Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q61245 (COBA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XI) chain
Gene names
Name:Col11a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1804 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.

Subunit structure

Trimers composed of three different chains: alpha 1(XI), alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational modification of alpha 1(II). Alpha 1(V) can also be found instead of alpha 3(XI)=1(II) By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Domain

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity.

Post-translational modification

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

N-glycosylated By similarity.

Involvement in disease

Defects in Col11a1 are associated with chondrodysplasia, an autosomal recessive disease characterized by skeletal defects caused by abnormalities in the cartilage of limbs, ribs, mandibles and trachea. Ref.3

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 6 collagen-like domains.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 laminin G-like domain.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainCollagen
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcartilage condensation

Inferred from mutant phenotype PubMed 3070812. Source: MGI

cartilage development

Inferred from mutant phenotype PubMed 4100752PubMed 4110409Ref.3PubMed 886247. Source: MGI

chondrocyte development

Inferred from mutant phenotype PubMed 4100752. Source: MGI

collagen fibril organization

Inferred from mutant phenotype PubMed 17029294PubMed 17683922PubMed 21467034PubMed 3070812PubMed 4100752PubMed 4110409Ref.3. Source: MGI

detection of mechanical stimulus involved in sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system morphogenesis

Inferred from mutant phenotype PubMed 4100752. Source: MGI

heart morphogenesis

Inferred from genetic interaction PubMed 17029294. Source: MGI

inner ear morphogenesis

Inferred from mutant phenotype PubMed 1952599. Source: MGI

proteoglycan metabolic process

Inferred from mutant phenotype PubMed 3070812. Source: MGI

skeletal system morphogenesis

Inferred from mutant phenotype Ref.3. Source: MGI

tendon development

Inferred from mutant phenotype PubMed 21467034. Source: MGI

ventricular cardiac muscle tissue morphogenesis

Inferred from mutant phenotype PubMed 17029294. Source: MGI

visual perception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcollagen

Inferred from direct assay PubMed 17683922. Source: MGI

extracellular matrix

Inferred from direct assay PubMed 17029294. Source: MGI

   Molecular_functionextracellular matrix structural constituent

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q61245-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: Q61245-2)

The sequence of this isoform differs from the canonical sequence as follows:
     329-413: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Potential
Propeptide35 – 511477N-terminal propeptide Potential
PRO_0000005777
Chain512 – 15611050Collagen alpha-1(XI) chain
PRO_0000005778
Propeptide1562 – 1804243C-terminal propeptide
PRO_0000005779

Regions

Domain70 – 242173Laminin G-like
Domain440 – 48849Collagen-like 1
Domain527 – 58458Collagen-like 2
Domain567 – 62357Collagen-like 3
Domain728 – 78154Collagen-like 4
Domain1427 – 148256Collagen-like 5
Domain1481 – 153959Collagen-like 6
Domain1575 – 1803229Fibrillar collagen NC1
Region229 – 417189Nonhelical region
Region418 – 50689Triple-helical region (interrupted)
Region507 – 5093Short nonhelical segment
Region510 – 52718Telopeptide
Region528 – 15401013Triple-helical region
Region1541 – 156121Nonhelical region (C-terminal)

Sites

Metal binding16231Calcium By similarity
Metal binding16251Calcium By similarity
Metal binding16261Calcium; via carbonyl oxygen By similarity
Metal binding16281Calcium; via carbonyl oxygen By similarity
Metal binding16311Calcium By similarity

Amino acid modifications

Modified residue6101Allysine
Modified residue14501Allysine
Glycosylation16381N-linked (GlcNAc...) Potential
Disulfide bond60 ↔ 242 By similarity
Disulfide bond181 ↔ 235 By similarity
Disulfide bond1605 ↔ 1637 By similarity
Disulfide bond1628Interchain By similarity
Disulfide bond1646 ↔ 1801 By similarity
Disulfide bond1712 ↔ 1755 By similarity

Natural variations

Alternative sequence329 – 41385Missing in isoform Short.
VSP_001147

Experimental info

Sequence conflict2121T → A in BAA07367. Ref.1
Sequence conflict3701L → V in BAA07367. Ref.1
Sequence conflict5471A → T in BAA07367. Ref.1
Sequence conflict6961P → S in BAA07367. Ref.1
Sequence conflict10651T → A in BAA07367. Ref.1
Sequence conflict14761T → S in BAA07367. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 918C3D4B8C964470

FASTA1,804181,032
        10         20         30         40         50         60 
MEPWSRWKTK RWIWDLTIST LALTFLFQAR EVRGAAPVDI LKALDFHNSP VGISKTTGFC 

        70         80         90        100        110        120 
TNRKNSKDPD VAYRVTEEAQ ISAPTKQLFP GGIFPQDFSI LFTIKPKKGT QAFLLSLYNE 

       130        140        150        160        170        180 
HGIQQLGVEV GRSPVFLFED HTGKPTPENY PLFSTVNIAD GKWHRVAISV EKKTVTMIVD 

       190        200        210        220        230        240 
CKKKITKPLD RSERSIVDTN GIMVFGTRIL ETDVFQGDIQ QFLITGDPKA AYDYCDHYSP 

       250        260        270        280        290        300 
DCDLTSKAAQ AQEPHIDEYA PEDIIEYDYE YGETDYKEAE SVTEMPTFTE ETVAQTEANI 

       310        320        330        340        350        360 
VDDFQDYNYG TMEPYQTETP RRVSGSNEPN PVEEGFTEEY LTGEDYDVQR NTSEDILYGN 

       370        380        390        400        410        420 
KGVDGRDSDL LVDGDLGEYD FYEYKEYEER TTTSPNEEFG PGVPAETDFT ETSINGHGAY 

       430        440        450        460        470        480 
GEKGQKGEPA VVEPGMLVEG PPGPAGPAGL MGPPGLQGPS GLPGDPGDRG PPGRPGLPGA 

       490        500        510        520        530        540 
DGLPGPPGTM LMLPFRYGGD GSKGPTISAQ EAQAQAILQQ ARIALRGPPG PMGLTGRPGP 

       550        560        570        580        590        600 
VGGPGSAGAK GESGDPGPQG PRGVQGPPGP TGKPGKRGRP GADGGRGMPG ESGSKGDRGF 

       610        620        630        640        650        660 
DGLPGLPGDK GHRGERGPQG PPGLPGDDGM RGEDGEIGPR GLPGEAGPRG LLGPRGTPGP 

       670        680        690        700        710        720 
PGQPGIGGID GPQGPKGNMG PQGEPGPPGQ QGNPGPQGLP GPQGPIGPPG EKGPQGKPGL 

       730        740        750        760        770        780 
AGLPGADGPP GHPGKEGQSG EKGALGPPGP QGPIGYPGPR GVKGADGVRG LKGSKGEKGE 

       790        800        810        820        830        840 
DGFPGFKGDM GLKGDRGEVG QVGPRGEDGP EGPKGRAGPT GDPGPSGQAG EKGKLGVPGL 

       850        860        870        880        890        900 
PGYPGRQGPK GSTGFPGFPG ANGEKGARGI AGKPGPRGQR GPTGPRGSRG ARGPTGKPGP 

       910        920        930        940        950        960 
KGTSGGDGPP GPPGERGPQG PQGPVGFPGP KGPPGPAGKD GLPGHPGQRG ETGFQGKTGP 

       970        980        990       1000       1010       1020 
PGPGGVVGPQ GPTGETGPIG ERGHPGPPGP PGEQGLPGAA GKEGAKGDPG PQGISGKDGP 

      1030       1040       1050       1060       1070       1080 
AGIRGFPGER GLPGAQGAPG LKGGEGPQGP QGPVGSPGER GSAGTAGPIG LPGRPGPQGP 

      1090       1100       1110       1120       1130       1140 
PGPAGEKGAP GEKGPQGPAG RDGVQGPVGL PGPAGPAGSP GEDGDKGEIG EPGQKGSKGD 

      1150       1160       1170       1180       1190       1200 
KGENGPPGPP GLQGPVGAPG IAGGDGEPGP RGQQGMFGQK GDEGARGFPG LPGPIGLQGL 

      1210       1220       1230       1240       1250       1260 
PGPPGEKGEN GDVGPMGPPG PPGPRGPQGP NGADGPQGPP GSIGSVGVVG DKGEPGEAGN 

      1270       1280       1290       1300       1310       1320 
PGPPGEAGSG GLKGERGEKG EAGPPGAAGP AGIKGPPGDD GPKGNPGPVG FPGDPGPPGE 

      1330       1340       1350       1360       1370       1380 
PGPAGQDGVG GDKGEDGDPG QPGPPGPSGE AGPPGPPGKR GPPGASGSEG RQGEKGAKGE 

      1390       1400       1410       1420       1430       1440 
AGAEGPPGKT GPVGPQGPSG KPGPEGLRGI PGPVGEQGLP GAAGQDGPPG PLGPPGLPGL 

      1450       1460       1470       1480       1490       1500 
KGDPGSKGEK GHPGLIGLIG PPGEQGEKGD RGLPGTQGSP GAKGDGGIPG PAGPIGPPGP 

      1510       1520       1530       1540       1550       1560 
PGLPGPAGPK GNKGSSGPTG QKGDSGMPGP PGPPGPPGEV IQPLPILSPK KTRRHTESIQ 

      1570       1580       1590       1600       1610       1620 
GDAGDNILDY SDGMEEIFGS LNSLKQDIEH MKFPMGTQTN PARTCKDLQL SHPDFPDGEY 

      1630       1640       1650       1660       1670       1680 
WIDPNQGCSG DSFKVYCNFT AGGETCIYPD KKSEGVRISS WPKEKPGSWY SEFKRGKLLS 

      1690       1700       1710       1720       1730       1740 
YLDVEGNSIN MVQMTFLKLL TASARQNFTY NCHQSAAWYD VLSGSYDKAL RFLGSNDEEM 

      1750       1760       1770       1780       1790       1800 
SYENNPHIKA LYDGCASRKG YEKTVIEINT PKIDQVPIID VMINDFGDQN QKFGFEVGPA 


CFLG 

« Hide

Isoform Short [UniParc].

Checksum: 82E461C5F6246038
Show »

FASTA1,719171,401

References

« Hide 'large scale' references
[1]"Coding sequence and alternative splicing of the mouse alpha 1(XI) collagen gene (Col11a1)."
Yoshioka H., Inoguchi K., Khaleduzzaman M., Ninomiya Y., Andrikopoulos K., Ramirez F.
Genomics 28:337-340(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), ALTERNATIVE SPLICING.
Tissue: Embryo.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Tissue: Embryo.
[3]"A fibrillar collagen gene, Col11a1, is essential for skeletal morphogenesis."
Li Y., Lacerda D.A., Warman M.L., Beier D.R., Yoshioka H., Ninomiya Y., Oxford J.T., Morris N.P., Andrikopoulos K., Ramirez F., Wardell B.B., Lifferth G.D., Teuscher C., Woodward S.R., Taylor B.A., Seegmiller R.E., Olsen B.R.
Cell 80:423-430(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 181-198, DISEASE.
Strain: C57BL/6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38162 mRNA. Translation: BAA07367.1.
BC052161 mRNA. Translation: AAH52161.1.
S74574 mRNA. Translation: AAB33439.1.
PIRA55648.
RefSeqNP_031755.2. NM_007729.2.
UniGeneMm.209715.

3D structure databases

ProteinModelPortalQ61245.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ61245.

Proteomic databases

PaxDbQ61245.
PRIDEQ61245.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092155; ENSMUSP00000089793; ENSMUSG00000027966. [Q61245-1]
GeneID12814.
KEGGmmu:12814.
UCSCuc008rbk.1. mouse. [Q61245-1]

Organism-specific databases

CTD1301.
MGIMGI:88446. Col11a1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00710000106385.
HOGENOMHOG000085654.
HOVERGENHBG004933.
KOK06236.
OMAHPGKEGQ.
OrthoDBEOG7XPZ4W.
TreeFamTF323987.

Gene expression databases

ArrayExpressQ61245.
BgeeQ61245.
CleanExMM_COL11A1.
GenevestigatorQ61245.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282270.
PROQ61245.
SOURCESearch...

Entry information

Entry nameCOBA1_MOUSE
AccessionPrimary (citable) accession number: Q61245
Secondary accession number(s): Q64047, Q80WR4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot