Search by BoMiProt ID - Bomi4817


Primary Information

BoMiProt ID Bomi4817
Protein Name Collagen alpha-2(XI) chain
Organism Bos taurus
Uniprot IdQ32S24
Milk FractionWhey
Ref Sequence Id NP_001039664.1
Aminoacid Length 1736
Molecular Weight 172238
Fasta Sequence https://www.uniprot.org/uniprot/Q32S24.fasta
Gene Name COL11A2
Gene Id 515435
Protein Existence Status reviewed

Secondary Information

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.
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
PTMs Disulfide bond formation, Glycosylation at Asn, Hydroxylation
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
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction 1TMH-(7-29)
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.
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.