Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Collagen alpha-1(I) chain

Gene

COL1A1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1266CalciumBy similarity1
Metal bindingi1268CalciumBy similarity1
Metal bindingi1269Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1271Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1274CalciumBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(I) chain
Alternative name(s):
Alpha-1 type I collagen
Gene namesi
Name:COL1A1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Add BLAST22
PropeptideiPRO_000000571623 – 151N-terminal propeptide1 PublicationAdd BLAST129
ChainiPRO_0000005717152 – 1205Collagen alpha-1(I) chainAdd BLAST1054
PropeptideiPRO_00000057181206 – 1453C-terminal propeptideAdd BLAST248

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei152Pyrrolidone carboxylic acid1
Modified residuei160AllysineBy similarity1
Modified residuei1794-hydroxyproline1 Publication1
Modified residuei1824-hydroxyproline1 Publication1
Modified residuei1854-hydroxyproline1 Publication1
Modified residuei1944-hydroxyproline1 Publication1
Modified residuei1974-hydroxyproline1 Publication1
Modified residuei2004-hydroxyproline1 Publication1
Modified residuei2154-hydroxyproline1 Publication1
Modified residuei2304-hydroxyproline1 Publication1
Modified residuei2364-hydroxyproline1 Publication1
Modified residuei2454-hydroxyproline1 Publication1
Modified residuei2514-hydroxyproline1 Publication1
Modified residuei2545-hydroxylysine1 Publication1
Glycosylationi254O-linked (Gal...); partial1 Publication1
Modified residuei2694-hydroxyproline1 Publication1
Modified residuei2784-hydroxyproline1 Publication1
Modified residuei2814-hydroxyproline1 Publication1
Modified residuei2874-hydroxyproline1 Publication1
Modified residuei2964-hydroxyproline1 Publication1
Modified residuei3024-hydroxyproline1 Publication1
Modified residuei3174-hydroxyproline1 Publication1
Modified residuei3234-hydroxyproline1 Publication1
Modified residuei3324-hydroxyproline1 Publication1
Modified residuei3354-hydroxyproline1 Publication1
Modified residuei3624-hydroxyproline1 Publication1
Modified residuei3654-hydroxyproline1 Publication1
Modified residuei3774-hydroxyproline1 Publication1
Modified residuei3834-hydroxyproline1 Publication1
Modified residuei3924-hydroxyproline1 Publication1
Modified residuei3984-hydroxyproline1 Publication1
Modified residuei4014-hydroxyproline1 Publication1
Modified residuei4164-hydroxyproline1 Publication1
Modified residuei4195-hydroxylysine1 Publication1
Modified residuei4254-hydroxyproline1 Publication1
Modified residuei4284-hydroxyproline1 Publication1
Modified residuei4404-hydroxyproline1 Publication1
Modified residuei4494-hydroxyproline1 Publication1
Modified residuei4644-hydroxyproline1 Publication1
Modified residuei4704-hydroxyproline1 Publication1
Modified residuei4794-hydroxyproline1 Publication1
Modified residuei4854-hydroxyproline1 Publication1
Modified residuei4945-hydroxylysine1 Publication1
Modified residuei4974-hydroxyproline1 Publication1
Modified residuei5034-hydroxyproline1 Publication1
Modified residuei5124-hydroxyproline1 Publication1
Modified residuei5184-hydroxyproline1 Publication1
Modified residuei5244-hydroxyproline1 Publication1
Modified residuei5334-hydroxyproline1 Publication1
Modified residuei5364-hydroxyproline1 Publication1
Modified residuei5454-hydroxyproline1 Publication1
Modified residuei5544-hydroxyproline1 Publication1
Modified residuei5604-hydroxyproline1 Publication1
Modified residuei5724-hydroxyproline1 Publication1
Modified residuei5814-hydroxyproline1 Publication1
Modified residuei5844-hydroxyproline1 Publication1
Modified residuei5904-hydroxyproline1 Publication1
Modified residuei5934-hydroxyproline1 Publication1
Modified residuei6114-hydroxyproline1 Publication1
Modified residuei6294-hydroxyproline1 Publication1
Modified residuei6354-hydroxyproline1 Publication1
Modified residuei6414-hydroxyproline1 Publication1
Modified residuei6474-hydroxyproline1 Publication1
Modified residuei6534-hydroxyproline1 Publication1
Modified residuei6594-hydroxyproline1 Publication1
Modified residuei6714-hydroxyproline1 Publication1
Modified residuei6804-hydroxyproline1 Publication1
Modified residuei6924-hydroxyproline1 Publication1
Modified residuei7044-hydroxyproline1 Publication1
Modified residuei7074-hydroxyproline1 Publication1
Modified residuei7134-hydroxyproline1 Publication1
Modified residuei7194-hydroxyproline1 Publication1
Modified residuei7284-hydroxyproline1 Publication1
Modified residuei7374-hydroxyproline1 Publication1
Modified residuei7405-hydroxylysine1 Publication1
Modified residuei7464-hydroxyproline1 Publication1
Modified residuei7614-hydroxyproline1 Publication1
Modified residuei7674-hydroxyproline1 Publication1
Modified residuei7764-hydroxyproline1 Publication1
Modified residuei7884-hydroxyproline1 Publication1
Modified residuei7944-hydroxyproline1 Publication1
Modified residuei7974-hydroxyproline1 Publication1
Modified residuei8064-hydroxyproline1 Publication1
Modified residuei8124-hydroxyproline1 Publication1
Modified residuei8304-hydroxyproline1 Publication1
Modified residuei8394-hydroxyproline1 Publication1
Modified residuei8484-hydroxyproline1 Publication1
Modified residuei8515-hydroxylysine1 Publication1
Modified residuei8604-hydroxyproline1 Publication1
Modified residuei8664-hydroxyproline1 Publication1
Modified residuei8754-hydroxyproline1 Publication1
Modified residuei8844-hydroxyproline1 Publication1
Modified residuei8874-hydroxyproline1 Publication1
Modified residuei9084-hydroxyproline1 Publication1
Modified residuei9114-hydroxyproline1 Publication1
Modified residuei9174-hydroxyproline1 Publication1
Modified residuei9204-hydroxyproline1 Publication1
Modified residuei9264-hydroxyproline1 Publication1
Modified residuei9354-hydroxyproline1 Publication1
Modified residuei9534-hydroxyproline1 Publication1
Modified residuei9624-hydroxyproline1 Publication1
Modified residuei9654-hydroxyproline1 Publication1
Modified residuei9714-hydroxyproline1 Publication1
Modified residuei9864-hydroxyproline1 Publication1
Modified residuei9924-hydroxyproline1 Publication1
Modified residuei9984-hydroxyproline1 Publication1
Modified residuei10074-hydroxyproline1 Publication1
Modified residuei10134-hydroxyproline1 Publication1
Modified residuei10225-hydroxylysine; partial1 Publication1
Modified residuei10344-hydroxyproline1 Publication1
Modified residuei10374-hydroxyproline1 Publication1
Modified residuei10404-hydroxyproline1 Publication1
Modified residuei10674-hydroxyproline1 Publication1
Modified residuei10855-hydroxylysine; partial1 Publication1
Modified residuei10975-hydroxylysine1 Publication1
Glycosylationi1097O-linked (Gal...); partial1 Publication1
Modified residuei11094-hydroxyproline1 Publication1
Modified residuei11124-hydroxyproline1 Publication1
Modified residuei11154-hydroxyproline1 Publication1
Modified residuei11334-hydroxyproline1 Publication1
Modified residuei11484-hydroxyproline1 Publication1
Modified residuei11533-hydroxyproline1 Publication1
Modified residuei11544-hydroxyproline1 Publication1
Modified residuei11694-hydroxyproline1 Publication1
Modified residuei11724-hydroxyproline1 Publication1
Modified residuei11754-hydroxyproline1 Publication1
Modified residuei11784-hydroxyproline1 Publication1
Disulfide bondi1248 ↔ 1280PROSITE-ProRule annotation
Disulfide bondi1254Interchain (with C-1271)PROSITE-ProRule annotation
Disulfide bondi1271Interchain (with C-1254)PROSITE-ProRule annotation
Disulfide bondi1288 ↔ 1451PROSITE-ProRule annotation
Glycosylationi1354N-linked (GlcNAc...)By similarity1
Disulfide bondi1359 ↔ 1404PROSITE-ProRule annotation

Post-translational modificationi

Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are 4-hydroxylated in some or all of the chains. Pro-1153 is the only 3-hydroxyproline and the only hydroxylated proline in position X.1 Publication
Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
O-linked glycans consist of Glc-Gal disaccharide bound to the hydroxyl group of 5-hydroxylysine.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1022Not glycosylated1
Sitei1085Not glycosylated1

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP02457.

Expressioni

Tissue specificityi

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP02457. 1 interactor.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 89VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1218 – 1453Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST236

Domaini

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity).By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG004933.
InParanoidiP02457.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 10 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSFVDSRLL LLIAATVLLT RGEGEEDIQT GSCVQDGLTY NDKDVWKPEP
60 70 80 90 100
CQICVCDSGN ILCDEVICED TSDCPNAEIP FGECCPICPD VDASPVYPES
110 120 130 140 150
AGVEGPKGDT GPRGDRGLPG PPGRDGIPGQ PGLPGPPGPP GPPGLGGNFA
160 170 180 190 200
PQMSYGYDEK SAGVAVPGPM GPAGPRGLPG PPGAPGPQGF QGPPGEPGEP
210 220 230 240 250
GASGPMGPRG PAGPPGKNGD DGEAGKPGRP GQRGPPGPQG ARGLPGTAGL
260 270 280 290 300
PGMKGHRGFS GLDGAKGQPG PAGPKGEPGS PGENGAPGQM GPRGLPGERG
310 320 330 340 350
RPGPSGPAGA RGNDGAPGAA GPPGPTGPAG PPGFPGAAGA KGETGPQGAR
360 370 380 390 400
GSEGPQGSRG EPGPPGPAGA AGPAGNPGAD GQPGAKGATG APGIAGAPGF
410 420 430 440 450
PGARGPSGPQ GPSGAPGPKG NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG
460 470 480 490 500
PAGEEGKRGA RGEPGPAGLP GPAGERGAPG SRGFPGADGI AGPKGPPGER
510 520 530 540 550
GSPGAVGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ
560 570 580 590 600
DGRPGPAGPP GARGQAGVMG FPGPKGAAGE PGKPGERGAP GPPGAVGAAG
610 620 630 640 650
KDGEAGAQGP PGPTGPAGER GEQGPAGAPG FQGLPGPAGP PGEAGKPGEQ
660 670 680 690 700
GVPGNAGAPG PAGARGERGF PGERGVQGPP GPQGPRGANG APGNDGAKGD
710 720 730 740 750
AGAPGAPGNE GPPGLEGMPG ERGAAGLPGA KGDRGDPGPK GADGAPGKDG
760 770 780 790 800
LRGLTGPIGP PGPAGAPGDK GEAGPPGPAG PTGARGAPGD RGEPGPPGPA
810 820 830 840 850
GFAGPPGADG QPGAKGETGD AGAKGDAGPP GPAGPTGAPG PAGZVGAPGP
860 870 880 890 900
KGARGSAGPP GATGFPGAAG RVGPPGPSGN IGLPGPPGPA GKZGSKGPRG
910 920 930 940 950
ETGPAGRPGE PGPAGPPGPP GEKGSPGADG PIGAPGTPGP QGIAGQRGVV
960 970 980 990 1000
GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE
1010 1020 1030 1040 1050
AGREGAPGAE GAPGRDGAAG PKGDRGETGP AGPPGAPGAP GAPGPVGPAG
1060 1070 1080 1090 1100
KNGDRGETGP AGPAGPPGPA GARGPAGPQG PRGDKGETGE QGDRGMKGHR
1110 1120 1130 1140 1150
GFSGLQGPPG PPGAPGEQGP SGASGPAGPR GPPGSAGAAG KDGLNGLPGP
1160 1170 1180 1190 1200
IGPPGPRGRT GEVGPVGPPG PPGPPGPPGP PSGGFDLSFL PQPPQEKAHD
1210 1220 1230 1240 1250
GGRYYRADDA NVMRDRDLEV DTTLKSLSQQ IENIRSPEGT RKNPARTCRD
1260 1270 1280 1290 1300
LKMCHGDWKS GEYWIDPNQG CNLDAIKVYC NMETGETCVY PTQATIAQKN
1310 1320 1330 1340 1350
WYLSKNPKEK KHVWFGETMS DGFQFEYGGE GSNPADVAIQ LTFLRLMSTE
1360 1370 1380 1390 1400
ATQNVTYHCK NSVAYMDHDT GNLKKALLLQ GANEIEIRAE GNSRFTYGVT
1410 1420 1430 1440 1450
EDGCTSHTGA WGKTVIEYKT TKTSRLPIID LAPMDVGAPD QEFGIDIGPV

CFL
Length:1,453
Mass (Da):137,755
Last modified:July 10, 2007 - v3
Checksum:i61C617239E271A82
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1441Q → H in AAA48671 (PubMed:6987088).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17839, M17838 Genomic DNA. Translation: AAA48704.1.
V00401 mRNA. Translation: CAA23695.1.
M10571 mRNA. Translation: AAA48671.1. Sequence problems.
M17607 mRNA. Translation: AAA48672.1.
PIRiA27179.
A90458. CGCH1S.
I50629.
S07234.
UniGeneiGga.2073.
Gga.43371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17839, M17838 Genomic DNA. Translation: AAA48704.1.
V00401 mRNA. Translation: CAA23695.1.
M10571 mRNA. Translation: AAA48671.1. Sequence problems.
M17607 mRNA. Translation: AAA48672.1.
PIRiA27179.
A90458. CGCH1S.
I50629.
S07234.
UniGeneiGga.2073.
Gga.43371.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02457. 1 interactor.

Proteomic databases

PRIDEiP02457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004933.
InParanoidiP02457.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 10 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO1A1_CHICK
AccessioniPrimary (citable) accession number: P02457
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 10, 2007
Last modified: September 16, 2015
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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.