ID   SPY1_BOVIN              Reviewed;         319 AA.
AC   A5D992;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Protein sprouty homolog 1;
DE            Short=Spry-1;
GN   Name=SPRY1;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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; BT030511; ABQ12951.1; -; mRNA.
DR   RefSeq; NP_001092836.1; NM_001099366.1.
DR   AlphaFoldDB; A5D992; -.
DR   SMR; A5D992; -.
DR   STRING; 9913.ENSBTAP00000028307; -.
DR   PaxDb; A5D992; -.
DR   PRIDE; A5D992; -.
DR   GeneID; 507095; -.
DR   KEGG; bta:507095; -.
DR   CTD; 10252; -.
DR   eggNOG; ENOG502QSDN; Eukaryota.
DR   InParanoid; A5D992; -.
DR   OrthoDB; 1157681at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048513; P:animal organ development; IBA:GO_Central.
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:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:1902747; P:negative regulation of lens fiber cell differentiation; ISS:UniProtKB.
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: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;
KW   Reference proteome.
FT   CHAIN           1..319
FT                   /note="Protein sprouty homolog 1"
FT                   /id="PRO_0000295297"
FT   DOMAIN          183..295
FT                   /note="SPR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00572"
FT   REGION          54..157
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;  34959 MW;  ADD0D786FD7D7D99 CRC64;
     MDPQNQHGSG SSLVVIQQPA LDNRQRLDYE REIQPAAILS LDQIKAIRGS NEYTEGPSVV
     KRPAPRTAPR QEKHERTHEI IPINVNNNYE HRPTSHLGHA GLSNNTRGPI LSRSTSTGSA
     ASSGSNSSAS SEQGLLGRSP PTRPIPGHRS ERAIRTQPKQ LIVDDLKGSL KEDLTQHKFI
     CEQCGKCKCG ECTAPRTLPS CLACNRQCLC SAESMVEYGT CMCLVKGIFY HCSNDDEGDS
     YSDNPCSCSQ SQCCSRYLCM GAMSLFLPCL LCYPPAKGCL KLCRGCYDWI HRPGCRCKNS
     NTVYCKLESC PSRGLGKPS