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FINC_CHICK
ID   FINC_CHICK              Reviewed;        2483 AA.
AC   P11722; F1NJT3; Q90921;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 4.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Fibronectin {ECO:0000250|UniProtKB:P02751};
DE            Short=FN;
DE   Flags: Precursor;
GN   Name=FN1 {ECO:0000250|UniProtKB:P02751};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 562-611.
RX   PubMed=6572007; DOI=10.1073/pnas.80.1.46;
RA   Hirano H., Yamada Y., Sullivan M., de Crombrugghe B., Pastan I.,
RA   Yamada K.M.;
RT   "Isolation of genomic DNA clones spanning the entire fibronectin gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:46-50(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1177-2382.
RC   STRAIN=White leghorn;
RA   Norton P.A.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1353-1541.
RX   PubMed=8603103; DOI=10.1016/0167-4889(95)00183-2;
RA   Gehris A.L., Brandli D.W., Lewis S.D., Bennett V.D.;
RT   "The exon encoding the fibronectin type III-9 repeat is constitutively
RT   included in the mRNA from chick limb mesenchyme and cartilage.";
RL   Biochim. Biophys. Acta 1311:5-12(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1453-1725.
RX   PubMed=2823899; DOI=10.1016/0167-4781(87)90070-4;
RA   Kubomura S., Obara M., Karasaki Y., Taniguchi H., Gotoh S., Tsuda T.,
RA   Higashi K., Ohsato K., Hiarno H.;
RT   "Genetic analysis of the cell binding domain region of the chicken
RT   fibronectin gene.";
RL   Biochim. Biophys. Acta 910:171-181(1987).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1177-2382.
RX   PubMed=2830487; DOI=10.1128/mcb.7.12.4297-4307.1987;
RA   Norton P.A., Hynes R.O.;
RT   "Alternative splicing of chicken fibronectin in embryos and in normal and
RT   transformed cells.";
RL   Mol. Cell. Biol. 7:4297-4307(1987).
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: Mostly heterodimers or multimers of alternatively spliced
CC       variants, connected by 2 disulfide bonds near the carboxyl ends; to a
CC       lesser extent homodimers. Interacts with FBLN7 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
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=P11722-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted by
CC       hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms),
CC       made by fibroblasts, epithelial and other cell types, is deposited as
CC       fibrils in the extracellular matrix.
CC   -!- PTM: Sulfated. {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).
CC       {ECO:0000250|UniProtKB:P11276}.
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DR   EMBL; AADN05000347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; V00432; CAA23714.1; -; Genomic_DNA.
DR   EMBL; U21327; AAA73566.1; -; mRNA.
DR   EMBL; X06533; CAA29781.1; -; Genomic_DNA.
DR   EMBL; M26186; AAA48772.1; -; Genomic_DNA.
DR   EMBL; U20386; AAB01062.1; -; mRNA.
DR   PIR; A28512; A28512.
DR   PIR; A29355; A29355.
DR   PIR; S71465; S71465mgcds.
DR   RefSeq; NP_001185641.1; NM_001198712.1. [P11722-1]
DR   AlphaFoldDB; P11722; -.
DR   SMR; P11722; -.
DR   STRING; 9031.ENSGALP00000005653; -.
DR   PaxDb; P11722; -.
DR   PRIDE; P11722; -.
DR   Ensembl; ENSGALT00000005664; ENSGALP00000005654; ENSGALG00000003578. [P11722-1]
DR   GeneID; 396133; -.
DR   KEGG; gga:396133; -.
DR   CTD; 2335; -.
DR   VEuPathDB; HostDB:geneid_396133; -.
DR   GeneTree; ENSGT00940000155126; -.
DR   HOGENOM; CLU_000916_0_0_1; -.
DR   InParanoid; P11722; -.
DR   OrthoDB; 6580at2759; -.
DR   PhylomeDB; P11722; -.
DR   TreeFam; TF329915; -.
DR   Proteomes; UP000000539; Chromosome 7.
DR   Bgee; ENSGALG00000003578; Expressed in granulocyte and 12 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0045178; C:basal part of cell; IDA:AgBase.
DR   GO; GO:0005604; C:basement membrane; IDA:AgBase.
DR   GO; GO:0009986; C:cell surface; IDA:AgBase.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:AgBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0031012; C:extracellular matrix; TAS:AgBase.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0005577; C:fibrinogen complex; IEA:Ensembl.
DR   GO; GO:0005614; C:interstitial matrix; IDA:AgBase.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR   GO; GO:0099512; C:supramolecular fiber; IDA:AgBase.
DR   GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR   GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR   GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0045176; P:apical protein localization; IDA:AgBase.
DR   GO; GO:0090245; P:axis elongation involved in somitogenesis; IDA:AgBase.
DR   GO; GO:0051702; P:biological process involved in interaction with symbiont; IEA:Ensembl.
DR   GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IDA:AgBase.
DR   GO; GO:0016477; P:cell migration; TAS:AgBase.
DR   GO; GO:0060974; P:cell migration involved in heart formation; IMP:AgBase.
DR   GO; GO:0008283; P:cell population proliferation; IDA:WormBase.
DR   GO; GO:0031589; P:cell-substrate adhesion; IMP:AgBase.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0048041; P:focal adhesion assembly; IDA:AgBase.
DR   GO; GO:0033622; P:integrin activation; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0150102; P:negative regulation of monocyte activation; IEA:Ensembl.
DR   GO; GO:0071635; P:negative regulation of transforming growth factor beta production; IEA:Ensembl.
DR   GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; IEA:Ensembl.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:Ensembl.
DR   GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0006929; P:substrate-dependent cell migration; IMP:AgBase.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   CDD; cd00061; FN1; 12.
DR   CDD; cd00062; FN2; 2.
DR   CDD; cd00063; FN3; 17.
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; 12.
DR   Pfam; PF00040; fn2; 2.
DR   Pfam; PF00041; fn3; 16.
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; 12.
DR   PROSITE; PS51091; FN1_2; 12.
DR   PROSITE; PS00023; FN2_1; 2.
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; DNA-binding; Extracellular matrix; Glycoprotein;
KW   Heparin-binding; Phosphoprotein; Pyrrolidone carboxylic acid;
KW   Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..2483
FT                   /note="Fibronectin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000158529"
FT   DOMAIN          52..92
FT                   /note="Fibronectin type-I 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          97..140
FT                   /note="Fibronectin type-I 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          141..184
FT                   /note="Fibronectin type-I 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          186..230
FT                   /note="Fibronectin type-I 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          231..275
FT                   /note="Fibronectin type-I 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          311..350
FT                   /note="Fibronectin type-I 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          360..408
FT                   /note="Fibronectin type-II 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          420..468
FT                   /note="Fibronectin type-II 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          473..516
FT                   /note="Fibronectin type-I 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          521..563
FT                   /note="Fibronectin type-I 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          564..607
FT                   /note="Fibronectin type-I 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          615..708
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          723..812
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          815..906
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          913..1002
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1003..1091
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1093..1179
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1180..1274
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1275..1363
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1275..1363
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          1364..1456
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1457..1544
FT                   /note="Fibronectin type-III 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1545..1638
FT                   /note="Fibronectin type-III 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1639..1730
FT                   /note="Fibronectin type-III 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1731..1818
FT                   /note="Fibronectin type-III 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1731..1818
FT                   /note="Fibronectin type-III 13; extra domain A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1819..1912
FT                   /note="Fibronectin type-III 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1913..2000
FT                   /note="Fibronectin type-III 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2001..2092
FT                   /note="Fibronectin type-III 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2200..2292
FT                   /note="Fibronectin type-III 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2300..2344
FT                   /note="Fibronectin type-I 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          2345..2387
FT                   /note="Fibronectin type-I 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          2389..2429
FT                   /note="Fibronectin type-I 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DNA_BIND        911..1176
FT                   /evidence="ECO:0000250|UniProtKB:P02751"
FT   REGION          21..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..274
FT                   /note="Fibrin- and heparin-binding 1"
FT                   /evidence="ECO:0000250|UniProtKB:P02751"
FT   REGION          313..613
FT                   /note="Collagen-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P02751"
FT   REGION          1362..1635
FT                   /note="Cell-attachment"
FT                   /evidence="ECO:0000250|UniProtKB:P02751"
FT   REGION          1816..2087
FT                   /note="Heparin-binding 2"
FT                   /evidence="ECO:0000250|UniProtKB:P02751"
FT   REGION          2088..2207
FT                   /note="V region (type III connecting segment, IIICS)"
FT                   /evidence="ECO:0000250|UniProtKB:P02751"
FT   REGION          2302..2433
FT                   /note="Fibrin-binding 2"
FT                   /evidence="ECO:0000250|UniProtKB:P02751"
FT   MOTIF           1619..1621
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000250|UniProtKB:P02751"
FT   COMPBIAS        33..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        533
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        547
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        881
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1011
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        54..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        78..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        99..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        125..137
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        143..171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        169..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        188..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        215..227
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        233..262
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        260..272
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        313..340
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        338..347
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        365..391
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        379..406
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        425..451
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        439..466
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        475..503
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        501..513
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        523..550
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        548..560
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        566..594
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        592..604
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        2302..2331
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        2329..2341
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        2347..2374
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        2372..2384
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        2391..2417
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DISULFID        2415..2426
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   CONFLICT        563
FT                   /note="V -> L (in Ref. 2; CAA23714)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1529
FT                   /note="R -> K (in Ref. 5; AAA48772)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1610
FT                   /note="T -> N (in Ref. 5; AAA48772)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1642
FT                   /note="Q -> P (in Ref. 5; CAA29781/AAA48772)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1695..1698
FT                   /note="EGLQ -> QGLE (in Ref. 5; AAA48772/CAA29781)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2370..2371
FT                   /note="MS -> ID (in Ref. 6; AAA73566)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2483 AA;  273248 MW;  8555FC671512D99E CRC64;
     MPGRGGLRLA LLALCLGAAA AGGGDGQRRG GKNRRQAQTA SVPQATPAQG KQTCFDNGRY
     YQINQQWERI YLGNTLVCTC YGGSRGFNCE SKPEPEETCF DKYTGSTYRV GETYERPKDS
     MIWDCTCIGA GRGRISCTIA NRCHEGGKSY KIGDTWRRPH ETGGYLLECV CLGNGKGEWT
     CKPLAERCYD NTAGTSYVVG ETWEKPYQGW MMVDCTCLGE GSGRITCTSR NRCNDQDTKT
     SYRIGDTWSK KDNRGNLLQC ICTGNGRGEW KCERHTSLHT TSTGSGSPSF TNVQTALYQP
     QPQQPQPQPH GHCVTDNGVV YSLGMQWLKT QGSQQMLCTC LGNGVSCQEI AVTQTYGGNS
     DGEACVLPFT YNGRTFYSCT TEGRTDGHLW CSTTSNFEQD RRYSFCTEQN VLVQTRGGNS
     NGALCHFPFL YNNRNYTDCT SEGRRDNMKW CGTTENYDAD QKFGFCPMAA HEEICTTNDG
     IMYRVGDQWD KQHDMGHMMR CTCVGNGRGE WTCIAYSQLR DQCIVDGITY DVNQTFHKRH
     DEGHMLNCTC FGQGRGRWKC DPVDQCQDSE TRTFYQIGDS WEKYVHGVRY QCYCYGRGIG
     EWHCQPLQAY AGATGPVQVI ITESTNQPNS HPIQWNAPKT SHISKYILRW RPKISGRHWK
     EATIPGHLNS YTISGLKPGV VYEGQLISVQ QHGPKEVTRF DFTTTSTTAV TSNTVSGETT
     LLPPMVATSE SVTEITASSF VVSWVSASDT VSGFRVEYEL SEEGDEPQYL DLPSTATSVN
     IPDLLPGRKY IVNVYQISEE GEQNLILSTS QTTAPDAPPE HSVESVDDTS IVISWSRPQA
     PITGYRIVYT PSVEGSSTEL NLPDTATSVT LSDLMPGVQY NISIYAVEEH QESTPVFIQQ
     ETTGVPRTDE VPSPKDLQFV EVSDVKVTIM WTPPQSQVSG YRVEAIPVNR PGQHGQRLPI
     TRSSFAEVVD LLPGTTYLFK IFAVSHGRES KPLTGEQTTK LDAPTNLRFI NTTEHSVLVL
     WTRPRAIISG YRLTAGPTRG GQPRTYNVGP SATKYLLRNL QPGTEYTVYL VAVKEDLQSA
     RETGVFTTYQ PVGSVPPFNT EVTETSIVIT WTPAPRIGFK LGVRPSQGGE APREVISDSG
     SIVISGLTPG VEYTYSLTVL MDGQERETPI IRRVTTPLSP PTNLRLEPNP DTGILIVSWD
     RSTTPGISGY RVTTAPTNGQ QGSTLEEVVG ADQTSCTFEN LNPGVEYNVS VYAVKDDQES
     IPISKTITQE VPQLTDLSFV DITDSSIGLR WTPLNASTII GYRITVVAAG ESVPIFEDFV
     DSSVGYYTVT GLEPGIDYDI SVITLINGGE SAPTTLTQQT AVPPPTDLRF TNVGPDTMRV
     TWTAPTSIVL SSFLVRYSPV KKEEDVAELT ISPSDNVVVL TNLLPGTEYL VRVYSVAEQH
     ESAPLSGIQK TGLDSPTGLD FSDITANSFT VHWIAPRATI TGYKIRHHPE HGVGRPKEDR
     VPPSRNSITL TNLLPGTEYV VSIIAVNGRE ESVPLVGQQT TVSDVPRDLE VNPTSPTSLE
     ISWDAPAVTV RYYRITYGET GGSSPVQEFT VPGTMSRATI TGLKPGVDYT ITVYAVTGRG
     DSPASSKPVT VTYKTEIDTP SQMQVTDVQD NSISIRWLPS SSPVTGYRVT AVPKKGHGPT
     KTKNVPPDQT QVTIEGLQPT VEYMVSVYAQ NQNGESLPLV ETAVTNIDRP KGLTFTEVDV
     DSIKIAWESP QGQVTRYRVT YSSPEDGIHE LLPAPGGEED TAELHGLRPG SEYTINIVAI
     YDDMESLPLT GTQSTAIPPP TNLKFTQVTP TSLTVNWNAP NVRLTGYRVR VNPKEKTGPM
     KEINLSPDST SAVVSGLMVA TKYEVSVYAL KDSLTSRPAQ GVVTTLENVS PPRRARVTDA
     TETTITITWR TKTETITGFQ IDAIPAASGQ NPIQRTISPD VRTYTITGLQ PGNDYKIYLY
     TLNENARSSP VVIDASTAID APSNLRFLTT TTNSLLASWQ PPRAKITGYI IRYDKPGSPA
     KELLPRPRPG TTEATITGLE PGTEYTIYII AVKNNQKSEP LVGRKRTDDL PTLITGPHPN
     QPDMLDVPSV DEGTPYLTNN RYDNGNGIQL PGTSGHPQTI GHQGQQVFFE EHGYRRPVPT
     TATPLRPGSR RQPPNVDEAI EIPGYQVPII VVPSYPHSRE PRRNDTTGQE ALSQTTISWR
     PLLESTEYII SCQPVSQDED TLQFRVPGTS SSATLTGLTR GATYNIIVEA LKDHRRQKVL
     EEVVTVGNTV SEGLNQPADD TCYDTYTGSF YSIGEEWERL SETGFKLWCQ CLGFGSGHFR
     CDSSKWCHDN GVNYKIGEKW DRQGENGQMM SCTCLGNGKG EFKCEPHETT CYDDGKMYQV
     GEQWQKEYFG AICSCTCYGG QQGWRCDNCR RPSVEVAPEG SAGHTYPQFT QRYHQATNTN
     VNCPIECFMP LDVQADTQHP RGK
 
 
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