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Database: UniProt
Entry: Q28749
LinkDB: Q28749
Original site: Q28749 
ID   FINC_RABIT              Reviewed;         100 AA.
AC   Q28749;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   18-JUL-2018, entry version 102.
DE   RecName: Full=Fibronectin;
DE            Short=FN;
DE   Flags: Fragment;
GN   Name=FN1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7579058;
RA   Sady S.P., Goyal M., Thomas P.E., Wharram B.L., Wiggins R.C.;
RT   "Fibronectin mRNA in the developing glomerular crescent in rabbit
RT   antiglomerular basement membrane disease.";
RL   J. Am. Soc. Nephrol. 5:2087-2090(1995).
CC   -!- FUNCTION: Fibronectins bind cell surfaces and various compounds
CC       including collagen, fibrin, heparin, DNA, and actin. Fibronectins
CC       are involved in cell adhesion, cell motility, opsonization, wound
CC       healing, and maintenance of cell shape. Involved in osteoblast
CC       compaction through the fibronectin fibrillogenesis cell-mediated
CC       matrix assembly process, essential for osteoblast mineralization.
CC       Participates in the regulation of type I collagen deposition by
CC       osteoblasts (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Mostly heterodimers or multimers of alternatively spliced
CC       variants, connected by 2 disulfide bonds near the carboxyl ends;
CC       to a lesser extent homodimers. Interacts with FBLN1, FBLN7, AMBP,
CC       TNR, LGALS3BP, COL13A1 and COMP. Interacts with FST3 and MYOC (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted
CC       by hepatocytes. Cellular FN (dimeric or cross-linked multimeric
CC       forms), made by fibroblasts, epithelial and other cell types, is
CC       deposited as fibrils in the extracellular matrix.
CC   -!- PTM: Sulfated. {ECO:0000250}.
CC   -!- PTM: Forms covalent cross-links mediated by a transglutaminase,
CC       such as F13A or TGM2, between a glutamine and the epsilon-amino
CC       group of a lysine residue, forming homopolymers and heteropolymers
CC       (e.g. fibrinogen-fibronectin, collagen-fibronectin
CC       heteropolymers).
CC   -!- PTM: Some lysine residues are oxidized to allysine by LOXL3,
CC       promoting fibronectin activation and matrix formation.
CC       {ECO:0000250|UniProtKB:P11276}.
DR   EMBL; S80206; AAB35493.1; -; mRNA.
DR   UniGene; Ocu.1875; -.
DR   ProteinModelPortal; Q28749; -.
DR   SMR; Q28749; -.
DR   STRING; 9986.ENSOCUP00000008718; -.
DR   PRIDE; Q28749; -.
DR   eggNOG; ENOG410IF4N; Eukaryota.
DR   eggNOG; ENOG410Y2NH; LUCA.
DR   HOVERGEN; HBG077359; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   InterPro; IPR000083; Fibronectin_type1.
DR   Pfam; PF00039; fn1; 1.
DR   SMART; SM00058; FN1; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01253; FN1_1; 1.
DR   PROSITE; PS51091; FN1_2; 1.
PE   2: Evidence at transcript level;
KW   Acute phase; Cell adhesion; Cell shape; Complete proteome;
KW   Disulfide bond; Extracellular matrix; Heparin-binding; Oxidation;
KW   Reference proteome; Repeat; Secreted; Sulfation.
FT   CHAIN        <1    100       Fibronectin.
FT                                /FTId=PRO_0000158531.
FT   DOMAIN       <1      5       Fibronectin type-I 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN        7     50       Fibronectin type-I 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   MOD_RES      16     16       Sulfotyrosine. {ECO:0000255}.
FT   DISULFID      9     35       {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID     31     47       {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID     33     44       {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID     81     81       Interchain (with C-85).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID     85     85       Interchain (with C-81).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   NON_TER       1      1
SQ   SEQUENCE   100 AA;  11530 MW;  5DFA17674EDDE415 CRC64;
     KCDPHEATCY DDGKTYHVGE QWQKEYLGAI CSCTCFGGQR GWRCDNCRRP GVEPSPDSST
     GHSYNQYTQR YHQRTNTNVN CPIECFMPLD VQADREDSRE
//
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