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P02457 (CO1A1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(I) chain
Alternative name(s):
Alpha-1 type I collagen
Gene names
Name:COL1A1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

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

Domain

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.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 VWFC domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Propeptide23 – 151129N-terminal propeptide
PRO_0000005716
Chain152 – 12051054Collagen alpha-1(I) chain
PRO_0000005717
Propeptide1206 – 1453248C-terminal propeptide
PRO_0000005718

Regions

Domain31 – 8959VWFC
Domain1218 – 1453236Fibrillar collagen NC1

Sites

Metal binding12661Calcium By similarity
Metal binding12681Calcium By similarity
Metal binding12691Calcium; via carbonyl oxygen By similarity
Metal binding12711Calcium; via carbonyl oxygen By similarity
Metal binding12741Calcium By similarity
Site10221Not glycosylated
Site10851Not glycosylated

Amino acid modifications

Modified residue1521Pyrrolidone carboxylic acid
Modified residue1601Allysine By similarity
Modified residue17914-hydroxyproline Ref.3
Modified residue18214-hydroxyproline Ref.3
Modified residue18514-hydroxyproline Ref.3
Modified residue19414-hydroxyproline Ref.3
Modified residue19714-hydroxyproline Ref.3
Modified residue20014-hydroxyproline Ref.3
Modified residue21514-hydroxyproline Ref.4
Modified residue23014-hydroxyproline Ref.4
Modified residue23614-hydroxyproline Ref.4
Modified residue24514-hydroxyproline Ref.4
Modified residue25114-hydroxyproline Ref.4
Modified residue25415-hydroxylysine Ref.4
Modified residue26914-hydroxyproline Ref.4
Modified residue27814-hydroxyproline Ref.4
Modified residue28114-hydroxyproline Ref.4
Modified residue28714-hydroxyproline Ref.4
Modified residue29614-hydroxyproline Ref.5
Modified residue30214-hydroxyproline Ref.5
Modified residue31714-hydroxyproline Ref.5
Modified residue32314-hydroxyproline Ref.5
Modified residue33214-hydroxyproline Ref.5
Modified residue33514-hydroxyproline Ref.5
Modified residue36214-hydroxyproline Ref.5
Modified residue36514-hydroxyproline Ref.5
Modified residue37714-hydroxyproline Ref.5
Modified residue38314-hydroxyproline Ref.5
Modified residue39214-hydroxyproline Ref.5
Modified residue39814-hydroxyproline Ref.5
Modified residue40114-hydroxyproline Ref.5
Modified residue41614-hydroxyproline Ref.5
Modified residue41915-hydroxylysine Ref.5
Modified residue42514-hydroxyproline Ref.5
Modified residue42814-hydroxyproline Ref.5
Modified residue44014-hydroxyproline Ref.5
Modified residue44914-hydroxyproline Ref.5
Modified residue46414-hydroxyproline Ref.5
Modified residue47014-hydroxyproline Ref.5
Modified residue47914-hydroxyproline Ref.5
Modified residue48514-hydroxyproline Ref.5
Modified residue49415-hydroxylysine Ref.5
Modified residue49714-hydroxyproline Ref.5
Modified residue50314-hydroxyproline Ref.5
Modified residue51214-hydroxyproline Ref.5
Modified residue51814-hydroxyproline Ref.5
Modified residue52414-hydroxyproline Ref.5
Modified residue53314-hydroxyproline Ref.5
Modified residue53614-hydroxyproline Ref.5
Modified residue54514-hydroxyproline Ref.5
Modified residue55414-hydroxyproline Ref.5
Modified residue56014-hydroxyproline Ref.5
Modified residue57214-hydroxyproline Ref.6
Modified residue58114-hydroxyproline Ref.6
Modified residue58414-hydroxyproline Ref.6
Modified residue59014-hydroxyproline Ref.6
Modified residue59314-hydroxyproline Ref.6
Modified residue61114-hydroxyproline Ref.6
Modified residue62914-hydroxyproline Ref.6
Modified residue63514-hydroxyproline Ref.6
Modified residue64114-hydroxyproline Ref.6
Modified residue64714-hydroxyproline Ref.6
Modified residue65314-hydroxyproline Ref.6
Modified residue65914-hydroxyproline Ref.6
Modified residue67114-hydroxyproline Ref.6
Modified residue68014-hydroxyproline Ref.6
Modified residue69214-hydroxyproline Ref.6
Modified residue70414-hydroxyproline Ref.6
Modified residue70714-hydroxyproline Ref.6
Modified residue71314-hydroxyproline Ref.6
Modified residue71914-hydroxyproline Ref.7
Modified residue72814-hydroxyproline Ref.7
Modified residue73714-hydroxyproline Ref.7
Modified residue74015-hydroxylysine Ref.7
Modified residue74614-hydroxyproline Ref.7
Modified residue76114-hydroxyproline Ref.7
Modified residue76714-hydroxyproline Ref.7
Modified residue77614-hydroxyproline Ref.7
Modified residue78814-hydroxyproline Ref.7
Modified residue79414-hydroxyproline Ref.7
Modified residue79714-hydroxyproline Ref.7
Modified residue80614-hydroxyproline Ref.7
Modified residue81214-hydroxyproline Ref.7
Modified residue83014-hydroxyproline Ref.7
Modified residue83914-hydroxyproline Ref.7
Modified residue84814-hydroxyproline Ref.7
Modified residue85115-hydroxylysine Ref.7
Modified residue86014-hydroxyproline Ref.7
Modified residue86614-hydroxyproline Ref.7
Modified residue87514-hydroxyproline Ref.7
Modified residue88414-hydroxyproline Ref.7
Modified residue88714-hydroxyproline Ref.7
Modified residue90814-hydroxyproline Ref.7
Modified residue91114-hydroxyproline Ref.7
Modified residue91714-hydroxyproline Ref.7
Modified residue92014-hydroxyproline Ref.7
Modified residue92614-hydroxyproline Ref.7
Modified residue93514-hydroxyproline Ref.7
Modified residue95314-hydroxyproline Ref.7
Modified residue96214-hydroxyproline Ref.7
Modified residue96514-hydroxyproline Ref.7
Modified residue97114-hydroxyproline Ref.7
Modified residue98614-hydroxyproline Ref.7
Modified residue99214-hydroxyproline Ref.8
Modified residue99814-hydroxyproline Ref.8
Modified residue100714-hydroxyproline Ref.8
Modified residue101314-hydroxyproline Ref.8
Modified residue102215-hydroxylysine; partial Ref.8
Modified residue103414-hydroxyproline Ref.8
Modified residue103714-hydroxyproline Ref.8
Modified residue104014-hydroxyproline Ref.8
Modified residue106714-hydroxyproline Ref.8
Modified residue108515-hydroxylysine; partial Ref.8
Modified residue109715-hydroxylysine Ref.9
Modified residue110914-hydroxyproline Ref.9
Modified residue111214-hydroxyproline Ref.9
Modified residue111514-hydroxyproline Ref.9
Modified residue113314-hydroxyproline Ref.9
Modified residue114814-hydroxyproline Ref.9
Modified residue115313-hydroxyproline Ref.9
Modified residue115414-hydroxyproline Ref.9
Modified residue116914-hydroxyproline Ref.9
Modified residue117214-hydroxyproline Ref.9
Modified residue117514-hydroxyproline Ref.9
Modified residue117814-hydroxyproline Ref.9
Glycosylation2541O-linked (Gal...); partial Ref.4
Glycosylation10971O-linked (Gal...); partial Ref.9
Glycosylation13541N-linked (GlcNAc...) By similarity
Disulfide bond1248 ↔ 1280 By similarity
Disulfide bond1254Interchain (with C-1271) By similarity
Disulfide bond1271Interchain (with C-1254) By similarity
Disulfide bond1288 ↔ 1451 By similarity
Disulfide bond1359 ↔ 1404 By similarity

Experimental info

Sequence conflict14411Q → H in AAA48671. Ref.12

Sequences

Sequence LengthMass (Da)Tools
P02457 [UniParc].

Last modified July 10, 2007. Version 3.
Checksum: 61C617239E271A82

FASTA1,453137,755
        10         20         30         40         50         60 
MFSFVDSRLL LLIAATVLLT RGEGEEDIQT GSCVQDGLTY NDKDVWKPEP CQICVCDSGN 

        70         80         90        100        110        120 
ILCDEVICED TSDCPNAEIP FGECCPICPD VDASPVYPES AGVEGPKGDT GPRGDRGLPG 

       130        140        150        160        170        180 
PPGRDGIPGQ PGLPGPPGPP GPPGLGGNFA PQMSYGYDEK SAGVAVPGPM GPAGPRGLPG 

       190        200        210        220        230        240 
PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PAGPPGKNGD DGEAGKPGRP GQRGPPGPQG 

       250        260        270        280        290        300 
ARGLPGTAGL PGMKGHRGFS GLDGAKGQPG PAGPKGEPGS PGENGAPGQM GPRGLPGERG 

       310        320        330        340        350        360 
RPGPSGPAGA RGNDGAPGAA GPPGPTGPAG PPGFPGAAGA KGETGPQGAR GSEGPQGSRG 

       370        380        390        400        410        420 
EPGPPGPAGA AGPAGNPGAD GQPGAKGATG APGIAGAPGF PGARGPSGPQ GPSGAPGPKG 

       430        440        450        460        470        480 
NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG PAGEEGKRGA RGEPGPAGLP GPAGERGAPG 

       490        500        510        520        530        540 
SRGFPGADGI AGPKGPPGER GSPGAVGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG 

       550        560        570        580        590        600 
KTGPPGPAGQ DGRPGPAGPP GARGQAGVMG FPGPKGAAGE PGKPGERGAP GPPGAVGAAG 

       610        620        630        640        650        660 
KDGEAGAQGP PGPTGPAGER GEQGPAGAPG FQGLPGPAGP PGEAGKPGEQ GVPGNAGAPG 

       670        680        690        700        710        720 
PAGARGERGF PGERGVQGPP GPQGPRGANG APGNDGAKGD AGAPGAPGNE GPPGLEGMPG 

       730        740        750        760        770        780 
ERGAAGLPGA KGDRGDPGPK GADGAPGKDG LRGLTGPIGP PGPAGAPGDK GEAGPPGPAG 

       790        800        810        820        830        840 
PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGETGD AGAKGDAGPP GPAGPTGAPG 

       850        860        870        880        890        900 
PAGZVGAPGP KGARGSAGPP GATGFPGAAG RVGPPGPSGN IGLPGPPGPA GKZGSKGPRG 

       910        920        930        940        950        960 
ETGPAGRPGE PGPAGPPGPP GEKGSPGADG PIGAPGTPGP QGIAGQRGVV GLPGQRGERG 

       970        980        990       1000       1010       1020 
FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE AGREGAPGAE GAPGRDGAAG 

      1030       1040       1050       1060       1070       1080 
PKGDRGETGP AGPPGAPGAP GAPGPVGPAG KNGDRGETGP AGPAGPPGPA GARGPAGPQG 

      1090       1100       1110       1120       1130       1140 
PRGDKGETGE QGDRGMKGHR GFSGLQGPPG PPGAPGEQGP SGASGPAGPR GPPGSAGAAG 

      1150       1160       1170       1180       1190       1200 
KDGLNGLPGP IGPPGPRGRT GEVGPVGPPG PPGPPGPPGP PSGGFDLSFL PQPPQEKAHD 

      1210       1220       1230       1240       1250       1260 
GGRYYRADDA NVMRDRDLEV DTTLKSLSQQ IENIRSPEGT RKNPARTCRD LKMCHGDWKS 

      1270       1280       1290       1300       1310       1320 
GEYWIDPNQG CNLDAIKVYC NMETGETCVY PTQATIAQKN WYLSKNPKEK KHVWFGETMS 

      1330       1340       1350       1360       1370       1380 
DGFQFEYGGE GSNPADVAIQ LTFLRLMSTE ATQNVTYHCK NSVAYMDHDT GNLKKALLLQ 

      1390       1400       1410       1420       1430       1440 
GANEIEIRAE GNSRFTYGVT EDGCTSHTGA WGKTVIEYKT TKTSRLPIID LAPMDVGAPD 

      1450 
QEFGIDIGPV CFL 

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References

[1]"Construction and characterization of cDNA clones encoding the 5' end of the chicken pro alpha 1(I) collagen mRNA."
Finer M.H., Boedtker H., Doty P.
Gene 56:71-78(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-153.
[2]"Unusual DNA sequences located within the promoter region and the first intron of the chicken pro-alpha 1(I) collagen gene."
Finer M.H., Aho S., Gerstenfeld L.C., Boedtker H., Doty P.
J. Biol. Chem. 262:13323-13332(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-144.
[3]"Amino acid sequence of cyanogen bromide peptides from the amino-terminal region of chick skicollagen."
Kang A.H., Gross J.
Biochemistry 9:796-804(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 152-206, HYDROXYLATION AT PRO-179; PRO-182; PRO-185; PRO-194; PRO-197 AND PRO-200.
[4]"The covalent structure of collagen. Amino acid sequence of alpha1-CB5 glycopeptide and alpha1-CB4 from chick skin collagen."
Kang A.H., Dixit S.N., Corbett C., Gross J.
J. Biol. Chem. 250:7428-7434(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 207-290, HYDROXYLATION AT PRO-215; PRO-230; PRO-236; PRO-245; PRO-251; LYS-254; PRO-269; PRO-278; PRO-281 AND PRO-287, GLYCOSYLATION AT LYS-254.
[5]"Amino acid sequence of chick skin collagen alpha 1(I)-CB8 and the complete primary structure of the helical portion of the chick skin collagen alpha 1(I) chain."
Highberger J.H., Corbett C., Dixit S.N., Yu W., Seyer J.M., Kang A.H., Gross J.
Biochemistry 21:2048-2055(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 291-569, HYDROXYLATION AT PRO-296; PRO-302; PRO-317; PRO-323; PRO-332; PRO-335; PRO-362; PRO-365; PRO-377; PRO-383; PRO-392; PRO-398; PRO-401; PRO-416; LYS-419; PRO-425; PRO-428; PRO-440; PRO-449; PRO-464; PRO-470; PRO-479; PRO-485; LYS-494; PRO-497; PRO-503; PRO-512; PRO-518; PRO-524; PRO-533; PRO-536; PRO-545; PRO-554 AND PRO-560.
[6]"Covalent structure of collagen: amino acid sequence of alpha1-CB3 of chick skin collagen."
Dixit S.N., Kang A.H., Gross J.
Biochemistry 14:1929-1933(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 570-718, HYDROXYLATION AT PRO-572; PRO-581; PRO-584; PRO-590; PRO-593; PRO-611; PRO-629; PRO-635; PRO-641; PRO-647; PRO-653; PRO-659; PRO-671; PRO-680; PRO-692; PRO-704; PRO-707 AND PRO-713.
[7]"The amino acid sequence of chick skin collagen alpha1-CB7."
Highberger J.H., Corbett C., Kang A.H., Gross J.
Biochemistry 14:2872-2881(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 719-989, HYDROXYLATION AT PRO-719; PRO-728; PRO-737; LYS-740; PRO-746; PRO-761; PRO-767; PRO-776; PRO-788; PRO-794; PRO-797; PRO-806; PRO-812; PRO-830; PRO-839; PRO-848; LYS-851; PRO-860; PRO-866; PRO-875; PRO-884; PRO-887; PRO-908; PRO-911; PRO-917; PRO-920; PRO-926; PRO-935; PRO-953; PRO-962; PRO-965; PRO-971 AND PRO-986.
[8]"Covalent structure of collagen: amino acid sequence of alpha1-CB6A of chick skin collagen."
Dixit S.N., Seyer J.M., Oronsky A.O., Corbett C., Kang A.H., Gross J.
Biochemistry 14:1933-1938(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 990-1096, HYDROXYLATION AT PRO-992; PRO-998; PRO-1007; PRO-1013; LYS-1022; PRO-1034; PRO-1037; PRO-1040; PRO-1067 AND LYS-1085, ABSENCE OF GLYCOSYLATION AT LYS-1022 AND LYS-1085.
[9]"Covalent structure of collagen: amino acid sequence of chick skin collagen alpha1(1)-CB6B."
Dixit S.N., Seyer J.M., Kang A.H., Gross J.
Biochemistry 17:5719-5722(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1097-1187, HYDROXYLATION AT LYS-1097; PRO-1109; PRO-1112; PRO-1115; PRO-1133; PRO-1148; PRO-1153; PRO-1154; PRO-1169; PRO-1172; PRO-1175 AND PRO-1178, GLYCOSYLATION AT LYS-1097.
[10]"Evidence for a previously undetected sequence at the carboxyterminus of the alpha 1 chain of chicken bone collagen."
Eyre D.R., Glimcher M.J.
Biochem. Biophys. Res. Commun. 48:720-726(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1200-1205.
[11]"Sequence determination and analysis of the 3' region of chicken pro-alpha 1(I) and pro-alpha 2(I) collagen messenger ribonucleic acids including the carboxy-terminal propeptide sequences."
Fuller F., Boedtker H.
Biochemistry 20:996-1006(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 981-1453.
[12]"Nucleotide sequence of a collagen cDNA-fragment coding for the carboxyl end of pro alpha 1(I)-chains."
Showalter A.M., Pesciotta D.M., Eikenberry E.F., Yamamoto T., Pastan I., Decrombrugghe B., Fietzek P.P., Olsen B.R.
FEBS Lett. 111:61-65(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1311-1453.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17839, M17838 Genomic DNA. Translation: AAA48704.1.
V00401 mRNA. Translation: CAA23695.1.
M10571 mRNA. Translation: AAA48671.1. Sequence problems.
M17607 mRNA. Translation: AAA48672.1.
PIRA27179.
CGCH1S. A90458.
I50629.
S07234.
UniGeneGga.2073.
Gga.43371.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP02457. 1 interaction.

Proteomic databases

PRIDEP02457.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004933.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 12 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP02457.

Entry information

Entry nameCO1A1_CHICK
AccessionPrimary (citable) accession number: P02457
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 10, 2007
Last modified: January 22, 2014
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families