CO2A1_MOUSE
ID CO2A1_MOUSE Reviewed; 1487 AA.
AC P28481; Q61428; Q62031; Q62032; Q62033; Q641K3; Q6LDB1; Q6LDI8; Q6LDI9;
AC Q80VY3; Q80X38; Q8CEF7; Q8K0N6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Collagen alpha-1(II) chain {ECO:0000250|UniProtKB:P02458};
DE AltName: Full=Alpha-1 type II collagen {ECO:0000250|UniProtKB:P02458};
DE Contains:
DE RecName: Full=Collagen alpha-1(II) chain {ECO:0000250|UniProtKB:P02458};
DE Contains:
DE RecName: Full=Chondrocalcin {ECO:0000250|UniProtKB:P02458};
DE Flags: Precursor;
GN Name=Col2a1 {ECO:0000312|MGI:MGI:88452};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=1885613; DOI=10.1016/s0021-9258(18)55382-5;
RA Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.;
RT "Mouse type II collagen gene. Complete nucleotide sequence, exon structure,
RT and alternative splicing.";
RL J. Biol. Chem. 266:16862-16869(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7).
RC STRAIN=C57BL/6J; TISSUE=Brain, Eye, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, AND DEVELOPMENTAL STAGE.
RX PubMed=1879363; DOI=10.1242/dev.111.4.945;
RA Cheah K.S., Lau E.T., Au P.K., Tam P.P.;
RT "Expression of the mouse alpha 1(II) collagen gene is not restricted to
RT cartilage during development.";
RL Development 111:945-953(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28; 1031-1145 AND 1359-1487.
RX PubMed=1797232; DOI=10.1007/bf00351064;
RA Cheah K.S., Au P.K., Lau E.T., Little P.F., Stubbs L.;
RT "The mouse Col2a-1 gene is highly conserved and is linked to Int-1 on
RT chromosome 15.";
RL Mamm. Genome 1:171-183(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 597-1487.
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1483-1487.
RX PubMed=2054384; DOI=10.1016/0167-4781(91)90014-d;
RA Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.;
RT "Specific hybridization probes for mouse type I, II, III and IX collagen
RT mRNAs.";
RL Biochim. Biophys. Acta 1089:241-243(1991).
RN [7]
RP VARIANT SEDC CYS-989.
RX PubMed=12968670; DOI=10.1359/jbmr.2003.18.9.1612;
RA Donahue L.R., Chang B., Mohan S., Miyakoshi N., Wergedal J.E.,
RA Baylink D.J., Hawes N.L., Rosen C.J., Ward-Bailey P., Zheng Q.Y.,
RA Bronson R.T., Johnson K.R., Davisson M.T.;
RT "A missense mutation in the mouse Col2a1 gene causes spondyloepiphyseal
RT dysplasia congenita, hearing loss, and retinoschisis.";
RL J. Bone Miner. Res. 18:1612-1621(2003).
CC -!- FUNCTION: Type II collagen is specific for cartilaginous tissues. It is
CC essential for the normal embryonic development of the skeleton, for
CC linear growth and for the ability of cartilage to resist compressive
CC forces.
CC -!- SUBUNIT: Homotrimers of alpha 1(II) chains.
CC -!- INTERACTION:
CC P28481; P28481: Col2a1; NbExp=2; IntAct=EBI-738477, EBI-738477;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=P28481-3; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=P28481-1; Sequence=VSP_022782;
CC Name=3; Synonyms=Short;
CC IsoId=P28481-2; Sequence=VSP_022780, VSP_022782;
CC Name=4;
CC IsoId=P28481-4; Sequence=VSP_022781, VSP_022784;
CC Name=5;
CC IsoId=P28481-5; Sequence=VSP_022783, VSP_022785;
CC Name=6;
CC IsoId=P28481-6; Sequence=VSP_022781, VSP_022785;
CC Name=7;
CC IsoId=P28481-7; Sequence=VSP_022780;
CC -!- DEVELOPMENTAL STAGE: Expressed in chondrogenic tissues in advance of
CC chondrocyte differentiation. Expressed early in embryogenesis at 9.5
CC days both in the cranial mesenchyme destined for the chondrocranium,
CC and the sclerotome of the somites, and at 12.5 days in the primordia of
CC the hyoid and the laryngeal cartilage. Detected in all the chondrogenic
CC tissues of the axial and appendicular skeleton until the onset of
CC endochondral ossification. Expression also observed in non-chondrogenic
CC tissues such as the notochord. Also expressed much later in the tail
CC tendon, at 16.5-18.5 days. Transiently expressed in the heart at 9.5-
CC 12.5 days, the epidermis at 10.5-14.5 days, the calvarial mesenchyme at
CC 12.5-16.5 days, the inner ear at 14.5 days and the fetal brain from
CC 9.5-14.5 days. Within the neural tube, expression is localized to the
CC proliferative ventricular cells of the forebrain and midbrain of 9.5-
CC 10.5 day embryos, and subsequently, restricted to the rhombencephalic
CC basal plate, the ventricular layer of the hindbrain and the cervical
CC spinal cord. {ECO:0000269|PubMed:1879363}.
CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC crucial roles in tissue growth and repair by controlling both the
CC intracellular assembly of procollagen molecules and the extracellular
CC assembly of collagen fibrils. It binds a calcium ion which is essential
CC for its function (By similarity). {ECO:0000250}.
CC -!- PTM: Contains mostly 4-hydroxyproline. Prolines at the third position
CC of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or
CC all of the chains. {ECO:0000250|UniProtKB:P05539}.
CC -!- PTM: Contains 3-hydroxyproline at a few sites. This modification occurs
CC on the first proline residue in the sequence motif Gly-Pro-Hyp, where
CC Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P05539}.
CC -!- PTM: Lysine residues at the third position of the tripeptide repeating
CC unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
CC {ECO:0000250|UniProtKB:P05539}.
CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
CC glycan consists of a Glc-Gal disaccharide.
CC {ECO:0000250|UniProtKB:P05539}.
CC -!- DISEASE: Note=Defects in Col2a1 are the cause of a phenotype resembling
CC human spondyloepiphyseal dysplasia congenita (sedc). Homozygous sedc
CC mice can be identified at birth by their small size and shortened
CC trunk. Adults have shortened noses, dysplastic vertebrae, femora and
CC tibias, and retinoschisis and hearing loss.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25865.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M65161; AAA68099.1; -; Genomic_DNA.
DR EMBL; M65161; AAA68100.1; -; Genomic_DNA.
DR EMBL; M65161; AAA68101.1; -; Genomic_DNA.
DR EMBL; M65161; AAA68102.1; -; Genomic_DNA.
DR EMBL; BC030913; AAH30913.1; -; mRNA.
DR EMBL; BC051383; AAH51383.1; -; mRNA.
DR EMBL; BC052326; AAH52326.1; -; mRNA.
DR EMBL; BC082331; AAH82331.1; -; mRNA.
DR EMBL; S63190; AAB19627.1; -; Genomic_DNA.
DR EMBL; M63708; AAA37436.1; -; Genomic_DNA.
DR EMBL; M63709; AAC06113.1; -; Genomic_DNA.
DR EMBL; M63710; AAA37435.1; -; Genomic_DNA.
DR EMBL; AK028295; BAC25865.1; ALT_INIT; mRNA.
DR EMBL; X57982; CAA41047.1; -; Genomic_DNA.
DR CCDS; CCDS37189.2; -. [P28481-3]
DR CCDS; CCDS49716.1; -. [P28481-7]
DR PIR; A41182; A41182.
DR PIR; B41182; B41182.
DR RefSeq; NP_001106987.2; NM_001113515.2. [P28481-7]
DR RefSeq; NP_112440.2; NM_031163.3. [P28481-3]
DR PDB; 2W65; X-ray; 2.21 A; E=530-538.
DR PDB; 4BKL; X-ray; 3.25 A; E/F/G=744-780.
DR PDB; 5MU0; X-ray; 2.70 A; Q/R/S/T/U/V/W/X=555-571.
DR PDB; 5MUB; X-ray; 3.10 A; E/H/K/N/Q/T/W/X=546-577.
DR PDB; 5MV3; X-ray; 2.95 A; E/H/K/N/Q/T/W/X=1179-1208.
DR PDB; 5MV4; X-ray; 2.90 A; E/H/K/N/Q/T/W/X=792-846.
DR PDBsum; 2W65; -.
DR PDBsum; 4BKL; -.
DR PDBsum; 5MU0; -.
DR PDBsum; 5MUB; -.
DR PDBsum; 5MV3; -.
DR PDBsum; 5MV4; -.
DR AlphaFoldDB; P28481; -.
DR SMR; P28481; -.
DR BioGRID; 198814; 6.
DR ComplexPortal; CPX-2957; Collagen type II trimer.
DR ComplexPortal; CPX-2975; Collagen type XI trimer variant 1.
DR IntAct; P28481; 1.
DR STRING; 10090.ENSMUSP00000023123; -.
DR GlyGen; P28481; 7 sites.
DR iPTMnet; P28481; -.
DR PhosphoSitePlus; P28481; -.
DR MaxQB; P28481; -.
DR PaxDb; P28481; -.
DR PeptideAtlas; P28481; -.
DR PRIDE; P28481; -.
DR ABCD; P28481; 19 sequenced antibodies.
DR Antibodypedia; 3697; 776 antibodies from 41 providers.
DR DNASU; 12824; -.
DR Ensembl; ENSMUST00000023123; ENSMUSP00000023123; ENSMUSG00000022483. [P28481-3]
DR Ensembl; ENSMUST00000088355; ENSMUSP00000085693; ENSMUSG00000022483. [P28481-7]
DR GeneID; 12824; -.
DR KEGG; mmu:12824; -.
DR UCSC; uc007xlp.2; mouse. [P28481-3]
DR UCSC; uc007xlq.2; mouse. [P28481-7]
DR CTD; 1280; -.
DR MGI; MGI:88452; Col2a1.
DR VEuPathDB; HostDB:ENSMUSG00000022483; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155224; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; P28481; -.
DR OMA; GWQPGPK; -.
DR OrthoDB; 337699at2759; -.
DR PhylomeDB; P28481; -.
DR TreeFam; TF344135; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474244; Extracellular matrix organization.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-419037; NCAM1 interactions.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12824; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Col2a1; mouse.
DR EvolutionaryTrace; P28481; -.
DR PRO; PR:P28481; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P28481; protein.
DR Bgee; ENSMUSG00000022483; Expressed in epithelium of cochlear duct and 297 other tissues.
DR Genevisible; P28481; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0005581; C:collagen trimer; IDA:MGI.
DR GO; GO:0005585; C:collagen type II trimer; IDA:MGI.
DR GO; GO:0005592; C:collagen type XI trimer; IC:ComplexPortal.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042289; F:MHC class II protein binding; ISO:MGI.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0097065; P:anterior head development; IMP:MGI.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0001502; P:cartilage condensation; IMP:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IDA:MGI.
DR GO; GO:0007417; P:central nervous system development; IEP:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; ISO:MGI.
DR GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0060174; P:limb bud formation; IEP:UniProtKB.
DR GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0030903; P:notochord development; IEP:UniProtKB.
DR GO; GO:0001503; P:ossification; IEP:UniProtKB.
DR GO; GO:0071599; P:otic vesicle development; IEP:UniProtKB.
DR GO; GO:0006029; P:proteoglycan metabolic process; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR GO; GO:0001501; P:skeletal system development; ISO:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR GO; GO:0007601; P:visual perception; ISO:MGI.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 10.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Collagen; Disease variant;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..181
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005732"
FT CHAIN 182..1241
FT /note="Collagen alpha-1(II) chain"
FT /id="PRO_0000005733"
FT CHAIN 1242..1487
FT /note="Chondrocalcin"
FT /id="PRO_0000005734"
FT DOMAIN 32..89
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1253..1487
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 96..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..1214
FT /note="Triple-helical region"
FT REGION 1215..1241
FT /note="Nonhelical region (C-terminal)"
FT COMPBIAS 132..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..173
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 181..182
FT /note="Cleavage; by procollagen N-endopeptidase"
FT /evidence="ECO:0000250"
FT SITE 1241..1242
FT /note="Cleavage; by procollagen C-endopeptidase"
FT /evidence="ECO:0000250"
FT MOD_RES 190
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 287
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 299
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 308
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 374
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 608
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 620
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 659
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 668
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 670
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 671
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 674
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 907
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 908
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 914
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 920
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1144
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1181
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1186
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1187
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1201
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1202
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1205
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1207
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1208
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1211
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1213
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT MOD_RES 1214
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P05539"
FT CARBOHYD 190
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 287
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 299
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 308
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 374
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 608
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 620
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250"
FT DISULFID 1283..1315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1289
FT /note="Interchain (with C-1306)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1306
FT /note="Interchain (with C-1289)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1323..1485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1393..1438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT VAR_SEQ 29..97
FT /note="QEAGSCLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIICEDPDCLNPEIP
FT FGECCPICPADLATASG -> R (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022780"
FT VAR_SEQ 103..113
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_022781"
FT VAR_SEQ 114..142
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_022782"
FT VAR_SEQ 114..124
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_022783"
FT VAR_SEQ 125..142
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_022784"
FT VAR_SEQ 143..177
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_022785"
FT VARIANT 989
FT /note="R -> C (in sedc mice)"
FT /evidence="ECO:0000269|PubMed:12968670"
FT CONFLICT 97
FT /note="G -> GR (in Ref. 1; AAA68100/AAA68101/AAA68099/
FT AAA68102)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="Q -> M (in Ref. 1; AAA68100/AAA68101/AAA68099/
FT AAA68102)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="T -> A (in Ref. 1; AAA68100/AAA68101/AAA68099/
FT AAA68102)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="V -> A (in Ref. 1; AAA68100/AAA68101/AAA68099/
FT AAA68102)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="R -> P (in Ref. 1; AAA68100/AAA68101/AAA68099)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="Q -> E (in Ref. 1; AAA68100/AAA68101/AAA68099/
FT AAA68102)"
FT /evidence="ECO:0000305"
FT CONFLICT 1119
FT /note="G -> R (in Ref. 2; AAH51383)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141..1145
FT /note="LPGPP -> SAWPS (in Ref. 4; AAC06113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1487 AA; 141973 MW; E52A7F3951C76701 CRC64;
MIRLGAPQSL VLLTLLIAAV LRCQGQDAQE AGSCLQNGQR YKDKDVWKPS SCRICVCDTG
NVLCDDIICE DPDCLNPEIP FGECCPICPA DLATASGKLG PKGQKGEPGD IRDIIGPRGP
PGPQGPAGEQ GPRGDRGDKG EKGAPGPRGR DGEPGTPGNP GPAGPPGPPG PPGLSAGNFA
AQMAGGYDEK AGGAQMGVMQ GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG
PRGPPGPAGK PGDDGEAGKP GKSGERGLPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP GPAGPPGPVG
PAGGPGFPGA PGAKGEAGPT GARGPEGAQG SRGEPGNPGS PGPAGASGNP GTDGIPGAKG
SAGAPGIAGA PGFPGPRGPP GPQGATGPLG PKGQAGEPGI AGFKGDQGPK GETGPAGPQG
APGPAGEEGK RGARGEPGGA GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLTG
PKGANGDPGR PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG
VMGFPGPKGA NGEPGKAGEK GLAGAPGLRG LPGKDGETGA AGPPGPSGPA GERGEQGAPG
PSGFQGLPGP PGPPGEGGKQ GDQGIPGEAG APGLVGPRGE RGFPGERGSP GAQGLQGPRG
LPGTPGTDGP KGAAGPDGPP GAQGPPGLQG MPGERGAAGI AGPKGDRGDV GEKGPEGAPG
KDGGRGLTGP IGPPGPAGAN GEKGEVGPPG PSGSTGARGA PGERGETGPP GPAGFAGPPG
ADGQPGAKGD QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG
AAGRVGPPGA NGNPGPAGPP GPAGKDGPKG VRGDSGPPGR AGDPGLQGPA GAPGEKGEPG
DDGPSGLDGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP SGEPGKQGAP GASGDRGPPG
PVGPPGLTGP AGEPGREGSP GADGPPGRDG AAGVKGDRGE TGALGAPGAP GPPGSPGPAG
PTGKQGDRGE AGAQGPMGPS GPAGARGIAG PQGPRGDKGE SGEQGERGLK GHRGFTGLQG
LPGPPGPSGD QGASGPAGPS GPRGPPGPVG PSGKDGSNGI PGPIGPPGPR GRSGETGPVG
PPGSPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPMQYMR ADEADSTLRQ HDVEVDATLK
SLNNQIESIR SPDGSRKNPA RTCQDLKLCH PEWKSGDYWI DPNQGCTLDA MKVFCNMETG
ETCVYPNPAT VPRKNWWSSK SKEKKHIWFG ETMNGGFHFS YGDGNLAPNT ANVQMTFLRL
LSTEGSQNIT YHCKNSIAYL DEAAGNLKKA LLIQGSNDVE MRAEGNSRFT YTALKDGCTK
HTGKWGKTVI EYRSQKTSRL PIIDIAPMDI GGAEQEFGVD IGPVCFL
