ID D3ZK14_RAT Unreviewed; 1562 AA.
AC D3ZK14;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 2.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Tenascin N {ECO:0000313|Ensembl:ENSRNOP00000003452.6};
GN Name=Tnn {ECO:0000313|Ensembl:ENSRNOP00000003452.6,
GN ECO:0000313|RGD:1306002};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000003452.6, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000003452.6, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000003452.6,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000003452.6}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000003452.6};
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 RefSeq; NP_001100659.2; NM_001107189.2.
DR AlphaFoldDB; D3ZK14; -.
DR SMR; D3ZK14; -.
DR STRING; 10116.ENSRNOP00000003452; -.
DR PaxDb; 10116-ENSRNOP00000003452; -.
DR Ensembl; ENSRNOT00000003452.8; ENSRNOP00000003452.6; ENSRNOG00000002548.8.
DR GeneID; 304913; -.
DR KEGG; rno:304913; -.
DR AGR; RGD:1306002; -.
DR CTD; 63923; -.
DR RGD; 1306002; Tnn.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000160553; -.
DR HOGENOM; CLU_001162_0_1_1; -.
DR InParanoid; D3ZK14; -.
DR OMA; EAPIDRY; -.
DR OrthoDB; 4173903at2759; -.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002548; Expressed in spleen and 3 other cell types or tissues.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1990026; C:hippocampal mossy fiber expansion; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0090733; C:tenascin complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0070593; P:dendrite self-avoidance; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:2001223; P:negative regulation of neuron migration; ISO:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; ISO:UniProtKB.
DR GO; GO:0002076; P:osteoblast development; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:RGD.
DR GO; GO:1903010; P:regulation of bone development; ISO:RGD.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:1905899; P:regulation of smooth muscle tissue development; ISO:RGD.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00063; FN3; 12.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 6.10.250.2590; -; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 12.
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 InterPro; IPR002049; LE_dom.
DR NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR PANTHER; PTHR46708:SF5; TENASCIN N; 1.
DR Pfam; PF18720; EGF_Tenascin; 2.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 12.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 12.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 7.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 12.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000002494};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1562
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003053385"
FT DOMAIN 264..353
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 354..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..622
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 623..706
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 709..798
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 799..882
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 885..970
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 973..1062
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1063..1144
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1149..1238
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1239..1327
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1323..1541
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 868..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..132
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1562 AA; 173250 MW; 953017AA79FA61D7 CRC64;
MGLWGMLAFP LGFLLASALL VASAPANPET PGCSHKDQQV TVSHTYKIDV PKSALVQVET
DPQSLSDDGT SLLVPGEDGE EQNIIFRHNI RLQTPQKNCE LADSVQDLLA RVKKLEEEMA
ELKEQCSTSR CCQGAADLSR HCSGHGTFFA ETCSCHCDQG WEGADCEQPT CPGACSGHGR
CVDGQCVCDQ PYVGVDCAYA ACPQDCSGHG VCVRGVCQCH KDFTAEDCSE QRCPGDCSGN
GFCDTGECYC EMGFTGPDCS QVVAPQGLQL LKSTENSLLV SWEPSSEVDH YLLSYYPLGK
EQATKQVRVP KEQHTYDITG LLPGTKYIVT LRNVKKDISS SPQHLLATTD LAVVGTAWVN
EETETSLDVE WENPLTEVDY YKLRYGPLTG QEVTEVTVPK SRDPKSRYDI TGLQPGTEYK
ITVVPIRGDL EGKPILLNGR TEIDGPTNVV TNQVTEDTAS VSWDPVRADI DKYVVRYISH
DGETKEKAVP KDQSSTVLTG LKPGEAYKVF VWAERGNQGS KKADTKALTE IDSPENLVTD
RVTENSLSVS WDPVEAEIDR YVVSYTSVDG ETKQVPVRKD QSSTVLTGLS PGVEYKVYVW
AEKGDRESKK ANTKAPTDID SPKNLVTDQV TENTLSVSWD PVQANIDRYM VSYTSADGET
REVPVPKEKS STVLTGLRPG MEYKVHVWAQ KGTQESRKAN TKAPTDIDGP KNLVTDQVTE
TTLSVSWDPV EADIDRYMVR YTSPDGETKE VPVSKDKSST VLRGLRPGVE YKVDVWAQKG
AQDSRKANTK APTDIDSPKN LVTEQVTEST ATVSWDPVEA DIDRYVVRYT SVDGETREFL
VGKDQTSTIL TGMKPGVEYQ VDVWAQKGTR ESRKTSTKAP TDIDGPKNLV TDQVTETTLS
VSWDPVEADI DRYMVRYTSP DGETKEVPVS KDKSSTVLRG LRPGVEYKVD VWAQKGAQDS
RKANTKAPTD IDSPKNLAIN QVTETTLSVS WDPVQADIDR YVVRYTSADG ESKEFLIGKE
QRSTVLTGLR PGVEYKVEVW AQKGARESKK ANTKGHTDID SPKNLVTNQV TENTATISWD
PVQADIDRYM VRYTSADGET REVPVRKEKS STVLTGLRPG VEYTVQVWAQ KGARESRKAK
TKAPTEIDSP KNLVTNRVTE NTATISWDPV RATIDRYMVR YTSADGETKE VPVSKDQSST
ILTGLKPGME YTIHVWAQKG ARESKKADTK ALTEIDPPKN FRPFGVTHSS GVLTWMPPSA
QIDGYILTYQ LPNGILKEVE LQRGQQRFEL QDLEQGVTYP VSLVAFKGNQ RSRSVSTTLS
TVDARFPHPS DCSQVQQNTN AAASGLYTIY LNGDASRPMQ VYCDMDTDGG GWIVFQRRNT
GQLDFFKRWR SYVEGFGDPM KEFWLGLDKL HNLTTGTTTR YEVRADLQTA NESAYAVYDF
FQVASSKERY KLSVGKYRGT AGDALTYHNG WKFTTFDRDN DIALSNCALT HHGGWWYKNC
HLANPNGKYG ETKHSEGVNW EPWKGHEFSI PYVELKIRPF GYSRDRFSGR KKRSIGGKAR
VF
//
