Q9QYP1
uniprot
Q9QYP1
canonical
amino_acid_sequence
MRRWWGALLLGALLCAHGTASNLECACGRSHFTCAVSALGECTCIPAQWQCDGDNDCGDHSDEDGCTLPTCSPLDFHCDNGKCIRRSWVCDGDNDCEDDSDEQDCPPRECEEDEFPCQNGYCIRSLWHCDGDNDCGDNSDEQCDMRKCSDKEFRCSDGSCIAEHWYCDGDTDCKDGSDEESCPSAVPSPPCNLEEFQCAYGRCILDIYHCDGDDDCGDWSDESDCSSHQPCRSGEFMCDSGLCVNAGWRCDGDADCDDQSDERNCTTSMCTAEQFRCRSGRCVRLSWRCDGEDDCADNSDEENCENTGSPQCASDQFLCWNGRCIGQRKLCNGVNDCGDNSDESPQQNCRPRTGEENCNVNNGGCAQKCQMIRGAVQCTCHTGYRLTEDGRTCQDVNECAEEGYCSQGCTNSEGAFQCWCEAGYELRPDRRSCKALGPEPVLLFANRIDIRQVLPHRSEYTLLLNNLENAIALDFHHRRELVFWSDVTLDRILRANLNGSNVEEVVSTGLESPGGLAVDWVHDKLYWTDSGTSRIEVANLDGAHRKVLLWQSLEKPRAIALHPMEGTIYWTDWGNTPRIEASSMDGSGRRIIADTHLFWPNGLTIDYAGRRMYWVDAKHHVIERANLDGSHRKAVISQGLPHPFAITVFEDSLYWTDWHTKSINSANKFTGKNQEIIRNKLHFPMDIHTLHPQRQPAGKNRCGDNNGGCTHLCLPSGQNYTCACPTGFRKINSHACAQSLDKFLLFARRMDIRRISFDTEDLSDDVIPLADVRSAVALDWDSRDDHVYWTDVSTDTISRAKWDGTGQKVVVDTSLESPAGLAIDWVTNKLYWTDAGTDRIEVANTDGSMRTVLIWENLDRPRDIVVEPMGGYMYWTDWGASPKIERAGMDASNRQVIISSNLTWPNGLAIDYGSQRLYWADAGMKTIEFAGLDGSKRKVLIGSQLPHPFGLTLYGQRIYWTDWQTKSIQSADRLTGLDRETLQENLENLMDIHVFHRQRPPVTTPCAVENGGCSHLCLRSPSPSGFSCTCPTGINLLLDGKTCSPGMNSFLIFARRIDVRMVSLDIPYFADVVVPINMTMKNTIAIGVDPLEGKVYWSDSTLHRISRASLDGSQHEDIITTGLQTTDGLAVDAIGRKVYWTDTGTNRIEVGNLDGSMRKVLVWQNLDSPRAIVLYHEMGFMYWTDWGENAKLERSGMDGSDRTVLINNNLGWPNGLTVDKTSSQLLWADAHTERIEVADLNGANRHTLVSPVQHPYGLTLLDSYIYWTDWQTRSIHRADKSTGSNVILVRSNLPGLMDIQAVDRAQPLGFNKCGSRNGGCSHLCLPRPSGFSCACPTGIQLKGDGKTCDPSPETYLLFSSRGSIRRISLDTDDHTDVHVPVPGLNNVISLDYDSVDGKVYYTDVFLDVIRRADLNGSNMETVIGHGLKTTDGLAVDWVARNLYWTDTGRNTIEASRLDGSCRKVLINNSLDEPRAIAVFPRKGYLFWTDWGHIAKIERANLDGSERKVLINADLGWPNGLTLDYDTRRIYWVDAHLDRIESADLNGKLRQVLVSHVSHPFALTQQDRWIYWTDWQTKSIQRVDKYSGRNKETVLANVEGLMDIIVVSPQRQTGTNACGVNNGGCSHLCFARASDFVCACPDEPDSHPCSLVPGLMPPAPRATSLNEKSPVLPNTLPTTLHSSTTRTRTSPEGAEGRCSERDAQLGLCAHSNEAVPAAPGEGLHVSYAVGGLLSVLLILLVTAALMLYRHRKSKFTDPGMGNLTYSNPSYRTSTQEVKIEAAPKPAMYNQLCYKKEGGPDHSYTKEKIKIVEGIHLLAGHDAEWGDLKQLRSSRGGLLRDHVCMKTDTVSIQASSGSLDDTETEQLLQEEQSECSSVHTATTPERRGSLPDTGWKHERKLSSESQV
uniprot
proteins
function
FUNCTION: Mediates SOST-dependent inhibition of bone formation (By similarity). Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling (By similarity). Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recruits it to the MUSK signaling complex. Mediates the AGRIN-induced phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Alternatively, may be involved in the negative regulation of the canonical Wnt signaling pathway, being able to antagonize the LRP6-mediated activation of this pathway. More generally, has been proposed to function as a cell surface endocytic receptor binding and internalizing extracellular ligands for degradation by lysosomes. Plays an essential role in the process of digit differentiation. {ECO:0000250|UniProtKB:Q8VI56}.
uniprot
proteins
mass_dalton
211880
uniprot
proteins
post_translational_modification
PTM: N-glycosylation is required for cell surface location. {ECO:0000250|UniProtKB:Q8VI56}.
uniprot
proteins
protein_family
LDLR family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
18848351
uniprot
proteins
pubmed
9693030
uniprot
proteins
sequence_length
1905
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VI56}; Single-pass type I membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 1724..1746; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins