Collagen alpha-1(II) chain precursor

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P02459 (CO2A1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Collagen alpha-1(II) chain

Alternative name(s):
Alpha-1 type II collagen

Gene names

Name:

COL2A1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1487 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 II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
Subunit structure	Homotrimers of alpha 1(II) chains.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
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	Probably 3-hydroxylated on prolines by LEPREL1 By similarity. Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains. O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.
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
Coding sequence diversity	Polymorphism
Domain	Collagen Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cartilage condensation Inferred from electronic annotation. Source: Compara cartilage development involved in endochondral bone morphogenesis Inferred from electronic annotation. Source: Compara cellular response to BMP stimulus Inferred from electronic annotation. Source: Compara central nervous system development Inferred from electronic annotation. Source: Compara chondrocyte differentiation Inferred from electronic annotation. Source: Compara collagen fibril organization Inferred from electronic annotation. Source: Compara embryonic skeletal joint morphogenesis Inferred from electronic annotation. Source: Compara endochondral ossification Inferred from electronic annotation. Source: Compara heart morphogenesis Inferred from electronic annotation. Source: Compara inner ear morphogenesis Inferred from electronic annotation. Source: Compara limb bud formation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara notochord development Inferred from electronic annotation. Source: Compara otic vesicle development Inferred from electronic annotation. Source: Compara palate development Inferred from electronic annotation. Source: Compara proteoglycan metabolic process Inferred from electronic annotation. Source: Compara regulation of gene expression Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from electronic annotation. Source: Compara tissue homeostasis Inferred from electronic annotation. Source: Compara visual perception Inferred from electronic annotation. Source: Compara
Cellular_component	basement membrane Inferred from electronic annotation. Source: Compara collagen type II 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: InterPro 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 – 25

Potential

Propeptide

26 – 181

156

N-terminal propeptide By similarity

PRO_0000401210

Chain

182 – 1487

1306

Collagen alpha-1(II) chain

PRO_0000005725

Regions

Domain

32 – 90

VWFC

Domain

1253 – 1487

235

Fibrillar collagen NC1

Region

201 – 1214

1014

Triple-helical region By similarity

Region

1215 – 1241

Nonhelical region (C-terminal) By similarity

Sites

Metal binding

1301

Calcium By similarity

Metal binding

1303

Calcium By similarity

Metal binding

1304

Calcium; via carbonyl oxygen By similarity

Metal binding

1306

Calcium; via carbonyl oxygen By similarity

Metal binding

1309

Calcium By similarity

Site

181 – 182

Cleavage; by procollagen N-endopeptidase By similarity

Site

1241 – 1242

Cleavage; by procollagen C-endopeptidase By similarity

Amino acid modifications

Modified residue

190

5-hydroxylysine By similarity

Modified residue

212

Hydroxyproline

Modified residue

218

Hydroxyproline

Modified residue

230

Hydroxyproline

Modified residue

233

Hydroxyproline

Modified residue

245

Hydroxyproline

Modified residue

248

Hydroxyproline

Modified residue

251

Hydroxyproline

Modified residue

260

Hydroxyproline

Modified residue

269

Hydroxyproline

Modified residue

278

Hydroxyproline

Modified residue

281

Hydroxyproline

Modified residue

284

Hydroxyproline

Modified residue

287

5-hydroxylysine Ref.2

Modified residue

293

Hydroxyproline

Modified residue

299

5-hydroxylysine Ref.2

Modified residue

305

Hydroxyproline

Modified residue

308

5-hydroxylysine Ref.2

Modified residue

314

Hydroxyproline

Modified residue

320

Hydroxyproline

Modified residue

329

Hydroxyproline

Modified residue

350

Hydroxyproline

Modified residue

356

Hydroxyproline

Modified residue

365

Hydroxyproline

Modified residue

368

Hydroxyproline

Modified residue

371

Hydroxyproline

Modified residue

374

5-hydroxylysine Ref.4

Modified residue

395

Hydroxyproline

Modified residue

398

Hydroxyproline

Modified residue

401

Hydroxyproline

Modified residue

410

Hydroxyproline

Modified residue

416

Hydroxyproline

Modified residue

419

5-hydroxylysine Ref.4

Modified residue

425

Hydroxyproline

Modified residue

431

Hydroxyproline

Modified residue

434

Hydroxyproline

Modified residue

440

Hydroxyproline

Modified residue

452

5-hydroxylysine Ref.4

Modified residue

458

Hydroxyproline

Modified residue

464

5-hydroxylysine Ref.4

Modified residue

470

5-hydroxylysine Ref.4

Modified residue

473

Hydroxyproline

Modified residue

482

Hydroxyproline

Modified residue

497

Hydroxyproline

Modified residue

506

Hydroxyproline

Modified residue

512

Hydroxyproline

Modified residue

518

Hydroxyproline

Modified residue

527

5-hydroxylysine Ref.4

Modified residue

530

Hydroxyproline

Modified residue

542

5-hydroxylysine Ref.4

Modified residue

551

Hydroxyproline

Modified residue

557

Hydroxyproline

Modified residue

566

Hydroxyproline

Modified residue

581

Hydroxyproline

Modified residue

587

Hydroxyproline

Modified residue

590

Hydroxyproline

Modified residue

599

Hydroxyproline

Modified residue

605

Hydroxyproline

Modified residue

608

5-hydroxylysine Ref.5

Modified residue

614

Hydroxyproline

Modified residue

620

5-hydroxylysine Ref.5

Modified residue

623

Hydroxyproline

Modified residue

626

Hydroxyproline

Modified residue

632

Hydroxyproline

Modified residue

644

Hydroxyproline

Modified residue

659

Hydroxyproline

Modified residue

668

Hydroxyproline

Modified residue

670

3-hydroxyproline By similarity

Modified residue

671

Hydroxyproline

Modified residue

674

Hydroxyproline

Modified residue

907

3-hydroxyproline By similarity

Modified residue

1130

5-hydroxylysine By similarity

Modified residue

1144

3-hydroxyproline By similarity

Modified residue

1186

3-hydroxyproline By similarity

Modified residue

1201

3-hydroxyproline By similarity

Modified residue

1207

3-hydroxyproline By similarity

Modified residue

1213

3-hydroxyproline By similarity

Glycosylation

190

O-linked (Gal...) By similarity

Glycosylation

287

O-linked (Gal...) Ref.2

Glycosylation

299

O-linked (Gal...) Ref.2

Glycosylation

308

O-linked (Gal...) Ref.2

Glycosylation

374

O-linked (Gal...) By similarity

Glycosylation

608

O-linked (Gal...) Ref.5

Glycosylation

620

O-linked (Gal...) Ref.5

Glycosylation

1130

O-linked (Gal...) By similarity

Glycosylation

1388

N-linked (GlcNAc...) Potential

Disulfide bond

1283 ↔ 1315

By similarity

Disulfide bond

1289

Interchain (with C-1306) By similarity

Disulfide bond

1306

Interchain (with C-1289) By similarity

Disulfide bond

1323 ↔ 1485

By similarity

Disulfide bond

1393 ↔ 1438

By similarity

Natural variations

Natural variant

349

Q → L. Ref.3

Experimental info

Sequence conflict

202

P → V AA sequence Ref.2

Sequence conflict

380

T → Q AA sequence Ref.4

Sequence conflict

400

S → A AA sequence Ref.4

Sequence conflict

412

T → A AA sequence Ref.4

Sequence conflict

436

P → A AA sequence Ref.4

Sequence conflict

443

Q → T AA sequence Ref.4

Sequence conflict

446

T → S AA sequence Ref.4

Sequence conflict

476

A → T in AAA30436. Ref.6

Sequence conflict

478

P → V AA sequence Ref.4

Sequence conflict

514

N → S AA sequence Ref.4

Sequence conflict

518

P → S in AAA30436. Ref.6

Sequence conflict

523

L → I AA sequence Ref.4

Sequence conflict

529

A → P AA sequence Ref.4

Sequence conflict

535 – 539

PSGLA → SPGAV AA sequence Ref.4

Sequence conflict

544 – 548

ANGDP → SPGEA AA sequence Ref.4

Sequence conflict

554

P → A AA sequence Ref.4

Sequence conflict

560

R → K AA sequence Ref.4

Sequence conflict

677

G → P AA sequence Ref.5

Sequence conflict

712

S → A in AAD42347. Ref.7

Sequence conflict

718

A → P in AAD42347. Ref.7

Sequence conflict

734

A → S in AAD42347. Ref.7

Sequence conflict

1372

N → D in CAA26269. Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

P02459 [UniParc].

Last modified November 30, 2010. Version 4.
Checksum: F99891F6FD1E47F9
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FASTA

1,487

141,828

        10         20         30         40         50         60 
MIRLGAPQTL VLLTLLVAAV LRCHGQDVQK AGSCVQDGQR YNDKDVWKPE PCRICVCDTG 

        70         80         90        100        110        120 
TVLCDDIICE DMKDCLSPET PFGECCPICS ADLPTASGQP GPKGQKGEPG DIKDIVGPKG 

       130        140        150        160        170        180 
PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA 

       190        200        210        220        230        240 
AQMAGGFDEK AGGAQMGVMQ GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG 

       250        260        270        280        290        300 
PRGPPGPPGK PGDDGEAGKP GKSGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG 

       310        320        330        340        350        360 
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP GPAGPPGPVG 

       370        380        390        400        410        420 
PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS PGPAGAAGNP GTDGIPGAKG 

       430        440        450        460        470        480 
SAGAPGIAGA PGFPGPRGPP GPQGATGPLG PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG 

       490        500        510        520        530        540 
APGPAGEEGK RGARGEPGGA GPAGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG 

       550        560        570        580        590        600 
PKGANGDPGR PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG 

       610        620        630        640        650        660 
VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA GERGEQGAPG 

       670        680        690        700        710        720 
PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE RGFPGERGSP GSQGLQGARG 

       730        740        750        760        770        780 
LPGTPGTDGP KGAAGPAGPP GAQGPPGLQG MPGERGAAGI AGPKGDRGDV GEKGPEGAPG 

       790        800        810        820        830        840 
KDGGRGLTGP IGPPGPAGAN GEKGEVGPPG PAGTAGARGA PGERGETGPP GPAGFAGPPG 

       850        860        870        880        890        900 
ADGQPGAKGE QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG 

       910        920        930        940        950        960 
AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGDPGLQGPA GPPGEKGEPG 

       970        980        990       1000       1010       1020 
DDGPSGPDGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP SGEPGKQGAP GASGDRGPPG 

      1030       1040       1050       1060       1070       1080 
PVGPPGLTGP AGEPGREGSP GADGPPGRDG AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG 

      1090       1100       1110       1120       1130       1140 
PIGKQGDRGE AGAQGPMGPA GPAGARGMPG PQGPRGDKGE TGEAGERGLK GHRGFTGLQG 

      1150       1160       1170       1180       1190       1200 
LPGPPGPSGD QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG 

      1210       1220       1230       1240       1250       1260 
PPGNPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPLQYMR ADEAAGNLRQ HDAEVDATLK 

      1270       1280       1290       1300       1310       1320 
SLNNQIESLR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI DPNQGCTLDA MKVFCNMETG 

      1330       1340       1350       1360       1370       1380 
ETCVYPNPAS VPKKNWWSSK SKDKKHIWFG ETINGGFHFS YGDDNLAPNT ANVQMTFLRL 

      1390       1400       1410       1420       1430       1440 
LSTEGSQNIT YHCKNSIAYL DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTVLKDGCTK 

      1450       1460       1470       1480 
HTGKWGKTMI EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of taurine cattle: a window to ruminant biology and evolution." The bovine genome sequencing and analysis consortium Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hereford.
[2]	"The covalent structure of cartilage collagen. Amino acid sequence of the NH2-terminal helical portion of the alpha 1 (II) chain." Butler W.T., Miller E.J., Finch J.E. Jr. Biochemistry 15:3000-3006(1976) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 201-362, HYDROXYLATION AT PRO-212; PRO-218; PRO-230; PRO-233; PRO-245; PRO-248; PRO-251; PRO-260; PRO-269; PRO-278; PRO-281; PRO-284; LYS-287; PRO-293; LYS-299; PRO-305; LYS-308; PRO-314; PRO-320; PRO-329; PRO-350 AND PRO-356, GLYCOSYLATION AT LYS-287; LYS-299 AND LYS-308. Tissue: Cartilage.
[3]	"The covalent structure of cartilage collagen. Evidence for sequence heterogeneity of bovine alpha1(II) chains." Butler W.T., Finch J.E. Jr., Miller E.J. J. Biol. Chem. 252:639-643(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 345-359, HYDROXYLATION AT PRO-350 AND PRO-356, VARIANT LEU-349. Tissue: Cartilage.
[4]	"Covalent structure of collagen. Amino acid sequence of an arthritogenic cyanogen bromide peptide from type II collagen of bovine cartilage." Seyer J.M., Hasty K.A., Kang A.H. Eur. J. Biochem. 181:159-173(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 324-602, HYDROXYLATION AT PRO-329; PRO-350; PRO-356; PRO-365; PRO-368; PRO-371; LYS-374; PRO-395; PRO-398; PRO-401; PRO-410; PRO-416; LYS-419; PRO-425; PRO-431; PRO-434; PRO-440; LYS-452; PRO-458; LYS-464; LYS-470; PRO-473; PRO-482; PRO-497; PRO-506; PRO-512; PRO-518; LYS-527; PRO-530; LYS-542; PRO-551; PRO-557; PRO-566; PRO-581; PRO-587; PRO-590 AND PRO-599, GLYCOSYLATION AT LYS-374; LYS-419; LYS-452; LYS-464; LYS-470; LYS-527 AND LYS-542. Tissue: Cartilage.
[5]	"Homologous regions of collagen alpha1(I) and alpha1(II) chains: apparent clustering of variable and invariant amino acid residues." Butler W.T., Miller E.J., Finch J.E. Jr., Inagami T. Biochem. Biophys. Res. Commun. 57:190-195(1974) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 603-677, HYDROXYLATION AT PRO-605; LYS-608; PRO-614; LYS-620; PRO-623; PRO-626; PRO-632; PRO-644; PRO-659; PRO-668; PRO-671 AND PRO-674, GLYCOSYLATION AT LYS-608 AND LYS-620.
[6]	"Characterization of the T cell determinants in the induction of autoimmune arthritis by bovine alpha 1(II)-CB11 in H-2q mice." Brand D.D., Myers L.K., Terato K., Whittington K.B., Stuart J.M., Kang A.H., Rosloniec E.F. J. Immunol. 152:3088-3097(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 323-602. Tissue: Chondrocyte.
[7]	"Molecular definition and characterization of recombinant bovine CB8 and CB10: immunogenicity and arthritogenicity." Tang B., Chiang T.M., Brand D.D., Gumanovskaya M.L., Stuart J.M., Kang A.H., Myers L.K. Clin. Immunol. 92:256-264(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 602-751. Tissue: Chondrocyte.
[8]	"Analysis of cDNA and genomic clones coding for the pro alpha 1 chain of calf type II collagen." Sangiorgi F.O., Benson-Chanda V., de Wet W.J., Sobel M.E., Ramirez F. Nucleic Acids Res. 13:2815-2826(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1307-1487.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFC03017082 Genomic DNA. No translation available. AAFC03017085 Genomic DNA. No translation available. AAFC03056593 Genomic DNA. No translation available. L28918 mRNA. Translation: AAA30436.2. AF138883 mRNA. Translation: AAD42346.1. AF138957 mRNA. Translation: AAD42347.1. X02420 mRNA. Translation: CAA26269.1.
IPI	IPI01028216.
PIR	CGBO6C. A90369. I45876.
RefSeq	NP_001001135.2. NM_001001135.2.
UniGene	Bt.21390.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P02459. 1 interaction.
STRING	9913.ENSBTAP00000017505.
Proteomic databases
PRIDE	P02459.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000017505; ENSBTAP00000017505; ENSBTAG00000013155.
GeneID	407142.
KEGG	bta:407142.
Organism-specific databases
CTD	1280.
Phylogenomic databases
eggNOG	NOG12793.
GeneTree	ENSGT00660000095287.
HOGENOM	HOG000085654.
HOVERGEN	HBG004933.
InParanoid	Q9XT25.
KO	K06236.
OMA	SSCRICV.
Enzyme and pathway databases
Reactome	REACT_133391. Extracellular matrix organization.
Gene expression databases
ArrayExpress	P02459.
Family and domain databases
InterPro	IPR008160. Collagen. IPR000885. Fib_collagen_C. IPR001007. VWF_C. [Graphical view]
Pfam	PF01410. COLFI. 1 hit. PF01391. Collagen. 10 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	20818406.
PMAP-CutDB	P02459.

Entry information

Entry name

CO2A1_BOVIN

Accession

Primary (citable) accession number: P02459
Secondary accession number(s): Q28070, Q9XT24, Q9XT25

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 30, 2010
Last modified:	April 3, 2013
This is version 115 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents