P97881
uniprot
P97881
canonical
amino_acid_sequence
MSQSSGGTSTPTTTATQPTSTSTQTPGTTQLLSTTSTPTTTATQPTSTSTQTPGTTQLPSTTSTPTTTATQPTXTSTQTPGTTQLPGTTSTPTTTATQPTSTSFQTPGTTQLPSSTSTPTTTATQPTSTASQTPGTTQPPGGASSPTTTVTQPTGSSSQTPGTTQPPGGASTPTTTVTQPTGSSSQTSGTTQPPGGASSSTVTSSSSTGSNDPCNSNPCKSPASCVKLYDSYFCLCLEGYYYNNSSSCVKGTTFPGEIGMSVNETTDLEDKNSVNYQTLHSSVVKFFENTFKKTDYGQTVILKVSKDSLMSSRSVMRAATQTVYVSVVNMFGENTKEDEESVASVIKEAVKTDNNVERYFQQDRCDYYGCVKSGSNVCRNGLQCTCKPGLERLNPQVPFCVAPTCSEPCSAEKKQLCLKKDNGAMECGCMAGYRKANGKCEECPFGYSGMDCKDQFQLILTIVGTIAGAFILILLIVFIVSMRSKNKKKSGEEQNLIEDDFHNLRMRPTGFSNFGADTSIFPKVKTGVPSQTSNPYANHRSMPRPDY
uniprot
proteins
function
FUNCTION: Epithelial and hemopoietic transmembrane mucin that may play a role in cell signaling.
uniprot
proteins
mass_dalton
57652
uniprot
proteins
post_translational_modification
PTM: Cleaved into two subunits, alpha and beta, probably between the first EGF domain and the SEA domain. Beta subunit contains the cytoplasmic tail and alpha subunit the extracellular tail. The homooligomerization into dimers is dependent on intrachain disulfide bonds (By similarity). {ECO:0000250}.; PTM: Highly glycosylated. {ECO:0000250}.
uniprot
proteins
sequence_length
547
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000250}. Note=Also exists as a soluble form. {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 459..479; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins