COCA1_BOVIN
ID COCA1_BOVIN Reviewed; 86 AA.
AC P25508;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 02-JUN-2021, entry version 87.
DE RecName: Full=Collagen alpha-1(XII) chain;
DE Flags: Fragments;
GN Name=COL12A1;
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 PROTEIN SEQUENCE, AND HYDROXYLATION AT PRO-6; PRO-9; PRO-12; PRO-18;
RP PRO-24; PRO-27; PRO-30; PRO-42; PRO-51; PRO-54; PRO-65; PRO-74; PRO-77 AND
RP PRO-80.
RX PubMed=3133242; DOI=10.1016/0014-5793(88)81379-6;
RA Dublet B., Dixon E., de Miguel E., van der Rest M.;
RT "Bovine type XII collagen: amino acid sequence of a 10 kDa pepsin fragment
RT from periodontal ligament reveals a high degree of homology with the
RT chicken alpha 1(XII) sequence.";
RL FEBS Lett. 233:177-180(1988).
CC -!- FUNCTION: Type XII collagen interacts with type I collagen-containing
CC fibrils, the COL1 domain could be associated with the surface of the
CC fibrils, and the COL2 and NC3 domains may be localized in the
CC perifibrillar matrix.
CC -!- SUBUNIT: Trimer of identical chains each containing 190 kDa of non-
CC triple-helical sequences.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- PTM: The triple-helical tail is stabilized by disulfide bonds at each
CC end.
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 {ECO:0000269|PubMed:3133242}.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR PIR; S00802; S00802.
DR PRIDE; P25508; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Collagen; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Hydroxylation; Reference proteome; Repeat; Secreted.
FT CHAIN <1..>86
FT /note="Collagen alpha-1(XII) chain"
FT /id="PRO_0000059401"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 9
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 12
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 18
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 24
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 27
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 30
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 42
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 51
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 54
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 65
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 74
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 77
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT MOD_RES 80
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3133242"
FT NON_CONS 15..16
FT /evidence="ECO:0000305"
FT NON_CONS 48..49
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 86
SQ SEQUENCE 86 AA; 8063 MW; 163A35AF553EA48D CRC64;
NQPGPPGPPG PPGSAGEPGP GGRPGFPGTP GMQGPQGERG LPGEXGERGL PGPPGPQGES
RTGPPGSTGS RGPPGPPGRP GDSGIR
