SPRE1_XENTR
ID SPRE1_XENTR Reviewed; 406 AA.
AC Q66JG9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Sprouty-related, EVH1 domain-containing protein 1;
DE Short=Spred-1;
GN Name=spred1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sivak J.M., Petersen L.F., Amaya E.;
RT "Sprouty and Spred proteins diverge functionally to coordinate FGF signal
RT interpretation during mesoderm formation.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 8-123.
RX PubMed=15710406; DOI=10.1016/j.febslet.2004.11.114;
RA Harmer N.J., Sivak J.M., Amaya E., Blundell T.L.;
RT "1.15 A crystal structure of the X. tropicalis Spred1 EVH1 domain suggests
RT a fourth distinct peptide-binding mechanism within the EVH1 family.";
RL FEBS Lett. 579:1161-1166(2005).
CC -!- FUNCTION: Tyrosine kinase substrate that inhibits growth-factor-
CC mediated activation of MAP kinase. {ECO:0000250|UniProtKB:Q924S8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q924S8};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q924S8}.
CC -!- PTM: Palmitoylated by ZDHHC17/HIP14. {ECO:0000250|UniProtKB:Q924S8}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q7Z699}.
CC -!- PTM: Phosphorylated on tyrosine. {ECO:0000250|UniProtKB:Q924S8}.
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 EMBL; AY714338; AAU43767.1; -; mRNA.
DR EMBL; BC080919; AAH80919.1; -; mRNA.
DR RefSeq; NP_001008037.1; NM_001008036.1.
DR PDB; 1TJ6; X-ray; 1.65 A; A/B=8-123.
DR PDB; 1XOD; X-ray; 1.15 A; A/B=8-123.
DR PDBsum; 1TJ6; -.
DR PDBsum; 1XOD; -.
DR AlphaFoldDB; Q66JG9; -.
DR SMR; Q66JG9; -.
DR PRIDE; Q66JG9; -.
DR DNASU; 493399; -.
DR Ensembl; ENSXETT00000039156; ENSXETP00000039156; ENSXETG00000018057.
DR GeneID; 493399; -.
DR KEGG; xtr:493399; -.
DR CTD; 161742; -.
DR Xenbase; XB-GENE-482851; spred1.
DR InParanoid; Q66JG9; -.
DR OrthoDB; 759156at2759; -.
DR Reactome; R-XTR-5658442; Regulation of RAS by GAPs.
DR Reactome; R-XTR-5658623; FGFRL1 modulation of FGFR1 signaling.
DR EvolutionaryTrace; Q66JG9; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000018057; Expressed in brain and 10 other tissues.
DR ExpressionAtlas; Q66JG9; baseline.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR CDD; cd10574; EVH1_SPRED-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR023337; KBD.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041937; SPRE_EVH1.
DR InterPro; IPR007875; Sprouty.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR Pfam; PF05210; Sprouty; 1.
DR Pfam; PF00568; WH1; 1.
DR SMART; SM00461; WH1; 1.
DR PROSITE; PS51488; KBD; 1.
DR PROSITE; PS51227; SPR; 1.
DR PROSITE; PS50229; WH1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..406
FT /note="Sprouty-related, EVH1 domain-containing protein 1"
FT /id="PRO_0000076909"
FT DOMAIN 3..120
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT DOMAIN 195..247
FT /note="KBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00821"
FT DOMAIN 296..404
FT /note="SPR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00572"
FT REGION 124..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:1XOD"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1XOD"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1XOD"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1XOD"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1XOD"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1XOD"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1XOD"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1XOD"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1XOD"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1XOD"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:1XOD"
FT HELIX 103..120
FT /evidence="ECO:0007829|PDB:1XOD"
SQ SEQUENCE 406 AA; 45905 MW; 417041C1CFF32CC5 CRC64;
MSGEQEPDDS YARVRAVVMT RDDSSGGWLQ LGGGGLSSVT VSKTLQPGDS GGTEFLVHGE
RLRDKTVVLE CVLRRDLVYN KVTPTFHHWR IGDKKFGLTF QSPADARAFD RGIRRAIEDL
SQGLPASCHG ESETSEDGPQ VNKEDHYSTH NNDHFFRSDS IPTEELYRTS VIRPSPFENL
NPRRAYIHNQ VPLKPIRHVS FQDEDEIVRI NPRDMIIRRY ADYRHPDIFR NDVDREEPED
VTFFTKTDSK KPSYLYSPAN GRDSLKEQKP VEVCKIQPTS SLKKSKGKKE DGEHSSCVYC
QERFNHEENG RGKCQDAPDP IQRCIYQVSC MLCAESMLYH CMSDSEGDYS DPCSCDASDE
NLCLRWLALI TLSFIAPCMC CYLPLRACHH CGEMCGCCGG KHKAAG
