entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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O35312
|
GDF8_RAT
|
Growth/differentiation factor 8 (GDF-8) (Myostatin)
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MIQKPQMYVYIYLFVLIAAGPVDLNEDSEREANVEKEGLCNACAWRQNTRYSRIEAIKIQILSKLRLETAPNISKDAIRQLLPRAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQADGKPKCCFFKFSSKIQYNKVVKAQLWIYLRAVKTPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMSPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
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Acts specifically as a negative regulator of skeletal muscle growth.
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O35314
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SCG1_RAT
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Secretogranin-1 (Chromogranin-B) (CgB) (Glucagonoma peptide) (Secretogranin-I) (SgI) [Cleaved into: PE-11; CCB peptide short form; CCB peptide long form]
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MQRAMLLGLLGAAALAAVISAPVDNRDHNEEMVTRCIIEVLSNALSKSSAPTITPECRQVLRKSGKEVKGEEKGENENSKFEVRLLRDPSDASVGRWASSREETGAPVEDSPGQAKVDNEEWTGGGGHSREAVDDQESLHPSNQQVSKEAKIRHSEERGGKEEEEEEGKIYPKGEHRGDAGEEKKHTEESGEKHNAFSNKRSEASAKKKEESVARAEAHFVELEKTHSREQSSQESGEETRRQEKPQELPDQDQSEEESEEGEEGEEGATSEVTKRRPRHHHWRSQSNKPSYEGRRPLSEERKHAAGESKDANVATANLGEKRGHHLAHYRASEEEPDYGEELRSYPGFQAPQGLQYQGRGSEEVRAPSPRSEESQEKEYKRNHPDSELESTANRHSEETEEERSYEGAKGRQHRGRGREPGAYPALDSRQEKRLLDEGHDPVHESPVDTAKRYPQSKWQEQEKNYLNYDEEGDQGRWWQQEEQLEPEESREEVSFPDRQYAPYPTTEKRKRLGALFNPYFDPLQWKNSDFEKKGNPDDSFLDDDGEDGNGVTMTEKNFFPEYNYDWWEKRPFSEDVNWGYEKRSFARAPHLDLKRQYDDGVAELDQLLHYRKKAAEFPDFYDSEEQMGPHQEAEDEKDRADQRVLTEEEKKELENLAAMDLELQKIAEKFSQRG
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Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.
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O35316
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SC6A6_MOUSE
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Sodium- and chloride-dependent taurine transporter (Solute carrier family 6 member 6)
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MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEADGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEVIIGQYTSEGGITCWEKICPLFSGIGYASIVIVSLLNVYYIVILAWATYYLFHSFQKDLPWAHCNHSWNTPQCMEDTLRRNESHWVSLSTANFTSPVIEFWERNVLSLSSGIDNPGSLKWDLALCLLLVWLVCFFCIWKGVRSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGEGIKFYLYPDISRLGDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIADVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQITSLVDLYPSFLRKGYRREIFIAILCSISYLLGLTMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIAWIYGGDNLYDGIEDMIGYRPGPWMKYSWAVITPALCVGCFVFSLVKYVPLTYNKVYRYPDWAIGLGWGLALSSMLCIPLVIVILLCRTEGPLRVRIKYLITPREPNRWAVEREGATPFHSRVTLMNGALMKPSHVIVETMM
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Mediates sodium- and chloride-dependent transport of taurine. Can also mediate transport of hypotaurine, beta-alanine and gamma-aminobutyric acid (GABA).
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O35317
|
PBX3_MOUSE
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Pre-B-cell leukemia transcription factor 3 (Homeobox protein PBX3)
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MDDQSRMLQTLAGVNLAGHSVQGGMALPPPPHGHEGADGDGRKQDIGDILHQIMTITDQSLDEAQAKKHALNCHRMKPALFSVLCEIKEKTGLSIRGAQEEDPPDPQLMRLDNMLLAEGVSGPEKGGGSAAAAAAAAASGGSSDNSIEHSDYRAKLTQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVGIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFSKQATEILNEYFYSHLSNPYPSEEAKEELAKKCSITVSQVSNWFGNKRIRYKKNIGKFQEEANLYAAKTAVTAAHAVAAAVQNNQTNSPTTPNSGSSGSFNLPNSGDMFMNMQSLNGDSYQGSQVGANVQSQVDTLRHVINQTGGYSDGLGANSLYSPHNLNANGGWQDATTPSSVTSPTEGPGSVHSDTSN
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Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'.
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O35324
|
SH21B_MOUSE
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SH2 domain-containing protein 1B (EWS/FLI1-activated transcript 2) (EAT-2)
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MDLPYYHGCLTKRECEALLLKGGVDGNFLIRDSESVPGALCLCVSFKKLVYSYRIFREKHGYYRIETDAHTPRTIFPNLQELVSKYGKPGQGLVVHLSNPIMRNNLCQRGRRMELELNVYENTDEEYVDVLP
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Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as CD84, SLAMF1, LY9 and CD244. In SLAM signaling seems to cooperate with SH2D1A/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction through CD244/2B4. However, conflicting results are reported which may reflect the use of different strain backgrounds. Proposed to act as an inhibitor of CD244-mediated NK cell function including cytotoxicity and IFN-gamma production, the latter found also by triggering KLRA4 and KLRK1 next to CD244. Seems to positively regulate CD244- and CD84-dependent NK cell functions implicating CD244-mediated phosphorylation of VAV1. Activation of SLAMF7-mediated NK cell function does not effect receptor tyrosine phosphorylation but distal signaling. In the context of NK cell-mediated cytotoxicity does not enhance conjugate formation with target cells but stimulates polarization of the microtubule-organizing center and cytotoxic granules toward the NK cell synapse. Negatively regulates CD40-induced cytokine production in dendritic cells downstream of SLAM family receptors probably by inducing activation of the PI3K pathway to inhibit p38 MAPK and JNK activation.
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O35326
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SRSF5_MOUSE
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Serine/arginine-rich splicing factor 5 (Delayed-early protein HRS) (Pre-mRNA-splicing factor SRP40) (Splicing factor, arginine/serine-rich 5)
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MSGCRVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCSERVTIEHARARSRGGRGRGRYSDRFSSRRPRNDRRNAPPVRTENRLIVENLSSRVSWQDLKDFMRQAGEVTFADAHRPKLNEGVVEFASYGDLKNAIEKLSGKEINGRKIKLIEGSKRHRSRSRSRSRTRSSSRSRSRSRSRRSKSYSRSRSRSRSRSKSRSGSRSPVPEKSQKRGSSSRSKSPASVDRQRSRSRSRSRSVDSGN
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May be required for progression through G1 and entry into S phase of cell growth. May play a regulatory role in pre-mRNA splicing. Autoregulates its own expression. Plays a role in constitutive splicing and can modulate the selection of alternative splice sites (By similarity).
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O35331
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PDXK_RAT
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Pyridoxal kinase (EC 2.7.1.35) (Pyridoxine kinase)
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MEGECRVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLTSQELHALYEGLKANNVNKYDYVLTGYTRDKSFLGMVVDIVQELKQQNSRLVYVCDPVMGDKWNGEGSMYVPQDLLPVYREKVVPMADIITPNQFEAELLSGRKIHSQEEAFAVMDVLHRMGPDTVVITSSDLPSPKGSDYLMALGSQRMRKPDGSTVTQRIRMEMRKVDPVFVGTGDLFAAMLLAWTHKHPDNLKVACEKTVSAMQHVLQRTIRCAKAEAGEGQKPSPAQLELRMVQSRKDIEDPEIVVQATVL
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Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (By similarity). PLP is the active form of vitamin B6, and acts as a cofactor for over 140 different enzymatic reactions (By similarity).
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O35343
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IMA3_MOUSE
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Importin subunit alpha-3 (Importin alpha Q1) (Qip1) (Karyopherin subunit alpha-4)
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MADNEKLDNQRLKNFKNKGRDLETMRRQRNEVVVELRKNKRDEHLLKRRNVPQEDICEDSDIDGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVHCLERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWALGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETIQEILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKVQTAALRAVGNIVTGTDEQTQVVLNCDALSHFPALLTHPKEKINKEAVWFLSNITAGNQQQVQAVIDANLVPMIIHLLDKGDFGTQKEAAWAISNLTISGRKDQVAYLIQQNVIPPFCNLLTVKDAQVVQVVLDGLSNILKMAEDQAETIANLIEECGGLEKIEQLQNHENEDIYKLAYEIIDQFFSSDDIDEDPSLVPESVQGGTFGFNSSTNVPTEGFQF
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Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
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O35345
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IMA7_MOUSE
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Importin subunit alpha-7 (Importin alpha-S2) (Karyopherin subunit alpha-6)
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METMASPGKDNYRMKSYKNNALNPEEMRRRREEEGIQLRKQKREQQLFKRRNVELINEEAAMFDSLLMDSYVSSTTGESVITREMVEMLFSDDSDLQLATTQKFRKLLSKEPSPPIDEVINTPGVVDRFVEFLKRNENCTLQFEAAWALTNIASGTSQQTKIVIEAGAVPIFIELLNSDFEDVQEQAVWALGNIAGDSSLCRDYVLNCSILNPLLTLLTKSTRLTMTRNAVWALSNLCRGKNPPPEFAKVSPCLPVLSRLLFSSDSDLLADACWALSYLSDGPNEKIQAVIDSGVCRRLVELLMHNDYKVASPALRAVGNIVTGDDIQTQVILNCSALPCLLHLLSSSKESIRKEACWTISNITAGNRAQIQAVIDANIFPVLIEILQKAEFRTRKEAAWAITNATSGGTPEQIRYLVSLGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQESKRSGSGVNPYCGLIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGVEDDDSSLAPQVDETQQQFIFQQPEAPMEGFQL
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Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
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O35346
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FAK1_RAT
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Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)
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MAAAYLDPNLNHTPSSSTKTHLGTGTERSPGAMERVLKVFHYFESSNEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQDIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANNEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGVYLSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKVQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQISGYPGSHGIPAMAGSIYPGQASLLDQTELWNHRPQEMSMWQPSVEDSAALDLRGMGQVLPPHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSFQGPTGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLSNLSSISSPAESYNEGVKPWRLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPILPASTHREIEMAQKLLNSDLGELISKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH
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Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (By similarity). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1 most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1 GIT2 and SHC1 this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1.
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O35348
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COLQ_MOUSE
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Acetylcholinesterase collagenic tail peptide (AChE Q subunit) (Acetylcholinesterase-associated collagen)
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MVVLNPMTLGIYLQLFFCSIVSQPTFINSVVPISAALPGLDQKKRGSHKACCLLMPPPPPLFPPPFFRGSRSPLLSPDMKNLLELEASPSPCIQGSLGSPGPPGPQGPPGLPGKTGPKGEKGDLGRPGRKGRPGPPGVPGMPGPVGWPGPEGPRGEKGDLGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESGLAGHRGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPPSAGQLVMGLKGERGFPGPPGRCLCGPPVNVNNPSYGDSMYGRGSPRVPAIFVVNNQEELERLNTQNAIAFRRDQRSLYFKDSLGWLPIQLTPFYPVGYTVKQPGTCGDGVLQPGEECDDGNPDVSDGCIDCHRAYCGDGYRHQGVEDCDGSDFGYLTCETYLPGSYGDLRCTQYCSIDSTPCRYFT
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Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.
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O35350
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CAN1_MOUSE
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Calpain-1 catalytic subunit (EC 3.4.22.52) (Calcium-activated neutral proteinase 1) (CANP 1) (Calpain mu-type) (Calpain-1 large subunit) (Micromolar-calpain) (muCANP)
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MTEELITPVYCTGVSAQVQKKRDKELGLGRHENAIKYLGQDYETLRARCLQSGVLFQDEAFPPVSHSLGFKELGPHSSKTYGIKWKRPTELMSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNETILHRVVPYGQSFQDGYAGIFHFQLWQFGEWVDVVIDDLLPTKDGKLVFVHSAQGNEFWSALLEKAYAKVNGSYEALSGGCTSEAFEDFTGGVTEWYDLQKAPSDLYQIILKALERGSLLGCSINISDIRDLEAITFKNLVRGHAYSVTGAKQVTYQGQRVNLIRMRNPWGEVEWKGPWSDSSYEWNKVDPYEREQLRVKMEDGEFWMSFRDFIREFTKLEICNLTPDALKSRTLRNWNTTFYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLEEVDDADDYDNRESGCSFLLALMQKHRRRERRFGRDMETIGFAVYQVPRELAGQPVHLKRDFFLANASRAQSEHFINLREVSNRIRLPPGEYIVVPSTFEPNKEGDFLLRFFSEKKAGTQELDDQIQANLPDEKVLSEEEIDDNFKTLFSKLAGDDMEISVKELQTILNRIISKHKDLRTNGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLTIFRKFDLDKSGSMSAYEMRMAIEAAGFKLNKKLHELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKLLDTDLDGVVTFDLFKWLQLTMFA
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Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-388' and 'His-410'. Cleaves and activates caspase-7 (CASP7).
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O35375
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NRP2_MOUSE
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Neuropilin-2 (Vascular endothelial cell growth factor 165 receptor 2)
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MDMFPLTWVFLALYFSGHEVRSQQDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWIVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSVLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPRMEIILQFLTFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSKLRSSTGILSLTFHTDMAVAKDGFSARYYLIHQEPPENFQCNVPLGMESGRIANEQISASSTFSDGRWTPQQSRLHGDDNGWTPNLDSNKEYLQVDLRFLTMLTAIATQGAISRETQKGYYVKSYKLEVSTNGEDWMVYRHGKNHKIFQANNDATEVVLNKLHMPLLTRFIRIRPQTWHLGIALRLELFGCRVTDAPCSNMLGMLSGLIADTQISASSTREYLWSPSAARLVSSRSGWFPRNPQAQPGEEWLQVDLGTPKTVKGVIIQGARGGDSITAVEARAFVRKFKVSYSLNGKDWEYIQDPRTQQTKLFEGNMHYDTPDIRRFDPVPAQYVRVYPERWSPAGIGMRLEVLGCDWTDSKPTVETLGPTVKSEETTTPYPMDEDATECGENCSFEDDKDLQLPSGFNCNFDFPEETCGWVYDHAKWLRSTWISSANPNDRTFPDDKNFLKLQSDGRREGQYGRLISPPVHLPRSPVCMEFQYQAMGGHGVALQVVREASQESKLLWVIREDQGSEWKHGRIILPSYDMEYQIVFEGVIGKGRSGEISIDDIRISTDVPLENCMEPISAFAGEDFKVDIPETHGGEGYEDEIDDEYEGDWSNSSSSTSGAGDPSSGKEKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKVKINHQKCCSEA
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High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.
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O35379
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MRP1_MOUSE
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Multidrug resistance-associated protein 1 (EC 7.6.2.2) (ATP-binding cassette sub-family C member 1) (Glutathione-S-conjugate-translocating ATPase ABCC1) (EC 7.6.2.3) (Leukotriene C(4) transporter) (LTC4 transporter)
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MALRSFCSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLTWVPCFYLWSCFPLYFFYLSRHDRGYIQMTHLNKTKTALGFFLWIICWADLFYSFWERSQGVLRAPVLLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALLCALAILRSKIISALKKDAHVDVFRDSTFYLYFTLVLVQLVLSCFSDCSPLFSETVHDRNPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNKEDTSEEVVPVLVNNWKKECDKSRKQPVRIVYAPPKDPSKPKGSSQLDVNEEVEALIVKSPHKDREPSLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRSIKSGEGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYANAEQDLASEDDSVSGSGKESKPVENGMLVTDTVGKHLQRHLSNSSSHSGDTSQQHSSIAELQKAGAKEETWKLMEADKAQTGQVQLSVYWNYMKAIGLFITFLSIFLFLCNHVSALASNYWLSLWTDDPPVVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSTWPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMAKDAGLV
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Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs by decreasing accumulation of drug in cells, and by mediating ATP- and GSH-dependent drug export. Hydrolyzes ATP with low efficiency. Catalyzes the export of sphingosine 1-phosphate from mast cells independently of their degranulation (By similarity). Participates in inflammatory response by allowing export of leukotriene C4 from leukotriene C4-synthezing cells. Mediates ATP-dependent, GSH-independent cyclic GMP-AMP (cGAMP) export. Thus, by limiting intracellular cGAMP concentrations negatively regulates the cGAS-STING pathway.
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O35381
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AN32A_MOUSE
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Acidic leucine-rich nuclear phosphoprotein 32 family member A (Acidic nuclear phosphoprotein pp32) (Leucine-rich acidic nuclear protein) (LANP) (Potent heat-stable protein phosphatase 2A inhibitor I1PP2A)
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MEMDKRIYLELRNRTPSDVKELVLDNCKSIEGKIEGLTDEFEELEFLSTINVGLTSISNLPKLNKLKKLELSENRISGDLEVLAEKCPNLKHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNAYRENVFKLLPQVMYLDGYDRDNKEAPDSDVEGYVEDDDEEDEDEEEYDEYAQLVEDEEEEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEEAGEEEGSQKRKREPDDEGEEDD
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Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription. Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation. In addition, plays a role in the modulation of histone acetylation and transcription as part of the INHAT (inhibitor of histone acetyltransferases) complex. Inhibits the histone-acetyltranferase activity of EP300/CREBBP (CREB-binding protein) and EP300/CREBBP-associated factor by histone masking. Preferentially binds to unmodified histone H3 and sterically inhibiting its acetylation and phosphorylation leading to cell growth inhibition. Participates in other biochemical processes such as regulation of mRNA nuclear-to-cytoplasmic translocation and stability by its association with ELAVL1 (Hu-antigen R). Plays a role in E4F1-mediated transcriptional repression as well as inhibition of protein phosphatase 2A (By similarity).
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O35382
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EXOC4_MOUSE
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Exocyst complex component 4 (Exocyst complex component Sec8)
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MAAEAAGGKYRSTVSKSKDPSGLLISVIRTLSTSDDVEDRENEKGRLEEAYEKCDRDLDELIVQHYTELTTAIRTYQSITERITNSRNKIKQVKENLLSCKMLLHCKRDELRKLWIEGIEHKHVLNLLDEIENIKQVPQKLEQCMASKHYLSATDMLVSAVESLEGPLLQVEGLSDLRLELHSKKMNLHLVLIEELHRHLYIKSTSRVVQRNKEKGKMSSHGKDPSPGPLIDVSNIPTPRKFLDASQYSAAGGSSVREMNLQDVKEDLECDPEENSTLFMGILIQGLARLKKIPETVKAIKERLEQELKQIVKRSTTQVADSAYQRGESLTVDNQPRLLLELLELLFDKFNAVATAHSVVLGYLQDSVGTQLTQQEEIKLYDMADVWVKIQDVLQMLLTEYLDMKNTRTASEPSAQLSYASTGREFAAFFAKKKPQRPKNSLFKFESSSHAISMSAYLREQRRELYSRSGELQGGPDDNLIEGGGTKFVCKPGARNITVIFHPLLRFIQEIEHALGLGPAKQCPLREFLTVYIKSIFLNQVLAEINKEIEGVTKTSDPLKILANADTMKVLGVQRPLLQSTIIVEKTVQDLMNLMHDLSAYSDQFLNMVCVKLQEYKDTCSTAYRGIVQSEEKLVISASWAKDDDISRLLKSLPNWTNMAQPKQLRPKREEEEDFIRAAFGKESEVLIGNLGDKLIPPQDILRDVSDLKALANMHESLEWLAGRTKSAFSNLSTSQMLSPAQESHVNMDLPPVSEQIMQTLSELAKTFQDMADRCLLVLHLEVRVHCFHYLIPLAKEGNYAIVANVESMDYDPLVVKLNKDISAMEEAMSASLQQHKFQYIFEGLGHLISCILINGAQYFRRISESGIKKMCRNIFVLQQNLTNITMSREADLDFARQYYEMLYNTADELLNLVVDQGVKYTELEYIHALTLLHRSQTGVGDQTTQNTRLQRLKEIICEQAAIKQATKDKKITTV
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Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
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O35385
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PPE2_MOUSE
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Serine/threonine-protein phosphatase with EF-hands 2 (PPEF-2) (EC 3.1.3.16)
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MGSSSSTQHHFAFQNAEKAFKAAALIQRWYRRYMARLEMRRRCTWNIFQSIEYAGQQDQVKLHEFFSYLVDHFTPSSHHERDFLNRMFTEERFAQDVETEEGGDFESIEVPDSYTGPRLSFPLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDKTDLELLAKLDRHKIVSTMRCKTRKESENREEQKRKDNQTSSGQKPTPWFLPQSRSLPSSPFHLGSGFKAYKAGRSCSIPCGSPNSKELSRRGQVRRSVDLELEQCRQQAGFLGIREKGESLPLAPDADCVADGGGVLEPTPEEWKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIVQYQANKATHRLTMRQRISRVEESALRALRQKLFAHSSDLLVEFRKRDPDESGVITLSDWATAVESVLHLGLPWRMLRPQLVNSSADNVLEYRSWLDSLAKEQLSRENIQSSLLEKLYRNRSNLETIFRIIDSDHSGFISLDEFRQTWKLFSSHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAFRLVEQSCLEGHASACLQSTDTAESGHSSPGPC
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May play a role in phototransduction. May dephosphorylate photoactivated rhodopsin. May function as a calcium sensing regulator of ionic currents, energy production or synaptic transmission.
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O35386
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PAHX_MOUSE
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Phytanoyl-CoA dioxygenase, peroxisomal (EC 1.14.11.18) (Lupus nephritis-associated peptide 1) (Phytanic acid oxidase) (Phytanoyl-CoA alpha-hydroxylase) (PhyH)
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MNLTRAGARLQVLLGHLGRPSAPTIVAQPVSGLASPASFQPEQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVSDDDIQRFRAEFERICREEVKPPGIVIMRDVALAKQDYMPSDRMVSKIQDFQEDEELFRYCLLPEILKYVECFTGPNIMALHGMLINKPPDVGKKTSRHPLHQDLHYFPFRPSNLIVCAWTAMEHIDRNNGCLVVLPGTHKGTLKPHDYPKWEGGVNKMYHGIQDYDPNSPRVHLVMEKGDTVFFHPLLIHGSGRNKTQGFRKAISCHFGSSDCQCIDVSGTSQENIAREVVEMAEKKYGFQGVMDFKDTWIFRSRLVKGERINI
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Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (By similarity). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl-and 4-methyl-branched acyl-CoAs (By similarity).
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O35387
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HAX1_MOUSE
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HCLS1-associated protein X-1 (HS1-associating protein X-1) (HAX-1) (HS1-binding protein 1) (HSP1BP-1)
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MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDDDDDDEAEEDRGAWGRESYAFDGSQPPEEFGFSFSPRGGMRFHGNFGFDDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESPKPAPDWGSQGPFHRLDDTWPVSPHSRAKEDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEERRTVVDSEGRRETTVTHQEAHDSSRSDPDSQRSSALDDPFSILDLLLGRWFRSR
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Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools.
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O35393
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EFNB3_MOUSE
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Ephrin-B3
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MGAPHFGPGGVQVGALLLLGFAGLVSGLSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSAEPGRDTIPGDPSSNATSRGAEGPLPPPSMPAVAGAAGGMALLLLGVAGAGGAMCWRRRRAKPSESRHPGPGSFGRGGSLGLGGGGGMGPREAEPGELGIALRGGGTADPPFCPHYEKVSGDYGHPVYIVQDGPPQSPPNIYYKV
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Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons.
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O35394
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PRAF1_RAT
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Prenylated Rab acceptor protein 1 (PRA1 family protein 1)
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MAAQKDQQKDAEVEGLSATTLLPKLIPSGAGREWLERRRATIRPWGTFVDQQRFSRPRNVGELCQRLVRNVEYYQSNYVFVFLGLILYCVVTSPMLLVALAVFFGACYILYLRTLQSKLVLFGREVSPAHQYALAGGVSFPFFWLAGAGSAVFWVLGATLVLIGSHAAFHQIEPADGEELQMEPV
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General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI1.
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O35397
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CASP6_RAT
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Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
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MTETDGFYRSREVLDPAEQYKMDHKRRGTALIFNHERFFWHLALPERRGTNADRDNPTRRFSELGFEVKCFNDLRAEELLLKIHEVSTSSHVDADCFLCVFLSHGEGNHIYAYDAKIEIQTLTGLFKGDKCQSLVGKPKIFIIQACRGSQHDVPLVPLDVVDHQTDKLDDNVTQVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLSEMLARHGSSLEFTELLTLVNRKVSQRRVDFCKDPGAIGKKQVPCFASMLTKKLHFCPKPSK
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Cysteine protease that plays essential roles in programmed cell death, axonal degeneration, development and innate immunity (By similarity). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein NUMA1 and lamin A/LMNA thereby inducing nuclear shrinkage and fragmentation. Lamin-A/LMNA cleavage is required for chromatin condensation and nuclear disassembly during apoptotic execution (By similarity). Acts as a regulator of liver damage by promoting hepatocyte apoptosis: in absence of phosphorylation by AMP-activated protein kinase (AMPK), catalyzes cleavage of BID, leading to cytochrome c release, thereby participating in nonalcoholic steatohepatitis. Cleaves PARK7/DJ-1 in cells undergoing apoptosis (By similarity). Involved in intrinsic apoptosis by mediating cleavage of RIPK1. Furthermore, cleaves many transcription factors such as NF-kappa-B and cAMP response element-binding protein/CREBBP (By similarity). Cleaves phospholipid scramblase proteins XKR4 and XKR9. In addition to apoptosis, involved in different forms of programmed cell death. Plays an essential role in defense against viruses by acting as a central mediator of the ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis), independently of its cysteine protease activity. PANoptosis is a unique inflammatory programmed cell death, which provides a molecular scaffold that allows the interactions and activation of machinery required for inflammasome/pyroptosis, apoptosis and necroptosis. Mechanistically, interacts with RIPK3 and enhances the interaction between RIPK3 and ZBP1, leading to ZBP1-mediated inflammasome activation and cell death. Plays an essential role in axon degeneration during axon pruning which is the remodeling of axons during neurogenesis but not apoptosis. Regulates B-cell programs both during early development and after antigen stimulation (By similarity).
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O35400
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ST2B1_MOUSE
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Sulfotransferase 2B1 (EC 2.8.2.2) (Alcohol sulfotransferase) (Hydroxysteroid sulfotransferase 2) (Sulfotransferase family cytosolic 2B member 1) (ST2B1)
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MDGPQPRALWSSSEKNVSEMSWNFGGEYFRYKGIPFPVGMYSPESLSLAENTSNVRDDDIFIVTYPKSGTNWMIEIVCLILKDGDPSWIRSEPIWQRAPWCETIISAFNVLDRPSPRIMSSHLPIELFTKAFFSSKAKVIYVGRNPRDVVVSLYYYSKIAGQLKDPGTPDQFLQNFLKGEVQFGSWFDHIKGWIRMQNQENFLFITYEELQQDLRGSVQRICEFLGRPLGEEALSSVVAHSAFAAMKANTMSNYSLLPASLLDHRQGEFLRKGISGDWKNHFTVAQSEAFDSVYREQMHGVQRFPWDTSEEDSSPDGQPDPEPSPSPASDDPNPGSSQ
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Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Preferentially sulfonates cholesterol. Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA). Cholesterol sulfation is approximately 10-fold higher than for pregnenolone and 20-fold higher than for DHEA. Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation (By similarity). [Isoform 2]: Strongly sulfonates pregnenolone, however is capable to sulfonate cholesterol with a high degree of efficiency. DHEA is a relatively poor substrate.
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O35405
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PLD3_MOUSE
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5'-3' exonuclease PLD3 (EC 3.1.16.1) (Choline phosphatase 3) (Phosphatidylcholine-hydrolyzing phospholipase D3) (Phospholipase D3) (PLD 3) (Schwannoma-associated protein 9) (SAM-9)
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MKPKLMYQELKVPVEEPAGELPLNEIEAWKAAEKKARWVLLVLILAVVGFGALMTQLFLWEYGDLHLFGPNQRPAPCYDPCEAVLVESIPEGLEFPNATTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTQEPSAQQGEEVLQQLQALAPRGVKVRIAVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARDLTKIFEAYWFLGQAGSSIPSTWPRSFDTRYNQETPMEICLNGTPALAYLASAPPPLCPSGRTPDLKALLNVVDSARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHSDPSMRSFLLSLAALHDNHTHSDIQVKLFVVPTDESQARIPYARVNHNKYMVTERASYIGTSNWSGSYFTETAGTSLLVTQNGHGGLRSQLEAVFLRDWESPYSHDLDTSANSVGNACRLL
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5'->3' DNA exonuclease which digests single-stranded DNA (ssDNA). Regulates inflammatory cytokine responses via the degradation of nucleic acids, by reducing the concentration of ssDNA able to stimulate TLR9, a nucleotide-sensing receptor in collaboration with PLD4. May be important in myotube formation. Plays a role in lysosomal homeostasis. Involved in the regulation of endosomal protein sorting (By similarity).
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O35409
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FOLH1_MOUSE
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Glutamate carboxypeptidase 2 (EC 3.4.17.21) (Folate hydrolase 1) (Folylpoly-gamma-glutamate carboxypeptidase) (FGCP) (Glutamate carboxypeptidase II) (GCPII) (Membrane glutamate carboxypeptidase) (mGCP) (N-acetylated-alpha-linked acidic dipeptidase I) (NAALADase I) (Prostate-specific membrane antigen homolog) (Pteroylpoly-gamma-glutamate carboxypeptidase)
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MWNALQDRDSAEVLGHRQRWLRVGTLVLALTGTFLIGFLFGWFIKPSNEATGNVSHSGMKKEFLHELKAENIKKFLYNFTRTPHLAGTQNNFELAKQIHDQWKEFGLDLVELSHYDVLLSYPNKTHPNYISIINEDGNEIFKTSLSEQPPPGYENISDVVPPYSAFSPQGTPEGDLVYVNYARTEDFFKLEREMKISCSGKIVIARYGKVFRGNMVKNAQLAGAKGMILYSDPADYFVPAVKSYPDGWNLPGGGVQRGNVLNLNGAGDPLTPGYPANEHAYRHELTNAVGLPSIPVHPIGYDDAQKLLEHMGGPAPPDSSWKGGLKVPYNVGPGFAGNFSTQKVKMHIHSYTKVTRIYNVIGTLKGALEPDRYVILGGHRDAWVFGGIDPQSGAAVVHEIVRSFGTLKKKGRRPRRTILFASWDAEEFGLLGSTEWAEEHSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELQSPDEGFEGKSLYDSWKEKSPSPEFIGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWKTNKVSSYPLYHSVYETYELVVKFYDPTFKYHLTVAQVRGAMVFELANSIVLPFDCQSYAVALKKYADTIYNISMKHPQEMKAYMISFDSLFSAVNNFTDVASKFNQRLQELDKSNPILLRIMNDQLMYLERAFIDPLGLPGRPFYRHIIYAPSSHNKYAGESFPGIYDALFDISSKVNASKAWNEVKRQISIATFTVQAAAETLREVA
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Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides (By similarity). In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.
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O35412
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SI1L1_RAT
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Signal-induced proliferation-associated 1-like protein 1 (SIPA1-like protein 1) (SPA-1-like protein p1294) (Spine-associated Rap GTPase-activating protein) (SPAR)
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MTSLKRSQTERPVTADRASVVSTDGTPKVHTDDFYMRRFRSQNGSLGSSVMAAVGPPRSEGPHHITSTPGVPKMGVRARIADWPPRKENVKESSRSSQEIETSSCLESLSSKGSPVSQGSSVSLNSNDSAMLKSIQNTLKNKTGPAESMDSRFLMPEAYPSSPRKALRRIRQRSNSDITISELDVDSFDECISPTYKSGPSLHREYGSTSSIDKQGTSGESFFGLLKGYKDDRADRGPTPTKLSDFLITGGGKGSGFSLDVIDGPISQRENLRLFKEREKPLKRRSKSETGDSSIFRKLRNAKGEELGKSSDLEDNRSEDSVRPWTCPKCFAHYDVQSILFDLNEAIMNRHNVIKRRNTTTGASAAAVASLVSGPLSHSTSFSSPMGSTEDFNSKGSLGMDQGDDKSNELVMSCPYFRNEIGGEGERKISLSKSNSGSFSGCESTSFESALSSHCTNAGVAVLEVPKESLMLHLDRVRRYTVEHVDLGAYYYRKCFYQKEHWNYFGADENLGPVAVSIRREKPEDMKENGSPYNYRIIFRTSELMTLRGSVLEDAIPSTAKHSTARGLPLKEVLEHVIPELNVQCLRLAFNTPKVTEQLMKLDEQGLNYQQKVGIMYCKAGQSTEEEMYNTPKVTEQFMKLDEQGLNYQQKVGIMYCKAGQSTEEEMYNNESAGPAFEEFLQLLGERVRLKGFEKYRAQLDTKTDSTGTHSLYTTYKDYEIMFHVSTMLPYTPNNKQQLLRKRHIGNDIVTIVFQEPGAQPFSPKNIRSHFQHVFVIVRAHNPCTESVCYSVAVTRSRDVPSFGPPIPKGVTFPKSNVFRDFLLAKVINAENAAHKSEKFRAMATRTRQEYLKDLAEKNVTNTPIDPSGKFPFISLASKKKEKSKPYPGAELSSMGAIVWAVRAKDYNKAMEFDCLLGISNEFIVLIEQETKSVVFNCSCRDVIGWTSSDSSLKIFYERGECISVESFMSSEDIKEIVKRLQFVSKGCESVEMTLRRNGLGQLGFHVNYEGIVADVEPYGYAWQAGLKQGSRLVEICKVAVATLSHEQMIDLLRTSVTVKVVIIPPHDDCTPRRSCSETYRMPVMEYKMNEGVSYEYKFPFRSNNKWQRNAGKGAHSPQVPLQLQSPMISRVNAGKGDGKMPLPERAANIPRSISSDGRPLERRLSPGSDIYVTVSSMALARSQCRNSPSNLSSSSETGSGGGTYRQKSMPEGFGVSRRSPASIDRQNTQSDIGGSGKSTPSWQRSEDSLADQMEPTCHLPAVSKVLPAFRESPSGRLMRQDPVVHLSPNKQGHSDSHYSSHSSSNTLSSNASSAHSDEKWYDGDRTESDLNSYNYLQGTSADSGIDTASYGLSHGSTASLGASTSSPRSGPGKEKVAPLWHSSSEVLSLADRTLETEGHGMDRKTESSLSLDIHSKSQGGSSPLTRENSTFSINDATSHTSTMSSRHSASPVVFSSARSSPKEELHPTTSSQLAPSFSSSSSSSSGPRTFYPRQGATSKYLIGWKKPEGTINSVGFMDTRKRHQSDGNEIAHTRLRASTRDLRASPKPTSKSTIEEDLKKLIDLESPTPESQKNFKFHGLSSPQSPFPSTPTSRRALHRTLSDESIYSSQREHFFTSRASLLDQALPNDVFFSSTYPSLPKSLPLRRPSYTLGMKSLHGEFFASDSSLTDIQETRRQPIPDPGLMPLPDTASDLDWSNLVDAAKAYEVQRASFFAASDENHRPLSAASNSDQLEEQALVQMKSYSSSKDSSPTLASKVDQLEGMLKMLREDLKKEKEDKAHLQAEVEHLREDNLRLQEESQNASDKLKKFTEWVFNTIDMS
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Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis.
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O35413
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SRBS2_RAT
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Sorbin and SH3 domain-containing protein 2 (Arg-binding protein 2) (ArgBP2) (Arg/Abl-interacting protein 2) (Neural ArgBP2) (nArgBP2) (Sorbin)
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MNTDSGGCARKRAAMSVTLTSVKRVQSSPNLLAAGRESHSPDSAWRSYNGRNPETLNGDATYSSLAAKGFRSVRPNLQDKKSPTQSHITINGNSGGAVSPVSYYQRPFSPSAYSLPASLNSSIIMPHGRSLDSAETYSQHAQSLDGTMGSSIPLYRSSEEEKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDEDTDMYNTPYTYNAGLYNSPYSAQSHPAAKTQTYRPLSKSHSDNGTDAFKEATSPVPPPHVPPRPRDQSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQHERPVSVYQSSIDRSLERPSSSASMAGDFRKRRKSEPAVGPPRGLGDHSSSRTSPGRADLPGSSSTFTTSFISSSPSSPSRAQGGDDSKMCPPLCSYSGLNGSPSSELECCGAYRRHLDVPQDSQRAITFKNGWQMARQNAEIWSSTEEAVSPKIKSRSCDDLLNDDCGSFPDPKTKSESMGSLLCDEGSKESDPMTWTSPYIPEVCGNSRSRLKHRSAHNAPGFLKMYKKMHRINRKDLMNSEVICSVKSRILQYEKEQQHRGLLHGWSQSSTEEVPRDVVPTRISEFEKLIQKSKSMPNLGDEMLSPVTLEPPQNGLCPKRRFSIESLLEEETQVRHPSQGQRSCKSNTLVPIHIEVTSDEQPRTHMEFSDSDQDGVVSDHSDNVHVERSSFCSESDFDHFSFTSSESFYGSSHHHHHHHHHHGHFISSCKGRCPASYTRFTTMLKHERAKHENIDRPRRQDMDPGLSKLAFLVSPVPFRRKKVLTPQKQTEQAKCKASVVEALDSALKDICDQIKAEKRRGSLPDNSILHRLISELLPQIPKRNSSLNALKRSPMHQPFHPLPQDGAIHCPLYQNDCGRMPHSASFPDVDTTSSYHAQDYGSVLSLQDHESPRSYSSTLTDLGRSVSRERRGTPEKEVKLPAKAVYDFKAQTSKELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKLTPPEKAQPARPPPPVQPGEIGEAIAKYNFNADTNVELSLRKGDRIILLKRVDQNWYEGKIPGTNRQGIFPVSYVEVVKRNTKGSEDYPDPPLPHSYSSDRIYSLSSNKPQRPVFSHENIQGGGEPFQALYNYTPRNEDELELRESDVVDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
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Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 (By similarity). May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (By similarity). Isoform 2 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000250, ECO:0000250|UniProtKB:O94875, ECO:0000269|PubMed:10521485}.
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O35417
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PDYN_MOUSE
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Proenkephalin-B (Beta-neoendorphin-dynorphin) (Preprodynorphin) [Cleaved into: Alpha-neoendorphin; Beta-neoendorphin; Big dynorphin (Big Dyn); Dynorphin A(1-17) (Dyn-A17) (Dynorphin A); Dynorphin A(1-13); Dynorphin A(1-8); Leu-enkephalin; Rimorphin (Dynorphin B) (Dyn-B) (Dynorphin B(1-13)); Leumorphin (Dynorphin B-29)]
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MAWSRLMLAACLLVMPSNVMADCLSLCSLCAVRIQDGPRPINPLICSLECQDLVPPSEEWETCRGFSSFLTLTVSGLRGKDDLEDEVALEEGISAHAKLLEPVLKELEKSRLLTSVPEEKFRGLSSSFGNGKESELAGADRMNDEAAQGRTVHFNEEDLRKQAKRYGGFLRKYPKRSSEMARDEDGGQDGDQVGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQENPNTYSEDLDV
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Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opioid activity, it is 700 times more potent than Leu-enkephalin (By similarity). Leumorphin has a typical opioid activity and may have anti-apoptotic effect.
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O35423
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AGT1_MOUSE
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Alanine--glyoxylate aminotransferase (AGT) (EC 2.6.1.44) (Serine--pyruvate aminotransferase, mitochondrial) (SPT) (EC 2.6.1.51)
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MFRMLAKASVTLGSRAAGWVRTMGSYQLLVPPPEALSKPLSVPTRLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGDSFLTGTNGIWGMRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKYKVYSRKTKPVSFYTDITYLAKLWGCEGETRVIHHTTPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKDPEIRLPTITTVTVPAGYNWRDIVSYVLDHFSIEISGGLGPTEERVLRIGLLGYNATTENVDRVAEALREALQHCPKNKL
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[Isoform Peroxisomal]: Catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification.
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O35425
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BOK_MOUSE
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Bcl-2-related ovarian killer protein (Apoptosis activator Mtd) (Protein matador)
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MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQIRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKTLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER
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Apoptosis regulator that functions through different apoptotic signaling pathways. Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner. In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response. Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD-proteasome degradation system, resulting in cytochrome c release. In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner. Plays a role in granulosa cell apoptosis by CASP3 activation (By similarity). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation. In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression.May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (By similarity).
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O35426
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XBP1_MOUSE
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X-box-binding protein 1 (XBP-1) (Tax-responsive element-binding protein 5) (TREB-5) [Cleaved into: X-box-binding protein 1, cytoplasmic form; X-box-binding protein 1, luminal form]
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MVVVAAAPSAATAAPKVLLLSGQPASGGRALPLMVPGPRAAGSEASGTPQARKRQRLTHLSPEEKALRRKLKNRVAAQTARDRKKARMSELEQQVVDLEEENHKLQLENQLLREKTHGLVVENQELRTRLGMDTLDPDEVPEVEAKGSGVRLVAGSAESAALRLCAPLQQVQAQLSPPQNIFPWTLTLLPLQILSLISFWAFWTSWTLSCFSNVLPQSLLVWRNSQRSTQKDLVPYQPPFLCQWGPHQPSWKPLMNSFVLTMYTPSL
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Functions as a transcription factor during endoplasmic reticulum stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development and the development of secretory tissues such as exocrine pancreas and salivary gland. Involved in differentiation of B lymphocytes to plasma cells and production of immunoglobulins. Modulates the cellular response to ER stress in a PIK3R-dependent manner. Binds to the cis-acting X box present in the promoter regions of major histocompatibility complex class II genes (By similarity). Involved in VEGF-induced endothelial cell (EC) proliferation and retinal blood vessel formation during embryonic development but also for angiogenesis in adult tissues under ischemic conditions. Functions also as a major regulator of the UPR in obesity-induced insulin resistance and type 2 diabetes for the management of obesity and diabetes prevention. [Isoform 1]: Plays a role in the unconventional cytoplasmic splicing processing of its own mRNA triggered by the endoplasmic reticulum (ER) transmembrane endoribonuclease ERN1: upon ER stress, the emerging XBP1 polypeptide chain, as part of a mRNA-ribosome-nascent chain (R-RNC) complex, cotranslationally recruits its own unprocessed mRNA through transient docking to the ER membrane and translational pausing, therefore facilitating efficient IRE1-mediated XBP1 mRNA isoform 2 production. In endothelial cells (EC), associated with KDR, promotes IRE1-mediated XBP1 mRNA isoform 2 production in a vascular endothelial growth factor (VEGF)-dependent manner, leading to EC proliferation and angiogenesis (By similarity). Functions as a negative feed-back regulator of the potent transcription factor XBP1 isoform 2 protein levels through proteasome-mediated degradation, thus preventing the constitutive activation of the ER stress response signaling pathway. Inhibits the transactivation activity of XBP1 isoform 2 in myeloma cells. Acts as a weak transcriptional factor. Together with HDAC3, contributes to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to EC survival under disturbed flow/oxidative stress. Binds to the ER stress response element (ERSE) upon ER stress. Binds to the consensus 5'-GATGACGTG[TG]N(3)[AT]T-3' sequence related to cAMP responsive element (CRE)-like sequences. Binds the Tax-responsive element (TRE) present in the long terminal repeat (LTR) of T-cell leukemia virus type 1 (HTLV-I) and to the TPA response elements (TRE). Associates preferentially to the HDAC3 gene promoter region in a static flow-dependent manner. Binds to the CDH5/VE-cadherin gene promoter region (By similarity). [Isoform 2]: Functions as a stress-inducible potent transcriptional activator during endoplasmic reticulum (ER) stress by inducing unfolded protein response (UPR) target genes via binding to the UPR element (UPRE). Up-regulates target genes encoding ER chaperones and ER-associated degradation (ERAD) components to enhance the capacity of productive folding and degradation mechanism, respectively, in order to maintain the homeostasis of the ER under ER stress. Plays a role in the production of immunoglobulins and interleukin-6 in the presence of stimuli required for plasma cell differentiation, and promotes as well membrane phospholipid biosynthesis necessary for ER expansion. Contributes to the VEGF-induced endothelial cell (EC) growth and proliferation in a Akt/GSK-dependent and/or -independent signaling pathway, respectively, leading to beta-catenin nuclear translocation and E2F2 gene expression. Promotes umbilical vein EC apoptosis and atherosclerotisis development in a caspase-dependent signaling pathway, and contributes to VEGF-induced EC proliferation and angiogenesis in adult tissues under ischemic conditions. Involved in the regulation of endostatin-induced autophagy in EC through BECN1 transcriptional activation. Plays a role as an oncogene by promoting tumor progression: stimulates zinc finger protein SNAI1 transcription to induce epithelial-to-mesenchymal (EMT) transition, cell migration and invasion of breast cancer cells (By similarity). Involved in adipocyte differentiation by regulating lipogenic gene expression during lactation. Plays a role in the survival of both dopaminergic neurons of the substantia nigra pars compacta (SNpc), by maintaining protein homeostasis and of myeloma cells. Increases insulin sensitivity in the liver as a response to a high carbohydrate diet, resulting in improved glucose tolerance. Improves also glucose homeostasis in an ER stress- and/or insulin-independent manner through both binding and proteasome-induced degradation of the transcription factor FOXO1, hence resulting in suppression of gluconeogenic genes expression and in a reduction of blood glucose levels. Controls the induction of de novo fatty acid synthesis in hepatocytes by regulating the expression of a subset of lipogenic genes in an ER stress- and UPR-independent manner. Binds to the 5'-CCACG-3' motif in the PPARG promoter. Associates preferentially to the HDAC3 gene promoter region in a disturbed flow-dependent manner. Binds to the BECN1 gene promoter region. Binds to the CDH5/VE-cadherin gene promoter region. Binds to the ER stress response element (ERSE) upon ER stress (By similarity).
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O35427
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RPC9_MOUSE
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DNA-directed RNA polymerase III subunit RPC9 (RNA polymerase III subunit C9) (Calcitonin gene-related peptide-receptor component protein) (CGRP-RCP) (CGRP-receptor component protein) (CGRPRCP)
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MEVKDANAALLSNYEVFQLLTDLKEQRKESGKNKHSAGQQNLNAITYETLKYISKTPCRNQSPAIVQEFLTAMKSHKLTKAEKLQLLNHRPMTAVEIQLMVEESEERLTEEQIEALLHTVTSILPAGPEDEQSKSTSNDVAMEEEEPA
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DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). Accessory protein for the calcitonin gene-related peptide (CGRP) receptor. It modulates CGRP responsiveness in a variety of tissues.
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O35430
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APBA1_RAT
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Amyloid-beta A4 precursor protein-binding family A member 1 (Adapter protein X11alpha) (Neuron-specific X11 protein) (Neuronal Munc18-1-interacting protein 1) (Mint-1)
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MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVEEEQQPSPPPPAGHAPEDHRAHPAPPPPPPPQEEEEERGECLARSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHAEAAQRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGLPAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPVDGDSPSPGSSSPLGAESSITPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDAKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI
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Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta.
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O35431
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APBA2_RAT
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Amyloid-beta A4 precursor protein-binding family A member 2 (Adapter protein X11beta) (Neuron-specific X11L protein) (Neuronal Munc18-1-interacting protein 2) (Mint-2)
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MAHRKRQSTASSMLDHRARPGPIPHDQEPENEDTELPLESYVPTGLELGTLRPDSPTPEEQECHNHSPDGDSSSDYVNNTSEEEDYDEGLPEEEEGVTYYIRYCPEDDSYLEGMDCNGEEYLAHGAHPVDTDECQEAVEDWTDSVGPHTHSHGAENSQEYPDSHLPIPEDDPTVLEVHDQEEDGHYCPSKESYQDYYPPETNGNTGGASPYRMRRGDGDLEEQEEDIDQIVAEIKMSLSMTSITSASEASPEHMPELDPGDSTEACSPSDTGRGPSRQEARPKSLNLPPEVKHSGDPQRGLKTKTRTPEERPKWPQEQVCNGLEQPRKQQRSDLNGPTDNNNIPETKKVASFPSFVAVPGPCEPEDLIDGIIFAANYLGSTQLLSERNPSKNIRMMQAQEAVSRVKRMQKAAKIKKKANSEGDAQTLTEVDLFISTQRIKVLNADTQETMMDHALRTISYIADIGNIVVLMARRRMPRSASQDCIETTPGAQEGKKQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDIINTQEMYNDDLIHFSNSENCKELQLEKHKGEILGVVVVESGWGSILPTVILANMMNGGPAARSGKLSIGDQIMSINGTSLVGLPLATCQGIIKGLKNQTQVKLNIVSCPPVTTVLIKRPDLKYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATAHEKIVQALSNSVGEIHMKTMPAAMFRLLTGQETPLYI
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Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta.
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O35433
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TRPV1_RAT
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Transient receptor potential cation channel subfamily V member 1 (TrpV1) (Capsaicin receptor) (Osm-9-like TRP channel 1) (OTRPC1) (Vanilloid receptor 1) (Vanilloid receptor type 1-like)
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MEQRASLDSEESESPPQENSCLDPPDRDPNCKPPPVKPHIFTTRSRTRLFGKGDSEEASPLDCPYEEGGLASCPIITVSSVLTIQRPGDGPASVRPSSQDSVSAGEKPPRLYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNNSLPMESTPHKCRGSACKPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRNWKNFALVPLLRDASTRDRHATQQEEVQLKHYTGSLKPEDAEVFKDSMVPGEK
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Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis. [Isoform 3]: Does not display channel activity in response to noxious chemical compounds, such as capsaicin and the vanilloid resiniferatoxin. Channel activity is not elicited by mildly acidic extracellular pH, and only slight channel activity is observed in response to noxiuos heat stimuli.
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O35435
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PYRD_MOUSE
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Dihydroorotate dehydrogenase (quinone), mitochondrial (DHOdehase) (EC 1.3.5.2) (Dihydroorotate oxidase)
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MAWRQLRKRALDAAIILGGGGLLFTSYLTATGDDHFYAEYLMPALQRLLDPESAHRLAVRVISLGLLPRATFQDSNMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSAVEHRLRARQQKQTQLTTDGLPLGINLGKNKTSVDAAADYVEGVRILGPLADYLVVNVSSPNTAGLRSLQGKTELRRLLSKVLQERDALKGPQKPAVLVKIAPDLTAQDKEDIASVARELGIDGLIITNTTVSRPVGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGTIPIIGVGGVSSGQDALEKIQAGASLVQLYTALTFLGPPVVARVKRELEALLKERGFNTVTDAIGVDHRR
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Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. Required for UMP biosynthesis via de novo pathway.
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O35437
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TCF21_MOUSE
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Transcription factor 21 (TCF-21) (Capsulin) (Epicardin) (Podocyte-expressed 1) (Pod-1)
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MSTGSLSDVEDLQEVEMLDCDSLKVDSNKEFGTSNESTEEGSNCENGSPQKGRGGLGKRRKAPTKKSPLSGVSQEGKQVQRNAANARERARMRVLSKAFSRLKTTLPWVPPDTKLSKLDTLRLASSYIAHLRQILANDKYENGYIHPVNLTWPFMVAGKPENDLKEVVTANRLCGTTAS
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Involved in epithelial-mesenchymal interactions in kidney and lung morphogenesis that include epithelial differentiation and branching morphogenesis. May be involved in the organogenesis of the spleen and heart and in cardiac and coronary artery development. May function in the development and sex differentiation of gonad via transcriptional regulation of AD4BP/SF-1.
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O35445
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RNF5_MOUSE
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E3 ubiquitin-protein ligase RNF5 (EC 2.3.2.27) (RING finger protein 5)
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MAAAEEEDGGPEGPNRERGGASATFECNICLETAREAVVSVCGHLYCWPCLHQWLETRPDRQECPVCKAGISREKVVPLYGRGSQKPQDPRLKTPPRPQGQRPAPESRGGFQPFGDAGGFHFSFGVGAFPFGFFTTVFNAHEPFRRGAGVDLGQGHPASSWQDSLFLFLAIFFFFWLLSI
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Membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination of target proteins. May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4 (By similarity). Mediates ubiquitination of PXN/paxillin,thereby regulating cell motility and localization of PXN/paxillin (By similarity). Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N (By similarity). Mediates the 'Lys-48'-linked polyubiquitination of STING1 at 'Lys-150' leading to its proteasomal degradation the ubiquitination occurs in mitochondria after viral transfection and regulates antiviral responses (By similarity). Catalyzes ubiquitination and subsequent degradation of ATG4B, thereby inhibiting autophagy.
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O35449
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PRRT1_MOUSE
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Proline-rich transmembrane protein 1 (Dispanin subfamily D member 1) (DSPD1) (Synapse differentiation-induced protein 4) (SynDIG4)
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MSSEKSGLPDSVPHTSPPPYNAPQPPAEPPIPPPQTAPSSHHHHHHHYHQSGTATLPRLGAGGLASAAASAQRGPSSSATLPRPPHHAPPGPAAGAPPPGCATLPRMPPDPYLQETRFEGPLPPPPPAAAAPPPPAPAPTAQAPGFVVPTHAGAVGTLPLGGYVAPGYPLQLQPCTAYVPVYPVGTPYAGGTPGGPGVTSTLPPPPQGPGLALLEPRRPPHDYMPIAVLTTICCFWPTGIIAIFKAVQVRTALARGDLVSAEIASREARNFSFISLAVGIAAMVLCTILTVVIIIAAQHHENYWDP
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Required to maintain a pool of extrasynaptic AMPA-regulated glutamate receptors (AMPAR) which is necessary for synapse development and function. Regulates AMPAR function and synaptic transmission during development but is dispensable at mature hippocampal synapses. Plays a role in regulating basal phosphorylation levels of glutamate receptor GRIA1 and promotes GRIA1 and GRIA2 cell surface expression.
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O35451
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ATF6B_MOUSE
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Cyclic AMP-dependent transcription factor ATF-6 beta (cAMP-dependent transcription factor ATF-6 beta) (Activating transcription factor 6 beta) (ATF6-beta) (cAMP response element-binding protein-related protein) (Creb-rp) (cAMP-responsive element-binding protein-like 1) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 beta]
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MAELMLLSEIADPTRFFTDNLLSPEDWDSTLYSGLDEVAEEQAQLFRCVEQDVPFDSSSLDVGMDVSPPEPPWDPLPIFPDLQVKSEPSSPCSSSSLSSESSHLSTEPPSQVPGVGEVLHVKMESLAPPLCLLGDDPASPFETVQITVGSASDDLSDIQTKLEPASPSSSVHSEASLLSADSPSQPFIGEEVLEVKTESPSPPGCLLWDVPASSLGAVQISMGPSPDSSSGKAPATRKPPLQPKPVVLTTVPVPPRAGPTSAAVLLQPLVQQPAVSPVVLIQGAIRVQPEGPAPAAPRPERKSIVPAPMPGNSCPPEVDAKLLKRQQRMIKNRESACQSRRKKKEYLQGLEARLQAVLADNQQLRRENAALRRRLEALLAENSGLKLGSGNRKVVCIMVFLLFIAFNFGPVSISEPPPAPMSPRMSREEPRPQRHLLGFSEPGPAHGMEPLREAAQSPGEQQPSSAGRPSFRNLTAFPGGAKELLLRDLDQLFLSSDCRHFNRTESLRLADELSGWVQRHQRGRRKIPHRAQERQKSQLRKKSPPVKPVPTQPPGPPERDPVGQLQLYRHPGRSQPEFLDAIDRREDTFYVVSFRRDHLLLPAISHNKTSRPKMSLVMPAMAPNETVSGRGPPGDYEEMMQIECEVMDTRVIHIKTSTVPPSLRKQPSPSPGNTTGGPLPGSAASPAHQASQPLYLNHP
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[Cyclic AMP-dependent transcription factor ATF-6 beta]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 beta), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR).
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O35453
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HEPS_MOUSE
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Serine protease hepsin (EC 3.4.21.106) [Cleaved into: Serine protease hepsin non-catalytic chain; Serine protease hepsin catalytic chain]
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MAKEDEEPGAHRGGSTCSRPQPGKGGRTAACCSRPKVAALIVGTLLFLTGIGAASWAIVTILLQSDQEPLYQVQLSPGDSRLAVFDKTEGTWRLLCSSRSNARVAGLGCEEMGFLRALAHSELDVRTAGANGTSGFFCVDEGGLPLAQRLLDVISVCDCPRGRFLTATCQDCGRRKLPVDRIVGGQDSSLGRWPWQVSLRYDGTHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVARTSPHAVQLGVQAVIYHGGYLPFRDPTIDENSNDIALVHLSSSLPLTEYIQPVCLPAAGQALVDGKVCTVTGWGNTQFYGQQAMVLQEARVPIISNEVCNSPDFYGNQIKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISGTSRWRLCGIVSWGTGCALARKPGVYTKVTDFREWIFKAIKTHSEASGMVTQP
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Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2 (By similarity). Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization.
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O35454
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CLCN6_MOUSE
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H(+)/Cl(-) exchange transporter 6 (Chloride channel protein 6) (ClC-6) (Chloride transport protein 6)
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MAGCRGSVCCCCRWCCCCGERESRTPEELTILGETQEEEDEILPRKDYESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFSVRLFTQLKFGVVQTSVEECSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPEIKCYLNGVKVPGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCSDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHPKPKLVRVLESLLVSLVTTVVVFVASMVLGECRQMSSTSQTGNGSFQLQVTSEDVNSTIKAFFCPNDTYNDMATLFFNSQESAILQLFHQDGTFSPVTLALFFILYFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGAAAFLGGVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDLFNKGIYDVHIGLRGVPLLEWETDVEMDKLRASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNEKEFMKGNQLISNNIKFKKSSILTRAGEQRKRGQSMKSYPSSELRNVCDEHVASEEPAEKEDLLQQMLERRYTPYPNLYPDQSPSEDWTMEERFRPLTFHGLVLRSQLVTLLVRGVCYSESQSSASQPRLSYAEMAEDYPRYPDIHDLDLTLLNPRMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQARLRQHYQTL
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Voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the late endosome lumen. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters.
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O35457
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CCRL2_MOUSE
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C-C chemokine receptor-like 2 (Chemokine receptor CCR11) (G-protein coupled beta chemokine receptor) (Lipopolysaccharide-inducible C-C chemokine receptor) (L-CCR)
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MDNYTVAPDDEYDVLILDDYLDNSGPDQVPAPEFLSPQQVLQFCCAVFAVGLLDNVLAVFILVKYKGLKNLGNIYFLNLALSNLCFLLPLPFWAHTAAHGESPGNGTCKVLVGLHSSGLYSEVFSNILLLVQGYRVFSQGRLASIFTTVSCGIVACILAWAMATALSLPESVFYEPRMERQKHKCAFGKPHFLPIEAPLWKYVLTSKMIILVLAFPLLVFIICCRQLRRRQSFRERQYDLHKPALVITGVFLLMWAPYNTVLFLSAFQEHLSLQDEKSSYHLDASVQVTQLVATTHCCVNPLLYLLLDRKAFMRYLRSLFPRCNDIPYQSSGGYQQAPPREGHGRPIELYSNLHQRQDII
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Receptor for CCL19 and chemerin/RARRES2. Does not appear to be a signaling receptor, but may have a role in modulating chemokine-triggered immune responses by capturing and internalizing CCL19 or by presenting RARRES2 ligand to CMKLR1, a functional signaling receptor. Plays a critical role for the development of Th2 responses (By similarity). {ECO:0000250, ECO:0000269|PubMed:12885941, ECO:0000269|PubMed:18794339, ECO:0000269|PubMed:20606167}.
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O35458
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VIAAT_RAT
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Vesicular inhibitory amino acid transporter (GABA and glycine transporter) (Solute carrier family 32 member 1) (Vesicular GABA transporter) (rGVAT) (rat UNC-47 homolog) (RUNC-47)
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MATLLRSKLTNVATSVSNKSQAKVSGMFARMGFQAATDEEAVGFAHCDDLDFEHRQGLQMDILKSEGEPCGDEGAEPPVEGDIHYQRGGAPLPPSGSKDQAVGAGGEFGGHDKPKITAWEAGWNVTNAIQGMFVLGLPYAILHGGYLGLFLIIFAAVVCCYTGKILIACLYEENEDGEVVRVRDSYVAIANACCAPRFPTLGGRVVNVAQIIELVMTCILYVVVSGNLMYNSFPGLPVSQKSWSIIATAVLLPCAFLKNLKAVSKFSLLCTLAHFVINILVIAYCLSRARDWAWEKVKFYIDVKKFPISIGIIVFSYTSQIFLPSLEGNMQQPSEFHCMMNWTHIAACVLKGLFALVAYLTWADETKEVITDNLPGSIRAVVNIFLVAKALLSYPLPFFAAVEVLEKSLFQEGSRAFFPACYGGDGRLKSWGLTLRCALVVFTLLMAIYVPHFALLMGLTGSLTGAGLCFLLPSLFHLRLLWRKLLWHQVFFDVAIFVIGGICSVSGFVHSLEGLIEAYRTNAED
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Antiporter that exchanges vesicular protons for cytosolic 4-aminobutanoate or to a lesser extend glycine, thus allowing their secretion from nerve terminals (By similarity). The transport is equally dependent on the chemical and electrical components of the proton gradient. May also transport beta-alanine. Acidification of GABAergic synaptic vesicles is a prerequisite for 4-aminobutanoate uptake (By similarity).
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O35460
|
ANGP1_RAT
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Angiopoietin-1 (ANG-1)
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MTVFLSFAFFAAILTHIGCSNQRRSPENGGRRYNRIQHGQCAYTFILPEHDGNCRESATEQYNTNALQRDAPHVETDFSSQKLQHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYELEKQLLQQTNEILKIQEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVTRQTFIIQELEKQLSRATSNNSVLQKQQLELMDTVHNLVSLCTKEVLLKGGKREEEKPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNEGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNQKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF
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Binds and activates TIE2 receptor by inducing its tyrosine phosphorylation. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. Mediates blood vessel maturation/stability. It may play an important role in the heart early development.
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O35462
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ANGP2_RAT
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Angiopoietin-2 (ANG-2)
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MWQIVFLTFGCDLVLASAYNNFRKSVDSTGRRQYQVQNGPCSYTFLLPETDSCRSSSSPYMSNAVQRDAPLDYDDSVQRLQVLENILENNTQWLMKLENYIQDNMKKEMVEIQQNVVQNQTAVMIEIGTSLLNQTAAQTRKLTDVEAQVLNQTTRLELQLLQHSISTNKLEKQILDQTSEINKLQDKNSFLEKKVLDMEDKHSVQLQSMKEQKDQLQVLVSKQSSVIDELEKKLVTATVNNSVLQKQQHDLMETVNSLLTMMSSPDYKSSVAVPKEEKTTFRDCAEIFKSGLTTSGIYTLTFPNSTEEVKAYCDMDMGGGGWTVIQHREDGSVDFQRTWKEYKEGFGSPLGEYWLGNEFVSQLTSGHRYVLKIQLKDWEGSEAHSLYEHFYLSGEESNYRIHLTGLTGTAGKISSISQPGSDFSTKDSDNDKCICKCSQMLTGGWWFDACGPSNLNGQYYPQKQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF
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Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal. Involved in the regulation of lymphangiogenesis.
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O35464
|
SEM6A_MOUSE
|
Semaphorin-6A (Semaphorin Q) (Sema Q) (Semaphorin VIA) (Sema VIA) (Semaphorin-6A-1) (SEMA6A-1)
|
MRPAALLLCLTLLHCAGAGFPEDSEPISISHGNYTKQYPVFVGHKPGRNTTQRHRLDIQMIMIMNRTLYVAARDHIYTVDIDTSHTEEIYCSKKLTWKSRQADVDTCRMKGKHKDECHNFIKVLLKKNDDTLFVCGTNAFNPSCRNYRVDTLETFGDEFSGMARCPYDAKHANIALFADGKLYSATVTDFLAIDAVIYRSLGDSPTLRTVKHDSKWLKEPYFVQAVDYGDYIYFFFREIAVEYNTMGKVVFPRVAQVCKNDMGGSQRVLEKQWTSFLKARLNCSVPGDSHFYFNILQAVTDVIRINGRDVVLATFSTPYNSIPGSAVCAYDMLDIANVFTGRFKEQKSPDSTWTPVPDERVPKPRPGCCAGSSSLEKYATSNEFPDDTLNFIKTHPLMDEAVPSIINRPWFLRTMVRYRLTKIAVDNAAGPYQNHTVVFLGSEKGIILKFLARIGSSGFLNGSLFLEEMNVYNPEKCSYDGVEDKRIMGMQLDRASGSLYVAFSTCVIKVPLGRCERHGKCKKTCIASRDPYCGWVRESGSCAHLSPLSRLTFEQDIERGNTDGLGDCHNSFVALNGHASSLYPSTTTSDSASRDGYESRGGMLDWNDLLEAPGSTDPLGAVSSHNHQDKKGVIRESYLKSNDQLVPVTLLAIAVILAFVMGAVFSGIIVYCVCDHRRKDVAVVQRKEKELTHSRRGSMSSVTKLSGLFGDTQSKDPKPEAILTPLMHNGKLATPSNTAKMLIKADQHHLDLTALPTPESTPTLQQKRKPNRGSREWERNQNIINACTKDMPPMGSPVIPTDLPLRASPSHIPSVVVLPITQQGYQHEYVDQPKMSEVVAQMALEDQAATLEYKTIKEHLSSKSPNHGVNLVENLDSLPPKVPQREASLGPPGTSLSQTGLSKRLEMQHSSSYGLEYKRSYPTNSLTRSHQTTTLKRNNTNSSNSSHLSRNQSFGRGDNPPPAPQRVDSIQVHSSQPSGQAVTVSRQPSLNAYNSLTRSGLKRTPSLKPDVPPKPSFAPLSTSMKPNDACT
|
Cell surface receptor for PLXNA2 that plays an important role in cell-cell signaling. Required for normal granule cell migration in the developing cerebellum. Promotes reorganization of the actin cytoskeleton and plays an important role in axon guidance in the developing central nervous system. Can act as repulsive axon guidance cue. Has repulsive action towards migrating granular neurons. May play a role in channeling sympathetic axons into the sympathetic chains and controlling the temporal sequence of sympathetic target innervation.
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O35465
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FKBP8_MOUSE
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Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (38 kDa FK506-binding protein) (38 kDa FKBP) (FKBP-38) (mFKBP38) (FK506-binding protein 8) (FKBP-8) (FKBPR38) (Rotamase)
|
MASWAEPSEPAALRLPGAPLLEGFEVLDGVDDAEEEDDLSGLPPLEDMGQPTVEEAEQPGALAREFLAATEPEPAPAPAPEEWLDILGNGLLRMKTLVPGPKGSSRPLKGQVVTVHLQMSLENGTRVQEEPELAFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAEDGPDLEMLSGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSNTKVDMTCEEEEELLQLKVKCLNNLAASQLKLDHYRAALRSCSQVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKRAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN
|
Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis (By similarity). Required for normal embryonic development.
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O35468
|
WNT9B_MOUSE
|
Protein Wnt-9b (Protein Wnt-14b) (Protein Wnt-15)
|
MRPAPALALAALCLLVLPAAAAAAAYFGLTGREVLTPFPGLGTAAAPAQAGAHLKQCDLLKLSRRQKQLCRREPGLAETLRDAAHLGLLECQFQFRQERWNCSLEGRTGLLQRGFKETAFLYAVSAAALTHALARACSAGRMERCTCDDSPGLESRQAWQWGVCGDNLKYSTKFLSNFLGPKRGSKDLRARADAHNTHVGIKAVKSGLRTTCKCHGVSGSCAVRTCWKQLSPFRETGQVLKLRYDTAVKVSSATNEALGRLELWAPAKPGGPAKGLAPRPGDLVYMEDSPSFCRPSKYSPGTAGRVCSRDSSCSSLCCGRGYDTQSRMVVFSCHCQVQWCCYVECQQCAQQELVYTCKR
|
Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway. Required for normal embryonic kidney development, and for normal development of the urogenital tract, including uterus and part of the oviduct and the upper vagina in females, and epididymis and vas deferens in males. Activates a signaling cascade in the metanephric mesenchyme that induces tubulogenesis. Acts upstream of WNT4 in the signaling pathways that mediate development of kidney tubules and the Muellerian ducts. Plays a role in cranofacial development and is required for normal fusion of the palate during embryonic development.
|
O35469
|
3BHS6_MOUSE
|
3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6 (EC 1.1.1.-) (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type VI) (3-beta-HSD VI) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)]
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MPGWSCLVTGAGGFLGQRIVQLLMQEKDLEEIRVLDKFFRPETREQFFNLDTNIKVTVLEGDILDTQYLRKACQGISVVIHTAAVIDVTGVIPRQTILDVNLKGTQNLLEACIQASVPAFIFSSSVDVAGPNSYKEIILNGNEEEHHESIWSDPYPYSKKMAEKAVLAANGSMLKIGGTLHTCALRPMYIYGERSPFISNTIITALKNKNILGCTGKFSTANPVYVGNVAWAHILAARGLRDPKKSPNIQGEFYYISDDTPHQSYDDLNYTLSKEWGFCPDSSWSLPVPLLYWLAFMLETVSFLLSPIYRFIPPFNRHLVTLTGSTFTFSYKKAQRDLGYEPLVSWEEAKQKTSEWIGTLVEQHRETLDTKSQ
|
3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. May be involved in local production of progesterone.
|
O35473
|
C1D_MOUSE
|
Nuclear nucleic acid-binding protein C1D (mC1D) (Small unique nuclear receptor corepressor) (Sun-CoR) (SunCoR)
|
MAGEEMNEDYPVEIHESLTALESSLGAVDDMLKTMMAVSRNELLQKLDPLEQAKVDLVSAYTLNSMFWVYLATQGVNPKEHPVKQELERIRVYMNRVKEITDKKKAAKLDRGAASRFVKNALWEPKAKSTPKVANKGKSKH
|
Plays a role in the recruitment of the RNA exosome complex to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA this function may include MPHOSPH6. Can activate PRKDC not only in the presence of linear DNA but also in the presence of supercoiled DNA. Can induce apoptosis in a p53/TP53 dependent manner. May regulate the TRAX/TSN complex formation. Potentiates transcriptional repression by NR1D1 and THRB (By similarity). {ECO:0000250, ECO:0000269|PubMed:10362552, ECO:0000269|PubMed:9405624}.
|
O35476
|
OPSG_RAT
|
Medium-wave-sensitive opsin 1 (Green cone photoreceptor pigment) (Green-sensitive opsin) (Medium wavelength-sensitive cone opsin)
|
MAQQLTGEQTLDHYEDSTQASIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSTWMILVVIASVFTNGLVLAATMRFKKLRHPLNWILVNLAVADLAETIIASTISVVNQIYGYFVLGHPLCVIEGYIVSLCGITGLWSLAIISWERWLVVCKPFGNVRFDAKLATVGIVFSWVWAAVWTAPPIFGWSRYWPYGLKTSCGPDVFSGTSYPGVQSYMMVLMVTCCIFPLSIIVLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMVFAYCLCWGPYTFFACFATAHPGYAFHPLVASLPSYFAKSATIYNPIIYVFMNRQFRNCILQLFGKKVDDSSELSSTSKTEVSSVSSVSPA
|
Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May increase spectral sensitivity in dim light.
|
O35484
|
AZIN1_MOUSE
|
Antizyme inhibitor 1 (AZI) (Ornithine decarboxylase antizyme inhibitor)
|
MKGFIDDANYSVGLLDEGTNLGNVIDNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQTVVAQIKPFYTVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIFTSPCKQVSQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKVLLHIATEDNIGGEDGNMKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEIQLEEVNHVISPLLDIYFPEGSGIQIISEPGSYYVSSAFTLAVNIIAKKVVENDKFSSGVEKNGSDEPAFVYYMNDGVYGSFASKLSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYFMMSFSDWYEMQDAGITSDAMMKNFFFAPSCIQLSQEDSFSTEA
|
Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding. Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production.
|
O35485
|
VEGFB_RAT
|
Vascular endothelial growth factor B (VEGF-B) (VEGF-related factor) (VRF)
|
MSPLLRRLLLVALLQLACTQAPVSQFDGPSHQKKVVSWIDVYARATCQPREVVVPLSMELMGNVVKQLVPSCVTVQRCGGCCPDDGLECVPIGQHQVRMQILMIQYPSSQLGEMSLEEHSQCECRPKRKESAVKPDRVAIPHHRPQPRSVLSWDSAPGASSPADIIHPTPAPGPSAHAAPSAVSALIPGPAVAAADAAASSIAKGGA
|
Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis (By similarity).
|
O35488
|
S27A2_MOUSE
|
Long-chain fatty acid transport protein 2 (Arachidonate--CoA ligase) (EC 6.2.1.15) (Fatty acid transport protein 2) (FATP-2) (Fatty-acid-coenzyme A ligase, very long-chain 1) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Phytanate--CoA ligase) (EC 6.2.1.24) (Solute carrier family 27 member 2) (Slc27a2) (THCA-CoA ligase) (EC 6.2.1.7) (Very long-chain acyl-CoA synthetase) (VLACS) (VLCS) (EC 6.2.1.-) (Very long-chain-fatty-acid-CoA ligase)
|
MLPVLYTGLAGLLLLPLLLTCCCPYLLQDVRYFLRLANMARRVRSYRQRRPVRTILRAFLEQARKTPHKPFLLFRDETLTYAQVDRRSNQVARALHDQLGLRQGDCVALFMGNEPAYVWIWLGLLKLGCPMACLNYNIRAKSLLHCFQCCGAKVLLASPDLQEAVEEVLPTLKKDAVSVFYVSRTSNTNGVDTILDKVDGVSAEPTPESWRSEVTFTTPAVYIYTSGTTGLPKAATINHHRLWYGTGLAMSSGITAQDVIYTTMPLYHSAALMIGLHGCIVVGATLALRSKFSASQFWDDCRKYNVTVIQYIGELLRYLCNTPQKPNDRDHKVKKALGNGLRGDVWREFIKRFGDIHVYEFYASTEGNIGFVNYPRKIGAVGRANYLQRKVARYELIKYDVEKDEPVRDANGYCIKVPKGEVGLLVCKITQLTPFIGYAGGKTQTEKKKLRDVFKKGDIYFNSGDLLMIDRENFVYFHDRVGDTFRWKGENVATTEVADIVGLVDFVEEVNVYGVPVPGHEGRIGMASLKIKENYEFNGKKLFQHIAEYLPSYARPRFLRIQDTIEITGTFKHRKVTLMEEGFNPTVIKDTLYFMDDAEKTFVPMTENIYNAIIDKTLKL
|
Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport across cell membranes, playing an important role in hepatic fatty acid uptake. Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake. Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid (By similarity). May contribute to the synthesis of sphingosine-1-phosphate (By similarity). Does not activate C24 bile acids, cholate and chenodeoxycholate (By similarity). In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. However, it is not critical for THCA activation and bile synthesis in vivo (By similarity).
|
O35491
|
CLK2_MOUSE
|
Dual specificity protein kinase CLK2 (EC 2.7.12.1) (CDC-like kinase 2)
|
MPHPRRYHSSERGSRGSYHEHYQSRKHKRRRSRSWSSSSDRTRRRRREDSYHVRSRSSYDDHSSDRRLYDRRYCGSYRRNDYSRDRGEAYYDTDFRQSYEYHRENSSYRSQRSSRRKHRRRRRRSRTFSRSSSHSSRRAKSVEDDAEGHLIYHVGDWLQERYEIVSTLGEGTFGRVVQCVDHRRGGTQVALKIIKNVEKYKEAARLEINVLEKINEKDPDNKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKDNNYLPYPIHQVRHMAFQLCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTAVRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPVPSRMIRKTRKQKYFYRGRLDWDENTSAGRYVRENCKPLRRYLTSEAEDHHQLFDLIENMLEYEPAKRLTLGEALQHPFFACLRTEPPNTKLWDSSRDISR
|
Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Phosphorylates PAGE4 at several serine and threonine residues and this phosphorylation attenuates the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (By similarity).
|
O35492
|
CLK3_MOUSE
|
Dual specificity protein kinase CLK3 (EC 2.7.12.1) (CDC-like kinase 3)
|
MPVLSARRKRLASTAGPRRGSGPSLAVRWVPPLGPEPSSDRGRAPMRPRGPTCSTTRRGAGRGPRLLPGPPGRDLHRCRPDPGGAGQSPRVCEFGARAVRPLGRVEPGPPTAASREGAVLPRAEARAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRIPYQRRYREHRDSDTYRCEERSPSFGEDCYGSSRSRHRRRSRERAPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFFAGLTPEERSFHSSRNPSR
|
Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.
|
O35493
|
CLK4_MOUSE
|
Dual specificity protein kinase CLK4 (EC 2.7.12.1) (CDC-like kinase 4)
|
MRHSKRTHCPDWDSRESWGHESYSGSHKRKRRSHSSTQENRHCKPHHQFKDSDCHYLEARCLNERDYRDRRYIDEYRNDYCEGYVPRHYHRDVESTYRIHCSKSSVRSRRSSPKRKRNRPCASHQSHSKSHRRKRSRSIEDDEEGHLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHGMDGLHVAVKIVKNVGRYREAARSEIQVLEHLNSTDPNSVFRCVQMLEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFQIDHIRQMAYQICQSINFLHHNKLTHTDLKPENILFVKSDYVVKYNSKMKRDERTLKNTDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPIPAHMIQKTRKRKYFHHNQLDWDEHSSAGRYVRRRCKPLKEFMLCHDEEHEKLFDLVRRMLEYDPARRITLDEALQHPFFDLLKRK
|
Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates SRSF1 and SRSF3. Required for the regulation of alternative splicing of MAPT/TAU. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.
|
O35495
|
CDK14_MOUSE
|
Cyclin-dependent kinase 14 (EC 2.7.11.22) (Cell division protein kinase 14) (Serine/threonine-protein kinase PFTAIRE-1)
|
MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKEDTTFDEICVTKMSTRNCQGTDSVIKHLDTIPEDKKVRVQRTQSTFDPFEKPANQVKRVHSENNACINFKSSSAGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPDNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLGTPNEDTWPGVHSLPHFKPERFTVYSSKSLRQAWNKLSYVNHAEDLASKLLQCSPKNRLSAQAALSHEYFSDLPPRLWELTDMSSIFTVPNVRLQPEAGESMRAFGKNNSYGKSLSNSKH
|
Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport (By similarity). {ECO:0000250, ECO:0000269|PubMed:9547506}.
|
O35505
|
CAC1C_CAVPO
|
Voltage-dependent L-type calcium channel subunit alpha-1C (Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) (Voltage-gated calcium channel subunit alpha Cav1.2)
|
MVPLVQPTTPAYRPLPSHLSADTEVRGRGTLVHEAQLNCFYISPGGSNYGSPRPAHANINANAAAGLAPEHIPTPGAALSWQAAIDAGRQAKLMGSAGNTTISTVSSTQRKRQQYGKPKKQSGTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHTALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGITDVPAEEDPSPCALESGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWMQDAMGYELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGVDEEKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPHWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRLDCFIVCGGILETILVETKIMSPLGISVLRCVRLLRIFKITRYWNSLSNLVASLLNSVRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMRTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQEVVEKPAVEETKEEKIELKSITADGESPPTTKINMDDLQPNENEDKSPYPNPDAAGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSPNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILFYFDIVFTTIFTIEIALKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAECKGNYITYKDGEVDQPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKHYFCDAWNTFDALIVVGSIVDIAITEVNPAEHTQCSPSMNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESDPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVVMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTAMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFGRAGGLFGNHVSYYQSDSRSTFPQTFTTQRPLHINKAGNNQGDTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRFPHPAGYPSTVSTVEGHRPPSSPATWAQEATRKLGAMRCHSRESQIAVVCQEEPSQDKTYDVELNKDAEYCSEPSLLSTEMLSYKDDENRQLTPPEEDKGDTRPSPKKGFLRSASLGRRASFHLECLKRQKNHGGDISQKTVLPLHLVHHQALAVAGLSPLLQRSHSPTAIPRPCATPPATPGSRGWPPKPIPTLRLEGAESCEKLNSSFPSIHCSSWSEEPSPCGGGSSAARRARPVSLMVPSQAGAPGRQFHGSASSLAEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIGEMENAADNILSGGAPQSPNGTLLPFVNCRDPGQDRAGGDEDEGCACALGRGWSEEELADSRVHVRSL
|
Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity). Plays an important role in excitation-contraction coupling in the heart (By similarity). Required for normal heart development and normal regulation of heart rhythm (By similarity). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine (By similarity). Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (By similarity). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (By similarity).
|
O35507
|
PPARA_CAVPO
|
Peroxisome proliferator-activated receptor alpha (PPAR-alpha) (Nuclear receptor subfamily 1 group C member 1)
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MVDMESPLCPLSPLEAEDLESPLSEYFLQEMGTIQDISRSLGEDSSGSFGFPEYQYLGSGPGSDGSVITDTLSPASSPSSVSYPEVPCGVDEPPSSALNIECRICGDKASGYHYGVHACEGCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSEKAKLKAEVLTCDRDSEGAETADLKSLAKRIYEAYLKNFHMNKVKARIILAGKTSSHPLFVIHDMETLCTAEKTLMAKVVSDGIRDKEAEVRIFHCCQCVSVETVTNLTEFAKAIPGFASLDLNDQVTLLKYGVYEAIFTMLSSTMNKDGMLVAYGHGFITREFLKNLRKPFCDMMEPKFNFAMKFNALELDDSDISLFVAAIICCGDRPGLLNIDHIEKMQEAIVHVLKLHLQSNHPDDTFLFPKLLQKLADLRQLVTEHAQLVQVIKTESDAALHPLLQEIYRDMY
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Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2 (By similarity).
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O35509
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RB11B_RAT
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Ras-related protein Rab-11B (EC 3.6.5.2)
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MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNNLSFIETSALDSTNVEEAFKNILTEIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQKPNKLQCCQNL
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The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The small Rab GTPase RAB11B plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis.
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O35516
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NOTC2_MOUSE
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Neurogenic locus notch homolog protein 2 (Notch 2) (Motch B) [Cleaved into: Notch 2 extracellular truncation; Notch 2 intracellular domain]
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MPALRPAALRALLWLWLCGAGPAHALQCRGGQEPCVNEGTCVTYHNGTGFCRCPEGFLGEYCQHRDPCEKNRCQNGGTCVPQGMLGKATCRCAPGFTGEDCQYSTSHPCFVSRPCQNGGTCHMLSRDTYECTCQVGFTGKQCQWTDACLSHPCENGSTCTSVASQFSCKCPAGLTGQKCEADINECDIPGRCQHGGTCLNLPGSYRCQCPQGFTGQHCDSPYVPCAPSPCVNGGTCRQTGDFTFECNCLPGFEGSTCERNIDDCPNHKCQNGGVCVDGVNTYNCRCPPQWTGQFCTEDVDECLLQPNACQNGGTCTNRNGGYGCVCVNGWSGDDCSENIDDCAYASCTPGSTCIDRVASFSCLCPEGKAGLLCHLDDACISNPCHKGALCDTNPLNGQYICTCPQGYKGADCTEDVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCEMDINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCELEVNECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQIDIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGILCDENIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICSDQIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGLNCEINFDDCASNPCMHGVCVDGINRYSCVCSPGFTGQRCNIDIDECASNPCRKGATCINDVNGFRCICPEGPHHPSCYSQVNECLSNPCIHGNCTGGLSGYKCLCDAGWVGVNCEVDKNECLSNPCQNGGTCNNLVNGYRCTCKKGFKGYNCQVNIDECASNPCLNQGTCFDDVSGYTCHCMLPYTGKNCQTVLAPCSPNPCENAAVCKEAPNFESFSCLCAPGWQGKRCTVDVDECISKPCMNNGVCHNTQGSYVCECPPGFSGMDCEEDINDCLANPCQNGGSCVDHVNTFSCQCHPGFIGDKCQTDMNECLSEPCKNGGTCSDYVNSYTCTCPAGFHGVHCENNIDECTESSCFNGGTCVDGINSFSCLCPVGFTGPFCLHDINECSSNPCLNAGTCVDGLGTYRCICPLGYTGKNCQTLVNLCSRSPCKNKGTCVQEKARPHCLCPPGWDGAYCDVLNVSCKAAALQKGVPVEHLCQHSGICINAGNTHHCQCPLGYTGSYCEEQLDECASNPCQHGATCNDFIGGYRCECVPGYQGVNCEYEVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCEENIDECAGGPHCLNGGQCVDRIGGYTCRCLPGFAGERCEGDINECLSNPCSSEGSLDCVQLKNNYNCICRSAFTGRHCETFLDVCPQKPCLNGGTCAVASNMPDGFICRCPPGFSGARCQSSCGQVKCRRGEQCIHTDSGPRCFCLNPKDCESGCASNPCQHGGTCYPQRQPPHYSCRCPPSFGGSHCELYTAPTSTPPATCQSQYCADKARDGICDEACNSHACQWDGGDCSLTMEDPWANCTSTLRCWEYINNQCDEQCNTAECLFDNFECQRNSKTCKYDKYCADHFKDNHCDQGCNSEECGWDGLDCASDQPENLAEGTLIIVVLLPPEQLLQDSRSFLRALGTLLHTNLRIKQDSQGALMVYPYFGEKSAAMKKQKMTRRSLPEEQEQEQEVIGSKIFLEIDNRQCVQDSDQCFKNTDAAAALLASHAIQGTLSYPLVSVFSELESPRNAQLLYLLAVAVVIILFFILLGVIMAKRKRKHGFLWLPEGFTLRRDSSNHKRREPVGQDAVGLKNLSVQVSEANLIGSGTSEHWVDDEGPQPKKAKAEDEALLSEDDPIDRRPWTQQHLEAADIRHTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVLCGPNRSFLSLKHTPMGKKARRPNTKSTMPTSLPNLAKEAKDAKGSRRKKCLNEKVQLSESSVTLSPVDSLESPHTYVSDATSSPMITSPGILQASPTPLLAAAAPAAPVHTQHALSFSNLHDMQPLAPGASTVLPSVSQLLSHHHIAPPGSSSAGSLGRLHPVPVPADWMNRVEMNETQYSEMFGMVLAPAEGAHPGIAAPQSRPPEGKHMSTQREPLPPIVTFQLIPKGSIAQAAGAPQTQSSCPPAVAGPLPSMYQIPEMPRLPSVAFPPTMMPQQEGQVAQTIVPTYHPFPASVGKYPTPPSQHSYASSNAAERTPSHGGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGGGGGQRGPGTHMSEPPHSNMQVYA
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Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation (By similarity). In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. Positively regulates self-renewal of liver cancer cells (By similarity).
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O35521
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PSB9_MUSTR
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Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
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MLRAGAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGAAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTNAITLAMNRDGSSGGVIYLVTITAAGVDHRVILGDELPKFYGE
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The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
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O35522
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PSB9_MUSMB
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Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
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MLRAGAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTISGSGSSYIYGYVDAAYKPGMTPEECRRFTTNAITLAMNRDGSSGGVIYLVTITAAGVDHRVILGDELPKFYDE
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The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
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O35523
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PSB9_MUSPL
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Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
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MLRAGAPTAGSFRTKEVHTGTTIMAVEFDGGVVVGSDSRVSAGEAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTSEECRRFTTNAITLAMNRDGSSGGVIYLVTITVAGVDHRVILGDELPKFYDE
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The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
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O35524
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PSB9_MUSSI
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Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)
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MLRAGAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTNAITLAMNRDGSSGGVIYLVTITAAGVDHRVILGDELPRFYDE
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The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides.
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O35526
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STX1A_MOUSE
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Syntaxin-1A (Neuron-specific antigen HPC-1)
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MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLETSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG
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Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis. Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane. STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion. Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm. Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1).
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O35543
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HPGDS_RAT
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Hematopoietic prostaglandin D synthase (H-PGDS) (EC 5.3.99.2) (GST class-sigma) (Glutathione S-transferase) (EC 2.5.1.18) (Glutathione-dependent PGD synthase) (Glutathione-requiring prostaglandin D synthase) (Prostaglandin-H2 D-isomerase)
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MPNYKLLYFNMRGRAEIIRYIFAYLDIKYEDHRIEQADWPKIKPTLPFGKIPVLEVEGLTLHQSLAIARYLTKNTDLAGKTELEQCQVDAVVDTLDDFMSLFPWAEENQDLKERTFNDLLTRQAPHLLKDLDTYLGDKEWFIGNYVTWADFYWDICSTTLLVLKPDLLGIYPRLVSLRNKVQAIPAISAWILKRPQTKL
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Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide.
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O35544
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EAA4_MOUSE
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Excitatory amino acid transporter 4 (High-affinity neuronal glutamate transporter) (Sodium-dependent glutamate/aspartate transporter) (Solute carrier family 1 member 6)
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MSSHGNSLFLRESGAGGGCLQGLQDSLQQRALRTRLRLQTMTREHVRRFLRRNAFILLTVSAVIIGVSLAFALRPYQLSYRQIKYFSFPGELLMRMLQMLVLPLIVSSLVTGMASLDNKATGRMGMRAAVYYMVTTVIAVFIGILMVTIIHPGKGSKEGLHREGRIETVPTADAFMDLVRNMFPPNLVEACFKQFKTQYSTRVVTRTIVRTDNGSELGASMSPTSSVENETSILENVTRALGTLQEVISFEETVPVPGSANGINALGLVVFSVAFGLVIGGMKHKGRVLRDFFDSLNEAIMRLVGIIIWYAPVGILFLIAGKILEMEDMAVLGGQLGMYTLTVIVGLFLHAGGVLPLIYFLVTHRNPFPFIGGMLQALITAMGTSSSSATLPITFRCLEEGLGVDRRITRFVLPVGATVNMDGTALYEALAAIFIAQVNNYELNLGQITTISITATAASVGAAGIPQAGLVTMVIVLTSVGLPTEDITLIIAVDWFLDRLRTMTNVLGDSIGAAVIEHLSQRELELQEAELTLPSLGKPYKSLMAQEKGASRGRGGNESVM
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Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (Probable).
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O35547
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ACSL4_RAT
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Long-chain-fatty-acid--CoA ligase 4 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 4) (LACS 4)
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MKLKLNVLTIVLLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVAKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKAALLDINCVKHIIYVDNKTINRAEYPEGLEIHSMQSVEELGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMYGGK
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Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially activates arachidonate and eicosapentaenoate as substrates. Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET. Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs. Modulates prostaglandin E2 secretion (By similarity).
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O35548
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MMP16_RAT
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Matrix metalloproteinase-16 (MMP-16) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 3) (MT-MMP 3) (MTMMP3) (Membrane-type-3 matrix metalloproteinase) (MT3-MMP) (MT3MMP)
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MILLAFSSGRRLDFVHRSGVFFFQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFNIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRRAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDRSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSVPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGNGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITIWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRDKEGLSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV
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Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. The short isoform efficiently converts progelatinase A to the intermediate form but not to the mature one. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.
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O35550
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RABE1_RAT
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Rab GTPase-binding effector protein 1 (Rabaptin-5) (Rabaptin-5alpha)
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MAQPGPAPQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERAQWAQYRESADREIADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEEDEQQRINKGKDNKKIDTEEEVKIPVVCALTQEESSTPLSNEEEHLDSTHGSVHSLDADLLLPSGDPFSKSDNDMFKEGLRRAQSTDSLGTSSSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTVSLGSLQMPSGFMLTKDQERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSETEWNLLQKEVHNAGNKLGRRCDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKEKQELEDFLRQSAEDSSHQISALVLRAQASEVLLEELQQSFSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQLAEDFILPDTVQVLRELVLKYRENIVHVRTAADHMEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKVNLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDINQLPET
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Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. Mediates the traffic of PKD1:PKD2 complex from the endoplasmic reticulum through the Golgi to the cilium.
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O35551
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RABE1_MOUSE
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Rab GTPase-binding effector protein 1 (Rabaptin-5) (Rabaptin-5alpha)
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MAQPGPAPQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQWREEVASLQAIMKETVRDYEHQFHLRLEQERAQWAQYRESAEREIADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEEDEQQRVNKRKDNKKTDTEEEVKIPVVCALTQEESSTPLSNEEEHLDSTHGSVHSLDADLMLPSGDPFSKSDNDMFKDGLRRAQSTDSLGTSSSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTVSLGSLQMPSGFMLTKDQERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSETEWNLLQKEVHNAGNKLGRRCDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKEKQELEDFLKQSAEDSSHQISALVLRAQASEVLLEELQQSFSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQLAEDFILPDTVEVLRELVLKYRENIVHVRTAADHMEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEMKVNLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDINQLPET
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Rab effector protein acting as linker between gamma-adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Involved in KCNH1 channels trafficking to and from the cell membrane. Stimulates RABGEF1 mediated nucleotide exchange on RAB5A. Mediates the traffic of PKD1:PKD2 complex from the endoplasmic reticulum through the Golgi to the cilium.
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O35552
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F263_RAT
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (6PF-2-K/Fru-2,6-P2ase 3) (PFK/FBPase 3) (6PF-2-K/Fru-2,6-P2ase brain-type isozyme) (RB2K) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)]
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MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMRVRKQCALAALRDVKSYLTKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRINCYEASYQPLDPDKCDRDLSFIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEYNVQGKIGGDSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVSTHRERSEAVKIQHFASVVRPSSYTELDFLSVESAKQDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQPLLGKACLRTVCHIFSKFSPY
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Catalyzes both the synthesis and degradation of fructose 2,6-bisphosphate.
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O35565
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FGF10_MOUSE
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Fibroblast growth factor 10 (FGF-10) (Keratinocyte growth factor 2)
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MWKWILTHCASAFPHLPGCCCCFLLLFLVSSFPVTCQALGQDMVSQEATNCSSSSSSFSSPSSAGRHVRSYNHLQGDVRWRRLFSFTKYFLTIEKNGKVSGTKNEDCPYSVLEITSVEIGVVAVKAINSNYYLAMNKKGKLYGSKEFNNDCKLKERIEENGYNTYASFNWQHNGRQMYVALNGKGAPRRGQKTRRKNTSAHFLPMTIQT
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Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. May play a role in wound healing.
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O35567
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PUR9_RAT
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Bifunctional purine biosynthesis protein ATIC (AICAR transformylase/inosine monophosphate cyclohydrolase) (ATIC) [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase) (AICAR formyltransferase) (AICAR transformylase); Inosine 5'-monophosphate cyclohydrolase (IMP cyclohydrolase) (EC 3.5.4.10) (IMP synthase) (Inosinicase)]
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MASSQLALFSVSDKTGLVEFARNLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPEDAADMARLDFNLIRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYGAVAAEMQGSGNKDTSLETRRHLALKAFTHTAQYDEAISDYFRRQYSKGISQMPLRYGMNPHQTPAQLYTLKPKLPITVLNGAPGFINLCDALNAWQLVTELRGAVDIPAAASFKHVSPAGAAVGVPLSEDEARVCMVYDLYPTLTPLAIAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIVAPGYEEEALKILSKKKNGSYCVLQMDQSYKPDENEVRTLFGLRLSQKRNNGVVDKSLFSNIVTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKDGQVIGIGAGQQSRIHCTRLAGDKANSWWLRHHPRVLSMKFKAGVKRAEVSNAIDQYVTGTIGEGEDLVKWKALFEEVPELLTEAEKKEWVDKLSGVSVSSDAFFPFRDNVDRAKRSGVAYIVAPSGSTADKVVIEACDELGIVLAHTDLRLFHH
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Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis. Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR). Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction. Also catalyzes the cyclization of FAICAR to IMP (By similarity). Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization.
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O35568
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FBLN3_RAT
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EGF-containing fibulin-like extracellular matrix protein 1 (Fibulin-3) (FIBL-3) (T16 protein)
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MLQTVFLTMLTLALVKSQVTEETITYTQCTDGYEWDPVRQQCKDIDECDIVPDACKGGMKCVNHYGGYLCLPKTAQIIVNNEQPQQETPAAEASSGAATGTIAARSMATSGVIPGGGFIASATAVAGPEVQTGRNNFVIRRNPADPQRIPSNPSHRIQCAAGYEQSEHNVCQDIDECTSGTHNCRLDQVCINLRGSFTCHCLPGYQKRGEQCVDIDECSVPPYCHQGCVNTPGSFYCQCNPGFQLAANNYTCVDINECDASNQCAQQCYNILGSFICQCNQGYELSSDRLNCEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGYQVVRSRTCQDINECETTNECREDEMCWNYHGGFRCYPQNPCQDPYVLTSENRCVCPVSNTMCRDVPQSIVYKYMNIRSDRSVPSDIFQIQATTIYANTINTFRIKSGNENGEFYLRQTSPVSAMLVLVKSLTGPREHIVGLEMLTVSSIGTFRTSSVLRLTIIVGPFSF
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Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth.
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O35569
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NRG2_RAT
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Pro-neuregulin-2, membrane-bound isoform (Pro-NRG2) [Cleaved into: Neuregulin-2 (NRG-2) (Neural- and thymus-derived activator for ERBB kinases) (NTAK)]
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MRQVCCSALPPPLEKARCSSYSYSDSSSSSSSNNSSSSTSSRSSSRSSSRSSRGSTTTTSSSENSGSNSGSIFRPAAPPEPRPQPQPQPRSPAARRAAARSRAAAAGGMRRDPAPGSSMLLFGVSLACYSPSLKSVQDQAYKAPVVVEGKVQGLAPAGGSSSNSTREPPASGRVALVKVLDKWPLRSGGLQREQVISVGSCAPLERNQRYIFFLEPTEQPLVFKTAFAPVDPNGKNIKKEVGKILCTDCATRPKLKKMKSQTGEVGEKQSLKCEAAAGNPQPSYRWFKDGKELNRSRDIRIKYGNGRKNSRLQFNKVKVEDAGEYVCEAENILGKDTVRGRLHVNSVSTTLSSWSGHARKCNETAKSYCVNGGVCYYIEGINQLSCKCPNGFFGQRCLEKLPLRLYMPDPKQKHLGFELKEAEELYQKRVLTITGICVALLVVGIVCVVAYCKTKKQRRQMHHHLRQNMCPAHQNRSLANGPSHPRLDPEEIQMADYISKNVPATDHVIRREAETTFSGSHSCSPSHHCSTATPTSSHRHESHTWSLERSESLTSDSQSGIMLSSVGTSKCNSPACVEARARRAAAYSQEERRRAAMPPYHDSIDSLRDSPHSERYVSALTTPARLSPVDFHYSLATQVPTFEITSPNSAHAVSLPPAAPISYRLAEQQPLLRHPAPPGPGPGPGADMQRSYDSYYYPAAGPGPRRGACALGGSLGSLPASPFRIPEDDEYETTQECAPPPPPRPRTRGASRRTSAGPRRWRRSRLNGLAAQRARAARDSLSLSSGSGCGSASASDDDADDADGALAAESTPFLGLRAAHDALRSDSPPLCPAADSRTYYSLDSHSTRASSRHSRGPPTRAKQDSGPL
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Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. May also promote the heterodimerization with the EGF receptor.
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O35587
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TMEDA_MESAU
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Transmembrane emp24 domain-containing protein 10 (Protein TMED10) (21 kDa transmembrane-trafficking protein) (Integral membrane protein p23) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)
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MSGSSGPLSWPGPRPCALLFLLLLGPSSVLAISFHLPVNSRKCLREEIHKDLLVTGAYEITDQSGGAGGLRTHLKITDSAGHILYAKEDATKGKFAFTTEDYDMFEVCFESKGTGRIPDQLVILDMKHGVEAKNYEEIAKVEKLKPLEVELRRLEDLSESIVNDFAYMKKREEEMRDTNESTNTRVLYFSIFSMLCLIGLATWQVFYLRRFFKAKKLIE
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Cargo receptor involved in protein vesicular trafficking and quality control in the endoplasmic reticulum (ER) and Golgi. The p24 protein family is a group of transmembrane proteins that bind coat protein complex I/COPI and coat protein complex II/COPII involved in vesicular trafficking between the membranes. Acts at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and involved in vesicle coat formation at the cytoplasmic side (By similarity). Mainly functions in the early secretory pathway and cycles between the ER, ER-Golgi intermediate compartment (ERGIC) and Golgi, mediating cargo transport through COPI and COPII-coated vesicles. In COPII vesicle-mediated anterograde transport, involved in the transport of GPI-anchored proteins by acting together with TMED2 as their cargo receptor the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER (By similarity). Recognizes GPI anchors structural remodeled in the ER by the GPI inositol-deacylase/PGAP1 and the metallophosphoesterase MPPE1/PGAP5 (By similarity). In COPI vesicle-mediated retrograde transport, involved in the biogenesis of COPI vesicles and vesicle coat recruitment. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent from the modulation of gamma-secretase activity) (By similarity). Involved in the KDELR2-mediated retrograde transport of the toxin A subunit (CTX-A-K63)together with COPI and the COOH terminus of KDELR2 (By similarity). On Golgi membranes, acts as primary receptor for ARF1-GDP, a GTP-binding protein involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2 which mediates the hydrolysis of ARF1-bound GTP and therefore modulates protein trafficking from the Golgi apparatus. Involved in the exocytic trafficking of G protein-coupled receptors F2LR1/PAR2 (trypsin and tryspin-like enzyme receptor), OPRM1 (opioid receptor) and P2RY4 (UTD and UDP receptor) from the Golgi to the plasma membrane, thus contributing to receptor resensitization. In addition to its cargo receptor activity, may also act as a protein channel after oligomerization, facilitating the post-translational entry of leaderless cytoplasmic cargo into the ERGIC. Involved in the translocation into ERGIC, the vesicle entry and the secretion of leaderless cargos (lacking the secretion signal sequence), including the mature form of interleukin 1/IL-1 family members, the alpha-crystallin B chain HSPB5, the carbohydrate-binding proteins galectin-1/LGALS1 and galectin-3/LGALS3, the microtubule-associated protein Tau/MAPT, and the annexin A1/ANXA1 the translocation process is dependent on cargo protein unfolding and enhanced by chaperones HSP90AB1 and HSP90B1/GRP9. Could also associates with the presenilin-dependent gamma-secretase complex in order to regulate gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40/Abeta40 (By similarity).
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O35593
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PSDE_MOUSE
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26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (MAD1)
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MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK
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Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading.
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O35594
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IFT81_MOUSE
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Intraflagellar transport protein 81 homolog (Carnitine deficiency-associated protein expressed in ventricle 1) (CDV-1)
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MSDQIKFIVDSLNKEPFKKNYNLITFDSLGPMQLLQVLNDVLAEIDPKQDVDIREEMPEQTAKRMLNLLGILKYKPPGNATDMSTFRQGLVIGSKPVIYPVLHWLLQRSNELKKRAYLARFLIKLEVPSEFLQDETVADTNKQYEELMEAFKTLHKECEQLKTSGFSTAEIRRDISAMEEEKDQLMKRVERLKKRVETVQNHQRMLKIARQLRVEKEREEFLAQQKQEQKNQLFHAVQRLQRVQNQLKSMRHAAADAKPESLMKRLEEEIKFNSYMVTEKFPKELESKKKELHFLQKVVSEPAMGHSDLLELETKVNEVNTEINQLIEKKMMRNEPIEGKLSLYRQQASIISRKKEAKAEELQETKEKLASLEREVLVKTNQTREFDGTEVLKGDEFKRYVSKLRSKSTVFKKKHQIIAEFKAEFGLLQRTEELLKQRQETIQHQLRTIEEKKGISGYSYTQEELERVSALKSEVDEMKGRTLDDMSEMVKKLNSLVSEKKSALAPVIKELRQLRQKCQELTQECDEKKAQYDSCAAGLESNRSKLEQEVRGLREECLQEESKYHYTNCMIKNLEVELRRATDEMKAYVSSDQQEKRKAIREQYTKNITEQENLGKKLREKQKAVRESHGPNMKQAKMWRDLEQLMECKKQCFLKQQSPASIGQVIQEGGEDRLVL
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Component of the intraflagellar transport (IFT) complex B: together with IFT74, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds tubulin via its CH (calponin-homology)-like region. Required for ciliogenesis. Required for proper regulation of SHH signaling (By similarity). Plays an important role during spermatogenesis by modulating the assembly and elongation of the sperm flagella.
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O35595
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PTC2_MOUSE
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Protein patched homolog 2 (PTC2)
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MVRPLSLGELPPSYTPPARSSAPHILAGSLQAPLWLRAYFQGLLFSLGCRIQKHCGKVLFLGLVAFGALALGLRVAVIETDLEQLWVEVGSRVSQELHYTKEKLGEEAAYTSQMLIQTAHQEGGNVLTPEALDLHLQAALTASKVQVSLYGKSWDLNKICYKSGVPLIENGMIERMIEKLFPCVILTPLDCFWEGAKLQGGSAYLPGRPDIQWTNLDPQQLLEELGPFASLEGFRELLDKAQVGQAYVGRPCLDPDDPHCPPSAPNRHSRQAPNVAQELSGGCHGFSHKFMHWQEELLLGGTARDLQGQLLRAEALQSTFLLMSPRQLYEHFRGDYQTHDIGWSEEQASMVLQAWQRRFVQLAQEALPANASQQIHAFSSTTLDDILRAFSEVSTTRVVGGYLLMLAYACVTMLRWDCAQSQGAVGLAGVLLVALAVASGLGLCALLGITFNAATTQVLPFLALGIGVDDIFLLAHAFTKAPPDTPLPERMGECLRSTGTSVALTSVNNMVAFFMAALVPIPALRAFSLQAAIVVGCNFAAVMLVFPAILSLDLRRRHRQRLDVLCCFSSPCSAQVIQMLPQELGDRAVPVGIAHLTATVQAFTHCEASSQHVVTILPPQAHLLSPASDPLGSELYSPGGSTRDLLSQEEGTGPQAACRPLLCAHWTLAHFARYQFAPLLLQTRAKALVLLFFGALLGLSLYGATLVQDGLALTDVVPRGTKEHAFLSAQLRYFSLYEVALVTQGGFDYAHSQRALFDLHQRFSSLKAVLPPPATQAPRTWLHYYRSWLQGIQAAFDQDWASGRITCHSYRNGSEDGALAYKLLIQTGNAQEPLDFSQLTTRKLVDKEGLIPPELFYMGLTVWVSSDPLGLAASQANFYPPPPEWLHDKYDTTGENLRIPAAQPLEFAQFPFLLHGLQKTADFVEAIEGARAACTEAGQAGVHAYPSGSPFLFWEQYLGLRRCFLLAVCILLVCTFLVCALLLLSPWTAGLIVLVLAMMTVELFGIMGFLGIKLSAIPVVILVASIGIGVEFTVHVALGFLTSHGSRNLRAASALEQTFAPVTDGAVSTLLGLLMLAGSNFDFIIRYFFVVLTVLTLLGLLHGLLLLPVLLSILGPPPQVVQVYKESPQTLNSAAPQRGGLRWDRPPTLPQSFARVTTSMTVALHPPPLPGAYVHPASEEPT
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Plays a role in the control of cellular growth (By similarity). May have a role in epidermal development. May act as a receptor for Sonic hedgehog (SHH).
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O35598
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ADA10_MOUSE
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Disintegrin and metalloproteinase domain-containing protein 10 (ADAM 10) (EC 3.4.24.81) (Kuzbanian protein homolog) (Mammalian disintegrin-metalloprotease) (CD antigen CD156c)
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MVLPTVLILLLSWAAGLGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLLLDFHAHGRQFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIKTRGGTFYIEPAERYIKDRILPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEGARAHPEKHAASSGPELLRKKRTTLAERNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTSDEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDDCCFDANQPEGKKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAKEGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYDLEECTCASSDGKDDKELCHVCCMKKMAPSTCASTGSLQWSKQFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPQLYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPPRQRPRESYQMGHMRR
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Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (By similarity). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) at '687-Lys-|-Leu-688' (By similarity). Contributes to the normal cleavage of the cellular prion protein (By similarity). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (By similarity). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (By similarity). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3. Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA. Enhances the cleavage of CHL1 by BACE1. Cleaves NRCAM. Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (By similarity). Involved in the development and maturation of glomerular and coronary vasculature. During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions. May regulate the EFNA5-EPHA3 signaling (By similarity).
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O35599
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OPSG_MOUSE
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Medium-wave-sensitive opsin 1 (Green cone photoreceptor pigment) (Green-sensitive opsin) (M opsin) (Medium wavelength-sensitive cone opsin)
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MAQRLTGEQTLDHYEDSTHASIFTYTNSNSTKGPFEGPNYHIAPRWVYHLTSTWMILVVVASVFTNGLVLAATMRFKKLRHPLNWILVNLAVADLAETIIASTISVVNQIYGYFVLGHPLCVIEGYIVSLCGITGLWSLAIISWERWLVVCKPFGNVRFDAKLATVGIVFSWVWAAIWTAPPIFGWSRYWPYGLKTSCGPDVFSGTSYPGVQSYMMVLMVTCCIFPLSIIVLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMVFAYCLCWGPYTFFACFATAHPGYAFHPLVASLPSYFAKSATIYNPIIYVFMNRQFRNCILHLFGKKVDDSSELSSTSKTEVSSVSSVSPA
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Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May increase spectral sensitivity in dim light.
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O35600
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ABCA4_MOUSE
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Retinal-specific phospholipid-transporting ATPase ABCA4 (EC 7.6.2.1) (ATP-binding cassette sub-family A member 4) (RIM ABC transporter) (RIM protein) (RmP) (Retinal-specific ATP-binding cassette transporter)
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MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGLLPWLQGIFCNMNNPCFQNPTPGESPGTVSNYNNSILARVYRDFQELFMDTPEVQHLGQVWAELRTLSQFMDTLRTHPERFAGRGLQIRDILKDEEALTLFLMRNIGLSDSVAHLLVNSQVRVEQFAYGVPDLELTDIACSEALLQRFIIFSQRRGAQTVRDALCPLSQVTLQWIEDTLYADVDFFKLFHVLPTLLDSSSQGINLRFWGGILSDLSPRMQKFIHRPSVQDLLWVSRPLLQNGGPETFTQLMSILSDLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPAYSYDKRTTSFCNSLIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPAARRIMKNANSTFEELDRVRKLVKAWEEVGPQIWYFFEKSTQMTVIRDTLQHPTVKDFINRQLGEEGITTEAVLNFFSNGPQEKQADDMTSFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFPGMYPWASSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGIVKSQMQAEPPIGVYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKGIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMALSIFLLTLFIMHGRILHYSDPFILFLFLLAFATATIMQSFLLSTLFSKASLAAACSGVIYFTLYLPHVLCFAWQDRMTADLKTTVSLLSSVAFGFGTEYLVRFEEQGLGLQWSNIGKSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEEMEDPEHPEGMNDSFFERELPGLVPGVCVKNLVKVFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLIGGKDIETNLDVVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDSKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGGCEGVCSCTSKGFSTRCPTRVDEITEEQVLDGDVQELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDAGAGSMFVGGAQQKREQAGLRHPCSAPTEKLRQYAQAPHTCSPGQVDPPKGQPSPEPEDPGVPFNTGARLILQHVQALLVKRFHHTIRSRKDFVAQIVLPATFVFLALMLSIIVPPFGEFPALTLHPWMYGHQYTFFSMDEPNNEHLEVLADVLLNRPGFGNRCLKEEWLPEYPCINATSWKTPSVSPNITHLFQKQKWTAAHPSPSCKCSTREKLTMLPECPEGAGGLPPPQRTQRSTEVLQDLTNRNISDYLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPISGEALVGFLSGLGQMMNVSGGPVTREASKEMLDFLKHLETTDNIKVWFNNKGWHALVSFLNVAHNAILRASLPRDRDPEEYGITVISQPLNLTKEQLSDITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVTKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPDNLPALVSLLMLYGWAVIPMMYPASFLFEVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEYSANPFQWDLIGKNLVAMAIEGVVYFLLTLLIQHHFFLTRWIAEPAREPVFDEDDDVAEERQRVMSGGNKTDILKLNELTKVYSGSSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTSISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPSKEIEKVANWGIQSLGLSLYADRLAGTYSGGNKRKLSTAIALTGCPPLLLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGTFQCLGTIQHLKYKFGDGYIVTMKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHHSMLQFQVPSSSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYDLPLHPRAAGASWQAKLEEKSGRLQTQEPLPAGSEQLANGSNPTAAEDKHTRSPQ
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Flippase that catalyzes in an ATP-dependent manner the transport of retinal-phosphatidylethanolamine conjugates like the 11-cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine from the lumen to the cytoplasmic leaflet of photoreceptor outer segment disk membranes, where N-cis-retinylidene-phosphatidylethanolamine (N-cis-R-PE) is then isomerized to its all-trans isomer (N-trans-R-PE) and reduced by RDH8 to produce all-trans-retinol (all-trans-rol) and therefore prevents the accumulation of excess of 11-cis-retinal and its schiff-base conjugate and the formation of toxic bisretinoid. Displays both ATPase and GTPase activity that is strongly influenced by the lipid environment and the presence of retinoid compounds (By similarity). Binds the unprotonated form of N-retinylidene-phosphatidylethanolamine with high affinity in the absence of ATP and ATP binding and hydrolysis induce a protein conformational change that causes the dissociation of N-retinylidene-phosphatidylethanolamine (By similarity).
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O35601
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FYB1_MOUSE
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FYN-binding protein 1 (Adhesion and degranulation promoting adaptor protein) (ADAP) (FYB-120/130) (p120/p130) (FYN-T-binding protein) (SLAP-130) (SLP-76-associated phosphoprotein)
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MAKFNTGSNPTEEAATSSRPFKVAGQSSPSGIQSRKNLFDNQGNASPPAGPSSMPKFGTTKPPLAAKPTYEEKPEKEPKPPFLKPTGGSPRFGTQPNSVSRDPEVKVGFLKPVSPKPTSLTKEDSKPVVLRPPGNKLHNLNQESDLKTPGPKPGPAPPVPENELKPGFSKVAGAKSKFMPAAQDTDSKPRFPRHTFGQKPSLSTEDSQEENTSKNVPVQKGSPVQLGAKSKGAPFKPPKEDPEDKDHGAPSSPFPGVVLKPAASRGSPGLSKNFEEKKEDRKTDLAKNIFLNKLNQEEPARFPKAPSKLTAGTPWGQSQEKEGDKNSATPKQKALPPLSVLGPPPPKPNRPPNVDLTRFRKADSANSATKSQTPYSTTSLPPPPPTHPASQPPLPASHPAHPPVPSLPPRNIKPPLDLKHPINDENQDGVMHSDGTGNLEEEQESEGETYEDIDSSKERDKKREKEEKKRLELERKEQKEREKKEQELKKKFKLTGPIQVIHHAKACCDVKGGKNELSFKQGEDIEIIRITDNPEGKWLGRTARGSYGYIKTTAVEIDYDSLKRKKNSLNAVPPRLVEDDQDVYDDVAEQDAPNSHGQSGSGGMFPPPPTDDEIYDGIEEEDDDDGSVPQVDEKTNAWSWGILKMLKGKDDRKKSIREKPKVSESDNNEGSSLPSQHKQLDVGEEVYDDVDASDFPPPPAEMSQGMSVGRAKTEEKDPKKLKKQEKEEKDLRKKFKYDGEIRVLYSTKVASSLTSKKWGARDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVDNDGEIYDDIADGCIYDND
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Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (By similarity). Modulates the expression of IL2. Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2 (By similarity). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells.
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O35604
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NPC1_MOUSE
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NPC intracellular cholesterol transporter 1 (Niemann-Pick C1 protein)
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MGAHHPALGLLLLLLCPAQVFSQSCVWYGECGIATGDKRYNCKYSGPPKPLPKDGYDLVQELCPGLFFDNVSLCCDIQQLQTLKSNLQLPLQFLSRCPSCFYNLMTLFCELTCSPHQSQFLNVTATEDYFDPKTQENKTNVKELEYFVGQSFANAMYNACRDVEAPSSNEKALGLLCGRDARACNATNWIEYMFNKDNGQAPFTIIPVFSDLSILGMEPMRNATKGCNESVDEVTGPCSCQDCSIVCGPKPQPPPPPMPWRIWGLDAMYVIMWVTYVAFLFVFFGALLAVWCHRRRYFVSEYTPIDSNIAFSVNSSDKGEASCCDPLGAAFDDCLRRMFTKWGAFCVRNPTCIIFFSLAFITVCSSGLVFVQVTTNPVELWSAPHSQARLEKEYFDKHFGPFFRTEQLIIQAPNTSVHIYEPYPAGADVPFGPPLNKEILHQVLDLQIAIESITASYNNETVTLQDICVAPLSPYNKNCTIMSVLNYFQNSHAVLDSQVGDDFYIYADYHTHFLYCVRAPASLNDTSLLHGPCLGTFGGPVFPWLVLGGYDDQNYNNATALVITFPVNNYYNDTERLQRAWAWEKEFISFVKNYKNPNLTISFTAERSIEDELNRESNSDVFTVIISYVVMFLYISLALGHIQSCSRLLVDSKISLGIAGILIVLSSVACSLGIFSYMGMPLTLIVIEVIPFLVLAVGVDNIFILVQTYQRDERLQEETLDQQLGRILGEVAPTMFLSSFSETSAFFFGALSSMPAVHTFSLFAGMAVLIDFLLQITCFVSLLGLDIKRQEKNHLDILCCVRGADDGQGSHASESYLFRFFKNYFAPLLLKDWLRPIVVAVFVGVLSFSVAVVNKVDIGLDQSLSMPNDSYVIDYFKSLAQYLHSGPPVYFVLEEGYNYSSRKGQNMVCGGMGCDNDSLVQQIFNAAELDTYTRVGFAPSSWIDDYFDWVSPQSSCCRLYNVTHQFCNASVMDPTCVRCRPLTPEGKQRPQGKEFMKFLPMFLSDNPNPKCGKGGHAAYGSAVNIVGDDTYIGATYFMTYHTILKTSADYTDAMKKARLIASNITETMRSKGSDYRVFPYSVFYVFYEQYLTIIDDTIFNLSVSLGSIFLVTLVVLGCELWSAVIMCITIAMILVNMFGVMWLWGISLNAVSLVNLVMSCGISVEFCSHITRAFTMSTKGSRVSRAEEALAHMGSSVFSGITLTKFGGIVVLAFAKSQIFEIFYFRMYLAMVLLGATHGLIFLPVLLSYIGPSVNKAKRHTTYERYRGTERERLLNF
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Intracellular cholesterol transporter which acts in concert with NPC2 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment. Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1. Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket (By similarity). May play a role in vesicular trafficking in glia, a process that may be crucial for maintaining the structural and functional integrity of nerve terminals (Probable). Inhibits cholesterol-mediated mTORC1 activation throught its interaction with SLC38A9 (By similarity).
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O35607
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BMPR2_MOUSE
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Bone morphogenetic protein receptor type-2 (BMP type-2 receptor) (BMPR-2) (EC 2.7.11.30) (BRK-3) (Bone morphogenetic protein receptor type II) (BMP type II receptor) (BMPR-II)
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MTSSLHRPFRVPWLLWAVLLVSTTAASQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSFNRDETIIIALASVSVLAVLIVALCFGYRMLTGDRKQGLHSMNMMEAAAAEPSLDLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERLTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNDGACVISDFGLSMRLTGNRLVRPGEEDNAAISEVGTIRYMAPEVLEGAVNLRDCESALKQVDMYALGLIYWEVFMRCTDLFPGESVPDYQMAFQTEVGNHPTFEDMQVLVSREKQRPKFPEAWKENSLAVRSLKETIEDCWDQDAEARLTAQCAEERMAELMMIWERNKSVSPTVNPMSTAMQNERNLSHNRRVPKIGPYPDYSSSSYIEDSIHHTDSIVKNISSEHSMSSTPLTIGEKNRNSINYERQQAQARIPSPETSVTSLSTNTTTTNTTGLTPSTGMTTISEMPYPDETHLHATNVAQSIGPTPVCLQLTEEDLETNKLDPKEVDKNLKESSDENLMEHSLKQFSGPDPLSSTSSSLLYPLIKLAVEVTGQQDFTQAANGQACLIPDVPPAQIYPLPKQQNLPKRPTSLPLNTKNSTKEPRLKFGNKHKSNLKQVETGVAKMNTINAAEPHVVTVTMNGVAGRSHNVNSHAATTQYANGAVPAGQAANIVAHRSQEMLQNQFIGEDTRLNINSSPDEHEPLLRREQQAGHDEGVLDRLVDRRERPLEGGRTNSNNNNSNPCSEQDILTQGVTSTAADPGPSKPRRAQRPNSLDLSATNILDGSSIQIGESTQDGKSGSGEKIKRRVKTPYSLKRWRPSTWVISTEPLDCEVNNNGSDRAVHSKSSTAVYLAEGGTATTTVSKDIGMNCL
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On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is weak but enhanced by the presence of type I receptors for BMPs. Mediates induction of adipogenesis by GDF6.
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O35608
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ANGP2_MOUSE
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Angiopoietin-2 (ANG-2)
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MWQIIFLTFGWDLVLASAYSNFRKSVDSTGRRQYQVQNGPCSYTFLLPETDSCRSSSSPYMSNAVQRDAPLDYDDSVQRLQVLENILENNTQWLMKLENYIQDNMKKEMVEIQQNVVQNQTAVMIEIGTSLLNQTAAQTRKLTDVEAQVLNQTTRLELQLLQHSISTNKLEKQILDQTSEINKLQNKNSFLEQKVLDMEGKHSEQLQSMKEQKDELQVLVSKQSSVIDELEKKLVTATVNNSLLQKQQHDLMETVNSLLTMMSSPNSKSSVAIRKEEQTTFRDCAEIFKSGLTTSGIYTLTFPNSTEEIKAYCDMDVGGGGWTVIQHREDGSVDFQRTWKEYKEGFGSPLGEYWLGNEFVSQLTGQHRYVLKIQLKDWEGNEAHSLYDHFYLAGEESNYRIHLTGLTGTAGKISSISQPGSDFSTKDSDNDKCICKCSQMLSGGWWFDACGPSNLNGQYYPQKQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF
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Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (By similarity). Involved in the regulation of lymphangiogenesis.
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O35609
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SCAM3_MOUSE
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Secretory carrier-associated membrane protein 3 (Secretory carrier membrane protein 3)
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MAQSRDTGNPFPDSGELDNPFQDPAVIQHRPSQQYATLDVYNPFENREPPPAYEPPAPAPAPLPPPSAPSVQSSRKLSPTEPRNYGSYSTQASAAAATAELLKKQEELNRKAEELDRRERELQHVALGGAGTRQNNWPPLPSFCPVKPCFFQDISMEIPQEFQKTVSTMYYLWMCSTLALLLNFFACLARFCVDTGSGSGFGLSMLWLLLFTPCSFVCWYRPMYKAFRSDSSFNFFVFFFIFFVQDVFFVLQAIGIPGWGFSGWVTALVVVGSKPAVAVLMLLVALLFTGIAVLGIVMLKRIHSLYRQTGASFQKAQQEFAAGVFSNPAVRTAAANAAAGAAENAFRAP
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Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.
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O35613
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DAXX_MOUSE
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Death domain-associated protein 6 (Daxx)
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MATDDSIIVLDDDDEDEAAAQPGPSNLPPNPASTGPGPGLSQQATGLSEPRVDGGSSNSGSRKCYKLDNEKLFEEFLELCKTETSDHPEVVPFLHKLQQRAQSVFLASAEFCNILSRVLARSRKRPAKIYVYINELCTVLKAHSIKKKLNLAPAASTTSEASGPNPPTEPPSDLTNTENTASEASRTRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSSYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGLDTFPDYGDVLRAVEKAATRHSLGLPRQQLQLLAQDAFRDVGVRLQERRHLDLIYNFGCHLTDDYRPGVDPALSDPTLARRLRENRTLAMNRLDEVISKYAMMQDKTEEGERQKRRARLLGTAPQPSDPPQASSESGEGPSGMASQECPTTSKAETDDDDDDDDDDDEDNEESEEEEEEEEEEKEATEDEDEDLEQLQEDQGGDEEEEGGDNEGNESPTSPSDFFHRRNSEPAEGLRTPEGQQKRGLTETPASPPGASLDPPSTDAESSGEQLLEPLLGDESPVSQLAELEMEALPEERDISSPRKKSEDSLPTILENGAAVVTSTSVNGRVSSHTWRDASPPSKRFRKEKKQLGSGLLGNSYIKEPMAQQDSGQNTSVQPMPSPPLASVASVADSSTRVDSPSHELVTSSLCSPSPSLLLQTPQAQSLRQCIYKTSVATQCDPEEIIVLSDSD
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Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs) the process is independent of ATRX and facilitated by ASF1A PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (By similarity).
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O35615
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FOG1_MOUSE
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Zinc finger protein ZFPM1 (Friend of GATA protein 1) (FOG-1) (Friend of GATA 1) (Zinc finger protein multitype 1)
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MSRRKQSNPRQIKRSLRDMEAGEEAKAMDSSPKEQEAPDPEAPAIEEPPSPPREDVSPPAVPAPPESPEDPEDMEGQELEMRPQDEEKEEKEEEAAMASPWSGPEELELALQDGQRCVRARLSLTEGLSWGPFYGSIQTRALSPEREEPGPAVTLMVDESCWLRMLPQVLTEEAANSEIYRKDDALWCRVTKVVPSGGLLYVRLVTEPHGAPRHPVQEPVEPGGLAPVHTDIQLLPQQAGMASILATAVINKDVFPCKDCGIWYRSERNLQAHLLYYCASRQRAGSPVSATEEKPKETYPNERVCPFPQCRKSCPSASSLEIHMRSHSGERPFVCLICLSAFTTKANCERHLKVHTDTLSGVCHNCGFISTTRDILYSHLVTNHMVCQPGSKGEIYSPGAGHPAAKLPPDSLAGFQQHSLMHSPLVPADKAPTPSSGLDSKAEVTNGETRVPPQNGGSSESPAAPRTIKVEAAEEPEATRASGPGEPGPQAPSRTPSPHSPNPVRVKTELSSPTPGSSPGPGELTMAGTLFLPQYVFSPDAGTTTVPTAPQASEILAKMSELVHNRLQQGAGSSGAAGTPTGLFSGTKGATCFECEITFNNINNFYVHKRLYCSGRRAPEDPPTVRRPKAATGPARAPAGAAAEPDPSRSSPGPGPREEEASGTTTPEAEAAGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHETYTVHKRYYCASRHDPPPRRPPAPTTAPGPAAPALTAPPVRTRRRRKLYELPAAGAPPPAAGPAPVPVVPSPTAELPSSPRPGSASAGPAPALSPSPVPDGPIDLSKRPRRQSPDAPTALPALADYHECTACRVSFHSLEAYLAHKKYSCPAAPLRTTALCPYCPPNGRVRGDLVEHLRQAHGLQVAKPAASPGAEPRTPAERAPRDSPDGRAPRSPSPAPENTPSDPADQGARTPSKGPPAPAPAPGGGGGHRYCRLCNIRFSSLSTFIAHKKYYCSSHAAEHVK
|
Transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. The heterodimer formed with GATA proteins is essential to activate expression of genes such as NFE2, ITGA2B, alpha- and beta-globin, while it represses expression of KLF1. May be involved in regulation of some genes in gonads. May also be involved in cardiac development, in a non-redundant way with ZFPM2/FOG2.
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O35618
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MDM4_MOUSE
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Protein Mdm4 (Double minute 4 protein) (Mdm2-like p53-binding protein) (Protein Mdmx) (p53-binding protein Mdm4)
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MTSHSTSAQCSASDSACRISSEQISQVRPKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLLGCQSFSVKDPSPLYDMLRKNLVTSASINTDAAQTLALAQDHTMDFPSQDRLKHGATEYSNPRKRTEEEDTHTLPTSRHKCRDSRADEDLIEHLSQDETSRLDLDFEEWDVAGLPWWFLGNLRNNCIPKSNGSTDLQTNQDIGTAIVSDTTDDLWFLNETVSEQLGVGIKVEAANSEQTSEVGKTSNKKTVEVGKDDDLEDSRSLSDDTDVELTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSNITAIPEKKDNEGIDVPDCRRTISAPVVRPKDGYLKEEKPRFDPCNSVGFLDLAHSSESQEIISSAREQTDIFSEQKAETESMEDFQNVLKPCSLCEKRPRDGNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIKVFIA
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Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. The short isoform is a more potent inhibitor of TP53 activity than the long isoform.
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O35621
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PMM1_MOUSE
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Phosphomannomutase 1 (PMM 1) (EC 5.4.2.8)
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MAVAVEGARRKERILCLFDVDGTLTPARQKIDPEVSAFLQKLRSRVQIGVVGGSDYSKIAEQLGEGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYMALLRLPKKRGTFIEFRNGMLNVSPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDEDSFDIIHFFGNETSPGGNDFEIYADPRTVGHSVVSPQDTVQRCRELFFPETAHEA
|
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.
|
O35622
|
FGF15_MOUSE
|
Fibroblast growth factor 15 (FGF-15)
|
MARKWNGRAVARALVLATLWLAVSGRPLAQQSQSVSDEDPLFLYGWGKITRLQYLYSAGPYVSNCFLRIRSDGSVDCEEDQNERNLLEFRAVALKTIAIKDVSSVRYLCMSADGKIYGLIRYSEEDCTFREEMDCLGYNQYRSMKHHLHIIFIQAKPREQLQDQKPSNFIPVFHRSFFETGDQLRSKMFSLPLESDSMDPFRMVEDVDHLVKSPSFQK
|
Involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression.
|
O35625
|
AXIN1_MOUSE
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Axin-1 (Axis inhibition protein 1) (Protein Fused)
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MNVQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDSRPVNHSFCSGKGTSIKSETSTATPRRSDLDLGYEPEGSASPTPPYLRWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACSGFRKLEPCDSNEEKRLKLARAIYRKYILDSNGIVSRQTKPATKSFIKDCVMKQQIDPAMFDQAQTEIQSTMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGMSGYLPTLNEDEEWKCDQDADEDDGRDPLPPSRLTQKLLLETAAPRAPSSRRYNEGRELRYGSWREPVNPYYVNSGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESIQVNGRVPLPHIPRTYRMPKEIRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGEMPSGPMASHKLPSVPAWHHFPPRYVDMGCSGLRDAHEENPESILDEHVQRVMRTPGCQSPGPGHRSPDSGHVAKTAVLGGTASGHGKHVPKLGLKLDTAGLHHHRHVHHHVHHNSARPKEQMEAEVARRVQSSFSWGPETHGHAKPRSYSENAGTTLSAGDLAFGGKTSAPSKRNTKKAESGKNANAEVPSTTEDAEKNQKIMQWIIEGEKEISRHRKAGHGSSGLRKQQAHESSRPLSIERPGAVHPWVSAQLRNSVQPSHLFIQDPTMPPNPAPNPLTQLEEARRRLEEEEKRANKLPSKQRYVQAVMQRGRTCVRPACAPVLSVVPAVSDLELSETETKSQRKAGGGSAPPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAVLPVFEEKIIGKVEKVD
|
Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). Controls dorsoventral patterning via two opposing effects down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (By similarity). Also a component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.
|
O35626
|
RASD1_MOUSE
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Dexamethasone-induced Ras-related protein 1
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MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLKQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVEQREIEQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGDHGDAFGILAPFARRPSVHSDLMYIREKTSVGSQAKDKERCVIS
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Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity).
|
O35627
|
NR1I3_MOUSE
|
Nuclear receptor subfamily 1 group I member 3 (Constitutive androstane receptor) (CAR) (Orphan nuclear receptor MB67)
|
MTAMLTLETMASEEEYGPRNCVVCGDRATGYHFHALTCEGCKGFFRRTVSKTIGPICPFAGRCEVSKAQRRHCPACRLQKCLNVGMRKDMILSAEALALRRARQAQRRAEKASLQLNQQQKELVQILLGAHTRHVGPMFDQFVQFKPPAYLFMHHRPFQPRGPVLPLLTHFADINTFMVQQIIKFTKDLPLFRSLTMEDQISLLKGAAVEILHISLNTTFCLQTENFFCGPLCYKMEDAVHAGFQYEFLESILHFHKNLKGLHLQEPEYVLMAATALFSPDRPGVTQREEIDQLQEEMALILNNHIMEQQSRLQSRFLYAKLMGLLADLRSINNAYSYELQRLEELSAMTPLLGEICS
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Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element (By similarity). {ECO:0000250, ECO:0000269|PubMed:10462436}.
|
O35632
|
HYAL2_MOUSE
|
Hyaluronidase-2 (Hyal-2) (EC 3.2.1.35) (Hyaluronoglucosaminidase-2)
|
MRAGLGPIITLALVLEVAWAGELKPTAPPIFTGRPFVVAWNVPTQECAPRHKVPLDLRAFDVKATPNEGFFNQNITTFYYDRLGLYPRFDAAGTSVHGGVPQNGSLCAHLPMLKESVERYIQTQEPGGLAVIDWEEWRPVWVRNWQEKDVYRQSSRQLVASRHPDWPSDRVMKQAQYEFEFAARQFMLNTLRYVKAVRPQHLWGFYLFPDCYNHDYVQNWESYTGRCPDVEVARNDQLAWLWAESTALFPSVYLDETLASSVHSRNFVSFRVREALRVAHTHHANHALPVYVFTRPTYTRGLTGLSQVDLISTIGESAALGSAGVIFWGDSEDASSMETCQYLKNYLTQLLVPYIVNVSWATQYCSWTQCHGHGRCVRRNPSANTFLHLNASSFRLVPGHTPSEPQLRPEGQLSEADLNYLQKHFRCQCYLGWGGEQCQRNYKGAAGNASRAWAGSHLTSLLGLVAVALTWTL
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Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R (By similarity).
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