FINC_HORSE
ID FINC_HORSE Reviewed; 2477 AA.
AC Q28377; F7CS60; Q28378;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Fibronectin {ECO:0000250|UniProtKB:P02751};
DE Short=FN;
DE Contains:
DE RecName: Full=Anastellin;
DE Flags: Precursor;
GN Name=FN1 {ECO:0000250|UniProtKB:P02751};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred;
RX PubMed=19892987; DOI=10.1126/science.1178158;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1879-2400 (ISOFORMS 1 AND 2), AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=8702559; DOI=10.1074/jbc.271.31.18954;
RA Macleod J.N., Burton-Wurster N., Gu D.N., Lust G.;
RT "Fibronectin mRNA splice variant in articular cartilage lacks bases
RT encoding the V, III-15, and I-10 protein segments.";
RL J. Biol. Chem. 271:18954-18960(1996).
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 -!- FUNCTION: [Anastellin]: Binds fibronectin and induces fibril formation.
CC This fibronectin polymer, named superfibronectin, exhibits enhanced
CC adhesive properties. Both anastellin and superfibronectin inhibit tumor
CC growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and
CC inhibits lysophospholipid signaling. {ECO:0000250|UniProtKB:P02751}.
CC -!- FUNCTION: [Isoform 2]: Probably involved in matrix organization of
CC cartilage. {ECO:0000305|PubMed:8702559}.
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 FBLN1, AMBP, TNR, LGALS3BP and
CC COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP.
CC Interacts (via type III repeats 9-14) with TNFAIP6 (via CUB domain);
CC this interaction enhances fibronectin fibril assembly. TNFAIP6 may act
CC as a bridging molecule between FN1 and THBS1 (By similarity). Interacts
CC with TNR; the interaction inhibits cell adhesion and neurite outgrowth
CC (By similarity). Interacts with FST3 and MYOC (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P02751}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
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=Q28377-1; Sequence=Displayed;
CC Name=2; Synonyms=(V+C)-;
CC IsoId=Q28377-2; Sequence=VSP_003253, VSP_003254;
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. Isoform 2 is the major transcript
CC in articular cartilage; very low levels in lymph node, bone, aorta, and
CC skin; absent from liver, spleen, placenta, cardiac muscle, skeletal
CC muscle, stomach, small intestine, and kidney.
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.
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}.
CC -!- PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting
CC fibronectin activation and matrix formation.
CC {ECO:0000250|UniProtKB:P11276}.
CC -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia.
CC {ECO:0000250|UniProtKB:P07589}.
CC -!- MISCELLANEOUS: [Isoform 2]: Lacks repeat 15 of fibronectin type-III,
CC repeat 10 of fibronectin type-I, and the connecting strand 3.
CC {ECO:0000305}.
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DR EMBL; PJAA01000007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U52107; AAC48613.1; -; mRNA.
DR EMBL; U52108; AAC48614.1; -; mRNA.
DR AlphaFoldDB; Q28377; -.
DR SMR; Q28377; -.
DR STRING; 9796.ENSECAP00000005223; -.
DR PaxDb; Q28377; -.
DR PeptideAtlas; Q28377; -.
DR PRIDE; Q28377; -.
DR Ensembl; ENSECAT00000007204; ENSECAP00000005223; ENSECAG00000000701. [Q28377-1]
DR GeneTree; ENSGT00940000155126; -.
DR HOGENOM; CLU_000916_0_0_1; -.
DR InParanoid; Q28377; -.
DR TreeFam; TF329915; -.
DR Proteomes; UP000002281; Chromosome 6.
DR Bgee; ENSECAG00000000701; Expressed in articular cartilage of joint and 23 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005577; C:fibrinogen complex; IEA:Ensembl.
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: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:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
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:0042060; P:wound healing; IEA:Ensembl.
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; 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; 11.
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; Isopeptide bond; Oxidation; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..31
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT CHAIN 32..2477
FT /note="Fibronectin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000158530"
FT CHAIN 627..702
FT /note="Anastellin"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT /id="PRO_0000451753"
FT DOMAIN 50..90
FT /note="Fibronectin type-I 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 95..138
FT /note="Fibronectin type-I 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 139..182
FT /note="Fibronectin type-I 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 184..228
FT /note="Fibronectin type-I 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 229..273
FT /note="Fibronectin type-I 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 306..345
FT /note="Fibronectin type-I 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 355..403
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 415..463
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 468..511
FT /note="Fibronectin type-I 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 516..558
FT /note="Fibronectin type-I 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 559..602
FT /note="Fibronectin type-I 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 610..705
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 722..812
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 813..902
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 909..998
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 999..1088
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1089..1175
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1176..1270
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1271..1359
FT /note="Fibronectin type-III 8; extra domain B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1360..1452
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
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 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 2194..2288
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2295..2339
FT /note="Fibronectin type-I 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2340..2382
FT /note="Fibronectin type-I 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 2384..2424
FT /note="Fibronectin type-I 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DNA_BIND 907..1172
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 24..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..272
FT /note="Fibrin- and heparin-binding 1"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 308..608
FT /note="Collagen-binding"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 464..477
FT /note="Critical for collagen binding"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 1358..1631
FT /note="Cell-attachment"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 1660..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1812..2082
FT /note="Heparin-binding 2"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 1904..2082
FT /note="Binds to FBLN1"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 2083..2202
FT /note="V region (type III connecting segment, IIICS)"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT REGION 2149..2169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2297..2428
FT /note="Fibrin-binding 2"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOTIF 1615..1617
FT /note="Cell attachment site"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT COMPBIAS 24..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 663
FT /note="Important for superfibronectin formation"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT SITE 666
FT /note="Important for superfibronectin formation"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 32
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 876
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 881
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 2454
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT MOD_RES 2475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02751"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 52..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 76..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 97..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 123..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 141..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 167..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 186..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 213..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 231..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 258..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 308..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 333..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 360..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 374..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 420..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 434..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 470..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 496..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 518..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 543..555
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 561..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 587..599
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2297..2326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2324..2336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2342..2369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2367..2379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2386..2412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DISULFID 2410..2421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT CROSSLNK 34
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT CROSSLNK 35
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT CROSSLNK 47
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-?)"
FT /evidence="ECO:0000250|UniProtKB:P11276"
FT VAR_SEQ 2083
FT /note="D -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8702559"
FT /id="VSP_003253"
FT VAR_SEQ 2084..2340
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8702559"
FT /id="VSP_003254"
FT CONFLICT 2085
FT /note="L -> P (in Ref. 2; AAC48614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2477 AA; 272168 MW; E97A141F6CC39B0D CRC64;
MLRGPGPGLL LLVVLSLGTA VPSSGASKRK RQDQQIIQPQ SPVAVGQSKP GCYDNGKHYQ
INQQWERTYL GNALVCTCYG GSRGFNCESK PEPEETCFDK YTGNTYRVGD TYERPKDSMI
WDCTCIGAGR GRISCTIANR CHEGGQSYKI GDTWRRPHET GGYMLECVCL GNGKGEWTCK
PIAEKCFDHA AGTSYVVGET WEKPYQGWMM VDCTCLGEGN GRITCTSRNR CNDQDTRTSY
RIGDTWSKKD NRGNLLQCIC TGNGRGEWKC ERHASLQTTS TGSGPFTDVR TAIYQPQPHP
QPAPYGHCVT DSGVVYSVGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC
VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDSAVLVQT RGGNSNGALC
HFPFLYNNHN YTDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRV
GDQWDKQHDM GHMMRCTCVG NGRGEWTCVA YSQLRDQCIV DDITYNVNDT FHKRHEEGHM
LNCTCFGQGR GRWKCDPIDQ CQDSETRTFY QIGDSWEKYV HGVRYQCYCY GRGIGEWHCQ
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHISK YILRWKPKNA PGRWKEATIP
GHLNSYTIKG LRPGVVYEGQ LISVQHYGHK EVTRFDFTTT STSPAVTSNT VTGETTPFSP
VVATSESVTE ITASSFVVSW VSASDTVSGF RVEYELSEEG DEPQYLDLPS TATSVNIPDL
LPGRKYIVNV YQISEEGEQS LILSTSQTTA PDAPPDPTVD QVDDTSIVVR WSRPQAPITG
YRIVYSPSVE GSSTELTLPE TANSVTLSDL QPGVQYNITI YAVEENQEST PVFIQQETTG
VPRADKVPPP RDLQFVEVTD VKITIMWTPP ESAVTGYRVD VLPVNLPGEH GQRLPISRNT
FAEVTGLSPG VTYHFKIFAV NHGRESKPLT GEQTTKLDAP TNLRFINETE STVIVTWTPP
RARIAGYRLT VGLTRGGQPK QYNVGPSASQ YPLRSLQPGS EYTVTLVAVK GNQQSPKATG
VFTTLQSPGS IPPYNTEVTE TTIVITWTPA PRIGFKLGVR PSQGGEAPRE VTSDSGSIVV
SGLTPGVEYV YTISVLRDGQ ERDAPIVKKV VTPLSPPTNL HLEANPDTGV LTVSWERSTT
PDITGYRITT TPTSGQQGYS LEEVVHADQS SCTFENLSPG LEYNVSVYTV KDDKESVPIS
DTIIPEVPQL TDLSFVDITD SSIGLRWTPL NSSTIIGYRI TVVAAGEGIP IFEDFVDSSV
GYYTVTGLEP GIDYDISVIT LINGGESAPT TLTQQTAVPP PTDLRFTNVG PDTMRVTWAP
PPSIELTNLL VRYSPVKNEE DVAELSISPS DNAVVLTNLL PGTEYLVSVS SVYEQHESTP
LRGRQKTGLD SPTGIDFSDI TANSFTVHWI APRATITGYR IRHHPEHTGG RPREDRVPPS
RNSITLTNLN PGTEYVVSIV ALNGREESPP LVGQQSTVSD VPRDLEVIAT TPTSILISWD
APAVTVRYYR ITYGETGGNS PVQEFTVPGS KSTATISGLK PGVDYTITVY AVTGRGDSPA
SSKPISIDYR TEIDKPSQMQ VTDVQDNSIS VRWLPSSSPV TGYRVTTTPK NGPGQSKTKT
AGPDQTEMTI EGLQPTVEYV VSVYAQNQNG ESQPLVQTAV TNIDRPRGLA FTDVDVDSIK
IAWESPQGQV SRYRVTYSSP EDGIHELFPA PDGEEDTAEL QGLRPGSEYT VSVVALHDDM
ESQPLIGTQS TAIPAPTELK FTQVTPTSLT AQWTAPNVQL TGYRVRVTPK EKTGPMKEIN
LAPDSTSVVV SGLMVATKYE VSVYALKDTL TSRPAQGIVT TLENVSPPRR ARVTDATETT
ITISWRTKTE TITGFQVDAV PANGQPPIQR TIKPDVRSYT ITGLQPGTDY KIYLYTLNDN
ARSSPVIIDA STAIDAPSNL HFLATTPNSL LISWQPPRAR ITGYIIKYEK PGSPPREVVP
RPHPGVTEAT ITGLEPGTEY TIQVIAIKNN QKSEPLIGRR KTDELPQLVT LPHPNLHGPE
ILDVPSTVQK TPFITNPGYD NGNGIQLPGT SGQQPSVGQQ MIFEEHGFRR TTPPTTATPV
RHRPRPYPPN VNEEIQIGHV PRGDVDQHLY PHVLGLNPNT STGQEALSQT TISWTPFQES
SEYIISCHPV GIDEEPLQFR VPGTSASATL TGLTRGATYN IIVEALKDQK RHKVREEVVT
VGNSVDQGLG QPTADSCFDP YTVSHYAIGE EWERLSESGF KLSCQCLGFG SGHFRCDSSK
WCHDNGVNYK IGEKWDRQGE NGQMMSCTCL GNGKGEFKCD PHEATCYDDG KTYHVGEQWQ
KEYLGAICSC TCFGGQRGWR CDNCRRPGAE PGHEGSTGHS YNQYSQRYQQ RTNTNVNCPI
ECFMPLDVQA DRDDSRE
