ID   A0A3B4Z2U3_9TELE        Unreviewed;       945 AA.
AC   A0A3B4Z2U3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Tenascin N {ECO:0000313|Ensembl:ENSSPAP00000001009.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000001009.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000001009.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3B4Z2U3; -.
DR   Ensembl; ENSSPAT00000001022.1; ENSSPAP00000001009.1; ENSSPAG00000000740.1.
DR   GeneTree; ENSGT00940000166882; -.
DR   Proteomes; UP000261400; Unplaced.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00063; FN3; 5.
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; 5.
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; 3.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 5.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 5.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 4.
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   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..945
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017267122"
FT   DOMAIN          260..352
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          440..527
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          528..617
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          618..706
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          704..920
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   REGION          426..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  104758 MW;  5AE071C6924F926C CRC64;
     MTTRLLWRAL CLLALLCTVS HFSSATNHPD PSATEQGVTF SHVYKIDLPG SSSCKLESVP
     MQDNTGNEQK TTTNGENDII FKHNIRLQTP KCDCDESESF KSLLYRVNGL EEEVNYLKTQ
     CSQGCCGKGG AAGVDTSCSG HGTYQHDSCS CLCNPGWEGP DCSTSSCPDE CNDNGRCVDG
     KCVCHQGYTG DDCSQLMCPD NCNDKGQCVD GRCVCFPHFT GEDCSVQKCP NDCIGNGQCV
     DGQCVCDEGF YGEDCSLVLG PQGLRLVQVT DVSLLVEWEP VRGAEYYVLT YHPKFDEGAQ
     EQVRIPNTEN SYLITGLVPG VTYIVQVYAV IKDIQSEADK IEATTDVSTI DDIRVLGQTE
     VSIQVDWRNP QAEVDYFRLT HVDPAGQEEE LDVQRSQEAR TKHTIVGLYP GTEYQISVQA
     IKGTTEGKAS SATGATDIDS PTNLSTTEVT EDTATVSWDP VQAQIEGYML SYTSAEGSSS
     DIPVGRDSTS YRLVGLRPGV LHTVYIWAYR GDRVSRKSST EAETELDAPA NLLARDETES
     SFSVSWDPVQ ADIDGYILTY TSSDGSSGEI PVGPDRTSYL LTGLRPGVLY TVYIWAIKGS
     KATRKISTQA ETEIDSPKDL KAADVTMDSA SLTWIPPLAD IEGYILTYRD EEGNMETVEK
     QLGASERSFT ASGLEMGKRY IVTIIAYRGY KRSKVVETVF KTVGLLYPFP MDCVQIMKNG
     NRNSGVYTIY IANDRSKPVE VFCDMDTDGG GWLMLQRRNT GKLDFMKRWR QYIAGFGNLT
     DEFWIGLDKI YELTNTPTQY ELRFDLGLGS ERVYAVYDDF KIAPVKQKFK LTVGKYSGTA
     GDAMTYHQGR PWTTIDSDND IALGNCALTH RGAWWYKNCH LANLNGKWGD NRHSTGVNWE
     PWKGHLTSLD FTEMKIRPLG ALSSRKRRSL MMARERSRNT NLQRK
//