ID FINC_XENLA Reviewed; 2481 AA.
AC Q91740;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Fibronectin {ECO:0000250|UniProtKB:P02751};
DE Short=FN;
DE Flags: Precursor;
GN Name=fn1 {ECO:0000250|UniProtKB:P02751};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1730390; DOI=10.1016/0012-1606(92)90291-n;
RA Desimone D.W., Norton P.A., Hynes R.O.;
RT "Identification and characterization of alternatively spliced fibronectin
RT mRNAs expressed in early Xenopus embryos.";
RL Dev. Biol. 149:357-369(1992).
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 (By similarity). Involved in osteoblast
CC compaction through the fibronectin fibrillogenesis cell-mediated matrix
CC assembly process, essential for osteoblast mineralization. Participates
CC in the regulation of type I collagen deposition by osteoblasts (By
CC similarity). {ECO:0000250|UniProtKB:P02751,
CC ECO:0000250|UniProtKB:P11276}.
CC -!- SUBUNIT: Dimers or multimers of alternatively spliced variants,
CC connected by 2 disulfide bonds near the carboxyl ends. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. The diversity of isoforms
CC depends on the V region and either of the two extra domain which can
CC be either included or excluded (partially or completely for the V
CC region). {ECO:0000305};
CC Name=1;
CC IsoId=Q91740-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: In early Xenopus embryo, cellular forms of
CC fibronectin predominate which include both extra domains. In
CC fibronectin of embryonic and adult liver the connecting strand 3 can be
CC either completely excluded or included.
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 {ECO:0000250|UniProtKB:P11276}.
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DR EMBL; M77820; AAA49707.1; -; mRNA.
DR PIR; A43908; A43908.
DR AlphaFoldDB; Q91740; -.
DR SMR; Q91740; -.
DR GlyCosmos; Q91740; 7 sites, No reported glycans.
DR AGR; Xenbase:XB-GENE-865084; -.
DR Xenbase; XB-GENE-865084; fn1.S.
DR Proteomes; UP000186698; Genome assembly.
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; 12.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00063; FN3; 16.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 12.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 17.
DR InterPro; IPR000083; Fibronectin_type1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013806; Kringle-like.
DR PANTHER; PTHR46708:SF2; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR Pfam; PF00039; fn1; 11.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF00041; fn3; 17.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00058; FN1; 12.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 17.
DR SUPFAM; SSF49265; Fibronectin type III; 10.
DR SUPFAM; SSF57603; FnI-like domain; 12.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01253; FN1_1; 11.
DR PROSITE; PS51091; FN1_2; 12.
DR PROSITE; PS51092; FN2_2; 2.
DR PROSITE; PS50853; FN3; 17.
PE 2: Evidence at transcript level;
KW Acute phase; Alternative splicing; Cell adhesion; Cell shape;
KW Disulfide bond; Glycoprotein; Heparin-binding; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..2481
FT /note="Fibronectin"
FT /id="PRO_0000019238"
FT DOMAIN 53..93
FT /note="Fibronectin type-I 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 98..141
FT /note="Fibronectin type-I 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 142..185
FT /note="Fibronectin type-I 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 187..231
FT /note="Fibronectin type-I 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 232..276
FT /note="Fibronectin type-I 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 307..346
FT /note="Fibronectin type-I 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 356..404
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 416..464
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 469..512
FT /note="Fibronectin type-I 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 517..559
FT /note="Fibronectin type-I 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 560..603
FT /note="Fibronectin type-I 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 611..703
FT /note="Fibronectin type-III 1"
FT DOMAIN 720..808
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 811..904
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 909..998
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 999..1088
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1089..1175
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1176..1270
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1271..1359
FT /note="Fibronectin type-III 8; extra domain B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1360..1452
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1453..1540
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1541..1634
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1635..1726
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1727..1814
FT /note="Fibronectin type-III 13; extra domain A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT ProRule:PRU00479"
FT DOMAIN 1815..1908
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1909..1995
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1996..2086
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2195..2299
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2299..2343
FT /note="Fibronectin type-I 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2344..2386
FT /note="Fibronectin type-I 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2388..2431
FT /note="Fibronectin type-I 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DNA_BIND 907..1172
FT /evidence="ECO:0000250"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..275
FT /note="Fibrin- and heparin-binding 1"
FT REGION 309..609
FT /note="Collagen-binding"
FT REGION 1358..1631
FT /note="Cell-attachment"
FT REGION 1812..2082
FT /note="Heparin-binding 2"
FT REGION 2083..2205
FT /note="V region (type III connecting segment, IIICS)"
FT REGION 2111..2138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2301..2432
FT /note="Fibrin-binding 2"
FT MOTIF 1615..1617
FT /note="Cell attachment site"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..81
FT /evidence="ECO:0000250"
FT DISULFID 79..90
FT /evidence="ECO:0000250"
FT DISULFID 100..128
FT /evidence="ECO:0000250"
FT DISULFID 126..138
FT /evidence="ECO:0000250"
FT DISULFID 144..172
FT /evidence="ECO:0000250"
FT DISULFID 170..182
FT /evidence="ECO:0000250"
FT DISULFID 189..218
FT /evidence="ECO:0000250"
FT DISULFID 216..228
FT /evidence="ECO:0000250"
FT DISULFID 234..263
FT /evidence="ECO:0000250"
FT DISULFID 261..273
FT /evidence="ECO:0000250"
FT DISULFID 309..336
FT /evidence="ECO:0000250"
FT DISULFID 334..343
FT /evidence="ECO:0000250"
FT DISULFID 361..387
FT /evidence="ECO:0000250"
FT DISULFID 375..402
FT /evidence="ECO:0000250"
FT DISULFID 421..447
FT /evidence="ECO:0000250"
FT DISULFID 471..499
FT /evidence="ECO:0000250"
FT DISULFID 497..509
FT /evidence="ECO:0000250"
FT DISULFID 519..546
FT /evidence="ECO:0000250"
FT DISULFID 544..556
FT /evidence="ECO:0000250"
FT DISULFID 562..590
FT /evidence="ECO:0000250"
FT DISULFID 588..600
FT /evidence="ECO:0000250"
FT DISULFID 2301..2330
FT /evidence="ECO:0000250"
FT DISULFID 2328..2340
FT /evidence="ECO:0000250"
FT DISULFID 2346..2373
FT /evidence="ECO:0000250"
FT DISULFID 2371..2383
FT /evidence="ECO:0000250"
FT DISULFID 2390..2416
FT /evidence="ECO:0000250"
FT DISULFID 2414..2425
FT /evidence="ECO:0000250"
FT DISULFID 2459
FT /note="Interchain (with C-2463)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 2463
FT /note="Interchain (with C-2459)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2481 AA; 272680 MW; 7E47DF4F6CE72C93 CRC64;
MRRGALTGLL LVLCLSVVLR AAPSATSKKR RQAQQQQQQQ VVQPQGTQDN HQKGCYDNGK
YYQINQQWER TYLGNTLVCT CYGGGRGFNC ESKPESEETC FDKYTGVSYR VGETYERPKD
NMIWDCTCIG AGRGRISCTI ANRCHEGGQS YKIGDTWRRP HETGGYMLEC VCLGNGKGEW
TCKPVAERCY DNTAGTSYVV GQTWEKPYQG WMMVDCTCLG EGNGRITCSS KNRCNDQDTK
TSYRIGDTWS KTDTRGNLLQ CICTGNGRGE WKCERHSSAQ ATGTGSNPIT NIQTALYQPD
SQLEPYGHCV TDNGVLYSLG MRWLRTQGSK QMLCTCLGNG VSCEETVATI TFGGNANGEP
CAIPFTHDGK TYYSCTSEGR QDGKLWCATT SNYDSDKKYS FCTEQLALVQ TRGGNSNGAL
CNFPFLYNNL NYTDSTSEGR QDSMKWCGTT ANYDADQKFG FCPMAAHEEI CTTNEGVMYR
VGDQWDKQHD QGHMMRCTCV GNGRGEWSCV AYSQLKDQCI VDGLTYNVNS SFTKLHEEGH
MMNCTCFGQG RGRWKCDAID QCQDTETRQF YQIGDSWEKH LQGVQYQCYC YGKGIGEWHC
QPLSTSQAGT GPVQVIITES ANFPTSHPIQ WNAPQASHIK NYILRWKPKL KAGPWKQATI
PGHLNSYTIS GLKPGILYEG QLISILQYGN REVTTFDFTT TTTIHRHSQT ESGETTPLPP
LVSISESVTE ITASSFLVSW VSASDTVSGF RVEYELSEDG DEKRYLELPN TATSVNIPDL
LPGRRYNVNV YQITEEGEKS LILSTTQTTA PDAPPEHNVE NVDDTSIMIK WNKPQAPITG
YRVVYSPSVE GSSTELNLPS TANSVTLTEL LPGIEYNITI YAVEDSLESV PVFIQQGTTG
TPQTVIVPSP TDLQLVEVTD VKIIIMWTSP QSEVSGYRVV VKPVSPAGRD VQNLPVNRNT
FAEVVNLQPG RTYSFEVYAV NRGQESEPLV GEFATKLDAP TDLQFTDVTE STVVIIWIPP
QAKIGRYLLS VGQTRGGQPS QFPINPSVTN HKLDNLLPGT EYTVSLVALK GNQQSASASG
VFSTLEPVGS IPHYNTEVTE TTIVVTWTPV PRIGFKLDVR PSQGGEAPRE VISESGSIVI
SGLTPGVEYT YSISVLTDGV EKDIPITKTV VTPLSPPTNL RLQPSRDSAT LTVYWDRSIS
PGITGYRIST TPTPMQVGNS LEEEVGPSQT YCVFENLSPG VEYNVSVYAV KEEEESAPLS
QMFLQEIPQL TDIKYDDVTD TSIDLRWTPL NSSNIIGYRI TVVAAGESVP IYEEFVGPTD
GYYKVSGLEP GIDYEISLIT LINGGESAPT TIIQHTAVPP PTNLRFTNIG PDNIRVTWSP
PTSIELSSYL VRYSPVKKPD DVTELSLSPS TNMVVLSNLL PFTEYLVSVH SVYEERESSS
LNGVAKTHLD SPTGIAFSEI TPNSFTVHWI APRGPITGYR IRYQLESGAG RPKEERVPPS
RNSITLTHLI PGSEYLVSII AINGQQESLP LAGQQATVSD VPTDLEVTSS SPNTLTISWE
APAVSVRYYR ITYSQTGGHG PEKEFTVPGT SNTATIRGLN PGVSYTITVY AVTGRGDSPA
SSKPLTIIHK TDVDQPIDMA VTDIQDHSIH VKWSPPPGPV TGYRVTSVPK SGQGETFSQV
ISPDQTEVTI VGLQPAVEYV VSIYSQGENG ESEPLVETAV TNIDNPKGLT FTDVGVDSIR
LAWEVPDGQV TRYRVTYSSP EDGVKELFPA PEGDDDTAEL HGLRPGTEYT VSIVALHDDM
ESKPLIGIQS TAIPAPTNLQ FSQVTPSGFS LSWHAPTVHL TGYLVRVNPK EKTGPTKEVR
LSPGVAATTV TGLMVATKYE VNVYALKDSL TSQPLQGLIS TLDNVSPPRR PRIQDVTETT
VTLSWRTKTE TITGFQIDAI PADGQNPIRR TVDADLRTFT ITGLQPGTDY KIYLYTLNDN
ARSSPVTVDV TTAVDSPSNL RFLTTTSNSL LFTWQPPRAR ITGYIIRYEK AGGLIKEHLP
RLPAGTTEST LTNLEPGTEY IIYIIAVRNN MKSEPLVGRK RTDELPRLVT LPHPGQGPEI
LDVPTDEENT PHITQTKLDN GNGIQLPGSN GQQPSSDHEG QLIEEHGFRS PLAPTTAVPV
RPGKFAPGRY PQERVDIELD TFPVQHGDFD GPYPHGLGPQ LNDSGVQEVA SHTTISWRPE
LETTEYIISC HPIDHEEAPL QFRVPGTSSS ATLNGLTRGA TYNIVVEAQK GTDKHKVLEK
RVTVGSPGSP EGVLQPVEDT CYDTFSGAHY SVGQEWERMS ESGFRLWCKC LGYGSGHFRC
DSSKWCHDNG VNHRIGEKWD RRGENGQMMS CTCLGNGKGE FKCEPPEATC YDEGKMYNVG
EQWQKEYLGA ICSCTCYGGQ QGWRCDNCRR PGAVSPDGTA GQTVSQFTQR YQQNYNLNCP
IECYLPLGLQ ADTQHSQQTQ K
//
