SHOC2_RAT
ID SHOC2_RAT Reviewed; 582 AA.
AC Q6AYI5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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.
CC {ECO:0000250|UniProtKB:Q9UQ13}.
CC -!- SUBUNIT: Interacts with M-Ras/MRAS, and RAF1. Forms a multiprotein
CC complex with Ras (M-Ras/MRAS), Raf (RAF1) and protein phosphatase 1
CC (PPP1CA, PPP1CB and PPP1CC). Interacts with ERBIN; disrupts the
CC interaction with RAF1 and Ras, leading to prevent activation of the Ras
CC signaling pathway. Specifically binds K-Ras/KRAS, M-Ras/MRAS and N-
CC Ras/NRAS but not H-Ras/HRAS. Interacts with LZTR1.
CC {ECO:0000250|UniProtKB:Q9UQ13}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UQ13}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UQ13}. Note=Translocates from cytoplasm to
CC nucleus upon growth factor stimulation. {ECO:0000250|UniProtKB:Q9UQ13}.
CC -!- SIMILARITY: Belongs to the SHOC2 family. {ECO:0000305}.
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DR EMBL; BC079032; AAH79032.1; -; mRNA.
DR RefSeq; NP_001013173.1; NM_001013155.1.
DR AlphaFoldDB; Q6AYI5; -.
DR SMR; Q6AYI5; -.
DR BioGRID; 259419; 1.
DR STRING; 10116.ENSRNOP00000020580; -.
DR PhosphoSitePlus; Q6AYI5; -.
DR jPOST; Q6AYI5; -.
DR PaxDb; Q6AYI5; -.
DR PRIDE; Q6AYI5; -.
DR Ensembl; ENSRNOT00000020580; ENSRNOP00000020580; ENSRNOG00000015339.
DR GeneID; 309548; -.
DR KEGG; rno:309548; -.
DR UCSC; RGD:1308146; rat.
DR CTD; 8036; -.
DR RGD; 1308146; Shoc2.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000156270; -.
DR HOGENOM; CLU_000288_18_23_1; -.
DR InParanoid; Q6AYI5; -.
DR OMA; NQFTSYP; -.
DR OrthoDB; 287114at2759; -.
DR PhylomeDB; Q6AYI5; -.
DR Reactome; R-RNO-5673000; RAF activation.
DR PRO; PR:Q6AYI5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015339; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q6AYI5; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; ISS:UniProtKB.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:RGD.
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 GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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..582
FT /note="Leucine-rich repeat protein SHOC-2"
FT /id="PRO_0000317422"
FT REPEAT 101..122
FT /note="LRR 1"
FT REPEAT 124..145
FT /note="LRR 2"
FT REPEAT 147..169
FT /note="LRR 3"
FT REPEAT 170..191
FT /note="LRR 4"
FT REPEAT 193..215
FT /note="LRR 5"
FT REPEAT 216..237
FT /note="LRR 6"
FT REPEAT 239..260
FT /note="LRR 7"
FT REPEAT 262..283
FT /note="LRR 8"
FT REPEAT 285..307
FT /note="LRR 9"
FT REPEAT 308..329
FT /note="LRR 10"
FT REPEAT 332..353
FT /note="LRR 11"
FT REPEAT 356..377
FT /note="LRR 12"
FT REPEAT 380..400
FT /note="LRR 13"
FT REPEAT 403..424
FT /note="LRR 14"
FT REPEAT 426..448
FT /note="LRR 15"
FT REPEAT 449..470
FT /note="LRR 16"
FT REPEAT 472..494
FT /note="LRR 17"
FT REPEAT 495..516
FT /note="LRR 18"
FT REPEAT 518..540
FT /note="LRR 19"
FT REPEAT 542..563
FT /note="LRR 20"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 64921 MW; 27DFF097AD9FA37B CRC64;
MSSSLGKEKD SKEKDPKVPS AKEREKEAKA SGGFGKESKE KEPKTKGKDA KDGKKESSAA
QPGVAFSVDN TIKRPNPALG TRKKSSNAEV TKELNKCREE NSMRLDLSKR SIHILPPSVK
ELTQLTELYL YSNKLQSLPA EVGCLVNLMT LALSENSLTS LPDSLDNLKK LRMLDLRHNK
LREIPSVVYR LDSLTTLYLR FNRITAVEKD VRNLPRLSTL SIRENKIKQL PAEIGELCNL
ITLDVAHNQL EHLPKEIGNC TQITNLDLQH NELLDLPDTI GNLSSLNRLG LRYNRLSAIP
RSLAKCSALE ELNLENNNIS TLPESLLSSL VKLNSLTLAR NCFQLYPVGG PSQFSTIYSL
NMEHNRINKI PFGIFSRAKV LSKLNMKDNQ LTSLPLDFGT WTSMVELNLA TNQLTKIPED
VSGLVSLEVL ILSNNLLKKL PHGLGNLRKL RELDLEENKL ESLPNEIAYL KDLQKLVLTN
NQLTTLPRGI GHLTNLTHLG LGENLLTHLP EEIGTLENLE ELYLNDNPNL HSLPFELALC
SKLSIMSIEN CPLSHLPPQI VAGGPSFIIQ FLKMQGPYRA MV
