Reviewed, UniProtKB/Swiss-Prot P0C2W2 (CO1A1_TYREX)

Names and origin

Protein names

Recommended name:
    Collagen alpha-1(I) chain
Alternative name(s):
    Alpha-1 type I collagen

Gene names

Name:

COL1A1

Organism

Tyrannosaurus rex (Tyrant lizard king)

Taxonomic identifier

436495 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Tyrannosauridae › Tyrannosaurus

Protein attributes

Sequence length	570 AA.
Sequence status	Fragments.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Type I collagen is a member of group I collagen (fibrillar forming collagen).
Subunit structure	Trimers of one alpha 2(I) and two alpha 1(I) chains.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Post-translational modification	Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Miscellaneous	These protein fragments where extracted from a 68 million years old fossil. The tryptic peptides required multiple purification steps in order to eliminate contaminants and to increase the concentration of peptidic material.
Sequence similarities	Belongs to the fibrillar collagen family.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Domain	Collagen Repeat
PTM	Hydroxylation
Technical term	Direct protein sequencing Extinct organism protein
Gene Ontology (GO)
Cellular component	proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›570	›570	Collagen alpha-1(I) chain		PRO_0000286177
Amino acid modifications
	Modified residue	6	1	4-hydroxyproline Ref.1
	Modified residue	12	1	4-hydroxyproline Ref.1
	Modified residue	15	1	4-hydroxyproline Ref.1
	Modified residue	30	1	4-hydroxyproline Ref.1
	Modified residue	294	1	4-hydroxyproline Ref.1
	Modified residue	474	1	4-hydroxyproline Ref.1
	Modified residue	480	1	4-hydroxyproline Ref.1
	Modified residue	567	1	4-hydroxyproline Ref.1
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	570	1

Sequences

	Sequence		Length	Mass (Da)
	P0C2W2-1 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: FE4DE139C463BEBF	FASTA	570	61,737
	10 20 30 40 50 60 GATGAPGIAG APGFPGARGA PGPQGPSGAP GPKXXXXXXX XXXXXXXXXX XXXXXXXXXX 70 80 90 100 110 120 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 130 140 150 160 170 180 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 190 200 210 220 230 240 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 250 260 270 280 290 300 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXGV QGPPGPQGPR 310 320 330 340 350 360 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 370 380 390 400 410 420 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 430 440 450 460 470 480 XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXGS AGPPGATGFP 490 500 510 520 530 540 GAAGRXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 550 560 570 XXXXXXXXXX XXXXXXXXXX XGVVGLPGQR

References

[1]	"Protein sequences from Mastodon and Tyrannosaurus rex revealed by mass spectrometry." Asara J.M., Schweitzer M.H., Freimark L.M., Phillips M., Cantley L.C. Science 316:280-285(2007) [PubMed: 17431180] [Abstract] Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, HYDROXYLATION AT PRO-6; PRO-12; PRO-15; PRO-30; PRO-294; PRO-474; PRO-480 AND PRO-567. Tissue: Bone.
[2]	Asara J.M. Submitted (SEP-2007) to UniProtKB Cited for: SEQUENCE REVISION TO 27 AND 470. Tissue: Bone.
[3]	"Interpreting sequences from mastodon and T. rex." Asara J.M., Garavelli J.S., Slatter D.A., Schweitzer M.H., Freimark L.M., Phillips M., Cantley L.C. Science 317:1324-1325(2007) [PubMed: 17823333] [Abstract] Cited for: COMMENTS ON INTERPRETATION OF POTENTIAL HYDROXYLATION SITES.

Cross-references

3D structure databases
ModBase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

CO1A1_TYREX

Accession

Primary (citable) accession number: P0C2W2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	November 13, 2007
Last modified:	January 19, 2010
This is version 12 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)