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Database: UniProt
Entry: Q91289
LinkDB: Q91289
Original site: Q91289 
ID   FINC_PLEWA              Reviewed;        1328 AA.
AC   Q91289;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAY-2019, entry version 84.
DE   RecName: Full=Fibronectin;
DE            Short=FN;
DE   Flags: Fragment;
OS   Pleurodeles waltl (Iberian ribbed newt).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Caudata; Salamandroidea; Salamandridae;
OC   Pleurodelinae; Pleurodeles.
OX   NCBI_TaxID=8319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8081872;
RA   Cavalier L., Riou J., Desimone D.W.;
RT   "Amphibian Pleurodeles waltl fibronectin: cDNA cloning and
RT   developmental expression of spliced variants.";
RL   Cell Adhes. Commun. 1:83-91(1993).
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. May be involved in
CC       osteoblast compaction (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Dimers or multimers of alternatively spliced variants,
CC       connected by 2 disulfide bonds near the carboxyl ends.
CC       {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).
DR   EMBL; X66813; CAA47292.1; -; mRNA.
DR   SMR; Q91289; -.
DR   PRIDE; Q91289; -.
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; 3.
DR   CDD; cd00063; FN3; 11.
DR   Gene3D; 2.60.40.10; -; 11.
DR   InterPro; IPR000083; Fibronectin_type1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00039; fn1; 3.
DR   Pfam; PF00041; fn3; 11.
DR   SMART; SM00058; FN1; 3.
DR   SMART; SM00060; FN3; 11.
DR   SUPFAM; SSF49265; SSF49265; 7.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01253; FN1_1; 1.
DR   PROSITE; PS51091; FN1_2; 3.
DR   PROSITE; PS50853; FN3; 11.
PE   2: Evidence at transcript level;
KW   Acute phase; Cell adhesion; Cell shape; Disulfide bond; Glycoprotein;
KW   Heparin-binding; Repeat.
FT   CHAIN        <1   1328       Fibronectin.
FT                                /FTId=PRO_0000158533.
FT   DOMAIN       <1     14       Fibronectin type-III 1.
FT   DOMAIN       17    112       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      114    202       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      205    295       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      296    386       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      387    480       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      481    572       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      573    660       Fibronectin type-III 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      661    754       Fibronectin type-III 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      755    841       Fibronectin type-III 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      842    933       Fibronectin type-III 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1054   1145       Fibronectin type-III 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1155   1199       Fibronectin type-I 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN     1200   1243       Fibronectin type-I 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN     1245   1287       Fibronectin type-I 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DNA_BIND     <1     13       {ECO:0000250}.
FT   REGION      203    477       Cell-attachment.
FT   REGION      658    929       Heparin-binding 2. {ECO:0000250}.
FT   REGION      930   1064       Connecting strand 3 (CS-3) (V region).
FT   REGION     1157   1288       Fibrin-binding 2. {ECO:0000250}.
FT   MOTIF       461    463       Cell attachment site.
FT   CARBOHYD     89     89       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   1157   1186       {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID   1184   1196       {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID   1202   1229       {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID   1227   1240       {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID   1247   1272       {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID   1270   1281       {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID   1320   1320       Interchain (with C-1324).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DISULFID   1324   1324       Interchain (with C-1320).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   NON_TER       1      1
SQ   SEQUENCE   1328 AA;  145037 MW;  E31BF7968A1D1E74 CRC64;
     HESEAPITRT VVTPISPPTD LHLEPSPDFA TLTVSWSRSP SPGITGYRIN TALLLGIRLH
     SGYTLEEEVT ESQSRVCIFD NLSPGVEYNV SVVSVKDDQE SEPIWKTITQ EVPSLTDLNF
     VDVTDTSIDL RWTPLKGPTI IGYRVTVVAA GESVPIYEDK VGPTQGYYKV SGLEPGIDYD
     ISVITLVTDG ESAPTTLTTA DCCPTATDLR FTNVGPDSML VTWSAPPSMV LSSFLVRYVP
     SKNEEDAAEL TISPSDNMVV LTNLLPGTEY IVSVFAVYEE RESTPLTGVQ RTGLDSPTGL
     DFSDTTSSSF TVYWMAPRAT VTGYKIQYHP ETGGAGQKEE RCVPPSRNSL TLTNLTPGTE
     YVVSIFAVNG RQESVPLVGQ QATVSDTPTN LEVTSSTPTS MSISWDAPPV GVRYYRITYT
     ETGGETPVQE FTVPGDRSDA PIRGLKPGAE YIITVYAVTG RGDSPASSKP VTVTHKTVVD
     KPTQLQVTDV QDHSIQVRWM PSSTPVTGYR VTSVPKSGVG PTVSHVVPPD QTEMTIEGLE
     PTVEYVVSVY AQGKNGETEP LVETAVTNID RPKGLAFTEV DVDSLKLVWE SPKGQVTTYK
     VTYSNPEDGI HELVPAPNGD EDTAQLHGLR PGAEYTVSVV ALHDDMESQP LIGTQVTAIP
     PPTNLLFSQI TPTSVTVSWR PPNVQLTGYR VRVHPKEKAG PMKEINLSPD STSAVVTGLM
     VATKYEVSVY ALKDSLTSRP AQGIVTTQEN VSPPRRRRIT DVTETTVTIT WRTKTETITG
     FHIDAIPAGG QNPIQRTISP DLRTYVITGL QPGTDYKIHI YTLNDNARSS PVTIDATTAV
     DSPSNLRFLT TTSNSLLFSW QPPRSKLTGY IIKYEKPGGP VREVVPRPHP GATESQQSQN
     LEPGTEYTIY IIAVRSNYKS GPLVGKKRTD ELPRLVTLAQ PGQQGRILDV PSLVENTPFI
     SQTSFDNGNG IQLPGTSGQQ NIGHQGQQVF LEEHGFRSPV LPTTATPVKP GYQAPEQHTL
     DKYTPGQHVP TIREDIELAR FPPRQIDMDR PTSHDSGPQQ VDRTGQEAQT TISWRPLLET
     TEYIITCHPV GNEETPQQFT VPGTSSSATL NGLTRGATYN IIVEALKGKN KHKSRELVTV
     TSAAHGSGVL HGLEDTCYDI TTGSSYSIGQ EWERMSESGF KLWCRCLGLG SGHFKCDSSK
     WCHDSGLNYR VGEKWDRSGE NGQMMSCTCL GMEWKGEFKC EPHEATCYDD GKMYVGEQWQ
     KEYLGAICSC TCYGGQQGWR CDNCRRPGAG VTPSADGVVG QTLSHFSQRY QQNANFNLKC
     PIECYLPL
//
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