1433E_SHEEP
ID 1433E_SHEEP Reviewed; 255 AA.
AC P62262; P29360; P42655; Q63631;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=14-3-3 protein epsilon;
DE Short=14-3-3E;
DE AltName: Full=Protein kinase C inhibitor protein 1;
DE Short=KCIP-1;
GN Name=YWHAE;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pineal gland;
RX PubMed=8024705; DOI=10.1089/dna.1994.13.629;
RA Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A.,
RA Moffet J.R., Namboodiri M.A., Klein D.C.;
RT "Cloning and characterization of the epsilon and zeta isoforms of the 14-3-
RT 3 proteins.";
RL DNA Cell Biol. 13:629-640(1994).
RN [2]
RP PROTEIN SEQUENCE OF 1-152; 165-184 AND 216-255.
RC TISSUE=Brain;
RX PubMed=1317796; DOI=10.1111/j.1432-1033.1992.tb16946.x;
RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.;
RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) from
RT sheep brain. Amino acid sequence of phosphorylated forms.";
RL Eur. J. Biochem. 206:453-461(1992).
RN [3]
RP PROTEIN SEQUENCE OF 1-23 AND 125-140.
RC TISSUE=Brain;
RX PubMed=2143472; DOI=10.1111/j.1432-1033.1990.tb19138.x;
RA Toker A., Ellis C.A., Sellers L.A., Aitken A.;
RT "Protein kinase C inhibitor proteins. Purification from sheep brain and
RT sequence similarity to lipocortins and 14-3-3 protein.";
RL Eur. J. Biochem. 191:421-429(1990).
RN [4]
RP INTERACTION WITH AANAT.
RX PubMed=11427721; DOI=10.1073/pnas.141118798;
RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-
RT binding switch in melatonin synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner.
CC -!- SUBUNIT: Homodimer. Heterodimerizes with YWHAZ. Interacts with NDEL1,
CC ARHGEF28 and TIAM2. Interacts with ABL1 (phosphorylated form); the
CC interaction retains it in the cytoplasm. Weakly interacts with CDKN1B.
CC Interacts with GAB2. Interacts with phosphorylated GRB10 (By
CC similarity). Interacts with PKA-phosphorylated AANAT (PubMed:11427721).
CC Interacts with the phosphorylated (by AKT1) form of SRPK2. Interacts
CC with KSR1 (By similarity). Interacts with DENND1A (By similarity).
CC Interacts with the phosphorylated (by AKT1) form of SRPK2. Interacts
CC with TIAM2. Interacts with PI4KB, TBC1D22A and TBC1D22B.Interacts with
CC the 'Ser-1134' and 'Ser-1161' phosphorylated form of SOS1 (By
CC similarity). Interacts with ZFP36 (via phosphorylated form) (By
CC similarity). Interacts with SLITRK1 (By similarity). Interacts with
CC RIPOR2 (By similarity). Interacts with KLHL22; required for the nuclear
CC localization of KLHL22 upon amino acid starvation (By similarity).
CC Interacts with CRTC1 (By similarity). Interacts with CRTC2 (probably
CC when phosphorylated at 'Ser-173') (By similarity). Interacts with CRTC3
CC (probably when phosphorylated at 'Ser-138' and/or 'Ser-249') (By
CC similarity). Interacts with ATP2B1 and ATP2B3; this interaction
CC inhibits calcium-transporting ATPase activity (By similarity).
CC Interacts with MEFV (By similarity). {ECO:0000250|UniProtKB:P62258,
CC ECO:0000250|UniProtKB:P62259, ECO:0000269|PubMed:11427721}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; L07914; AAC37321.1; -; mRNA.
DR AlphaFoldDB; P62262; -.
DR SMR; P62262; -.
DR MINT; P62262; -.
DR STRING; 9940.ENSOARP00000013117; -.
DR PRIDE; P62262; -.
DR Ensembl; ENSOART00020017982; ENSOARP00020014847; ENSOARG00020011717.
DR eggNOG; KOG0841; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..255
FT /note="14-3-3 protein epsilon"
FT /id="PRO_0000058621"
FT REGION 234..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 57
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 130
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 50
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62260"
FT MOD_RES 69
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62260"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62260"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT CONFLICT 129
FT /note="H -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64;
MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW
RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF
YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE
EQNKEALQDV EDENQ
