FINC_PLEWA
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 03-AUG-2022, entry version 92.
DE RecName: Full=Fibronectin;
DE Short=FN;
DE Flags: Fragment;
OS Pleurodeles waltl (Iberian ribbed newt).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae;
OC Pleurodeles.
OX NCBI_TaxID=8319;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8081872; DOI=10.3109/15419069309095683;
RA Cavalier L., Riou J., Desimone D.W.;
RT "Amphibian Pleurodeles waltl fibronectin: cDNA cloning and developmental
RT 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 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 -!- 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).
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DR EMBL; X66813; CAA47292.1; -; mRNA.
DR AlphaFoldDB; Q91289; -.
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; 2.
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
FT /note="Fibronectin"
FT /id="PRO_0000158533"
FT DOMAIN <1..14
FT /note="Fibronectin type-III 1"
FT DOMAIN 17..112
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 114..202
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 205..295
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 296..386
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 387..480
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 481..572
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 573..660
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 661..754
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 755..841
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 842..933
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1054..1145
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1155..1199
FT /note="Fibronectin type-I 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 1200..1243
FT /note="Fibronectin type-I 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 1245..1287
FT /note="Fibronectin type-I 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DNA_BIND <1..13
FT /evidence="ECO:0000250"
FT REGION 203..477
FT /note="Cell-attachment"
FT REGION 658..929
FT /note="Heparin-binding 2"
FT /evidence="ECO:0000250"
FT REGION 930..1064
FT /note="Connecting strand 3 (CS-3) (V region)"
FT REGION 1045..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1288
FT /note="Fibrin-binding 2"
FT /evidence="ECO:0000250"
FT MOTIF 461..463
FT /note="Cell attachment site"
FT COMPBIAS 1052..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1157..1186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 1184..1196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 1202..1229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 1227..1240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 1247..1272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 1270..1281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 1320
FT /note="Interchain (with C-1324)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 1324
FT /note="Interchain (with C-1320)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT NON_TER 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
