TENR_MOUSE
ID TENR_MOUSE Reviewed; 1358 AA.
AC Q8BYI9; A2RT70; O88717;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Tenascin-R;
DE Short=TN-R;
DE AltName: Full=Janusin;
DE AltName: Full=Neural recognition molecule J1-160/180;
DE AltName: Full=Restrictin;
DE Flags: Precursor;
GN Name=Tnr;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-24.
RC TISSUE=Brain;
RX PubMed=10341229; DOI=10.1523/jneurosci.19-11-04245.1999;
RA Weber P., Bartsch U., Rasband M.N., Czaniera R., Lang Y., Bluethmann H.,
RA Margolis R.U., Levinson S.R., Shrager P., Montag D.;
RT "Mice deficient for tenascin-r display alterations of the extracellular
RT matrix and decreased axonal conduction velocities in the CNS.";
RL J. Neurosci. 19:4245-4262(1999).
RN [4]
RP TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE.
RX PubMed=2477380; DOI=10.1083/jcb.109.4.1765;
RA Pesheva P., Spiess E., Schachner M.;
RT "J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates
RT for cell adhesion.";
RL J. Cell Biol. 109:1765-1778(1989).
RN [5]
RP INTERACTION WITH CNTN1, AND FUNCTION.
RX PubMed=7678967; DOI=10.1016/0896-6273(93)90243-k;
RA Pesheva P., Gennarini G., Goridis C., Schachner M.;
RT "The F3/11 cell adhesion molecule mediates the repulsion of neurons by the
RT extracellular matrix glycoprotein J1-160/180.";
RL Neuron 10:69-82(1993).
RN [6]
RP FUNCTION, AND BINDING TO MEMBRANE SURFACE SULFATIDES OF OLIGODENDROCYTES.
RX PubMed=9169525; DOI=10.1523/jneurosci.17-12-04642.1997;
RA Pesheva P., Gloor S., Schachner M., Probstmeier R.;
RT "Tenascin-R is an intrinsic autocrine factor for oligodendrocyte
RT differentiation and promotes cell adhesion by a sulfatide-mediated
RT mechanism.";
RL J. Neurosci. 17:4642-4651(1997).
RN [7]
RP FUNCTION, AND BINDING TO MEMBRANE SURFACE GANGLIOSIDES OF OLIGODENDROCYTES.
RX PubMed=10383637; DOI=10.1046/j.1460-9568.1999.00670.x;
RA Probstmeier R., Michels M., Franz T., Chan B.M.C., Pesheva P.;
RT "Tenascin-R interferes with integrin-dependent oligodendrocyte precursor
RT cell adhesion by a ganglioside-mediated signalling mechanism.";
RL Eur. J. Neurosci. 11:2474-2488(1999).
RN [8]
RP GLYCOSYLATION.
RX PubMed=10406848; DOI=10.1093/glycob/9.8.823;
RA Zamze S., Harvey D.J., Pesheva P., Mattu T.S., Schachner M., Dwek R.A.,
RA Wing D.R.;
RT "Glycosylation of a CNS-specific extracellular matrix glycoprotein,
RT tenascin-R, is dominated by O-linked sialylated glycans and 'brain-type'
RT neutral N-glycans.";
RL Glycobiology 9:823-831(1999).
RN [9]
RP GLYCOSYLATION, INTERACTION WITH FN1 AND TNC, AND FUNCTION.
RX PubMed=10773191; DOI=10.1016/s0006-8993(00)02075-8;
RA Probstmeier R., Braunewell K.-H., Pesheva P.;
RT "Involvement of chondroitin sulfates on brain-derived tenascin-R in
RT carbohydrate-dependent interactions with fibronectin and tenascin-C.";
RL Brain Res. 863:42-51(2000).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Neural extracellular matrix (ECM) protein involved in
CC interactions with different cells and matrix components. Theses
CC interactions can influence cellular behavior by either evoking a stable
CC adhesion and differentiation, or repulsion and inhibition of neurite
CC growth. Binding to cell surface gangliosides inhibits RGD-dependent
CC integrin-mediated cell adhesion and results in an inhibition of
CC PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to
CC membrane surface sulfatides results in a oligodendrocyte adhesion and
CC differentiation. Interaction with CNTN1 induces a repulsion of neurons
CC and an inhibition of neurite outgrowth. Interacts with SCN2B may play a
CC crucial role in clustering and regulation of activity of sodium
CC channels at nodes of Ranvier. TNR-linked chondroitin sulfate
CC glycosaminoglycans are involved in the interaction with FN1 and
CC mediates inhibition of cell adhesion and neurite outgrowth. The highly
CC regulated addition of sulfated carbohydrate structure may modulate the
CC adhesive properties of TNR over the course of development and during
CC synapse maintenance (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10383637, ECO:0000269|PubMed:10773191,
CC ECO:0000269|PubMed:7678967, ECO:0000269|PubMed:9169525}.
CC -!- SUBUNIT: Interacts with BCAN and ACAN in a calcium-dependent manner.
CC Interacts with SCN2B, PTPRZ1, and CSPG3 (By similarity). Forms
CC oligomers. Isoforms 1 and 2 form respectively trimeric (tribrachion)
CC and dimeric kink-armed rodlike structures, which are linked by
CC disulfide bridges. Interacts with CNTN1, TNC and FN1. {ECO:0000250,
CC ECO:0000269|PubMed:10773191, ECO:0000269|PubMed:7678967}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=J1-180, TN-R 180;
CC IsoId=Q8BYI9-1; Sequence=Displayed;
CC Name=2; Synonyms=J1-160, TN-R 160;
CC IsoId=Q8BYI9-2; Sequence=VSP_012994;
CC -!- TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:2477380}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is barely detectable at 17 dpc and
CC increases in intensity until postnatal day 15, when it reaches adult
CC levels. Isoform 2 is detectable from postnatal day 5 and reaches adult
CC levels also at postnatal day 15. {ECO:0000269|PubMed:2477380}.
CC -!- DOMAIN: The EGF-like domains mediate interaction with CNTN1. The
CC fibronectin type-III domains 3-5 mediate interaction with BCAN. The
CC fibronectin type-III domains 1-2 and 7-9 mediate interaction with SCN2B
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Contains N-linked oligosaccharides with a sulfated carbohydrate
CC structures (By similarity). Contains N-linked oligosaccharides, O-
CC linked sialylated structures and O-linked chondroitin sulfate
CC glycosaminoglycans. {ECO:0000250, ECO:0000269|PubMed:10406848,
CC ECO:0000269|PubMed:10773191}.
CC -!- MISCELLANEOUS: Knockout mice display alterations of the extracellular
CC matrix, and decreased axonal conduction velocities in the CNS.
CC -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
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DR EMBL; AK039390; BAC30335.1; -; mRNA.
DR EMBL; BC132392; AAI32393.1; -; mRNA.
DR EMBL; BC138043; AAI38044.1; -; mRNA.
DR EMBL; AJ005844; CAA06739.1; -; mRNA.
DR CCDS; CCDS15403.1; -. [Q8BYI9-1]
DR RefSeq; NP_071707.2; NM_022312.3. [Q8BYI9-1]
DR RefSeq; XP_006496805.1; XM_006496742.3. [Q8BYI9-1]
DR RefSeq; XP_006496806.1; XM_006496743.2. [Q8BYI9-1]
DR RefSeq; XP_006496807.1; XM_006496744.3. [Q8BYI9-1]
DR AlphaFoldDB; Q8BYI9; -.
DR SMR; Q8BYI9; -.
DR BioGRID; 204272; 25.
DR ComplexPortal; CPX-1033; Tenascin-R complex.
DR IntAct; Q8BYI9; 15.
DR MINT; Q8BYI9; -.
DR STRING; 10090.ENSMUSP00000107298; -.
DR GlyConnect; 590; 25 N-Linked glycans (5 sites), 2 O-Linked glycans.
DR GlyGen; Q8BYI9; 14 sites, 36 N-linked glycans (6 sites), 3 O-linked glycans (1 site).
DR iPTMnet; Q8BYI9; -.
DR PhosphoSitePlus; Q8BYI9; -.
DR SwissPalm; Q8BYI9; -.
DR MaxQB; Q8BYI9; -.
DR PaxDb; Q8BYI9; -.
DR PeptideAtlas; Q8BYI9; -.
DR PRIDE; Q8BYI9; -.
DR ProteomicsDB; 263275; -. [Q8BYI9-1]
DR ProteomicsDB; 263276; -. [Q8BYI9-2]
DR Antibodypedia; 20571; 141 antibodies from 25 providers.
DR DNASU; 21960; -.
DR Ensembl; ENSMUST00000111669; ENSMUSP00000107298; ENSMUSG00000015829. [Q8BYI9-1]
DR Ensembl; ENSMUST00000192069; ENSMUSP00000141553; ENSMUSG00000015829. [Q8BYI9-1]
DR GeneID; 21960; -.
DR KEGG; mmu:21960; -.
DR UCSC; uc007dea.2; mouse. [Q8BYI9-1]
DR CTD; 7143; -.
DR MGI; MGI:99516; Tnr.
DR VEuPathDB; HostDB:ENSMUSG00000015829; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157761; -.
DR HOGENOM; CLU_001162_0_0_1; -.
DR InParanoid; Q8BYI9; -.
DR OMA; RPYNHRP; -.
DR OrthoDB; 18592at2759; -.
DR PhylomeDB; Q8BYI9; -.
DR TreeFam; TF329915; -.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 21960; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tnr; mouse.
DR PRO; PR:Q8BYI9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BYI9; protein.
DR Bgee; ENSMUSG00000015829; Expressed in dentate gyrus of hippocampal formation granule cell and 87 other tissues.
DR ExpressionAtlas; Q8BYI9; baseline and differential.
DR Genevisible; Q8BYI9; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:ComplexPortal.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0072534; C:perineuronal net; IDA:MGI.
DR GO; GO:0098966; C:perisynaptic extracellular matrix; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0090733; C:tenascin complex; IPI:ComplexPortal.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0046625; F:sphingolipid binding; TAS:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0048675; P:axon extension; IDA:MGI.
DR GO; GO:0048677; P:axon extension involved in regeneration; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0035641; P:locomotory exploration behavior; IMP:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:MGI.
DR GO; GO:0030517; P:negative regulation of axon extension; IDA:MGI.
DR GO; GO:0048692; P:negative regulation of axon extension involved in regeneration; IMP:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:ComplexPortal.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IMP:MGI.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IMP:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:ComplexPortal.
DR GO; GO:0045595; P:regulation of cell differentiation; IDA:ComplexPortal.
DR GO; GO:0030334; P:regulation of cell migration; IDA:ComplexPortal.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0022029; P:telencephalon cell migration; IMP:MGI.
DR CDD; cd00063; FN3; 9.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 2.60.40.10; -; 9.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
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; IPR033079; TNR.
DR PANTHER; PTHR19143:SF254; PTHR19143:SF254; 3.
DR Pfam; PF18720; EGF_Tenascin; 4.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 9.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 9.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Coiled coil; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Phosphoprotein;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Sialic acid; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1358
FT /note="Tenascin-R"
FT /id="PRO_0000007748"
FT DOMAIN 188..199
FT /note="EGF-like 1"
FT DOMAIN 219..230
FT /note="EGF-like 2"
FT DOMAIN 250..261
FT /note="EGF-like 3"
FT DOMAIN 281..292
FT /note="EGF-like 4"
FT DOMAIN 312..323
FT /note="EGF-like 5"
FT DOMAIN 328..420
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 421..505
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 506..597
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 598..687
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 688..777
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 778..865
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 866..955
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 956..1042
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1043..1131
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1129..1344
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 37..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 127..157
FT /evidence="ECO:0000255"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05546"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1046
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 297..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 314..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT VAR_SEQ 773..862
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_012994"
FT CONFLICT 54
FT /note="Y -> H (in Ref. 1; BAC30335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1358 AA; 149589 MW; 354D2E71AB356952 CRC64;
MGIDGETVVL KNMLIGVNLI LLGSMLKPSE CRLEVTTERA QRQTVEEEGG ASSYNTSSKE
QPMVFNHVYN INVPLESLCS SGLEASAEQD MSAEDDTLAE YIGQTSDHES QVTFTHKINL
PKKACPCASS SQVLQELLSR IEMLEREVSL LRDQCNTNCC QESAATGQLD YVPHCSGHGN
FSFESCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS
SRGLCVDGEC VCEEPYTGED CRELRCPGDC SGKGQCANGT CLCQEGYAGE DCSQRRCLNA
CSGRGHCQEG LCICEEGYQG PDCSAVAPPE DLRVAGISDR SIELEWDGPM AVTEYVISYQ
PTALGGLQLQ QRVPGDWSGV TIMELEPGLT YNISVYAVIS NILSLPITAK VATHLSTPQG
LQFKTITETT VEVQWEPFSF SFDGWEISFI PKNNEGGVIA QLPSDVTSFN QTGLKPGEEY
IVNVVALKEQ ARSPPTSASV STVIDGPTQI LVRDVSDTVA FVEWTPPRAK VDFILLKYGL
VGGEGGKTTF RLQPPLSQYS VQALRPGSRY EVSISAVRGT NESEASSTQF TTEIDAPKNL
RVGSRTATSL DLEWDNSEAE AQEYKVVYST LAGEQYHEVL VPKGIGPTTK TTLTDLVPGT
EYGVGISAVM NSKQSIPATM NARTELDSPR DLMVTASSET SISLIWTKAS GPIDHYRITF
TPSSGISSEV TVPRDRTSYT LTDLEPGAEY IISITAERGR QQSLESTVDA FTGFRPISHL
HFSHVTSSSV NITWSDPSPP ADRLILNYSP RDKEEDMLEV LLDATKRHAV LMGLQPATEY
IVNLVAVHGT VTSEPIVGSI TTGIDPPKNI TISNVTKDSL TVSWSSPVAP FDYYRVSYRP
TQVGRLDSSV VPNTVTEFAI TRLYPATEYE ISLNSVRGRE ESERICTLVH TAMDSPMDLI
ATNITPTEAL LQWKAPMGEV ENYVIVLTHF AIAGETILVD GVSEEFQLVD LLPSTHYTVT
MYATSGPLMS GTIATNFSTL LDPPDNLTAS EVTRQSALIS WQPPRAAIEN YVLTYKSTDG
SRKELIVDAE DTWIRLEGLS ENTDYTVLLQ AAQEATRSSL TSTVFTTGGR VFSHPQDCAQ
HLMNGDTLSG VYTIFLNGEL SHKLQVYCDM TTDGGGWIVF QRRQNGQTDF FRKWADYRVG
FGNLEDEFWL GLDNIHRITA QGRYELRVDM RDGQEAVFAY YDKFAVEDSR SLYKIRIGSY
NGTAGDSLSY HQGRPFSTED RDNDVAVTNC AMSYKGAWWY KNCHRTNLNG KYGESRHSQG
INWYHWKGHE FSIPFVEMKM RPYIHRLTAG RKRRALKF
