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FINC_XENLA
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   25-MAY-2022, entry version 109.
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   PRIDE; Q91740; -.
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; 2.10.10.10; -; 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; 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
 
 
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