ID H3BFP1_LATCH Unreviewed; 1170 AA.
AC H3BFP1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Thrombospondin 1 {ECO:0000313|Ensembl:ENSLACP00000020712.2};
GN Name=THBS1 {ECO:0000313|Ensembl:ENSLACP00000020712.2};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000020712.2, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000020712.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AFYH01013691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005988414.1; XM_005988352.2.
DR AlphaFoldDB; H3BFP1; -.
DR STRING; 7897.ENSLACP00000020712; -.
DR Ensembl; ENSLACT00000020852.2; ENSLACP00000020712.2; ENSLACG00000018199.2.
DR GeneID; 102358103; -.
DR KEGG; lcm:102358103; -.
DR CTD; 561901; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000155832; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR InParanoid; H3BFP1; -.
DR OMA; AVPDDKF; -.
DR OrthoDB; 5345349at2759; -.
DR TreeFam; TF324917; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000018199; Expressed in pelvic fin and 5 other cell types or tissues.
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:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 6.20.200.20; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
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; IPR024731; EGF_dom.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF78; THROMBOSPONDIN-1; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF00090; TSP_1; 3.
DR Pfam; PF02412; TSP_3; 6.
DR Pfam; PF05735; TSP_C; 1.
DR Pfam; PF00093; VWC; 1.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00209; TSP1; 3.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50092; TSP1; 3.
DR PROSITE; PS51234; TSP3; 4.
DR PROSITE; PS51236; TSP_CTER; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 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}; Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1170
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003581306"
FT DOMAIN 316..373
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 547..587
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 646..690
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 727..762
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 786..821
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 883..918
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 919..954
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 958..1170
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 724..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 129805 MW; CCD35C32D1B1B5A1 CRC64;
MKLPQGVFLL IMLVGLCGAS RSLESGGDDN GVYDLFEITK ATRKYYGVNL ITGPDPSSPT
YKILNVDRIP PVPESIFLEL LDQIQTERGF LLLATLKQLK GTRGSLLAVE NQDQPGHVFD
ILSNGKAGTL DLTFTVDGKQ HVVSLEEAKL ATAHWKNITL FVQEDRAQLY VGCDKIENVE
LEAPIQKILH PSIASTTRLR LAKGNVKENN FQGSLSNVRF VFGTTLEAIL RNKGCSSFST
ETIKLDNPVN GSSPAIRSNY IGHKIKNVCG FTCDELTEMF KEMKGLQSVI TQLVEDLNNM
RQLNEMTGGR IGISQGTCIY KGNVHRENEE WTVDNCMECS CKNSATFCSK VSCPLVSCAN
ATVPDGECCP RCLPNDSAED SWSPWSEWTP CSVSCGIGTQ QRGRSCDRIN NICLGPSVQT
RTCHIQECDK RFRQDGGWSY WSPWSSCSVT CGIGVKTRIR LCNSPTPQMG GRQCEGEGRE
TQECQKDPCP INGNWGPWSP WNTCTVTCGG GIQKHSRLCD SPMPKYGGKE CVGEATATQI
CNKEDCPIDG CLSNPCFAGT KCTSFPDGSW KCGACPAGYQ GNGVQCEDID ECKEVPDTCF
VFNGVHRCEN TEPGYNCLPC PPRFNGLQPY GRGVEEATGN KQVCKPRNPC TDGTHNCNKH
ARCIYLGHYS DPMFRCECRP GYAGNGIICG EDTDLDGWPN QDLLCVANAT YHCTKDNCPT
LPNSGQEDYD KDGIGDACDK DDDDDGIPDE RDNCPLIFNP QQYDYDRDDV GDRCDNCPYN
HNPDQTDTDA NGEGDACAKD IDGDGIPNER DNCPYVYNVN QKDTDWDGVG DQCDNCPLEN
NPDQTDSDSD RVGDKCDSNQ DIDEDGHQNN LDNCPYIPNA NQADHDKDGK GDACDHDDDN
DGIPDDKDNC RLAFNPDQLD SDGDGRGDAC KDDFDQDNVP DIYDVCPENF EISETDFRRF
QMVPLDPKGT SQIDPNWVVR HQGKELVQTV NCDPGIAVGY DEFNAVDFSG TFFINTERDD
DYAGFVFGYQ SSSRFYVVMW KQITQTYWDT TPTKAQGYSG LSIKVVNSTT GPGEHLRNAL
WHTGHTAGQV RTLWHDPRHT GWKDFTAYRW HLTHRPKTGY IRVVMYEGKK IMADSGAIYD
KTYAGGRLGL FVFSQEMVYF SDLKYECRDT
//
