ID F6YNG1_CALJA Unreviewed; 1299 AA.
AC F6YNG1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Tenascin N {ECO:0000313|Ensembl:ENSCJAP00000016401.5};
GN Name=TNN {ECO:0000313|Ensembl:ENSCJAP00000016401.5};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000016401.5, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000016401.5}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000016401.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the tenascin family.
CC {ECO:0000256|ARBA:ARBA00008673}.
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DR Ensembl; ENSCJAT00000017346.5; ENSCJAP00000016401.5; ENSCJAG00000008930.5.
DR GeneTree; ENSGT00940000160553; -.
DR OMA; EAPIDRY; -.
DR Proteomes; UP000008225; Chromosome 18.
DR Bgee; ENSCJAG00000008930; Expressed in ovary and 1 other cell type or tissue.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:1990026; C:hippocampal mossy fiber expansion; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0090733; C:tenascin complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:1903010; P:regulation of bone development; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR GO; GO:1905899; P:regulation of smooth muscle tissue development; IEA:Ensembl.
DR CDD; cd00035; ChtBD1; 1.
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; 3.
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; IPR020837; Fibrinogen_CS.
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:SF5; TENASCIN N; 1.
DR Pfam; PF18720; EGF_Tenascin; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 9.
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; PS01186; EGF_2; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 9.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1299
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035157477"
FT DOMAIN 264..352
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 353..444
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 445..532
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 533..623
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 624..709
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 710..800
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 801..886
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 887..976
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 977..1063
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1061..1278
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 958..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1299 AA; 144354 MW; 6F43B46DD2061413 CRC64;
MSLQEMFCFP LGLLLGSVLL VASAPATLEL PGCSNKEQQV TVSHTYKIDV PKSALVQMEA
DPQPLSDDGT SLLALGEARE EQNIIFRHNI RLQTPQKDCE LATSVQDLLA RVKKLEEEMM
EMKKQCSAQR CCQGATDLRH HCSGHGTFSL ETCSCHCQEG WEGTTCEQQA CPGACSGHGR
CVDGHCLCHE PYVGADCGYP PCPENCSGHG ECVRGVCQCH EDFTSEDCSE RRCPGDCSGH
GFCDTGECYC EEGFAGLDCA QVVVPQGLQL LKSTEDSLLV SWEPSSQVDH YLLSYYPLGK
EISGKQIQVP KEQHSYEILN LLPGTKYVVT LRNVKKEVSS SPQHLLATTD HAVLGTAWVT
DETENSLDVE WENPSTEVDY YKLRYGPMTG QEVAEVTVPK SSDPKSRYDI TGLHPGTEYK
ITVVPMRGEL EGKPILLNGR TEIDSPTNVI TDRVTENTAT VSWDPVQAVI DKYVVRYTSA
DGDTEEMAVH KDESSTVLTG LKPGEAYKVY VWAERGNQGS KKADTNALTE IDSPANLVTD
RVTEHTATIS WDPVQATIDK YVVSYASADD QETREVPVGK EQSSTVLTGL RPGVEYMVHV
WAQKGDRESK RADTKAPTDI DSPKNLVTDR VTENMATVSW DPVQAAIDKY VVRYTSADGE
TREVPVGKEQ SSTVLMGLRP GVEYTVHVWA QKGDQESKKA DTKAQTDIDS PQNLVTDRVT
ENMAIVSWDP VQATIDRYVV RYTSAEDGET REVPVEKEER STVLTGLRPG VEYTVHVWAE
KGAQESKKAD TKAQTDIDSP KNLVTDEVTE NMATVSWDPV QAAIDKYMVR YTSADGETRE
VPVGKEQSST VLMGLRPGVE YTVHVWAQKG DQESKKADTK AQTEMDSPKN LMIDQVTENM
ATVSWDPVQA PIDKYVVRYA SADGETREVP VGKEQSSTVL MGLRPGVEYT VHVWAQKGDR
ESKKADTKAQ TELDPPRNLR PSAVTQSAGI LTWTPPSAQI HGYILTYQFP DGTVKEMQLG
REDQRFELQG LEQGATYPVS LVAFKGDRRS RNVSTTLSTV GARFPHPSDC SQVRQNNNAA
SGLYTIYLHG DASRPLQVYC DMDTDGGGWT VFQRRNTGQL DFFKRWRSYV EGFGDPRKEF
WLGLDNLHNL TTGTPTRYEV RVDLQTANES AYAIYDFFQV ASSKERYKLT VGKYRGTAGD
ALSYHNGWKF TTFDRDNDIA LSNCALTHHG GWWYKNCHLA NPNGRYGETK HSEGVNWEPW
KGHEFSIPYV ELKIRPRGYS SEPVLGRKKR TLGGMLRTF
//
