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SHOC2_CHICK
ID   SHOC2_CHICK             Reviewed;         529 AA.
AC   Q5F4C4;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=RCJMB04_1b13;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ851376; CAH65010.1; -; mRNA.
DR   RefSeq; NP_001026407.1; NM_001031236.1.
DR   AlphaFoldDB; Q5F4C4; -.
DR   SMR; Q5F4C4; -.
DR   STRING; 9031.ENSGALP00000014251; -.
DR   PaxDb; Q5F4C4; -.
DR   GeneID; 423894; -.
DR   KEGG; gga:423894; -.
DR   CTD; 8036; -.
DR   VEuPathDB; HostDB:geneid_423894; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; Q5F4C4; -.
DR   PhylomeDB; Q5F4C4; -.
DR   PRO; PR:Q5F4C4; -.
DR   Proteomes; UP000000539; Unplaced.
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; 4.
DR   SMART; SM00369; LRR_TYP; 15.
DR   PROSITE; PS51450; LRR; 17.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Leucine-rich repeat; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..529
FT                   /note="Leucine-rich repeat protein SHOC-2"
FT                   /id="PRO_0000385627"
FT   REPEAT          99..122
FT                   /note="LRR 1"
FT   REPEAT          123..145
FT                   /note="LRR 2"
FT   REPEAT          146..168
FT                   /note="LRR 3"
FT   REPEAT          169..191
FT                   /note="LRR 4"
FT   REPEAT          193..214
FT                   /note="LRR 5"
FT   REPEAT          215..237
FT                   /note="LRR 6"
FT   REPEAT          239..260
FT                   /note="LRR 7"
FT   REPEAT          262..283
FT                   /note="LRR 8"
FT   REPEAT          284..306
FT                   /note="LRR 9"
FT   REPEAT          307..329
FT                   /note="LRR 10"
FT   REPEAT          331..353
FT                   /note="LRR 11"
FT   REPEAT          354..377
FT                   /note="LRR 12"
FT   REPEAT          379..400
FT                   /note="LRR 13"
FT   REPEAT          401..424
FT                   /note="LRR 14"
FT   REPEAT          425..447
FT                   /note="LRR 15"
FT   REPEAT          448..471
FT                   /note="LRR 16"
FT   REPEAT          473..493
FT                   /note="LRR 17"
FT   REPEAT          494..516
FT                   /note="LRR 18"
FT   REGION          1..87
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"
FT   COMPBIAS        57..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  59162 MW;  7D7090387ABBA363 CRC64;
     MSSNLGKEKD CKEKDPKVPS SKEREKESKA SGGFGKESKE KEPKTKGKDA KDGKKDSSST
     QPGVAFSVDN TIKRPNPATG TRKKSSNAEV IKELNKCREE NSMRLDLAKR SIHMLPSAVK
     ELTQLTELYL YSNKLQSLPA EVGCLVNLVT LALSENSLTS LPDSLDNLKK LRMLDLRHNK
     LREIPSVVYR LTSLATLYLR FNRITTVEKD IKTLSKLTML SIRENKIKQL PAEIGELCNL
     ITLDVAHNQL EHLPEEIGSC TQITNLDLQH NELLDLPETI GNLSSLSRLG LRYNRLSAIP
     KSLAKCSELD ELNLENNNIS TLPEGLLSSL VKLTSLTLAR NCFQSYPVGG PSQFSTIYSL
     NMEHNRINKI PFGIFSRAKV LSKLNMKDNQ LTSLPLDFGT WTSMVELNLA TNQLTKIPED
     VSGLVSLEVL ILSNNLLKKL PHGIGNLRKL RELDLEENKL ESLPNEIAYL KDLQKLVLTN
     NQLTTLPRGI GHLTNLTHLG LGENLLTHLP EEIGKILFFF FFNVSFLFV
 
 
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