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Protein

Collagen alpha-1(I) chain

Gene

COL1A1

Organism
Tyrannosaurus rex (Tyrant lizard king)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(I) chain
Alternative name(s):
Alpha-1 type I collagen
Gene namesi
Name:COL1A1
OrganismiTyrannosaurus rex (Tyrant lizard king)
Taxonomic identifieri436495 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaTyrannosauridaeTyrannosaurus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000286177‹1 – ›570Collagen alpha-1(I) chainAdd BLAST›570

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei64-hydroxyproline1 Publication1
Modified residuei124-hydroxyproline1 Publication1
Modified residuei154-hydroxyproline1 Publication1
Modified residuei304-hydroxyproline1 Publication1
Modified residuei2944-hydroxyproline1 Publication1
Modified residuei4744-hydroxyproline1 Publication1
Modified residuei4804-hydroxyproline1 Publication1
Modified residuei5674-hydroxyproline1 Publication1

Post-translational modificationi

Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.1 Publication

Keywords - PTMi

Hydroxylation

Proteomic databases

PRIDEiP0C2W2.

Interactioni

Subunit structurei

Trimers of one alpha 2(I) and two alpha 1(I) chains.

Structurei

3D structure databases

ProteinModelPortaliP0C2W2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the fibrillar collagen family.Curated

Keywords - Domaini

Collagen, Repeat

Sequencei

Sequence statusi: Fragments.

P0C2W2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GATGAPGIAG APGFPGARGA PGPQGPSGAP GPKXXXXXXX XXXXXXXXXX
60 70 80 90 100
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
110 120 130 140 150
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
160 170 180 190 200
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
210 220 230 240 250
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
260 270 280 290 300
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXGV QGPPGPQGPR
310 320 330 340 350
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
360 370 380 390 400
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
410 420 430 440 450
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
460 470 480 490 500
XXXXXXXXXX XXXXXXXXGS AGPPGATGFP GAAGRXXXXX XXXXXXXXXX
510 520 530 540 550
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
560 570
XXXXXXXXXX XGVVGLPGQR
Length:570
Mass (Da):61,737
Last modified:November 13, 2007 - v2
Checksum:iFE4DE139C463BEBF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei5701

Cross-referencesi

3D structure databases

ProteinModelPortaliP0C2W2.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP0C2W2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiCO1A1_TYREX
AccessioniPrimary (citable) accession number: P0C2W2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: November 13, 2007
Last modified: October 5, 2016
This is version 25 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

These protein fragments where extracted from a 68-million-year-old fossil. The tryptic peptides required multiple purification steps in order to eliminate contaminants and to increase the concentration of peptidic material.

Keywords - Technical termi

Direct protein sequencing, Extinct organism protein

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.