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P28481

- CO2A1_MOUSE

UniProt

P28481 - CO2A1_MOUSE

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Protein

Collagen alpha-1(II) chain

Gene

Col2a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei181 – 1822Cleavage; by procollagen N-endopeptidaseBy similarity
Sitei1241 – 12422Cleavage; by procollagen C-endopeptidaseBy similarity
Metal bindingi1301 – 13011CalciumBy similarity
Metal bindingi1303 – 13031CalciumBy similarity
Metal bindingi1304 – 13041Calcium; via carbonyl oxygenBy similarity
Metal bindingi1306 – 13061Calcium; via carbonyl oxygenBy similarity
Metal bindingi1309 – 13091CalciumBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. identical protein binding Source: IntAct
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. bone development Source: MGI
  2. cartilage condensation Source: MGI
  3. cartilage development Source: MGI
  4. cartilage development involved in endochondral bone morphogenesis Source: MGI
  5. cellular response to BMP stimulus Source: MGI
  6. central nervous system development Source: UniProtKB
  7. chondrocyte differentiation Source: UniProtKB
  8. collagen fibril organization Source: MGI
  9. embryonic skeletal joint morphogenesis Source: Ensembl
  10. endochondral ossification Source: MGI
  11. heart morphogenesis Source: MGI
  12. inner ear development Source: MGI
  13. inner ear morphogenesis Source: MGI
  14. limb bud formation Source: UniProtKB
  15. limb morphogenesis Source: MGI
  16. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  17. notochord development Source: UniProtKB
  18. ossification Source: UniProtKB
  19. otic vesicle development Source: UniProtKB
  20. palate development Source: MGI
  21. proteoglycan metabolic process Source: MGI
  22. regulation of gene expression Source: MGI
  23. sensory perception of sound Source: Ensembl
  24. skeletal system morphogenesis Source: MGI
  25. tissue homeostasis Source: MGI
  26. visual perception Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(II) chain
Alternative name(s):
Alpha-1 type II collagen
Cleaved into the following 2 chains:
Gene namesi
Name:Col2a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:88452. Col2a1.

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. collagen trimer Source: MGI
  3. collagen type II trimer Source: MGI
  4. cytoplasm Source: MGI
  5. extracellular matrix Source: MGI
  6. extracellular space Source: MGI
  7. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in Col2a1 are the cause of a phenotype resembling human spondyloepiphyseal dysplasia congenita (sedc). Homozygous sedc mice can be identified at birth by their small size and shortened trunk. Adults have shortened noses, dysplastic vertebrae, femora and tibias, and retinoschisis and hearing loss.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Propeptidei26 – 181156N-terminal propeptideBy similarityPRO_0000005732Add
BLAST
Chaini182 – 12411060Collagen alpha-1(II) chainPRO_0000005733Add
BLAST
Chaini1242 – 1487246ChondrocalcinPRO_0000005734Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 19015-hydroxylysineBy similarity
Glycosylationi190 – 1901O-linked (Gal...)By similarity
Modified residuei287 – 28715-hydroxylysineBy similarity
Glycosylationi287 – 2871O-linked (Gal...)By similarity
Modified residuei299 – 29915-hydroxylysineBy similarity
Glycosylationi299 – 2991O-linked (Gal...)By similarity
Modified residuei308 – 30815-hydroxylysineBy similarity
Glycosylationi308 – 3081O-linked (Gal...)By similarity
Modified residuei374 – 37415-hydroxylysineBy similarity
Glycosylationi374 – 3741O-linked (Gal...)By similarity
Modified residuei608 – 60815-hydroxylysineBy similarity
Glycosylationi608 – 6081O-linked (Gal...)By similarity
Modified residuei620 – 62015-hydroxylysineBy similarity
Glycosylationi620 – 6201O-linked (Gal...)By similarity
Modified residuei670 – 67013-hydroxyprolineBy similarity
Modified residuei907 – 90713-hydroxyprolineBy similarity
Modified residuei1144 – 114413-hydroxyprolineBy similarity
Modified residuei1186 – 118613-hydroxyprolineBy similarity
Modified residuei1201 – 120113-hydroxyprolineBy similarity
Modified residuei1207 – 120713-hydroxyprolineBy similarity
Modified residuei1213 – 121313-hydroxyprolineBy similarity
Disulfide bondi1283 ↔ 1315PROSITE-ProRule annotation
Disulfide bondi1289 – 1289Interchain (with C-1306)PROSITE-ProRule annotation
Disulfide bondi1306 – 1306Interchain (with C-1289)PROSITE-ProRule annotation
Disulfide bondi1323 ↔ 1485PROSITE-ProRule annotation
Disulfide bondi1393 ↔ 1438PROSITE-ProRule annotation

Post-translational modificationi

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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP28481.
PaxDbiP28481.
PRIDEiP28481.

PTM databases

PhosphoSiteiP28481.

Expressioni

Developmental stagei

Expressed in chondrogenic tissues in advance of chondrocyte differentiation. Expressed early in embryogenesis at 9.5 days both in the cranial mesenchyme destined for the chondrocranium, and the sclerotome of the somites, and at 12.5 days in the primordia of the hyoid and the laryngeal cartilage. Detected in all the chondrogenic tissues of the axial and appendicular skeleton until the onset of endochondral ossification. Expression also observed in non-chondrogenic tissues such as the notochord. Also expressed much later in the tail tendon, at 16.5-18.5 days. Transiently expressed in the heart at 9.5-12.5 days, the epidermis at 10.5-14.5 days, the calvarial mesenchyme at 12.5-16.5 days, the inner ear at 14.5 days and the fetal brain from 9.5-14.5 days. Within the neural tube, expression is localized to the proliferative ventricular cells of the forebrain and midbrain of 9.5-10.5 day embryos, and subsequently, restricted to the rhombencephalic basal plate, the ventricular layer of the hindbrain and the cervical spinal cord.1 Publication

Gene expression databases

BgeeiP28481.
CleanExiMM_COL2A1.
ExpressionAtlasiP28481. baseline and differential.
GenevestigatoriP28481.

Interactioni

Subunit structurei

Homotrimers of alpha 1(II) chains.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-738477,EBI-738477

Protein-protein interaction databases

IntActiP28481. 1 interaction.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W65X-ray2.21E530-538[»]
4BKLX-ray3.25E/F/G744-780[»]
ProteinModelPortaliP28481.
SMRiP28481. Positions 29-96, 1271-1487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28481.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 8958VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1253 – 1487235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 12141014Triple-helical regionAdd
BLAST
Regioni1215 – 124127Nonhelical region (C-terminal)Add
BLAST

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

eggNOGiNOG12793.
GeneTreeiENSGT00760000118776.
HOVERGENiHBG004933.
InParanoidiP28481.
KOiK06236.
OMAiPLQYMRA.
OrthoDBiEOG7TJ3HH.
PhylomeDBiP28481.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 11 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]

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P28481-3) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MIRLGAPQSL VLLTLLIAAV LRCQGQDAQE AGSCLQNGQR YKDKDVWKPS
60 70 80 90 100
SCRICVCDTG NVLCDDIICE DPDCLNPEIP FGECCPICPA DLATASGKLG
110 120 130 140 150
PKGQKGEPGD IRDIIGPRGP PGPQGPAGEQ GPRGDRGDKG EKGAPGPRGR
160 170 180 190 200
DGEPGTPGNP GPAGPPGPPG PPGLSAGNFA AQMAGGYDEK AGGAQMGVMQ
210 220 230 240 250
GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG PRGPPGPAGK
260 270 280 290 300
PGDDGEAGKP GKSGERGLPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG
310 320 330 340 350
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP
360 370 380 390 400
GPAGPPGPVG PAGGPGFPGA PGAKGEAGPT GARGPEGAQG SRGEPGNPGS
410 420 430 440 450
PGPAGASGNP GTDGIPGAKG SAGAPGIAGA PGFPGPRGPP GPQGATGPLG
460 470 480 490 500
PKGQAGEPGI AGFKGDQGPK GETGPAGPQG APGPAGEEGK RGARGEPGGA
510 520 530 540 550
GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLTG PKGANGDPGR
560 570 580 590 600
PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG
610 620 630 640 650
VMGFPGPKGA NGEPGKAGEK GLAGAPGLRG LPGKDGETGA AGPPGPSGPA
660 670 680 690 700
GERGEQGAPG PSGFQGLPGP PGPPGEGGKQ GDQGIPGEAG APGLVGPRGE
710 720 730 740 750
RGFPGERGSP GAQGLQGPRG LPGTPGTDGP KGAAGPDGPP GAQGPPGLQG
760 770 780 790 800
MPGERGAAGI AGPKGDRGDV GEKGPEGAPG KDGGRGLTGP IGPPGPAGAN
810 820 830 840 850
GEKGEVGPPG PSGSTGARGA PGERGETGPP GPAGFAGPPG ADGQPGAKGD
860 870 880 890 900
QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG
910 920 930 940 950
AAGRVGPPGA NGNPGPAGPP GPAGKDGPKG VRGDSGPPGR AGDPGLQGPA
960 970 980 990 1000
GAPGEKGEPG DDGPSGLDGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP
1010 1020 1030 1040 1050
SGEPGKQGAP GASGDRGPPG PVGPPGLTGP AGEPGREGSP GADGPPGRDG
1060 1070 1080 1090 1100
AAGVKGDRGE TGALGAPGAP GPPGSPGPAG PTGKQGDRGE AGAQGPMGPS
1110 1120 1130 1140 1150
GPAGARGIAG PQGPRGDKGE SGEQGERGLK GHRGFTGLQG LPGPPGPSGD
1160 1170 1180 1190 1200
QGASGPAGPS GPRGPPGPVG PSGKDGSNGI PGPIGPPGPR GRSGETGPVG
1210 1220 1230 1240 1250
PPGSPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPMQYMR ADEADSTLRQ
1260 1270 1280 1290 1300
HDVEVDATLK SLNNQIESIR SPDGSRKNPA RTCQDLKLCH PEWKSGDYWI
1310 1320 1330 1340 1350
DPNQGCTLDA MKVFCNMETG ETCVYPNPAT VPRKNWWSSK SKEKKHIWFG
1360 1370 1380 1390 1400
ETMNGGFHFS YGDGNLAPNT ANVQMTFLRL LSTEGSQNIT YHCKNSIAYL
1410 1420 1430 1440 1450
DEAAGNLKKA LLIQGSNDVE MRAEGNSRFT YTALKDGCTK HTGKWGKTVI
1460 1470 1480
EYRSQKTSRL PIIDIAPMDI GGAEQEFGVD IGPVCFL

Note: No experimental confirmation available.

Length:1,487
Mass (Da):141,973
Last modified:February 6, 2007 - v2
Checksum:iE52A7F3951C76701
GO
Isoform 2 (identifier: P28481-1) [UniParc]FASTAAdd to Basket

Also known as: Long

The sequence of this isoform differs from the canonical sequence as follows:
     114-142: Missing.

Show »
Length:1,458
Mass (Da):139,110
Checksum:i5B28FCBC6BFB3A95
GO
Isoform 3 (identifier: P28481-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     29-97: QEAGSCLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNPEIPFGECCPICPADLATASG → R
     114-142: Missing.

Show »
Length:1,390
Mass (Da):131,859
Checksum:i514E8A3086208F1B
GO
Isoform 4 (identifier: P28481-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     103-113: Missing.
     125-142: Missing.

Show »
Length:1,458
Mass (Da):139,027
Checksum:i0D7D97A4DD9E1540
GO
Isoform 5 (identifier: P28481-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-124: Missing.
     143-177: Missing.

Show »
Length:1,441
Mass (Da):137,868
Checksum:i88086B838B2876F9
GO
Isoform 6 (identifier: P28481-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     103-113: Missing.
     143-177: Missing.

Show »
Length:1,441
Mass (Da):137,785
Checksum:iAB4C30D6A44C5DDE
GO
Isoform 7 (identifier: P28481-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     29-97: QEAGSCLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNPEIPFGECCPICPADLATASG → R

Note: No experimental confirmation available.

Show »
Length:1,419
Mass (Da):134,722
Checksum:iF0173B07E7C72D5C
GO

Sequence cautioni

The sequence BAC25865.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971G → GR in AAA68100. (PubMed:1885613)Curated
Sequence conflicti97 – 971G → GR in AAA68101. (PubMed:1885613)Curated
Sequence conflicti97 – 971G → GR in AAA68099. (PubMed:1885613)Curated
Sequence conflicti97 – 971G → GR in AAA68102. (PubMed:1885613)Curated
Sequence conflicti272 – 2721Q → M in AAA68100. (PubMed:1885613)Curated
Sequence conflicti272 – 2721Q → M in AAA68101. (PubMed:1885613)Curated
Sequence conflicti272 – 2721Q → M in AAA68099. (PubMed:1885613)Curated
Sequence conflicti272 – 2721Q → M in AAA68102. (PubMed:1885613)Curated
Sequence conflicti539 – 5391T → A in AAA68100. (PubMed:1885613)Curated
Sequence conflicti539 – 5391T → A in AAA68101. (PubMed:1885613)Curated
Sequence conflicti539 – 5391T → A in AAA68099. (PubMed:1885613)Curated
Sequence conflicti539 – 5391T → A in AAA68102. (PubMed:1885613)Curated
Sequence conflicti806 – 8061V → A in AAA68100. (PubMed:1885613)Curated
Sequence conflicti806 – 8061V → A in AAA68101. (PubMed:1885613)Curated
Sequence conflicti806 – 8061V → A in AAA68099. (PubMed:1885613)Curated
Sequence conflicti806 – 8061V → A in AAA68102. (PubMed:1885613)Curated
Sequence conflicti824 – 8241R → P in AAA68100. (PubMed:1885613)Curated
Sequence conflicti824 – 8241R → P in AAA68101. (PubMed:1885613)Curated
Sequence conflicti824 – 8241R → P in AAA68099. (PubMed:1885613)Curated
Sequence conflicti947 – 9471Q → E in AAA68100. (PubMed:1885613)Curated
Sequence conflicti947 – 9471Q → E in AAA68101. (PubMed:1885613)Curated
Sequence conflicti947 – 9471Q → E in AAA68099. (PubMed:1885613)Curated
Sequence conflicti947 – 9471Q → E in AAA68102. (PubMed:1885613)Curated
Sequence conflicti1119 – 11191G → R in AAH51383. (PubMed:15489334)Curated
Sequence conflicti1141 – 11455LPGPP → SAWPS in AAC06113. (PubMed:1797232)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti989 – 9891R → C in sedc mice. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei29 – 9769QEAGS…ATASG → R in isoform 3 and isoform 7. 1 PublicationVSP_022780Add
BLAST
Alternative sequencei103 – 11311Missing in isoform 4 and isoform 6. CuratedVSP_022781Add
BLAST
Alternative sequencei114 – 14229Missing in isoform 2 and isoform 3. CuratedVSP_022782Add
BLAST
Alternative sequencei114 – 12411Missing in isoform 5. CuratedVSP_022783Add
BLAST
Alternative sequencei125 – 14218Missing in isoform 4. CuratedVSP_022784Add
BLAST
Alternative sequencei143 – 17735Missing in isoform 5 and isoform 6. CuratedVSP_022785Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M65161 Genomic DNA. Translation: AAA68099.1.
M65161 Genomic DNA. Translation: AAA68100.1.
M65161 Genomic DNA. Translation: AAA68101.1.
M65161 Genomic DNA. Translation: AAA68102.1.
BC030913 mRNA. Translation: AAH30913.1.
BC051383 mRNA. Translation: AAH51383.1.
BC052326 mRNA. Translation: AAH52326.1.
BC082331 mRNA. Translation: AAH82331.1.
S63190 Genomic DNA. Translation: AAB19627.1.
M63708 Genomic DNA. Translation: AAA37436.1.
M63709 Genomic DNA. Translation: AAC06113.1.
M63710 Genomic DNA. Translation: AAA37435.1.
AK028295 mRNA. Translation: BAC25865.1. Different initiation.
X57982 Genomic DNA. Translation: CAA41047.1.
CCDSiCCDS37189.2. [P28481-3]
CCDS49716.1. [P28481-7]
PIRiA41182.
B41182.
RefSeqiNP_001106987.2. NM_001113515.2. [P28481-7]
NP_112440.2. NM_031163.3. [P28481-3]
UniGeneiMm.2423.

Genome annotation databases

EnsembliENSMUST00000023123; ENSMUSP00000023123; ENSMUSG00000022483. [P28481-3]
ENSMUST00000088355; ENSMUSP00000085693; ENSMUSG00000022483. [P28481-7]
GeneIDi12824.
KEGGimmu:12824.
UCSCiuc007xlp.2. mouse. [P28481-3]
uc007xlq.2. mouse. [P28481-7]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M65161 Genomic DNA. Translation: AAA68099.1 .
M65161 Genomic DNA. Translation: AAA68100.1 .
M65161 Genomic DNA. Translation: AAA68101.1 .
M65161 Genomic DNA. Translation: AAA68102.1 .
BC030913 mRNA. Translation: AAH30913.1 .
BC051383 mRNA. Translation: AAH51383.1 .
BC052326 mRNA. Translation: AAH52326.1 .
BC082331 mRNA. Translation: AAH82331.1 .
S63190 Genomic DNA. Translation: AAB19627.1 .
M63708 Genomic DNA. Translation: AAA37436.1 .
M63709 Genomic DNA. Translation: AAC06113.1 .
M63710 Genomic DNA. Translation: AAA37435.1 .
AK028295 mRNA. Translation: BAC25865.1 . Different initiation.
X57982 Genomic DNA. Translation: CAA41047.1 .
CCDSi CCDS37189.2. [P28481-3 ]
CCDS49716.1. [P28481-7 ]
PIRi A41182.
B41182.
RefSeqi NP_001106987.2. NM_001113515.2. [P28481-7 ]
NP_112440.2. NM_031163.3. [P28481-3 ]
UniGenei Mm.2423.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2W65 X-ray 2.21 E 530-538 [» ]
4BKL X-ray 3.25 E/F/G 744-780 [» ]
ProteinModelPortali P28481.
SMRi P28481. Positions 29-96, 1271-1487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P28481. 1 interaction.

PTM databases

PhosphoSitei P28481.

Proteomic databases

MaxQBi P28481.
PaxDbi P28481.
PRIDEi P28481.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023123 ; ENSMUSP00000023123 ; ENSMUSG00000022483 . [P28481-3 ]
ENSMUST00000088355 ; ENSMUSP00000085693 ; ENSMUSG00000022483 . [P28481-7 ]
GeneIDi 12824.
KEGGi mmu:12824.
UCSCi uc007xlp.2. mouse. [P28481-3 ]
uc007xlq.2. mouse. [P28481-7 ]

Organism-specific databases

CTDi 1280.
MGIi MGI:88452. Col2a1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118776.
HOVERGENi HBG004933.
InParanoidi P28481.
KOi K06236.
OMAi PLQYMRA.
OrthoDBi EOG7TJ3HH.
PhylomeDBi P28481.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

ChiTaRSi COL2A1. mouse.
EvolutionaryTracei P28481.
NextBioi 282306.
PROi P28481.
SOURCEi Search...

Gene expression databases

Bgeei P28481.
CleanExi MM_COL2A1.
ExpressionAtlasi P28481. baseline and differential.
Genevestigatori P28481.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 11 hits.
PF00093. VWC. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse type II collagen gene. Complete nucleotide sequence, exon structure, and alternative splicing."
    Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.
    J. Biol. Chem. 266:16862-16869(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7).
    Strain: C57BL/6.
    Tissue: Brain, Eye and Olfactory epithelium.
  3. "Expression of the mouse alpha 1(II) collagen gene is not restricted to cartilage during development."
    Cheah K.S., Lau E.T., Au P.K., Tam P.P.
    Development 111:945-953(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, DEVELOPMENTAL STAGE.
  4. "The mouse Col2a-1 gene is highly conserved and is linked to Int-1 on chromosome 15."
    Cheah K.S., Au P.K., Lau E.T., Little P.F., Stubbs L.
    Mamm. Genome 1:171-183(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28; 1031-1145 AND 1359-1487.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 597-1487.
    Strain: C57BL/6J.
    Tissue: Head.
  6. "Specific hybridization probes for mouse type I, II, III and IX collagen mRNAs."
    Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.
    Biochim. Biophys. Acta 1089:241-243(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1483-1487.
  7. "A missense mutation in the mouse Col2a1 gene causes spondyloepiphyseal dysplasia congenita, hearing loss, and retinoschisis."
    Donahue L.R., Chang B., Mohan S., Miyakoshi N., Wergedal J.E., Baylink D.J., Hawes N.L., Rosen C.J., Ward-Bailey P., Zheng Q.Y., Bronson R.T., Johnson K.R., Davisson M.T.
    J. Bone Miner. Res. 18:1612-1621(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SEDC CYS-989.

Entry informationi

Entry nameiCO2A1_MOUSE
AccessioniPrimary (citable) accession number: P28481
Secondary accession number(s): Q61428
, Q62031, Q62032, Q62033, Q641K3, Q6LDB1, Q6LDI8, Q6LDI9, Q80VY3, Q80X38, Q8CEF7, Q8K0N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 6, 2007
Last modified: October 29, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3