P02453 (CO1A1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

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

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1463 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 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. Interacts with MRC2 By similarity. Interacts with TRAM2 By similarity.
Subcellular location	Secreted › extracellular space › extracellular 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 hydroxylated in some or all of the chains. Pro-1163 is the only 3-hydroxyproline and the only hydroxylated proline in position X. O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.
Sequence similarities	Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain. Contains 1 VWFC domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Domain	Collagen Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Hydroxylation Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood vessel development Inferred from electronic annotation. Source: Compara bone trabecula formation Inferred from electronic annotation. Source: Compara cartilage development involved in endochondral bone morphogenesis Inferred from electronic annotation. Source: Compara cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara collagen biosynthetic process Inferred from electronic annotation. Source: Compara collagen fibril organization Inferred from electronic annotation. Source: Compara embryonic skeletal system development Inferred from electronic annotation. Source: Compara endochondral ossification Inferred from electronic annotation. Source: Compara face morphogenesis Inferred from electronic annotation. Source: Compara intramembranous ossification Inferred from electronic annotation. Source: Compara negative regulation of cell-substrate adhesion Inferred from electronic annotation. Source: Compara osteoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of epithelial to mesenchymal transition Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara protein heterotrimerization Inferred from electronic annotation. Source: Compara protein localization to nucleus Inferred from electronic annotation. Source: Compara protein transport Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from electronic annotation. Source: Compara skin morphogenesis Inferred from electronic annotation. Source: Compara tooth mineralization Inferred from electronic annotation. Source: Compara visual perception Inferred from electronic annotation. Source: Compara
Cellular_component	collagen type I Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: Compara extracellular space Inferred from electronic annotation. Source: Compara
Molecular_function	extracellular matrix structural constituent Inferred from electronic annotation. Source: Compara metal ion binding 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 – 22	22	Potential
	Propeptide	23 – 161	139	N-terminal propeptide		PRO_0000236804
	Chain	162 – 1215	1054	Collagen alpha-1(I) chain		PRO_0000059396
	Propeptide	1216 – 1463	248	C-terminal propeptide		PRO_0000236805
Regions
	Domain	38 – 96	59	VWFC
	Domain	1228 – 1463	236	Fibrillar collagen NC1
	Region	162 – 177	16	Nonhelical region (N-terminal)
	Region	178 – 1191	1014	Triple-helical region
	Region	1192 – 1215	24	Nonhelical region (C-terminal)
	Motif	744 – 746	3	Cell attachment site Potential
	Motif	1092 – 1094	3	Cell attachment site Potential
Sites
	Metal binding	1276	1	Calcium By similarity
	Metal binding	1278	1	Calcium By similarity
	Metal binding	1279	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	1281	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	1284	1	Calcium By similarity
Amino acid modifications
	Modified residue	162	1	Pyrrolidone carboxylic acid Ref.2
	Modified residue	170	1	Allysine
	Modified residue	264	1	5-hydroxylysine
	Modified residue	276	1	5-hydroxylysine Potential
	Modified residue	285	1	5-hydroxylysine Potential
	Modified residue	708	1	5-hydroxylysine Potential
	Modified residue	780	1	5-hydroxylysine Potential
	Modified residue	861	1	5-hydroxylysine Potential
	Modified residue	933	1	5-hydroxylysine Potential
	Modified residue	1095	1	5-hydroxylysine Potential
	Modified residue	1107	1	5-hydroxylysine Potential
	Modified residue	1163	1	3-hydroxyproline
	Glycosylation	264	1	O-linked (Gal...)
	Disulfide bond	1258 ↔ 1290		By similarity
	Disulfide bond	1264		Interchain (with C-1281) By similarity
	Disulfide bond	1281		Interchain (with C-1264) By similarity
	Disulfide bond	1298 ↔ 1461		By similarity
	Disulfide bond	1369 ↔ 1414		By similarity
Experimental info
	Sequence conflict	687	1	Q → E AA sequence Ref.4
	Sequence conflict	790 – 792	3	Missing AA sequence Ref.5
	Sequence conflict	794	1	A → T AA sequence Ref.5
	Sequence conflict	1043	1	P → A AA sequence Ref.6
	Sequence conflict	1046	1	A → P AA sequence Ref.6
	Sequence conflict	1074	1	A → I AA sequence Ref.6
	Sequence conflict	1077	1	I → V AA sequence Ref.6
	Sequence conflict	1080	1	V → A AA sequence Ref.6
	Sequence conflict	1206	1	E → QZ AA sequence Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P02453 [UniParc]. Last modified May 30, 2006. Version 3. Checksum: 8A6E17F276C4C6FA	FASTA	1,463	138,938
	10 20 30 40 50 60 MFSFVDLRLL LLLAATALLT HGQEEGQEEG QEEDIPPVTC VQNGLRYHDR DVWKPVPCQI 70 80 90 100 110 120 CVCDNGNVLC DDVICDELKD CPNAKVPTDE CCPVCPEGQE SPTDQETTGV EGPKGDTGPR 130 140 150 160 170 180 GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA PQLSYGYDEK STGISVPGPM 190 200 210 220 230 240 GPSGPRGLPG PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PPGPPGKNGD DGEAGKPGRP 250 260 270 280 290 300 GERGPPGPQG ARGLPGTAGL PGMKGHRGFS GLDGAKGDAG PAGPKGEPGS PGENGAPGQM 310 320 330 340 350 360 GPRGLPGERG RPGAPGPAGA RGNDGATGAA GPPGPTGPAG PPGFPGAVGA KGEGGPQGPR 370 380 390 400 410 420 GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF PGARGPSGPQ 430 440 450 460 470 480 GPSGPPGPKG NSGEPGAPGS KGDTGAKGEP GPTGIQGPPG PAGEEGKRGA RGEPGPAGLP 490 500 510 520 530 540 GPPGERGGPG SRGFPGADGV AGPKGPAGER GAPGPAGPKG SPGEAGRPGE AGLPGAKGLT 550 560 570 580 590 600 GSPGSPGPDG KTGPPGPAGQ DGRPGPPGPP GARGQAGVMG FPGPKGAAGE PGKAGERGVP 610 620 630 640 650 660 GPPGAVGPAG KDGEAGAQGP PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ 670 680 690 700 710 720 GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGANG APGNDGAKGD AGAPGAPGSQ 730 740 750 760 770 780 GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK GADGAPGKDG VRGLTGPIGP PGPAGAPGDK 790 800 810 820 830 840 GEAGPSGPAG PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGEPGD AGAKGDAGPP 850 860 870 880 890 900 GPAGPAGPPG PIGNVGAPGP KGARGSAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPA 910 920 930 940 950 960 GKEGSKGPRG ETGPAGRPGE VGPPGPPGPA GEKGAPGADG PAGAPGTPGP QGIAGQRGVV 970 980 990 1000 1010 1020 GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE SGREGAPGAE 1030 1040 1050 1060 1070 1080 GSPGRDGSPG AKGDRGETGP AGPPGAPGAP GAPGPVGPAG KSGDRGETGP AGPAGPIGPV 1090 1100 1110 1120 1130 1140 GARGPAGPQG PRGDKGETGE QGDRGIKGHR GFSGLQGPPG PPGSPGEQGP SGASGPAGPR 1150 1160 1170 1180 1190 1200 GPPGSAGSPG KDGLNGLPGP IGPPGPRGRT GDAGPAGPPG PPGPPGPPGP PSGGYDLSFL 1210 1220 1230 1240 1250 1260 PQPPQEKAHD GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD 1270 1280 1290 1300 1310 1320 LKMCHSDWKS GEYWIDPNQG CNLDAIKVFC NMETGETCVY PTQPSVAQKN WYISKNPKEK 1330 1340 1350 1360 1370 1380 RHVWYGESMT GGFQFEYGGQ GSDPADVAIQ LTFLRLMSTE ASQNITYHCK NSVAYMDQQT 1390 1400 1410 1420 1430 1440 GNLKKALLLQ GSNEIEIRAE GNSRFTYSVT YDGCTSHTGA WGKTVIEYKT TKTSRLPIID 1450 1460 VAPLDVGAPD QEFGFDVGPA CFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal liver.
[2]	"Structural characterization of N-terminal antigenic determinants in calf and human collagen." Rauterberg J., Timpl R., Furthmayr H. Eur. J. Biochem. 27:231-237(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 162-180.
[3]	"The covalent structure of collagen: amino-acid sequence of the cyanogen-bromide peptides alpha-1-CB2, alpha-1-CB4 and alpha-1-CB5 from calf-skin collagen." Fietzek P.P., Kuehn K. Eur. J. Biochem. 52:77-82(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 181-306.
[4]	"The covalent structure of collagen: amino acid sequence of alpha-1-CB3 from calf skin collagen." Fietzek P.P., Wendt P., Kell I., Kuehn K. FEBS Lett. 26:74-76(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 580-728.
[5]	"The covalent structure of collagen. 2. The amino-acid sequence of alpha-1-CB7 from calf-skin collagen." Fietzek P.P., Rexrodt F.W., Hopper K.E., Kuehn K. Eur. J. Biochem. 38:396-400(1973) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 729-999.
[6]	"The covalent structure of collagen. The amino-acid sequence of the 112-residues. Amino-terminal part of peptide alpha-1-CB6 from calf-skin collagen." Wendt P., Mark K.V.D., Rexrodt F., Kuehn K. Eur. J. Biochem. 30:169-183(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1000-1112.
[7]	"The covalent structure of collagen. Amino-acid sequence of peptide alpha-1-CB6-C2." Fietzek P.P., Rexrodt F.W., Wendt P., Stark M., Kuehn K. Eur. J. Biochem. 30:163-168(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1113-1188.
[8]	"The amino acid sequence of the carboxyterminal nonhelical cross link region of the alpha 1 chain of calf skin collagen." Rauterberg J., Fietzek P., Rexrodt F., Becker U., Stark M., Kuehn K. FEBS Lett. 21:75-79(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1196-1215.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC105184 mRNA. Translation: AAI05185.1.
IPI	IPI00707857.
PIR	CGBO1S. A91193.
RefSeq	NP_001029211.1. NM_001034039.2.
UniGene	Bt.23316.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P02453. 1 interaction.
Proteomic databases
PaxDb	P02453.
PRIDE	P02453.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000017420; ENSBTAP00000017420; ENSBTAG00000013103.
GeneID	282187.
KEGG	bta:282187.
Organism-specific databases
CTD	1277.
Phylogenomic databases
eggNOG	NOG12793.
GeneTree	ENSGT00660000095287.
HOGENOM	HOG000085654.
HOVERGEN	HBG004933.
InParanoid	P02453.
KO	K06236.
OMA	VAYMDQQ.
OrthoDB	EOG4S4PHP.
Gene expression databases
ArrayExpress	P02453.
Family and domain databases
InterPro	IPR008160. Collagen. IPR000885. Fib_collagen_C. IPR001007. VWF_C. [Graphical view]
Pfam	PF01410. COLFI. 1 hit. PF01391. Collagen. 11 hits. PF00093. VWC. 1 hit. [Graphical view]
ProDom	PD002078. Fib_collagen_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00038. COLFI. 1 hit. SM00214. VWC. 1 hit. [Graphical view]
PROSITE	PS51461. NC1_FIB. 1 hit. PS01208. VWFC_1. 1 hit. PS50184. VWFC_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20806015.
PMAP-CutDB	P02453.

Entry information

Entry name

CO1A1_BOVIN

Accession

Primary (citable) accession number: P02453
Secondary accession number(s): Q3MHM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	May 30, 2006
Last modified:	April 3, 2013
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program