ID   TENR_HUMAN              Reviewed;        1358 AA.
AC   Q92752; C9J563; Q15568; Q5R3G0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 3.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Tenascin-R;
DE            Short=TN-R;
DE   AltName: Full=Janusin;
DE   AltName: Full=Restrictin;
DE   Flags: Precursor;
GN   Name=TNR;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP   VARIANT VAL-17.
RC   TISSUE=Brain;
RX   PubMed=8626505; DOI=10.1074/jbc.271.14.8157;
RA   Carnemolla B., Leprini A., Borsi L., Querze G., Urbini S., Zardi L.;
RT   "Human tenascin-R: complete primary structure, pre-mRNA alternative
RT   splicing and gene localization on chromosome 1q23-q24.";
RL   J. Biol. Chem. 271:8157-8160(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-17.
RC   TISSUE=Brain;
RA   Williams H., Schachner M., Wang B., Goodfellow P., Kenwrick S.;
RT   "Isolation of the gene for neural cell adhesion molecule tenascin-R and
RT   fine mapping relative to loci in 1q25-31.";
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-37, AND STRUCTURE OF
RP   CARBOHYDRATES.
RC   TISSUE=Cerebrospinal fluid;
RX   PubMed=19838169; DOI=10.1038/nmeth.1392;
RA   Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA   Larson G.;
RT   "Enrichment of glycopeptides for glycan structure and attachment site
RT   identification.";
RL   Nat. Methods 6:809-811(2009).
RN   [5]
RP   VARIANTS NEDSTO 69-TYR--PHE-1358 DEL; THR-397; ASN-532; 905-ARG--PHE-1358
RP   DEL; ARG-1119 AND TRP-1192, AND INVOLVEMENT IN NEDSTO.
RX   PubMed=32099069; DOI=10.1038/s41436-020-0768-7;
RA   Wagner M., Levy J., Jung-Klawitter S., Bakhtiari S., Monteiro F.,
RA   Maroofian R., Bierhals T., Hempel M., Elmaleh-Berges M., Kitajima J.P.,
RA   Kim C.A., Salomao J.G., Amor D.J., Cooper M.S., Perrin L., Pipiras E.,
RA   Neu A., Doosti M., Karimiani E.G., Toosi M.B., Houlden H., Jin S.C.,
RA   Si Y.C., Rodan L.H., Venselaar H., Kruer M.C., Kok F., Hoffmann G.F.,
RA   Strom T.M., Wortmann S.B., Tabet A.C., Opladen T.;
RT   "Loss of TNR causes a nonprogressive neurodevelopmental disorder with
RT   spasticity and transient opisthotonus.";
RL   Genet. Med. 22:1061-1068(2020).
CC   -!- FUNCTION: Neural extracellular matrix (ECM) protein involved in
CC       interactions with different cells and matrix components. These
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 mediate
CC       inhibition of cell adhesion and neurite outgrowth. The highly regulated
CC       addition of sulfated carbohydrate structure may modulate the adhesive
CC       properties of TNR over the course of development and during synapse
CC       maintenance (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms oligomers. Interacts with CNTN1, TNC, and FN1. Interacts
CC       with BCAN and ACAN in a calcium-dependent manner. Interacts with SCN2B,
CC       PTPRZ1, and CSPG3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q92752-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92752-2; Sequence=VSP_012993;
CC   -!- TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:8626505}.
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, O-linked sialylated structures
CC       and O-linked chondroitin sulfate glycosaminoglycans. Contains N-linked
CC       oligosaccharides with a sulfated carbohydrate structure (By
CC       similarity). O-glycosylated on Thr-36 or Thr-37 with a core 1 or
CC       possibly core 8 glycan. {ECO:0000250, ECO:0000269|PubMed:19838169}.
CC   -!- DISEASE: Neurodevelopmental disorder, non-progressive, with spasticity
CC       and transient opisthotonus (NEDSTO) [MIM:619653]: An autosomal
CC       recessive disorder characterized by delayed motor milestones, delayed
CC       walking, speech delay, axial hypotonia, and peripheral spasticity
CC       apparent from infancy or early childhood. Affected individuals often
CC       show transient opisthotonic posturing in infancy, and later show
CC       abnormal involuntary movements. Variably impaired intellectual
CC       development, and brain myelination defects are present in some
CC       patients. {ECO:0000269|PubMed:32099069}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
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DR   EMBL; Z67996; CAA91947.1; -; mRNA.
DR   EMBL; X98085; CAA66709.1; -; mRNA.
DR   EMBL; AL021919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL023285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL136530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z94055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z94057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS1318.1; -. [Q92752-1]
DR   RefSeq; NP_003276.3; NM_003285.2. [Q92752-1]
DR   RefSeq; XP_016857707.1; XM_017002218.1.
DR   RefSeq; XP_016857708.1; XM_017002219.1.
DR   PDB; 8FN9; X-ray; 1.80 A; A/C/E/G=1129-1358.
DR   PDB; 8FNA; X-ray; 1.75 A; A=1129-1358.
DR   PDBsum; 8FN9; -.
DR   PDBsum; 8FNA; -.
DR   AlphaFoldDB; Q92752; -.
DR   SMR; Q92752; -.
DR   BioGRID; 112997; 13.
DR   ComplexPortal; CPX-1019; Tenascin-R complex.
DR   IntAct; Q92752; 4.
DR   STRING; 9606.ENSP00000356646; -.
DR   UniLectin; Q92752; -.
DR   GlyCosmos; Q92752; 14 sites, No reported glycans.
DR   GlyGen; Q92752; 17 sites.
DR   iPTMnet; Q92752; -.
DR   PhosphoSitePlus; Q92752; -.
DR   SwissPalm; Q92752; -.
DR   BioMuta; TNR; -.
DR   DMDM; 311033534; -.
DR   jPOST; Q92752; -.
DR   MassIVE; Q92752; -.
DR   PaxDb; 9606-ENSP00000356646; -.
DR   PeptideAtlas; Q92752; -.
DR   ProteomicsDB; 75442; -. [Q92752-1]
DR   ProteomicsDB; 75443; -. [Q92752-2]
DR   Antibodypedia; 20571; 156 antibodies from 25 providers.
DR   DNASU; 7143; -.
DR   Ensembl; ENST00000367674.7; ENSP00000356646.1; ENSG00000116147.18. [Q92752-1]
DR   GeneID; 7143; -.
DR   KEGG; hsa:7143; -.
DR   MANE-Select; ENST00000367674.7; ENSP00000356646.1; NM_003285.3; NP_003276.3.
DR   UCSC; uc009wwu.2; human. [Q92752-1]
DR   AGR; HGNC:11953; -.
DR   CTD; 7143; -.
DR   DisGeNET; 7143; -.
DR   GeneCards; TNR; -.
DR   HGNC; HGNC:11953; TNR.
DR   HPA; ENSG00000116147; Group enriched (brain, retina).
DR   MalaCards; TNR; -.
DR   MIM; 601995; gene.
DR   MIM; 619653; phenotype.
DR   neXtProt; NX_Q92752; -.
DR   OpenTargets; ENSG00000116147; -.
DR   PharmGKB; PA36642; -.
DR   VEuPathDB; HostDB:ENSG00000116147; -.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; KOG2579; Eukaryota.
DR   GeneTree; ENSGT00940000157761; -.
DR   HOGENOM; CLU_001162_0_0_1; -.
DR   InParanoid; Q92752; -.
DR   OMA; QCVCDSD; -.
DR   OrthoDB; 5489847at2759; -.
DR   PhylomeDB; Q92752; -.
DR   TreeFam; TF329915; -.
DR   PathwayCommons; Q92752; -.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   SignaLink; Q92752; -.
DR   BioGRID-ORCS; 7143; 16 hits in 1148 CRISPR screens.
DR   ChiTaRS; TNR; human.
DR   GeneWiki; Tenascin-R; -.
DR   GenomeRNAi; 7143; -.
DR   Pharos; Q92752; Tbio.
DR   PRO; PR:Q92752; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q92752; Protein.
DR   Bgee; ENSG00000116147; Expressed in CA1 field of hippocampus and 82 other cell types or tissues.
DR   ExpressionAtlas; Q92752; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:ComplexPortal.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0072534; C:perineuronal net; ISO:ComplexPortal.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0090733; C:tenascin complex; ISO:ComplexPortal.
DR   GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR   GO; GO:0048677; P:axon extension involved in regeneration; IEA:Ensembl.
DR   GO; GO:0007411; P:axon guidance; NAS:ProtInc.
DR   GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0048692; P:negative regulation of axon extension involved in regeneration; IEA:Ensembl.
DR   GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISO:ComplexPortal.
DR   GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl.
DR   GO; GO:0097402; P:neuroblast migration; IEA:Ensembl.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR   GO; GO:0007158; P:neuron cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR   GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IEA:Ensembl.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISO:ComplexPortal.
DR   GO; GO:0045595; P:regulation of cell differentiation; ISO:ComplexPortal.
DR   GO; GO:0030334; P:regulation of cell migration; ISO:ComplexPortal.
DR   GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR   GO; GO:0022029; P:telencephalon cell migration; IEA:Ensembl.
DR   CDD; cd00063; FN3; 9.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR   Gene3D; 2.10.25.10; Laminin; 4.
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   NCBIfam; NF040941; GGGWT_bact; 1.
DR   PANTHER; PTHR46708; TENASCIN; 1.
DR   PANTHER; PTHR46708:SF6; TENASCIN-R; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF18720; EGF_Tenascin; 2.
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; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 5.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 9.
DR   Genevisible; Q92752; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Coiled coil;
KW   Disease variant; Disulfide bond; EGF-like domain; Extracellular matrix;
KW   Glycoprotein; Phosphoprotein; Proteoglycan; Reference proteome; Repeat;
KW   Secreted; Sialic acid; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..1358
FT                   /note="Tenascin-R"
FT                   /id="PRO_0000007747"
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..595
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          596..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..1130
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   COILED          127..157
FT                   /evidence="ECO:0000255"
FT   MOD_RES         724
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05546"
FT   CARBOHYD        36
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000305|PubMed:19838169"
FT   CARBOHYD        37
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000305|PubMed:19838169"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
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        271
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
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        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        292..301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        297..312
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:0000303|PubMed:8626505"
FT                   /id="VSP_012993"
FT   VARIANT         17
FT                   /note="I -> V (in dbSNP:rs859398)"
FT                   /evidence="ECO:0000269|PubMed:8626505, ECO:0000269|Ref.2"
FT                   /id="VAR_021479"
FT   VARIANT         69..1358
FT                   /note="Missing (in NEDSTO)"
FT                   /evidence="ECO:0000269|PubMed:32099069"
FT                   /id="VAR_086584"
FT   VARIANT         128
FT                   /note="A -> S (in dbSNP:rs2239819)"
FT                   /id="VAR_021906"
FT   VARIANT         293
FT                   /note="G -> S (in dbSNP:rs3752516)"
FT                   /id="VAR_021907"
FT   VARIANT         302
FT                   /note="S -> N (in dbSNP:rs35736986)"
FT                   /id="VAR_055780"
FT   VARIANT         397
FT                   /note="A -> T (in NEDSTO; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:32099069"
FT                   /id="VAR_086585"
FT   VARIANT         532
FT                   /note="D -> N (in NEDSTO; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:32099069"
FT                   /id="VAR_086586"
FT   VARIANT         643
FT                   /note="R -> K (in dbSNP:rs859427)"
FT                   /id="VAR_030737"
FT   VARIANT         905..1358
FT                   /note="Missing (in NEDSTO)"
FT                   /evidence="ECO:0000269|PubMed:32099069"
FT                   /id="VAR_086587"
FT   VARIANT         1119
FT                   /note="S -> R (in NEDSTO; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:32099069"
FT                   /id="VAR_086588"
FT   VARIANT         1192
FT                   /note="R -> W (in NEDSTO)"
FT                   /evidence="ECO:0000269|PubMed:32099069"
FT                   /id="VAR_086589"
FT   CONFLICT        629
FT                   /note="S -> I (in Ref. 2; CAA66709)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1138..1143
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   STRAND          1150..1155
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   HELIX           1156..1158
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   HELIX           1160..1162
FT                   /evidence="ECO:0007829|PDB:8FN9"
FT   STRAND          1163..1169
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   HELIX           1172..1174
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   STRAND          1177..1186
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   HELIX           1194..1199
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   STRAND          1206..1209
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   HELIX           1212..1219
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   STRAND          1224..1232
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   STRAND          1235..1246
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   TURN            1249..1253
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   STRAND          1255..1257
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   STRAND          1260..1264
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   HELIX           1269..1271
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   STRAND          1284..1288
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   HELIX           1290..1293
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   STRAND          1301..1303
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   TURN            1317..1319
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   HELIX           1324..1327
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   STRAND          1334..1342
FT                   /evidence="ECO:0007829|PDB:8FNA"
FT   HELIX           1343..1347
FT                   /evidence="ECO:0007829|PDB:8FN9"
SQ   SEQUENCE   1358 AA;  149562 MW;  E4DE356B44D117E7 CRC64;
     MGADGETVVL KNMLIGINLI LLGSMIKPSE CQLEVTTERV QRQSVEEEGG IANYNTSSKE
     QPVVFNHVYN INVPLDNLCS SGLEASAEQE VSAEDETLAE YMGQTSDHES QVTFTHRINF
     PKKACPCASS AQVLQELLSR IEMLEREVSV LRDQCNANCC QESAATGQLD YIPHCSGHGN
     FSFESCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS
     SRGLCVDGEC VCEEPYTGED CRELRCPGDC SGKGRCANGT CLCEEGYVGE DCGQRQCLNA
     CSGRGQCEEG LCVCEEGYQG PDCSAVAPPE DLRVAGISDR SIELEWDGPM AVTEYVISYQ
     PTALGGLQLQ QRVPGDWSGV TITELEPGLT YNISVYAVIS NILSLPITAK VATHLSTPQG
     LQFKTITETT VEVQWEPFSF SFDGWEISFI PKNNEGGVIA QVPSDVTSFN QTGLKPGEEY
     IVNVVALKEQ ARSPPTSASV STVIDGPTQI LVRDVSDTVA FVEWIPPRAK VDFILLKYGL
     VGGEGGRTTF RLQPPLSQYS VQALRPGSRY EVSVSAVRGT NESDSATTQF TTEIDAPKNL
     RVGSRTATSL DLEWDNSEAE VQEYKVVYST LAGEQYHEVL VPRGIGPTTR ATLTDLVPGT
     EYGVGISAVM NSQQSVPATM NARTELDSPR DLMVTASSET SISLIWTKAS GPIDHYRITF
     TPSSGIASEV TVPKDRTSYT LTDLEPGAEY IISVTAERGR QQSLESTVDA FTGFRPISHL
     HFSHVTSSSV NITWSDPSPP ADRLILNYSP RDEEEEMMEV SLDATKRHAV LMGLQPATEY
     IVNLVAVHGT VTSEPIVGSI TTGIDPPKDI TISNVTKDSV MVSWSPPVAS FDYYRVSYRP
     TQVGRLDSSV VPNTVTEFTI TRLNPATEYE ISLNSVRGRE ESERICTLVH TAMDNPVDLI
     ATNITPTEAL LQWKAPVGEV ENYVIVLTHF AVAGETILVD GVSEEFRLVD LLPSTHYTAT
     MYATNGPLTS GTISTNFSTL LDPPANLTAS EVTRQSALIS WQPPRAEIEN YVLTYKSTDG
     SRKELIVDAE DTWIRLEGLL ENTDYTVLLQ AAQDTTWSSI TSTAFTTGGR VFPHPQDCAQ
     HLMNGDTLSG VYPIFLNGEL SQKLQVYCDM TTDGGGWIVF QRRQNGQTDF FRKWADYRVG
     FGNVEDEFWL GLDNIHRITS QGRYELRVDM RDGQEAAFAS YDRFSVEDSR NLYKLRIGSY
     NGTAGDSLSY HQGRPFSTED RDNDVAVTNC AMSYKGAWWY KNCHRTNLNG KYGESRHSQG
     INWYHWKGHE FSIPFVEMKM RPYNHRLMAG RKRQSLQF
//