EFHD2_MOUSE
ID EFHD2_MOUSE Reviewed; 240 AA.
AC Q9D8Y0; Q9D0P4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=EF-hand domain-containing protein D2;
DE AltName: Full=Swiprosin-1;
GN Name=Efhd2; Synonyms=Sws1;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PROTEIN SEQUENCE OF 177-188 AND 198-206, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=15749887; DOI=10.4049/jimmunol.174.6.3508;
RA Mielenz D., Vettermann C., Hampel M., Lang C., Avramidou A., Karas M.,
RA Jacek H.-M.;
RT "Lipid rafts associate with intracellular B cell receptors and exhibit a B
RT cell stage-specific protein composition.";
RL J. Immunol. 174:3508-3517(2005).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17673920; DOI=10.1038/sj.cdd.4402206;
RA Avramidou A., Kroczek C., Lang C., Schuh W., Jaeck H.-M., Mielenz D.;
RT "The novel adaptor protein Swiprosin-1 enhances BCR signals and contributes
RT to BCR-induced apoptosis.";
RL Cell Death Differ. 14:1936-1947(2007).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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: 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.
CC {ECO:0000269|PubMed:17673920}.
CC -!- SUBUNIT: Interacts with CASP9; with inactive form. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane raft {ECO:0000269|PubMed:15749887}.
CC Note=In immature B-cell line WEHI-231.
CC -!- TISSUE SPECIFICITY: Detected in thymus, kidney, spleen, lung, liver and
CC brain. Highest abundance in brain and lowest in kidney and thymus.
CC {ECO:0000269|PubMed:17673920}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout B-cell differentiation, with
CC highest expression in immature bone marrow B-cells.
CC {ECO:0000269|PubMed:17673920}.
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DR EMBL; AK007560; BAB25108.1; -; mRNA.
DR EMBL; AK011219; BAB27476.1; -; mRNA.
DR CCDS; CCDS18885.1; -.
DR AlphaFoldDB; Q9D8Y0; -.
DR SMR; Q9D8Y0; -.
DR IntAct; Q9D8Y0; 3.
DR STRING; 10090.ENSMUSP00000044502; -.
DR iPTMnet; Q9D8Y0; -.
DR PhosphoSitePlus; Q9D8Y0; -.
DR REPRODUCTION-2DPAGE; Q9D8Y0; -.
DR CPTAC; non-CPTAC-3789; -.
DR EPD; Q9D8Y0; -.
DR jPOST; Q9D8Y0; -.
DR MaxQB; Q9D8Y0; -.
DR PaxDb; Q9D8Y0; -.
DR PeptideAtlas; Q9D8Y0; -.
DR PRIDE; Q9D8Y0; -.
DR ProteomicsDB; 275441; -.
DR MGI; MGI:106504; Efhd2.
DR eggNOG; KOG0041; Eukaryota.
DR InParanoid; Q9D8Y0; -.
DR PhylomeDB; Q9D8Y0; -.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR ChiTaRS; Efhd2; mouse.
DR PRO; PR:Q9D8Y0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D8Y0; protein.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
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..240
FT /note="EF-hand domain-containing protein D2"
FT /id="PRO_0000073646"
FT DOMAIN 92..127
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 128..163
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 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 152
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 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
FT MOD_RES 83
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96C19"
FT CONFLICT 14
FT /note="L -> V (in Ref. 1; BAB27476)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="Q -> H (in Ref. 1; BAB27476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 26791 MW; F11E549BFCB2C247 CRC64;
MATDELASKL SRRLQMEGEG GEATEQPGLN GAAAAAAAEA PDETAQALGS ADDELSAKLL
RRADLNQGIG EPQSPSRRVF NPYTEFKEFS RKQIKDMEKM FKQYDAGRDG FIDLMELKLM
MEKLGAPQTH LGLKSMIQEV DEDFDSKLSF REFLLIFRKA AAGELQEDSG LQVLARLSEI
DVSTEGVKGA KNFFEAKVQA INVSSRFEEE IKAEQEERKK QAEEVKQRKA AFKELQSTFK
