EFHD2_RAT
ID EFHD2_RAT Reviewed; 239 AA.
AC Q4FZY0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=EF-hand domain-containing protein D2;
DE AltName: Full=Swiprosin-1;
GN Name=Efhd2; Synonyms=Sws1;
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=Placenta;
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 [2]
RP PROTEIN SEQUENCE OF 123-133; 151-157; 159-187; 197-217 AND 233-239, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May regulate B-cell receptor (BCR)-induced immature and
CC primary B-cell apoptosis. Plays a role as negative regulator of the
CC canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis
CC through the regulation of BCL2L1 abundance. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CASP9; with inactive form. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane raft {ECO:0000250}. Note=In a mouse
CC immature B-cell line WEHI-231. {ECO:0000250}.
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; BC098936; AAH98936.1; -; mRNA.
DR RefSeq; NP_001026818.1; NM_001031648.1.
DR AlphaFoldDB; Q4FZY0; -.
DR SMR; Q4FZY0; -.
DR BioGRID; 255962; 4.
DR IntAct; Q4FZY0; 2.
DR STRING; 10116.ENSRNOP00000018864; -.
DR iPTMnet; Q4FZY0; -.
DR PhosphoSitePlus; Q4FZY0; -.
DR jPOST; Q4FZY0; -.
DR PaxDb; Q4FZY0; -.
DR PRIDE; Q4FZY0; -.
DR Ensembl; ENSRNOT00000018864; ENSRNOP00000018864; ENSRNOG00000013783.
DR GeneID; 298609; -.
DR KEGG; rno:298609; -.
DR UCSC; RGD:1307585; rat.
DR CTD; 79180; -.
DR RGD; 1307585; Efhd2.
DR eggNOG; KOG0041; Eukaryota.
DR GeneTree; ENSGT00390000012058; -.
DR HOGENOM; CLU_094429_0_0_1; -.
DR InParanoid; Q4FZY0; -.
DR OMA; SPREFML; -.
DR OrthoDB; 1511376at2759; -.
DR PhylomeDB; Q4FZY0; -.
DR TreeFam; TF320736; -.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR PRO; PR:Q4FZY0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013783; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q4FZY0; RN.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR040365; EFHD1/2.
DR PANTHER; PTHR13025; PTHR13025; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Direct protein sequencing; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
FT CHAIN 2..239
FT /note="EF-hand domain-containing protein D2"
FT /id="PRO_0000287580"
FT DOMAIN 91..126
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 127..162
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
FT MOD_RES 82
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8Y0"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
SQ SEQUENCE 239 AA; 26759 MW; BDA6F71C95D77ABB CRC64;
MATDELASKL SRRLQMEDEG GEATEQPGLN GAAAAAAEAP DETAQALGSA DDELSAKLLR
RADLNQGIGE PQSPSRRVFN PYTEFKEFSR KQIKDMEKMF KQYDAGKDGF IDLMELKLMM
EKLGAPQTHL GLKSMIQEVD EDFDSKLSFR EFLLIFRKAA AGELQEDSGL HVLARLSEID
VSTEGVKGAK NFFEAKVQAI NVSSRFEEEI KAEQEERKKQ AEEVKQRKAA FKELQSTFK
