Q14055 (CO9A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-2(IX) chain

Gene names

Name:

COL9A2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	689 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Structural component of hyaline cartilage and vitreous of the eye.
Subunit structure	Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha 3(IX) chain.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Post-translational modification	Covalently linked to the telopeptides of type II collagen by lysine-derived cross-links. 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	Multiple epiphyseal dysplasia 2 (EDM2) [MIM:600204]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.8 Stickler syndrome 5 (STL5) [MIM:614284]: An autosomal recessive form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. STL5 is characterized by high myopia, vitreoretinal degeneration, retinal detachment, mild to moderate sensorineural hearing loss, short stature in childhood, and absence of cleft palate and Pierre Robin sequence. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7
Sequence similarities	Belongs to the fibril-associated collagens with interrupted helices (FACIT) family.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Deafness Disease mutation Dwarfism Stickler syndrome
Domain	Collagen Repeat Signal
PTM	Disulfide bond Glycoprotein Hydroxylation Proteoglycan
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome extracellular matrix organization Traceable author statement. Source: Reactome skeletal system development Traceable author statement Ref.6. Source: ProtInc
Cellular_component	collagen type IX Inferred from direct assay PubMed 8660302. Source: BHF-UCL endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular_function	extracellular matrix structural constituent conferring tensile strength Inferred by curator PubMed 8660302. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 689	666	Collagen alpha-2(IX) chain		PRO_0000005837
Regions
	Region	27 – 163	137	Triple-helical region 4 (COL4)
	Region	164 – 180	17	Nonhelical region 4 (NC4)
	Region	181 – 519	339	Triple-helical region 3 (COL3)
	Region	520 – 549	30	Nonhelical region 3 (NC3)
	Region	550 – 632	83	Triple-helical region 2 (COL2)
	Region	633 – 634	2	Nonhelical region 2 (NC2)
	Region	635 – 664	30	Triple-helical region 1 (COL1)
	Region	665 – 689	25	Nonhelical region 1 (NC1)
Amino acid modifications
	Glycosylation	169	1	O-linked (Xyl...) (glycosaminoglycan) By similarity
	Disulfide bond	174		Interchain Potential
	Disulfide bond	178		Interchain Potential
Natural variations
	Natural variant	246	1	T → M. Ref.9 Corresponds to variant rs2228565 [ dbSNP | Ensembl ].		VAR_026465
	Natural variant	326	1	Q → R. Ref.8 Ref.9 Corresponds to variant rs2228564 [ dbSNP | Ensembl ].		VAR_012659
	Natural variant	326	1	Q → W in IDD; requires 2 nucleotide substitutions. Ref.8		VAR_012658
	Natural variant	335	1	L → V. Ref.9 Corresponds to variant rs2228567 [ dbSNP | Ensembl ].		VAR_026466
	Natural variant	581	1	V → I. Corresponds to variant rs3737821 [ dbSNP | Ensembl ].		VAR_020014

Sequences

	Sequence		Length	Mass (Da)
	Q14055 [UniParc]. Last modified May 1, 1999. Version 2. Checksum: EB6106E02F6FA862	FASTA	689	65,131
	10 20 30 40 50 60 MAAATASPRS LLVLLQVVVL ALAQIRGPPG ERGPPGPPGP PGVPGSDGID GDNGPPGKAG 70 80 90 100 110 120 PPGPKGEPGK AGPDGPDGKP GIDGLTGAKG EPGPMGIPGV KGQPGLPGPP GLPGPGFAGP 130 140 150 160 170 180 PGPPGPVGLP GEIGIRGPKG DPGPDGPSGP PGPPGKPGRP GTIQGLEGSA DFLCPTNCPP 190 200 210 220 230 240 GMKGPPGLQG VKGHAGKRGI LGDPGHQGKP GPKGDVGASG EQGIPGPPGP QGIRGYPGMA 250 260 270 280 290 300 GPKGETGPHG YKGMVGAIGA TGPPGEEGPR GPPGRAGEKG DEGSPGIRGP QGITGPKGAT 310 320 330 340 350 360 GPPGINGKDG TPGTPGMKGS AGQAGQPGSP GHQGLAGVPG QPGTKGGPGD QGEPGPQGLP 370 380 390 400 410 420 GFSGPPGKEG EPGPRGEIGP QGIMGQKGDQ GERGPVGQPG PQGRQGPKGE QGPPGIPGPQ 430 440 450 460 470 480 GLPGVKGDKG SPGKTGPRGK VGDPGVAGLP GEKGEKGESG EPGPKGQQGV RGEPGYPGPS 490 500 510 520 530 540 GDAGAPGVQG YPGPPGPRGL AGNRGVPGQP GRQGVEGRDA TDQHIVDVAL KMLQEQLAEV 550 560 570 580 590 600 AVSAKREALG AVGMMGPPGP PGPPGYPGKQ GPHGHPGPRG VPGIVGAVGQ IGNTGPKGKR 610 620 630 640 650 660 GEKGDPGEVG RGHPGMPGPP GIPGLPGRPG QAINGKDGDR GSPGAPGEAG RPGLPGPVGL 670 680 PGFCEPAACL GASAYASARL TEPGSIKGP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human COL9A1 and COL9A2 genes. Two genes of 90 and 15 kb code for similar polypeptides of the same collagen molecule." Pihlajamaa T., Vuoristo M.M., Annunen S., Peraelae M., Prockop D.J., Ala-Kokko L. Matrix Biol. 17:237-241(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Foreskin.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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. , 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].
[4]	"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]. Tissue: Brain.
[5]	"Molecular cloning of the human alpha 2(IX) collagen cDNA and assignment of the human COL9A2 gene to chromosome 1." Peraelae M., Haenninen M., Haestbacka J., Elima K., Vuorio E. FEBS Lett. 319:177-180(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-668. Tissue: Cartilage.
[6]	"Identification of novel pro-alpha2(IX) collagen gene mutations in two families with distinctive oligo-epiphyseal forms of multiple epiphyseal dysplasia." Holden P., Canty E.G., Mortier G.R., Zabel B., Spranger J., Carr A., Grant M.E., Loughlin J.A., Briggs M.D. Am. J. Hum. Genet. 65:31-38(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN EDM2.
[7]	"A loss of function mutation in the COL9A2 gene causes autosomal recessive Stickler syndrome." Baker S., Booth C., Fillman C., Shapiro M., Blair M.P., Hyland J.C., Ala-Kokko L. Am. J. Med. Genet. A 155:1668-1672(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN STL5.
[8]	"An allele of COL9A2 associated with intervertebral disc disease." Annunen S., Paassilta P., Lohiniva J., Peraelae M., Pihlajamaa T., Karppinen J., Tervonen O., Kroeger H., Laehde S., Vanharanta H., Ryhaenen L., Goering H.H.H., Ott J., Prockop D.J., Ala-Kokko L. Science 285:409-412(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT IDD TRP-326, VARIANT ARG-326.
[9]	"A mutation in COL9A1 causes multiple epiphyseal dysplasia: further evidence for locus heterogeneity." Czarny-Ratajczak M., Lohiniva J., Rogala P., Kozlowski K., Peraelae M., Carter L., Spector T.D., Kolodziej L., Seppaenen U., Glazar R., Krolewski J., Latos-Bielenska A., Ala-Kokko L. Am. J. Hum. Genet. 69:969-980(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MET-246; ARG-326 AND VAL-335.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF019406 Genomic DNA. Translation: AAC33512.1. AL050341 Genomic DNA. Translation: CAB81611.1. CH471059 Genomic DNA. Translation: EAX07229.1. BC136326 mRNA. Translation: AAI36327.1. BC136327 mRNA. Translation: AAI36328.1. M95610 mRNA. Translation: AAA80977.1.
IPI	IPI00019088.
PIR	S32436.
RefSeq	NP_001843.1. NM_001852.3.
UniGene	Hs.418012.
3D structure databases
ProteinModelPortal	Q14055.
SMR	Q14055. Positions 21-55, 632-666.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14055. 3 interactions.
STRING	9606.ENSP00000361834.
PTM databases
PhosphoSite	Q14055.
Polymorphism databases
DMDM	20137328.
Proteomic databases
PaxDb	Q14055.
PRIDE	Q14055.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000372748; ENSP00000361834; ENSG00000049089.
GeneID	1298.
KEGG	hsa:1298.
UCSC	uc001cfh.1. human.
Organism-specific databases
CTD	1298.
GeneCards	GC01M040766.
H-InvDB	HIX0028759.
HGNC	HGNC:2218. COL9A2.
HPA	HPA056316.
MIM	120260. gene. 600204. phenotype. 603932. phenotype. 614284. phenotype.
neXtProt	NX_Q14055.
Orphanet	250984. Autosomal recessive Stickler syndrome. 166002. Multiple epiphyseal dysplasia due to collagen 9 anomaly.
PharmGKB	PA26734.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000085653.
HOVERGEN	HBG004933.
InParanoid	Q14055.
KO	K08131.
OMA	TSDQHIV.
OrthoDB	EOG46T324.
PhylomeDB	Q14055.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction. REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q14055.
Bgee	Q14055.
CleanEx	HS_COL9A2.
Genevestigator	Q14055.
GermOnline	ENSG00000049089. Homo sapiens.
Family and domain databases
InterPro	IPR008160. Collagen. [Graphical view]
Pfam	PF01391. Collagen. 10 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1298.
NextBio	5271.
SOURCE	Search...

Entry information

Entry name

CO9A2_HUMAN

Accession

Primary (citable) accession number: Q14055
Secondary accession number(s): B2RMP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.