ID A0A091PZ25_LEPDC Unreviewed; 1177 AA.
AC A0A091PZ25;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE SubName: Full=Tenascin-R {ECO:0000313|EMBL:KFQ12566.1};
DE Flags: Fragment;
GN ORFNames=N330_11463 {ECO:0000313|EMBL:KFQ12566.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ12566.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ12566.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ12566.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK680963; KFQ12566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PZ25; -.
DR Proteomes; UP000053001; Unassembled WGS sequence.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00063; FN3; 8.
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; 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; PF18720; EGF_Tenascin; 4.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 8.
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; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 8.
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:UP000053001};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 162..252
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 253..343
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 417..508
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 509..598
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 599..685
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 686..774
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 775..861
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 862..950
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 948..1163
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 325..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ12566.1"
FT NON_TER 1177
FT /evidence="ECO:0000313|EMBL:KFQ12566.1"
SQ SEQUENCE 1177 AA; 129135 MW; 638CC3D69FC65BD5 CRC64;
GQLDYTPQCS GHGNFSLESC SCVCMEGWAG SNCSEPRCPR GCSSRGVCLE GQCICDNDYG
GEDCSQLRCP AGCGSHGLCV DGECICEEGF TGEDCSQLRC PHDCSGKGHC ANGTCICQEG
YAGEDCGWLH CPNACSGRGV CRDGLCICEE GYEGQDCSAV APPENLRVTG IGDSSIELTW
DSPRAATEYV ISYQPVGPGG TQLQQRVPGD WSSITITELE PGVAYNISVY AVISDVLSIP
VTSKVMTNLA MPQGLKFKTI TETTAEVQWE PFSFPFDGWE ISFIPKNNEG GVIAQLPSTV
TTFNQTGLKP GEEYTVTVVA LKEQARSPPT SDSVSTPQSS PPAVPPRSAR CGLIETSPGQ
AQIFLSLGTT FRLQPPLSQY SLQALRPGAR YHLAVSALRG ANESRPALTQ FTTEIDAPKN
LRVGSRTPTS LELAWDNSEA EAQSYRVVYS TLAGEHYHEV LVPRDTGPTT RATLADLVPG
TEYGIGISAV MDNQQSVPAT MNARTELDSP RDLLVTASTE TSISLAWTKA TGPIDHYRIT
FTPASGMASE VTVPRDESQL TLLELEPGTE YTISIIAERG RQQSLEATVD AFTGVRPITQ
LHFSQLTSSS VNVTWSDPSP PADRLILTYS PRDEEETQQV TLDGTRRHAS LMGLQPATEY
LVSLVAVHGT ISSEPVVGSI TTGIDAPKDL RVGNITQESM MVYWSPPIAA FDHYRIFYRT
AEGRTDSTSI VSDATEYALR HLQPATKYEI GVKSVRGREE SEVASITVHT AMDAPLGVTA
TNITPTEALL QWNPPLSEVE SYTLILTRHA VAGETILVDG VNQEYQLTSL LPSTTYIVSM
YATNGPLTSQ IISTNFTTLL DPPTNLTASE VTRRSALLSW VPPVGQIENY IMTYRSTDGS
RKELIVDAED TWIRLEGLSE TTEYTVRLQA AQNTMRSGFI STTFTTGGRV FANPQDCAQH
LMNGDTLSGI YTISINGDLS QRVQVYCDMT TDGGGWIVFQ RRQNGLTDFF RKWADYRVGF
GNLEDEFWLG LDNIHKITSQ GRYELRIDMR DGQEVAYAYY DKFSIGDSRS LYKLRIGDYN
GTSGDSLTYH QGRPFSTKDR DNDVAVTNCA MSYKGAWWYK NCHRTNLNGK YGESRHSQGI
NWYHWKGHEF SIPFVEMKMR PYNHRNISGR KRRSPQL
//
