SPY4_BOVIN
ID SPY4_BOVIN Reviewed; 299 AA.
AC A2VDU1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein sprouty homolog 4;
DE Short=Spry-4;
GN Name=SPRY4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Suppresses the insulin receptor and EGFR-transduced MAPK
CC signaling pathway, but does not inhibit MAPK activation by a
CC constitutively active mutant Ras. Probably impairs the formation of
CC GTP-Ras (By similarity). Inhibits Ras-independent, but not Ras-
CC dependent, activation of RAF1 (By similarity). Represses integrin-
CC mediated cell spreading via inhibition of TESK1-mediated
CC phosphorylation of cofilin (By similarity).
CC {ECO:0000250|UniProtKB:Q9C004}.
CC -!- SUBUNIT: Interacts (via C-terminus) with TESK1 (via both C- and N-
CC termini); the interaction inhibits TESK1 kinase activity (By
CC similarity). Interacts with RAF1 (By similarity). Interacts with CAV1
CC (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:Q9C004,
CC ECO:0000250|UniProtKB:Q9WTP2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C004}. Cell
CC projection, ruffle membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Found in the
CC cytoplasm in unstimulated cells but is translocated to the membrane
CC ruffles in cells stimulated with EGF (epidermal growth factor) (By
CC similarity). Colocalizes with TESK1 in vesicular spots in the cytoplasm
CC (By similarity). {ECO:0000250|UniProtKB:Q9C004,
CC ECO:0000250|UniProtKB:Q9WTP2}.
CC -!- DOMAIN: The Cys-rich domain is responsible for the localization of the
CC protein to the membrane ruffles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sprouty family. {ECO:0000305}.
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DR EMBL; BC133401; AAI33402.1; -; mRNA.
DR RefSeq; NP_001074981.1; NM_001081512.1.
DR RefSeq; XP_005209581.1; XM_005209524.3.
DR RefSeq; XP_005209583.1; XM_005209526.3.
DR RefSeq; XP_005209584.1; XM_005209527.3.
DR RefSeq; XP_015327768.1; XM_015472282.1.
DR AlphaFoldDB; A2VDU1; -.
DR STRING; 9913.ENSBTAP00000010852; -.
DR PaxDb; A2VDU1; -.
DR Ensembl; ENSBTAT00000010852; ENSBTAP00000010852; ENSBTAG00000008250.
DR GeneID; 504593; -.
DR KEGG; bta:504593; -.
DR CTD; 81848; -.
DR VEuPathDB; HostDB:ENSBTAG00000008250; -.
DR VGNC; VGNC:35244; SPRY4.
DR eggNOG; ENOG502QQ4V; Eukaryota.
DR GeneTree; ENSGT00950000183055; -.
DR HOGENOM; CLU_077696_0_0_1; -.
DR InParanoid; A2VDU1; -.
DR OMA; MCLVQGV; -.
DR OrthoDB; 1157681at2759; -.
DR TreeFam; TF325070; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000008250; Expressed in adenohypophysis and 100 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:InterPro.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IBA:GO_Central.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR InterPro; IPR007875; Sprouty.
DR InterPro; IPR030790; SPRY4.
DR PANTHER; PTHR12365:SF6; PTHR12365:SF6; 1.
DR Pfam; PF05210; Sprouty; 1.
DR PROSITE; PS51227; SPR; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cell projection; Cytoplasm;
KW Developmental protein; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..299
FT /note="Protein sprouty homolog 4"
FT /id="PRO_0000295303"
FT DOMAIN 166..273
FT /note="SPR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00572"
FT REGION 50..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9C004"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C004"
SQ SEQUENCE 299 AA; 32376 MW; B522BD140F373E03 CRC64;
MEPPIPQSVP LTPSSVMVQP LLDSRTAHSR LQHPLTILPI DQMKTSHVEN DYIDNPGLAP
PSGPKRTRGG APELAPTPAR CDQDVTHHWI SFSGRPSSVS SSSSTSSDQR LLDHMAPPPV
ADQASPRAVR IQPKAIHCKP LDLKGPAGPP ELDKHFLLCE ACGKCKCKEC ASPRTLPSCW
VCNQECLCSA QTLVNYGTCM CLVQGIFYHC TNEDDEGSCA DHPCSCSRSN CCARWSFMGA
LSLVLPCLLC YLPATGCVKL AQRGYDRLRR PGCRCKHTNS VICKAAAGDA KASRPDKPF
