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
