Peptide Sequence

ANSLLEETKQGNLERECIEELCNKEEAREVFENDPETDYFYPKYLVCLRSFQTGLFTAARQSTNAYPDLRSCVNAIPDQC SPLPCNEDGYMSCKDGKASFTCTCKPGWQGEKCEFDINECKDPSNINGGCSQICDNTPGSYHCSCKNGFVMLSNKKDCKD VDECSLKPSICGTAVCKNIPGDFECECPEGYRYNLKSKSCEDIDECSENMCAQLCVNYPGGYTCYCDGKKGFKLAQDQKS CEVVSVCLPLNLDTKYELLYLAEQFAGVVLYLKFRLPEISRFSAEFDFRTYDSEGVILYAESIDHSAWLLIALRGGKIEV QLKNEHTSKITTGGDVINNGLWNMVSVEELEHSISIKIAKEAVMDINKPGPLFKPENGLLETKVYFAGFPRKVESELIKP INPRLDGCIRSWNLMKQGASGIKEIIQEKQNKHCLVTVEKGSYYPGSGIAQFHIDYNNVSSAEGWHVNVTLNIRPSTGTG VMLALVSGNNTVPFAVSLVDSTSEKSQDILLSVENTVIYRIQALSLCSDQQSHLEFRVNRNNLELSTPLKIETISHEDLQ RQLAVLDKAMKAKVATYLGGLPDVPFSATPVNAFYNGCMEVNINGVQLDLDEAISKHNDIRAHSCPSVWKKTKNS

Selected 3D Structures

PDB Id: 1z6c

Post-translational Modification

Glutamic acid residues at positions 6,7,14,16,19,20,25,26,29,32 and 36 are 4-carboxyglutamate; asparagine residues at positions 458 and 489 are N-linked glycosylated, and disulphide bonds are formed between cysteine residues at positions 164 and 176, 171 and 185, 187 and 200, 206 and 215, 211 and 224 and 226 and 241. Predicted (3R)-3-hydroxyaspartate formationfrom aspartate residue at positiomn 195; predicted N-linked glycosylation of asparagine residue at position 465. Predicted disulphide bond formation between cysteine resdiues at positions 17 and 22, 80 and 93, 85 and 102, 104 and 113, 120 and 144, 130 and 143, 145 and 158, 408 and 434, and 598 and 625