ID A0A1A6HXY1_NEOLE Unreviewed; 873 AA.
AC A0A1A6HXY1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Thrombospondin-3 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=A6R68_22884 {ECO:0000313|EMBL:OBS83106.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS83106.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS83106.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS83106.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS83106.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC {ECO:0000256|ARBA:ARBA00009456}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBS83106.1}.
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DR EMBL; LZPO01007959; OBS83106.1; -; Genomic_DNA.
DR STRING; 56216.A0A1A6HXY1; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008201; F:heparin binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd16079; TSP-3cc; 1.
DR Gene3D; 1.20.5.10; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR024665; TSP/COMP_coiled-coil.
DR InterPro; IPR046970; TSP/COMP_coiled-coil_sf.
DR InterPro; IPR028507; TSP3_coiled-coil.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF89; THROMBOSPONDIN-3; 1.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 4.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51234; TSP3; 2.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00634}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 269..307
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 468..503
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 605..640
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 644..858
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 463..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 873
FT /evidence="ECO:0000313|EMBL:OBS83106.1"
SQ SEQUENCE 873 AA; 95340 MW; 5CF044217DECD733 CRC64;
MVAVAEKIRT ALLTAGDIYL LSTFRLPPKQ GGVLFGLYSR QDNTRWLEAS VVGKINKVLV
RYQREDGKVH AVNLQQAGLA DGRTHTAILR LRGPSRPSPG LQLYVDCKLG DQHAGLPALA
PIPPAEVSGL EIRTGQKAYL RMQGFVESMK IIIGGSMARV GALSECPFQG DESIHSAGEQ
TKALVTQLTL FNQILVELRD DIRDQVKEMS LIRNTIMECQ VCGFHEQRSH CSPNPCFRGV
DCMEVYEYPG YRCGPCPPGL QGNGTHCDDI NECAHSDPCF PGSSCINTMP GFHCEACPHG
YKGTRVSGVG IDYARASKQV CHDIDECNDG NNGGCDPNSI CTNTVGSFKC GPCRLGFLGN
QSQGCLPART CHSPAHSPCH VHAHCLFERN GAVSCQCNVG WAGNGNVCGP DTDIDGYPDQ
ALPCMDNNKH CKQDNCRLFP NKDQQNSDTD SFGDACDNCP NVPNNDQKDT DGNGEGDACD
NDVDGDGIPN GLDNCPKVPN PLQTDRDEDG VGDACDSCPE MSNPTQTDAD XDLVGDVCDT
NEDSDGDGHQ DTKDNCPQLP NSSQLDSDND GLGDECDGDD DNDGVPDYVP PGPDNCRLVP
NPNQKDSDGN GVGDVCEDDF DNDAVVDPLD VCPESAEVTL TDFRAYQTVV LDPEGDAQID
PNWVVLNQGM EIVQTMNSDP GLAVGYTAFN GVDFEGTFHV NTVTDDDYAG FLFSYQDSGR
FYVVMWKQTE QTYWQATPFR AVAQPGLQLK AVTSVSGPGE HLRNAXWHTG HTPDQVRLLW
TDPRNVGWRD KTSYRWQLLH RPQVGYIRVK LYEGPQLVAD SGVIIDTSMR GGRLGVFCFS
QENIIWSNLQ YRCNDTVPED FEPFRRQLLQ GRV
//
