COCA1_RAT
ID COCA1_RAT Reviewed; 317 AA.
AC P70560; P70559;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Collagen alpha-1(XII) chain;
DE Flags: Fragment;
GN Name=Col12a1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC STRAIN=CD Charles River;
RX PubMed=10419532; DOI=10.1074/jbc.274.31.22053;
RA Kania A.M., Reichenberger E., Baur S.T., Karimbux N.Y., Taylor R.W.,
RA Olsen B.R., Nishimura I.;
RT "Structural variation of type XII collagen at its carboxyl-terminal NC1
RT domain generated by tissue-specific alternative splicing.";
RL J. Biol. Chem. 274:22053-22059(1999).
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. {ECO:0000250}.
CC -!- SUBUNIT: Trimer of identical chains each containing 190 kDa of non-
CC triple-helical sequences. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long; Synonyms=AK#M;
CC IsoId=P70560-1; Sequence=Displayed;
CC Name=Short; Synonyms=AK#G;
CC IsoId=P70560-2; Sequence=VSP_001153, VSP_001154;
CC -!- PTM: The triple-helical tail is stabilized by disulfide bonds at each
CC end. {ECO:0000250}.
CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
CC -!- PTM: O-glycosylated; glycosaminoglycan of chondroitin-sulfate type.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; U57362; AAB07870.1; -; mRNA.
DR EMBL; U57361; AAB07869.1; -; mRNA.
DR AlphaFoldDB; P70560; -.
DR PhosphoSitePlus; P70560; -.
DR PRIDE; P70560; -.
DR UCSC; RGD:2374; rat. [P70560-1]
DR RGD; 2374; Col12a1.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005595; C:collagen type XII trimer; IDA:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome;
KW Repeat; Secreted.
FT CHAIN <1..317
FT /note="Collagen alpha-1(XII) chain"
FT /id="PRO_0000059403"
FT REGION <1..97
FT /note="Triple-helical region (COL2) with 1 imperfection"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..140
FT /note="Nonhelical region (NC2)"
FT REGION 130..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..243
FT /note="Triple-helical region (COL1) with 2 imperfections"
FT REGION 244..262
FT /note="Nonhelical region (NC1)"
FT MOTIF 94..96
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 23..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 146
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 149
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 164
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 167
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 170
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 182
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 199
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 213
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 222
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 225
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 228
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT VAR_SEQ 260..262
FT /note="EPY -> GSG (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10419532"
FT /id="VSP_001153"
FT VAR_SEQ 263..317
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10419532"
FT /id="VSP_001154"
FT CONFLICT 134
FT /note="H -> Y (in Ref. 1; AAB07869)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="A -> R (in Ref. 1; AAB07869)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="R -> P (in Ref. 1; AAB07869)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 317 AA; 32001 MW; 859C0FDA6FB166BC CRC64;
PGEPGRQGMK GDAGEPGLPG RTGTPGLPGP PGPMGPPGDR GFTGKDGAMG PRGPPGPPGT
PGSPGVAGPS GKPGKPGDHG RPGQSGLKGE KGDRGDIASQ NMMRAVARQV CEQLISGQMS
RFNQMLNQIP NDYHSNRNQP GPPGPPGPPG AAGARGEPGP GGAPGFPGRP GVQGPPGERG
LPGEKGERGI GSQGPRGPPG PPGPQGESRT GPPGSTGSRG PPGPPGRPGN SGIRGPPGPP
GYCDSSQCAS IPYNGQGYPE PYVPEGGAYL PDREPFIVPV EPERTAEYED DYGADEPEQQ
HPDHRRWRRA LRPGPGQ
