Search by BoMiProt ID - Bomi115


Primary Information

BoMiProt ID Bomi115
Protein Name Conglutinin
Organism Bos taurus
Uniprot IdP23805
Milk FractionWhey
Ref Sequence Id NP_783630.2
Amino Acid Lenth 371
Molecular Weight 37995
Fasta Sequence https://www.uniprot.org/uniprot/P23805.fasta
Gene Name CGN1
Gene Id 281068
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Protein Function conglutinin in the serum of dairy cows depends on many factors such as breeding, the season of the year, the stage of the reproductive cycle and infection
Biochemical Properties Conglutinin contain 4 trimeric units; there are 7 cysteine residues present which are capable of forming inter – and/or intramolecular disulfide bridges; The collagen- like region of conglutinin contains eight hydroxylysine residues, which are possible glycosylation sites; conglutinin molecules adhere to each other in the central lob region, forming rosette-like aggregates
Significance in milk effector molecules in innate immunity; . Conglutinin does not appear in the serum of calves until after it has received colostrum; then its concentration gradually increases up to the 80th week of life, when it reaches the level characteristic for adult cattle
PTMs presence of O-linked glycans of β(1-3)-GalNAc and α-(2-3) linked sialic acid type. No N-linked glycans were detected
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P23805|CONG_BOVIN Conglutinin OS=Bos taurus OX=9913 GN=CGN1 PE=1 SV=2
MLLLPLSVLLLLTQPWRSLGAEMTTFSQKILANACTLVMCSPLESGLPGHDGQDGRECPH GEKGDPGSPGPAGRAGRPGWVGPIGPKGDNGFVGEPGPKGDTGPRGPPGMPGPAGREGPS GKQGSMGPPGTPGPKGETGPKGGVGAPGIQGFPGPSGLKGEKGAPGETGAPGRAGVTGPS GAIGPQGPSGARGPPGLKGDRGDPGETGAKGESGLAEVNALKQRVTILDGHLRRFQNAFS QYKKAVLFPDGQAVGEKIFKTAGAVKSYSDAEQLCREAKGQLASPRSSAENEAVTQMVRA QEKNAYLSMNDISTEGRFTYPTGEILVYSNWADGEPN*337NSDEGQPENCVEIFPDGKWNDVP CSKQLLVICEF
Bibliography 1. Dec, M., & Wernicki, A. (2006). Conglutinin, CL-43 and CL-46--three bovine collectins. Polish Journal of Veterinary Sciences, 9(4), 265–275. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/17203746.
2. Andersen, O., Nielsen, E. H., Storgaard, P., Højrup, P., Friis, P., Leslie, G., & Svehag, S. E. (n.d.). Biochemical and ultrastructural studies of the C-type lectin bovine conglutinin. Journal of Structural Biology, 109(3), 201–207. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1296754.