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P28481 (CO2A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(II) chain
Alternative name(s):
Alpha-1 type II collagen

Cleaved into the following 2 chains:

  1. Collagen alpha-1(II) chain
  2. Chondrocalcin
Gene names
Name:Col2a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1487 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular matrix By similarity.

Developmental stage

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. Ref.3

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.

Involvement in disease

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.

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 VWFC domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainCollagen
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone development

Inferred from mutant phenotype PubMed 11254354. Source: MGI

cartilage condensation

Inferred from mutant phenotype PubMed 3070812. Source: MGI

cartilage development

Inferred from mutant phenotype PubMed 10100048PubMed 11171689PubMed 11680679PubMed 7276808PubMed 7590256PubMed 9061443PubMed 9165353PubMed 9832566. Source: MGI

cartilage development involved in endochondral bone morphogenesis

Inferred from mutant phenotype PubMed 11680679PubMed 8989518PubMed 9022054. Source: MGI

cellular response to BMP stimulus

Inferred from direct assay PubMed 20501701. Source: MGI

central nervous system development

Inferred from expression pattern PubMed 9119111. Source: UniProtKB

chondrocyte differentiation

Inferred from expression pattern PubMed 9119111. Source: UniProtKB

collagen fibril organization

Inferred from mutant phenotype PubMed 11171689PubMed 3070812PubMed 7276808PubMed 7590256PubMed 8989518PubMed 9022054PubMed 9832566PubMed 9915573. Source: MGI

embryonic skeletal joint morphogenesis

Inferred from electronic annotation. Source: Ensembl

endochondral ossification

Inferred from mutant phenotype PubMed 10100048. Source: MGI

heart morphogenesis

Inferred from mutant phenotype PubMed 7590256. Source: MGI

inner ear development

Inferred from mutant phenotype PubMed 10100048. Source: MGI

inner ear morphogenesis

Inferred from mutant phenotype PubMed 9165353. Source: MGI

limb bud formation

Inferred from expression pattern PubMed 20940257. Source: UniProtKB

limb morphogenesis

Inferred from mutant phenotype PubMed 10100048. Source: MGI

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from mutant phenotype PubMed 9299161. Source: MGI

notochord development

Inferred from expression pattern PubMed 9119111. Source: UniProtKB

ossification

Inferred from expression pattern PubMed 9119111. Source: UniProtKB

otic vesicle development

Inferred from expression pattern PubMed 9119111. Source: UniProtKB

palate development

Inferred from mutant phenotype PubMed 7276808. Source: MGI

proteoglycan metabolic process

Inferred from mutant phenotype PubMed 3070812PubMed 7276808. Source: MGI

regulation of gene expression

Inferred from mutant phenotype PubMed 9299161. Source: MGI

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

skeletal system morphogenesis

Inferred from mutant phenotype PubMed 7276808PubMed 7590256PubMed 8192242PubMed 9915573. Source: MGI

tissue homeostasis

Inferred from mutant phenotype PubMed 11237662. Source: MGI

visual perception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 11273670. Source: MGI

collagen trimer

Inferred from direct assay PubMed 17683922PubMed 20812917. Source: MGI

collagen type II trimer

Inferred from direct assay PubMed 9880238. Source: MGI

cytoplasm

Inferred from direct assay PubMed 12799063PubMed 14614991. Source: MGI

extracellular matrix

Inferred from direct assay PubMed 16079159PubMed 1879364PubMed 21624478PubMed 24191021PubMed 9449075. Source: MGI

extracellular space

Inferred from direct assay PubMed 12799063PubMed 14614991. Source: MGI

   Molecular_functionextracellular matrix structural constituent

Inferred from electronic annotation. Source: InterPro

identical protein binding

Inferred from physical interaction PubMed 22248926. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-738477,EBI-738477

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28481-3)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: P28481-1)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     114-142: Missing.
Isoform 3 (identifier: P28481-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     29-97: QEAGSCLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNPEIPFGECCPICPADLATASG → R
     114-142: Missing.
Isoform 4 (identifier: P28481-4)

The sequence of this isoform differs from the canonical sequence as follows:
     103-113: Missing.
     125-142: Missing.
Isoform 5 (identifier: P28481-5)

The sequence of this isoform differs from the canonical sequence as follows:
     114-124: Missing.
     143-177: Missing.
Isoform 6 (identifier: P28481-6)

The sequence of this isoform differs from the canonical sequence as follows:
     103-113: Missing.
     143-177: Missing.
Isoform 7 (identifier: P28481-7)

The sequence of this isoform differs from the canonical sequence as follows:
     29-97: QEAGSCLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNPEIPFGECCPICPADLATASG → R
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 181156N-terminal propeptide By similarity
PRO_0000005732
Chain182 – 12411060Collagen alpha-1(II) chain
PRO_0000005733
Chain1242 – 1487246Chondrocalcin
PRO_0000005734

Regions

Domain32 – 8958VWFC
Domain1253 – 1487235Fibrillar collagen NC1
Region201 – 12141014Triple-helical region
Region1215 – 124127Nonhelical region (C-terminal)

Sites

Metal binding13011Calcium By similarity
Metal binding13031Calcium By similarity
Metal binding13041Calcium; via carbonyl oxygen By similarity
Metal binding13061Calcium; via carbonyl oxygen By similarity
Metal binding13091Calcium By similarity
Site181 – 1822Cleavage; by procollagen N-endopeptidase By similarity
Site1241 – 12422Cleavage; by procollagen C-endopeptidase By similarity

Amino acid modifications

Modified residue19015-hydroxylysine By similarity
Modified residue28715-hydroxylysine By similarity
Modified residue29915-hydroxylysine By similarity
Modified residue30815-hydroxylysine By similarity
Modified residue37415-hydroxylysine By similarity
Modified residue60815-hydroxylysine By similarity
Modified residue62015-hydroxylysine By similarity
Modified residue67013-hydroxyproline By similarity
Modified residue90713-hydroxyproline By similarity
Modified residue114413-hydroxyproline By similarity
Modified residue118613-hydroxyproline By similarity
Modified residue120113-hydroxyproline By similarity
Modified residue120713-hydroxyproline By similarity
Modified residue121313-hydroxyproline By similarity
Glycosylation1901O-linked (Gal...) By similarity
Glycosylation2871O-linked (Gal...) By similarity
Glycosylation2991O-linked (Gal...) By similarity
Glycosylation3081O-linked (Gal...) By similarity
Glycosylation3741O-linked (Gal...) By similarity
Glycosylation6081O-linked (Gal...) By similarity
Glycosylation6201O-linked (Gal...) By similarity
Disulfide bond1283 ↔ 1315 By similarity
Disulfide bond1289Interchain (with C-1306) By similarity
Disulfide bond1306Interchain (with C-1289) By similarity
Disulfide bond1323 ↔ 1485 By similarity
Disulfide bond1393 ↔ 1438 By similarity

Natural variations

Alternative sequence29 – 9769QEAGS…ATASG → R in isoform 3 and isoform 7.
VSP_022780
Alternative sequence103 – 11311Missing in isoform 4 and isoform 6.
VSP_022781
Alternative sequence114 – 14229Missing in isoform 2 and isoform 3.
VSP_022782
Alternative sequence114 – 12411Missing in isoform 5.
VSP_022783
Alternative sequence125 – 14218Missing in isoform 4.
VSP_022784
Alternative sequence143 – 17735Missing in isoform 5 and isoform 6.
VSP_022785
Natural variant9891R → C in sedc mice. Ref.7

Experimental info

Sequence conflict971G → GR in AAA68100. Ref.1
Sequence conflict971G → GR in AAA68101. Ref.1
Sequence conflict971G → GR in AAA68099. Ref.1
Sequence conflict971G → GR in AAA68102. Ref.1
Sequence conflict2721Q → M in AAA68100. Ref.1
Sequence conflict2721Q → M in AAA68101. Ref.1
Sequence conflict2721Q → M in AAA68099. Ref.1
Sequence conflict2721Q → M in AAA68102. Ref.1
Sequence conflict5391T → A in AAA68100. Ref.1
Sequence conflict5391T → A in AAA68101. Ref.1
Sequence conflict5391T → A in AAA68099. Ref.1
Sequence conflict5391T → A in AAA68102. Ref.1
Sequence conflict8061V → A in AAA68100. Ref.1
Sequence conflict8061V → A in AAA68101. Ref.1
Sequence conflict8061V → A in AAA68099. Ref.1
Sequence conflict8061V → A in AAA68102. Ref.1
Sequence conflict8241R → P in AAA68100. Ref.1
Sequence conflict8241R → P in AAA68101. Ref.1
Sequence conflict8241R → P in AAA68099. Ref.1
Sequence conflict9471Q → E in AAA68100. Ref.1
Sequence conflict9471Q → E in AAA68101. Ref.1
Sequence conflict9471Q → E in AAA68099. Ref.1
Sequence conflict9471Q → E in AAA68102. Ref.1
Sequence conflict11191G → R in AAH51383. Ref.2
Sequence conflict1141 – 11455LPGPP → SAWPS in AAC06113. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: E52A7F3951C76701

FASTA1,487141,973
        10         20         30         40         50         60 
MIRLGAPQSL VLLTLLIAAV LRCQGQDAQE AGSCLQNGQR YKDKDVWKPS SCRICVCDTG 

        70         80         90        100        110        120 
NVLCDDIICE DPDCLNPEIP FGECCPICPA DLATASGKLG PKGQKGEPGD IRDIIGPRGP 

       130        140        150        160        170        180 
PGPQGPAGEQ GPRGDRGDKG EKGAPGPRGR DGEPGTPGNP GPAGPPGPPG PPGLSAGNFA 

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

       250        260        270        280        290        300 
PRGPPGPAGK PGDDGEAGKP GKSGERGLPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG 

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

       370        380        390        400        410        420 
PAGGPGFPGA PGAKGEAGPT GARGPEGAQG SRGEPGNPGS PGPAGASGNP GTDGIPGAKG 

       430        440        450        460        470        480 
SAGAPGIAGA PGFPGPRGPP GPQGATGPLG PKGQAGEPGI AGFKGDQGPK GETGPAGPQG 

       490        500        510        520        530        540 
APGPAGEEGK RGARGEPGGA GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLTG 

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

       610        620        630        640        650        660 
VMGFPGPKGA NGEPGKAGEK GLAGAPGLRG LPGKDGETGA AGPPGPSGPA GERGEQGAPG 

       670        680        690        700        710        720 
PSGFQGLPGP PGPPGEGGKQ GDQGIPGEAG APGLVGPRGE RGFPGERGSP GAQGLQGPRG 

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

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

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

       910        920        930        940        950        960 
AAGRVGPPGA NGNPGPAGPP GPAGKDGPKG VRGDSGPPGR AGDPGLQGPA GAPGEKGEPG 

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

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

      1090       1100       1110       1120       1130       1140 
PTGKQGDRGE AGAQGPMGPS GPAGARGIAG PQGPRGDKGE SGEQGERGLK GHRGFTGLQG 

      1150       1160       1170       1180       1190       1200 
LPGPPGPSGD QGASGPAGPS GPRGPPGPVG PSGKDGSNGI PGPIGPPGPR GRSGETGPVG 

      1210       1220       1230       1240       1250       1260 
PPGSPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPMQYMR ADEADSTLRQ HDVEVDATLK 

      1270       1280       1290       1300       1310       1320 
SLNNQIESIR SPDGSRKNPA RTCQDLKLCH PEWKSGDYWI DPNQGCTLDA MKVFCNMETG 

      1330       1340       1350       1360       1370       1380 
ETCVYPNPAT VPRKNWWSSK SKEKKHIWFG ETMNGGFHFS YGDGNLAPNT ANVQMTFLRL 

      1390       1400       1410       1420       1430       1440 
LSTEGSQNIT YHCKNSIAYL DEAAGNLKKA LLIQGSNDVE MRAEGNSRFT YTALKDGCTK 

      1450       1460       1470       1480 
HTGKWGKTVI EYRSQKTSRL PIIDIAPMDI GGAEQEFGVD IGPVCFL 

« Hide

Isoform 2 (Long) [UniParc].

Checksum: 5B28FCBC6BFB3A95
Show »

FASTA1,458139,110
Isoform 3 (Short) [UniParc].

Checksum: 514E8A3086208F1B
Show »

FASTA1,390131,859
Isoform 4 [UniParc].

Checksum: 0D7D97A4DD9E1540
Show »

FASTA1,458139,027
Isoform 5 [UniParc].

Checksum: 88086B838B2876F9
Show »

FASTA1,441137,868
Isoform 6 [UniParc].

Checksum: AB4C30D6A44C5DDE
Show »

FASTA1,441137,785
Isoform 7 [UniParc].

Checksum: F0173B07E7C72D5C
Show »

FASTA1,419134,722

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS37189.2. [P28481-3]
CCDS49716.1. [P28481-7]
PIRA41182.
B41182.
RefSeqNP_001106987.2. NM_001113515.2. [P28481-7]
NP_112440.2. NM_031163.3. [P28481-3]
UniGeneMm.2423.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W65X-ray2.21E530-538[»]
4BKLX-ray3.25E/F/G744-780[»]
ProteinModelPortalP28481.
SMRP28481. Positions 29-96, 1271-1487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP28481. 1 interaction.

PTM databases

PhosphoSiteP28481.

Proteomic databases

PaxDbP28481.
PRIDEP28481.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023123; ENSMUSP00000023123; ENSMUSG00000022483. [P28481-3]
ENSMUST00000088355; ENSMUSP00000085693; ENSMUSG00000022483. [P28481-7]
GeneID12824.
KEGGmmu:12824.
UCSCuc007xlp.2. mouse. [P28481-3]
uc007xlq.2. mouse. [P28481-7]

Organism-specific databases

CTD1280.
MGIMGI:88452. Col2a1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00740000114967.
HOVERGENHBG004933.
InParanoidP28481.
KOK06236.
OMAPLQYMRA.
OrthoDBEOG7TJ3HH.
PhylomeDBP28481.
TreeFamTF344135.

Gene expression databases

BgeeP28481.
CleanExMM_COL2A1.
GenevestigatorP28481.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 11 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

ChiTaRSCOL2A1. mouse.
EvolutionaryTraceP28481.
NextBio282306.
PROP28481.
SOURCESearch...

Entry information

Entry nameCO2A1_MOUSE
AccessionPrimary (citable) accession number: P28481
Secondary accession number(s): Q61428 expand/collapse secondary AC list , Q62031, Q62032, Q62033, Q641K3, Q6LDB1, Q6LDI8, Q6LDI9, Q80VY3, Q80X38, Q8CEF7, Q8K0N6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 6, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot