Search by BoMiProt ID - Bomi4813


Primary Information

BoMiProt ID Bomi4813
Protein Name Collagen alpha-1(XVII) chain/180 kDa bullous pemphigoid antigen 2/Bullous pemphigoid antigen 2
Organism Bos taurus
Uniprot IdA6QPB3
Milk FractionWhey
Ref Sequence Id NP_001095450.1
Aminoacid Length 1473
Molecular Weight 149154
Fasta Sequence https://www.uniprot.org/uniprot/A6QPB3.fasta
Gene Name COL17A1/BP180/BPAG2
Gene Id 513804
Protein Existence Status reviewed

Secondary Information

Protein Function a critical molecule for hair follicle stem cell (HFSC) maintenance.promote the formation of multilayered, transformed epithelia
Biochemical Properties The cDNA sequence of collagen XVII encodes a type II integral transmembrane protein of 1497 amino acid residues.Structural component of hemidesmosomes,180-kDa bullous pemphigoid antigen (BP180), is a transmembrane protein.Collagen XVII exists in two molecular forms,i.e. as a full-length transmembrane homotrimer of three 180-kDa α1(XVII) chains and as a 120-kDa soluble form. The latter corresponds to the extracellular domain and is presumably released from the cell surface by furin-mediated proteolytic processing.Higher content of hydroxyproline residues in the C-terminal region.39 amino acid residues (positions 471–509) close to the transmembrane region can form a three-stranded coiled-coil that may play a role in assembly.
PTMs Glycosylation,Disulfide bond,Hydroxylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|A6QPB3|COHA1_BOVIN Collagen alpha-1(XVII) chain OS=Bos taurus OX=9913 GN=COL17A1 PE=2 SV=1 MDITQKNKRDGTEVTERIITETVTTRLTSLPPKGGTSNGYAKTGSLGGGSRLEKQSLTHG SSGYINSSGSLRGNASTSSYRRAHSPASTLPNSPGSTFERKTHVTRHGTYEGSSSGNSSP EYPRKEFASSSTRGRSQTRESEIRVRLQSASPSTRWTELDDVKRLLKGSRSASVSPTRNS SNTLPIPKKGTVETKVVTASSQSVSGTYDTTILDANLPSHVWSSTLPAGSSMGTYHNNIT TQSSSLLNTNAYSAGSVFGVPNNMASCSATLQPGISTSSSVFGMQNNLAPSSSTLSHGMA ATSTAYGVKKNMPQSPTAVSTGVSTSAASTTNVQNDDLLHKDCKFLILEKDNTPAKKEME LLIMTKDSGKVFTASPASVAATSFSEDTLKKEKQAAYTDTYLVSEANGDVKTVTAKGNGA SADIHGYDHRRGGGGGGGSGGALGSGAAGGGGKGSWGAAPTWCPCGSWCSWWKWLLGLLL TWLLLLGLLFGLIALAEEVRKLKARVEELEKMRGRLSYNEKMERSSQDSVQGVAPRLGEG LGKSELDDYNLEDVWQFMKVRLMTEQENGNLRGSPGPKGDMGVQGPKGDRGFPGTPGIPG PLGHQGPEGPKGQKGNVGEPGMEGPMGQRGREGPMGPRGEPGPPGFGEKGDRGDAGKPGI PGPPGVPGSVGPKGSIGPQGLRGEVGLPGIKGDKGPMGPPGPKGDQGEKGPRGLTGEPGL KGLPGAVGEPGAKGAMGPAGPDGHQGPRGEQGLPGMPGTRGLPGPSGDPGKPGLTGPQGP QGIPGTPGRPGVKGEPGAPGKIMTSEGSSTITVPGPPGPPGAMGPPGPPGAPGPVGPAGL PGQQGPRGEPGLAGESFMGSSSSFSEVLSTQGIDLRGPPGPPGPPGPPGEGLPGPPGPPG SLLTSSETFFSGPPGPPGPPGPKGDQGPPGPRGHQGERGFPGLSGSGSSSLGLNLQGPPG PPGPQGPKGDKGDPGVPGAPGIPGGPSRGGSSSSTTFMQGPPGPPGPPGPPGSLSSSGLE IQQYISDYMQSDSIRPYLSGVQGPPGPPGPPGPVTTITGETFNYSELASLVVSYLQTSGY NIGTSSTSISSEDILAALRRDDVRQYLQQYLMPQGAGGDWFLQSLDYAELSNRILSYMSS TGVSIGLPGPPGPPGLPGTSYEELLSLLQGSEFRGIVGPPGPPGPPGLPGSSWSSISTED LSSYLQTAGLSSIPGPPGPPGPPGPRGPPGISGALATYAAENSDSFRSELISYLTSPDVR SFIVGPPGPPGPQGPPGDTRLVSTDSSYSRSGSSSSFSRDTSYSSSMGIGGASGGSLGEA GAFGMDMGRGYGAAAESGMYGGNGRFGTSFAGGLDYNELAVRVSESLQRQGLLQGMAYTV QGPPGRPGPQGPPGISKIFSAYSN*1404VTEDLMDFFRTYGAIPGPPGQKGEMGIPGPKGERGP AGPPGPRGHKGEKGDKGDQFYIGRRRRSIAVKP
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction 1TMH; (474-496)
Significance of PTMs During biosynthesis, collagen acquires a number of post-translational modifications, including lysine modifications, that are critical to the structure and biological functions of this protein.Specific hydroxylysine residues located in the helical domain of the molecule are glycosylated by the addition of galactose or glucose-galactose.
Additional Comments Mutations in the collagen XVII gene,COL17A1, lead to junctional epidermolysis bullosa, a hereditary blistering skin disease with epidermal detachment from the basement membrane
Bibliography 1.Yamauchi M, Sricholpech M. Lysine post-translational modifications of collagen. Essays Biochem. 2012;52:113-33. doi: 10.1042/bse0520113. PMID: 22708567; PMCID: PMC3499978. 2.Areida SK, Reinhardt DP, Muller PK, Fietzek PP, Kowitz J, Marinkovich MP, Notbohm H. Properties of the collagen type XVII ectodomain. Evidence for n- to c-terminal triple helix folding. J Biol Chem. 2001 Jan 12;276(2):1594-601. doi: 10.1074/jbc.M008709200. PMID: 11042218.