Primary Information |
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| BoMiProt ID | Bomi4813 |
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| Protein Name | Collagen alpha-1(XVII) chain/180 kDa bullous pemphigoid antigen 2/Bullous pemphigoid antigen 2 |
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| Organism | Bos taurus |
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| Uniprot ID | A6QPB3 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001095450.1 |
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| Aminoacid Length | 1473 |
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| Molecular Weight | 149154 |
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| FASTA Sequence |
Download |
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| Gene Name | COL17A1/BP180/BPAG2 |
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| Gene ID | 513804 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | a critical molecule for hair follicle stem cell (HFSC) maintenance.promote the formation of multilayered, transformed epithelia |
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| 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. |
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| PTMs | Glycosylation,Disulfide bond,Hydroxylation |
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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
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH; (474-496) |
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| 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. |
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| 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 |
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| 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. |
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