entry
stringlengths 6
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stringlengths 5
11
| protein_name
stringlengths 3
2.44k
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stringlengths 2
35.2k
| function
stringlengths 7
11k
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O87605
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PIKC_STRVZ
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Cytochrome P450 monooxygenase PikC (EC 1.14.15.33) (Cytochrome P450 monooxygenase PicK) (Narbomycin C-12 hydroxylase) (Pikromycin synthase CYP107L1)
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MRRTQQGTTASPPVLDLGALGQDFAADPYPTYARLRAEGPAHRVRTPEGDEVWLVVGYDRARAVLADPRFSKDWRNSTTPLTEAEAALNHNMLESDPPRHTRLRKLVAREFTMRRVELLRPRVQEIVDGLVDAMLAAPDGRADLMESLAWPLPITVISELLGVPEPDRAAFRVWTDAFVFPDDPAQAQTAMAEMSGYLSRLIDSKRGQDGEDLLSALVRTSDEDGSRLTSEELLGMAHILLVAGHETTVNLIANGMYALLSHPDQLAALRADMTLLDGAVEEMLRYEGPVESATYRFPVEPVDLDGTVIPAGDTVLVVLADAHRTPERFPDPHRFDIRRDTAGHLAFGHGIHFCIGAPLARLEARIAVRALLERCPDLALDVSPGELVWYPNPMIRGLKALPIRWRRGREAGRRTG
|
Catalyzes the hydroxylation of narbomycin to give rise to pikromycin, and of 10-deoxymethymycin (YC-17) to give rise to methymycin and neomethymycin during macrolide antibiotic biosynthesis. In addition, produces low amounts of neopicromycin, novapikromycin and novamethymycin. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase.
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O87761
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PYRG_LACLM
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CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
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MSTKYIFVTGGGTSSMGKGIVAASLGRLLKNRGLKVTVQKFDPYLNIDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDINLNKYSNVTSGKVYSEILRKERKGEYLGATVQMVPHVTNMLKEKIKRAATTTDADIIITEVGGTVGDMESLPFIEALRQMKAEVGADNVMYIHTVPILHLRAAGELKTKIAQNATKTLREYGIQANMLVLRSEVPITTEMRDKIAMFCDVAPEAVIQSLDVEHLYQIPLNLQAQNMDQIVCDHLKLDAPKADMAEWSAMVDHVMNLKKKVKIALVGKYVELPDAYISVTEALKHAGYASDAEVDINWVNANDVTDENVAELVGDAAGIIVPGGFGQRGTEGKIAAIKYARENDVPMLGICLGMQLTAVEFARNVLGLEGAHSFELDPETKYPVIDIMRDQVDVEDMGGTLRLGLYPAKLKNGSRAKAAYNDAEVVQRRHRHRYEFNNKYREDFEKAGFVFSGVSPDNRLVEIVELSGKKFFVACQYHPELQSRPNRPEELYTEFIRVAVENSK
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Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Is essential for the synthesis of CTP de novo. Contrary to other bacterial CTP synthases, the lactococcal enzyme is also able to convert dUTP to dCTP, but this reaction may not play a significant physiological role. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity). {ECO:0000255|HAMAP-Rule:MF_01227, ECO:0000269|PubMed:11500486}.
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O87953
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KTRB_VIBAL
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Ktr system potassium uptake protein B (K(+)-uptake protein KtrB)
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MTQFHQRGVFYVPDGKRDKAKGGEPRIILLSFLGVLLPSAVLLTLPVFSVSGLSITDALFTATSAISVTGLGVVDTGQHFTLAGKILLMCLMQIGGLGQMTLSAVLLYMFGVRLSLRQQALAKEALGQERQVNLRRLVKKIVTFALVAEAIGFVFLSYRWVPEMGWQTGMFYALFHSISAFNNAGFALFSDSMMSFVNDPLVSFTLAGLFIFGGLGFTVIGDVWRHWRKGFHFLHIHTKIMLIATPLLLLVGTVLFWLLERHNPNTMGSLTTGGQWLAAFFQSASARTAGFNSVDLTQFTQPALLIMIVLMLIGAGSTSTGGGIKVSTFAVAFMATWTFLRQKKHVVMFKRTVNWPTVTKSLAIIVVSGAILTTAMFLLMLTEKASFDKVMFETISAFATVGLTAGLTAELSEPGKYIMIVVMIIGRIGPLTLAYMLARPEPTLIKYPEDTVLTG
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Part of the Na(+)-dependent high affinity K(+) uptake system KtrAB. KtrB is the K(+)-translocating subunit.
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O88037
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RAMC_STRCO
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Probable SapB synthase (EC 2.7.-.-)
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MTAATVRGGTPRDSVVSVSNRWEGAGVNKGYAVYCDADPYFYDAPHRTADRTGAARSRYAAASSPVPEGWQRHESGDWLALRPADADLPAQGWKIHVSACLDNAESVLDRVWRHCVDGGTAFKFVPSRYLLHQRNAKYADRAGSGKFVTVYPADEAEFERLVGELSELLAGEPGPHILSDLRIGDGPVHVRYGGFTRRDCYDADGELRPAVSGPDGVLVPDLRGPVFRIPEWVDPPAFLRPHLDARSAVTVTGMPYTVESALHFSNGGGVYLARDTRTGARVVLKEARPHAGLAADGADAVTRLHRERRALERLSGLACTPEVLDHRTVGEHHFLVLEHIDGKPLNTFFARRHPLIEADPGERRLAEYTDWALDVHARVERAVAEVHARGVVFNDLHLFNIMVRDDDSVALLDFEAAHHVDEAGRQIVANPGFVAPPDRRGVAVDRYALACLRIVLFLPLTSLLAVDRHKAAHLAEVVAEQFPVDRAFLDAAVEEITRVDGSTRVDGSTRADETTRADETTRLDVTTRVHGAPDAARRPAGPVAPVRPDDWPRSRDSMAAAIRASATPSRTDRLFPGDIAQFATAGGGLAFAHGAAGVLYALAESGAGRDEDGEQWLLERTKRPPSGMPLGFHDGLAGLAWTLERLGHRDRALDLAELLLDQPLDHLGPDLHGGTAGLGLALESLAATTGQAALHSAALHCAELAADGLPGGSVPADRVSRGRARAGLLYGGAGRALLFLRLFERTRDSALLDLARDALRQDLARCVRGAGGALQVDEGWRTMPYLGAGSVGIGMVLDDYLAHRADEEFARAANEIVAAAQAMFYAQPGLYRGVAGMVLHLGRTTATAPGTGPRAVRRQLDALSWHAMSYRDRLAFPGEQMMRLSMDLSTGTAGCLLAVASVLGDAPAGLPFLPPPRRSGGPLTRPHQEP
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Required for aerial hyphae formation. Probably involved in processing the precursor of SapB to its mature form (Probable).
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O88038
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LANSB_STRCO
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Lanthionine-containing peptide SapB precursor RamS (ProSapB) [Cleaved into: Lanthionine-containing peptide SapB (Morphogen SapB) (Rapid aerial mycelium protein S) (Spore-associated protein B)]
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MNLFDLQSMETPKEEAMGDVETGSRASLLLCGDSSLSITTCN
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[Lanthionine-containing peptide SapB precursor RamS]: Stably accumulated precursor of SapB. [Lanthionine-containing peptide SapB]: Lanthionine-containing peptide devoid of antibiotic properties. A surface active peptide involved in the efficient formation of aerial mycelium when cells are grown in rich media. Has an overlapping function with the surface-active chaplin proteins chaplins are essential on minimal medium while on rich medium both chaplins and SapB are required for efficient aerial hyphae formation. Required under conditions of high osmolarity where it may change the physical properties of the chaplin layer to allow hyphae to grow into air (Probable). Suggested to self-assemble at air-water interfaces, thus providing a film of surfactant through which nascent aerial hyphae can emerge the aerial hyphae differentiate further into spores. Application to bald mutants (bld, unable to make aerial hyphae) restores hyphae growth. Application to chaplin negative mutants as well as ramC-ramS-ramA-ramB and ramR deletions also restores aerial hyphae growth and sporulation. Reduces surface tension of water from 72 to 30 mJ/m(2).
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O88070
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GLNA4_STRCO
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Gamma-glutamylethanolamide synthetase GlnA4 (EC 6.3.1.-)
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MSPGQKEALPVADRTPPLGVEELHALVAAGDIDTVVLAFPDMQGRLQGKRFAARFFLDEVLEHGTEGCNYLLAVDADMNTVDGYAMSSWDRGYGDFAMRADPATLRRLPWNEGTAMAVADLAWEDGSPVLAAPRQILRRQLERLAGHGYTAQVGTELEFIVFRDTYEHAWDANYRGLTPANQYNVDYSVLGTGRVEPLLRRIRNEMAGAGLTVESAKGECNPGQHEIAFRYDEALVTCDQHAVYKTGAKEIAAQEGMSLTFMAKYNELEGNSCHIHLSLADADGRNAMAEGGGMSDVMRHFLAGQLVALREFSLLYAPHINSYKRFQPGSFAPTAVAWGHDNRTCALRVVGHGRSLRFENRLPGGDVNPYLAVAGLVAAGLHGIEQRLELPEPCPGNAYTADFAHVPTTLREAAELWENSTLAKAAFGDEVVAHYRNMARVELDAFDAAVTDWELRRSFERM
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Involved in the catabolism of monoamine ethanolamine. Catalyzes the ATP-dependent gamma-glutamylation of ethanolamine. No activity with polyamines. No complementation of the L-glutamine auxotrophy of an E.coli glnA mutant. Enables survival of S.coelicolor under high local environmental ethanolamine conditions. May play a role during starvation conditions to limit intracellular ethanolamine concentration, which in excess is toxic to the cells.
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O88093
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HBP_ECOLX
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Hemoglobin-binding protease hbp autotransporter (EC 3.4.21.-) [Cleaved into: Hemoglobin-binding protease hbp; Hemoglobin-binding protease hbp translocator (Helper peptide)]
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MNRIYSLRYSAVARGFIAVSEFARKCVHKSVRRLCFPVLLLIPVLFSAGSLAGTVNNELGYQLFRDFAENKGMFRPGATNIAIYNKQGEFVGTLDKAAMPDFSAVDSEIGVATLINPQYIASVKHNGGYTNVSFGDGENRYNIVDRNNAPSLDFHAPRLDKLVTEVAPTAVTAQGAVAGAYLDKERYPVFYRLGSGTQYIKDSNGQLTKMGGAYSWLTGGTVGSLSSYQNGEMISTSSGLVFDYKLNGAMPIYGEAGDSGSPLFAFDTVQNKWVLVGVLTAGNGAGGRGNNWAVIPLDFIGQKFNEDNDAPVTFRTSEGGALEWSFNSSTGAGALTQGTTTYAMHGQQGNDLNAGKNLIFQGQNGQINLKDSVSQGAGSLTFRDNYTVTTSNGSTWTGAGIVVDNGVSVNWQVNGVKGDNLHKIGEGTLTVQGTGINEGGLKVGDGKVVLNQQADNKGQVQAFSSVNIASGRPTVVLTDERQVNPDTVSWGYRGGTLDVNGNSLTFHQLKAADYGAVLANNVDKRATITLDYALRADKVALNGWSESGKGTAGNLYKYNNPYTNTTDYFILKQSTYGYFPTDQSSNATWEFVGHSQGDAQKLVADRFNTAGYLFHGQLKGNLNVDNRLPEGVTGALVMDGAADISGTFTQENGRLTLQGHPVIHAYNTQSVADKLAASGDHSVLTQPTSFSQEDWENRSFTFDRLSLKNTDFGLGRNATLNTTIQADNSSVTLGDSRVFIDKNDGQGTAFTLEEGTSVATKDADKSVFNGTVNLDNQSVLNINDIFNGGIQANNSTVNISSDSAVLGNSTLTSTALNLNKGANALASQSFVSDGPVNISDATLSLNSRPDEVSHTLLPVYDYAGSWNLKGDDARLNVGPYSMLSGNINVQDKGTVTLGGEGELSPDLTLQNQMLYSLFNGYRNIWSGSLNAPDATVSMTDTQWSMNGNSTAGNMKLNRTIVGFNGGTSPFTTLTTDNLDAVQSAFVMRTDLNKADKLVINKSATGHDNSIWVNFLKKPSNKDTLDIPLVSAPEATADNLFRASTRVVGFSDVTPILSVRKEDGKKEWVLDGYQVARNDGQGKAAATFMHISYNNFITEVNNLNKRMGDLRDINGEAGTWVRLLNGSGSADGGFTDHYTLLQMGADRKHELGSMDLFTGVMATYTDTDASADLYSGKTKSWGGGFYASGLFRSGAYFDVIAKYIHNENKYDLNFAGAGKQNFRSHSLYAGAEVGYRYHLTDTTFVEPQAELVWGRLQGQTFNWNDSGMDVSMRRNSVNPLVGRTGVVSGKTFSGKDWSLTARAGLHYEFDLTDSADVHLKDAAGEHQINGRKDSRMLYGVGLNARFGDNTRLGLEVERSAFGKYNTDDAINANIRYSF
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Interacts with hemoglobin, degrades it and subsequently binds the released heme. Could make heme accessible not only for E.coli, but also for B.fragilis during mixed intra-abdominal infections. Has a role in abscess formation.
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O88174
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MCP_MOUSE
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Membrane cofactor protein (CD antigen CD46)
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MTAAPLMPDSTHPCRRRKSYTFFWCSLGVYAEALLFLLSHLSDACELPRPFEAMELKGTPKLFYAVGEKIEYKCKKGYLYLSPYLMIATCEPNHTWVPISDAGCIKVQCTMLQDPSFGKVYYIDGSFSWGARAKFTCMEGYYVVGMSVLHCVLKGDDEAYWNGYPPHCEKIYCLPPPKIKNGTHTLTDINVFKYHEAVSYSCDPTPGPDKFSLVGTSMIFCAGHNTWSNSPPECKVVKCPNPVLQNGRLISGAGEIFSYQSTVMFECLQGFYMEGSSMVICSANNSWEPSIPKCLKGPRPTHPTKPPVYNYTGYPSPREGIFSQELDAWIIALIVITSIVGVFILCLIVLRCFEHRKKTNVSAAR
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May be involved in the fusion of the spermatozoa with the oocyte during fertilization.
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O88181
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BARH2_RAT
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BarH-like 2 homeobox protein (Bar-class homeodomain protein MBH1) (Homeobox protein B-H1)
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MTAMEGASGSSFGIDTILSGAGSGSPGMMNGDFRSLGEARTTDFRSQATPSPCSEIDTVGTAPSSPISVTLEPPEPHLVTDGPQHHHHLHHGQQPPPPSAPPAQSLQPSPQQQPPPQPQSAAQQLGSAAAAPRTSTSSFLIKDILGDSKPLAACAPYSTSVSSPHHTPKQECNAAHESFRPKLEQEDSKTKLDKREDSQSDIKCHGTKEEGDREITSSRESPPVRAKKPRKARTAFSDHQLNQLERSFERQKYLSVQDRMDLAAALNLTDTQVKTWYQNRRTKWKRQTAVGLELLAEAGNYSALQRMFPSPYFYHPSLLGSMDSTTAAAAAAAMYSSMYRTPPAPHPQLQRPLVPRVLIHGLGPGGQPALNPLSNPIPGTPHPR
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Potential regulator of neural basic helix-loop-helix genes. It may down-regulate expression of ASCL1 and, within the thalamus, up-regulate NGN2, thereby regulating distinct patterns of neuronal differentiation.
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O88182
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FGF18_RAT
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Fibroblast growth factor 18 (FGF-18)
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MYSAPSACTCLCLHFLLLCFQVQVLAAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQTELQKPFKYTTVTKRSRRIRPTHPG
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Plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. Required for normal ossification and bone development. Stimulates hepatic and intestinal proliferation (By similarity).
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O88188
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LY86_MOUSE
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Lymphocyte antigen 86 (Ly-86) (Protein MD-1)
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MNGVAAALLVWILTSPSSSDHGSENGWPKHTACNSGGLEVVYQSCDPLQDFGLSIDQCSKQIQSNLNIRFGIILRQDIRKLFLDITLMAKGSSILNYSYPLCEEDQPKFSFCGRRKGEQIYYAGPVNNPGLDVPQGEYQLLLELYNENRATVACANATVTSS
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May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression.
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O88196
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TTC3_MOUSE
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E3 ubiquitin-protein ligase TTC3 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TTC3) (TPR repeat protein D) (Mtprd)
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MDDFAEGGLSLADDILLEDYPYEDDCICTPDFTTDDYVRVTQLYYEGVGMQYKDYAQSEKNLEYDICNIWCSKPLSILQDYCDAIKLYIFWPLLFQHQHSSIISRLHPCVEAIRSRAAEISLKKLQHLELMEDIVDLAKKVANDSFLIEGLLKIGYKIENKILAMEDALNWIKYTGDVTILPKLGSVDNCWPMLSIFFTEYKYHITRVVTENCNLLEEFRRHSCMQCVKQGELMKMRGNEEFSKEKFEIAVIYYTRAIEYRPENHLLYGNRALCFLRMGQFRNALSDGKRAIVLKNTWPKGHYRYCDALCMLGEYDWALQANIKAQKLCKNDPEGIKDLIQQHVKLQKQIEDLQGRTSNKNPIKAFYESRAYIPRNSSAPAFRTSLNFVETERGFRKTKYKMANGGDQNQKVADEALKGDDCDCHPEFLPPPSQPPRHKGKQKSRNNESEKPSFNSEVSLQVDLKSILEKQFSKSSRAAHQDFANIMKMLRSLIQDGYTALLEQRCRSAAQAFTELLNGLDPQKIKQLNLAMINYVLVVYGLAVSLLGIGRPEELSEAENQFKRIIEHYPNEGLDCLAYCGIGKVYLKKNRFLEALNHFEKAKTLISRLPGILTWPTSNVIIEESKPEKVKVMLEKFVEECKFPPVPDAVCCYQKCRGYSKIQIYLTDPDFKGFIRISCCQYCKVEFHMNCWKKLKTTTFNDKIDKDFLQGICLTPDCEGIISKIIIYSSGGQVKCEFEHKVIKEKVPSRPVLKQKCSSLEKLRLKEDKKLKRKIQKQEAKKLAQERMEEDLRESNPPKNEEPEETSDSAQRCQFLDDRILQCIKQNADKIKSVVLNTSTLLKELLSWKVLSTEDYTTCFSSKNFVHEAVDYVIGHLIQEKNRVKTRIFLHVLSELKELDPKLAPWIQRLNSFGLDAIGPFFTRYGASLKELDFHVVTVLWDEKYGHKLGSIEGKQLDYFFEPASAMEARCLIWLLEEHRDKFPALHSALDEFFDIMDSRCTVLRKQDSDEMPFGCIKVKNKGKKKKPKDSKPMLVGSGAASVAPSSEAVTPEDHSRRNSDSAGPFAVPDHLRQDVEEFEALYDQHSSEYVVRNKKLWDINPKQKCSTLYDYFSQLLEEHGPLDMSDRMFSEEYEFFPEETRQILEKAGGLKSFLLGCPRFVVIDNCIALKKVASRLKKKRKKKNMKAKVEDISKTGEYLRVKLPLNPTAREFQPDVKSEALSEDVKSIPGPADSSTLAAEDLKAQLDSDSSSGSASEDSRLEVASPDSPTPLCEDASPSPTPAPEEAKPTYWAQSHLVTGFCTYLPFQGFGITQRPAYINMVPSLSQFTSIYTPLANISSEYPMQRSMPVVPSFVASNRADENAAAYFESPNLNTEHDSGDHMASETQILEDTLGVCVRSQGSAADADPALSEPEGNSEHSGSSDSLWEASLENVSGTTDAPAAPSVAIQVSRSMVHQEVNTEPYEPFETQQGDLSQKEKECHLLREQLKVACENCEQIELRSSQEIKDLEEKLQRHTEENKISKTELDWFLQDLDREIKKWQQEKKEIQERLKALKKKIKKVINTSEMSAQKNDGFDKECEPHPDQSLGFSSALTDEKTKAEESVRKGKELYEESHQRAVAAEVSVLENWKEREVCKLQGVASQSEAYLKSLKLMSSDSATYPDVEYDILSWESFLSTVREEIESKKSQFEEHIKAIKNGSRLSDLSSVQLSEVSFPGCSTIHPQFLSESSGHEDPGLVACVDSMTGAVLNDPYMDSASGCPEEVPELSLGSPTHQPEVTQQLELKGASQVSPSEQSPEADEKLSGQATRSSQSPKKPSNSIIEHLSVIFPCYTSTELAGFIKKVRNKTKNSFSGLTIEEIVEKVTEHIVDEQKKKKPNPGKDKKTSEAHSAASVAKSSQSPPLAAAGPSARTKGQKKDDVPAPDGNSCEICHEIFKSKNMRVLKCGHKFHKGCFKQWLKGQSTCPTCGSSDLLSEE
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E3 ubiquitin-protein ligase which catalyzes the formation of 'Lys-48'-polyubiquitin chains (By similarity). Mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus (By similarity). Acts as a terminal regulator of Akt signaling after activation its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation (By similarity). Positively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation by mediating the ubiquitination and subsequent degradation of SMURF2 (By similarity). Regulates neuronal differentiation by regulating actin remodeling and Golgi organization via a signaling cascade involving RHOA, CIT and ROCK (By similarity). Inhibits cell proliferation (By similarity).
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O88199
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CHST3_MOUSE
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Carbohydrate sulfotransferase 3 (EC 2.8.2.17) (EC 2.8.2.21) (Chondroitin 6-O-sulfotransferase 1) (C6ST-1) (Chondroitin 6-sulfotransferase) (C6ST) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0) (GST-0)
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MEKGLALPQDFRDLVHSLKIRGRYVLFLAFVVIVFIFIEKENKIISRVSDKLKQIPHFVADANSTDPALLLSENASLLSLSELDSTFSHLRSRLHNLSLQLGVEPAMESQEAGAEKPSQQAGAGTRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVFFQQRGASAAGSALVYRDVLKQLLLCDLYVLEPFISPPPEDHLTQFLFRRGSSRSLCEDPVCTPFVKKVFEKYHCRNRRCGPLNVTLAGEACRRKDHVALKAVRIRQLEFLQPLVEDPRLDLRVIQLVRDPRAVLASRIVAFAGKYENWKKWLSEGQDQLSEDEVQRLRGNCESIRLSAELGLRQPAWLRGRYMLVRYEDVARRPLQKAREMYSFAGIPLTPQVEDWIQKNTQATRDSSDVYSTQKNSSEQFEKWRFSMPFKLAQVVQAACGPTMHLFGYKLARDAASLTNRSISLLEERGTFWVT
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Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Catalyzes with a lower efficiency the sulfation of Gal residues of keratan sulfate, another glycosaminoglycan. Can also catalyze the sulfation of the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides (By similarity). May play a role in the maintenance of naive T-lymphocytes in the spleen.
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O88202
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LPP60_RAT
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60 kDa lysophospholipase (EC 3.1.1.5) (Lysophospholipase-transacylase) [Includes: L-asparaginase (EC 3.5.1.1) (L-asparagine amidohydrolase); 1-alkyl-2-acetylglycerophosphocholine esterase (EC 3.1.1.47) (Platelet-activating factor acetylhydrolase) (PAF acetylhydrolase)]
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MARATGPEQRLLAIYTGGTIGMRSEGGVLVPGRGLAAVLRTLHMLHDEEYARAHSLPEDTLVLPPASSDQRIIYKVLECQPLFDSSDMTITEWVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKASWKSHLVVHSNMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVTSDYAPGMAMAGAGIISGFDMTSEAALAKLSYVLGQPGLSLSDRKKLLAKDLRGEMTLPTTDDLLGDDMLGCRATWLLSMNGSQDADAMKDVLLPGLALAAAHAGDLDTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLSPQELEDVGTELCRLASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSLEDRVSAQPQPH
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Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities. Can catalyze three types of transacylation reactions: (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC) to the sn-1(3) positions of glycerol and 2-acylglycerol (sn-1 to -1(3) transfer), (2) acyl transfer from 1-acyl-GPC to the sn-2 positions of 1-acyl-GPC, 1-acyl-sn-glycero-3-phosphoethanolamine (1-acyl-GPE), and other lysophospholipids (sn-1 to -2 transfer) and (3) acyl transfer from 2-acyl-GPC to the sn-1 position of 2-acyl-GPC and 2-acyl-GPE (sn-2 to -1 transfer). Mediates the synthesis of 1-arachidonoyl species of phospholipids by transferring the arachidonoyl residue from 2-arachidonoyl lysophospholipid to the sn-1 position of 2-acyl lysophospholipid.
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O88207
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CO5A1_MOUSE
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Collagen alpha-1(V) chain
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MDVHTRWKAARPGALLLSSPLLLFLLLLWAPPSSRAAQPADLLEMLDFHNLPSGVTKTTGFCATRRSSSEPDVAYRVSKDAQLSMPTKQLYPESGFPEDFSILTTVKAKKGSQAFLVSIYNEQGIQQLGLELGRSPVFLYEDHTGKPGPEEYPLFPGINLSDGKWHRIALSVYKKNVTLILDCKKKITKFLSRSDHPIIDTNGIVMFGSRILDDEIFEGDIQQLLFVSDNRAAYDYCEHYSPDCDTAVPDTPQSQDPNPDEYYPEGEGETYYYEYPYYEDPEDPGKEPAPTQKPVEAARETTEVPEEQTQPLPEAPTVPETSDTADKEDSLGIGDYDYVPPDDYYTPPPYEDFGYGEGVENPDQPTNPDSGAEVPTSTTVTSNTSNPAPGEGKDDLGGEFTEETIKNLEENYYDPYFDPDSDSSVSPSEIGPGMPANQDTIFEGIGGPRGEKGQKGEPAIIEPGMLIEGPPGPEGPAGLPGPPGTTGPTGQMGDPGERGPPGRPGLPGADGLPGPPGTMLMLPFRFGGGGDAGSKGPMVSAQESQAQAILQQARLALRGPAGPMGLTGRPGPMGPPGSGGLKGEPGDMGPQGPRGVQGPPGPTGKPGRRGRAGSDGARGMPGQTGPKGDRGFDGLAGLPGEKGHRGDPGPSGPPGIPGDDGERGDDGEVGPRGLPGEPGPRGLLGPKGPPGPPGPPGVTGMDGQPGPKGNVGPQGEPGPPGQQGNPGAQGLPGPQGAIGPPGEKGPLGKPGLPGMPGADGPPGHPGKEGPPGEKGGQGPPGPQGPIGYPGPRGVKGADGIRGLKGTKGEKGEDGFPGFKGDMGIKGDRGEIGPPGPRGEDGPEGPKGRGGPNGDPGPLGPTGEKGKLGVPGLPGYPGRQGPKGSIGFPGFPGANGEKGGRGTPGKPGPRGQRGPTGPRGERGPRGITGKPGPKGNSGGDGPAGPPGERGPNGPQGPTGFPGPKGPPGPPGKDGLPGHPGQRGETGFQGKTGPPGPPGVVGPQGPTGETGPMGERGHPGPPGPPGEQGLPGAAGKEGTKGDPGPAGLPGKDGPPGLRGFPGDRGLPGPVGALGLKGSEGPPGPPGPAGSPGERGPAGAAGPIGIPGRPGPQGPPGPAGEKGLPGEKGPQGPAGRDGLQGPVGLPGPAGPVGPPGEDGDKGEIGEPGQKGSKGDKGEQGPPGPTGPQGPIGQPGPSGADGEPGPRGQQGLFGQKGDEGSRGFPGPPGPVGLQGLPGPPGEKGETGDVGQMGPPGPPGPRGPSGAPGADGPQGPPGGIGNPGAVGEKGEPGEAGDPGLPGEGGPLGPKGERGEKGEAGPSGAAGPPGPKGPPGDDGPKGSPGPVGFPGDPGPPGEPGPAGQDGPPGDKGDDGEPGQTGSPGPTGEPGPSGPPGKRGPPGPAGPEGRQGEKGAKGEAGLEGPPGKTGPIGPQGAPGKPGPDGLRGIPGPVGEQGLPGSPGPDGPPGPMGPPGLPGLKGDSGPKGEKGHPGLIGLIGPPGEQGEKGDRGLPGPQGSSGPKGDQGITGPSGPLGPPGPPGLPGPPGPKGAKGSSGPTGPKGEAGHPGLPGPPGPPGEVIQPLPIQASRTRRNIDASQLLDDGAGESYVDYADGMEEIFGSLNSLKLEIEQMKRPLGTQQNPARTCKDLQLCHPDFPDGEYWVDPNQGCSRDSFKVYCNFTAGGSTCVFPDKKSEGARITSWPKENPGSWFSEFKRGKLLSYVDAEGNPVGVVQMTFLRLLSASAHQNVTYNCYQSVAWQDAATGSYDKAIRFLGSNDEEMSYDNNPYIRALVDGCATKKGYQKTVLEIDTPKVEQVPIVDIMFNDFGEASQKFGFEVGPACFLG
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Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin (By similarity). Transcriptionally activated by CEBPZ, which recognizes a CCAAT-like motif, CAAAT in the COL5A1 promoter. {ECO:0000250, ECO:0000269|PubMed:15246108}.
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O88267
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ACOT1_RAT
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Acyl-coenzyme A thioesterase 1 (Acyl-CoA thioesterase 1) (EC 3.1.2.-) (CTE-I) (Inducible cytosolic acyl-coenzyme A thioester hydrolase) (LACH2) (ACH2) (Long chain acyl-CoA thioester hydrolase) (Long chain acyl-CoA hydrolase) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2)
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MEATLSLEPAGRSCWDEPLSITVRGLVPEQPVTLRAALRDEKGALFRARALYRADAHGELDLARAPALGGSFTGLEPMGLIWAMEPERPFWRLVKRDVQTPFVVELEVLDGHEPDGGRLLARAVHERHFMAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKTMETMRIEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTICYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVEQKSFIPVERSDTTFLFLVGQDDHNWKSEFYANEISKRLQAHGKEKPQIICYPEAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLGGKSHGVSPKI
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Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20).
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O88269
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MRP6_RAT
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ATP-binding cassette sub-family C member 6 (EC 7.6.2.-) (EC 7.6.2.3) (MRP-like protein 1) (MLP-1) (Multidrug resistance-associated protein 6)
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MNGEHSMATPGESCAGLRVWNQTEQEPVAYHLLNLCFLRAAGSWVPPMYLWVLGPIYLLYIHRHGCCYLRMSRLFKIKMVLGFALILLYTFNAAVPLWRIHRGMPQAPELLIHPTVWLTTMSFATFLIHMERKKGVRASGLLFGYWLLCCLVPAIDTVQQASAGSFRQEPLHHLATYLCLSLVVAELVLSCLVDQPPFFSEDSKPLNPCPEAEASFPSKAMFWWASGLLWKGYRKLLGPKDLWSLERENSSEELVSQLEREWRRNFSELPGHKGHSGMGTPETEAFLQPERSQRGPLLRAIWRVFRSTFLLGTLSLVISDAFRFAVPKLLSLFLEFMGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFLVALVVFAVHTLVAEDNAMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRLAAFLCLEEVDPNGMVLSPSRCSSKDRISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIGPSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGLLDGARQPAGEGEGEAHAAATSDDLGGFSGGGTPTRRPERPRPSDAAPVKGSTSEAQMEPSLDDVEVTGLTAGEDSVQYGRVKSATYLSYLRAVGTPLCTYTLFLFLCQQVASFCQGYWLSLWADDPVVDGKQMHSALRGSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLVFVAATCAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYVHTPKEAPWRLPSSAAQPLWPCGGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQESGLA
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ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of glutathione conjugates such as leukotriene-c4 (LTC4) and N-ethylmaleimide S-glutathione (NEM-GS) (in vitro) (By similarity). Transports also an anionic cyclopentapeptide endothelin antagonist, BQ-123. May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity). Mediates the release of nucleoside triphosphates, predominantly ATP, into the circulation, where it is rapidly converted into AMP and the mineralization inhibitor inorganic pyrophosphate (PPi) by the ecto-enzyme ectonucleotide pyrophosphatase phosphodiesterase 1 (ENPP1), therefore playing a role in PPi homeostasis.
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O88271
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CFDP1_MOUSE
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Craniofacial development protein 1 (27 kDa craniofacial protein) (Bucentaur) (Protein Cp27)
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MEEFDSEDFSTSDEDEDYLPSGGEYSEDDVNELVKEDEVDGEEQAEKTKGKRRKAQGIPARKRKQSGLLLEEEEDGKEDSGGSSSEEDEEEQEGGLGSENARKKKEDELWASFLNDVGPKSKAAPGSQTKVAEETEEISSNKPLVKADELDKPRESEKVKITKVFDFAGEEVRVTKEVDAASKEAKSFLKQTEREKPQALVTSPATPLPAGSGIKRASGMSSLLGKIGAKKQKMSTLEKSKLDWESFKEEEGIGEELAIHNRGKEGYIERKAFLDRVDHRQFEIERDLRLSKMKP
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May play a role during embryogenesis. May modulate tooth organogenesis since alterations of this protein function affect tooth organs size as well as individual cell fate and survival. In embryonic cells, blockage of the function results in increased number of apoptotic cells, reduced proliferation, alterations in cell shape and fibronection matrix synthesis.
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O88272
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MMP23_RAT
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Matrix metalloproteinase-23 (MMP-23) (EC 3.4.24.-) (metalloprotease in the female reproductive tract) (MIFR) [Cleaved into: Matrix metalloproteinase-23, soluble form]
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MGWRACLRPEASGAVQGRWLGAVLSGLCLLSALAFLEWLGSPTETAWNAAQGNVDAPDVGGSTPQVPSLLSMLVTRRRRYTLTPARLRWDHFNLTYRILSFPRNLLSPEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPVNHTDCLVSALHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTDLVHVAAHEIGHALGLMHSQQDQALMHLNATLRGWKALSQDELWGLHRLYGCLDRIFVCTSWARKGFCDVRQRLMKRLCPRSCDFCYEFPFPTVATTTSPTRTKTRFVREGRNMTFHCGQKILHKKGKVYWYKDQEPLEFSYPGYLALGEARLSIIANAVNEGTYTCVVRHRQRVLTTYSWRVRVRS
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Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum.
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O88273
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GREM2_MOUSE
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Gremlin-2 (Cysteine knot superfamily 1, BMP antagonist 2) (Protein related to DAN and cerberus) (PRDC)
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MFWKLSLTLLLVAVLVKVAETRKNRPAGAIPSPYKDGSSNNSERWHHQIKEVLASSQEALVVTERKYLKSDWCKTQPLRQTVSEEGCRSRTILNRFCYGQCNSFYIPRHVKKEEDSFQSCAFCKPQRVTSVIVELECPGLDPPFRIKKIQKVKHCRCMSVNLSDSDKQ
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Cytokine that inhibits the activity of BMP2 and BMP4 in a dose-dependent manner, and thereby modulates signaling by BMP family members. Contributes to the regulation of embryonic morphogenesis via BMP family members. Antagonizes BMP4-induced suppression of progesterone production in granulosa cells.
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O88275
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PPARG_RAT
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Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3)
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MGETLGDPPVDPEHGAFADALPMSTSQEITMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISAPHYEDIPFTRADPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNRPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFINLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKVLQKMTDLRQIVTEHVQLLHVIKKTETDMSLHPLLQEIYKDLY
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Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels.
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O88277
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FAT2_RAT
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Protocadherin Fat 2 (Multiple epidermal growth factor-like domains protein 1) (Multiple EGF-like domains protein 1)
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MTLVLLGLAILLLHRAACEKSLEETIPPLSWRFTHSLYNATIYENSAPKTYVESPVKMGMYLAEPHWVVKYRIISGDAAGVFKTEEHVVGNFCFLRIRTKSSNTALLNREVRDSYTLIVQASDKSLEFEALTQVVVHILDQNDLKPLFSPPSYRVTISEDRPLKSPICKVTATDADLGQNAEFYYAFNARSEVFAIHPTSGVVTVAGKLNVTRRGKYELQVLAVDRMRKISEGNGFGNLASLVIRVEPVHRKPPAINLVVLNPPEGDEGDIYAIVTVDTNGSGAEVDSLEVVGGDPGKYFKVLRSYAQGNEFNLVAVRDINWAEHPHGFNISLQTHSWSRFPPHSIIRAFHLPSWKLANLRFEKAVYRVKLSEFSPPGSRVALVKVTTALPNLRYSLKPSSRNTAFKLNARTGLITTTKLVDFHEQNQYQLHVKTSLGQATTTVIIDIVDCNNHAPVFNRSSYEGTLDENIPPGTSVLTVTATDQDHGDNGHITYSIAGPKAVPFSIDPLLGVISTTKPMDYELMKRIYTFRVRASDWGSPFRQEKEVSVSLRLKNLNDNQPMFEEVNCTVSLRQDVPVGKSIMAVSAIDMDELQNLKYEIVSGNEQDYFHLNHFSGVISLKRSFMNLTAVRPTIYSLKITASDGKNYASPTTLKVTVVKDPHSEVPVQCDKTGVLTHITKTILQSAGLQSQELGEEEFTSLSNYQINHHSPQFEDHFPQSIDILEQVPINTPLARLAATDPDTGFHGKLVYVISDGNEEGCFDIELETGLLMVAAALDYETTSFYVLNVTVYDLGTPPKSSWKLLTVTVKDWNDNPPRFPPGGYQLTISEDTEVGTTIAELKTEDADSEDNRRVRYTLLTPTEKFSLHPFTGELVVTGHLDRESESQYILKAEARDQPTKGHQLFSVTDLIVTLEDINDNPPQCITEHRRLKVPEDMPLGTVLTFLDASDPDLGPAGEVKYILVEDAHGTFQVHPMTGALSLEKELDFERRAGYNLSFWASDSGKPLSRRTLCHVEVLVMDVNENLHSPHFSSFVYQGQVQENSPAGTPVMVVTAQDDDSGLDGELQYFLRAGTGLETFSINQDTGMLETLAPLDREFTPYYWLTVLAVDRGSVPLSAVTEVYIEVTDINDNIPSMSRPVFYPSVLEDAPLGTSVLQLEAWDPDSSSQGKLTFNLTSGNHLGHFIVHPFTGLLTTAKQLDRENKDEYVLEVTVQDNGDPSLRSTSRVVVCILDVNDNPPMFSHKLFNVRLSERLSPLSPEPVYRLVASDPDEGLNGSVTYSIEESDEESFRIDPVTGVVSSSSTFAAGEYNILTIKATDSGQPALSTSVRLHIEWIPQPRPSSIPLSFDESYYSFTVMETDPVNHMVGVISVEGRPGLFWFHISDGDKDMDFDIEKTTGSIVIARPLDTRRKSSYNLTVEVTDGFHTIATQVHIFMIANINHHRPQFLQDHYEIRVPQDTLPGVELLRVQATDQDHGKGLIYTILSSQDPGSANLFQLDPSSGVLVTVGTLELHSGPSQHILTVMVRDQEMPIKRNFVWVTIHVEDGNLHSPHFTQLRYEANVPDTTAPGTELLQVRAVDADRGANAEIHYSFLKGNSDGFFNIDSLLGIITVAQRLYHVHLTRHALTVKAEDQGSPRRHDLALVVIHVHPSDSSAPVFSKDEYFIEIPESVPIGSPILLLSAGSSSEVTYELREGNKDSVFSMNSYSGLISTQKRLDHEKVPSYRLRIRGSNMAGVFTEVVALVYIIDENDNPPAFGKPTFLGHISEAAPLHSLILGEDNSPLVVRASDSDREANSLLVYKILEPEALKFFKIDPSMGTLTTTSELDFEDTPLFQFNIYVHDQGTPILFAPRSAKVIIHVRDVNDSPPRFSEQIYEVAVVEPIHPGMGLLTVQAEDNDSRVTYSIKTSNADEAVTIHPTTGQISVVNPATLRLFQKFSIRASDGLYHDTAVVKISLTQVLDKSLQFDQDVYRARVTENTPHRKALVILGVHGNHLNDTLSYFLLNGTDLFHMIESAGVLQTRGGTFDREQQDTHEVAVEVRDNRVPQRVAQALVRVSVEDVNDNIPEFQHLPYYTVIQDGTEPGDVLFQVSATDKDLGANGSVTYGFAEDYAYFRIDPYVGDISLKKPFDYQALNKYHLRVIARDSGIPPLQTEVEVHVTVRNKSNPLFQSPYYKVKVPENITLYTPILHTQARSPEGLRLIYNIVEEEPLMLFTTDFKTGVLTVTGPLDYESKNKHVFTVRATDTALGSFSEATVEVLVEDINDNPPTFSQLVYTTSVSEGSPAQTPVIQLLASDQDSGQNQDVSYQIVEDGSDVSKFFRINGSTGEIFTIQELDYETHQHFRVKVRAMDKGDPPLTGETLVVVNVSDINDNPPKFREPQYEANVSELATCGHLVLKVQALDPDIGDTSRLEYLILSGNQDRHFSINSTSGIISMFNLCKKQLDSSYNLRVGASDGVFRATVPVYINTTNANKYSPEFQQNVYEAELAENAKVGTKVIELLAIDKDSGPYGTVDYTIINKLAGERFFINPRGQITTLQKLDRENSTERVIAIKVMARDGGGKVAFCTVKIILTDENDNAPQFKASGYTVSIPSNVSRDSPIIQVLAYDADEGRNADVTYSVDSTEDLAEEIIEVNPTTGVVKVKESLVGLENRAVDFNIKAQDGGPPHWDSLVPVRLQVVPNEIPLPKFSEPLYTFSAPEDLPEGSEIGSVKAVAAQDPIIYSLVQGTTPESNSDDVFSLDQDTGVLKVRKAMDHESTKWYQIDLMAHCPHEDTDLVSLVSVSIQVEDVNDNRPVFEADPYKAFLTENMPGGTTVIQVTANDQDTGSDGQVSYRLSVEPGSNIHELFAVDSESGWITTLQELDCETQQTYRFYVVAFDHGQTIQLSSQALVEVSITDENDNPPRFASEDYRGSVVENNEPGELVATLKTLDADVSDQNRQVTCYITEGDPLGQFSISQVGDEWRISSRKTLDREHIAKYLLRVTASDGKFQASVPVEVFVVDINDNSPQCSQLLYTGKVREDVTPGHFILKVSAIDVDMDTNAQITYSLHGPGAQEFKLDPHTGELTTLTVLDRERKDVYNLVAKATDGGGQSCQAEVTLHIEDVNDNAPRFFPSHCDVAVFDNTTVKTPVAVVFARDPDQGANAQVVYSLTDSADGQFSIDATSGVIRLEKPLQVRASSAVELTVRASDLGTPIPLSTLGTVTVSVVGLEDYLPIFLNAEHSTQVPEDAPIDMEVLHLATLTRPGSEKTGYHITGGNEQGKFRLDAHTGILYVNGSLDFETNPKYFLSIECSRKSSSSLSDVTTIVINVTDVNEHHPRFTHDLYTVRVLENAVVGDVILTVSASDDDGPVNSAITYSLVGGNQLGHFTINPKKGKLQVAKALDWEQTPSYSLRLRATDSGQPPLHEDTEVAVEVVDVNDNPPRFFQLNYSTSVQENSPIGIKVLQLILDDPDSPQNGPPYFFRITEGNTGSVFRVTPDGWLVTAASLSKKAREWYQLHIEVSDSGLPPLSSSTLVRVQVTEQSRYPPSTLPLEISITKGEEEFQGGMIGKIHATDRDPQDTLTYSLEQEGGLDRYFTVGASDGKIIASQGLPHGRYSFNVTVSDGTFTTTTGVHVHVWHMEPEVPQQAVWLGFHQLTPEELVSDHWRNLQRFLSNLLDVKRANIHLASLQPAEVTAGVDVLLVFERHSGTSYDLQELASAIAHSVREIEHSVGIRMRSALPVVPCQGQSCQDQTCQETVSLEPRVGPSYSTARLSILTPRHHLGRNCSCNGTTLRFSGQSYVQYRPLEAQNWQIHFYLKTLQPWALLMFTNETASISLKLANGFSHLEYHCPGGFYGNLSSRYPVNDGQWHSMLLEERDTSVHLLVDITDNASLVIPEECQGLRTERQLLLGGLVPSNPSSNVSLGFEGCLDAVVVNGERLELLGREKKMEGRLETWALSQCCWPGTACSQSPCLNGGSCSPALGSGYLCRCPPPFSGRNCELGRENCTSAPCQEGGTCVSSPEGTSCNCPHPYTGDRCEMEARGCSGGHCLITPEIKRGDWGQQEFLVITVALPLVIIATVGLLLYCRRRKSHKPVTMEDPDLLARSIGVDTQASPAIELDPLNTSSCNNLNQPEPSKTSVPNELVTFGPSSKQRPMVCSVPPRLPPAAVSSHPGHEPIIKRTWSGEELVYPSGAAVWPPTYSRKKHWEYPHPETMQGTLPPSPRRHVGPAVMPDPTGLYGGFPFPLELENKRAPLPPRYSNQNLEDLMPPRPPSPREHLLAPCLNEYTAISYYHSQFRQGGGGPCLAEGGYKGVSMRLSRAGPSYADCEVNGGPATGRSQPRAPPNYEGSDMVESDYGSCEEVMF
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Involved in the regulation of cell migration. May be involved in mediating the organization of the parallel fibers of granule cells during cerebellar development.
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O88278
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CELR3_RAT
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Cadherin EGF LAG seven-pass G-type receptor 3 (Multiple epidermal growth factor-like domains protein 2) (Multiple EGF-like domains protein 2)
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MARRPLWWGLPGPSTPLLLLLLFSLFPSSREEMGGGGDQGWDPGVATATGPRAQIGSGAVALCPESPGVWEDGDPGLGVREPVFMKLRVGRQNARNGRGAPEQPNREPVVQALGSREQEAGQGSGYLLCWHPEISSCGRTGHLRRGSLPLDALSPGDSDLRNSSPHPSELLAQPDSPRPVAFQRNGRRSIRKRVETFRCCGKLWEPGHKGQGERSATSTVDRGPLRRDCLPGSLGSGLGEDSAPRAVRTAPAPGSAPHESRTAPERMRSRGLFRRGFLFERPGPRPPGFPTGAEAKRILSTNQARSRRAANRHPQFPQYNYQTLVPENEAAGTAVLRVVAQDPDPGEAGRLVYSLAALMNSRSLELFSIDPQSGLIRTAAALDRESMERHYLRVTAQDHGSPRLSATTMVAVTVADRNDHAPVFEQAQYRETLRENVEEGYPILQLRATDGDAPPNANLRYRFVGSPAARTAAAAAFEIDPRSGLISTSGRVDREHMESYELVVEASDQGQEPGPRSATVRVHITVLDENDNAPQFSEKRYVAQVREDVRPHTVVLRVTATDKDKDANGLVHYNIISGNSRGHFAIDSLTGEIQVMAPLDFEAEREYALRIRAQDAGRPPLSNNTGLASIQVVDINDHSPIFVSTPFQVSVLENAPLGHSVIHIQAVDADHGENSRLEYSLTGVASDTPFVINSATGWVSVSGPLDRESVEHYFFGVEARDHGSPPLSASASVTVTVLDVNDNRPEFTMKEYHLRLNEDAAVGTSVVSVTAVDRDANSAISYQITGGNTRNRFAISTQGGMGLVTLALPLDYKQERYFKLVLTASDRALHDHCYVHINITDANTHRPVFQSAHYSVSMNEDRPVGSTVVVISASDDDVGENARITYLLEDNLPQFRIDADSGAITLQAPLDYEDQVTYTLAITARDNGIPQKADTTYVEVMVNDVNDNAPQFVASHYTGLVSEDAPPFTSVLQISATDRDAHANGRVQYTFQNGEDGDGDFTIEPTSGIVRTVRRLDREAVPVYELTAYAVDRGVPPLRTPVSIQVTVQDVNDNAPVFPAEEFEVRVKENSIVGSVVAQITAVDPDDGPNAHIMYQIVEGNIPELFQMDIFSGELTALIDLDYEARQEYVIVVQATSAPLVSRATVHVRLVDQNDNSPVLNNFQILFNNYVSNRSDTFPSGIIGRIPAYDPDVSDHLFYSFERGNELQLLVVNQTSGELRLSRKLDNNRPLVASMLVTVTDGLHSVTAQCVLRVVIITEELLANSLTVRLENMWQERFLSPLLGHFLEGVAAVLATPTEDVFIFNIQNDTDVGGTVLNVSFSALAPRGAGAGAAGPWFSSEELQEQLYVRRAALAARSLLDVLPFDDNVCLREPCENYMKCVSVLRFDSSAPFLASASTLFRPIQPIAGLRCRCPPGFTGDFCETELDLCYSNPCRNGGACARREGGYTCVCRPRFTGEDCELDTEAGRCVPGVCRNGGTCTNAPNGGFRCQCPAGGAFEGPRCEVAARSFPPSSFVMFRGLRQRFHLTLSLSFATVQPSGLLFYNGRLNEKHDFLALELVAGQVRLTYSTGESSTVVSPTVPGGLSDGQWHTVHLRYYNKPRTDALGGAQGPSKDKVAVLSVDDCNVAVALRFGAEIGNYSCAAAGVQTSSKKSLDLTGPLLLGGVPNLPENFPVSRKDFIGCMRDLHIDGRRVDMAAFVANNGTTAGCQAKSHFCASGPCKNGGLCSERWGGFSCDCPVGFGGKDCRLTMAHPYHFQGNGTLSWDFGNDMPVSVPWYLGLSFRTRATKGVLMQVQLGPHSVLLCKLDQGLLSVTLSRASGHAVHLLLDQMTVSDGRWHDLRLELQEEPGGRRGHHIFMVSLDFTLFQDTMAMGSELEGLKVKHLHVGGPPPSSKEEGPQGLVGCIQGVWTGFTPFGSSALPPPSHRINVEPGCTVTNPCASGPCPPHANCKDLWQTFSCTCWPGYYGPGCVDACLLNPCQNQGSCRHLQGGPHGYTCDCASGYFGQHCEHRMDQQCPRGWWGSPTCGPCNCDVHKGFDPNCNKTSGQCHCKEFHYRPRGSDSCLPCDCYPVGSTSRSCAPHSGQCPCRPGALGRQCNSCDSPFAEVTASGCRVLYDACPKSLRSGVWWPQTKFGVLATVPCPRGALGLRGTGAAVRLCDEDHGWLEPDFFNCTSPAFRELSLLLDGLELNKTALDTVEAKKLAQRLREVTGQTDHYFSQDVRVTARLLAYLLAFESHQQGFGLTATQDAHFNENLLWAGSALLAPETGDLWAALGQRAPGGSPGSAGLVRHLEEYAATLARNMDLTYLNPVGLVTPNIMLSIDRMEQPSSSQGAHRYPRYHSNLFRGQDAWDPHTHVLLPSQSPQPSPSEVLPTSSNAENATASGVVSPPAPLEPESEPGISIVILLVYRALGGLLPAQFQAERRGARLPQNPVMNSPVVSVAVFRGRNFLRGALVSPINLEFRLLQTANRSKAICVQWDPPGPADQHGMWTARDCELVHRNGSHARCRCSRTGTFGVLMDASPRERLEGDLELLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMNGIMFLLAARTSCSTGQREAKKTSVLRTLRSSFLLLLLVSASWLFGLLAVNHSVLAFHYLHAGLCGLQGLAVLLLFCVLNADARAAWTPACLGKKAAPEETRPAPGPGSGAYNNTALFEESGLIRITLGASTVSSVSSARSGRAQDQDSQRGRSYLRDNVLVRHGSTAEHAEHSLQAHAGPTDLDVAMFHRDAGADSDSDSDLSLEEERSLSIPSSESEDNGRTRGRFQRPLRRAAQSERLLAHPKDVDGNDLLSYWPALGECEAAPCALQAWGSERRLGLDSNKDAANNNQPELALTSGDETSLGRAQRQRKGILKNRLQYPLVPQTRGTPELSWCRAATLGHRAVPAASYGRIYAGGGTGSLSQPASRYSSREQLDLLLRRQLSRERLEEVPVPAPVLHPLSRPGSQERLDTAPARLEPRDRGSTLPRRQPPRDYPGTMAGRFGSRDALDLGAPREWLSTLPPPRRNRDLDPQHPPLPLSPQRPLSRDPLLPSRPLDSLSRISNSRERLDQVPSRHPSREALGPAPQLLRAREDPASGPSHGPSTEQLDILSSILASFNSSALSSVQSSSTPSGPHTTATPSATASALGPSTPRSATSHSISELSPDSEVPRSEGHS
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Receptor that may have an important role in cell/cell signaling during nervous system formation.
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O88279
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SLIT1_RAT
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Slit homolog 1 protein (Slit-1) (Multiple epidermal growth factor-like domains protein 4) (Multiple EGF-like domains protein 4)
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MALTPQRGSSSGLSRPELWLLLWAAAWRLGATACPALCTCTGTTVDCHGTGLQAIPKNIPRNTERLELNGNNITRIHKNDFAGLKQLRVLQLMENQIGAVERGAFDDMKELERLRLNRNQLQVLPELLFQNNQALSRLDLSENSLQAVPRKAFRGATDLKNLQLDKNQISCIEEGAFRALRGLEVLTLNNNNITTIPVSSFNHMPKLRTFRLHSNHLFCDCHLAWLSQWLRQRPTIGLFTQCSGPASLRGLNVAEVQKSEFSCSGQGEAAQVPACTLSSGSCPAMCSCSNGIVDCRGKGLTAIPANLPETMTEIRLELNGIKSIPPGAFSPYRKLRRIDLSNNQIAEIAPDAFQGLRSLNSLVLYGNKITDLPRGVFGGLYTLQLLLLNANKINCIRPDAFQDLQNLSLLSLYDNKIQSLAKGTFTSLRAIQTLHLAQNPFICDCNLKWLADFLRTNPIETTGARCASPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYHLNSECTSDVACPHKCRCEASVVECSGLKLSKIPERIPQSTTELRLNNNEISILEATGLFKKLSHLKKINLSNNKVSEIEDGTFEGATSVSELHLTANQLESVRSGMFRGLDGLRTLMLRNNRISCIHNDSFTGLRNVRLLSLYDNHITTISPGAFDTLQALSTLNLLANPFNCNCQLAWLGDWLRKRKIVTGNPRCQNPDFLRQIPLQDVAFPDFRCEEGQEEVGCLPRPQCPQECACLDTVVRCSNKHLQALPKGIPKNVTELYLDGNQFTLVPGQLSTFKYLQLVDLSNNKISSLSNSSFTNMSQLTTLILSYNALQCIPPLAFQGLRSLRLLSLHGNDVSTLQEGIFADVTSLSHLAIGANPLYCDCHLRWLSSWVKTGYKEPGIARCAGPPEMEGKLLLTTPAKKFECQGPPSLAVQAKCDPCLSSPCQNQGTCHNDPLEVYRCTCPSGYKGRNCEVSLDSCSSNPCGNGGTCHAQEGEDAGFTCSCPSGFEGLTCGMNTDDCVKHDCVNGGVCVDGIGNYTCQCPLQYTGRACEQLVDFCSPDLNPCQHEAQCVGTPEGPRCECVPGYTGDNCSKNQDDCKDHQCQNGAQCVDEINSYACLCAEGYSGQLCEIPPAPRNSCEGTECQNGANCVDQGSRPVCQCLPGFGGPECEKLLSVNFVDRDTYLQFTDLQNWPRANITLQVSTAEDNGILLYNGDNDHIAVELYQGHVRVSYDPGSYPSSAIYSAETINDGQFHTVELVTFDQMVNLSIDGGSPMTMDNFGKHYTLNSEAPLYVGGMPVDVNSAAFRLWQILNGTSFHGCIRNLYINNELQDFTKTQMKPGVVPGCEPCRKLYCLHGICQPNATPGPVCHCEAGWGGLHCDQPVDGPCHGHKCVHGKCVPLDALAYSCQCQDGYSGALCNQVGAVAEPCGGLQCLHGHCQASATRGAHCVCSPGFSGELCEQESECRGDPVRDFHRVQRGYAICQTTRPLSWVECRGACPGQGCCQGLRLKRRKLTFECSDGTSFAEEVEKPTKCGCAPCA
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Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb (By similarity). {ECO:0000250, ECO:0000269|PubMed:10864956}.
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O88280
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SLIT3_RAT
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Slit homolog 3 protein (Slit-3) (Multiple epidermal growth factor-like domains protein 5) (Multiple EGF-like domains protein 5)
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MAPGRTGAGAAVRARLALALALASILSGPPAAACPTKCTCSAASVDCHGLGLRAVPRGIPRNAERLDLDRNNITRITKMDFTGLKNLRVLHLEDNQVSVIERGAFQDLKQLERLRLNKNKLQVLPELLFQSTPKLTRLDLSENQIQGIPRKAFRGVTGVKNLQLDNNHISCIEDGAFRALRDLEILTLNNNNISRILVTSFNHMPKIRTLRLHSNHLYCDCHLAWLSDWLRQRRTIGQFTLCMAPVHLRGFSVADVQKKEYVCPGPHSEAPACNANSLSCPSACSCSNNIVDCRGKGLTEIPANLPEGIVEIRLEQNSIKSIPAGAFIQYKKLKRIDISKNQISDIAPDAFQGLKSLTSLVLYGNKITEIPKGLFDGLVSLQLLLLNANKINCLRVNTFQDLQNLNLLSLYDNKLQTISKGLFAPLQSIQTLHLAQNPFVCDCHLKWLADYLQDNPIETSGARCSSPRRLANKRISQIKSKKFRCSGSEDYRNRFSSECFMDLVCPEKCRCEGTIVDCSNQKLSRIPSHLPEYTTDLRLNDNDIAVLEATGIFKKLPNLRKINLSNNRIKEVREGAFDGAAGVQELMLTGNQLETMHGRMFRGLSGLKTLMLRSNLISCVNNDTFAGLSSVRLLSLYDNRITTISPGAFTTLVSLSTINLLSNPFNCNCHMAWLGRWLRKRRIVSGNPRCQKPFFLKEIPIQDVAIQDFTCEGNEENSCQLSPRCPEQCTCVETVVRCSNRGLHTLPKGMPKDVTELYLEGNHLTAVPKELSTFRQLTLIDLSNNSISMLTNHTFSNMSHLSTLILSYNRLRCIPVHAFNGLRSLRVLTLHGNDISSVPEGSFNDLTSLSHLALGINPLHCDCSLRWLSEWIKAGYKEPGIARCSSPESMADRLLLTTPTHRFQCKGPVDINIVAKCNACLSSPCKNNGTCSQDPVEQYRCTCPYSYKGKDCTVPINTCVQNPCQHGGTCHLSESHRDGFSCSCPLGFEGQRCEINPDDCEDNDCENSATCVDGINNYACVCPPNYTGELCDEVIDYCVPEMNLCQHEAKCISLDKGFRCECVPGYSGKLCETDNDDCVAHKCRHGAQCVDAVNGYTCICPQGFSGLFCEHPPPMVLLQTSPCDQYECQNGAQCIVVQQEPTCRCPPGFAGPRCEKLITVNFVGKDSYVELASAKVRPQANISLQVATDKDNGILLYKGDNDPLALELYQGHVRLVYDSLSSPPTTVYSVETVNDGQFHSVELVMLNQTLNLVVDKGAPKSLGKLQKQPAVGINSPLYLGGIPTSTGLSALRQGADRPLGGFHGCIHEVRINNELQDFKALPPQSLGVSPGCKSCTVCRHGLCRSVEKDSVVCECHPGWTGPLCDQEAQDPCLGHSCSHGTCVATGNSYVCKCAEGYEGPLCDQKNDSANACSAFKCHHGQCHISDRGEPYCLCQPGFSGNHCEQENPCLGEIVREAIRRQKDYASCATASKVPIMVCRGGCGSQCCQPIRSKRRKYVFQCTDGSSFVEEVERHLECGCRECS
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May act as molecular guidance cue in cellular migration, and function may be mediated by interaction with roundabout homolog receptors.
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O88282
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BCL6B_MOUSE
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B-cell CLL/lymphoma 6 member B protein (Bcl6-associated zinc finger protein)
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MGSTAAPEGALGYVREFTRHSSDVLSNLNELRLRGILTDVTLLVGGQPLRAHKAVLIACSGFFYSIFRGRAGLGVDVLSLPGGPEARGFAPLLDFMYTSRLRLSPATAPAVLAAATYLQMEHVVQACHRFIQASYEPLGISLRPVEVEPPRPPTVAPPGSPRRSEGHPDPPTESRSCSQGSPSPASPDPKACNWKKYKFIVLNSQTSQAGSLVGESSGQPCPQARLPSGDEACSSSSSSEEGTTPGLQSRLSLATTTARFKCGALANNSYLFTPRAQETSLPASKQANPPPGSEFFSCQNCEAVAGCSSGLELLAPGDEDKPYKCQLCRSAFRYKGNLASHRTVHTGEKPYRCSICGARFNRPANLKTHSRIHSGEKPYKCETCGSRFVQVAHLRAHVLIHTGEKPYPCPTCGTRFRHLQTLKSHVRIHTGEKPYHCDPCGLHFRHKSQLRLHLRQKHGAATNTKVRYHILGGP
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Acts as a sequence-specific transcriptional repressor in association with BCL6. Necessary for activation of naive T-cells to antigenic stimulation. May attenuate the regulatory effect of BCL6 on antigenic activation of naive CD4 T-cells by forming a heterodimer with BCL6.
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O88286
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WIZ_MOUSE
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Protein Wiz (Widely-interspaced zinc finger-containing protein)
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MEGLLAGGLAAPDHPRGPAPREDIESGAEAAEGEGDIFPSSHYLPITKEGPRDILDGRSGISDGQPHPGLSEALPRATSATHRISSCYWDGDSLDFQPGSPPPHLLGPFPASLDVQGSWEHPMVQEAREGTPSEQRFKDSVIVRTMKPYAKLKGSRKFLHHQGEVKFLEKYSPSHHKFDWLQDTDEQGPLKDTGLHLDLPAQPPTVTSFRRVIVPVDNTPKTLDMEVMGTREDLEDFGQVAQPSEWGLHTSASEVATQTWTVNSEASVERLQPLLSPVQTGPYLCELLQEVAGGVDSNEEEEEEPAVFPCIECSIYFKHKEHLLEHMSQHRRAPGQEPPADLAPLACSECGWAFTEPTALEQHWQLHQASREKIIEEIQKLKQFPGDEGREARLQCSKCVFGTNSSRAFMQHAKLHVRGSLPSRQATEPFRGGSPVLDVSTLVYPSYGDSSGLNTCVHCGFTAPSKSLLREHTRLVHAHHAHWEEVGEAFEDLTSQPCTSQDAYTHSPDTATVDYFSKSEPLLASVWQENPSGYDPDLAFGPDYQQPGMRNFPLLNSGQQSLGKLAFPSPMASASYSIQRNRNKSTVHLQRMEDKSHLWSEEEEEEDEDVVLTSERDFTPENGAFPPLAIPSLIPQPALELKQTFQDALQAVDASETQQQQLQGMVPIVLMAKLRPQVIAATTRASPQLPPEEPELRSTHPLDFLLLDAPLGGSLGLNTLLEGDPAMALKHEERKCPYCPDRFHYGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQKKKKKVANFDPGTFSLMRCDFCGAGFDTRAGLSSHARAHLRDFGITNWELTISPINILQELLATSAAELPPSPLGREPGGPPRSFLTSRRPRLPLTMPFPPTWAEDPGPIYGDAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAPLGLTPSLTKKSNSPKEFLAGAARPGLLTLAKPMDAPAVNKAIKSPPGFSAKGLTHPSSSPLLKKAPLTLAGSPTPKNPEDKSPQLSLSPRPTSPKAQWPQSEDEGPLNLTSGPEPTRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGHLHPPGPSPKALAKVLSTGGPGSSLEARSPSDLHISPLTKKLPPPPGSPLGHSPTASPPPTARKMFSGLATPSLPKKLKPEHMRVEIKREMLPGTLHGEPHPSEGPWGTPREDMAPLNLSARAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKLCLIKKEPPAGDLAPALTEDGSPTAAPGALHSPLPLSPLASRPGKPGAGPTQVPRELSLSPITGSKPSAASYLGPVATKRPLQEDRFLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPPLGLAPGGLSLVGRSAGGEPGLEAGRAADSGERPLATSPPGTVKSEEHQRQNINKFERRQARPSDASAARGGEEVNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEEPQAPQAQTAAVEAP
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May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization.
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O88291
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ZN326_MOUSE
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DBIRD complex subunit ZNF326 (Zinc finger protein 326) (Zinc finger protein interacting with mRNPs) (Zinc finger protein-associated with nuclear matrix of 75 kDa)
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MDFEDDYVHSTCRGAYQDFNGMDRDYGPGSYGGLDRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGGGSRFGPYESYDSRSSLGGRDLYRSGYGFNEPEQTRFGGSYGGRFESSYRNSLDSFGGRNQGGSSWEAPYSRSKLRPGFMEDRGRENYSSYSSFSSPHMKPAPVGSRGRGTPAYPESTFGSRSYDAFGGPSTGRGRGRGHMGDFGSFHRPGIIVDYQNKPANVTIATARGIKRKMMQIFIKPGGAFIKKPKLAKPMDKMNLSKSPTKTDPKNEEEEKRRIEARREKQRRRREKNSEKYGDGYRMAFTCSFCKFRTFEEKDIELHLESSSHQETLDHIQKQTKFDKVVMEFLHECMVNKFKKASIRKQQTLNHPEAYKIIEKDIMEGVTADDHMMKVETVHCSACSVYIPALHSSVQLHLKSPDHSKGKQAYKEQIKRESVLTATSILNNPIVKARYERFVKGENPFEIQDHPQDQQIEGDEEDEEKIDEPIEEEEEEEEEEEEEGEEAGSVEEEGDVEGEEGTAEAAAAGEADAVGEAEGAGEAEEAEEEEEEEGTQEFAAQACATEQCEHRQM
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Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions (By similarity). May also play a role in neuronal differentiation. Able to bind DNA and activate expression in vitro. {ECO:0000250, ECO:0000269|PubMed:10798446}.
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O88307
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SORL_MOUSE
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Sortilin-related receptor (Gp250) (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (SorLA-1) (Sorting protein-related receptor containing LDLR class A repeats) (mSorLA)
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MATRSSRRESRLPFLFALVALLPRGALGGGWTQRLHGGPAPLPQDRGFFVVQGDPRDLRLGTHGDAPGASPAARKPLRTRRSAALQPQPIQVYGQVSLNDSHNQMVVHWAGEKSNVIVALARDSLALARPKSSDVYVSYDYGKSFSKISEKLNFGVGNNSEAVISQFYHSPADNKRYIFVDAYAQYLWITFDFCSTIHGFSIPFRAADLLLHSKASNLLLGFDRSHPNKQLWKSDDFGQTWIMIQEHVKSFSWGIDPYDQPNAIYIERHEPFGFSTVLRSTDFFQSRENQEVILEEVRDFQLRDKYMFATKVVHLPGSQQQSSVQLWVSFGRKPMRAAQFVTKHPINEYYIADAAEDQVFVCVSHSNNSTNLYISEAEGLKFSLSLENVLYYSPGGAGSDTLVRYFANEPFADFHRVEGLQGVYIATLINGSMNEENMRSVITFDKGGTWEFLQAPAFTGYGEKINCELSQGCSLHLAQRLSQLLNLQLRRMPILSKESAPGLIIATGSVGKNLASKTNVYISSSAGARWREALPGPHYYTWGDHGGIIMAIAQGMETNELKYSTNEGETWKTFVFSEKPVFVYGLLTEPGEKSTVFTIFGSNKESVHSWLILQVNATDALGVPCTENDYKLWSPSDERGNECLLGHKTVFKRRTPHATCFNGEDFDRPVVVSNCSCTREDYECDFGFKMSEDLSLEVCVPDPEFSGKPYSPPVPCPVGSSYRRTRGYRKISGDTCSGGDVEARLEGELVPCPLAEENEFILYAMRKSIYRYDLASGATEQLPLSGLRAAVALDFDYERNCLYWSDLALDTIQRLCLNGSTGQEVIINSGLETVEALAFEPLSQLLYWVDAGFKKIEVANPDGDFRLTIVNSSVLDRPRALVLVPQEGVMFWTDWGDLKPGIYRSYMDGSAAYRLVSEDVKWPNGISVDSQWIYWTDAYLDCIERITFSGQQRSVILDSLPHPYAIAVFKNEIYWDDWSQLSIFRASKHSRSQVEILASQLTGLMDMKVFYKGKNAGSNACVPQPCSLLCLPKANNSKSCRCPEGVASSVLPSGDLMCDCPQGYQRKNNTCVKEENTCLRNQYRCSNGNCINSIWWCDFDNDCGDMSDERNCPTTVCDADTQFRCQESGTCIPLSYKCDLEDDCGDNSDESHCEMHQCRSDEFNCSSGMCIRSSWVCDGDNDCRDWSDEANCTAIYHTCEASNFQCHNGHCIPQRWACDGDADCQDGSDEDPVSCEKKCNGFHCPNGTCIPSSKHCDGLRDCPDGSDEQHCEPFCTRFMDFVCKNRQQCLFHSMVCDGIVQCRDGSDEDAAFAGCSQDPEFHKECDEFGFQCQNGVCISLIWKCDGMDDCGDYSDEANCENPTEAPNCSRYFQFHCENGHCIPNRWKCDRENDCGDWSDEKDCGDSHVLPSPTPGPSTCLPNYFHCSSGACVMGTWVCDGYRDCADGSDEEACPSLANSTAASTPTQFGQCDRFEFECHQPKKCIPNWKRCDGHQDCQDGQDEANCPTHSTLTCTSREFKCEDGEACIVLSERCDGFLDCSDESDEKACSDELTVYKVQNLQWTADFSGDVTLTWMRPKKMPSASCVYNVYYRVVGESIWKTLETHSNKTSTVLKVLKPDTTYQVKVQVHCLNKVHNTNDFVTLRTPEGLPDAPRNLQLSLNSEEEGVILGHWAPPVHTHGLIREYIVEYSRSGSKMWASQRAASNSTEIKNLLLNALYTVRVAAVTSRGIGNWSDSKSITTIKGKVIQAPNIHIDSYDENSLSFTLTMDGDIKVNGYVVNLFWSFDAHKQEKKTLSFRGGSALSHRVSNLTAHTSYEISAWAKTDLGDSPLAFEHILTRGSSPPAPSLKAKAINQTAVECIWTGPKNVVYGIFYATSFLDLYRNPKSVTTSLHNKTVIVSKDEQYLFLVRVLIPYQGPSSDYVVVKMIPDSRLPPRHLHAVHIGKTSALIKWESPYDSPDQDLFYAIAVKDLIRKTDRSYKVRSRNSTVEYSLSKLEPGGKYHIIVQLGNMSKDSSIKITTVSLSAPDALKIITENDHVLLFWKSLALKEKQFNETRGYEIHMSDSAVNLTAYLGNTTDNFFKVSNLKMGHNYTFTVQARCLFGSQICGEPAVLLYDELSSGADAAVIQAARSTDVAAVVVPILFLILLSLGVGFAILYTKHRRLQSSFSAFANSHYSSRLGSAIFSSGDDLGEDDEDAPMITGFSDDVPMVIA
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Sorting receptor that directs several proteins to their correct location within the cell. Along with AP-1 complex, involved Golgi apparatus - endosome sorting. Sorting receptor for APP, regulating its intracellular trafficking and processing into amyloidogenic-beta peptides. Retains APP in the trans-Golgi network, hence preventing its transit through late endosomes where amyloid beta peptides Abeta40 and Abeta42 are generated. May also sort newly produced amyloid-beta peptides to lysosomes for catabolism. Does not affect APP trafficking from the endoplasmic reticulum to Golgi compartments (By similarity). Sorting receptor for the BDNF receptor NTRK2/TRKB that facilitates NTRK2 trafficking between synaptic plasma membranes, postsynaptic densities and cell soma, hence positively regulates BDNF signaling by controlling the intracellular location of its receptor. Sorting receptor for GDNF that promotes GDNF regulated, but not constitutive secretion. Sorting receptor for the GDNF-GFRA1 complex, directing it from the cell surface to endosomes. GDNF is then targeted to lysosomes and degraded, while its receptor GFRA1 recycles back to the cell membrane, resulting in a GDNF clearance pathway. The SORL1-GFRA1 complex further targets RET for endocytosis, but not for degradation, affecting GDNF-induced neurotrophic activities. Sorting receptor for ERBB2/HER2. Regulates ERBB2 subcellular distribution by promoting its recycling after internalization from endosomes back to the plasma membrane, hence stimulating phosphoinositide 3-kinase (PI3K)-dependent ERBB2 signaling (By similarity). Sorting receptor for lipoprotein lipase LPL. Promotes LPL localization to endosomes and later to the lysosomes, leading to degradation of newly synthesized LPL (By similarity). Potential sorting receptor for APOA5, inducing APOA5 internalization to early endosomes, then to late endosomes, wherefrom a portion is sent to lysosomes and degradation, another portion is sorted to the trans-Golgi network (By similarity). Sorting receptor for the insulin receptor INSR. Promotes recycling of internalized INSR via the Golgi apparatus back to the cell surface, thereby preventing lysosomal INSR catabolism, increasing INSR cell surface expression and strengthening insulin signal reception in adipose tissue. Does not affect INSR internalization. Plays a role in renal ion homeostasis, controlling the phospho-regulation of SLC12A1/NKCC2 by STK39/SPAK kinase and PPP3CB/calcineurin A beta phosphatase, possibly through intracellular sorting of STK39 and PPP3CB. Stimulates, via the N-terminal ectodomain, the proliferation and migration of smooth muscle cells, possibly by increasing cell surface expression of the urokinase receptor uPAR/PLAUR. This may promote extracellular matrix proteolysis and hence facilitate cell migration (By similarity). By acting on the migration of intimal smooth muscle cells, may accelerate intimal thickening following vascular injury. Promotes adhesion of monocytes (By similarity). Stimulates proliferation and migration of monocytes/macrophages. Through its action on intimal smooth muscle cells and macrophages, may accelerate intimal thickening and macrophage foam cell formation in the process of atherosclerosis. Regulates hypoxia-enhanced adhesion of hematopoietic stem and progenitor cells to the bone marrow stromal cells via a PLAUR-mediated pathway. This function is mediated by the N-terminal ectodomain. Metabolic regulator, which functions to maintain the adequate balance between lipid storage and oxidation in response to changing environmental conditions, such as temperature and diet. The N-terminal ectodomain negatively regulates adipose tissue energy expenditure, acting through the inhibition the BMP/Smad pathway. May regulate signaling by the heterodimeric neurotrophic cytokine CLCF1-CRLF1 bound to the CNTFR receptor by promoting the endocytosis of the tripartite complex CLCF1-CRLF1-CNTFR and lysosomal degradation. May regulate IL6 signaling, decreasing cis signaling, possibly by interfering with IL6-binding to membrane-bound IL6R, while up-regulating trans signaling via soluble IL6R.
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O88310
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ITL1A_MOUSE
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Intelectin-1a (Galactofuranose-binding lectin) (Intestinal lactoferrin receptor)
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MTQLGFLLFIMVATRGCSAAEENLDTNRWGNSFFSSLPRSCKEIKQEHTKAQDGLYFLRTKNGVIYQTFCDMTTAGGGWTLVASVHENNMRGKCTVGDRWSSQQGNRADYPEGDGNWANYNTFGSAEAATSDDYKNPGYFDIQAENLGIWHVPNKSPLHNWRKSSLLRYRTFTGFLQHLGHNLFGLYKKYPVKYGEGKCWTDNGPALPVVYDFGDARKTASYYSPSGQREFTAGYVQFRVFNNERAASALCAGVRVTGCNTEHHCIGGGGFFPEGNPVQCGDFASFDWDGYGTHNGYSSSRKITEAAVLLFYR
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Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner. Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO). Binds to glycans from Gram-positive and Gram-negative bacteria, including K.pneumoniae, S.pneumoniae, Y.pestis, P.mirabilis and P.vulgaris. Does not bind mammalian glycans. Probably plays a role in the defense system against microorganisms. May function as adipokine that has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. Increases AKT phosphorylation in the absence and presence of insulin. May interact with lactoferrin/LTF and increase its uptake, and may thereby play a role in iron absorption (By similarity).
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O88312
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AGR2_MOUSE
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Anterior gradient protein 2 homolog (AG-2) (mAG-2) (Protein Gob-4) (Secreted cement gland protein XAG-2 homolog)
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MEKFSVSAILLLVAISGTLAKDTTVKSGAKKDPKDSRPKLPQTLSRGWGDQLIWTQTYEEALYRSKTSNRPLMVIHHLDECPHSQALKKVFAEHKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIVFVDPSLTVRADITGRYSNRLYAYEPSDTALLYDNMKKALKLLKTEL
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Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells. Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth (By similarity). Promotes cell adhesion (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O95994, ECO:0000269|PubMed:19359471}.
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O88319
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NTR1_MOUSE
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Neurotensin receptor type 1 (NT-R-1) (NTR1)
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MHLNSSVQQGAPSEPGAQPFPHPQFGLETMLLALSLSNGSGNSSESILEPNSNLDVNTDIYSKVLVTAVYLALFVVGTVGNSVTAFTLARKKSLQSLQSTVHYHLGSLALSDLLILLLAMPVELYNFIWVHHPWAFGDAGCRGYYFLRDACTYATALNVASLSVERYLAICHPFKAKTLMSRSRTKKFISAIWLASALLAVPMLFTMGLQNRSADGQHPGGLVCTPTVDTATVKVVIQVNTFMSFLFPMLIISILNTVIANKLTVMVHQAAEQGRGVCTVGTHNSLEHSTFNMSIEPGRVQALRHGVLVLRAVVIAFVVCWLPYHVRRLMFCYISDEQWTTFLFDFYHYFYMLTNALFYVSSAINPILYNLVSANFRQVFLSTLACLCPGWRRRRKKRPTFSRKPNSMSSNHAFSTSATRETLY
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G-protein coupled receptor for the tridecapeptide neurotensin (NTS). Signaling is effected via G proteins that activate a phosphatidylinositol-calcium second messenger system. Signaling leads to the activation of downstream MAP kinases and protects cells against apoptosis.
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O88322
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NID2_MOUSE
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Nidogen-2 (NID-2) (Entactin-2)
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MFRDPTAGWLTPPSPLSLLVMLLLLSRVGALRPDELFPYGESWGDQLLPEGDDESSAAVKLAIPLRFYDAQFSSLYVGTNGIISTQDFPRETQYVDDDFPTDFPAIAPFLADIDTSHSRGRILYREDTSGAVLSLAARYVRTGFPLSGSSFTPTHAFLATWEHVGAYEEVSRGAAPSGELNTFQAVLASDESDTYALFLYPANGLQFFGTRPKESYNVQLQLPARVGFCRGEADDLKREALYFSLTNTEQSVKNLYQLSNLGIPGVWAFHIGSRFALDNVRPATVGGDPSTARSSALEHPFSHAAALESYTEDSFHYYDENEEDVEYPPVEPGEAPEGHSRIDVSFNSKADPGLVDVGTSSPGSDRASPWPYPAPGNWPSYRETESASLDPQTKQGRPVGEGEVLDFRDPAELLDQMGTRAPAPPEADAALLTPVNEDLGGRNTQSYPEAGPVPSEPDVPVPPLEGEVLPHYPESGHVPPLRGGKYVIGLEDHVGSNDQVFTYNGANLETCEHSHGRCSQHAFCTDYTTGFCCHCQSRFYGNGKHCLPEGAPHRVNGKVSGRLRVGHIPVHFTDVDLHAYIVGNDGRAYTAISHVPQPAAQALLPVLPIGGLFGWLFALEKPGSENGFSLTGATFVHDVEVTFHPGEERVRITQTAEGLDPENYLSIKTNIEGQVPFIPANFTAHITPYKEFYHYRDSVVTSSSSRSFSLTSGSINQTWSYHIDQNITYQACRHAPRHLAIPATQQLTVDRAFALYSEDEGVLRFAVTNQIGPVEVDSAPVGVNPCYDGSHTCDTTARCHPGTGVDYTCECTPGFQGDGRSCVDVNECATGFHRCGPNSVCVNLVGSYRCECRSGYEFADDQHTCILIAPPPNPCLDGSHTCAPEGQARCIHHGGSSFSCACLPGFIGTGHQCSDVDECAENRCHEAAICYNTPGSFSCRCQPGYRGDGFHCTSDTVPEDSISGLKPCEYQQRYAQTQHAYPGSRIHIPQCDDQGNFVPLQCHGSTGFCWCVDRNGHEVPGTQTPPGSTPPHCGPPPEPTQRPRTVCERWRESLLEHYGGTPRDDQYVPQCDDLGHFIPLQCHGKSDFCWCVDKDGRELQGTRSQPGTRPACIPTVAPPVVRPTPRPDVTPPSVGTFLLYAQGQQIGHLPLNGSRLQKDAARTLLSLHGSIVVGIDYDCRERMVYWTDVAGRTISRASLEAGAEPETIITSGLISPEGLAIDHFRRTMYWTDSGLDKIERAELDGSERKVLFHTDLVNPRAITVDPIRGNLYWTDWNREAPKIETSSLDGENRRILINKDIGLPNGLTFDPFSKLLCWADAGTKKLECTLPDGTGRRVIQNHLNYPFSIVSYADHFYHTDWRRDGVISVNKDSGQFTDEFLPEQRSHLYGITAVYPYCPTGRK
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Cell adhesion glycoprotein. Might be involved in osteoblast differentiation. It probably has a role in cell-extracellular matrix interactions.
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O88329
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MYO1A_MOUSE
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Unconventional myosin-Ia (Brush border myosin I) (BBM-I) (BBMI) (Myosin I heavy chain) (MIHC)
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MPLLEGPVGVEDLILLEPLDEESLIKNLQLRYENKEIYTYIGNVVISMNPYEQLPIYGPEFIAKYRDYTFYELKPHIYALANVAYQSLKDRDRDQCILITGESGAGKTEASKLVMSYVAAVCGKGEQVNSVKEQLLQSNPVLEAFGNAKTIRNNNSSRFGKYMDIEFDFKGSPLGGVITNYLLEKSRVVKQLKGERNFHIFYQLLAGADAQLLKALKLEEDTSVYGYLNGEVSKVNGMDDASNFRAVQHAMSVIGFSEEEIRQVLEVTALVLKLGNVKLTDEFQANGIPASGICDGKGIQEIGEMMGLNSTELERALCSRTMETGKEKVVTVLNVTQAQYARDALAKNIYSRLFDWIVKRINESIKVGTGEKKKVMGVLDIYGFEILEDNSFEQFVINYCNERLQQVFIELTLKEEQEEYKREGIPWTKVEYFDNGIICNLIEHSQRGILAMLDEECLRPGVVSDSTFLAKLNQLFSKHSHYESKVSQNAQRQYDRTMGLSCFRISHYAGKVTYNVTGFIDKNNDLLFRDLSQTMWKAQHPLLKSLFPEGNPKEASLKRPPTAGTQFKNSVAVLMKNLYSKNPNYIRCIKPNDQQQKGRFTSEMVMVQARYLGLLENVRVRRAGYAFRQGYKPFLERYRLLSRSTWPRWNGDDREGVEKVLGSLTLSSEELAYGKTKIFIRSPKTLFYLEEQRRLRLQQLATLIQKVYRGWRCRTHYQQMRKSQILISAWFRGNKQKKHYGKIRSSVLLIQAFVRGWRARKNYRKYFRSGAALTLANFIYQSMAQKFLLNLKKNLPSTKVLDNTWPAAPYRCFNTANQELQRLFYQWKCKKFRDQLSPKQVQTLREKLCASELFKGKKASYPQSVPIPFRGDYIGLQGNPKLQRLKGREEGPVLVADTVKKVNRGNGKTSARILLLTKGHVILTDAKKSQAQIVIGLEDVAGVSVSSLQDGLFSLHLSEMSSAVSKGDILLVSDHVVELLTKMYQAVLDATQRQLSVTVTEKFSVRFKEGSVAVKVIQGPEGGGNRKLICKKKGSNAMEVTVR
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Involved in directing the movement of organelles along actin filaments.
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O88335
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KCNJ1_MOUSE
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ATP-sensitive inward rectifier potassium channel 1 (ATP-regulated potassium channel ROM-K) (Inward rectifier K(+) channel Kir1.1) (Potassium channel, inwardly rectifying subfamily J member 1)
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MFKHLRRWFVTHIFGRSRQRARLVSKDGRCNIEFGNVDAQSRFIFFVDIWTTVLDLKWRYKMTVFITAFLGSWFLFGLLWYVVAYVHKDLPEFYPPDNRTPCVENINGMTSAFLFSLETQVTIGYGFRFVTEQCATAIFLLIFQSILGVIINSFMCGAILAKISRPKKRAKTITFSKNAVISKRGGKLCLLIRVANLRKSLLIGSHIYGKLLKTTITPEGETIILDQTNINFVVDAGNENLFFISPLTIYHIIDHNSPFFHMAAETLSQQDFELVVFLDGTVESTSATCQVRTSYIPEEVLWGYRFVPIVSKTKEGKYRVDFHNFGKTVEVETPHCAMCLYNEKDARARMKRGYDNPNFVLSEVDETDDTQM
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In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium (By similarity).
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O88339
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EPN1_RAT
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Epsin-1 (EPS-15-interacting protein 1)
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MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL
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Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis (By similarity).
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O88342
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WDR1_MOUSE
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WD repeat-containing protein 1 (Actin-interacting protein 1) (AIP1)
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MPYEIKKVFASLPQVERGVSKILGGDPKGDHFLYTNGKCVILRNIDNPAIADIYTEHAHQVVVAKYAPSGFYIASGDISGKLRIWDTTQKEHLLKYEYQPFAGKIKDIAWTEDSKRIAVVGEGREKFGAVFLWDTGSSVGEITGHNKVINSVDIKQTRPYRLATGSDDNCAAFFEGPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIFIYDGKTGEKVCALGESKAHDGGIYAISWSPDSTHLLSASGDKTSKIWDVNVNSVVSTFPMGSNVLDQQLGCLWQKDHLLSISLSGYINYLDKNNPSKPLRVIKGHSKSIQCLTVHRNGGKSYIYSGSHDGHINYWDSETGENDSFSGKGHTNQVSRMTVNESEQLVSCSMDDTVRYTNLTLRDYSGQGVVKLDVQPKCVAVGPGGYTVVVCIGQIVLLKDQKKCFSIDNPGYEPEVVAVHPGGDTVAVGGTDGNVRVYSILASTLKDEGKLLEAKGPVTDVAYSHDGAFLAVCDASKVVTVFSVADGYSENNVFYGHHAKIVCLAWSPDNEHFASGGMDMMVYVWTLSDPETKVKIQDAHRLHHVSSLAWLDEHTLVTTSHDASVKEWTITY
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Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins (By similarity). Enhances cofilin-mediated actin severing. Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions (By similarity). Involved in myocardium sarcomere organization. Required for cardiomyocyte growth at the postnatal and maintenance at the adult stage. Involved in neutrophil actin dynamics and migration. Involved in megakaryocyte maturation and platelet shedding. Required for the establishment of planar cell polarity (PCP) during follicular epithelium development and for cell shape changes during PCP the function seems to implicate cooperation with CFL1 and/or DSTN/ADF. Involved in the generation/maintenance of cortical tension. Involved in assembly and maintenance of epithelial apical cell junctions and plays a role in the organization of the perijunctional actomyosin belt (By similarity).
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O88343
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S4A4_MOUSE
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Electrogenic sodium bicarbonate cotransporter 1 (Sodium bicarbonate cotransporter) (Na(+)/HCO3(-) cotransporter) (Solute carrier family 4 member 4)
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MEDEAVLDRGASFLKHVCDEEEVEGHHTIYIGVHVPKSYRRRRRHKRKAGHKEKKEKERISENYSDKSDVENADESSSSILKPLISPAAERIRFILGEEDDSPAPPQLFTELDELLAVDGQEMEWKETARWIKFEEKVEQGGERWSKPHVATLSLHSLFELRTCMEKGSIMLDREASSLPQLVEMIADHQIETGLLKPDLKDKVTYTLLRKHRHQTKKSNLRSLADIGKTVSSASRMFSNPDNGSPAMTHRNLTSSSLNDISDKPEKDQLKNKFMKKLPRDAEASNVLVGEVDFLDTPFIAFVRLQQAVMLGALTEVPVPTRFLFILLGPKGKAKSYHEIGRAIATLMSDEVFHDIAYKAKDRHDLIAGIDEFLDEVIVLPPGEWDPTIRIEPPKSLPSSDKRKNMYSGGENVQMNGDTPHDGGHGGGGHGDCEELQRTGRFCGGLIKDIKRKAPFFASDFYDALNIQALSAILFIYLATVTNAITFGGLLGDATDNMQGVLESFLGTAVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDHNFDYLEFRLWIGLWSAFMCLVLVATDASFLVQYFTRFTEEGFSSLISFIFIYDAFKKMIKLADYYPINSDFKVGYNTHFSCACLPPDPVNLSVSNDTTLAPEDLPTISSTDMYHNVTFDWAYLSKKECVKYGGKLVGNNCDFVPDITLMSFILFLGTYTSSMAMKKFKTSRYFPTTARKLISDFAIILSILIFCVIDALVGVDTPKLIVPSEFKPTSPNRGWFVPPFGGNPWWVCLAAAIPALLVTILIFMDQQITAVIVNRKEHKLKKGAGYHLDLFWVAILMVVCSFMALPWYVAATVISIAHIDSLKMETETSAPGEQPKFLGVREQRVTGTLVFILTGLSVFMAPILKFIPMPVLYGVFLYMGVASLNGVQFMDRLKLLLMPLKHQPDFIYLRHVPLRRVHLFTFLQVLCLALLWILKSTVAAIIFPVMILALVAVRKGMDYLFSQHDLSFLDDVIPEKDKKKKEDEKKKKKKKGSLDSDNDDSDCPYSEKVPSIKIPMDIMEQQPFLSDNKPLDRERSSTFLERHTSC
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Electrogenic sodium/bicarbonate cotransporter with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH.
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O88351
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IKKB_MOUSE
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Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB) (Serine/threonine protein kinase IKBKB) (EC 2.7.11.1)
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MSWSPSLPTQTCGAWEMKERLGTGGFGNVIRWHNQATGEQIAIKQCRQELSPKNRNRWCLEIQIMRRLNHPNVVAARDVPEGMQNLAPNDLPLLAMEYCQGGDLRRYLNQFENCCGLREGAVLTLLSDIASALRYLHENRIIHRDLKPENIVLQQGEKRLIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHSKVRQKSEVDIVVSEDLNGAVKFSSSLPFPNNLNSVLAERLEKWLQLMLMWHPRQRGTDPQYGPNGCFRALDDILNLKLVHVLNMVTGTVHTYPVTEDESLQSLKTRIQENTGILETDQELLQKAGLVLLPDKPATQCISDSKTNEGLTLDMDLVFLLDNSKINYETQITPRPPPESVSCILQEPKRNLSFFQLRKVWGQVWHSIQTLKEDCNRLQQGQRAAMMSLLRNNSCLSKMKNAMASTAQQLKAKLDFFKTSIQIDLEKYKEQTEFGITSDKLLLAWREMEQAVEQCGRENDVKHLVERMMALQTDIVDLQRSPMGRKQGGTLDDLEEQARELYRKLREKPRDQRTEGDSQEMVRLLLQAIQSFEKKVRVIYTQLSKTVVCKQKALELLPKVEEVVSLMNEDERTVVRLQEKRQKELWNLLKIACSKVRGPVSGSPDSMNVSRLSHPGQLMSQPSSACDSLPESDKKSEELVAEAHALCSRLESALQDTVKEQDRSFTTLDWSWLQMEDEERCSLEQACD
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Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (By similarity). Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation (By similarity). Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues (By similarity). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (By similarity). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (By similarity). In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (By similarity). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs (By similarity). Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (By similarity). Also phosphorylates other substrates including NAA10, NCOA3, BCL10 and IRS1 (By similarity). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death. Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus.
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O88354
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LIPP_ICTTR
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Pancreatic triacylglycerol lipase (PL) (PTL) (Pancreatic lipase) (EC 3.1.1.3) (Heart pancreatic lipase) (PL-h)
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MLLVWSLALLLGAVAGKEVCYDRLGCFSDDSPWSGIVERPLKVLPWSPADVNTRFLLYTNENQDNYQQITADSSRIQSSNFKTNRKTRFIIHGFIDKGEESWLANMCKKMFQVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVDFLRTQLGYSPSNVHVIGHSLGSHAAGEAGRRTNGAIGRITGLDPAEPCFEGTPELVRLDPSDAQFVDAIHTDGAPIVPNLGFGMSQTVGHLDFFPNGGIEMPGCQKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPTGFAAFSCASYSVFSANKCFPCPSGGCPQMGHYADRYSGKTNGVGQKFYLNTGDKSNFSRWRYKVSVTLSGQKVTGHILVSLFGNAGNSKQYEIYKGSLHPGYTHSNEFDSDVDVGDLQRVKFIWYNNVINPSLPRVGASSISVERNDGRVFKFCSAETVREDVLLTLNAC
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Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones (By similarity). Plays a role in hibernation as a key enzyme that shows high activity at low temperatures. When expressed in the hibernating heart it liberates fatty acids from triglycerides at temperatures as low as 0 degrees Celsius.
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O88368
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MITF_RAT
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Microphthalmia-associated transcription factor
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MQSESGIVADFEVGEEFHEEPKTYYELKSQPLKSSSSAEHSGASKPPLSSSTMTSRILLRQQLMREQMQEQERREQQQKLQAAQFMQQRVAVSQTPAINVSVPTTLPSATQVPMEVLKVQTHLENPTKYHIQQAQRHQVKQYLSTTLANKHAGQVLSPPCPNQPGDHAMPPVPGSSAPNSPMAMLTLNSNCEKEAFYKFEEQSRAESECPGMNTHSRASCMQMDDVIDDIISLESSYNEEILGLMDPALQMANTLPVSGNLIDLYSNQGLPPPGLTISNSCPANLPNIKRELTACIFPTESEARALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQREQQRAKDLENRQKKLEHANRHLLLRVQELEMQARAHGLSLIPSTGLCSPDLVNRIIKQEPVLENCSQELVQHQADLTCTTTLDLTDGTISFTNNLGTMPESSPAYSIPRKMASNLEDILMDDALSPVGVTDPLLSSVSPGASKTSSRRSSMSAEETEHAC
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Transcription factor that regulates the expression of genes with essential roles in cell differentiation, proliferation and survival. Binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoters of target genes, such as BCL2 and tyrosinase (TYR). Plays an important role in melanocyte development by regulating the expression of tyrosinase (TYR) and tyrosinase-related protein 1 (TYRP1). Plays a critical role in the differentiation of various cell types, such as neural crest-derived melanocytes, mast cells, osteoclasts and optic cup-derived retinal pigment epithelium.
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O88370
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PI42C_RAT
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Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma (EC 2.7.1.149) (Phosphatidylinositol 5-phosphate 4-kinase type II gamma) (PI(5)P 4-kinase type II gamma) (PIP4KII-gamma)
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MASSSVPPATAPAAAGGPGPGFGFASKTKKKHFVQQKVKVFRAADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPPSETEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVENEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEGPVREEESEWDGDCNLTGPPALVGSYGTSPEGIGGYIHSHRPLGPGEFESFIDVYAIRSAEGAPEGGVFHGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFISNIFA
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Phosphatidylinositol 5-phosphate 4-kinase with low enzymatic activity. May be a GTP sensor, has higher GTP-dependent kinase activity than ATP-dependent kinase activity (By similarity). PIP4Ks negatively regulate insulin signaling through a catalytic-independent mechanism. They interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (By similarity).
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O88377
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PI42B_RAT
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Phosphatidylinositol 5-phosphate 4-kinase type-2 beta (EC 2.7.1.149) (1-phosphatidylinositol 5-phosphate 4-kinase 2-beta) (Diphosphoinositide kinase 2-beta) (Phosphatidylinositol 5-phosphate 4-kinase type II beta) (PI(5)P 4-kinase type II beta) (PIP4KII-beta) (Phosphatidylinositol-phosphate kinase IIgamma) (PIPKIIgamma) (PtdIns(5)P-4-kinase isoform 2-beta)
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MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLRVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEETEVEDRAEEEECENDGVGGGLLCSYGTPPDSPGNLLSFPRFFGPGEFDPSVDVYAMKSHESAPKKEVYFMAIIDILTPYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSNILT
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Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Preferentially utilizes GTP, rather than ATP, for PI(5)P phosphorylation and its activity reflects changes in direct proportion to the physiological GTP concentration. Its GTP-sensing activity is critical for metabolic adaptation (By similarity). PIP4Ks negatively regulate insulin signaling through a catalytic-independent mechanism. They interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (By similarity).
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O88379
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BAZ1A_MOUSE
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Bromodomain adjacent to zinc finger domain protein 1A (Cbp146)
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MPLLHRKPFVRQKPPGDLRPDEEVFYCKVTNEIFRHYDDFFERTILCNSLVWSCAVTGRPGLTYQEALESERKARQNLQSFPEPLIIPVLYLTNLTRRSRLHEICDDIFAYVKDRYFVEETVEVIRNNGTRLQCRILEVLPPLHQNGFANGHLSSADGETIVISDSDDSETQSSSFHHGKKKDAIDPLLFRYRVQPTKKEMYESAVVKATQISRRKHLFSRDKLKLFLKQHCEAQDGVIKIKASSFSAYNIAEQDFSYFFPDDPPTFIFSPANRRRGRPPKRISFGQEDSIASKQTAARYRNKAIKERDKLLKQEEMRALAFEKAKLKRERADALEARKREKEDKEKKREELKKMVEEERLKKKEEKERLKIEREKEREKLREEKRKYMEYLKQWSKPREDMECDDLKELPEPTPVKTRLPPEVFGDALMVLEFLNAFGELFDLQDEFPEGVTLAEVLEEALVGNDSEGPLCELLFFFLTAIFQAMAEEEEEVAKEQITDADTKDLTEALDEDADPTKSALSAVAALAAAWPQLHQGCSLKSLDLDSCTLSEILRLHILASGADVTSANAKYRYQKRGGFDATDDACMELRLSNPSLVKKLSSTSVYDLTPGEKMKILHALCGKLLTLVSTRDFIEDYVDVLRQAKQEFRELKAEQHRKEREATAARIRRRKEEKLKEQEQKMKEKQEKLKEDEQRNSAAVPGYGEEEREDFDTSTENKNIEQKDLDPDVVTEDEDDPGSHKRSRRGKVGQTAVKQCIKQEEMNYCIKQEPLSADAEEALRQEQQQKEKELLDKIQSAIACTNIFPLGRDRLYRRYWIFPSIPGLFIEEDYSGLTEDMLLPRPSSFHNNAQPRDPQVSIKTEESFLSESTSSLDQGPFDDSVLLPKPVHKPNRWCFYSSCAQLDQLIDALNSRGHRESALKETLLQEKSRICAQLAHFSEEKFHFSDKPQADSKPVSSRGRSSGACDISQMSAERQLELRLRDFLLDIEDRIYQGTLGAIKVTDRQVWRSALENGRYELLSEESKENGVIKTVNEDVEEMEMEQARVIVRDRLLGIKTETPSTISTSASTPQSVSNVVHYLALALFQIEQGIERRFLKAPLDGNDSGRSYKTVLDRWRESLLSSASLSQVFLHLSTLDRSVMWSKSILNARCKICRKKGDAENMVLCDGCDRGHHTYCVRPKLKAVPDGDWFCPECRPKQRSRRLSSRQRPSLESDEEMEEGMEDDDDEVDDDDEEGQSEEEEYEVEQDEEDSDDDEALSPPKRGRPQVRLPIKTKGRFGPSFPSRSQRQDPGRYPSRSQQSTPKNTAKSASKNLRKTRSAPPTETRSLRVGSRSTRHSPSALQDVFVELLSPHSKRRGRKGADHTPEHSPSFTNFRVSTSRSSRQLIPLNTAESLSLQHSESKRRGRKRQSTESSPVPLNRRSSGRQGGVHELSAFEQLVVELVRHDDSWPFLKLVSKIQVPDYYDIIKKPIALNIIREKVNKCEYKLASEFIDDIELMFSNCFEYNPRNTSEAKAGTRLQAFFHIQAQKLGLHVSPSTVDQVSTPLAAKKSRI
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Regulatory subunit of the ATP-dependent ACF-1 and ACF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and slide edge- and center-positioned histone octamers away from their original location on the DNA template to facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (By similarity). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template in an ATP-dependent manner (By similarity). The ACF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the ACF-5 ISWI chromatin remodeling complex (By similarity). Has a role in sensing the length of DNA which flank nucleosomes, which modulates the nucleosome spacing activity of the ACF-5 ISWI chromatin remodeling complex (By similarity). Involved in DNA replication and together with SMARCA5/SNF2H is required for replication of pericentric heterochromatin in S-phase (By similarity). May have a role in nuclear receptor-mediated transcription repression (By similarity).
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O88382
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MAGI2_RAT
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Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Atrophin-1-interacting protein 1) (AIP-1) (Membrane-associated guanylate kinase inverted 2) (MAGI-2) (Synaptic-scaffolding molecule) (S-SCAM)
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MSKSLKKKSHWTSKVHESVIGRNPEGQLGFELKGGAENGQFPYLGEVKPGKVAYESGSKLVSEELLLEVNETPVAGLTIRDVLAVIKHCKDPLRLKCVKQGGIVDKDLRHYLNLRFQKGSVDHELQQIIRDNLYLRTVPCTTRPHKEGEVPGVDYIFITVEDFMELEKSGALLESGTYEDNYYGTPKPPAEPAPLLLNVTDQILPGATPSAEGKRKRNKSVTNMEKASIEPPEEEEEERPVVNGNGVVITPESSEHEDKSAGASGETPSQPYPAPVYSQPEELKDQMDDTKSTKPEENEDSDPLPDNWEMAYTEKGEVYFIDHNTKTTSWLDPRLAKKAKPAEECKENELPYGWEKIDDPIYGTYYVDHINRRTQFENPVLEAKRKLQQHNMPHTELGTKPLQAPGFREKPLFTRDASQLKGTFLSTTLKKSNMGFGFTIIGGDEPDEFLQVKSVIPDGPAAQDGKMETGDVIVYINEVCVLGHTHADVVKLFQSVPIGQSVNLVLCRGYPLPFDPEDPANSMVPPLAIMERPPPVMVNGRHNYETYLEYISRTSQSVPDITDRPPHSLHSMPADGQLDGTYPPPVHDDNVSVASSGATQAELMTLTIVKGAKGFGFTIADSPTGQRVKQILDIQGCPGLCEGDLIVEINQQNVQNLSHTEVVDILKDCPVGSETSLIIHRGGFFSPWKTPKPMVDRWENQGSPQTSLSAPAVPQSLPFPPALHRSSFPDSTEAFDPRKPDPYELYEKSRAIYESRQQVPPRTSFRMDSSGPDYKELDVHLRRMESGFGFRILGGDEPGQPILIGAVIAMGSADRDGRLHPGDELVYVDGIPVAGKTHRYVIDLMHHAARNGQVNLTVRRKVLCGGEPCPENGRSPGSVSTHHSSPRSDYATYANSNHAAPSNNASPPEGFASHSLQTSDVIIHRKENEGFGFVIISSLNRPESGATITVPHKIGRIIDGSPADRCAKLKVGDRILAVNGQSIINMPHADIVKLIKDAGLSVTLRIIPQEELNNPTSAPSSEKQSPMAQQHSPLAQQHSPLAQPSPATPNSPVAQPAPPQPLQLQGHENSYRSEVKARQDVKPDIRQPPFTDYRQPPLDYRQPPGGDYSQPSPLDYRQHSPDTRQYPLSDYRQPQDFDYFTVDMEKGAKGFGFSIRGGREYKMDLYVLRLAEDGPAIRNGRMRVGDQIIEINGESTRDMTHARAIELIKSGGRRVRLLLKRGTGQVPEYGMVPSSLSMCMKSDKHGSPYFYLLGHPKDTTNPTPGALPLPPPQACRK
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Seems to act as scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in regulating activin-mediated signaling in neuronal cells (By similarity). Enhances the ability of PTEN to suppress AKT1 activation (By similarity). Plays a role in receptor-mediated clathrin-dependent endocytosis which is required for ciliogenesis (By similarity).
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O88384
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VTI1B_MOUSE
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Vesicle transport through interaction with t-SNAREs homolog 1B (Vesicle transport v-SNARE protein Vti1-like 1) (Vti1-rp1)
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MAASAASSEHFEKLHEIFRGLLEDLQGVPERLLGTAGTEEKKKLVRDFDENQQEANETLAEMEEELRYAPLTFRNPMMSKLRNYRKDLAKLHREVRSTPLTAAPGGRGDLKYGTYTLENEHLNRLQSQRALLLQGTESLNRATQSIERSHRIATETDQIGTEIIEELGEQRDQLERTKSRLVNTNENLSKSRKILRSMSRKVITNKLLLSVIILLELAILVGLVYYKFFRHH
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V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers.
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O88387
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FGD4_RAT
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FYVE, RhoGEF and PH domain-containing protein 4 (Actin filament-binding protein frabin) (FGD1-related F-actin-binding protein)
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MEESNPAPTSCASKGKHSKVSDLISHFEGGSVLSSYTDVQKDSTMNLNIPQTPRQHGLTSTTPQKLPSHKSPQKQEKDSDQNQGQHGCLANGVAAAQSQMECETEKEAALSPETDTQTAAASPDAHVLNGVRNETTTDSASSVTNSHDENACDSSCRTQGTDLGLPSKEGEPVIEAELQERENGLSTEGLNPLDQHHEVKETNEQKLHKIATELLLTERAYVSRLNLLDQVFYCKLLEEANRGSFPAEMVNKIFSNISSINAFHSKFLLPELEKRMQEWETTPRIGDILQKLAPFLKMYGEYVKGFDNAVELVKNMTERVPQFKSVTEEIQKQKICGSLTLQHHMLEPIQRIPRYEMLLKDYLKKLSPDAPDWNDAKKSLEIISTAASHSNSAIRKMENLKKLLEIYEMLGEEEDIVNPSNELIKEGQILKLAARNTSAQERYLFLFNNMLLYCVPRFSLVGSKFTVRTRVGIDGMKIVETHNEEYPHTFQVSGKERTLELQASSEQDKEEWIKALQESIDAFHQRHETFRNAIAKENDIPLEVSTAELGKRAPRWIRDNEVTMCMKCKESFNALTRRRHHCRACGHVVCWKCSDYKAQLEYDGGRLNKVCKDCYQIMSGFAESEEKKRRGILEIESAEVSGNSEVCSFLQYMEKSKPWQKIWCVIPKQDPLVLYMYGAPQDVRAQATIPLLGYIVDDMPKSADLPHSFKLTQSKSVHSFAADSEELKQKWLKIILLAVTGETPDGPSEHLDTLDNLPGPKEKSEC
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Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. Activates MAPK8.
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O88393
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TGBR3_MOUSE
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Transforming growth factor beta receptor type 3 (TGF-beta receptor type 3) (TGFR-3) (Betaglycan) (Transforming growth factor beta receptor III) (TGF-beta receptor type III)
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MAVTSHHMVPVFVLMSACLATAGPEPSTRCELSPISASHPVQALMESFTVLSGCASRGTTGLPREVHILNLRSTDQGLGQPQREVTLHLNPIASVHTHHKPVVFLLNSPQPLVWHVKTERLAAGVPRLFLVSEGSVVQFSSGNFSLTAETEERSFPQENEHLLHWAQKEYGAVTSFTELKIARNIYIKVGEDQVFPPTCNIGKNFLSLNYLAEYLQPKAAEGCVLASQPHEKEVHIIELISPNSNPYSTFQVDIIIDIRPAREDPEVVKNLVLILKCKKSVNWVIKSFDVKGNLKVIAPDSIGFGKESERSMTVTKLVRNDYPSTQENLMKWALDNGYSPVTSYTIAPVANRFHLRLENNEEMRDEEVHTIPPELRILLGPDHLPALDSPPFQGEIPNGGFPFPFPDIPRRGWKEGEDRIPRPKEPIIPRVQLLPDHREPEEVQGGVNIALSVKCDNEKMVVAVDKDSFQTNGYSGMELTLLDPSCKAKMNGTHFVLESPLNGCGTRHRRSAPDGVVYYNSIVVQAPSPGDSSGWPDGYEDLESGDNGFPGDTDEGETAPLSRAGVVVFNCSLRQLRSPSGFQDQLDGNATFNMELYNTDLFLVPSPGVFSVAENEHVYVEVSVTKADQDLGFAIQTCFISPYSNPDRMSDYTIIENICPKDDSVKFYSSKRVHFPIPHAEVDKKRFSFVFKSVFNTSLLFLHCELTLCSRNKGSQKLPKCVTPDDACTSLDATMIWTMMQNKKTFTKPLAVVLQVDYKENVPNMKESSPVPPPPQIFHGLDTLTVMGIAFAAFVIGALLTGALWYIYSHTGETARRQQVPTSPPASENSSAAHSIGSTQSTPCSSSSTA
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Binds to TGF-beta. Could be involved in capturing and retaining TGF-beta for presentation to the signaling receptors (By similarity). In gonadotrope cells, acts as an inhibin A coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility.
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O88397
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SO1A5_RAT
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Solute carrier organic anion transporter family member 1A5 (Organic anion-transporting polypeptide 3) (OATP-3) (Sodium-independent organic anion transporter 3) (Solute carrier family 21 member 7)
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MGETEKRVATHEVRCFSKIKMFLLALTWAYVSKSLSGIYMNTMLTQIERQFDIPTSIVGFINGSFEIGNLLLIIFVSYFGTKLHRPIMIGVGCVIMGLGCFLMSLPHFLMGRYEYETTISPTSNLSSNSFLCMENRSQTLKPTQDPAECIKEMKSLMWIYVLVGNIIRGIGETPIMPLGISYIEDFAKSENSPLYIGILETGKVFGPIVGLLLGSFCASIYVDTGSVNTDDLTITPTDTRWVGAWWIGFLICAGVNILSSIPFFFFPKTLPKEGLQDDVDGTNNDKEEKHREKAKEENRGITKDFLPFMKSLSCNPIYMLLILTSVLQINAFINMFTFLPKYLEQQYGKSTAEVVLLIGVYNLPPICIGYLLIGFIMKKFKITVKKAAYMAFCLSLFEYLLYFLHFMITCDNFPVAGLTASYEGVHHPLYVENKVLADCNRGCSCSTNSWDPVCGDNGLAYMSACLAGCKKSVGTGTNMVFQNCSCIRSSGNSSAVLGLCKKGPECANKLQYFLIMSVIGSFIYSITAIPGYMVLLRCIKPEEKSLGIGLHAFCTRVFAGIPAPIYFGALIDRTCLHWGTLKCGEPGACRMYNINNFRRIYLVLPAALRGSSYLPALFILILMRKFQFPGEIDSSETELAEMKITVKKSECTDVHGSPQVENDGELKTRL
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Na(+)-independent transporter that mediates the cellular uptake of a broad range of organic anions such as the endogenous bile salts cholate and deoxycholate, either in their unconjugated or conjugated forms (taurocholate and glycocholate), estrone 3-sulfate and prostaglandin E2, at the plasma membrane. Responsible for intestinal absorption of bile acids. Capable of thyroid hormone transport (both T3 or 3,3',5'-triiodo-L-thyronine, and T4 or L-tyroxine). Plays roles in blood-brain and -cerebrospinal fluid barrier transport of organic anions and signal mediators, and in hormone uptake by neural cells (By similarity). May also play a role in the reuptake of neuropeptides such as substance P/TAC1 and vasoactive intestinal peptide/VIP released from retinal neurons (By similarity). Shows a pH-sensitive substrate specificity which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment. Hydrogencarbonate/HCO3(-) acts as the probable counteranion that exchanges for organic anions. May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (By similarity).
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O88398
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AVIL_MOUSE
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Advillin (Actin-binding protein DOC6) (p92)
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MSLSSAFRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGSLLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQYHESDTFRGYFKQGIIYKKGGVASGMKHVETNTYDVKRLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAASPGLMTVLQDTLGRRSMIKPAVSDEIMDQQQKSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTNVETVNDGAESAMFKQLFQKWSVKDQTTGLGKIFSTGKIAKIFQDKFDVSLLHTKPEVAAQERMVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVRVSMGKEPRHFMAIFKGKLVIYEGGTSRKGNEEPDPPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDGNADTVAEGQEPPEFWDLLGGKTAYANDKRLQQETLDVQVRLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRDPDTPILIIKQGFEPPTFTGWFLAWDPHIWSEGKSYEQLKNELGDATAIVRITADMKNATLYLNPSDGEPKYYPVEVLLKGQNQELPEDVDPAKKENYLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF
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Ca(2+)-regulated actin-binding protein which plays an important role in actin bundling. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis. In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (By similarity).
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O88406
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SMAD7_RAT
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Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (SMAD family member 7) (SMAD 7) (Smad7)
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MFRTKRSALVRRLWRSRAPGGEDEEEGVGGGGGGGGLRGEGATDGRAYGAGGGGAGRAGCCLGKAVRGAKGHHHPHPPSSGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPASAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSDETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR
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Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
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O88407
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LFG2_RAT
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Protein lifeguard 2 (Fas apoptotic inhibitory molecule 2) (Neural membrane protein 35)
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MTQGKLSVANKAPGTEGQQQANGEKKDAPAVPSAPPSYEEATSGEGLKAGAFPQGPTAVPLHPSWAYVDPSSSSGYEGGFPAGHHELFSTFSWDDQKVRQLFIRKVYTILLVQLLVTLAVVALFTFCDVVKDYVQANPGWYWASYAVFFATYLTLACCSGPRRHFPWNLILLTIFTLSMAYLTGMLSSYYNTTSVLLCLGITALVCLSVTIFSFQTKFDFTSCHGVLFVLLMTLFFSGLLLAILLPFQYVPWLHAVYAVLGAGVFTLFLAFDTQLLMGNRRHSLSPEEYIFGALNIYLDIIYIFTFFLQLFGTNRE
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Antiapoptotic protein which protects cells uniquely from Fas-induced apoptosis. Regulates Fas-mediated apoptosis in neurons by interfering with caspase-8 activation. Plays a role in cerebellar development by affecting cerebellar size, internal granular layer (IGL) thickness, and Purkinje cell (PC) development (By similarity).
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O88410
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CXCR3_MOUSE
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C-X-C chemokine receptor type 3 (CXC-R3) (CXCR-3) (Interferon-inducible protein 10 receptor) (IP-10 receptor) (CD antigen CD183)
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MYLEVSERQVLDASDFAFLLENSTSPYDYGENESDFSDSPPCPQDFSLNFDRTFLPALYSLLFLLGLLGNGAVAAVLLSQRTALSSTDTFLLHLAVADVLLVLTLPLWAVDAAVQWVFGPGLCKVAGALFNINFYAGAFLLACISFDRYLSIVHATQIYRRDPRVRVALTCIVVWGLCLLFALPDFIYLSANYDQRLNATHCQYNFPQVGRTALRVLQLVAGFLLPLLVMAYCYAHILAVLLVSRGQRRFRAMRLVVVVVAAFAVCWTPYHLVVLVDILMDVGVLARNCGRESHVDVAKSVTSGMGYMHCCLNPLLYAFVGVKFREQMWMLFTRLGRSDQRGPQRQPSSSRRESSWSETTEASYLGL
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Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and mediates the proliferation, survival and angiogenic activity of mesangial cells through a heterotrimeric G-protein signaling pathway. Probably promotes cell chemotaxis response (By similarity). Binds to CCL21. {ECO:0000250, ECO:0000269|PubMed:9653165, ECO:0000269|PubMed:9790904}.
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O88413
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TULP3_MOUSE
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Tubby-related protein 3 (Tubby-like protein 3)
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MEAARCAPGPRGDSAFDDETLRLRQLKLDNQRALLEKKQRKKRLEPLMVQPNPEARLRRLKPRGSEEHTPLVDPQMPRSDVILHGIDGPAAFLKPEAQDLESKPQVLSVGSPAPEEGTEGSADGESPEETAPKPDLQEILQKHGILSSVNYDEEPDKEEDEGGNLSSPSARSEESAAASQKAASETGASGVTAQQGDAQLGEVENLEDFAYSPAPRGVTVKCKVTRDKKGMDRGLFPTYYMHLEREENRKIFLLAGRKRKKSKTSNYLVSTDPTDLSREGESYIGKLRSNLMGTKFTVYDHGVNPVKAQGLVEKAHTRQELAAICYETNVLGFKGPRKMSVIIPGMNMNHERIPFRPRNEHESLLSKWQNKSMENLIELHNKAPVWNDDTQSYVLNFHGRVTQASVKNFQIVHGNDPDYIVMQFGRVADDVFTLDYNYPLCALQAFAIGLSSFDSKLACE
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Negative regulator of the Shh signaling transduction pathway: recruited to primary cilia via association with the IFT complex A (IFT-A) and is required for recruitment of G protein-coupled receptor GPR161 to cilia, a promoter of PKA-dependent basal repression machinery in Shh signaling. Binds to phosphorylated inositide (phosphoinositide) lipids. Both IFT-A- and phosphoinositide-binding properties are required to regulate ciliary G protein-coupled receptor trafficking. During adipogenesis, regulates ciliary trafficking of FFAR4 in preadipocytes.
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O88419
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B4GT6_RAT
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Beta-1,4-galactosyltransferase 6 (Beta-1,4-GalTase 6) (Beta4Gal-T6) (b4Gal-T6) (EC 2.4.1.-) (Glucosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.274) (Lactosylceramide synthase) (LacCer synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 6) (UDP-Gal:glucosylceramide beta-1,4-galactosyltransferase) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 6)
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MSALKRMMRVSNRSLIAFIFFFSLSTSCLYFIYVAPGIANTYLFMVQARGIMLRENVKTIGHMIRLYTNKNTTLNGTDYPEGNNTSDYLVQTTTYLPQNFTYSPHLPCPEKLPYMRGFLSVNVSEISFDEVHQLFSKDSEIEPGGHWRPQDCKPRWKVAVLIPFRNRHEHLPIFFLHLIPMLQKQRLEFAFYVIEQTGTQPFNRAMLFNVGFKEAMKDRAWDCVIFHDVDHLPENDRNYYGCGEMPRHFAAKLDKYMYILPYKEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVHYSGYNVTRPEGDLGKYTSIPHHHRGEVQFLGRYKLLRYSKERQFIDGLNNLLYTPKILVDRLYTNISVNLMPELAPVEDY
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Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity).
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O88420
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SCN8A_RAT
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Sodium channel protein type 8 subunit alpha (Peripheral nerve protein type 4) (PN4) (Sodium channel 6) (NaCh6) (Sodium channel protein type VIII subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.6)
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MAARLLAPPGPDSFKPFTPESLANIERRIAESKLKKPPKADGSHREDDEDSKPKPNSDLEAGKSLPFIYGDIPQGLVAVPLEDFDPYYLTQKTFVVLNRGKTLFRFSATPALYILSPFNLIRRIAIKILIHSVFSMIIMCTILTNCVFMTFSNPPEWSKNVEYTFTGIYTFESLVKIIARGFCIDGFTFLRDPWNWLDFSVIMMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVVWPINFNESYLENGTRGFDWEEYINNKTNFYMVPGMLEPLLCGNSSDAGQCPEGFQCMKAGRNPNYGYTSFDTFSWAFLALFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFVGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFKAMLEQLKKQQEEAQAAAMATSAGTVSEDAIEEEGEDGVGSPRSSSELSKLSSKSAKERRNRRKKRKQKELSEGEEKGDPEKVFKSESEDGMRRKAFRLPDNRIGRKFSIMNQSLLSIPGSPFLSRHNSKSSIFSFRGPGRFRDPGSENEFADDEHSTVEESEGRRDSLFIPIRARERRSSYSGYSGYSQCSRSSRIFPSLRRSVKRNSTVDCNGVVSLIGPGSHIGRLLPEATTEVEIKKKGPGSLLVSMDQLASYGRKDRINSIMSVVTNTLVEELEESQRKCPPCWYKFANTFLIWECHPYWIKLKEIVNLIVMDPFVDLAITICIVLNTLFMAMEHHPMTPQFEHVLAVGNLVFTGIFTAEMFLKLIAMDPYYYFQEGWNIFDGFIVSLSLMELSLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINQECKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDGEMNNLQISVIRIKKGVAWTKVKVHAFMQAHFKQREADEVKPLDELYEKKANCIANHTGVDIHRNGDFQKNGNGTTSGIGSSVEKYIIDEDHMSFINNPNLTVRVPIAVGESDFENLNTEDVSSESDPEGSKDKLDDTSSSEGSTIDIKPEVEEVPVEQPEEYLDPDACFTEGCVQRFKCCQVNIEEGLGKSWWILRKTCFLIVEHNWFETFIIFMILLSSGALAFEDIYIEQRKTIRTILEYADKVFTYIFILEMLLKWTAYGFVKFFTNAWCWLDFLIVAVSLVSLIANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKYHYCFNETSEIRFEIDIVNNKTDCEKLMEGNSTEIRWKNVKINFDNVGAGYLALLQVATFKGWMDIMYAAVDSRKPDEQPDYEGNIYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKIQGIVFDFVTQQAFDIVIMMLICLNMVTMMVETDTQSKQMENILYWINLVFVIFFTCECVLKMFALRHYYFTIGWNIFDFVVVILSIVGMFLADIIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIFSIFGMSNFAYVKHEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLLPILNRPPDCSLDKEHPGSGFKGDCGNPSVGIFFFVSYIIISFLIVVNMYIAIILENFSVATEESADPLSEDDFETFYEIWEKFDPDATQFIEYCKLADFADALEHPLRVPKPNTIELIAMDLPMVSGDRIHCLDILFAFTKRVLGDSGELDILRQQMEERFVASNPSKVSYEPITTTLRRKQEEVSAVVLQRAYRGHLARRGFICRKMASNKLENGGTHRDKKESTPSTASLPSYDSVTKPDKEKQQRAEEGRRERAKRQKEVRESKC
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Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.
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O88422
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GALT5_RAT
|
Polypeptide N-acetylgalactosaminyltransferase 5 (EC 2.4.1.41) (Polypeptide GalNAc transferase 5) (GalNAc-T5) (pp-GaNTase 5) (Protein-UDP acetylgalactosaminyltransferase 5) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5)
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MNKIRKFFRGSGRVLAFIFVASVIWLLFDMAALRLSFSEINTGILKEDIMRREQTGFRVEADQMTILSPSSRGMRPPRNGAGGKESFRKAENRVLKVEENVDQVQRKGKMQFLLGRGKAVSLWHRTHVQTLPVTLPMQKTQGRDSKPEVSSLHMMSKQTTVLGSEKDSFTVSRGVPLNKTAEHTETLDKKQEAPENYNLSSDTSKQASQRALNVTISVRTDRSKQQSQTVTKSSIQFASLPILKPEEVTVTKKTEAQGKDLKYEAHKARPLLKFTADVGHLKKQSTNETGLGVLPEADGAKVAPGKKLNFSESQIVIITKEEGQKTDTKEVPNSKIQTVFPKLLGESQGKHIPRSQSQTLSSPLAPKRAVSQSKPTLAEELHTARSNLTAKATTVGHQQSHANISENPGKHHVLRIDVTLSPRDLNAPGQFGRPVVVPPGKKKEAEQRWKEGNFNVYLSDLIPVDRAIEDTRPAGCAEQLVHNDLPTTSIIMCFVDEVWSALLRSVHSVLNRSPPHLIKEILLVDDFSTKDYLKANLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHVECNVGWLEPLLERVYLNRKKVACPVIEVINDKDMSYMTVDNFQRGVFTWPMNFGWRTIPPDVIAKNGIKETDIIRCPVMAGGLFSIDKSYFYELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRNDNPYSFPKDRMKTVERNLVRVAEVWLDEYKELFYGHGDHLIDQGLDVGNLTQQRELRKKLKCQSFKWYLDNVFPDLKAPVVRASGVFINLALGKCVSIKNITVVLEDCDGSSELQQFNYTWVRLIKHGEWCVAPIPDKGSLTLYPCDNRNNRLKWLHRSASAFHPELVDHIVFESYQQLLCMEGNFSQKTLKLAACNPTEPQQKWKFEKYYDV
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Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2, Muc1b, rMuc-2 or mG-Muc substrates.
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O88427
|
CAC1H_MOUSE
|
Voltage-dependent T-type calcium channel subunit alpha-1H (Voltage-gated calcium channel subunit alpha Cav3.2)
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MTEGTLAADEVRVPLGASPSAPAAPVRASPASPGVPGREEQRGSGSSVLAPESPGTECGADLGADEEQPVPYPALAATVFFCLGQTTRPRSWCLRLVSRRWFEHISMLVIMLNCVTLGMFRPCEDVECRSERCSILEAFDDFIFAFFAVEMVIKMVALGLFGQKCYLGDTWNRLDFFIVMAGMMEYSLDGHNVSLSAIRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLDSAFVRNNNLTFLRPYYQTEEGEENPFICSSRRDNGMQKCSHIPSRRELRVQCTLGWEAYGQPQAEDGGAGRNACINWNQYYNVCRSGEFNPHNGAINFDNIGYAWIAIFQVITLEGWVDIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRENQLMREQRARYLSNDSTLASFSEPGSCYEELLKYVGHIFRKVKRRSLRLYARWQSRWRKKVDPSSTLHGQGPRRRPRRAGRRTASVHHLVYHHHHHHHHHYHFSHGGPRRPSPEPGAGDTRLVRACVPPSPPSPGHGPPDSESVHSIYHADCHVEGPQERARVAHTIATAASLKLASGLGTMNYPTILPSGAVNSKGSTSSRPKGLRSAGTPGATAHSPLSLGSPSPYEKIQHVVGEQGLGRASSHLSGLSVPCPLPSPQAGTLTCELKSCPYCASALEDPEFEFSGSESGDSDAHGVYEFTQDVRHGDCRDPVQQPHEGGTPGHGNERWRPPLRTASQPGGLGRLWASFSSKLRRIVDSKYFNRGIMAAILVNTLSMGVEYHEQPDELTNALEISNIVFTSMFALEMLLKLLACGPLGYIRNPYNIFDGIVVIISVWEIVGQADGGLSVLRTFRLLRVLKLVRFLPALRRQLVVLMRTMDNVATFCMLLMLFIFIFSILGMHLFGCKFSLKTDSGDTVPDRKNFDSLLWAIVTVFQILTQEDWNVVLYNGMASTSSWAALYFVALMTFGNYVLFNLLVAILVEGFQAEGDATRSDTDEDKTSTHLEEDFDKLRDVQATEMKMYSLAVTPNGHLEGRGSLPPPLITHTAATPMPTPKSSPHLDMAHTLLDSRRSSSGSVDPQLGDQKSLASLRSSPCAPWGPNSAGSSRRSSWNSLGRAPSLKRRSQCGERESLLSGEGKGSTDDEAEDSRPNSGTHPGASPGPRATPLRRAESLGHRSTMDLCPPRPATLLPTKFRDCNGQMVALPSEFFLRIDSHKEDAAEFDDDIEDSCCFRLHKVLEPYAPQWCSSRESWALYLFPPQNRLRVSCQKVIAHKMFDHVVLVFIFLNCITIALERPDIDPGSTERAFLSVSNYIFTAIFVVEMMVKVVALGLLWGEHAYLQSSWNVLDGLLVLVSLVDIIVAVASAGGAKILGVLRVLRLLRTLRPLRVISRAPGLKLVVETLISSLRPIGNIVLICCAFFIIFGILGVQLFKGKFYYCEGTDTRNITTKAECHAAHYRWVRRKYNFDNLGQALMSLFVLSSKDGWVNIMYDGLDAVGIDQQPVQNHNPWMLLYFISFLLIVSFFVLNMFVGVVVENFHKCRQHQEAEEARRREEKRLRRLERRRRSTFPNPEAQRRPYYADYSHTRRSIHSLCTSHYLDLFITFIICLNVITMSMEHYNQPKSLDEALKYCNYVFTIVFVFEAALKLVAFGFRRFFKDRWNQLDLAIVLLSIMGIALEEIEMNAALPINPTIIRIMRVLRIARVLKLLKMATGMRALLDTVVQALPQVGNLGLLFMLLFFIYAALGVELFGRLECSEDNPCEGLSRHATFTNFGMAFLTLFRVSTGDNWNGIMKDTLRECTREDKHCLSYLPALSPVYFVTFVLVAQFVLVNVVVAVLMKHLEESNKEAREDAEMDAEIELEIAQGSTAQPPSTAQESQGTEPDTPNLLVVRKVSVSRMLSLPNDSYMFRPVAPAAAPHSHPLQEVEMETYTGPVTSAHSPSLEPRTSFQVPSAASSPARVSDPLCALSPRDTPRSLSLSRILCRQEAMHAESLEGQIDDAGEDSIPDYTEPAENISMSQAPLGTLRSPPCSPRPASVRTRKHTFGQHCISSRPPTLGGDDAEAADPADEEVSHITSSAHPWPATEPHSPEASPTASPAKGTVGSGRDPHRFCSVDAQSFLDKPGRPDAQRWSSVELDNGDGHLESGEVRARASELEPALGARRKKKMSPPCISIDPPTEDEGSSRPPAAEGGNTTLRRRTPSCEAALHRDCPESTEGPGTGGDPVAKGERWGQASCRAEHLTVPNFAFEPLDMGGPGGDCFLDSDQSVTPEPRVSSLGAIVPLILETELSMPSGDPPEKEQGLYLTVPQTPLKKPGSPPATPAPDDSGDEPV
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Voltage-sensitive calcium channel that gives rise to T-type calcium currents. T-type calcium channels belong to the 'low-voltage activated (LVA)' group. A particularity of this type of channel is an opening at quite negative potentials, and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons. In the adrenal zona glomerulosa, participates in the signaling pathway leading to aldosterone production in response to either AGT/angiotensin II, or hyperkalemia.
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O88428
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PAPS2_MOUSE
|
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 (PAPS synthase 2) (PAPSS 2) (Sulfurylase kinase 2) (SK 2) (SK2) [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (3'-phosphoadenosine-5'-phosphosulfate synthase) (APS kinase) (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenylylsulfate 3'-phosphotransferase)]
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MSANFKMNHKRDQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITSFISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKTNLSSVSDCVQQVVELLQEQNIVPHTTIKGIHELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDGVVPRDGVINMSIPIVLPVSADDKARLEGCSKFALMYEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDGLDQYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLEWRMKQHAAVLEERVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVAAYNKIKKAMDFYDPARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLEKTN
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Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate/PAPS, the activated sulfate donor used by sulfotransferases. In mammals, PAPS is the sole source of sulfate while APS appears to only be an intermediate in the sulfate-activation pathway. May have an important role in skeletogenesis during postnatal growth.
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O88430
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CCL22_MOUSE
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C-C motif chemokine 22 (Activated B and dendritic cell-derived) (CC chemokine ABCD-1) (Small-inducible cytokine A22)
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MATLRVPLLVALVLLAVAIQTSDAGPYGANVEDSICCQDYIRHPLPSRLVKEFFWTSKSCRKPGVVLITVKNRDICADPRQVWVKKLLHKLS
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Chemotactic for activated T-lymphocytes. May play an important role in the collaboration of dendritic cells and B-lymphocytes with T-cells in immune responses.
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O88436
|
PAX4_RAT
|
Paired box protein Pax-4
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MQQDGLSSVNQLGGLFVNGRPLPLDTRQQIVQLAIRGMRPCDISRSLKVSNGCVSKILGRYYRTGVLEPKGIGGSKPRLATPAVVARIAQLKDEYPALFAWEIQRQLCAEGLCTQDKAPSVSSINRVLRALQEDQRLHWTQLRSPAVLAPALPSPHSNCEAPRGPHPGTSHRNRTIFSPGQAEALEKEFQRGQYPDSVVRGKLAAATSLPEDTVRVWFSNRRAKWRRQEKLKWETQMPGASQDLMVPKDSPGIISAQQSPGSVPSAALPVLEQLNPSFCQLCWGAVPDRCSSDTTSQACLQPYWECHSLLPVASSSYMEFAWPCLTTHPVHHLIGGPGQAPSTYYLHWP
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Plays an important role in the differentiation and development of pancreatic islet beta cells. Transcriptional repressor that competes with PAX6 in binding to a common element in the glucagon, insulin and somatostatin promoters (By similarity).
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O88444
|
ADCY1_MOUSE
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Adenylate cyclase type 1 (EC 4.6.1.1) (ATP pyrophosphate-lyase 1) (Adenylate cyclase type I) (Adenylyl cyclase 1) (Ca(2+)/calmodulin-activated adenylyl cyclase)
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MAGAPRGQGGGGGAGEPGGAERAAGPGGRRGFRACGEEFACPELEALFRGYTLRLEQAATLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCILFLALFVVTNVRSLQVSQLQQVGQLALFFSLTFALLCCPFALGGPARSSAGGAMGSTVAEQGVWQLLLVTFVSYALLPVRSLLAIGFGLVVAASHLLVTAALVPAKRPRLWRTLGANALLFFGVNMYGVFVRILTERSQRKAFLQARNCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGHGHERNTFLRTHNIETFFIVPSHRRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALRTASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQKYHQLQDEYFTSAVVLALILAALFGLIYLLVIPQSVAVLLLLVFSICFLVACTLYLHITRVQCFPGCLTIQIRTALCVFIVVLIYSVAQGCVVGCLPWAWSSQSNSSLVVLAAGGRRTVLPALPCESAHHALLCCLVGTLPLAIFLRVSSLPKMILLSGLTTSYILVLELSGYTKVGGGALSGRSYEPIMAILLFSCTLALHARQVDVRLRLDYLWAAQAEEERDDMERVKLDNKRILFNLLPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEIIADFDELMDKDFYKDLEKIKTIGSTYMAAVGLAPTAGTRAKKSISSHLCTLADFAIDMFDVLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQVTEEVHRLLKRCSYQFVCRGKVSVKGKGEMLTYFLEGRTDGNSSHGRTFRLERRMCPYGRGGGQARRPPLCPAAGPPVRPGLPPAPTSQYLSSTAAGKEA
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Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates responses to increased cellular Ca(2+)/calmodulin levels. May be involved in regulatory processes in the central nervous system. May play a role in memory and learning. Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina.
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O88445
|
AURKC_MOUSE
|
Aurora kinase C (EC 2.7.11.1) (Aurora 3) (Aurora/IPL1-related kinase 3) (ARK-3) (Aurora-related kinase 3) (Aurora/IPL1/Eg2 protein 1) (Serine/threonine-protein kinase 13) (Serine/threonine-protein kinase aurora-C)
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MEPSTSTRKHFTINDFEIGRPLGRGKFGRVYLARLKENHFIVALKVLFKSEIEKEGLEHQLRREVEIQAHLQHRNILRLYNYFYDDTRIYLILEYAPGGELYKELQRHQKLDQQRTATIIQELSDALTYCHEKKVIHRDIKPENLLLGLNGEVKISDFGWSVHTPSLRRKTMCGTLDYLPPEMIAQKPYNEMVDLWCIGVLCYELLVGKPPFESSTSSETYRRIRQVDFKFPSSVPAGAQDLISKLLRYHPSERLSLAQVLKHPWVREHSRRVLPC
|
Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Also plays a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin and INCENP leading to increased AURKC activity. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'.
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O88446
|
S22A3_RAT
|
Solute carrier family 22 member 3 (Extraneuronal monoamine transporter) (EMT) (Organic cation transporter 3) (OCT3)
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MPTFDQALRKAGEFGRFQRRVFLLLCLTGVTFAFLFVGVVFLGSQPDYYWCRGPRATALAERCAWSPEEEWNLTTPELHVPAERRGQGHCHRYLLEDTNTSSELSCDPLAAFPNRSAPLVPCSGDWRYVETHSTIVSQFDLVCGNAWMLDLTQAILNLGFLAGAFTLGYAADRYGRLIVYLISCFGVGITGVVVAFAPNFSVFVIFRFLQGVFGKGAWMTCFVIVTEIVGSKQRRIVGIVIQMFFTLGIIILPGIAYFTPSWQGIQLAISLPSFLFLLYYWVVPESPRWLITRKQGEKALQILRRVAKCNGKHLSSNYSEITVTDEEVSNPSCLDLVRTPQMRKCTLILMFAWFTSAVVYQGLVMRLGLIGGNLYMDFFISGLVELPGALLILLTIERLGRRLPFAASNIVAGVSCLVTAFLPEGIPWLRTTVATLGRLGITMAFEIVYLVNSELYPTTLRNFGVSLCSGLCDFGGIIAPFLLFRLAAIWLELPLIIFGILASVCGGLVMLLPETKGIALPETVEDVEKLGSSQLHQCGRKKKTQVSTSNV
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Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics. Cation cellular uptake or release is driven by the electrochemical potential, i.e. membrane potential and concentration gradient. Functions as a Na(+)- and Cl(-)-independent, bidirectional uniporter. Implicated in neuronal monoamine neurotransmitters cellular uptake such as dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, histamine, serotonin and tyramine, thereby supporting a role in homeostatic regulation of aminergic neurotransmission in the brain. Transports dopaminergic neuromodulators cyclo(his-pro) and salsolinol with low efficiency (By similarity). May be involved in the uptake and disposition of cationic compounds by renal clearance from the blood flow (By similarity). May contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier. Mediates the transport of polyamine spermidine and putrescine. Mediates the bidirectional transport of polyamine agmatine. Also transports guanidine. May also mediate intracellular transport of organic cations, thereby playing a role in amine metabolism and intracellular signaling.
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O88447
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KLC1_MOUSE
|
Kinesin light chain 1 (KLC 1)
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MYDNMSTMVYIKEEKLENVTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSSMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQNVRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDSDSSKEPLDDLFPNDEDEPGQGIQHSDSSAAAARQGYEIPARLRTLHNLVIQYASQGRYEVAVPSCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGRDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALGIYQTKLGPDRTPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEAEFGSVDDENKPIWMHAEEREECKGKQKDGSAFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPESMEKRRSRESLNMDVVKYESGPDGGEEA
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Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity.
|
O88448
|
KLC2_MOUSE
|
Kinesin light chain 2 (KLC 2)
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MATMVLPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLASHEAGEAEPGSQERCLLLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEMLPQEEKGDVPKDSLDDLFPNEDEQSPAPSPGGGDVAAQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHPDVAKQLSNLALLCQNQGKAEEVEYYYRRALEIYATRLGPDDPNVAKTKNNLASCYLKQGKYQDAETLYKEILTRAHEKEFGSVNGENKPIWMHAEEREESKDKRRDRRPMEYGSWYKACKVDSPTVNTTLRTLGALYRPEGKLEAAHTLEDCASRSRKQGLDPASQTKVVELLKDGSGRGHRRGSRDVAGPQSESDLEESGPAAEWSGDGSGSLRRSGSFGKLRDALRRSSEMLVRKLQGGGPQEPNSRMKRASSLNFLNKSVEEPVQPGGRVFLTAAL
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Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends.
|
O88450
|
DEAF1_RAT
|
Deformed epidermal autoregulatory factor 1 homolog (Nuclear DEAF-1-related transcriptional regulator) (NUDR) (Suppressin)
|
MEDSDSAAKQLGLAEAAAVAAAAAVAAAAAAAAESEAEEPVLSRDEDSEEDADSEAERETRRVTAVAVMAAESGHMDMGTEALPSPDEAAAAAAFAEVTTVTVANVGSSADNVFTTSVANAASISGHVLSGRTALQIGDSLNTEKATLIVVHTDGSIVETTGLKGPAAPLTPGPQSPPTPLAPGQEKGGTKYNWDPSVYDSELPVRCRNISGTLYKSRLGSGGRGRCIKQGENWYSPTEFEAMAGRASSKDWKRSIRYAGRPLQCLIQDGILNPHAASCTCAACCDDMTLSGPVRLFVPYKRRKKENELPTTPVKKDSPKNITLLPATAATTFTVTPSGQITTSGALTFDRASTVEATAVISESPAQGDVFAGATVQEAGVQPPCRVGHPEPHYPGYQDSCQIAPFPEAALPTSHPKIVLTSLPALAVPPSTPTKAVSPTVVSGLEMSEHRSWLYLEEMVNSLLNTAQQLKTLFEQAKQASSCREAAVTQARMQVDAERKEQSCVNCGREAMSECTGCHKVNYCSTFCQRKDWKDHQHVCGQSASVTVQADDVHVEESVIEKVAV
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Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction. When secreted, behaves as an inhibitor of cell proliferation, by arresting cells in the G0 or G1 phase. Regulates epithelial cell proliferation and side-branching in the mammary gland. Required for neural tube closure and skeletal patterning. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Transcriptional activator of EIF4G3. May also involved in behavior (By similarity).
|
O88452
|
STC2_MOUSE
|
Stanniocalcin-2 (STC-2)
|
MCAERLGQFVTLALVFATLDPAQGTDSTNPPEGPQDRSSQQKGRLSLQNTAEIQHCLVNAGDVGCGVFECFENNSCEIQGLHGICMTFLHNAGKFDAQGKSFIKDALRCKAHALRHKFGCISRKCPAIREMVFQLQRECYLKHDLCSAAQENVGVIVEMIHFKDLLLHEPYVDLVNLLLTCGEDVKEAVTRSVQAQCEQSWGGLCSILSFCTSNIQRPPTAAPEHQPLADRAQLSRPHHRDTDHHLTANRGAKGERGSKSHPNAHARGRTGGQSAQGPSGSSEWEDEQSEYSDIRR
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Has an anti-hypocalcemic action on calcium and phosphate homeostasis.
|
O88453
|
SAFB1_RAT
|
Scaffold attachment factor B1 (SAF-B) (SAF-B1)
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MAETLSGLGDSGAASAAAVSSAASETGTRRLSDLRVIDLRAELRKRNLTSSGNKSVLMERLKKAIEEEGGNPDEIEVISEGNKKMPKRPSKGKKPEDEGVEDNGLEENSGDGQEDVETSLENLQDMDMMDISVLDEADIDNGSVADCVEEEEEATLPEGLGLLRIGRLQSKGLPEQLQELAIDDKEAINNVDTSSSDFTILQEMEEASLEPENEKILDILGETCKSEPVKEEGSELEQPFAQATSSVGPDRKLAEEEDLFESCGHPEEEEEEEEEEEQEEEQEEEGDLALASSSKSESSSTRCQWSEADALLAVVKREPAEAPGGGTGMDREPVGLEEPVEQSSTAAQLPETTSQELVRAPTAAPSPEPRDSKDDVKKFAFDACNDVPAAPKESSASEGADQKMSSVEDDSDTKRLSREEKGRSSCGRNFWVSGLSSTTRATDLKNLFSRYGKVVGAKVVTNARSPGARCYGFVTMSTAEEATKCINHLHKTELHGKMISVEKAKSEPAGKRVPDRRDGDSKKEKTSTSDRSANLKREEKGDRKDDAKKTDDGSTEKSKDADDQKPGPSERSRTTKSGSRGTERTVVMDKSKGVPVISVKTSGSKERASKSQDRKSVSREKRSVVSFDKVKESRKSRDSESRRERERERSEREQRLQAQWEREERERLEIARERLAFHRHRLERERMERERLERERMHVEQERRREQERIHREREELRRQQELRYEQERRPAVRRPYEVDGRRDDAYWPEAKRAALDDRYHSDFSRQDRFHDFDHRDRGRYPNHSVDRREGSRSMMGDREGQHYPERHGGPERHGRDSRDGWGYGSNKRLSEGRGLPLLPRRDWGEHARRLEDDRAWQGTADGGMMERDQQRWQGGERSMSGHSGPGHMMNRGGMSGRGSFAPGGASRRHVIPRGGMQAGFGGTEPGQQTQ
|
Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (By similarity). Functions as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription (By similarity). Thereby acts as a negative regulator of cell proliferation (By similarity). When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (By similarity).
|
O88454
|
KCNK4_MOUSE
|
Potassium channel subfamily K member 4 (TWIK-related arachidonic acid-stimulated potassium channel protein) (TRAAK)
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MRSTTLLALLALVLLYLVSGALVFQALEQPHEQQAQKKMDHGRDQFLRDHPCVSQKSLEDFIKLLVEALGGGANPETSWTNSSNHSSAWNLGSAFFFSGTIITTIGYGNIVLHTDAGRLFCIFYALVGIPLFGMLLAGVGDRLGSSLRRGIGHIEAIFLKWHVPPGLVRSLSAVLFLLIGCLLFVLTPTFVFSYMESWSKLEAIYFVIVTLTTVGFGDYVPGDGTGQNSPAYQPLVWFWILFGLAYFASVLTTIGNWLRAVSRRTRAEMGGLTAQAASWTGTVTARVTQRTGPSAPPPEKEQPLLPSSLPAPPAVVEPAGRPGSPAPAEKVETPSPPTASALDYPSENLAFIDESSDTQSERGCALPRAPRGRRRPNPSKKPSRPRGPGRLRDKAVPV
|
Voltage-insensitive potassium channel. Channel opening is triggered by mechanical forces that deform the membrane. Channel opening is triggered by raising the intracellular pH to basic levels (By similarity). The channel is inactive at 24 degrees Celsius (in vitro) raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius (By similarity). Plays a role in the sensory perception of pain caused by pressure. Plays a role in the perception of pain caused by heat.
|
O88455
|
DHCR7_MOUSE
|
7-dehydrocholesterol reductase (7-DHC reductase) (EC 1.3.1.21) (Sterol Delta(7)-reductase)
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MASKSQHNAPKVKSPNGKAGSQGQWGRAWEVDWFSLASIIFLLLFAPFIVYYFIMACDQYSCSLTAPALDIATGHASLADIWAKTPPVTAKAAQLYALWVSFQVLLYSWLPDFCHRFLPGYVGGVQEGAITPAGVVNKYEVNGLQAWLITHILWFVNAYLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMIKGYLFPTSAEDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQQELYGHVTNSMILVNVLQAIYVLDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPNALGILLLGLVGYYIFRMTNHQKDLFRRTDGRCLIWGKKPKAIECSYTSADGLKHHSKLLVSGFWGVARHFNYTGDLMGSLAYCLACGGGHLLPYFYIIYMTILLTHRCLRDEHRCANKYGRDWERYTAAVPYRLLPGIF
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7-dehydrocholesterol reductase of the cholesterol biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-3beta-ol, two intermediates in that pathway.
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O88456
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CPNS1_MOUSE
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Calpain small subunit 1 (CSS1) (Calcium-activated neutral proteinase small subunit) (CANP small subunit) (Calcium-dependent protease small subunit) (CDPS) (Calcium-dependent protease small subunit 1) (Calpain regulatory subunit)
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MFLVNSFLKGGGGGGGGGGLGGGLGNVLGGLISGAAGGGGGGGGGMGLGGGGGGGGTAMRILGGVISAISEAAAQYNPEPPPPRSHYSNIEANESEEVRQFRKLFVQLAGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKKWQAIYKRFDTDRSGTIGSHELPGAFEAAGFHLNEHLYSMIIRRYADESGNMDFDNFISCLVRLDAMFRAFKSLDKNGTGQIQVNIQEWLQLTMYS
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Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Essential for embryonic development.
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O88457
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SCNBA_RAT
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Sodium channel protein type 11 subunit alpha (NaN) (Sensory neuron sodium channel 2) (Sodium channel protein type XI subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.9)
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MEERYYPVIFPDERNFRPFTSDSLAAIEKRIAIQKERKKSKDKAAAEPQPRPQLDLKASRKLPKLYGDIPPELVAKPLEDLDPFYKDHKTFMVLNKKRTIYRFSAKRALFILGPFNPLRSLMIRISVHSVFSMFIICTVIINCMFMANSMERSFDNDIPEYVFIGIYILEAVIKILARGFIVDEFSFLRDPWNWLDFIVIGTAIATCFPGSQVNLSALRTFRVFRALKAISVISGLKVIVGALLRSVKKLVDVMVLTLFCLSIFALVGQQLFMGILNQKCIKHNCGPNPASNKDCFEKEKDSEDFIMCGTWLGSRPCPNGSTCDKTTLNPDNNYTKFDNFGWSFLAMFRVMTQDSWERLYRQILRTSGIYFVFFFVVVIFLGSFYLLNLTLAVVTMAYEEQNRNVAAETEAKEKMFQEAQQLLREEKEALVAMGIDRSSLNSLQASSFSPKKRKFFGSKTRKSFFMRGSKTAQASASDSEDDASKNPQLLEQTKRLSQNLPVDLFDEHVDPLHRQRALSAVSILTITMQEQEKFQEPCFPCGKNLASKYLVWDCSPQWLCIKKVLRTIMTDPFTELAITICIIINTVFLAVEHHNMDDNLKTILKIGNWVFTGIFIAEMCLKIIALDPYHYFRHGWNVFDSIVALLSLADVLYNTLSDNNRSFLASLRVLRVFKLAKSWPTLNTLIKIIGHSVGALGNLTVVLTIVVFIFSVVGMRLFGTKFNKTAYATQERPRRRWHMDNFYHSFLVVFRILCGEWIENMWGCMQDMDGSPLCIIVFVLIMVIGKLVVLNLFIALLLNSFSNEEKDGSLEGETRKTKVQLALDRFRRAFSFMLHALQSFCCKKCRRKNSPKPKETTESFAGENKDSILPDARPWKEYDTDMALYTGQAGAPLAPLAEVEDDVEYCGEGGALPTSQHSAGVQAGDLPPETKQLTSPDDQGVEMEVFSEEDLHLSIQSPRKKSDAVSMLSECSTIDLNDIFRNLQKTVSPKKQPDRCFPKGLSCHFLCHKTDKRKSPWVLWWNIRKTCYQIVKHSWFESFIIFVILLSSGALIFEDVNLPSRPQVEKLLRCTDNIFTFIFLLEMILKWVAFGFRRYFTSAWCWLDFLIVVVSVLSLMNLPSLKSFRTLRALRPLRALSQFEGMKVVVYALISAIPAILNVLLVCLIFWLVFCILGVNLFSGKFGRCINGTDINMYLDFTEVPNRSQCNISNYSWKVPQVNFDNVGNAYLALLQVATYKGWLEIMNAAVDSREKDEQPDFEANLYAYLYFVVFIIFGSFFTLNLFIGVIIDNFNQQQKKLGGQDIFMTEEQKKYYNAMKKLGTKKPQKPIPRPLNKCQAFVFDLVTSQVFDVIILGLIVLNMIIMMAESADQPKDVKKTFDILNIAFVVIFTIECLIKVFALRQHYFTNGWNLFDCVVVVLSIISTLVSRLEDSDISFPPTLFRVVRLARIGRILRLVRAARGIRTLLFALMMSLPSLFNIGLLLFLVMFIYAIFGMSWFSKVKKGSGIDDIFNFETFTGSMLCLFQITTSAGWDTLLNPMLEAKEHCNSSSQDSCQQPQIAVVYFVSYIIISFLIVVNMYIAVILENFNTATEESEDPLGEDDFEIFYEVWEKFDPEASQFIQYSALSDFADALPEPLRVAKPNKFQFLVMDLPMVMGDRLHCMDVLFAFTTRVLGDSSGLDTMKTMMEEKFMEANPFKKLYEPIVTTTKRKEEEQGAAVIQRAYRKHMEKMVKLRLKDRSSSSHQVFCNGDLSSLDVAKVKVHND
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This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant sodium channel isoform. Also involved, with the contribution of the receptor tyrosine kinase NTRK2, in rapid BDNF-evoked neuronal depolarization (By similarity). {ECO:0000250, ECO:0000269|PubMed:10196578}.
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O88466
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ZN106_MOUSE
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Zinc finger protein 106 (Zfp-106) (H3a minor histocompatibility antigen) (Son of insulin receptor mutant) (Zinc finger protein 474)
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MVRERKCILCHIVYGSKKEMDEHMRSMLHHRELENLKGRDISHECRVCRVTEVGLSAYAKHISGQLHKDNVDAQEREDDGKEEEEEEYFDKELVQLIQERKEQSRQDEPPSNSQEVNSDDRQPQWRREDRIPYQDRESYSQPPRHHRGPPQRDWKWEKDGFNSTRKNSFPHSLRNSGGPRGSSVWHKGATRGSSTWFLNHSNSGGGWHSNNGMVDWNYNGTGRNSSWHSEGTGGFPSWHMNNSNGNWKSSVRGTNSWNYNGLGDKFQQGRNRNPNYQMEDMTKMWNKKSNKPSKYSQERCKWQRQDRDKAAKYRSPPEGYASDTFPSEGLLEFNFEQRESQTTKQTDTAASKINGKNGTKARDKFRRWTPYPSQKTLDLQSALKEVIGSKSDTLEKPLFNFSLITAGLRKPVDKTSNPPVIKTQKAGPPGSPSHKAISDGTAFCEVARACSITEQSEPHQKSNKIPLLKSPLLPLPTPKSGPHKQNLKNRSKNKETKSFPSGDHSHLLNTSTLEGSHGSSYTSKSLGLCPRVLKENKTVSGTQKEPDEKLNNTSQKAQDTVLQCPKTLQNPLPTTPKRMENDAKESSVEESAKDSLSIESQPHSAGNSAMTSDAENHGIKSEGVASLTTEVVSCSTHTVDKEQGSQIPGTPENLSTSPRNSTVLQKEAEVQVSAATSPHSGLLLDLKTSLEDAQDNNLVKSDGPFETESFEDTSLDTELQKPDLNNQPPGTLLPELSKLGFPASLQRDLSRHISLKSKTGTHLPEPNLNSARRIRNVSGHRKNETEKESGLKPTLRQILNASRRNVNWEQVIQQVTKKKQELGKGLPRFGIEMVPLVQNEQEVLDLDEEPDLSSLEGFQWEGVSIPSSSGLARKRSLSESSVVMDRAPVYSFFTGEGTGKENEAQQSPSPNTALSAAQSQKTAMYLEQEVAPLTPSVGTGERVGNIPTQRRHSAQLPSGHIMPVMHSARDLHSQERSTPLSERHAQESTGEGNSLSSNASSGHAVSSLADAATDSSCTSGAEQTDGHSIRKKRRATGDGSSPELPSLERKNKRRKIKGKKERSQVDQLLTISLREEELSKSLQCMDNKLLQARAALQTAYVEVQRLLVLKQQITVEMSALRTHRIQILQGLQETYEPPEHPDQAPCSLISREQRNSRSQTSFETALLPAPFFPGFLDPPPSHASLPSPGNPLQITMSTFQAHGTAPDSSVQIKQEPMSPEQEGNMNALPQGCASNVSKELLQTNRVVDDGSSVYPAIPAVIASESTENCQEVSKDLNFSVEQGNSRSKGNSPSCQSPDLPGINRGEETAKGSSGSEACSSSFLRLSFTPETPAEKETQSPADQPEQQAESTLASAETRGSKKKKKLRKKKTLRATHVPENSDTEQDVFTAKPARKVKTAKAAKGAKVTTSQTGQEQGTARDEPDSDSSLEVLEVTNPQLEVVAIDTSESGDEKPDSPSKKDAWIAAEQNPIETSRSGCDEVSSTSELGTRYKDGVPVSVAETQTVISIKASKHSSEISSEPGDDEEPTEGSFEGHQAAVNAIQIFGNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLVTHTSGKSSVLYTGSSDHTIRCYNIKTRECMEQLQLEDRVLCLHNRWRTLYAGLANGTVVTFDIKNNKRQEIFECHGPRAVSCLATAQEGARKLLVVGSYDCTISVRDARNGLLLRTLEGHSKTVLCMKVVNDLVFSGSSDQSVHAHNIHTGELVRIYKGHNHAVTVVNILGKVMVTACLDKFVRVYELQSHDRLQVYGGHKDMIMCMTIHKSVIYTGCYDGSIQAVRLNLMQNYRCWWYGCTLIFGVVDHLKQHLLTDHTNPNFQTLKCRWRNCDAFFTARKGSKQDVAGHIERHAEDDSKIDS
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RNA-binding protein. Specifically binds to 5'-GGGGCC-3' sequence repeats in RNA. Essential for maintenance of peripheral motor neuron and skeletal muscle function. Required for normal expression and/or alternative splicing of a number of genes in spinal cord and skeletal muscle, including the neurite outgrowth inhibitor RTN4. Also contributes to normal mitochondrial respiratory function in motor neurons, via an unknown mechanism.
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O88470
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FOXL2_MOUSE
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Forkhead box protein L2 (Pituitary forkhead factor) (P-Frk)
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MMASYPEPEDTAGTLLAPESGRAVKEAEASPPSPGKGGGTTPEKPDPAQKPPYSYVALIAMAIRESAEKRLTLSGIYQYIIAKFPFYEKNKKGWQNSIRHNLSLNECFIKVPREGGGERKGNYWTLDPACEDMFEKGNYRRRRRMKRPFRPPPAHFQPGKGLFGSGGAAGGCGVPGAGADGYGYLAPPKYLQSGFLNNSWPLPQPPSPMPYASCQMAAAAAAAAAAAAAAGPGSPGAAAVVKGLAGPAASYGPYSRVQSMALPPGVVNSYNGLGGPPAAPPPPPPPPHPHPHPHAHHLHAAAAPPPAPPHHGAAAPPPGQLSPASPATAAPPAPAPTSAPGLQFACARQPELAMMHCSYWDHDSKTGALHSRLDL
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Transcriptional regulator. Critical factor essential for ovary differentiation and maintenance, and repression of the genetic program for somatic testis determination. Prevents trans-differentiation of ovary to testis through transcriptional repression of the Sertoli cell-promoting gene SOX9. Has apoptotic activity in ovarian cells. Suppresses ESR1-mediated transcription of PTGS2/COX2 stimulated by tamoxifen. Activates SIRT1 transcription under cellular stress conditions. Activates transcription of OSR2. Is a regulator of CYP19 expression. Is a transcriptional repressor of STAR. Participates in SMAD3-dependent transcription of FST via the intronic SMAD-binding element.
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O88477
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IF2B1_MOUSE
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Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2 mRNA-binding protein 1) (IMP-1) (Coding region determinant-binding protein) (CRD-BP) (IGF-II mRNA-binding protein 1) (VICKZ family member 1) (Zipcode-binding protein 1) (ZBP-1)
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MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQITQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQPVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVVITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNLAQARRK
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RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells (By similarity). Binds to the oncofetal H19 transcript and regulates its localization (By similarity). Binds to and stabilizes BTRC/FBW1A mRNA (By similarity). Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2 (By similarity). During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts (By similarity). Interacts with GAP43 transcript and transports it to axons. Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. Binding to MYC mRNA is enhanced by m6A-modification of the CRD (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA. Binds to the neuron-specific TAU mRNA and regulates its localization. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons. During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing. {ECO:0000250, ECO:0000250|UniProtKB:Q9NZI8, ECO:0000269|PubMed:15355996, ECO:0000269|PubMed:17264115, ECO:0000269|PubMed:21964071, ECO:0000269|PubMed:22465430}.
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O88480
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CABIN_RAT
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Calcineurin-binding protein cabin-1 (Calcineurin inhibitor) (CAIN)
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MIRIAALNASSTIEDDHEGSFKSHKIQTKEAQEAEAFALYHKALDLQKHDRFEESAKAYHELLEARLLREAVSSGDEKEGLKHPGLILKYSTYKNLAQLAAQREDLETAMEFYLEAVMLDSTDVNLWYKIGHVALRLIRLPLARHAFEEGLRCNPDHWPCLDNLITVLYTLSDYTTCLYFICKALEKDCRYSKGLVLKEKIFEEQPCLRKDSLRMFLKCDMSVHEVSVNAAETQAIVDEALGLRKKRQALIVREKEPDLKLVQPIPFFTWKCLGESLLAMYNHLTTCEPPRPSLGKRIDLSDYQDPSQLLAPSIVVTPVSVVQPSPVCTNPTVAVAEPVLSYTSVTTTSFPLHSPGLLDTGTPMGDVSGGDKSKKGVKRKKTLEESGETAKRRSARVRNTKCKKEEKVDFQGLLVKFLPSRLRKLDPEEEDDPFNNYEVQSEAKLESFSNVGPHRLSFDSATFMESEKQDVHAFLMENLTNGGVLELMMRYLKSMGHKFLLKWPPGLAEVVLSVYHSWRRHSTSLPNPLLRDCSNKHIKDMMLMSLSCMELQLDQWLLTKGRSSTVSPRNCPAGVVTGRFGPDFPGTHCLGDLLQLSFASSQRDLFEDGWLEFVVRVYWLKARFLALQGDMEQALENYDICTEILQSSTALQAQAGAEQRDIVIRLPNLHNDSIVSLEEIDKNLKSLERCQSLEEIQRLFEAGDYKAVVQLLRPTLCTSGFDRAKHLEFMTSIPERPAQLLLLQDSLLRLEEHRQCFECSDVALNEAVQQMLNSSDSAAKEEWAATVTQLLLGMEQALSSDSRGSILKESSSPTGLVRLTNNLIQVIDCSMAVQEEPKEPYVSSVLPWIILHRIIWQEEDTFRSLCHQQQLQNPTEEGISEMPMLPSSLMLLNTAHEYLGRRSWCCNSDGALLRFYVHVLQKELAASASEDTHPYKEELETALEQCFYCLYSFPSKKSKARYLEEHSAQQVDLTWEDALFMFEYFKPKTLPEFDSYKTSTVSADLANLLKRIATIVPRTEKPALSMDKVSAYIEGTSAEVPCLPDGADPAPPVLNELYYLLADYHFKNKEQSKAIKFYMHDICICPNRFDSWAGMALARASRIQDKLNSNELKSDGPIWRHATPVLNCFRRALEIDSSNLSLWIEYGTMSYALHSFASRQLKQWRAELPPEVVQQMEDRRDSMLETARHCFTSAAHCEGDGDEEEWLIHYMLGKVAEKQQQPPTVYLLHYRQAGHYLHEEAARYPKKIHYHNPPELAMEALEVYFRLHASILKLLGKPDSGVSAEVLVSFMKEAAEGPFARGEEKNTPKASEKEKACLVDEDSHSSAGTLPGPGASLPSSSGPGLTSPPYTATPIDHDYVKCKKPRQQATPDDRSQDSTAVALSDSSSTQDFFNEPTSLLDGSRKLLPEKRISGLSAQAGPSGKDLPGPTEERGKTEESLESTEAFRVVEPSVQKPVADSSASAYIPSKPAVSTPPPWDGKKRSDPLGEPVAFPQGLPAGAEEQRQFLTEQCIASFCLCLSRFPQHYKSLYRLAFLYTYSKTHRNLQWARDVLLGSSIPWQQLQHMPAQGLFCERNKTNFFNGIWRIPVDEIDRPGSFAWHMNRSIVLLLKVLAQLRDHSTLLKVSSMLQRTPDQGKKYLRDADRQVLAQRAFILTVKVLEDTLSELAEGLEHPGSKACGLSGARMTTDVSHKASPEDGQESLPHPKKLPLADGSGPGPEPGGKVGPLHQLPVATDTRDNTEQGGEPKDKERPPVGPTEPMDTGETAARHPDLEPTPRLLPGRPPRDRGPESRSAELSLEELSISTRQQPAPLVPSPVTPTTAAPTTMGARAAGHPEEAPPRPNRKRKLLQDTESGKTLLLDAYRVWQQGQKAMAYDLSRIEKIMSETYMLIKQVDEETALEQAVKFCQVHLGAAAQRQASGDAPTTPKHPKDSRENFFPATVAPSAPDTTAPDALQRPSDSHLKPGLAAAITCPPSASASTPDPGIPQPHRPEAVPSRAPLSPDGEEVSGVTEGPSFLSQEPRHSHQMKMAATGPLAEQHCWPVEAACQTGAEPTFSQATSTKVPSSGSTQTPESHQGKTESSRAKSRLLPNMPKLVIPSATTKFPPEITVTPPTPTLLSPKGSISEETKQKLKSAILSAQSAANVRKESLCQPALEVLETSSQESSLESETDEDDDFMDV
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May be required for replication-independent chromatin assembly (By similarity). May serve as a negative regulator of T-cell receptor (TCR) signaling via inhibition of calcineurin. {ECO:0000250, ECO:0000269|PubMed:9660798}.
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O88483
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PDP1_RAT
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[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (PDP 1) (EC 3.1.3.43) (Protein phosphatase 2C) (Pyruvate dehydrogenase phosphatase catalytic subunit 1) (PDPC 1)
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MPAPTQLFFPLVRNCELSRIYGTACYCHHKHLCCSPPYIPQNRLRYTPHPAYATFCRPRENWWQYTQGRRYASTPQKFYLTPPQVNSILKANEYSFKVPEFDGKNVSSILGFDSNRLPANAPIEDRRSATTCLQTRGMLLGVFDGHAGCACSQAVSERLFYYIAVSLLPHETLLEIENAVESGRALLPILQWHKHPNDYFSKEASKLYFNGLRTYWQELIDLNTGESADIDVKEALINAFKRLDNDISLEAQVGDPNSFLNYLVLRVAFSGATACVAHVDGVDLHVANTGDSRAMLGVQEEDGSWSAVTLSNDHNAQNERELQRLKLEHPKNEAKSVVKQDRLLGLLMPFRAFGDVKFKWSIDLQKRVIESGPDQLNDNEYTKFIPPNYHTPPYLTAEPEVTYHRLRPQDKFLVLATDGLWETMHRQDVVRIVGEYLTGMHHQQPIAVGGYKVTLGQMHGLLTERRAKMSSVFEDQNAATHLIRHAVGNNEFGAVDHERLSKMLSLPEELARMYRDDITIIVVQFNSHVVGAYQNQEQ
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Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.
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O88485
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DC1I1_MOUSE
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Cytoplasmic dynein 1 intermediate chain 1 (Cytoplasmic dynein intermediate chain 1) (Dynein intermediate chain 1, cytosolic) (DH IC-1)
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MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVQDDSDLDRKRRETEALLQSIGISPEPPLVPTPMSPSSKSVSTPSDAGSQDSGDLGPLTRTLQWDTDPSVLQLQSDSELGRRLHKLGVSKVTQVDFLPREVVSYSKETQTPLATHQSEEDEEDEEMVEPKIGHDSELENQEKKQETKEAPPRELTEEEKQQILHSEEFLIFFDRTIRVIERALAEDSDIFFDYSGRELEEKDGDVQAGANLSFNRQFYDEHWSKHRVVTCMDWSLQYPELMVASYSNNEDAPHEPDGVALVWNMKFKKTTPEYVFHCQSSVMSVCFARFHPNLVVGGTYSGQIVLWDNRSHRRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLITVSTDGKMCSWSLDMLSTPQESMELVYNKSKPVAVTGMAFPTGDVNNFVVGSEEGTVYTACRHGSKAGIGEVFEGHQGPVTGINCHMAVGPIDFSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNSDTEVPTASVAIEGASALNRVRWAQGGKEVAVGDSEGRIWIYDVGELAVPHNDEWTRFARTLVEIRANRADSEEEGAVELAA
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Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1. May play a role in mediating the interaction of cytoplasmic dynein with membranous organelles and kinetochores.
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O88487
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DC1I2_MOUSE
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Cytoplasmic dynein 1 intermediate chain 2 (Cytoplasmic dynein intermediate chain 2) (Dynein intermediate chain 2, cytosolic) (DH IC-2)
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MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAAVSVQEESDLEKKRREAEALLQSMGLTTDSPIVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRRGPIKLGMAKITQVDFPPREIVTYTKETQTPVTAQPKEDEEEEDDVATPKPPVEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEEAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA
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Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function (By similarity). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (By similarity). The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes.
|
O88488
|
PTPRQ_RAT
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Phosphatidylinositol phosphatase PTPRQ (EC 3.1.3.-) (Protein-tyrosine phosphatase receptor-type expressed by glomerular mesangial cells protein 1) (rPTP-GMC1) (Receptor-type tyrosine-protein phosphatase Q) (PTP-RQ) (R-PTP-Q) (EC 3.1.3.48)
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MMDFHFSFLFLLIGTSESQVDVSSSFDGTGYDITLSSVSATTYSSPVSRTLATNVTKPGPPVFLAGERVGSAGILLSWNTPPNPNGRIISYVVKYKEVCPWMQTAYTRARAKPDSLEVLLTNLNPGTTYEIKVAAENNAGIGVFSDPFLFQTAESAPGKVVNLTVEALNYSAVNLIWYLPRQPNGKITSFKISVKHARSGIVVKDVSLRVEDILSGKLPECNENSESFLWSTTSPSPTLGRVTPTVRTTQSSSTAARSKISSVWKEPISFVVTHLRPYTTYLFEVSAVTTEAGYIDSTIVRTPESVPEGPPQNCIMGNVTGKAFSISWDPPTIVTGKFSYRVELYGPSGRILDNSTKDLRFAFTHLTPFTMYDVYVAAETSAGVGPKSNLSVFTPPDVPGAVFDLQIAEVEATEIRITWRKPRQPNGIISQYRVKVSVLETGVVLENTLLTGQDESISNPMSPEIMNLVDPMIGFYEGSGEMSSDLHSPASFIYNSHPHNDFPASTRAEEQSSPVVTTRNQYMTDITAEQLSYVVRRLVPFTEHTISVSAFTIMGEGPPTVLTVRTREQVPSSIQIINYKNISSSSILLYWDPPEYPNGKITHYTIYATELDTNRAFQMTTVDNSFLITGLKKYTRYKMRVAASTHVGESSLSEENDIFVRTPEDEPESSPQDVQVTGVSPSELRLKWSPPEKPNGIIIAYEVLYQNADTLFVKNTSTTDIIISDLKPYTLYNISIRSYTRLGHGNQSSSLLSVRTSETVPDSAPENITYKNISSGEIEISFLPPRSPNGIIQKYTIYLKRSNSHEARTINTTSLTQTIGGLKKYTHYVIEVSASTLKGEGIRSRPISILTEEDAPDSPPQNFSVKQLSGVTVMLSWQPPLEPNGIILYYTVYVWDKSSLRAINATEASLVLSDLDYNVDYGACVTASTRFGDGNARSSIINFRTPEGEPSDPPNDVHYVNLSSSSIILFWTPPVKPNGIIQYYSVYYQNTSGTFVQNFTLLQVTKESDNVTVSARIYRLAIFSYYTFWLTASTSVGNGNKSSDIIHVYTDQDIPEGPVGNLTFESISSTAIHVSWEPPSQPNGLVFYYLSLNLQQSPPRHMIPPLVTYENSIDFDDLEKYTDYIFKITPSTEKGFSETYTTQLHIKTEEDVPDTPPIINTFKNLSSTSILLSWDPPLKPNGAILGYHLTLQGPHANHTFVTSGNHIVLEELSPFTLYSFFAAARTMKGLGPSSILFFYTDESAPLAPPQNLTLINYTSDFVWLTWSPSPLPGGIVKVYSFKIHEHETDTVFYKNISGLQTDAKLEGLEPVSTYSVSVSAFTKVGNGNQYSNVVEFTTQESVPEAVRNIECVARDWQSVSVRWDPPRKTNGIIIHYMITVGGNSTKVSPRDPTYTFTKLLPNTSYVFEVRASTSAGEGNESRCDISTLPETVPSAPTNVAFSNVQSTSATLTWTKPDTIFGYFQNYKITTQLRAQKCREWEPEECIEHQKDQYLYEANQTEETVHGLKKFRWYRFQVAASTNVGYSNASEWISTQTLPGPPDGPPENVHVVATSPFGINISWSEPAVITGPTFYLIDVKSVDDDDFNISFLKSNEENKTTEINNLEVFTRYSVVITAFVGNVSRAYTDGKSSAEVIITTLESVPKDPPNNMTFQKIPDEVTKFQLTFLPPSQPNGNIRVYQALVYREDDPTAVQIHNFSIIQKTDTSIIAMLEGLKGGHTYNISVYAINSAGAGPKVQMRITMDIKAPARPKSKPIPIRDATGKLLVTSTTITIRMPICYYNDDHGPIRNVQVLVAETGAQQDGNVTKWYDAYFNKARPYFTNEGFPNPPCIEGKTKFSGNEEIYVIGADNACMIPGNEEKICNGPLKPKKQYLFKFRATNVMGQFTDSEYSDPIKTLGEGLSERTVEIILSVTLCILSIILLGTAIFAFVRIRQKQKEGGTYSPRDAEIIDTKFKLDQLITVADLELKDERLTRLLSYRKSIKPISKKSFLQHVEELCTNSNLKFQEEFSELPKFLQDLSSTDADLPWNRAKNRFPNIKPYNNNRVKLIADVSLPGSDYINASYVSGYLCPNEFIATQGPLPGTVGDFWRMVWETRTKTLVMLTQCFEKGRIRCHQYWPEDNKPVTVFGDIVITKLMEDIQIDWTIRDLKIERHGDCMTVRQCNFTGWPEHGVPENTTPLIHFVKLVRTSRAHDTTPMVVHCSAGVGRTGVFIALDHLTQHINNHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQCILDLLSNKGGHQPVCFVNYSTLQKMDSLDAMEGDVELEWEETTM
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Phosphatidylinositol phosphatase required for auditory function. May act by regulating the level of phosphatidylinositol 4,5-bisphosphate (PIP2) level in the basal region of hair bundles. Can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. Has low tyrosine-protein phosphatase activity however, the relevance of such activity in vivo is unclear. Plays an important role in adipogenesis of mesenchymal stem cells (MSCs). Regulates the phosphorylation state of AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs and preadipocyte cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:12802008}.
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O88491
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NSD1_MOUSE
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Histone-lysine N-methyltransferase, H3 lysine-36 specific (EC 2.1.1.357) (H3-K36-HMTase) (Nuclear receptor-binding SET domain-containing protein 1) (NR-binding SET domain-containing protein)
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MDRTCELSRRNCLLSFSNPVNLDASEDKDSPFGNGQSNFSEPLNGCTMQLPTAASGTSQNAYGQDSPSCYIPLRRLQDLASMINVEYLSGSADGSESFQDPAKSDSRAQSPIVCTSLSPGGPTALAMKQEPTCNNSPELQLRVTKTTKNGFLHFENFTGVDDADVDSEMDPEQPVTEDESIEEIFEETQTNATCNYEPKSENGVEVAMGSEQDSMPESRHGAVERPFLPLAPQTEKQKNKQRSEVDGSNEKTALLPAPTSLGDTNVTVEEQFNSINLSFQDDPDSSPSPLGNMLEIPGTSSPSTSQELPFVPQKILSKWEASVGLAEQYDVPKGSKNQKCVSSSVKLDSEEDMPFEDCTNDPDSEHLLLNGCLKSLAFDSEHSADEKEKPCAKSRVRKSSDNIKRTSVKKDLVPFESRKEERRGKIPDNLGLDFISGGVSDKQASNELSRIANSLTGSSTAPGSFLFSSSVQNTAKTDFETPDCDSLSGLSESALISKHSGEKKKLHPGQVCSSKVQLCYVGAGDEEKRSNSVSVSTTSDDGCSDLDPTEHNSGFQNSVLGITDAFDKTENALSVHKNETQYSRYPVTNRIKEKQKSLITNSHADHLMGSTKTMEPETAELSQVNLSDLKISSPIPKPQPEFRNDGLTTKFSAPPGIRNENPLTKGGLANQTLLPLKCRQPKFRSIKCKHKESPAVAETSATSEDLSLKCCSSDTNGSPLANISKSGKGEGLKLLNNMHEKTRDSSDIETAVVKHVLSELKELSYRSLSEDVSDSGTAKASKPLLFSSASSQNHIPIEPDYKFSTLLMMLKDMHDSKTKEQRLMTAQNLASYRTPDRGDCSSGSPVGTSKVLVLGSSTPNSEKPGDSTQDSVHQSPGGGDSALSGELSSSLSSLASDKRELPACGKIRSNCIPRRNCGRAKPSSKLRETISAQMVKPSVNPKALKTERKRKFSRLPAVTLAANRLGNKESGSVNGPSRGGAEDPGKEEPLQQMDLLRNEDTHFSDVHFDSKAKQSDPDKNLEKEPSFENRKGPELGSEMNTENDELHGVNQVVPKKRWQRLNQRRPKPGKRANRFREKENSEGAFGVLLPADAVQKAREDYLEQRAPPTSKPEDSAADPNHGSHSESVAPRLNVCEKSSVGMGDVEKETGIPSLMPQTKLPEPAIRSEKKRLRKPSKWLLEYTEEYDQIFAPKKKQKKVQEQVHKVSSRCEDESLLARCQPSAQNKQVDENSLISTKEEPPVLEREAPFLEGPLAQSDLGVTHAELPQLTLSVPVAPEASPRPALESEELLVKTPGNYESKRQRKPTKKLLESNDLDPGFMPKKGDLGLSRKCFEASRSGNGIVESRATSHLKEFSGGTTKIFDKPRKRKRQRLVTARVHYKKVKKEDLTKDTPSSEGELLIHRTAASPKEILEEGVEHDPGMSASKKLQVERGGGAALKENVCQNCEKLGELLLCEAQCCGAFHLECLGLPEMPRGKFICNECHTGIHTCFVCKQSGEDVKRCLLPLCGKFYHEECVQKYPPTVTQNKGFRCPLHICITCHAANPANVSASKGRLMRCVRCPVAYHANDFCLAAGSKILASNSIICPNHFTPRRGCRNHEHVNVSWCFVCSEGGSLLCCDSCPAAFHRECLNIDIPEGNWYCNDCKAGKKPHYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTYKKALQEAAARFEELKARKELRQLQEDRKNDKKPPPYKHIKVNRPIGRVQIFTADLSEIPRCNCKATDENPCGIDSECINRMLLYECHPTVCPAGVRCQNQCFSKRQYPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLGVRPKNQPIVTEEKSRKFKRKPHGKRRSQGEVTKEREDECFSCGDAGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWHQCDVCGKEAASFCEMCPSSFCKQHREGMLFISKLDGRLSCTEHDPCGPNPLEPGEIREYVPPTATSPPSPGTQPKEQSSEMATQGPKKSDQPPTDATQLLPLSKKALTGSCQRPLLPERPPERTDSSSHLLDRIRDLAGSGTKSQSLVSSQRPQDRPPAKEGPRPQPPDRASPMTRPSSSPSVSSLPLERPLRMTDSRLDKSIGAASPKSQAVEKTPASTGLRLSSPDRLLTTNSPKPQISDRPPEKSHASLTQRLPPPEKVLSAVVQSLVAKEKALRPVDQNTQSKHRPAVVMDLIDLTPRQKERAASPQEVTPQADEKTAMLESSSWPSSKGLGHIPRATEKISVSESLQPSGKVAAPSEHPWQAVKSLTHARFLSPPSAKAFLYESATQASGRTPVGAEQTPGPPSPAPGLVKQVKQLSRGLTAKSGQSFRSLGKISASLPNEEKKLTTTEQSPWGLGKASPGAGLWPIVAGQTLAQACWSAGGTQTLAQTCWSLGRGQDPKPENAIQALNQAPSSRKCADSEKK
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Histone methyltransferase that dimethylates Lys-36 of histone H3 (H3K36me2). Transcriptional intermediary factor capable of negatively influencing transcription. May also positively influence transcription. Essential for early post-implantation development.
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O88496
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VKGC_RAT
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Vitamin K-dependent gamma-carboxylase (EC 4.1.1.90) (Gamma-glutamyl carboxylase) (Peptidyl-glutamate 4-carboxylase) (Vitamin K gamma glutamyl carboxylase)
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MAVHRGSARAAPASDKVQKNKPAQTSGLEQGSRMARIFGFEWADLSSWQSVVTLLNRPTDPANLAVFRFLFAFLMLLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLWYRLSCMLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLSAQKKNAHVPLWNYTVLRGQIFIVYFIAGVKKLDADWVEGYSMEHLSRHWLFSPFKLVLSEELTSLLVVHWCGLLLDLSAGFLLFFDASRPIGLVFVSYFHCMNSQLFSIGMFPYVMLASSPLFCSAEWPRKLVARCPKRLQELLPAKAAPRPSASCVYKRARAKAGQKPGLRHHLGTVFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGLTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSLLLPKYNVTEPQIYFDIWVSINDRFQQRLFDPRVDIVQAVWSPFRRTPWVQPLLMDLSPWRTKLQDIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTVSSSPSCYMYIYVNTTEVALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQRKLQEIERRRNSPLHERFLRFVLRKLYVFRRSFLMTRISLRNLLFGRPSLEQLAQEVTYANLRPFEPVDESSASNTDSSDPHPSEPDSEHVHSEL
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Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. Catalyzes gamma-carboxylation of various proteins, such as blood coagulation factors (F2, F7, F9 and F10), osteocalcin (BGLAP) or matrix Gla protein (MGP).
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O88498
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B2L11_RAT
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Bcl-2-like protein 11 (Bcl2-L-11) (Bcl-2-related ovarian death protein) (Bcl2-interacting mediator of cell death)
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MAKQPSDVNSECDREGGQLQPAERPPQLRPGAPTSLQTESQGNPDGEGDRCPHGSPQGPLAPPASPGPFATRSPLFIFVRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRAFANDYREAEDHPQMVILQLLRFIFRLVWRRH
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Induces apoptosis and anoikis.
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O88502
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PDE8A_MOUSE
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High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A (MmPDE8) (EC 3.1.4.53)
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MGCAPSIHTSENRTFSHSDGEDEDVDVDVPGPAPRSIQRWSTAPGLVEPQPRDNGASKVSVADVQFGPMRFHQDQLQVLLVFTKEDSQCNGFHRACEKAGFKCTVTKEVQTVLTCFQDKLHDIIIIDHRYPRQMDAETLCRSIRSSKFSENTVIVGVVRRVDKEESSLMPFLAAGFTRRFIENPNVMACYNELLQLACGEVRSQLKLRACNSVFTALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHTQKKNGDNIQQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKVETTTECVQTDSQTDNQAGKHKDRRKHSMDAKAVSSRTSDVSSQRRHSSLARIHSMMIEAPITKVINIINAAQENSPVPVTEALNRVLDILRTTELYSPQFNAQDDPHATDLVGGLMSDGLRRFSGNEYILATKNLPPLSNNLATPVSLHDVPPRIALAIENEEQWDFDIFELEVATQNRPLIYLGLKTFARFGMCEFLQCSETTLRSWFQMIESNYHSSNPYHNSTHAADVLHATAYFLSRDKIKETLDRIDEVAALIAATVHDVDHPGRTNSFLCNAGNQLAVLYNDTAVLESHHVALAFQLTLENDQCNIFKQMERNDYRTLRQSIIDMVLATEMTKHFEHVNKFINSINKPLTAQESEEPDRSLEDIKAMLKTPESRALIKRMMIKCADVSNPCRPLEHCIEWAARISEEYFSQTDEEKQLDLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFVDLPNLMQHLDDNFRYWKGLDEKKLRSLRPPPE
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Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development. Binding to RAF1 reduces RAF1 'Ser-259' inhibitory-phosphorylation and stimulates RAF1-dependent EGF-activated ERK-signaling. Protects against cell death induced by hydrogen peroxide and staurosporine.
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O88506
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STK39_RAT
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STE20/SPS1-related proline-alanine-rich protein kinase (Ste-20-related kinase) (EC 2.7.11.1) (Pancreatic serine/threonine-protein kinase) (PS/TK) (PSTK1) (Serine/threonine-protein kinase 39)
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MAEPSGSPVHVQLPQQAAPVTAAAAAPAAATSAPAPAPAPAAPAAPAPAPAAAPAPAPAAQAVGWPICRDAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPNVVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGLDYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDKEMMKKYGKSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEKLLTRTPDIAQRAKKVRRVPGSSGHLHKTEDGDWEWSDDEMDEKSEEGKAAASQEKSRRVKEENPEISVNAGGIPEQIQSLSVHDSQGQPNANEDYREGPCAVNLVLRLRNSRKELNDIRFEFTPGRDTADGVSQELFSAGLVDGHDVVIVAANLQKIVDDPKALKTLTFKLASGCDGAEIPDEVKLIGFAQLSVS
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Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure. Specifically recognizes and binds proteins with a RFXV motif (By similarity). Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity. Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases (By similarity). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux. Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4 (By similarity). Mediates the inhibition of SLC4A4, SLC26A6 as well as CFTR activities. Phosphorylates RELT (By similarity).
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O88507
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CNTFR_MOUSE
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Ciliary neurotrophic factor receptor subunit alpha (CNTF receptor subunit alpha) (CNTFR-alpha)
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MAASVPWACCAVLAAAAAAVYTQKHSPQEAPHVQYERLGADVTLPCGTASWDAAVTWRVNGTDLAPDLLNGSQLILRSLELGHSGLYACFHRDSWHLRHQVLLHVGLPPREPVLSCRSNTYPKGFYCSWHLPTPTYIPNTFNVTVLHGSKIMVCEKDPALKNRCHIRYMHLFSTIKYKVSISVSNALGHNTTAITFDEFTIVKPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQHVELSDGTAHTITDAYAGKEYIIQVAAKDNEIGTWSDWSVAAHATPWTEEPRHLTTEAQAPETTTSTTSSLAPPPTTKICDPGELGSGGGPSILFLTSVPVTLVLAAAAATANNLLI
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Binds to CNTF. The alpha subunit provides the receptor specificity (By similarity).
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O88508
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DNM3A_MOUSE
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DNA (cytosine-5)-methyltransferase 3A (Dnmt3a) (EC 2.1.1.37) (Cysteine methyltransferase DNMT3A) (EC 2.1.1.-) (DNA methyltransferase MmuIIIA) (DNA MTase MmuIIIA) (M.MmuIIIA)
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MPSSGPGDTSSSSLEREDDRKEGEEQEENRGKEERQEPSATARKVGRPGRKRKHPPVESSDTPKDPAVTTKSQPMAQDSGPSDLLPNGDLEKRSEPQPEEGSPAAGQKGGAPAEGEGTETPPEASRAVENGCCVTKEGRGASAGEGKEQKQTNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAVMNAVEENQASGESQKVEEASPPAVQQPTDPASPTVATTPEPVGGDAGDKNATKAADDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPACHDSDESDSGKAVEVQNKQMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTTEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV
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Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity. Also has weak auto-methylation activity on Cys-706 in absence of DNA.
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O88509
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DNM3B_MOUSE
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DNA (cytosine-5)-methyltransferase 3B (Dnmt3b) (EC 2.1.1.37) (DNA methyltransferase MmuIIIB) (DNA MTase MmuIIIB) (M.MmuIIIB)
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MKGDSRHLNEEEGASGYEECIIVNGNFSDQSSDTKDAPSPPVLEAICTEPVCTPETRGRRSSSRLSKREVSSLLNYTQDMTGDGDRDDEVDDGNGSDILMPKLTRETKDTRTRSESPAVRTRHSNGTSSLERQRASPRITRGRQGRHHVQEYPVEFPATRSRRRRASSSASTPWSSPASVDFMEEVTPKSVSTPSVDLSQDGDQEGMDTTQVDAESRDGDSTEYQDDKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMPGMRWVQWFGDGKFSEISADKLVALGLFSQHFNLATFNKLVSYRKAMYHTLEKARVRAGKTFSSSPGESLEDQLKPMLEWAHGGFKPTGIEGLKPNKKQPVVNKSKVRRSDSRNLEPRRRENKSRRRTTNDSAASESPPPKRLKTNSYGGKDRGEDEESRERMASEVTNNKGNLEDRCLSCGKKNPVSFHPLFEGGLCQSCRDRFLELFYMYDEDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGAGTAEDAKLQEPWSCYMCLPQRCHGVLRRRKDWNMRLQDFFTTDPDLEEFEPPKLYPAIPAAKRRPIRVLSLFDGIATGYLVLKELGIKVEKYIASEVCAESIAVGTVKHEGQIKYVNDVRKITKKNIEEWGPFDLVIGGSPCNDLSNVNPARKGLYEGTGRLFFEFYHLLNYTRPKEGDNRPFFWMFENVVAMKVNDKKDISRFLACNPVMIDAIKVSAAHRARYFWGNLPGMNRPVMASKNDKLELQDCLEFSRTAKLKKVQTITTKSNSIRQGKNQLFPVVMNGKDDVLWCTELERIFGFPAHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE
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Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing. In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Functions as a transcriptional corepressor by associating with ZHX1 (By similarity). Required for DUX4 silencing in somatic cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UBC3, ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:11836534, ECO:0000269|PubMed:11919202, ECO:0000269|PubMed:16567415, ECO:0000269|PubMed:18056424, ECO:0000269|PubMed:18567530}.
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O88513
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GEMI_MOUSE
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Geminin
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MNLSMKQKQEGAQENVKNSPVPRRTLKMIQPSADGSLVGRENELPKGLFKRKLWDDQLASQTSSCGPEANENKDVGDLTQEAFDLISKENPSSQYWKEVAEQRRKALYEALKENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQYMAEVIERLSNEPLDNFESPDSQEFDSEEEAVEYSELEDSGAGTCAEETVSSSTDARPCT
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Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC). It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle. Inhibits histone acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, inhibiting histone H4 acetylation and DNA replication licensing (By similarity). Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control (By similarity).
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O88516
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DLL3_MOUSE
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Delta-like protein 3 (Drosophila Delta homolog 3) (Delta3) (M-Delta-3)
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MVSLQVSPLSQTLILAFLLPQALPAGVFELQIHSFGPGPGLGTPRSPCNARGPCRLFFRVCLKPGVSQEATESLCALGAALSTSVPVYTEHPGESAAALPLPDGLVRVPFRDAWPGTFSLVIETWREQLGEHAGGPAWNLLARVVGRRRLAAGGPWARDVQRTGTWELHFSYRARCEPPAVGAACARLCRSRSAPSRCGPGLRPCTPFPDECEAPSVCRPGCSPEHGYCEEPDECRCLEGWTGPLCTVPVSTSSCLNSRVPGPASTGCLLPGPGPCDGNPCANGGSCSETSGSFECACPRGFYGLRCEVSGVTCADGPCFNGGLCVGGEDPDSAYVCHCPPGFQGSNCEKRVDRCSLQPCQNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGSRRCSCALGFGGRDCRERADPCASRPCAHGGRCYAHFSGLVCACAPGYMGVRCEFAVRPDGADAVPAAPRGLRQADPQRFLLPPALGLLVAAGLAGAALLVIHVRRRGPGQDTGTRLLSGTREPSVHTLPDALNNLRLQDGAGDGPSSSADWNHPEDGDSRSIYVIPAPSIYAREDWLIQVLF
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Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm.
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O88522
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NEMO_MOUSE
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NF-kappa-B essential modulator (NEMO) (IkB kinase-associated protein 1) (IKKAP1) (mFIP-3) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
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MNKHPWKNQLSEMVQPSGGPAEDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVETPQPPLLPAPAHHSFHLALSNQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE
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Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much highr affinity for linear polyubiquitin. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response this function requires 'Lys-27'-linked polyubiquitination (By similarity).
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O88529
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BMAL1_MESAU
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Basic helix-loop-helix ARNT-like protein 1 (Aryl hydrocarbon receptor nuclear translocator-like protein 1) (Brain and muscle ARNT-like 1)
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MADQRMDISSTISDFMSPGPTDLLSSSLGTSGVDCNRKRKGSATDYQESMDTDKDDPHGRLEYAEHQGRIKNAREAHSQIEKRRRDKMNSFIDELASLVPTCNAMSRKLDKLTVLRMAVQHMKTLRGATNPYTEANYKPTFLSDDELKHLILRAADGFLFVVGCDRGKILFVSESVFKILNYSQNDLIGQSLFDYLHPKDIAKVKEQLSSSDTAPRERLIDAKTGLPVKTDITPGPSRLCSGARRSFFCRMKCNRPSVKVEDKDFASTCSKKKADRKSFCTIHSTGYLKSWPPTKMGLDEDNEPDNEGCNLSCLVAIGRLHSHVVPQPVNGEIRVKSMEYVSRHAIDGKFVFVDQRATAILAYLPQELLGTSCYEYFHQDDIGHLAECHRQVLQTREKITTNCYKFKIKDGSFITLRSRWFSFMNPWTKEVEYIVSTNTVVLANVLEGGDPTFPQLTASPHSMDSMLPSGEGGPKRTHPTVPGIPGGTRAGAGKIGRMIAEEIMEIHRIRGSSPSSCGSSPLNITSTPPPDASSPGGKKILNGGTPDIPSTGLLPGQAQETPGYPYSDSSSILGENPHIGIDMIDNDQGSSSPSNDEAAMAVIMSLLEADAGLGGPVDFSDLPWPL
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Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. BMAL1 positively regulates myogenesis and negatively regulates adipogenesis via the transcriptional control of the genes of the canonical Wnt signaling pathway. Plays a role in normal pancreatic beta-cell function regulates glucose-stimulated insulin secretion via the regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2, PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling pathway regulates the expression of MTOR and DEPTOR. Controls diurnal oscillations of Ly6C inflammatory monocytes rhythmic recruitment of the PRC2 complex imparts diurnal variation to chemokine expression that is necessary to sustain Ly6C monocyte rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1, CYP19A1 and LHCGR in the ovary and also the genes involved in hair growth. Plays an important role in adult hippocampal neurogenesis by regulating the timely entry of neural stem/progenitor cells (NSPCs) into the cell cycle and the number of cell divisions that take place prior to cell-cycle exit. Regulates the circadian expression of CIART and KLF11. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The NPAS2-BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence. CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3'. The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3'. Essential for the rhythmic interaction of CLOCK with ASS1 and plays a critical role in positively regulating CLOCK-mediated acetylation of ASS1. Plays a role in protecting against lethal sepsis by limiting the expression of immune checkpoint protein CD274 in macrophages in a PKM2-dependent manner (By similarity). Regulates the diurnal rhythms of skeletal muscle metabolism via transcriptional activation of genes promoting triglyceride synthesis (DGAT2) and metabolic efficiency (COQ10B) (By similarity).
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O88531
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PPT1_MOUSE
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Palmitoyl-protein thioesterase 1 (PPT-1) (EC 3.1.2.22) (Palmitoyl-protein hydrolase 1)
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MASSCSRRLLAAALLPWCCAAWALGHLDPPSPPPLVIWHGMGDSCCNPMSMGVIKKMVEKEIPGIYVLSLEIGKNMMEDVENSFFLNVNVQVNMVCQILEKDPKLQQGYNAIGFSQGGQFLRAVAQRCPTPPMMTLISVGGQHQGVFGLPRCPGESSHICDFIRKSLNAGAYSKLVQERLVQAQYWHDPIKESVYRNYSIFLADINQERCVNESYKKNLMALKKFVMVKFFNDSIVDPVDSEWFGFYRSGQAKETIPLQESTLYTEDRLGLKKMDKAGKLVFLAKEGDHLQISKEWFTAHIIPFLK
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Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.
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O88533
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DDC_MOUSE
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Aromatic-L-amino-acid decarboxylase (AADC) (EC 4.1.1.28) (DOPA decarboxylase) (DDC)
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MDSREFRRRGKEMVDYIADYLDGIEGRPVYPDVEPGYLRPLIPATAPQEPETYEDIIKDIEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPEAFLAGRAGEGGGVIQGSASEATLVALLAARTKVIRQLQAASPEFTQAAIMEKLVAYTSDQAHSSVERAGLIGGIKLKAVPSDGNFSMRASALREALERDKAAGLIPFFVVATLGTTSCCSFDNLLEVGPICNQEGVWLHIDAAYAGSAFICPEFRYLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKRRTDLTGAFNMDPVYLKHSHQDSGFITDYRHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVELSHEFESLVRQDPRFEICTEVILGLVCFRLKGSNELNETLLQRINSAKKIHLVPCRLRDKFVLRFAVCARTVESAHVQLAWEHISDLASSVLRAEKE
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Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
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O88536
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FPR2_MOUSE
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Formyl peptide receptor 2 (Formylpeptide receptor-related sequence 2) (Lipoxin A4 receptor-like protein) (N-formylpeptide receptor-like 2)
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MESNYSIHLNGSEVVVYDSTISRVLWILSMVVVSITFFLGVLGNGLVIWVAGFRMPHTVTTIWYLNLALADFSFTATLPFLLVEMAMKEKWPFGWFLCKLVHIVVDVNLFGSVFLIALIALDRCICVLHPVWAQNHRTVSLARKVVVGPWIFALILTLPIFIFLTTVRIPGGDVYCTFNFGSWAQTDEEKLNTAITFVTTRGIIRFLIGFSMPMSIVAVCYGLIAVKINRRNLVNSSRPLRVLTAVVASFFICWFPFQLVALLGTVWFKETLLSGSYKILDMFVNPTSSLAYFNSCLNPMLYVFMGQDFRERFIHSLPYSLERALSEDSGQTSDSSTSSTSPPADIELKAP
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High affinity receptor for N-formyl-methionyl peptides (FMLP), which are powerful neutrophil chemotactic factors. Stimulates chemotaxis in immune cells to site of infection or tissue damage upon recognition of several ligands, such as FMLP, or ligand involved in cell damage, disease or inflammation. Receptor for the chemokine-like protein FAM19A5, mediating FAM19A5-stimulated macrophage chemotaxis and the inhibitory effect on TNFSF11/RANKL-induced osteoclast differentiation.
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O88537
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FPRS3_MOUSE
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Formyl peptide receptor-related sequence 3
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MEANSSIPLNGSEVVFYDSTTSRVLWILSVIVLSITFVLGVLGNGLVIWVAGFRMAHTVTTICYLNLALGDFSFMVTLPLHIISMVMKGKWLFGWFLCKFVLSIVHINLFVSVFLITLIAMDRCTCVLHPVWVQNHRTVSLARKVIVGAWILSLLLTLPHFLFLTTVRDARGEVHCTCNFESVVANPEEQLKVSITVSTATGIISFIIGFSLPMSFIAVCYGLMAAKICRKGFLNSSRPLRVLTAVAISFFMCWFPFQLIILLGNIWNKETPSSIHILLNPASTLASFNSCLNPILYVFLGQEFREKLIYSLSASLERALREDSVLSSGKSSNFSSCPADSEL
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May have an olfactory function associated with the identification of pathogens or of pathogenic states.
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O88543
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CSN3_MOUSE
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COP9 signalosome complex subunit 3 (SGN3) (Signalosome subunit 3) (JAB1-containing signalosome subunit 3)
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MASALEQFVNSVRQLSAQGQMTQLCELINKSGELLAKNLSHLDTVLGALDVQEHSLGVLAVLFVKFSMPSVPDFETLFSQVQLFISTCNGEHIRYATDTFAGLCHQLTNALVERKQPLRGIGILKQAIDKMQMNTNQLTSVHADLCQLCLLAKCFKPALPYLDVDMMDICKENGAYDAKHFLCYYYYGGMIYTGLKNFERALYFYEQAITTPAMAVSHIMLESYKKYILVSLILLGKVQQLPKYTSQIVGRFIKPLSNAYHELAQVYSTNNPSELRNLVSKHSETFTRDNNMGLVKQCLSSLYKKNIQRLTKTFLTLSLQDMASRVQLSGPQEAEKYVLHMIEDGEIFASINQKDGMVSFHDNPEKYNNPAMLHNIDQEMLKCIELDERLKAMDQEITVNPQFVQKSMGSQEDDSGNKPSSYS
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Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes (By similarity). The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 (By similarity). The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases (By similarity). CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity). Essential to maintain the survival of epiblast cells and thus the development of the postimplantation embryo.
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O88551
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CLD1_MOUSE
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Claudin-1
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MANAGLQLLGFILASLGWIGSIVSTALPQWKIYSYAGDNIVTAQAIYEGLWMSCVSQSTGQIQCKVFDSLLNLNSTLQATRALMVIGILLGLIAIFVSTIGMKCMRCLEDDEVQKMWMAVIGGIIFLISGLATLVATAWYGNRIVQEFYDPLTPINARYEFGQALFTGWAAASLCLLGGVLLSCSCPRKTTSYPTPRPYPKPTPSSGKDYV
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Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions.
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O88552
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CLD2_MOUSE
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Claudin-2
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MASLGVQLVGYILGLLGLLGTSIAMLLPNWRTSSYVGASIVTAVGFSKGLWMECATHSTGITQCDIYSTLLGLPADIQAAQAMMVTSSAMSSLACIISVVGMRCTVFCQDSRAKDRVAVVGGVFFILGGILGFIPVAWNLHGILRDFYSPLVPDSMKFEIGEALYLGIISALFSLVAGVILCFSCSPQGNRTNYYDGYQAQPLATRSSPRSAQQPKAKSEFNSYSLTGYV
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Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
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