EFHC1_MOUSE
ID EFHC1_MOUSE Reviewed; 648 AA.
AC Q9D9T8;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=EF-hand domain-containing protein 1;
DE AltName: Full=Myoclonin-1;
GN Name=Efhc1;
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=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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15258581; DOI=10.1038/ng1393;
RA Suzuki T., Delgado-Escueta A.V., Aguan K., Alonso M.E., Shi J., Hara Y.,
RA Nishida M., Numata T., Medina M.T., Takeuchi T., Morita R., Bai D.,
RA Ganesh S., Sugimoto Y., Inazawa J., Bailey J.N., Ochoa A., Jara-Prado A.,
RA Rasmussen A., Ramos-Peek J., Cordova S., Rubio-Donnadieu F., Inoue Y.,
RA Osawa M., Kaneko S., Oguni H., Mori Y., Yamakawa K.;
RT "Mutations in EFHC1 cause juvenile myoclonic epilepsy.";
RL Nat. Genet. 36:842-849(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=15670853; DOI=10.1016/j.febslet.2004.12.070;
RA Ikeda T., Ikeda K., Enomoto M., Park M.K., Hirono M., Kamiya R.;
RT "The mouse ortholog of EFHC1 implicated in juvenile myoclonic epilepsy is
RT an axonemal protein widely conserved among organisms with motile cilia and
RT flagella.";
RL FEBS Lett. 579:819-822(2005).
RN [4]
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: Microtubule-associated protein which regulates cell division
CC and neuronal migration during cortical development. Necessary for
CC mitotic spindle organization. Necessary for radial and tangential cell
CC migration during brain development, possibly acting as a regulator of
CC cell morphology and process formation during migration (By similarity).
CC May enhance calcium influx through CACNA1E and stimulate programmed
CC cell death. Overexpression of EFHC1 in hippocampal primary culture
CC neurons induced apoptosis (PubMed:15258581). Microtubule inner protein
CC (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia
CC axoneme, which is required for motile cilia beating (By similarity).
CC {ECO:0000250|UniProtKB:E1BKH1, ECO:0000250|UniProtKB:Q5JVL4,
CC ECO:0000269|PubMed:15258581}.
CC -!- SUBUNIT: Interacts with the C-terminus of CACNA1E. InteractS with
CC alpha-tubulin. {ECO:0000250|UniProtKB:Q5JVL4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q5JVL4}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q5JVL4}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q5JVL4}. Cytoplasm,
CC cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:E1BKH1}.
CC -!- TISSUE SPECIFICITY: Expressed in adult brain including hippocampus,
CC cerebellum, cerebral cortex, thalamus, hypothalamus, amygdala and upper
CC brainstem. Expressed in soma and dentrites of pyramidal neurons of the
CC hippocampal CA1 region, pyramidal neurons of the cerebral cortex and
CC Purkinje cells of cerebellum. Highly expressed in testis, trachea, and
CC oviduct, moderately in lung, and slightly in brain. Highly expressed in
CC sperm flagella and tracheal cilia (at protein level).
CC {ECO:0000269|PubMed:15258581, ECO:0000269|PubMed:15670853}.
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DR EMBL; AK006489; BAB24614.1; -; mRNA.
DR CCDS; CCDS48227.1; -.
DR RefSeq; NP_082250.1; NM_027974.1.
DR AlphaFoldDB; Q9D9T8; -.
DR SMR; Q9D9T8; -.
DR STRING; 10090.ENSMUSP00000042343; -.
DR iPTMnet; Q9D9T8; -.
DR PhosphoSitePlus; Q9D9T8; -.
DR MaxQB; Q9D9T8; -.
DR PaxDb; Q9D9T8; -.
DR PRIDE; Q9D9T8; -.
DR ProteomicsDB; 277552; -.
DR DNASU; 71877; -.
DR GeneID; 71877; -.
DR KEGG; mmu:71877; -.
DR CTD; 114327; -.
DR MGI; MGI:1919127; Efhc1.
DR eggNOG; KOG0043; Eukaryota.
DR InParanoid; Q9D9T8; -.
DR OrthoDB; 236088at2759; -.
DR PhylomeDB; Q9D9T8; -.
DR BioGRID-ORCS; 71877; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9D9T8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D9T8; protein.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; NAS:UniProtKB.
DR GO; GO:0021795; P:cerebral cortex cell migration; ISO:MGI.
DR GO; GO:0060285; P:cilium-dependent cell motility; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR006602; DM10_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR040193; EFHC1/EFHC2/EFHB.
DR PANTHER; PTHR12086; PTHR12086; 1.
DR Pfam; PF06565; DUF1126; 3.
DR SMART; SM00676; DM10; 3.
DR SMART; SM00054; EFh; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS51336; DM10; 3.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Cytoskeleton; Reference proteome; Repeat.
FT CHAIN 1..648
FT /note="EF-hand domain-containing protein 1"
FT /id="PRO_0000073878"
FT DOMAIN 93..198
FT /note="DM10 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00665"
FT DOMAIN 239..359
FT /note="DM10 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00665"
FT DOMAIN 416..520
FT /note="DM10 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00665"
FT DOMAIN 582..617
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..45
FT /note="Required for its localization in the mitotic spindle
FT and interaction with alpha-tubulin"
FT /evidence="ECO:0000250|UniProtKB:Q5JVL4"
SQ SEQUENCE 648 AA; 75142 MW; BBA3377AADB9D373 CRC64;
MGTNPVHGLP FLPGSSFTDS TKTAFHRSQT LNYRNGYAVV RRPTMGIGGD RLHYNQLSQA
ELDELANKAP ILTYGPLKQA PLAEFVPAHV AFDKKVLKFS AYFQEDVPIS MEEHYRIRHV
NIYYYLEDDS MSVIEPVVEN SGIPQGKLIK RQRFTKNDMG DHYHWKDLNR GINLTVYGKT
FRIVDCDRFT QDFLESQGIE LNPSEKIPLD PYTQLRKEPV RKYVTPSDFD QLKQFLTFDK
QVLRFYAIWD DTDSLFGECR HYIIHYYLMD DTVEIREVHE RNNGRDPFPL LMNRQRMPKV
LVENAKNFPK CVLEISDQEV LEWYTAKDFI VGKPLTILGR TFFIYDCDPF TRQFYKDKFG
MPDLPPVDVT KKEPPPVKQE LPPYNGYGLI EDSAQNCFAL IPKAPRKDVV KMLMNDNKVL
RYLAALESPI PEDKDRRFVF SYFLATDMIS IFEPPVRNSG IIGGKFLGRT KVVKSFSPVD
NPIYYSPSDF FIGAVIEVFG HRFVILDTDE YVLKYMESNA SQYSPEALAS IQNRIQKPEL
PAPELESKQA TGEPMVQGTE ESKVQDLDAL IDQIHMHLKY NSYKENLRET FQMYDKDESG
YVDRETFFKI CETLNVPVDD SLIKELIRLC THGEGRINYY NFVRAFSN
