TENA_MOUSE
ID TENA_MOUSE Reviewed; 2110 AA.
AC Q80YX1; Q64706; Q80YX2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Tenascin;
DE Short=TN;
DE AltName: Full=Hexabrachion;
DE AltName: Full=Tenascin-C;
DE Short=TN-C;
DE Flags: Precursor;
GN Name=Tnc {ECO:0000312|MGI:MGI:101922};
GN Synonyms=Hxb {ECO:0000312|MGI:MGI:101922};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA14355.1, ECO:0000312|PIR:JQ1322}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=GR/J {ECO:0000312|EMBL:BAA14355.1};
RC TISSUE=Mammary tumor {ECO:0000269|PubMed:1717349};
RX PubMed=1717349; DOI=10.1016/0378-1119(91)90248-a;
RA Saga Y., Tsukamoto T., Jing N., Kusakabe M., Sakakura T.;
RT "Murine tenascin: cDNA cloning, structure and temporal expression of
RT isoforms.";
RL Gene 104:177-185(1991).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA39751.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
RC STRAIN=NMRI X 129 {ECO:0000312|EMBL:CAA39751.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:CAA39751.1};
RX PubMed=1703162; DOI=10.1083/jcb.112.2.355;
RA Weller A., Beck S., Ekblom P.;
RT "Amino acid sequence of mouse tenascin and differential expression of two
RT tenascin isoforms during embryogenesis.";
RL J. Cell Biol. 112:355-362(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14709716; DOI=10.1242/jcs.00867;
RA Scherberich A., Tucker R.P., Samandari E., Brown-Luedi M., Martin D.,
RA Chiquet-Ehrismann R.;
RT "Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at
RT sites of bone and smooth muscle development.";
RL J. Cell Sci. 117:571-581(2004).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16553788; DOI=10.1111/j.1460-9568.2006.04657.x;
RA Morellini F., Schachner M.;
RT "Enhanced novelty-induced activity, reduced anxiety, delayed
RT resynchronization to daylight reversal and weaker muscle strength in
RT tenascin-C-deficient mice.";
RL Eur. J. Neurosci. 23:1255-1268(2006).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1394.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Extracellular matrix protein implicated in guidance of
CC migrating neurons as well as axons during development, synaptic
CC plasticity as well as neuronal regeneration. Promotes neurite outgrowth
CC when provided to neurons in culture. May play a role in supporting the
CC growth of epithelial tumors. Ligand for integrins ITGA8:ITGB1,
CC ITGA9:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6. In tumors, stimulates
CC angiogenesis by elongation, migration and sprouting of endothelial
CC cells (By similarity). {ECO:0000250|UniProtKB:P24821,
CC ECO:0000269|PubMed:16553788}.
CC -!- SUBUNIT: Homohexamer; disulfide-linked. A homotrimer may be formed in
CC the triple coiled-coil region and may be stabilized by disulfide rings
CC at both ends. Two of such half-hexabrachions may be disulfide linked
CC within the central globule. Interacts with CSPG4 (By similarity).
CC {ECO:0000250|UniProtKB:P24821}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q80YX1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:1717349};
CC IsoId=Q80YX1-2; Sequence=VSP_052147;
CC Name=3 {ECO:0000269|PubMed:1717349};
CC IsoId=Q80YX1-3; Sequence=VSP_052146;
CC Name=4 {ECO:0000269|PubMed:1717349};
CC IsoId=Q80YX1-4; Sequence=VSP_052145;
CC Name=5 {ECO:0000269|PubMed:1717349};
CC IsoId=Q80YX1-5; Sequence=VSP_052144;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, aortic valve, corneal limbus,
CC periosteum around the ribs, cerebellum, stomach and intestine
CC (PubMed:14709716). High levels of isoform 2 in lung and brain of
CC newborn mice. High levels of isoform 5 in thymus, moderate levels in
CC brain of newborn and adult mice. Low level of isoform 2 in adult brain.
CC {ECO:0000269|PubMed:14709716, ECO:0000269|PubMed:1717349}.
CC -!- DEVELOPMENTAL STAGE: At day 11.5 dpc, expressed in maxillary process.
CC at, 14.5 dpc, also detected in the stomach and at 15.5 dpc expressed in
CC developing bones. During embryogenesis, also expressed in lung,
CC cartilages, liver, brain and peripheral nerves (PubMed:14709716). In
CC kidney, isoform 2 is expressed at birth and isoform 5 at 2 weeks of
CC age. In intestine, isoform 5 is expressed at 13 dpc and isoform 2 at
CC birth. In cerebellum, high levels of isoform 2 at 17 dpc are down-
CC regulated to moderate levels in newborn mice and undetectable levels in
CC adult mice. Similarly, moderate levels of isoform 2 expressed in
CC cerebrum of 17 dpc are gradually down-regulated to undetectable levels
CC in adult mice. {ECO:0000269|PubMed:14709716,
CC ECO:0000269|PubMed:1703162, ECO:0000269|PubMed:1717349}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16944957,
CC ECO:0000269|PubMed:1703162}.
CC -!- DISRUPTION PHENOTYPE: Mice show enhanced novelty-induced activity,
CC reduced anxiety, delayed resynchronization to daylight reversal and
CC weaker muscle strength. {ECO:0000269|PubMed:16553788}.
CC -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000255}.
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DR EMBL; D90343; BAA14355.1; -; mRNA.
DR EMBL; X56304; CAA39751.1; -; mRNA.
DR EMBL; AL732556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18265.1; -. [Q80YX1-2]
DR CCDS; CCDS89763.1; -. [Q80YX1-1]
DR PIR; JQ1322; JQ1322.
DR RefSeq; NP_035737.2; NM_011607.3. [Q80YX1-2]
DR RefSeq; XP_006537837.1; XM_006537774.1.
DR AlphaFoldDB; Q80YX1; -.
DR SMR; Q80YX1; -.
DR BioGRID; 204237; 9.
DR ComplexPortal; CPX-471; Tenascin-C complex.
DR STRING; 10090.ENSMUSP00000102995; -.
DR GlyConnect; 2754; 3 N-Linked glycans (3 sites).
DR GlyGen; Q80YX1; 20 sites, 3 N-linked glycans (3 sites).
DR iPTMnet; Q80YX1; -.
DR PhosphoSitePlus; Q80YX1; -.
DR CPTAC; non-CPTAC-3359; -.
DR jPOST; Q80YX1; -.
DR MaxQB; Q80YX1; -.
DR PeptideAtlas; Q80YX1; -.
DR PRIDE; Q80YX1; -.
DR ProteomicsDB; 263268; -. [Q80YX1-1]
DR ProteomicsDB; 263269; -. [Q80YX1-2]
DR ProteomicsDB; 263270; -. [Q80YX1-3]
DR ProteomicsDB; 263271; -. [Q80YX1-4]
DR ProteomicsDB; 263272; -. [Q80YX1-5]
DR ABCD; Q80YX1; 15 sequenced antibodies.
DR Antibodypedia; 1348; 997 antibodies from 44 providers.
DR DNASU; 21923; -.
DR Ensembl; ENSMUST00000030056; ENSMUSP00000030056; ENSMUSG00000028364. [Q80YX1-2]
DR Ensembl; ENSMUST00000107372; ENSMUSP00000102995; ENSMUSG00000028364. [Q80YX1-1]
DR Ensembl; ENSMUST00000107377; ENSMUSP00000103000; ENSMUSG00000028364. [Q80YX1-2]
DR GeneID; 21923; -.
DR KEGG; mmu:21923; -.
DR UCSC; uc008thg.2; mouse. [Q80YX1-2]
DR CTD; 3371; -.
DR MGI; MGI:101922; Tnc.
DR VEuPathDB; HostDB:ENSMUSG00000028364; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000155188; -.
DR HOGENOM; CLU_001162_1_1_1; -.
DR InParanoid; Q80YX1; -.
DR OMA; DVEWDPL; -.
DR OrthoDB; 18592at2759; -.
DR PhylomeDB; Q80YX1; -.
DR TreeFam; TF329915; -.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 21923; 1 hit in 59 CRISPR screens.
DR ChiTaRS; Tnc; mouse.
DR PRO; PR:Q80YX1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80YX1; protein.
DR Bgee; ENSMUSG00000028364; Expressed in diaphysis of femur and 242 other tissues.
DR ExpressionAtlas; Q80YX1; baseline and differential.
DR Genevisible; Q80YX1; MM.
DR GO; GO:0005604; C:basement membrane; IDA:ComplexPortal.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:ComplexPortal.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0098966; C:perisynaptic extracellular matrix; IDA:SynGO.
DR GO; GO:0090733; C:tenascin complex; IPI:ComplexPortal.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0045545; F:syndecan binding; ISO:MGI.
DR GO; GO:0060447; P:bud outgrowth involved in lung branching; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060739; P:mesenchymal-epithelial cell signaling involved in prostate gland development; IMP:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:ComplexPortal.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:ComplexPortal.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IMP:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IC:ComplexPortal.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:ComplexPortal.
DR GO; GO:0009611; P:response to wounding; ISO:MGI.
DR CDD; cd00063; FN3; 14.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 2.60.40.10; -; 14.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR041161; EGF_Tenascin.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR033078; TNC.
DR PANTHER; PTHR46708:SF1; PTHR46708:SF1; 5.
DR Pfam; PF07974; EGF_2; 5.
DR Pfam; PF18720; EGF_Tenascin; 7.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 14.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 14.
DR SUPFAM; SSF49265; SSF49265; 11.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 14.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 14.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Coiled coil; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P24821"
FT CHAIN 23..2110
FT /note="Tenascin"
FT /evidence="ECO:0000250|UniProtKB:P24821"
FT /id="PRO_0000248607"
FT DOMAIN 174..185
FT /note="EGF-like 1; incomplete"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 186..216
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 217..247
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 248..279
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 280..310
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 311..341
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 342..372
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 373..403
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 404..434
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 435..465
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 466..496
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 497..527
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 528..558
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 559..589
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 590..621
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 625..715
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 716..804
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 805..894
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 895..988
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 989..1077
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1078..1165
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1167..1259
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1260..1348
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1349..1440
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1442..1530
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1531..1620
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1621..1710
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1711..1797
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1798..1886
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1884..2099
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 69..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 118..142
FT /evidence="ECO:0000255"
FT COMPBIAS 76..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24821"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24821"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24821"
FT MOD_RES 905
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24821"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1018
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1093
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 1443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1969
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2071
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 190..200
FT /evidence="ECO:0000255"
FT DISULFID 194..205
FT /evidence="ECO:0000255"
FT DISULFID 207..216
FT /evidence="ECO:0000255"
FT DISULFID 221..231
FT /evidence="ECO:0000255"
FT DISULFID 225..236
FT /evidence="ECO:0000255"
FT DISULFID 238..247
FT /evidence="ECO:0000255"
FT DISULFID 252..263
FT /evidence="ECO:0000255"
FT DISULFID 256..268
FT /evidence="ECO:0000255"
FT DISULFID 270..279
FT /evidence="ECO:0000255"
FT DISULFID 284..294
FT /evidence="ECO:0000255"
FT DISULFID 288..299
FT /evidence="ECO:0000255"
FT DISULFID 301..310
FT /evidence="ECO:0000255"
FT DISULFID 315..325
FT /evidence="ECO:0000255"
FT DISULFID 319..330
FT /evidence="ECO:0000255"
FT DISULFID 332..341
FT /evidence="ECO:0000255"
FT DISULFID 346..356
FT /evidence="ECO:0000255"
FT DISULFID 350..361
FT /evidence="ECO:0000255"
FT DISULFID 363..372
FT /evidence="ECO:0000255"
FT DISULFID 377..387
FT /evidence="ECO:0000255"
FT DISULFID 381..392
FT /evidence="ECO:0000255"
FT DISULFID 394..403
FT /evidence="ECO:0000255"
FT DISULFID 408..418
FT /evidence="ECO:0000255"
FT DISULFID 412..423
FT /evidence="ECO:0000255"
FT DISULFID 425..434
FT /evidence="ECO:0000255"
FT DISULFID 439..449
FT /evidence="ECO:0000255"
FT DISULFID 443..454
FT /evidence="ECO:0000255"
FT DISULFID 456..465
FT /evidence="ECO:0000255"
FT DISULFID 470..480
FT /evidence="ECO:0000255"
FT DISULFID 474..485
FT /evidence="ECO:0000255"
FT DISULFID 487..496
FT /evidence="ECO:0000255"
FT DISULFID 501..511
FT /evidence="ECO:0000255"
FT DISULFID 505..516
FT /evidence="ECO:0000255"
FT DISULFID 518..527
FT /evidence="ECO:0000255"
FT DISULFID 532..542
FT /evidence="ECO:0000255"
FT DISULFID 536..547
FT /evidence="ECO:0000255"
FT DISULFID 549..558
FT /evidence="ECO:0000255"
FT DISULFID 563..573
FT /evidence="ECO:0000255"
FT DISULFID 567..578
FT /evidence="ECO:0000255"
FT DISULFID 580..589
FT /evidence="ECO:0000255"
FT DISULFID 594..604
FT /evidence="ECO:0000255"
FT DISULFID 598..609
FT /evidence="ECO:0000255"
FT DISULFID 611..620
FT /evidence="ECO:0000255"
FT VAR_SEQ 1072..1616
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:1703162,
FT ECO:0000303|PubMed:1717349"
FT /id="VSP_052144"
FT VAR_SEQ 1163..1616
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1717349"
FT /id="VSP_052145"
FT VAR_SEQ 1254..1616
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1717349"
FT /id="VSP_052146"
FT VAR_SEQ 1436..1526
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1703162,
FT ECO:0000303|PubMed:1717349"
FT /id="VSP_052147"
FT CONFLICT 202
FT /note="D -> E (in Ref. 2; CAA39751)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="D -> S (in Ref. 2; CAA39751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1019
FT /note="Y -> S (in Ref. 2; CAA39751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1025
FT /note="Q -> H (in Ref. 2; CAA39751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1306
FT /note="G -> S (in Ref. 2; CAA39751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2110 AA; 231807 MW; A1FEA96F8BC2FE51 CRC64;
MGAVTWLLPG IFLALFALTP EGGVLKKIIR HKRESGLNMT LPEENQPVVF NHIYNIKLPM
GSQCSVDLES ASGEKDLTPT PESSGSFQEH TVDGENQIVF THRINIPRRA CGCAAAPDVK
ELLSRLEELE LLVSSLREQC TMGTGCCLQP AEGRLDTRPF CSGRGNFSAE GCGCVCEPGW
KGPNCSEPDC PGNCNLRGQC LDGQCICDEG FTGEDCSQLA CPNDCNDQGR CVNGVCVCFE
GYAGPDCGLE VCPVPCSEEH GMCVDGRCVC KDGFAGEDCN EPLCLNNCYN RGRCVENECV
CDEGFTGEDC SELICPNDCF DRGRCINGTC YCEEGFTGED CGELTCPNDC QGRGQCEEGQ
CVCNEGFAGA DCSEKRCPAD CHHRGRCLNG QCECDDGFTG ADCGDLQCPN GCSGHGRCVN
GQCVCDEGYT GEDCSQRRCP NDCHNRGLCV QGKCICEQGF KGFDCSEMSC PNDCHQHGRC
VNGMCICDDD YTGEDCRDRR CPRDCSQRGR CVDGQCICED GFTGPDCAEL SCPSDCHGHG
RCVNGQCICH EGFTGKDCKE QRCPSDCHGQ GRCEDGQCIC HEGFTGLDCG QRSCPNDCSN
QGQCVSGRCI CNEGYTGIDC SEVSPPKDLI VTEVTEETVN LAWDNEMRVT EYLIMYTPTH
ADGLEMQFRV PGDQTSTTIR ELEPGVEYFI RVFAILENKR SIPVSARVAT YLPAPEGLKF
KSIKETSVEV EWDPLDIAFE TWEIIFRNMN KEDEGEITKS LRRPETSYRQ TGLAPGQEYE
ISLHIVKNNT RGPGLKKVTT TRLDAPSHIE VKDVTDTTAL ITWFKPLAEI DSIELSYGIK
DVPGDRTTID LTHEDNQYSI GNLRPDTEYE VSLISRRVDM ASNPAKETFI TGLDAPRNLR
RVSQTDNSIT LEWRNVKADI DSYRIKYAPI SGGDHAEIDV PKSQQATTKT TLTGLRPGTE
YGIGVSAVKG DKESDPATIN AATEIDAPKD LRVSETTQDS LTFFWTTPLA KFDRYRLNYS
LPTGQSMEVQ LPKDATSHVL TDLEPGQEYT VLLIAEKGRH KSKPARVKAS TEEVPSLENL
TVTEAGWDGL RLNWTADDLA YEYFVIQVQE ANNVETAHNF TVPGNLRAAD IPGLKVATSY
RVSIYGVARG YRTPVLSAET STGTTPNLGE VTVAEVGWDA LTLNWTAPEG AYKNFFIQVL
EADTTQTVQN LTVPGGLRSV DLPGLKAATR YYITLRGVTQ DFGTAPLSVE VLTEDLPQLG
GLSVTEVSWD GLTLNWTTDD LAYKHFVVQV QEANNVEAAQ NLTVPGSLRA VDIPGLKADT
PYRVSIYGVI QGYRTPMLST DVSTAREPEI GNLNVSDVTP KSFNLSWTAT DGIFDMFTIE
IIDSNRLLQT AEHNISGAER TAHISGLPPS TDFIVYLSGI APSIRTKTIS TTATTEALPL
LENLTISDTN PYGFTVSWTA SENAFDSFLV TVVDSGKLLD PQEFTLSGTQ RKLELRGLIT
GIGYEVLVSG FTQGHQTKPL RAETITEAEP EVDNLLVSDA TPDGFRLSWT ADEGIFDSFV
IRIRDTKKQS EPQEISLPSP ERTRDITGLR EATEYEIELY GISRGRRSQP VSAIATTAMG
SPKEIMFSDI TENAATVSWR APTAQVESFR ITYVPMTGGA PSMVTVDGTD TETRLVKLTP
GVEYRVSVIA MKGFEESDPV SGTLITALDG PSGLLIANIT DSEALAMWQP AIATVDSYVI
SYTGERVPEV TRTVSGNTVE YELHDLEPAT EYILSIFAEK GQQKSSTIAT KFTTDLDSPR
EFTATEVQSE TALLTWRPPR ASVTGYLLVY ESVDGTVKEV IVGPDTTSYS LADLSPSTHY
SARIQALSGS LRSKLIQTIF TTIGLLYPFP RDCSQAMLNG DTTSGLYTIY INGDKTQALE
VYCDMTSDGG GWIVFLRRKN GREDFYRNWK AYAAGFGDRR EEFWLGLDNL SKITAQGQYE
LRVDLQDHGE SAYAVYDRFS VGDAKSRYKL KVEGYSGTAG DSMNYHNGRS FSTYDKDTDS
AITNCALSYK GAFWYKNCHR VNLMGRYGDN NHSQGVNWFH WKGHEYSIQF AEMKLRPSNF
RNLEGRRKRA
