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Q03692 (COAA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(X) chain
Gene names
Name:COL10A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length680 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage.

Subunit structure

Homotrimer.

Subcellular location

Secretedextracellular spaceextracellular matrix 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.

Involvement in disease

Schmid type metaphyseal chondrodysplasia (SMCD) [MIM:156500]: Dominantly inherited disorder of the osseous skeleton. The cardinal features of the phenotype are mild short stature, coxa vara and a waddling gait. Radiography usually shows sclerosis of the ribs, flaring of the metaphyses, and a wide irregular growth plate, especially of the knees. A variant form of SMCD is spondylometaphyseal dysplasia Japanese type. It is characterized by spinal involvement comprising mild platyspondyly, vertebral body abnormalities, and end-plate irregularity.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20

Sequence similarities

Contains 1 C1q domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 680662Collagen alpha-1(X) chain
PRO_0000005770

Regions

Domain547 – 680134C1q
Region19 – 5638Nonhelical region (NC2)
Region57 – 519463Triple-helical region
Region520 – 680161Nonhelical region (NC1)

Sites

Metal binding6341Calcium

Natural variations

Natural variant181G → E in SMCD. Ref.17 Ref.20
VAR_001838
Natural variant181G → R in SMCD. Ref.17 Ref.20
VAR_001839
Natural variant271M → T. Ref.1 Ref.20
Corresponds to variant rs1064583 [ dbSNP | Ensembl ].
VAR_023186
Natural variant981G → R.
Corresponds to variant rs2243370 [ dbSNP | Ensembl ].
VAR_048767
Natural variant1981R → H. Ref.20
Corresponds to variant rs148785195 [ dbSNP | Ensembl ].
VAR_023187
Natural variant5451G → R. Ref.15 Ref.20
Corresponds to variant rs2228547 [ dbSNP | Ensembl ].
VAR_001840
Natural variant5821Y → D in SMCD. Ref.20
VAR_023188
Natural variant5911C → R in SMCD. Ref.13 Ref.20
VAR_001841
Natural variant5951G → E in SMCD and spondylometaphyseal dysplasia Japanese type. Ref.15 Ref.18 Ref.20
VAR_001842
Natural variant5951G → R in SMCD. Ref.20
VAR_023189
Natural variant5971Y → C in SMCD. Ref.19 Ref.20
VAR_008039
Natural variant5971Y → H in SMCD. Ref.15 Ref.20
VAR_001843
Natural variant5981Y → D in SMCD. Ref.12 Ref.20
VAR_001844
Natural variant6001S → P in SMCD. Ref.16 Ref.20
VAR_001845
Natural variant6031V → M. Ref.20
VAR_023190
Natural variant6141L → P in SMCD. Ref.12 Ref.20
VAR_001846
Natural variant6171N → K in SMCD. Ref.15 Ref.20
VAR_001847
Natural variant6181G → V in SMCD. Ref.14 Ref.20
VAR_001848
Natural variant6441L → R in SMCD. Ref.15 Ref.20
VAR_001849
Natural variant6481D → G in SMCD. Ref.15 Ref.20
VAR_001850
Natural variant6511W → R in SMCD. Ref.20
VAR_023191
Natural variant6531Q → P in SMCD. Ref.20
VAR_023192
Natural variant6711S → P in SMCD. Ref.20
VAR_023193

Experimental info

Sequence conflict5001H → P in CAA42933. Ref.1

Secondary structure

....................... 680
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03692 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: E2F98E53E7882459

FASTA68066,158
        10         20         30         40         50         60 
MLPQIPFLLL VSLNLVHGVF YAERYQMPTG IKGPLPNTKT QFFIPYTIKS KGIAVRGEQG 

        70         80         90        100        110        120 
TPGPPGPAGP RGHPGPSGPP GKPGYGSPGL QGEPGLPGPP GPSAVGKPGV PGLPGKPGER 

       130        140        150        160        170        180 
GPYGPKGDVG PAGLPGPRGP PGPPGIPGPA GISVPGKPGQ QGPTGAPGPR GFPGEKGAPG 

       190        200        210        220        230        240 
VPGMNGQKGE MGYGAPGRPG ERGLPGPQGP TGPSGPPGVG KRGENGVPGQ PGIKGDRGFP 

       250        260        270        280        290        300 
GEMGPIGPPG PQGPPGERGP EGIGKPGAAG APGQPGIPGT KGLPGAPGIA GPPGPPGFGK 

       310        320        330        340        350        360 
PGLPGLKGER GPAGLPGGPG AKGEQGPAGL PGKPGLTGPP GNMGPQGPKG IPGSHGLPGP 

       370        380        390        400        410        420 
KGETGPAGPA GYPGAKGERG SPGSDGKPGY PGKPGLDGPK GNPGLPGPKG DPGVGGPPGL 

       430        440        450        460        470        480 
PGPVGPAGAK GMPGHNGEAG PRGAPGIPGT RGPIGPPGIP GFPGSKGDPG SPGPPGPAGI 

       490        500        510        520        530        540 
ATKGLNGPTG PPGPPGPRGH SGEPGLPGPP GPPGPPGQAV MPEGFIKAGQ RPSLSGTPLV 

       550        560        570        580        590        600 
SANQGVTGMP VSAFTVILSK AYPAIGTPIP FDKILYNRQQ HYDPRTGIFT CQIPGIYYFS 

       610        620        630        640        650        660 
YHVHVKGTHV WVGLYKNGTP VMYTYDEYTK GYLDQASGSA IIDLTENDQV WLQLPNAESN 

       670        680 
GLYSSEYVHS SFSGFLVAPM 

« Hide

References

« Hide 'large scale' references
[1]"The human collagen X gene. Complete primary translated sequence and chromosomal localization."
Thomas J.T., Cresswell C.J., Rash B., Nicolai H., Jones T., Solomon E., Grant M.E., Boot-Handford R.P.
Biochem. J. 280:617-623(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-27.
[2]"Genomic organization and full-length cDNA sequence of human collagen X."
Reichenberger E., Beier F., LuValle P., Olsen B.R., von der Mark K., Bertling W.M.
FEBS Lett. 311:305-310(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Beier F., Lammi M.B., von der Mark K.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
[7]"Cloning of the human and mouse type X collagen genes and mapping of the mouse type X collagen gene to chromosome 10."
Apte S.S., Seldin M.F., Hayashi M., Olsen B.R.
Eur. J. Biochem. 206:217-224(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-680.
[8]"Cloning of human alpha 1(X) collagen DNA and localization of the COL10A1 gene to the q21-q22 region of human chromosome 6."
Apte S., Mattei M.-G., Olsen B.R.
FEBS Lett. 282:393-396(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 561-666.
[9]"In situ hybridization studies on the expression of type X collagen in fetal human cartilage."
Reichenberger E., Aigner T., von der Mark K., Stoeb H., Bertling W.
Dev. Biol. 148:562-572(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 547-655.
[10]"Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer."
Bogin O., Kvansakul M., Rom E., Singer J., Yayon A., Hohenester E.
Structure 10:165-173(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 521-680, CALCIUM-BINDING.
[11]"Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels."
Kuivaniemi H., Tromp G., Prockop D.J.
Hum. Mutat. 9:300-315(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[12]"Amino acid substitutions of conserved residues in the carboxyl-terminal domain of the alpha 1(X) chain of type X collagen occur in two unrelated families with metaphyseal chondrodysplasia type Schmid."
Wallis G.A., Rash B., Sweetman W.A., Thomas J.T., Super M., Evans G., Grant M.E., Boot-Handford R.P.
Am. J. Hum. Genet. 54:169-178(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SMCD ASP-598 AND PRO-614.
[13]"Additional mutations of type X collagen confirm COL10A1 as the Schmid metaphyseal chondrodysplasia locus."
McIntosh I., Abbott M.H., Warman M.L., Olsen B.R., Francomano C.A.
Hum. Mol. Genet. 3:303-307(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SMCD ARG-591.
[14]"Type X collagen multimer assembly in vitro is prevented by a Gly618 to Val mutation in the alpha 1(X) NC1 domain resulting in Schmid metaphyseal chondrodysplasia."
Chan D., Cole W.G., Rogers J.G., Bateman J.F.
J. Biol. Chem. 270:4558-4562(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SMCD VAL-618.
[15]"Mutations in three subdomains of the carboxy-terminal region of collagen type X account for most of the Schmid metaphyseal dysplasias."
Bonaventure J., Chaminade F., Maroteaux P.
Hum. Genet. 96:58-64(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SMCD ARG-545; GLU-595; HIS-597; LYS-617; ARG-644 AND GLY-648.
[16]"Mutations within the gene encoding the alpha 1 (X) chain of type X collagen (COL10A1) cause metaphyseal chondrodysplasia type Schmid but not several other forms of metaphyseal chondrodysplasia."
Wallis G.A., Rash B., Sykes B., Bonaventure J., Maroteaux P., Zabel B., Wynne-Davies R., Grant M.E., Boot-Handford R.P.
J. Med. Genet. 33:450-457(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SMCD PRO-600.
[17]"Mutations in the N-terminal globular domain of the type X collagen gene (COL10A1) in patients with schmid metaphyseal chondrodysplasia."
Ikegawa S., Nakamura K., Nagano A., Haga N., Nakamura Y.
Hum. Mutat. 9:131-135(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SMCD GLU-18 AND ARG-18.
[18]"Mutation of the type X collagen gene 'COL10A1' causes spondylometaphyseal dysplasia."
Ikegawa S., Nishimura G., Nagai T., Hasegawa T., Ohashi H., Nakamura Y.
Am. J. Hum. Genet. 63:1659-1662(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPONDYLOMETAPHYSEAL DYSPLASIA JAPANESE TYPE GLU-595.
[19]"Novel missense mutation resulting in the substitution of tyrosine by cysteine at codon 597 of the type X collagen gene associated with Schmid metaphyseal chondrodysplasia."
Sawai H., Ida A., Nakata Y., Koyama K.
J. Hum. Genet. 43:259-261(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SMCD CYS-597.
[20]"Mutations of COL10A1 in Schmid metaphyseal chondrodysplasia."
Bateman J.F., Wilson R., Freddi S., Lamande S.R., Savarirayan R.
Hum. Mutat. 25:525-534(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SMCD ARG-18; GLU-18; ASP-582; ARG-591; ARG-595; GLU-595; HIS-597; CYS-597; ASP-598; PRO-600; PRO-614; LYS-617; VAL-618; ARG-644; GLY-648; ARG-651; PRO-653 AND PRO-671, VARIANTS THR-27; HIS-198; ARG-545 AND MET-603.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60382 Genomic DNA. Translation: CAA42933.1.
X72579, X72580 Genomic DNA. Translation: CAA51170.1.
X98568 Genomic DNA. Translation: CAA67178.1.
AL121963 Genomic DNA. Translation: CAB87590.1.
CH471051 Genomic DNA. Translation: EAW48240.1.
BC130621 mRNA. Translation: AAI30622.1.
BC130623 mRNA. Translation: AAI30624.1.
X65120 Genomic DNA. Translation: CAA46236.1.
X58879 Genomic DNA. Translation: CAA41686.1.
M74050 Genomic DNA. Translation: AAA61221.1.
S68531 mRNA. Translation: AAC60615.1.
PIRCGHU1D. S26396.
RefSeqNP_000484.2. NM_000493.3.
UniGeneHs.520339.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GR3X-ray2.00A521-680[»]
ProteinModelPortalQ03692.
SMRQ03692. Positions 549-680.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107697. 1 interaction.
MINTMINT-101719.
STRING9606.ENSP00000243222.

Polymorphism databases

DMDM2506306.

Proteomic databases

PaxDbQ03692.
PRIDEQ03692.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243222; ENSP00000243222; ENSG00000123500.
ENST00000327673; ENSP00000327368; ENSG00000123500.
GeneID1300.
KEGGhsa:1300.
UCSCuc003pwm.3. human.

Organism-specific databases

CTD1300.
GeneCardsGC06M116440.
HGNCHGNC:2185. COL10A1.
HPAHPA053268.
MIM120110. gene.
156500. phenotype.
neXtProtNX_Q03692.
Orphanet174. Metaphyseal chondrodysplasia, Schmid type.
PharmGKBPA26701.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG114228.
HOGENOMHOG000085653.
HOVERGENHBG108220.
InParanoidQ03692.
OMAYTYDEYS.
OrthoDBEOG70ZZPW.
PhylomeDBQ03692.
TreeFamTF334029.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ03692.
BgeeQ03692.
CleanExHS_COL10A1.
GenevestigatorQ03692.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR001073. C1q.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamPF00386. C1q. 1 hit.
PF01391. Collagen. 4 hits.
[Graphical view]
PRINTSPR00007. COMPLEMNTC1Q.
SMARTSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS50871. C1Q. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ03692.
GeneWikiCollagen,_type_X,_alpha_1.
GenomeRNAi1300.
NextBio5279.
PROQ03692.
SOURCESearch...

Entry information

Entry nameCOAA1_HUMAN
AccessionPrimary (citable) accession number: Q03692
Secondary accession number(s): A1L4P2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM