Primary Information |
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| BoMiProt ID | Bomi4817 |
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| Protein Name | Collagen alpha-2(XI) chain |
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| Organism | Bos taurus |
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| Uniprot ID | Q32S24 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001039664.1 |
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| Aminoacid Length | 1736 |
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| Molecular Weight | 172238 |
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| FASTA Sequence |
Download |
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| Gene Name | COL11A2 |
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| Gene ID | 515435 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | Shows interaction of collagen fibrils with other molecules of the extracellular matrix and more specifically with sulfated glycosaminoglycan chains or with hyaluronan. Such interactions may play a key role in establishing both the organization of the collagen fibrils within the extracellular matrix and in limiting the diameter of collagen fibrils. |
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| Biochemical Properties | Collagen type XI is a component of hyaline cartilage consisting of alpha 1(XI), alpha 2(XI), and alpha 3(XI) chains; with 5-10% of the total collagen content, it is a minor but significant component next to type II collagen |
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| PTMs | Disulfide bond formation, Glycosylation at Asn, Hydroxylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q32S24|COBA2_BOVIN Collagen alpha-2(XI) chain OS=Bos taurus OX=9913 GN=COL11A2 PE=3 SV=1
MERCSRCHHLLLLVLLLLWLSAAPAWAGTAPVDVLRALRFPALPDGVRRARGICPADVAY
RVSRPAQLSAPTRQLFPGGFPKDFSLLTAVRARPGLQAPLLTLYSAQGVRQLGLELGRPV
RFLYEDQTGRPQPPAQPVFRGLSLADGKWHRVAVAVKGQSVTLIIDCKKRVTRPLPRSAR
PVLDTRGVIIFGARILDEEVFEGDIQELSIIPGVQAAYESCDQKELECEGGWRERPQRQP
SHRTQRSPKQQPPRLHRPQNQEPQAQSTESLYYDYEPPYYDVMTTGTTPDYQDPTPGEEE
GILESSPLPPPEEEQTDLQVPPTADRFLTEEYGEGGTEPPAGPYDYTYAYGDDYHEETEL
GPALSAETARSEAAARGPRGLKGEKGEPAVLEPGMLVEGPPGPEGPAGFPGPPGIQGNPG
PVGDPGERGPPGRAGLPGSDGAPGPPGTSLMLPFRFGSGGGDKGPVVAAQEAQAQAILQQ
ARVALRGPPGPMGYTGRPGPLGQPGSPGMKGESGDLGPQGPRGPQGLMGPPGKAGRRGRA
GADGARGMPGEPGVKGDRGFDGLPGLPGEKGHRGDTGAQGLPGPPGEDGERGDDGEIGPR
GLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPHGPKGSLGPQGEPGPPGQQGTPGTQGLP
GPQGAIGPHGEKGPRGKPGLPGMPGSDGPPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPR
GIKGVDGIRGLKGHKGEKGEDGFPGFKGDMGVKGDRGEVGVPGSRGEDGPEGPKGRTGPT
GDPGPPGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGER
GPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPPGPPGKD
GLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGAAGETGPMGERGHPGPPGPPGEQGLTGTA
GKEGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPAGPPGPAGSPGER
GSAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVA
GEDGDKGEVGDPGQKGAKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAK
GDEGTRGFNGPPGPIGLQGLPGPSGEKGETGDVGPMGPPGPPGPRGPAGPNGADGPQGPP
GGVGNLGPPGEKGEPGESGSPGVQGEPGVKGPRGERGEKGETGQAGEAGPPGPKGPTGDD
GPKGNPGPVGFPGDPGPPGEVGPRGQDGAKGDRGEDGEPGQPGSPGPTGENGPPGPLGKR
GPAGTPGPEGRQGEKGAKGDPGAVGAPGKTGPVGPAGPAGKPGPDGLRGLPGSVGQQGRP
GATGQAGPPGPVGPPGLPGLRGDTGAKGEKGHPGLIGLIGPPGEQGEKGDRGLPGPQGST
GQKGETGIPGASGPIGPGGPPGLPGPAGPKGAKGATGPAGPKGEKGVQGPPGHPGPPGEV
IQPLPIQMPKKTRRSVDGSRLMQEDEAVPTGGAPGSPGGLEEIFGSLDSLREEIEQMRRP
MGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCN*1604FTAGGETCVTPRDDVT
QFSYVDSEGAPVGVVQLTFLRLLSVSARQN*1650ISYPCSGEAQDSPLKLRGANEDELSPETSP
YIKEIRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSELGAPPRRGGVLLGPVCFMG
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH-(7-29) |
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| Additional Comments | The alpha 2(XI) chain was assumed to be the same length as the alpha 1(XI). One intermediate was identified from the alpha 2(XI) chain and with starting position at residue 495, and three from the alpha 3(XI) with starting positions at residues 519, 585, and 618. |
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| Bibliography | 1.Swoboda B, Holmdahl R, Stöss H, von der Mark K. Cellular heterogeneity in cultured human chondrocytes identified by antibodies specific for alpha 2(XI) collagen chains. J Cell Biol. 1989 Sep;109(3):1363-9. doi: 10.1083/jcb.109.3.1363. PMID: 2670958; PMCID: PMC2115754.Zhidkova NI, Justice SK, Mayne R. Alternative mRNA processing occurs in the variable region of the pro-alpha 1(XI) and pro-alpha 2(XI) collagen chains. J Biol Chem. 1995 Apr 21;270(16):9486-93. doi: 10.1074/jbc.270.16.9486. PMID: 7721876. 3.Morris NP, Watt SL, Davis JM, Bächinger HP. Unfolding intermediates in the triple helix to coil transition of bovine type XI collagen and human type V collagens alpha 1(2) alpha 2 and alpha 1 alpha 2 alpha 3. J Biol Chem. 1990 Jun 15;265(17):10081-7. PMID: 2351650. |
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