SHOC2_DANRE
ID SHOC2_DANRE Reviewed; 561 AA.
AC Q1L8Y7; A0JMD9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
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; ORFNames=si:ch211-159c12.3, si:ch211-197i12.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2007) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1L8Y7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1L8Y7-2; Sequence=VSP_038197;
CC -!- SIMILARITY: Belongs to the SHOC2 family. {ECO:0000305}.
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DR EMBL; AL772158; CAK04058.1; -; Genomic_DNA.
DR EMBL; CR450802; CAK04354.1; -; Genomic_DNA.
DR EMBL; BC125839; AAI25840.1; -; mRNA.
DR EMBL; BC155579; AAI55580.1; -; mRNA.
DR RefSeq; NP_001038251.1; NM_001044786.1. [Q1L8Y7-1]
DR RefSeq; XP_005161853.1; XM_005161796.3. [Q1L8Y7-1]
DR AlphaFoldDB; Q1L8Y7; -.
DR SMR; Q1L8Y7; -.
DR STRING; 7955.ENSDARP00000110805; -.
DR PaxDb; Q1L8Y7; -.
DR Ensembl; ENSDART00000059882; ENSDARP00000059881; ENSDARG00000040853. [Q1L8Y7-1]
DR Ensembl; ENSDART00000184718; ENSDARP00000150764; ENSDARG00000116564. [Q1L8Y7-1]
DR Ensembl; ENSDART00000191544; ENSDARP00000156603; ENSDARG00000112058. [Q1L8Y7-1]
DR GeneID; 555476; -.
DR KEGG; dre:555476; -.
DR CTD; 8036; -.
DR ZFIN; ZDB-GENE-050208-523; shoc2.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000156270; -.
DR HOGENOM; CLU_000288_18_23_1; -.
DR InParanoid; Q1L8Y7; -.
DR OMA; NQFTSYP; -.
DR OrthoDB; 287114at2759; -.
DR PhylomeDB; Q1L8Y7; -.
DR TreeFam; TF315742; -.
DR Reactome; R-DRE-5673000; RAF activation.
DR PRO; PR:Q1L8Y7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 22.
DR Bgee; ENSDARG00000040853; Expressed in mature ovarian follicle and 20 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:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
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; 3.
DR SMART; SM00369; LRR_TYP; 15.
DR PROSITE; PS51450; LRR; 18.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Leucine-rich repeat; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..561
FT /note="Leucine-rich repeat protein SHOC-2"
FT /id="PRO_0000385628"
FT REPEAT 80..101
FT /note="LRR 1"
FT REPEAT 103..124
FT /note="LRR 2"
FT REPEAT 126..148
FT /note="LRR 3"
FT REPEAT 149..170
FT /note="LRR 4"
FT REPEAT 172..193
FT /note="LRR 5"
FT REPEAT 195..216
FT /note="LRR 6"
FT REPEAT 218..239
FT /note="LRR 7"
FT REPEAT 241..262
FT /note="LRR 8"
FT REPEAT 264..286
FT /note="LRR 9"
FT REPEAT 287..308
FT /note="LRR 10"
FT REPEAT 311..332
FT /note="LRR 11"
FT REPEAT 335..356
FT /note="LRR 12"
FT REPEAT 359..379
FT /note="LRR 13"
FT REPEAT 382..403
FT /note="LRR 14"
FT REPEAT 405..427
FT /note="LRR 15"
FT REPEAT 428..449
FT /note="LRR 16"
FT REPEAT 451..473
FT /note="LRR 17"
FT REPEAT 474..495
FT /note="LRR 18"
FT REPEAT 497..519
FT /note="LRR 19"
FT REPEAT 521..542
FT /note="LRR 20"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 261..561
FT /note="NLASINRLGLRYNRLSAIPRSLAKCRELEELNLENNNISVLPEGLLSSLVNL
FT TSLTLARNCFQSYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLT
FT SLPLDFGTWTSMVELNLATNQLTKIPEDICGLVSLEMLTLSNNLLKKLPYGIGNLRKLR
FT ELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTYLGLGENLLQHLP
FT EEIGTLENLEDLYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQIVAGGPSFII
FT QFLKMQGPYRAMV -> EDELKKTSLGLLPVFLF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_038197"
SQ SEQUENCE 561 AA; 62696 MW; E805D3A5EC4516F1 CRC64;
MSSTLGKDKD SKEREPKAEG KSKTKGKDAK DGKKDTSGAS PAVAFTLDST IKRPNPPPST
RKKSSNAEVI KELNKCREEN SMRLDLSKRS IHLLPSSIKE LTQLTELYLY SNKLQSLPPE
VGCLSGLVTL ALSENSLTSL PDSLDNLKKL RMLDLRHNKL REIPAVVYRV SSLTTLYLRF
NRITTVEKDI KNLSKLTMLS IRENKIKQLP AEIGELCNLI TLDVAHNQLE HLPKEIGNCT
QITNLDLQHN DLLDLPETIG NLASINRLGL RYNRLSAIPR SLAKCRELEE LNLENNNISV
LPEGLLSSLV NLTSLTLARN CFQSYPVGGP SQFSTIYSLN MEHNRINKIP FGIFSRAKVL
SKLNMKDNQL TSLPLDFGTW TSMVELNLAT NQLTKIPEDI CGLVSLEMLT LSNNLLKKLP
YGIGNLRKLR ELDLEENKLE SLPNEIAYLK DLQKLVLTNN QLTTLPRGIG HLTNLTYLGL
GENLLQHLPE EIGTLENLED LYLNDNPNLH SLPFELALCS KLSIMSIENC PLSHLPPQIV
AGGPSFIIQF LKMQGPYRAM V