ID A0A3B3R7S8_9TELE Unreviewed; 953 AA.
AC A0A3B3R7S8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Thrombospondin-3a-like {ECO:0000313|Ensembl:ENSPKIP00000014433.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000014433.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000014433.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B3R7S8; -.
DR STRING; 1676925.ENSPKIP00000014433; -.
DR Ensembl; ENSPKIT00000038873.1; ENSPKIP00000014433.1; ENSPKIG00000001460.1.
DR GeneTree; ENSGT00940000159283; -.
DR OrthoDB; 5345349at2759; -.
DR Proteomes; UP000261540; Unplaced.
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:0048856; P:anatomical structure development; IEA:UniProt.
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; 6.
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; 2.
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; 4.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..953
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017336891"
FT DOMAIN 319..357
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 494..529
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 553..588
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 612..649
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 690..725
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 729..943
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 484..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..670
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 103203 MW; C830CBAAB116F991 CRC64;
MSAILMQRFP VLLSVSASLL IYTCAMSDPQ VIDLLTLSDA KQSAVAVERL ASALDTVSDI
YIVSTFRLPP KLGGVLLGLY GKQDNRKYLE LAVMGKINKV LVRYTREDGK LHTVNLQGTN
LADGRSHSAI LHIGGLRRDN LQLQLYVNCR LADSSHGHPL PVPLPPNGEA VDIRNGHKAY
ARLQGSVESL KMALGGSLAK AGILMDCPFQ GDSSQHISGG SELNSILGDH TKALIGQLII
FNQILGELRQ DIREQVKEMS LIRNTILECQ VCGFHEPHSR CLPSPCYQGV SCMETLDYPG
YRCGPCPEGM MGNGTHCQDA DECSLVQPCF SAAACVNSAP GFSCQPCPPG FTGPPVTGVG
LEFAKIHKQE CSDVDECVNG SGACVPNSIC INTVGSYKCG PCKAGFAGNQ LTGCFPQRSC
STLGYDPCDV NAHCLIERSG EVSCVCNVGW AGNGNTCGPD TDLDGYPDES LPCIDNDKHC
KPDNCPQTPN SGQEDTDSDG VGDQCDEDAD GDGIKNVEDN CRLTPNKDQQ NSDTDSFGDA
CDNCPNVANG DQKDTDGNGE GDMCDNDIDG DGIPNVLDNC PRVPNPMQTD RDSDGVGDAC
DSCPEASNPT QTDIDNDLVG DVCDTNLDYD GDGLQNSRDN CPEVPNSSQL DSDNDGIGDE
CDEDDDNDGI PDYGGPGPDN CRLIPNPNQK DSDGDGVGDV CEEDFDNDMV LDVVDVCPES
AEVTVTDFRS YQTVILDPEG DAQIDPSWVV LNQGMEIVQT MNSDPGLAVG YTAFNGVDFE
GTFHINTVTD DDYVGFIFGY QDSSSFYVVM WKQTEQAYWQ LLPFRAMAEP GLQLKAVKSR
TGPGEFLRNA LWHTGNTNGE VKLLWKDPRN VGWRDKTSYR WQLNHRPQVG YIRVQLYEGM
AVVADSGMVI DTTMRGGRLG VFCFSQENII WSNLRYRCND TVPDSFSLYR TQA
//
