ID A0A060WS70_ONCMY Unreviewed; 838 AA.
AC A0A060WS70;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=TSP C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSONMT00044427001 {ECO:0000313|EMBL:CDQ67914.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ67914.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ67914.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ67914.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) 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}.
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DR EMBL; FR904603; CDQ67914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060WS70; -.
DR STRING; 8022.A0A060WS70; -.
DR PaxDb; 8022-A0A060WS70; -.
DR Proteomes; UP000193380; 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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 1.20.5.10; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
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; IPR028974; TSP_type-3_rpt.
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; 6.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51234; TSP3; 3.
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:UP000193380};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 297..339
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 375..410
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 434..469
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 571..606
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 610..824
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 397..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..551
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 91251 MW; 7BAB3B9C2B1D548D CRC64;
MELYVNCRLA DSAQVLPSFV QLPSEAESVE IRNGQKAYAR LQGSVDSLKM ALGGSIAKAG
ILTDCPFQGD TYFQNSAGAD VNAILGDHTK ALIGQLIIFN QILGELREDI REQVKEMSLI
RNTILECQAC GECLKSSTIL RLVNYGQGVT LGLSFHEPHS RCEPNLCYKG VPCTETREYP
GYRCGACPEG MTGNGTHCQD IDECAVARPC FSPEGCVNTA KGFTCEPCPV GFSGSLLSGV
GVEFAKSHKQ ECTDVDECAD LSNTCVPNSV CINTEGSFRC GLCKESFVGN QTVGCFLRRS
CATLGFNPCD VNGHCVIKGA AEVSCKCNVG WAGNGYTCGP DTDSDGYPDQ PLPCIDNDYH
CRADNCVNTP NSGQEDADGD GIGDQCDEDA DGDGIQNVED NCRLVPNKDQ QNSDTDSYGD
ACDNCPNVPN GSQKDTDGNG AGDTCDNDID GDGIPNVLDN CPKMPNPMQT DRDGDGVGDA
CDSCPEVNDP LQSDMDNDLV GDVCDTNQDM DGDGHQDSRD NCPDVPNSSQ LDSDNDGIGD
ECDDDDDNDG IPDAGPPGPD NCRLIPNPSQ TDTDRNGIGD MCENDFDNDS VIDLIDVCPE
SAEVTMTDFR AYQTVILDQE GEAQIDPNWI VLNRGMEIVQ TMNSDPGLAI GITAFNGVDF
EGTFHINTAT DDDYVGFIFS YQDSSSFYVV MWKQMEQTYW QSLPFRAMAQ PGLQLKAVKS
RTGPGEYLRN ALWHTGDTPG EVTLLWKDPR NVGWRDKTSY RWHLSHRPQV GYIRVRLYEG
MTLVADSGVV VDTSMRGGRL GVFCFSQEQI IWSNLGYRCN DTVPEDYEFY RKQMHIRV
//
