ID   FINC_NOTVI              Reviewed;         190 AA.
AC   Q91400;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Fibronectin;
DE            Short=FN;
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=7734733; DOI=10.1002/aja.1002020207;
RA   Nace J.D., Tassava R.A.;
RT   "Examination of fibronectin distribution and its sources in the
RT   regenerating newt limb by immunocytochemistry and in situ hybridization.";
RL   Dev. Dyn. 202:153-164(1995).
CC   -!- FUNCTION: Fibronectins bind cell surfaces and various compounds
CC       including collagen, fibrin, heparin, DNA, and actin. Fibronectins are
CC       involved in cell adhesion, cell motility, opsonization, wound healing,
CC       and maintenance of cell shape. May be involved in osteoblast compaction
CC       (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Beneath wound epithelium, fibronectin probably provides a
CC       substrate on which the dedifferentiation stump tissue cells will
CC       migrate and accumulate.
CC   -!- SUBUNIT: Dimers or multimers of alternatively spliced variants,
CC       connected by 2 disulfide bonds near the carboxyl ends. {ECO:0000250}.
CC   -!- PTM: Forms covalent cross-links mediated by a transglutaminase, such as
CC       F13A or TGM2, between a glutamine and the epsilon-amino group of a
CC       lysine residue, forming homopolymers and heteropolymers (e.g.
CC       fibrinogen-fibronectin, collagen-fibronectin heteropolymers).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; S76886; AAB34250.1; -; mRNA.
DR   PIR; I51279; I51279.
DR   AlphaFoldDB; Q91400; -.
DR   SMR; Q91400; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd00061; FN1; 1.
DR   CDD; cd00062; FN2; 1.
DR   Gene3D; 2.10.10.10; -; 1.
DR   InterPro; IPR000083; Fibronectin_type1.
DR   InterPro; IPR000562; FN_type2_dom.
DR   InterPro; IPR036943; FN_type2_sf.
DR   InterPro; IPR013806; Kringle-like.
DR   Pfam; PF00039; fn1; 3.
DR   Pfam; PF00040; fn2; 1.
DR   SMART; SM00058; FN1; 3.
DR   SMART; SM00059; FN2; 1.
DR   SUPFAM; SSF57440; SSF57440; 1.
DR   PROSITE; PS01253; FN1_1; 1.
DR   PROSITE; PS51091; FN1_2; 3.
DR   PROSITE; PS51092; FN2_2; 1.
PE   2: Evidence at transcript level;
KW   Acute phase; Cell adhesion; Cell shape; Disulfide bond; Glycoprotein;
KW   Heparin-binding; Repeat.
FT   CHAIN           <1..>190
FT                   /note="Fibronectin"
FT                   /id="PRO_0000158532"
FT   DOMAIN          <1..50
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT                   ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          55..98
FT                   /note="Fibronectin type-I 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          103..145
FT                   /note="Fibronectin type-I 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          146..>190
FT                   /note="Fibronectin type-I 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        7..33
FT                   /evidence="ECO:0000250"
FT   DISULFID        21..48
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        83..95
FT                   /evidence="ECO:0000250"
FT   DISULFID        105..132
FT                   /evidence="ECO:0000250"
FT   DISULFID        130..142
FT                   /evidence="ECO:0000250"
FT   DISULFID        174..186
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         190
SQ   SEQUENCE   190 AA;  21960 MW;  2C2033226D6B4233 CRC64;
     NSNGASCHFP FLYNNRNYTD CTSEGRRDSM KWCGTTLNLY ADQKFGFCPM AAHEEICTTN
     EGVMYRVGVQ VDKQHDQGHM MRCTCVGNGR GEWNCVAYSQ LRDQCIVDGI TYDVNHTFTK
     RHEEGHMMNC TCYGQGRGWW KCDAIDQCQD SETRQFYQIG DSWEKHVQGV RYQCYSIGRG
     IGEWHCQPLQ