SPY1_MOUSE
ID SPY1_MOUSE Reviewed; 313 AA.
AC Q9QXV9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein sprouty homolog 1;
DE Short=Spry-1;
GN Name=Spry1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=10498682; DOI=10.1242/dev.126.20.4465;
RA Minowada G., Jarvis L.A., Chi C.L., Neubueser A., Sun X., Hacohen N.,
RA Krasnow M.A., Martin G.R.;
RT "Vertebrate sprouty genes are induced by FGF signaling and can cause
RT chondrodysplasia when overexpressed.";
RL Development 126:4465-4475(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBUNIT, AND INTERACTION WITH CAV1 AND SPRY1.
RX PubMed=16877379; DOI=10.1074/jbc.m603921200;
RA Cabrita M.A., Jaeggi F., Widjaja S.P., Christofori G.;
RT "A functional interaction between sprouty proteins and caveolin-1.";
RL J. Biol. Chem. 281:29201-29212(2006).
RN [4]
RP INTERACTION WITH TESK1.
RX PubMed=17974561; DOI=10.1074/jbc.m705457200;
RA Chandramouli S., Yu C.Y., Yusoff P., Lao D.H., Leong H.F., Mizuno K.,
RA Guy G.R.;
RT "Tesk1 interacts with Spry2 to abrogate its inhibition of ERK
RT phosphorylation downstream of receptor tyrosine kinase signaling.";
RL J. Biol. Chem. 283:1679-1691(2008).
RN [5]
RP FUNCTION.
RX PubMed=25576668; DOI=10.1016/j.exer.2015.01.001;
RA Zhao G., Wojciechowski M.C., Jee S., Boros J., McAvoy J.W., Lovicu F.J.;
RT "Negative regulation of TGFbeta-induced lens epithelial to mesenchymal
RT transition (EMT) by RTK antagonists.";
RL Exp. Eye Res. 132:9-16(2015).
RN [6]
RP FUNCTION.
RX PubMed=29501879; DOI=10.1016/j.exer.2018.02.025;
RA Zhao G., Bailey C.G., Feng Y., Rasko J., Lovicu F.J.;
RT "Negative regulation of lens fiber cell differentiation by RTK antagonists
RT Spry and Spred.";
RL Exp. Eye Res. 170:148-159(2018).
CC -!- FUNCTION: Inhibits fibroblast growth factor (FGF)-induced retinal lens
CC fiber differentiation, probably by inhibiting FGF-mediated
CC phosphorylation of ERK1/2 (PubMed:29501879). Inhibits TGFB-induced
CC epithelial-to-mesenchymal transition in lens epithelial cells
CC (PubMed:25576668). {ECO:0000269|PubMed:25576668,
CC ECO:0000269|PubMed:29501879}.
CC -!- SUBUNIT: Forms heterodimers with SPRY2 (PubMed:16877379). Interacts
CC with TESK1 (PubMed:17974561). Interacts with CAV1 (via C-terminus)
CC (PubMed:16877379). {ECO:0000269|PubMed:16877379,
CC ECO:0000269|PubMed:17974561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Note=Found in the cytoplasm in unstimulated cells but is translocated
CC to the membrane ruffles in cells stimulated with EGF (epidermal growth
CC factor).
CC -!- DEVELOPMENTAL STAGE: At 8.5 dpc, expressed in the primitive streak,
CC rostral forebrain, cells lateral to the posterior hindbrain, anterior
CC hindbrain and developing midbrain (PubMed:10498682). At 9.5 dpc,
CC continues to be expressed in the rostral forebrain and primitive
CC streak, and is also detected in the branchial arches and the forelimb
CC bud (PubMed:10498682). At 10.5 dpc, expressed in the somites,
CC frontonasal processes, tailbud, and hindlimb bud (PubMed:10498682).
CC {ECO:0000269|PubMed:10498682}.
CC -!- DOMAIN: The Cys-rich domain is responsible for the localization of the
CC protein to the membrane ruffles.
CC -!- SIMILARITY: Belongs to the sprouty family. {ECO:0000305}.
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; AF176903; AAD56004.1; -; mRNA.
DR EMBL; BC053428; AAH53428.1; -; mRNA.
DR EMBL; BC069914; AAH69914.1; -; mRNA.
DR CCDS; CCDS17322.1; -.
DR RefSeq; NP_001292369.1; NM_001305440.1.
DR RefSeq; NP_001292370.1; NM_001305441.1.
DR RefSeq; NP_001292371.1; NM_001305442.1.
DR RefSeq; NP_036026.1; NM_011896.3.
DR AlphaFoldDB; Q9QXV9; -.
DR SMR; Q9QXV9; -.
DR BioGRID; 204876; 7.
DR STRING; 10090.ENSMUSP00000049292; -.
DR iPTMnet; Q9QXV9; -.
DR PhosphoSitePlus; Q9QXV9; -.
DR MaxQB; Q9QXV9; -.
DR PaxDb; Q9QXV9; -.
DR PRIDE; Q9QXV9; -.
DR ProteomicsDB; 257064; -.
DR Antibodypedia; 26880; 275 antibodies from 31 providers.
DR DNASU; 24063; -.
DR Ensembl; ENSMUST00000038569; ENSMUSP00000049292; ENSMUSG00000037211.
DR Ensembl; ENSMUST00000108107; ENSMUSP00000103742; ENSMUSG00000037211.
DR Ensembl; ENSMUST00000108109; ENSMUSP00000103744; ENSMUSG00000037211.
DR GeneID; 24063; -.
DR KEGG; mmu:24063; -.
DR UCSC; uc008pax.2; mouse.
DR CTD; 10252; -.
DR MGI; MGI:1345139; Spry1.
DR VEuPathDB; HostDB:ENSMUSG00000037211; -.
DR eggNOG; ENOG502QSDN; Eukaryota.
DR GeneTree; ENSGT00950000183055; -.
DR HOGENOM; CLU_077696_0_0_1; -.
DR InParanoid; Q9QXV9; -.
DR OMA; AGHQFIC; -.
DR OrthoDB; 1157681at2759; -.
DR PhylomeDB; Q9QXV9; -.
DR TreeFam; TF325070; -.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR BioGRID-ORCS; 24063; 0 hits in 59 CRISPR screens.
DR PRO; PR:Q9QXV9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9QXV9; protein.
DR Bgee; ENSMUSG00000037211; Expressed in secondary oocyte and 107 other tissues.
DR ExpressionAtlas; Q9QXV9; baseline and differential.
DR Genevisible; Q9QXV9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR GO; GO:0060449; P:bud elongation involved in lung branching; IGI:MGI.
DR GO; GO:0060940; P:epithelial to mesenchymal transition involved in cardiac fibroblast development; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IGI:MGI.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:MGI.
DR GO; GO:0001656; P:metanephros development; IGI:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IDA:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:MGI.
DR GO; GO:1902747; P:negative regulation of lens fiber cell differentiation; IDA:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:MGI.
DR GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; IDA:MGI.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0001759; P:organ induction; IMP:MGI.
DR GO; GO:0001657; P:ureteric bud development; IMP:MGI.
DR InterPro; IPR007875; Sprouty.
DR InterPro; IPR030783; SPRY1.
DR PANTHER; PTHR12365:SF10; PTHR12365:SF10; 1.
DR Pfam; PF05210; Sprouty; 1.
DR PROSITE; PS51227; SPR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Developmental protein; Membrane;
KW Reference proteome.
FT CHAIN 1..313
FT /note="Protein sprouty homolog 1"
FT /id="PRO_0000076899"
FT DOMAIN 177..289
FT /note="SPR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00572"
FT REGION 43..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43609"
SQ SEQUENCE 313 AA; 34004 MW; CD3C27F7022C0B99 CRC64;
MDSPSQHGSH TSLVVIQPPA VEGRQRLDYD RDTQPATILS LDQIKAIRGS NEYTEGPSVA
RRPAPRTAPR PEKQERTHEI IPANVNSSYE HRPASHPGNA RGSVLSRSTS TGSAASSGSS
SSVSSEQGLL GRSPPTRPIP GHRSDRVIRT QPKQLLVEDL KASLKEDPTQ HKFICEQCGK
CKCGECTAPR ALPSCLACDR QCLCSAESMV EYGTCMCLVK GIFYHCSNDD DGGSYSDNPC
SCSQSHCCSR YLCMGALSLC LPCLLCYPPA KGCLKLCRGC YDWTHRPGCR CRNSNTVYCK
LESCPSRAQG KLS
