COCA1_NOTVI
ID COCA1_NOTVI Reviewed; 929 AA.
AC Q91145;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Collagen alpha-1(XII) chain;
DE Flags: Fragment;
OS Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae;
OC Notophthalmus.
OX NCBI_TaxID=8316;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7729585; DOI=10.1006/dbio.1995.1098;
RA Wei Y., Yang E.V., Klatt K.P., Tassava R.A.;
RT "Monoclonal antibody MT2 identifies the urodele alpha 1 chain of type XII
RT collagen, a developmentally regulated extracellular matrix protein in
RT regenerating newt limbs.";
RL Dev. Biol. 168:503-513(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 (By similarity). Could play a developmental role
CC in regeneration. {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 -!- DEVELOPMENTAL STAGE: Expression starts at 3 days after amputation in
CC cells of the basal layer of the wound epithelium. At day 10, expression
CC is found in both the basal wound epithelial cells and the distal
CC mesenchyme cells. At mid-bud and late-bud blastema stages, wound
CC epithelium expression has decreased, whereas the mesenchyme remains
CC strongly active in transcription and showed a tendency toward distal
CC regionalization. Condensing cartilage shows no signal. Finally, at the
CC late digit stage, expression becomes largely restricted to the
CC perichondrium.
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 -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; U19494; AAA80217.1; -; mRNA.
DR PIR; I51027; I51027.
DR AlphaFoldDB; Q91145; -.
DR SMR; Q91145; -.
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; 7.
DR Gene3D; 2.60.40.10; -; 7.
DR Gene3D; 3.40.50.410; -; 2.
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; 7.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00060; FN3; 7.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF53300; SSF53300; 2.
DR PROSITE; PS50853; FN3; 7.
DR PROSITE; PS50234; VWFA; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Collagen; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Proteoglycan; Repeat; Secreted.
FT CHAIN <1..>929
FT /note="Collagen alpha-1(XII) chain"
FT /id="PRO_0000059404"
FT DOMAIN <1..49
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 67..156
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 158..250
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 251..340
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 342..432
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 434..521
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 523..613
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 633..805
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 821..910
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 929
SQ SEQUENCE 929 AA; 101647 MW; AE5D7485254FD954 CRC64;
DVEIFAVGVK DAVRSELEAI ATPPTATHVY TVEDFDAFQR ISFELTQSIW LRIEQELKSI
KVKSLTPPRD LSFAEVTSSS FRVSWSPAAE DAIAYLVNYT VALGGEEFVV SVPAPTTSTV
LTNLFPKTTY EVRVVAEYPE GESPPLKGEE TTLEVRGAPR NLRVTDETTD SFKVGWTPAP
GNVLRYRIAY RPVAGGERKE VTVQGNERAT TLYNLFPDTK YHVSGVPEYQ SGPGTALNGN
GATEEVVGEP KNLRVSEPTT STAMRLTWDK APGKVQRYLR NLHSRSAGGD IKEVTVKGDT
STTVLKELDP GTAYTLSVNP LYASGAGTAV TGEGATLQER GSPRDLIIKD ITDTTIGTSW
TAAPGMVRGY RIAWQSLFDD KTGENHVPGD TTNTVLRNLD PETKYRLSVY ANYASGEGDP
LSGEATTEAS PDGKIVKISE ETETTMKATW QPAPGNVLNY RVVYRPRAGG RQIVAKVPPA
VTSTVLRRLT PLTTYDISVI PVYKEGDGKT RQGSGTTLSP FNAPRSIKTS EPTRSTFRVT
WEPAPGEVKG YKITFHPEGD DGYLGEMMVG PYDSTVVLEE LRARTSYKVN VFGVFDDGQS
PPLIGHETTT LRDAPRSPIP SSGLDCTTKA QADIVLLVDG SWSIGRPNFK IVRNFISRVV
EVFDIGSDRV QIAVSQYSGD PRTEWQLNTH KTKKSLMDAV ANLPYKGGNT NTGSALKFIL
ENNFRPGVGM REKARKIAIL LTDGKSQDDI VAPSKRYADE GIELYAVGIK NADENELKEI
ASDPDELYMY NVADFSLLTN IVNDLTENVC NSVKGPGGLN PPSNLVTSEP TPRSFRVTWV
PPSQSVERFK VEYYPVAGGR PQEVYVRGTQ TTTVLVGLKP ETEYYVNVYS VEGNEISEPL
AGTETTLPIP SVRNMNLYDI GTTTMRVKW
