ID   SPY1_CEREL              Reviewed;         319 AA.
AC   Q1L0X2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Protein sprouty homolog 1;
DE            Short=Spry-1;
GN   Name=SPRY1;
OS   Cervus elaphus (Red deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Cervus.
OX   NCBI_TaxID=9860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17146666; DOI=10.1007/s00438-006-0190-0;
RA   Gyurjan I. Jr., Molnar A., Borsy A., Steger V., Hackler L. Jr.,
RA   Zomborszky Z., Papp P., Duda E., Deak F., Lakatos P., Puskas L.G.,
RA   Orosz L.;
RT   "Gene expression dynamics in deer antler: mesenchymal differentiation
RT   toward chondrogenesis.";
RL   Mol. Genet. Genomics 277:221-235(2007).
CC   -!- FUNCTION: Inhibits fibroblast growth factor (FGF)-induced retinal lens
CC       fiber differentiation, probably by inhibiting FGF-mediated
CC       phosphorylation of ERK1/2 (By similarity). Inhibits TGFB-induced
CC       epithelial-to-mesenchymal transition in lens epithelial cells (By
CC       similarity). {ECO:0000250|UniProtKB:Q9QXV9}.
CC   -!- SUBUNIT: Forms heterodimers with SPRY2 (By similarity). Interacts with
CC       TESK1 (By similarity). Interacts with CAV1 (via C-terminus) (By
CC       similarity). {ECO:0000250|UniProtKB:Q9QXV9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=Found in the cytoplasm
CC       in unstimulated cells but is translocated to the membrane ruffles in
CC       cells stimulated with EGF (epidermal growth factor). {ECO:0000250}.
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; DQ239787; ABF29589.1; -; mRNA.
DR   AlphaFoldDB; Q1L0X2; -.
DR   SMR; Q1L0X2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro.
DR   GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:1902747; P:negative regulation of lens fiber cell differentiation; ISS:UniProtKB.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001759; P:organ induction; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Developmental protein; Membrane.
FT   CHAIN           1..319
FT                   /note="Protein sprouty homolog 1"
FT                   /id="PRO_0000295298"
FT   DOMAIN          183..295
FT                   /note="SPR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00572"
FT   REGION          54..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..137
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   319 AA;  34952 MW;  D463705F97A58218 CRC64;
     MDPQNQHGSG SSLVVIQQPA LDNRQRLDYE REIQPAAILS LDQIKAIRGS NEYTEGPSVV
     KRPAPRTAPR QEKHERTHEI IPINVNNNYE HRPTSHLGHT GLSNNTRGPI LSRSTSTGSA
     ASSGSNSSAS SEQGLLGRSP PTRPIPGHRS ERAIRTQPKQ LIVDDLKGSL KEDLTQHKFI
     CEQCGKCKCG ECTAPRTLPS CLACNRQCLC SAESMVEYGT CMCLVKGIFY HCSNDDEGDS
     YSDNPCSCSQ SQCCSRYLCM GAMSLFLPCL LCYPPAKGCL KLCKGCYDWI HRPGCRCENS
     NTVYCKLESC SSRGLGKPS