P08125 (COAA1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(X) chain

Gene names

Name:

COL10A1

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	674 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	Type X collagen is a product of hyperthrophic chondrotocytes and has been localized to presumptive mineralization zones of hyaline cartilage.
Subunit structure	Homotrimer.
Subcellular location	Secreted › extracellular space › extracellular 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.
Sequence similarities	Contains 1 C1q domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Domain	Collagen Repeat Signal
PTM	Hydroxylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	collagen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Ref.3
	Chain	19 – 674	656	Collagen alpha-1(X) chain		PRO_0000005769
Regions
	Domain	541 – 674	134	C1q
	Region	19 – 52	34	Nonhelical region (NC2)
	Region	53 – 512	460	Triple-helical region
	Region	513 – 674	162	Nonhelical region (NC1)
Amino acid modifications
	Modified residue	453	1	Hydroxyproline
	Modified residue	456	1	Hydroxyproline
Experimental info
	Sequence conflict	25	1	E → Q AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P08125 [UniParc]. Last modified November 1, 1991. Version 4. Checksum: EAB48B1EF174B145	FASTA	674	66,433
	10 20 30 40 50 60 MHLQISLLLL FCLNIVHGSD GYFSERYQKQ SSIKGPPHFL PFNVKSQGVQ MRGEQGPPGP 70 80 90 100 110 120 PGPIGPRGQP GPAGKPGFGS PGPQGPPGPL GPPGFSTVGK LGMPGLPGKP GERGLNGEKG 130 140 150 160 170 180 EAGPVGLPGA RGPQGPPGIP GPAGLSVLGK PGPQGPPGAQ GPRGPPGEKG EPGVPGINGQ 190 200 210 220 230 240 KGEMGFGVPG RPGNRGLPGP QGPQGLPGSA GIGKPGENGL PGQPGMKGDR GLPGARGEAG 250 260 270 280 290 300 IPGPQGPPGE PGEVGIGKPG PMGPPGPAGI PGAKGLPGPA GLPGSPGLPG FGKPGLPGMK 310 320 330 340 350 360 GHRGPEGPPG FPGPKGDQGP AGVPGELGPA GPQGNMGPQG LKGLPGENGL PGPKGDMGPV 370 380 390 400 410 420 GPAGFPGAKG ERGLPGLDGK PGYPGEQGLP GPKGHPGLPG QKGDTGHAGH PGLPGPVGPQ 430 440 450 460 470 480 GVKGVPGING EPGPRGPSGI PGVRGPIGPP GMPGAPGAKG EAGAPGLPGP AGIVTKGLRG 490 500 510 520 530 540 PMGPLGPPGP KGNSGEPGLP GPPGPPGPPG QSTIPEGYVK GESRELSGMS FMKAGANQAL 550 560 570 580 590 600 TGMPVSAFTV ILSKAYPGAT VPIKFDKILY NRQQHYDPRT GIFTCRIPGL YYFSYHVHAK 610 620 630 640 650 660 GTNVWVALYK NGSPVMYTYD EYQKGYLDQA SGSAVIDLME NDQVWLQLPN SESNGLYSSE 670 YVHSSFSGFL FAQI

References

[1]	"The developmentally regulated type X collagen gene contains a long open reading frame without introns." Ninomiya Y., Gordon M., van der Rest M., Schmid T., Linsenmayer T., Olsen B.R. J. Biol. Chem. 261:5041-5050(1986) [PubMed: 3082876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-674, PROTEIN SEQUENCE OF 103-117 AND 453-466.
[2]	"The type X collagen gene. Intron sequences split the 5'-untranslated region and separate the coding regions for the non-collagenous amino-terminal and triple-helical domains." LuValle P., Ninomiya Y., Rosenblum N.D., Olsen B.R. J. Biol. Chem. 263:18378-18385(1988) [PubMed: 2461368] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
[3]	"Monoclonal antibodies to type X collagen. Biosynthetic studies using an antibody to the amino-terminal domain." Summers T.A., Irwin M.H., Mayne R., Balian G. J. Biol. Chem. 263:581-587(1988) [PubMed: 2826450] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-34.
[4]	"The cloning and sequencing of alpha 1(VIII) collagen cDNAs demonstrate that type VIII collagen is a short chain collagen and contains triple-helical and carboxyl-terminal non-triple-helical domains similar to those of type X collagen." Yamaguchi N., Benya P.D., van der Rest M., Ninomiya Y. J. Biol. Chem. 264:16022-16029(1989) [PubMed: 2476437] [Abstract] Cited for: SEQUENCE REVISION TO C-TERMINUS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M13496 Genomic DNA. Translation: AAA48736.1. Sequence problems. J04194 Genomic DNA. Translation: AAA48634.1.
IPI	IPI00600819.
PIR	S23297.
3D structure databases
ProteinModelPortal	P08125.
SMR	P08125. Positions 543-672.
ModBase	Search...
Protein-protein interaction databases
STRING	P08125.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	veNOG15501.
GeneTree	ENSGT00590000082736.
HOGENOM	HBG444750.
HOVERGEN	HBG108220.
InParanoid	P08125.
OrthoDB	EOG4FFD29.
Family and domain databases
InterPro	IPR001073. C1q. IPR008160. Collagen. IPR008983. Tumour_necrosis_fac-like. [Graphical view]
Gene3D	G3DSA:2.60.120.40. Tumour_necrosis_fac-like. 1 hit.
Pfam	PF00386. C1q. 1 hit. PF01391. Collagen. 4 hits. [Graphical view]
PRINTS	PR00007. COMPLEMNTC1Q.
SMART	SM00110. C1Q. 1 hit. [Graphical view]
SUPFAM	SSF49842. TNF_like. 1 hit.
PROSITE	PS50871. C1Q. 1 hit. [Graphical view]
ProtoNet	Search...
Other
PMAP-CutDB	P08125.

Entry information

Entry name

COAA1_CHICK

Accession

Primary (citable) accession number: P08125

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	November 1, 1991
Last modified:	September 21, 2011
This is version 92 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program