}. Nucleus {ECO:0000250|UniProtKB:Q53GT1}. Lysosome {ECO:0000250|UniProtKB:Q53GT1}. No... | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q53GT1}. | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent re... | Rattus norvegicus (Rat) |
D4A055 | CACB4_RAT | MSSSYAKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTSTSFILRQGSADSYTSRPSDSDVSLEEDREAIRQEREQQAAIQLERAKSKPVAFAVKTNVSYCGALDEDVPVPSTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCEIGFIPSPLRLENIRIQQEQKRGRFHGGKSSGNSSSSLGEMVSGTFRATPTTTAKQKQKVTEHIPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKRAIIERSNTRSSLAEVQSEIERIFELARSLQLVVLDADTINHPAQ... | null | null | adult walking behavior [GO:0007628]; calcium ion transport [GO:0006816]; cAMP metabolic process [GO:0046058]; cellular response to leukemia inhibitory factor [GO:1990830]; chemical synaptic transmission [GO:0007268]; detection of light stimulus involved in visual perception [GO:0050908]; gamma-aminobutyric acid secreti... | glutamatergic synapse [GO:0098978]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; voltage-gated calcium channel complex [GO:0005891] | high voltage-gated calcium channel activity [GO:0008331]; protein kinase binding [GO:0019901]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels [GO:0099626] | PF00625;PF12052; | 3.40.50.300;2.30.30.40; | Calcium channel beta subunit family | null | null | null | null | null | null | null | FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting. {ECO:0000250|U... | Rattus norvegicus (Rat) |
D4A1F2 | MICA2_RAT | MGENEDEKQAQASQVFENFVQATTCKGTLQAFNILTCLLDLDPLDHRNFYTQLKSKVNTWKAKALWHKLDKRGSHKEYKRGKACSNTKCLIVGGGPCGLRTAIELAYLGAKVVVVEKRDTFSRNNVLHLWPFTIHDLRGLGAKKFYGKFCAGSIDHISIRQLQLILFKVALMLGVEIHVNVEFVRVREPPKDQENRKIGWRAEFLPADHALSNFEFDVIIGADGHRNTLEGFRRKEFRGKLAIAITANFINRNSTAEAKVEEISGVAFIFNQKFFQDLKEETGIDLENIVYYKDSTHYFVMTAKKQSLLDKGVILNDYID... | 1.14.13.225 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q8TDZ2}; | actin filament depolymerization [GO:0030042]; cytoskeleton organization [GO:0007010]; heart development [GO:0007507]; heart looping [GO:0001947]; positive regulation of transcription by RNA polymerase II [GO:0045944]; sulfur oxidation [GO:0019417] | actin filament [GO:0005884]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | actin binding [GO:0003779]; FAD binding [GO:0071949]; metal ion binding [GO:0046872]; mitogen-activated protein kinase binding [GO:0051019]; monooxygenase activity [GO:0004497]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, wi... | PF12130;PF00307;PF01494;PF00412; | 1.10.418.10;2.10.110.10;3.50.50.60; | Mical family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94851}. Cytoplasm {ECO:0000250|UniProtKB:Q8BML1}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-(R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044, ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:5834... | null | null | null | null | FUNCTION: Methionine monooxygenase that promotes depolymerization of F-actin by mediating oxidation of residues 'Met-44' and 'Met-47' on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization (By similarity). Regulates the disassembly of branched actin networks also ... | Rattus norvegicus (Rat) |
D4A1J4 | DHRS6_RAT | MGRLEGKVIVLTAAAQGIGRASALAFAREGAKVIATDINEAKLQELENYPGIQTRVLDVTKKRQIDQFASEIEKIDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVENRCVYSATKAAVIGLTKSVAADFIQQGIRCNCVCPGTVDTPSLQERIQARDDPKEALKAFLNRQKTGRFASAEEVALLCVYLASDESAYVTGTPVVIDGGWSL | 1.1.1.-; 1.1.1.104; 1.1.1.30 | null | epithelial cell differentiation [GO:0030855]; fatty acid beta-oxidation [GO:0006635]; heme metabolic process [GO:0042168]; intracellular sequestering of iron ion [GO:0006880]; siderophore biosynthetic process [GO:0019290] | cytoplasm [GO:0005737] | 3-hydroxybutyrate dehydrogenase activity [GO:0003858]; 4-oxoproline reductase activity [GO:0016617]; NAD binding [GO:0051287]; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor [GO:0016628] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BUT1}. | CATALYTIC ACTIVITY: Reaction=cis-4-hydroxy-L-proline + NAD(+) = 4-oxo-L-proline + H(+) + NADH; Xref=Rhea:RHEA:13601, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:63727, ChEBI:CHEBI:84813; EC=1.1.1.104; Evidence={ECO:0000269|PubMed:35150746}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=387 uM for 4-oxo-L-proline {ECO:0000269|PubMed:35150746}; KM=10232 uM for (R)-3-hydroxybutanoate {ECO:0000269|PubMed:35150746}; Vmax=28 umol/min/mg enzyme toward 4-oxo-L-proline {ECO:0000269|PubMed:35150746}; Vmax=0.04 umol/min/mg enzyme toward (R)-3-hydroxybutanoa... | PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:35150746}.; PATHWAY: Siderophore biosynthesis. {ECO:0000250|UniProtKB:Q8JZV9}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. Active from 5.5 to 9.0 with 4-oxo-L-proline. {ECO:0000269|PubMed:35150746}; | null | FUNCTION: NAD(H)-dependent dehydrogenase/reductase with a preference for cyclic substrates (By similarity). Catalyzes stereoselective conversion of 4-oxo-L-proline to cis-4-hydroxy-L-proline, likely a detoxification mechanism for ketoprolines (PubMed:35150746). Mediates the formation of 2,5-dihydroxybenzoate (2,5-DHBA)... | Rattus norvegicus (Rat) |
D4A1R8 | CPNE1_RAT | MAHCVTLVQLSVSCDHLIDKDIGSKSDPLCVLLQDVGGAWAELCRTERVRNCSSPAFSKTLQIEYYFETVQKLRFGIYDIDNKTPELGDDDFLGGAECSLGQIVSSQTLTLPLMLKPGKPAGRGTITVSAQELKDSRVVTMEVEARNLDKKDFLGKSDPFLEFFRQGDGKWHLAYRTEVVKNNLNPTWKRFSVSLQHFCGGDLNTPIQVRCSDYDSDGSHDLIGTFHTTLAQLQAVPAEFECIHPEKQQRKKSYKNSGTVCVKTCRVETEYSFLDYVMGGCQINFTVGVDFTGSNGDPSSPDSLHYLSPTGVNEYLTALW... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; | cellular response to calcium ion [GO:0071277]; negative regulation of gene expression [GO:0010629]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; neuron projection extension [GO:1990138]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of phosphatidylin... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; endopeptidase activity [GO:0004175]; identical protein binding [GO:0042802]; NF-kappaB binding [GO:0051059]; phosphatidylserine binding [GO:0001786] | PF00168;PF07002; | 2.60.40.150;3.40.50.410; | Copine family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99829}. Cytoplasm {ECO:0000250|UniProtKB:Q99829}. Cell membrane {ECO:0000250|UniProtKB:Q99829}. Note=Translocates to the cell membrane in a calcium-dependent manner. {ECO:0000250|UniProtKB:Q99829}. | null | null | null | null | null | FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Involved in the TNF-alpha receptor signaling pathway in a calcium-dependent manner. Exhibits calcium-dependent phospholipid binding properties. Plays a role in neuronal progenitor cell differentiation... | Rattus norvegicus (Rat) |
D4A1W8 | MTP_RAT | MILLAVLFLCFFSSYSASVKGHTTGLSLNNERLYKLTYSTEVFLDGGKGKLQDSVGYRISSDVDVVLLWRNPDGDDDQLIQVTITAVNVENAGQQRGEKSIFKGKSTPKIVGKDNLEALRRPMLLHLVRGKVKEFYSYENEPVGIENLKRGLASLFQMQLTSGTTNEVDISGDCKVTYQAQQDKVVKIKALDTCKIERSGFTTANQVLGVTSKATSVTTYKIEDSFVTAVVAEETRAFALNFLQTVAGKIVSKQKLELKTTEAGPRMVPGKQVAGVIKAIDSKYKAIPIVGQVLQSVCKGCPSLAEHWQSIRKHLEPENL... | null | null | cholesterol homeostasis [GO:0042632]; circadian rhythm [GO:0007623]; establishment of localization in cell [GO:0051649]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]; lipoprotein transport [GO:0042953]; low-density lipoprotein particle remodeling [GO:003... | basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; microvillus membrane [GO:0031528]; receptor complex [GO:0043235]; vesicle [GO:0031982] | apolipoprotein binding [GO:0034185]; ceramide 1-phosphate transfer activity [GO:1902388]; cholesterol transfer activity [GO:0120020]; lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]; phosphatidylcholine transfer activity [GO:0120019]; phosphatidylethanolamine transfer activity [GO:1904121]; phosphol... | PF19444;PF01347; | 1.25.10.20; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P55157}. Golgi apparatus {ECO:0000250|UniProtKB:P55157}. Note=Colocalizes with P4HB/PDI in the endoplasmic reticulum. {ECO:0000250|UniProtKB:P55157}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:16478722}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; Evidence={ECO:0000305|PubMed:16478722}; CATALYTIC ACTIVI... | null | null | null | null | FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces (PubMed:15897609, PubMed:16478722). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B (By similarity). May be involved in regulating cholesteryl ester biosynthe... | Rattus norvegicus (Rat) |
D4A1X2 | EXOSX_RAT | MAPPSPREHQSAPATGATKPDAEMVLPGFPDADSFVKFALGSVVAVTKASGGLPQVGDEYDFYRSFPAFQAFCETQGDRLLQCMSRVMQYHGCRSNIKDRSKVTELEDKFDLLVDTNDVILERVGILLDEASGVNKHQQPVLPAGLQVPKTIVSSWNRKAGEYGKKAKAETFRLLHAKNILRPQLRFREKIDNSNTPFLPKIFVKPNARKPLPQALSKERRERPQDRPEDLDVPPALADFIHQQRAQQVEQDVFAHPYQYELDHFTPPPSVLQRPQPQLYRPVEETPCHVVSSLDELVELNEKLLGCQEFAVDLEHHSYR... | 3.1.13.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q01780}; | CUT catabolic process [GO:0071034]; DNA repair [GO:0006281]; exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; histone mRNA catabolic process [GO:0071044]; maturation of 5.8S rRNA [GO:0000460]; negative regulation of telomere m... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; euchromatin [GO:0000791]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; small-subunit processome [GO:0032040] | 3'-5'-RNA exonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA exonuclease activity [GO:0004532]; single-stranded RNA binding [GO:0003727] | PF01612;PF00570;PF08066; | 1.10.150.80;3.30.420.10; | Exosome component 10/RRP6 family | PTM: Sumoylated by USP36; sumoylation does not significantly affect EXOSC10 nucleolar localization and association with core exosome and USP36, but regulates the nucleolar RNA exosome activity in rRNA processing by promoting binding of EXOSC10 to pre-rRNAs. Effects of sumoylation on EXOSC10 levels vary between differen... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01780}. Nucleus {ECO:0000250|UniProtKB:Q01780}. Nucleus, nucleolus {ECO:0000269|PubMed:29118343}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q01780}. Note=Strongly enriched in the nucleolus and a small amount has been found in cytoplasm supporting the existence o... | null | null | null | null | null | FUNCTION: Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elim... | Rattus norvegicus (Rat) |
D4A208 | SRGP2_RAT | MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDIIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENL... | null | null | actin filament severing [GO:0051014]; dendritic spine development [GO:0060996]; excitatory synapse assembly [GO:1904861]; extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration [GO:0021816]; filopodium assembly [GO:0046847]; inhibitory synapse assembly [GO:1904862]; lam... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; dendritic spine head [GO:0044327]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211] | GTPase activator activity [GO:0005096]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267] | PF00611;PF00620;PF00018; | 1.20.1270.60;1.10.555.10;2.30.30.40; | null | PTM: Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions. {ECO:0000250|UniProtKB:O75044}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75044}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:O75044}. Postsynaptic density {ECO:0000250|UniProtKB:Q91Z67}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q91Z67}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O75044}. Cytoplasmic ... | null | null | null | null | null | FUNCTION: Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex. Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons. SRGAP2/SRGAP2A limits excitatory and inhibitory sy... | Rattus norvegicus (Rat) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.