ID A0A3P8ZZI7_ESOLU Unreviewed; 781 AA.
AC A0A3P8ZZI7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Thrombospondin-4 {ECO:0000313|Ensembl:ENSELUP00000033889.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000033889.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000033889.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000033889.2}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3P8ZZI7; -.
DR Ensembl; ENSELUT00000020150.2; ENSELUP00000033889.2; ENSELUG00000012323.2.
DR GeneTree; ENSGT00940000166148; -.
DR OMA; ACGMGGM; -.
DR Proteomes; UP000265140; LG08.
DR Bgee; ENSELUG00000012323; Expressed in embryo and 3 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: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; 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; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199:SF88; CARTILAGE OLIGOMERIC MATRIX PROTEIN; 1.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 5.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
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:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 144..181
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 241..283
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 317..352
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 376..411
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 513..548
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 552..766
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 402..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 85718 MW; E82BDCE9C25AA0F9 CRC64;
TSTHIQVEDP GRGDIHLSLS CHLFGHTYPF TVFCIQGLFC QLTLVILVSV ETYTKLKNGH
ERFPNQQQME PLDVRTVESG TFCQAAFCAD MLCITLSPGM RAPLPPSCHP NPCHPGVECT
GTPEGIRCGP CPEGMVGDGT HCKDVDECAV TPCHMGVRCI NTSPGYRCGP CPAGYTSPQA
QGVGLSYATK NKQVCKDINE CQGSRNGGCV ENSNCINTPG SFRCGPCKAG YVGDQRKGCK
PERACGNGQP NPCHASADCI VQREGKKECQ CAVGWAGNGF FCGSDIDIDG FPDEKLECAE
RNCDKDNCLT VPNSGQEDAD KDGIGDACDE DADGDGILNT QDNCVLVPNV DQRNVDDDNF
GDACDNCRII KNNDQKDTDV DRLGDECDED IDGDGIPNNL DNCKRVPNVD QKDRDGDKVG
DACDSCPYVR NPDQLDMDND LIGDPCDTNK DSDGDGHQDS QDNCPAVINS AQLDTDKDGR
GDECDDDDDD DGIPDLLPPG PDNCRLIPNP LQEDFDSDGV GNVCENDFDN DTVIDSIDVC
PENAEVTLTD FRAYQTVVLD PEGDAQTDPN WVVLNQGREI VQTMNSDPGL AVGYTAFNGV
DFEGTFHVNT VTDDDYAGFI FGYQDSSSFY VVMWKQVEQI YWQANPFRAV AEPGIQLKAV
KSKTGPGEHL RNSLWHTGDT SDQVKLLWKD ARNVGWKDKT SYRWFLQHRP HDGYIRVRFY
EGPQVVADTG IIIDTTMRGG RLGVFCFSQE NIIWANLRYR CNDTIPEDFD SYQARQVQLQ
F
//
