ID   COCA1_RABIT             Reviewed;         639 AA.
AC   Q28902;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Collagen alpha-1(XII) chain;
DE   Flags: Fragment;
GN   Name=COL12A1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cornea;
RX   PubMed=7615021; DOI=10.1016/s0014-4835(05)80070-3;
RA   Zhan Q., Burrows R., Cintron C.;
RT   "Localization of type XII collagen in normal and healing rabbit cornea by
RT   in situ hybridization.";
RL   Exp. Eye Res. 60:551-561(1995).
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   -!- PTM: The triple-helical tail is stabilized by disulfide bonds at each
CC       end. {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. {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; S78179; AAB34889.2; -; mRNA.
DR   AlphaFoldDB; Q28902; -.
DR   SMR; Q28902; -.
DR   STRING; 9986.ENSOCUP00000013193; -.
DR   PRIDE; Q28902; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   InParanoid; Q28902; -.
DR   Proteomes; UP000001811; 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   CDD; cd00063; FN3; 5.
DR   Gene3D; 2.60.40.10; -; 6.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF00041; fn3; 5.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00060; FN3; 5.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49265; SSF49265; 4.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   PROSITE; PS50853; FN3; 5.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Collagen; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Hydroxylation; Reference proteome; Repeat; Secreted.
FT   CHAIN           <1..>639
FT                   /note="Collagen alpha-1(XII) chain"
FT                   /id="PRO_0000059402"
FT   DOMAIN          <1..114
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          130..219
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          220..310
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          311..401
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          402..490
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          491..585
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          586..>639
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          473..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         639
SQ   SEQUENCE   639 AA;  71033 MW;  162C6A923F551E6C CRC64;
     CRKSLLQAVA NLPYKGGNTL TGMALNFIRQ QNFKTQAGMR PRARKIGVLI TDGKSQDDVE
     APSKKLKDEG VELFAIGIKN ADEVELKMIA TDPDDTHAYN VADFDSLSKI VDDLTINLCN
     SVKGPGDLEA PSNLVISERT HRSFRVSWTP PSDSVDRYKV EYYPVSGGKR QEFYVSRLET
     STVLKDLKPE TEYVVNVYSV VEDEYSEPLK GTEKTLPVPI VSLNIYDIGP TTMRVQWQPV
     GGATGYTVSY EPVKTTESTK PKEMRVGPTV NDVQLTDLLP STEYEVTVQA VLHDLTSEPA
     TAREMTLPLP RPQDVKLRDV THSTMSVFWE PVLGKVRKYV VRYQTPEEDV KEVEVDRSRT
     STSLKDLLSQ TLYTVSVSAV YDEGESPPVT AQETTRPVPA PTNLRITEVT PESFRGTWDH
     GASDVSLYRI TWAPFGSSDK METILNGDEN TLVFENLNPN TLYEVSVTAI YPDESESDDL
     TGSERTSPKS GPRNLQVYNA TSNSLTVKWD PASGRVQKYR ITYQPSRGEG NEQTTTIGGR
     QNSVVLQKLK PDTPYTITVS SLYPDGEGGR MTGRGKTKPL NTVRNLRVYD PSTSTLNVRW
     DHAEGNPRQY KLFYAPTAGG SEELVPIPGN TNYAILRNL