EFHC1_BOVIN
ID EFHC1_BOVIN Reviewed; 640 AA.
AC E1BKH1;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=EF-hand domain-containing protein 1;
DE AltName: Full=Myoclonin-1;
GN Name=EFHC1;
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 {ECO:0000312|Proteomes:UP000009136};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2] {ECO:0007744|PDB:7RRO}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=34715025; DOI=10.1016/j.cell.2021.10.007;
RA Gui M., Farley H., Anujan P., Anderson J.R., Maxwell D.W., Whitchurch J.B.,
RA Botsch J.J., Qiu T., Meleppattu S., Singh S.K., Zhang Q., Thompson J.,
RA Lucas J.S., Bingle C.D., Norris D.P., Roy S., Brown A.;
RT "De novo identification of mammalian ciliary motility proteins using cryo-
RT EM.";
RL Cell 184:5791-5806.e19(2021).
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. May enhance
CC calcium influx through CACNA1E and stimulate programmed cell death (By
CC similarity). Microtubule inner protein (MIP) part of the dynein-
CC decorated doublet microtubules (DMTs) in cilia axoneme, which is
CC required for motile cilia beating (PubMed:34715025).
CC {ECO:0000250|UniProtKB:Q5JVL4, ECO:0000269|PubMed:34715025}.
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:0000269|PubMed:34715025}.
CC -!- TISSUE SPECIFICITY: Expressed in trachea multiciliated cells.
CC {ECO:0000269|PubMed:34715025}.
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DR RefSeq; NP_001179173.1; NM_001192244.1.
DR PDB; 7RRO; EM; 3.40 A; T/U/V=1-640.
DR PDBsum; 7RRO; -.
DR SMR; E1BKH1; -.
DR STRING; 9913.ENSBTAP00000023678; -.
DR PaxDb; E1BKH1; -.
DR Ensembl; ENSBTAT00000023678.5; ENSBTAP00000023678.4; ENSBTAG00000017810.6.
DR GeneID; 510124; -.
DR KEGG; bta:510124; -.
DR CTD; 114327; -.
DR VEuPathDB; HostDB:ENSBTAG00000017810; -.
DR VGNC; VGNC:28351; EFHC1.
DR eggNOG; KOG0043; Eukaryota.
DR GeneTree; ENSGT00530000063528; -.
DR HOGENOM; CLU_018366_0_1_1; -.
DR InParanoid; E1BKH1; -.
DR OMA; EDTYASC; -.
DR OrthoDB; 236088at2759; -.
DR TreeFam; TF314504; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000017810; Expressed in spermatid and 98 other tissues.
DR ExpressionAtlas; E1BKH1; baseline and differential.
DR GO; GO:0005879; C:axonemal microtubule; IDA:UniProtKB.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl.
DR GO; GO:0060285; P:cilium-dependent cell motility; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0051302; P:regulation of cell division; IEA:Ensembl.
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 SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS51336; DM10; 3.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cytoplasm; Cytoskeleton; Reference proteome;
KW Repeat.
FT CHAIN 1..640
FT /note="EF-hand domain-containing protein 1"
FT /id="PRO_0000456158"
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 574..609
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 640 AA; 74032 MW; A31979F58B6B7039 CRC64;
MVSNPVHGLP FLPGTSFKDL TKTAFHRSQT LGYRNGYAVV RRPTVGIGGD RLQVNQLSQA
DLDELASKIP ILTYGQARQA PPAAFVPAHV AFDKKVLKFD AYFQEDVPMS IEEHYRIRQV
HIYYYLEDDS MSVIEPVVEN SGIPQGKLIK RQRLSKNDRG DHYHWKDLNR GINITIYGKT
FRIVDCDKFT QVFLESQGIE LNPPEKMALD PYTELRKQPL RKYVTPTDFD QLKQFLTFDK
QVLRFYAIWD DTDSMFGECR TYIIHYYLMD DTVEIREVHE RNDGRDPFPL LMNRQRMPKV
LVENAKNFPR CVLEISDKEV LEWYTAKDFI VGKPLTILGR TFFIYDCDPF TRQYYQEKFG
ISDLPRIDMS KKEPPPMKQE LPPYNGFGLI EDSAQNCFAL IPKAPQKDVI KMLMNENKVL
RYLATLESPF PEDKGRRFVL SYFLATDMIS IFEPPVRNSG IIGGKYLGRT KVVKPGSSVE
NPVYYGPSDF FIGAVIEVFG HRFVILDTDD YVLKYMESNA AQYSPEALLS IQNHIRKQEA
PAPELDGQQA EEDPGVRDLE ALIDTIQKQL KDRPCRDNIR EAFQIYDKEA SGYVDRETFF
KICGSYQLPV DDSLIKELIR MCSHGEDKID YYNFVRAFSN
