ID CHERP_MOUSE Reviewed; 936 AA.
AC Q8CGZ0; Q8K291; Q8VCD2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 137.
DE RecName: Full=Calcium homeostasis endoplasmic reticulum protein;
DE AltName: Full=SR-related CTD-associated factor 6;
GN Name=Cherp {ECO:0000312|MGI:MGI:106417};
GN Synonyms=Scaf6 {ECO:0000312|EMBL:AAN77182.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN77182.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sampson N.D., Hewitt J.E.;
RT "Functional characterization of the novel SR-related CTD associated factor,
RT SCAF6.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-723, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824; SER-826 AND THR-828, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-822; SER-824; SER-826 AND
RP THR-828, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in calcium homeostasis, growth and proliferation.
CC {ECO:0000250|UniProtKB:Q8IWX8}.
CC -!- INTERACTION:
CC Q8CGZ0; Q15637: SF1; Xeno; NbExp=3; IntAct=EBI-2366446, EBI-744603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IWX8}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8IWX8}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IWX8}. Note=Distributed
CC throughout the cytoplasm and also localizes to the perinuclear region.
CC Colocalizes with ITPR1 (By similarity). {ECO:0000250|UniProtKB:Q8IWX8}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF536541; AAN77182.1; -; mRNA.
DR EMBL; BC020488; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_613051.3; NM_138585.3.
DR AlphaFoldDB; Q8CGZ0; -.
DR SMR; Q8CGZ0; -.
DR BioGRID; 205695; 4.
DR IntAct; Q8CGZ0; 3.
DR MINT; Q8CGZ0; -.
DR STRING; 10090.ENSMUSP00000148273; -.
DR iPTMnet; Q8CGZ0; -.
DR PhosphoSitePlus; Q8CGZ0; -.
DR EPD; Q8CGZ0; -.
DR jPOST; Q8CGZ0; -.
DR MaxQB; Q8CGZ0; -.
DR PaxDb; 10090-ENSMUSP00000078469; -.
DR ProteomicsDB; 281612; -.
DR Pumba; Q8CGZ0; -.
DR DNASU; 27967; -.
DR GeneID; 27967; -.
DR KEGG; mmu:27967; -.
DR UCSC; uc009mgb.1; mouse.
DR AGR; MGI:106417; -.
DR CTD; 10523; -.
DR MGI; MGI:106417; Cherp.
DR eggNOG; KOG4368; Eukaryota.
DR InParanoid; Q8CGZ0; -.
DR OrthoDB; 1220847at2759; -.
DR PhylomeDB; Q8CGZ0; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 27967; 22 hits in 77 CRISPR screens.
DR ChiTaRS; Cherp; mouse.
DR PRO; PR:Q8CGZ0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CGZ0; Protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 1.10.10.790; Surp module; 1.
DR InterPro; IPR039037; CHERP.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR PANTHER; PTHR12323:SF0; CALCIUM HOMEOSTASIS ENDOPLASMIC RETICULUM PROTEIN; 1.
DR PANTHER; PTHR12323; SR-RELATED CTD ASSOCIATED FACTOR 6; 1.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF01805; Surp; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00648; SWAP; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF109905; Surp module (SWAP domain); 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50128; SURP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..936
FT /note="Calcium homeostasis endoplasmic reticulum protein"
FT /id="PRO_0000299493"
FT REPEAT 15..57
FT /note="SURP motif"
FT /evidence="ECO:0000255"
FT DOMAIN 149..289
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT DOMAIN 850..900
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 77..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..630
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..825
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT MOD_RES 723
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 828
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT MOD_RES 888
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT CROSSLNK 853
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT CROSSLNK 881
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWX8"
FT CONFLICT 348..349
FT /note="Missing (in Ref. 2; BC020488)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 936 AA; 106169 MW; 8C29DF0822CA9EB3 CRC64;
MEMPMPPDDQ ELRNVIDKLA QFVARNGPEF EKMTMEKQKD NPKFSFLFGG EFYSYYKCKL
ALEQQQLICK QQAPELEPTS AMPPLPQPPL APTASLTPAQ GTPSMDELIQ QSQWSLQQQE
QHLLALRQEQ VTTAVAHAVE QQMQKLLEET QLDMSEFDNL LQPIIDTCTK DAISAGKNWM
FSNAKSPPHC ELMAGHLRNR ITADGAHFEL RLHLIYLIND VLHHCQRKQA RELLAALQKV
VVPIYCTSFL AVEEDKQQKI ARLLQLWEKN GYFDDSIIQQ LQSPALGLGQ YQATLINEYS
SVVQPVQLAF QQQIQSLKTQ HEEFVSSLAQ QQQQQQQQQQ QQPQPQPQPQ IQLPQMEADV
KATPPPPAPP PASAPAPTIP PTTQPDDNKP PIQMPGSSEY DTSAGVQDPA AAGPRGPGPH
EQIPPNKPPW FDQPHPVAPW GQQQPPEQPP YPHHQGGPPH CPPWNNSHEG MWGEQRGDPG
WNGQRDAPWN NQPDPNWNNQ FEGPWNNQHE PPPWGGAQRE PPFRMQRPPH FRGPFPPHQQ
HPQFNQPPHP HNFNRFPPRF MQDDFPPRHP FERPPYPHRF DYPQGDFPAD MGPPHHHPGH
RMPHPGINEH PPWAGPQHPD FGPPPHGFNG QPPHMRRQGP PHINHDDPSL VPNVPYFDLP
AGLMAPLVKL EDHEYKPLDP KDIRLPPPMP PSERLLAAVE AFYSPPSHDR PRNSEGWEQN
GLYEFFRAKM RARRRKGQEK RNSGPSRSRS RSKSRGRSSS RSSSRSSKSS RSSSRSHSRS
RSRSSSRSRS RSRSRSRSSR SRSRSRSRSR SKSYSPGRRR RSRSRSPTPP SAAGLGSNSA
PPIPDSRLGE ENKGHQMLVK MGWSGSGGLG AKEQGIQDPI KGGDVRDKWD QYKGVGVALD
DPYENYRRNK SYSFIARMKA RDEFSTFGTR KEEKED
//
