SHOC2_XENLA
ID SHOC2_XENLA Reviewed; 577 AA.
AC Q8AVI4;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Leucine-rich repeat protein SHOC-2;
DE AltName: Full=Protein soc-2 homolog;
DE AltName: Full=Protein sur-8 homolog;
GN Name=shoc2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory subunit of protein phosphatase 1 (PP1c) that acts
CC as a M-Ras/MRAS effector and participates in MAPK pathway activation.
CC Upon M-Ras/MRAS activation, targets PP1c to specifically
CC dephosphorylate the 'Ser-259' inhibitory site of raf1 kinase and
CC stimulate raf1 activity at specialized signaling complexes (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SHOC2 family. {ECO:0000305}.
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DR EMBL; BC042263; AAH42263.1; -; mRNA.
DR RefSeq; NP_001080350.1; NM_001086881.1.
DR AlphaFoldDB; Q8AVI4; -.
DR SMR; Q8AVI4; -.
DR IntAct; Q8AVI4; 1.
DR DNASU; 380042; -.
DR GeneID; 380042; -.
DR KEGG; xla:380042; -.
DR CTD; 380042; -.
DR Xenbase; XB-GENE-493506; shoc2.S.
DR OrthoDB; 287114at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 380042; Expressed in internal ear and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISS:UniProtKB.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027036; SHOC2.
DR PANTHER; PTHR48051:SF9; PTHR48051:SF9; 1.
DR Pfam; PF13855; LRR_8; 5.
DR SMART; SM00369; LRR_TYP; 16.
DR PROSITE; PS51450; LRR; 17.
PE 2: Evidence at transcript level;
KW Cytoplasm; Leucine-rich repeat; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..577
FT /note="Leucine-rich repeat protein SHOC-2"
FT /id="PRO_0000385629"
FT REPEAT 96..118
FT /note="LRR 1"
FT REPEAT 119..140
FT /note="LRR 2"
FT REPEAT 142..164
FT /note="LRR 3"
FT REPEAT 165..186
FT /note="LRR 4"
FT REPEAT 188..209
FT /note="LRR 5"
FT REPEAT 211..232
FT /note="LRR 6"
FT REPEAT 234..255
FT /note="LRR 7"
FT REPEAT 257..278
FT /note="LRR 8"
FT REPEAT 280..302
FT /note="LRR 9"
FT REPEAT 303..324
FT /note="LRR 10"
FT REPEAT 327..348
FT /note="LRR 11"
FT REPEAT 351..372
FT /note="LRR 12"
FT REPEAT 375..395
FT /note="LRR 13"
FT REPEAT 398..419
FT /note="LRR 14"
FT REPEAT 421..443
FT /note="LRR 15"
FT REPEAT 444..465
FT /note="LRR 16"
FT REPEAT 467..489
FT /note="LRR 17"
FT REPEAT 490..511
FT /note="LRR 18"
FT REPEAT 513..535
FT /note="LRR 19"
FT REPEAT 537..558
FT /note="LRR 20"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 64100 MW; D5E04AFF5EF60BF2 CRC64;
MSSSAGKDKE PKVSSGTKER EKEAKAVGPV KESKDKDLKS KVKDAKEGKR DPVGAQAGVA
FSLDNTIKRA NPASGMRKKA SNAEVIKELS KCREENSTRL DLAKKSIHML PVSIKDLTQI
TELYLYGNKL QSLPAEVGNL VNLVKLALSE NSLTSLPDSL DNLKKLCMLD LRHNKLREIP
PVVYRLSSLT TLFLRFNRIT AVEKDLKMLP KLTMLSIREN KIKHLPAEIG ELCNLITLDV
AHNQLEHLPK EIGNCTQITN LDLQHNELLD LPDTIGNLSS LSRLGLRYNR LSAVPRSLSK
CSELDELNLE NNNISTLPEG LLSSLVKVNS LTLARNCFQS YPVGGPSQFS SIYSLNMEHN
RINKIPFGIF SRAKVLSKLN MKDNQLTSLP LDFGTWTSMV ELNLATNQLT KIPEDVSGLV
SIEVLILSNN LLKKLPHGIG NLRKLRELDL EENKLESLPN EIAYLKDLQK LVLTNNQLTT
LPRGIGHLTN LTHLGLGENL LTHLPEEIGT LENLEELYLN DNPNLHSLPF ELALCSKLSI
MSIENCPLSH LPPQIVAGGP SFIIQFLKMQ GPYRAMV