CO1A2_BOVIN
ID CO1A2_BOVIN Reviewed; 1364 AA.
AC P02465; A6QP13; O62649;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Collagen alpha-2(I) chain;
DE AltName: Full=Alpha-2 type I collagen;
DE Flags: Precursor;
GN Name=COL1A2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aorta;
RX PubMed=9628255; DOI=10.1016/s0945-053x(98)90127-5;
RA Shirai T., Hattori S., Sakaguchi M., Inouye S., Kimura A., Ebihara T.,
RA Irie S., Nagai Y., Hori H.;
RT "The complete cDNA coding sequence for the bovine proalpha2(I) chain of
RT type I procollagen.";
RL Matrix Biol. 17:85-88(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 80-98, PYROGLUTAMATE FORMATION AT GLN-80, AND ALLYSINE
RP AT LYS-84.
RC TISSUE=Skin;
RX PubMed=4609475; DOI=10.1016/0005-2795(74)90001-4;
RA Fietzek P.P., Breitkreutz D., Kuehn K.;
RT "Amino acid sequence of the amino-terminal region of calf skin collagen.";
RL Biochim. Biophys. Acta 365:305-310(1974).
RN [4]
RP PROTEIN SEQUENCE OF 95-415, SEQUENCE REVISION, AND HYDROXYLATION AT
RP PRO-100; PRO-106; PRO-115; PRO-118; PRO-121; PRO-133; PRO-136; PRO-145;
RP PRO-151; PRO-166; PRO-169; PRO-172; LYS-175; PRO-190; PRO-193; LYS-196;
RP PRO-199; PRO-202; PRO-208; PRO-217; PRO-226; PRO-253; PRO-256; PRO-259;
RP LYS-262; PRO-271; PRO-286; PRO-295; PRO-304; LYS-307; PRO-313; PRO-319;
RP PRO-322; PRO-328; PRO-346; LYS-352; PRO-361; PRO-367; PRO-370; PRO-391;
RP PRO-394; PRO-400 AND PRO-406.
RC TISSUE=Skin;
RX PubMed=173531; DOI=10.1111/j.1432-1033.1975.tb02431.x;
RA Fietzek P.P., Rexrodt F.W.;
RT "The covalent structure of collagen. The amino-acid sequence of alpha2-CB4
RT from calf-skin collagen.";
RL Eur. J. Biochem. 59:113-118(1975).
RN [5]
RP PROTEIN SEQUENCE OF 416-445, AND HYDROXYLATION AT PRO-439 AND PRO-442.
RC TISSUE=Skin;
RX PubMed=4412529; DOI=10.1111/j.1432-1033.1974.tb03689.x;
RA Fietzek P.P., Furthmayr H., Kuehn K.;
RT "Comparative sequence studies on alpha2-CB2 from calf, human, rabbit and
RT pig-skin collagen.";
RL Eur. J. Biochem. 47:257-261(1974).
RN [6]
RP PROTEIN SEQUENCE OF 446-481.
RC TISSUE=Skin;
RX PubMed=4435743; DOI=10.1515/bchm2.1974.355.1.647;
RA Fietzek P.P., Kuehn K.;
RT "The covalent structure of collagen: amino acid sequence of the N-terminal
RT region of alpha2-CB3 from rat skin collagen and alpha2-CB3.5 from calf skin
RT collagen.";
RL Hoppe-Seyler's Z. Physiol. Chem. 355:647-650(1974).
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen).
CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones.
CC In bones the fibrils are mineralized with calcium hydroxyapatite.
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: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; AB008683; BAA25171.1; -; mRNA.
DR EMBL; BC149095; AAI49096.1; -; mRNA.
DR PIR; A90596; CGBO2S.
DR RefSeq; NP_776945.1; NM_174520.2.
DR AlphaFoldDB; P02465; -.
DR ComplexPortal; CPX-3101; Collagen type I trimer.
DR IntAct; P02465; 1.
DR MINT; P02465; -.
DR STRING; 9913.ENSBTAP00000033771; -.
DR Allergome; 3550; Bos d alpha2I.0101.
DR Allergome; 896; Bos d alpha2I.
DR PaxDb; P02465; -.
DR PeptideAtlas; P02465; -.
DR PRIDE; P02465; -.
DR Ensembl; ENSBTAT00000033863; ENSBTAP00000033771; ENSBTAG00000013472.
DR GeneID; 282188; -.
DR KEGG; bta:282188; -.
DR CTD; 1278; -.
DR VEuPathDB; HostDB:ENSBTAG00000013472; -.
DR VGNC; VGNC:27561; COL1A2.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155639; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; P02465; -.
DR OMA; SFYWIDP; -.
DR OrthoDB; 1406711at2759; -.
DR TreeFam; TF344135; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000013472; Expressed in uterine cervix and 105 other tissues.
DR ExpressionAtlas; P02465; baseline and differential.
DR GO; GO:0005584; C:collagen type I trimer; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 5.
DR SMART; SM00038; COLFI; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P02466"
FT PROPEP 23..79
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000269|PubMed:4609475"
FT /id="PRO_0000005798"
FT CHAIN 80..1117
FT /note="Collagen alpha-2(I) chain"
FT /id="PRO_0000005799"
FT PROPEP 1118..1364
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT /id="PRO_0000005800"
FT DOMAIN 1131..1364
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 26..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..812
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT MOD_RES 80
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:4609475"
FT MOD_RES 84
FT /note="Allysine"
FT /evidence="ECO:0000305|PubMed:4609475"
FT MOD_RES 100
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 106
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 115
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 118
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 121
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 133
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 136
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 145
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 151
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 166
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 169
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 172
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 175
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 190
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 193
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 196
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 199
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 202
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 208
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 217
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 226
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 253
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 256
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 259
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 262
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 271
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 286
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 295
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 304
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 307
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 313
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 319
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 322
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 328
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 346
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 352
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 361
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 367
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 370
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 391
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 394
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 400
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 406
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:173531"
FT MOD_RES 439
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4412529"
FT MOD_RES 442
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4412529"
FT CARBOHYD 175
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT CARBOHYD 1265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1161..1193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1201..1362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1270..1315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT CONFLICT 157
FT /note="V -> P (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="K -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="T -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 298..300
FT /note="PGA -> AGP (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 423..424
FT /note="AT -> TA (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1364 AA; 129064 MW; 5593F4D6B9ED119A CRC64;
MLSFVDTRTL LLLAVTSCLA TCQSLQEATA RKGPSGDRGP RGERGPPGPP GRDGDDGIPG
PPGPPGPPGP PGLGGNFAAQ FDAKGGGPGP MGLMGPRGPP GASGAPGPQG FQGPPGEPGE
PGQTGPAGAR GPPGPPGKAG EDGHPGKPGR PGERGVVGPQ GARGFPGTPG LPGFKGIRGH
NGLDGLKGQP GAPGVKGEPG APGENGTPGQ TGARGLPGER GRVGAPGPAG ARGSDGSVGP
VGPAGPIGSA GPPGFPGAPG PKGELGPVGN PGPAGPAGPR GEVGLPGLSG PVGPPGNPGA
NGLPGAKGAA GLPGVAGAPG LPGPRGIPGP VGAAGATGAR GLVGEPGPAG SKGESGNKGE
PGAVGQPGPP GPSGEEGKRG STGEIGPAGP PGPPGLRGNP GSRGLPGADG RAGVMGPAGS
RGATGPAGVR GPNGDSGRPG EPGLMGPRGF PGSPGNIGPA GKEGPVGLPG IDGRPGPIGP
AGARGEPGNI GFPGPKGPSG DPGKAGEKGH AGLAGARGAP GPDGNNGAQG PPGLQGVQGG
KGEQGPAGPP GFQGLPGPAG TAGEAGKPGE RGIPGEFGLP GPAGARGERG PPGESGAAGP
TGPIGSRGPS GPPGPDGNKG EPGVVGAPGT AGPSGPSGLP GERGAAGIPG GKGEKGETGL
RGDIGSPGRD GARGAPGAIG APGPAGANGD RGEAGPAGPA GPAGPRGSPG ERGEVGPAGP
NGFAGPAGAA GQPGAKGERG TKGPKGENGP VGPTGPVGAA GPSGPNGPPG PAGSRGDGGP
PGATGFPGAA GRTGPPGPSG ISGPPGPPGP AGKEGLRGPR GDQGPVGRSG ETGASGPPGF
VGEKGPSGEP GTAGPPGTPG PQGLLGAPGF LGLPGSRGER GLPGVAGSVG EPGPLGIAGP
PGARGPPGNV GNPGVNGAPG EAGRDGNPGN DGPPGRDGQP GHKGERGYPG NAGPVGAAGA
PGPQGPVGPV GKHGNRGEPG PAGAVGPAGA VGPRGPSGPQ GIRGDKGEPG DKGPRGLPGL
KGHNGLQGLP GLAGHHGDQG APGAVGPAGP RGPAGPSGPA GKDGRIGQPG AVGPAGIRGS
QGSQGPAGPP GPPGPPGPPG PSGGGYEFGF DGDFYRADQP RSPTSLRPKD YEVDATLKSL
NNQIETLLTP EGSRKNPART CRDLRLSHPE WSSGYYWIDP NQGCTMDAIK VYCDFSTGET
CIRAQPEDIP VKNWYRNSKA KKHVWVGETI NGGTQFEYNV EGVTTKEMAT QLAFMRLLAN
HASQNITYHC KNSIAYMDEE TGNLKKAVIL QGSNDVELVA EGNSRFTYTV LVDGCSKKTN
EWQKTIIEYK TNKPSRLPIL DIAPLDIGGA DQEIRLNIGP VCFK
