GenomeNet

Database: UniProt
Entry: Q91740
LinkDB: Q91740
Original site: Q91740 
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   18-JUL-2018, entry version 100.
DE   RecName: Full=Fibronectin;
DE            Short=FN;
DE   Flags: Precursor;
GN   Name=fn1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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
RT   fibronectin 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
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. Each of the "extra
CC         domain" and the connecting strand 3 are present in some forms of
CC         fibronectin and absent in others.;
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
CC       can be either completely excluded or included.
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; M77820; AAA49707.1; -; mRNA.
DR   PIR; A43908; A43908.
DR   UniGene; Xl.2243; -.
DR   ProteinModelPortal; Q91740; -.
DR   SMR; Q91740; -.
DR   PRIDE; Q91740; -.
DR   HOVERGEN; HBG005731; -.
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; 2.10.10.10; -; 2.
DR   Gene3D; 2.60.40.10; -; 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   Pfam; PF00039; fn1; 11.
DR   Pfam; PF00040; fn2; 2.
DR   Pfam; PF00041; fn3; 17.
DR   SMART; SM00058; FN1; 12.
DR   SMART; SM00059; FN2; 2.
DR   SMART; SM00060; FN3; 17.
DR   SUPFAM; SSF49265; SSF49265; 10.
DR   SUPFAM; SSF57440; SSF57440; 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; Repeat; Signal.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32   2481       Fibronectin.
FT                                /FTId=PRO_0000019238.
FT   DOMAIN       53     93       Fibronectin type-I 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN       98    141       Fibronectin type-I 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      142    185       Fibronectin type-I 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      187    231       Fibronectin type-I 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      232    276       Fibronectin type-I 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      307    346       Fibronectin type-I 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      356    404       Fibronectin type-II 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      416    464       Fibronectin type-II 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      469    512       Fibronectin type-I 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      517    559       Fibronectin type-I 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      560    603       Fibronectin type-I 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN      611    703       Fibronectin type-III 1.
FT   DOMAIN      720    808       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      811    904       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      909    998       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      999   1088       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1089   1175       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1176   1270       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1271   1359       Fibronectin type-III 8; extra domain.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1360   1452       Fibronectin type-III 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1453   1540       Fibronectin type-III 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1541   1634       Fibronectin type-III 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1635   1726       Fibronectin type-III 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1727   1814       Fibronectin type-III 13; extra domain.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN     1815   1908       Fibronectin type-III 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1909   1995       Fibronectin type-III 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1996   2086       Fibronectin type-III 16.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2195   2299       Fibronectin type-III 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2299   2343       Fibronectin type-I 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN     2344   2386       Fibronectin type-I 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DOMAIN     2388   2431       Fibronectin type-I 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478}.
FT   DNA_BIND    907   1172       {ECO:0000250}.
FT   REGION       55    275       Fibrin- and heparin-binding 1.
FT   REGION      309    609       Collagen-binding.
FT   REGION     1358   1631       Cell-attachment.
FT   REGION     1812   2082       Heparin-binding 2.
FT   REGION     2083   2205       Connecting strand 3 (CS-3) (V region).
FT   REGION     2301   2432       Fibrin-binding 2.
FT   MOTIF      1615   1617       Cell attachment site.
FT   CARBOHYD    431    431       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    529    529       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    543    543       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    877    877       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1244   1244       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1291   1291       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2202   2202       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     55     81       {ECO:0000250}.
FT   DISULFID     79     90       {ECO:0000250}.
FT   DISULFID    100    128       {ECO:0000250}.
FT   DISULFID    126    138       {ECO:0000250}.
FT   DISULFID    144    172       {ECO:0000250}.
FT   DISULFID    170    182       {ECO:0000250}.
FT   DISULFID    189    218       {ECO:0000250}.
FT   DISULFID    216    228       {ECO:0000250}.
FT   DISULFID    234    263       {ECO:0000250}.
FT   DISULFID    261    273       {ECO:0000250}.
FT   DISULFID    309    336       {ECO:0000250}.
FT   DISULFID    334    343       {ECO:0000250}.
FT   DISULFID    361    387       {ECO:0000250}.
FT   DISULFID    375    402       {ECO:0000250}.
FT   DISULFID    421    447       {ECO:0000250}.
FT   DISULFID    471    499       {ECO:0000250}.
FT   DISULFID    497    509       {ECO:0000250}.
FT   DISULFID    519    546       {ECO:0000250}.
FT   DISULFID    544    556       {ECO:0000250}.
FT   DISULFID    562    590       {ECO:0000250}.
FT   DISULFID    588    600       {ECO:0000250}.
FT   DISULFID   2301   2330       {ECO:0000250}.
FT   DISULFID   2328   2340       {ECO:0000250}.
FT   DISULFID   2346   2373       {ECO:0000250}.
FT   DISULFID   2371   2383       {ECO:0000250}.
FT   DISULFID   2390   2416       {ECO:0000250}.
FT   DISULFID   2414   2425       {ECO:0000250}.
FT   DISULFID   2459   2459       Interchain (with C-2463).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DISULFID   2463   2463       Interchain (with C-2459).
FT                                {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
//
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