SPRE2_PONAB
ID SPRE2_PONAB Reviewed; 418 AA.
AC Q5RDN2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Sprouty-related, EVH1 domain-containing protein 2;
DE Short=Spred-2;
GN Name=SPRED2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Negatively regulates Ras signaling pathways and downstream
CC activation of MAP kinases (By similarity). Inhibits fibroblast growth
CC factor (FGF)-induced retinal lens fiber differentiation, probably by
CC inhibiting FGF-mediated phosphorylation of ERK1/2 (By similarity).
CC Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens
CC epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q7Z698,
CC ECO:0000250|UniProtKB:Q924S7}.
CC -!- SUBUNIT: Homodimer and heterodimer (By similarity). Able to interact
CC with SPRED1 to form heterodimers (By similarity). Interacts with RAS
CC (By similarity). May interact with ZDHHC13 (via ANK repeats) and
CC ZDHHC17 (via ANK repeats) (By similarity).
CC {ECO:0000250|UniProtKB:Q924S7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q924S7};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q924S7}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q924S7}. Cytoplasmic vesicle, secretory
CC vesicle membrane {ECO:0000250|UniProtKB:Q7Z698}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q7Z698}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q7Z698}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q7Z698}. Note=Detected in the cytoplasm of the
CC stratum spinosum cells, where it is associated with cytoplasmic
CC vesicles that are supposed to be secretory granules.
CC {ECO:0000250|UniProtKB:Q7Z698}.
CC -!- PTM: Phosphorylated on serine and threonine residues. Phosphorylated on
CC tyrosine. Phosphorylation of Tyr-228 and Tyr-231 are required for
CC ubiquitination. {ECO:0000250|UniProtKB:Q7Z698}.
CC -!- PTM: Ubiquitinated; leading to degradation by the proteasome.
CC {ECO:0000250|UniProtKB:Q7Z698}.
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DR EMBL; CR857872; CAH90125.1; -; mRNA.
DR RefSeq; NP_001127241.1; NM_001133769.1.
DR AlphaFoldDB; Q5RDN2; -.
DR BMRB; Q5RDN2; -.
DR SMR; Q5RDN2; -.
DR STRING; 9601.ENSPPYP00000013781; -.
DR GeneID; 100174296; -.
DR KEGG; pon:100174296; -.
DR CTD; 200734; -.
DR eggNOG; KOG4590; Eukaryota.
DR InParanoid; Q5RDN2; -.
DR OrthoDB; 759156at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
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:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Membrane; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..418
FT /note="Sprouty-related, EVH1 domain-containing protein 2"
FT /id="PRO_0000354678"
FT DOMAIN 5..122
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT DOMAIN 201..257
FT /note="KBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00821"
FT DOMAIN 308..416
FT /note="SPR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00572"
FT REGION 127..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z698"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z698"
FT MOD_RES 231
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z698"
SQ SEQUENCE 418 AA; 47572 MW; E235D5B01FDCD38B CRC64;
MTEETHPDDD SYIVRVKAVV MTRDDSSGGW FPQEGGGISR VGVCKVMHPE GNGRSGFLIH
GERQKDKLVV LECYVRKDLV YTKANPTFHH WKVDNRKFGL TFQSPADARA FDRGVRKAIE
DLIEGSTTSS STIHNEAELG DDDVFTTATD SSSNSSQKRE QPTRTVSSPT SCEHRRIYTL
GHLHDSYPTD HYHLDQPMPR PYRQVSFPDD DEEIVRINPR EKIWMTGYED YRHAPVRGKY
PDPSEDVDSS YVRFAKGEVP KHDYNYPYVD SSDFGLGEDP KGRGGSVIKT QPSRGKSRRR
KEDGERSRCV YCRDMFNHEE NRRGHCQDAP DSVRTCIRRV SCMWCADSML YHCMSDPEGD
YTDPCSCDTS DEKFCLRWMA LIALSFLAPC MCCYLPLRAC YHCGVMCRCC GGKHKAAA
