EFHD2_BOVIN
ID EFHD2_BOVIN Reviewed; 242 AA.
AC A5D7A0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=EF-hand domain-containing protein D2;
DE AltName: Full=Swiprosin-1;
GN Name=EFHD2; Synonyms=SWS1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC140480; AAI40481.1; -; mRNA.
DR RefSeq; NP_001096715.1; NM_001103245.1.
DR AlphaFoldDB; A5D7A0; -.
DR SMR; A5D7A0; -.
DR STRING; 9913.ENSBTAP00000042244; -.
DR PaxDb; A5D7A0; -.
DR PeptideAtlas; A5D7A0; -.
DR PRIDE; A5D7A0; -.
DR Ensembl; ENSBTAT00000044780; ENSBTAP00000042244; ENSBTAG00000009048.
DR GeneID; 514259; -.
DR KEGG; bta:514259; -.
DR CTD; 79180; -.
DR VEuPathDB; HostDB:ENSBTAG00000009048; -.
DR VGNC; VGNC:28353; EFHD2.
DR eggNOG; KOG0041; Eukaryota.
DR GeneTree; ENSGT00390000012058; -.
DR HOGENOM; CLU_094429_0_0_1; -.
DR InParanoid; A5D7A0; -.
DR OMA; SPREFML; -.
DR OrthoDB; 1511376at2759; -.
DR TreeFam; TF320736; -.
DR Reactome; R-BTA-9013405; RHOD GTPase cycle.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000009048; Expressed in monocyte and 106 other tissues.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Calcium; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
FT CHAIN 2..242
FT /note="EF-hand domain-containing protein D2"
FT /id="PRO_0000319961"
FT DOMAIN 94..129
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 130..165
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 154
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 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
FT MOD_RES 85
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8Y0"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
SQ SEQUENCE 242 AA; 26918 MW; 776E8EE493F2B70E CRC64;
MATDELASKL SRRLQMEGEG GGEAPEQPGL NGAAAAAAAA GAPDETAEAL GSADEELSAK
LLRRADLNQG IGEPQSPSRR VFNPYTEFKE FSRKQIKDME KMFKEYDAGR DGFIDLMELK
LMMEKLGAPQ THLGLKNMIK EVDEDFDSKL SFREFLLIFR KAAAGELQED SGLHVLARLS
EIDVSTEGVK GAKSFFEAKV QAMNVSSRFE EEIKAEQEER KKQAEEMKQR KAAFKELQST
FK
