EFHD1_MOUSE
ID EFHD1_MOUSE Reviewed; 240 AA.
AC Q9D4J1; Q543U4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=EF-hand domain-containing protein D1;
DE AltName: Full=EF-hand domain-containing protein 1;
DE AltName: Full=Mitocalcin {ECO:0000303|PubMed:16336229};
DE AltName: Full=Swiprosin-2;
GN Name=Efhd1; Synonyms=Sws2;
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, and NOD; TISSUE=Corpora quadrigemina, Spleen, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary gland;
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12270117; DOI=10.1016/s0006-291x(02)02225-8;
RA Tominaga M., Tomooka Y.;
RT "Novel genes cloned from a neuronal cell line newly established from a
RT cerebellum of an adult p53(-/-) mouse.";
RL Biochem. Biophys. Res. Commun. 297:473-479(2002).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16336229; DOI=10.1111/j.1471-4159.2005.03554.x;
RA Tominaga M., Kurihara H., Honda S., Amakawa G., Sakai T., Tomooka Y.;
RT "Molecular characterization of mitocalcin, a novel mitochondrial Ca2+-
RT binding protein with EF-hand and coiled-coil domains.";
RL J. Neurochem. 96:292-304(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Acts as a calcium sensor for mitochondrial flash (mitoflash)
CC activation, an event characterized by stochastic bursts of superoxide
CC production (By similarity). May play a role in neuronal differentiation
CC (PubMed:16336229). {ECO:0000250|UniProtKB:Q9BUP0,
CC ECO:0000269|PubMed:16336229}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16336229}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:16336229). Highest
CC expression in testis, followed by ovary, kidney, cerebrum, cerebellum,
CC heart, liver, and spleen (PubMed:12270117). In the cerebrum and
CC cerebellum, undetectable at embryonic stages, expression increases
CC after birth up to adult stage (PubMed:12270117). In adult CNS, detected
CC in neurons of the cerebellum, cerebrum and hippocampus formation,
CC including dentate gyrus and Cornu Ammonis, but not in the white matter
CC (PubMed:12270117). In the testis, expressed in spermatocytes, but not
CC in spermatogonia nor in interstitial cells (PubMed:12270117). In ovary,
CC found predominantly in mural granulosa cells and those of the cumulus
CC oophorus (PubMed:12270117). In kidney, expressed in collecting ducts,
CC but not in glomeruli (PubMed:12270117). Not detected in skeletal muscle
CC (PubMed:12270117). {ECO:0000269|PubMed:12270117,
CC ECO:0000269|PubMed:16336229}.
CC -!- DEVELOPMENTAL STAGE: In the cerebral cortex, at birth, confined in the
CC Purkinje cell layer (PCL) and in cerebellar nuclei. Not detected in the
CC external germinal layer (EGL). At P5 and P10, predominantly found in
CC the PCL and internal germinal layer (IGL). Not detected in the EGL. At
CC P10 and P20, up-regulated. At P20, expression similar to that of the
CC adult cerebellum. {ECO:0000269|PubMed:12270117}.
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DR EMBL; AK016491; BAB30268.1; -; mRNA.
DR EMBL; AK045911; BAC32529.1; -; mRNA.
DR EMBL; AK144175; BAE25747.1; -; mRNA.
DR EMBL; AK171846; BAE42694.1; -; mRNA.
DR EMBL; BC019531; AAH19531.1; -; mRNA.
DR EMBL; BC085088; AAH85088.1; -; mRNA.
DR CCDS; CCDS15132.1; -.
DR RefSeq; NP_083165.1; NM_028889.2.
DR PDB; 7CLT; X-ray; 2.07 A; A=69-199.
DR PDBsum; 7CLT; -.
DR AlphaFoldDB; Q9D4J1; -.
DR SMR; Q9D4J1; -.
DR BioGRID; 221041; 1.
DR STRING; 10090.ENSMUSP00000027472; -.
DR iPTMnet; Q9D4J1; -.
DR PhosphoSitePlus; Q9D4J1; -.
DR MaxQB; Q9D4J1; -.
DR PaxDb; Q9D4J1; -.
DR PeptideAtlas; Q9D4J1; -.
DR PRIDE; Q9D4J1; -.
DR ProteomicsDB; 275440; -.
DR Antibodypedia; 34436; 305 antibodies from 30 providers.
DR DNASU; 98363; -.
DR Ensembl; ENSMUST00000027472; ENSMUSP00000027472; ENSMUSG00000026255.
DR Ensembl; ENSMUST00000118687; ENSMUSP00000112980; ENSMUSG00000026255.
DR GeneID; 98363; -.
DR KEGG; mmu:98363; -.
DR UCSC; uc007bwo.1; mouse.
DR CTD; 80303; -.
DR MGI; MGI:1921607; Efhd1.
DR VEuPathDB; HostDB:ENSMUSG00000026255; -.
DR eggNOG; KOG0041; Eukaryota.
DR GeneTree; ENSGT00390000012058; -.
DR HOGENOM; CLU_094429_0_0_1; -.
DR InParanoid; Q9D4J1; -.
DR OMA; RQDINEG; -.
DR OrthoDB; 1511376at2759; -.
DR PhylomeDB; Q9D4J1; -.
DR TreeFam; TF320736; -.
DR BioGRID-ORCS; 98363; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Efhd1; mouse.
DR PRO; PR:Q9D4J1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D4J1; protein.
DR Bgee; ENSMUSG00000026255; Expressed in seminiferous tubule of testis and 186 other tissues.
DR Genevisible; Q9D4J1; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0061891; F:calcium ion sensor activity; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:1900069; P:regulation of cellular hyperosmotic salinity response; ISS:UniProtKB.
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 3D-structure; Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat.
FT CHAIN 1..240
FT /note="EF-hand domain-containing protein D1"
FT /id="PRO_0000073644"
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 17..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Pro residues"
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 HELIX 81..84
FT /evidence="ECO:0007829|PDB:7CLT"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:7CLT"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:7CLT"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:7CLT"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:7CLT"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:7CLT"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:7CLT"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:7CLT"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:7CLT"
SQ SEQUENCE 240 AA; 27000 MW; 8C8B94F1A23E6FD4 CRC64;
MSSEELACKL QRRLRLEVRA ETDQGDPQPA PCDAPAGHPE PEPPARAPTA SADSELNLKL
SRRLDIHQGT ARPGRSKVFN PYTEFPEFSR RLLKDLEKMF KTYDAGRDGF IDLMELKLMM
EKLGAPQTHL GLKSMIKEVD EDFDGKLSFR EFLLIFHKAA AGELQEDSGL LALAKFSEID
VALEGVRGAK NFFEAKAQAL SCSSKFEAEL KAEQEERKRE EEARRLRQAA FRELKAAFSA
