MYO3B_MOUSE
ID MYO3B_MOUSE Reviewed; 1305 AA.
AC Q1EG27; A2AR19; Q1EG26;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Myosin-IIIb;
DE EC=2.7.11.1;
GN Name=Myo3b;
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 [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Retina;
RA Dalal J.S., Dose A.C., Burnside B., Battelle B.-A.;
RT "Myosin IIIB expression in mouse retina.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION.
RX PubMed=22264607; DOI=10.1016/j.cub.2011.12.053;
RA Merritt R.C., Manor U., Salles F.T., Grati M., Dose A.C., Unrath W.C.,
RA Quintero O.A., Yengo C.M., Kachar B.;
RT "Myosin IIIB uses an actin-binding motif in its espin-1 cargo to reach the
RT tips of actin protrusions.";
RL Curr. Biol. 22:320-325(2012).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=26754646; DOI=10.1083/jcb.201509017;
RA Lelli A., Michel V., Boutet de Monvel J., Cortese M., Bosch-Grau M.,
RA Aghaie A., Perfettini I., Dupont T., Avan P., El-Amraoui A., Petit C.;
RT "Class III myosins shape the auditory hair bundles by limiting microvilli
RT and stereocilia growth.";
RL J. Cell Biol. 212:231-244(2016).
RN [5]
RP INTERACTION WITH ESPN AND ESPNL, AND TISSUE SPECIFICITY.
RX PubMed=26926603; DOI=10.1038/ncomms10833;
RA Ebrahim S., Avenarius M.R., Grati M., Krey J.F., Windsor A.M., Sousa A.D.,
RA Ballesteros A., Cui R., Millis B.A., Salles F.T., Baird M.A.,
RA Davidson M.W., Jones S.M., Choi D., Dong L., Raval M.H., Yengo C.M.,
RA Barr-Gillespie P.G., Kachar B.;
RT "Stereocilia-staircase spacing is influenced by myosin III motors and their
RT cargos espin-1 and espin-like.";
RL Nat. Commun. 7:10833-10833(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1216-1251, AND INTERACTION WITH
RP ESPN.
RX PubMed=26785147; DOI=10.7554/elife.12856;
RA Liu H., Li J., Raval M.H., Yao N., Deng X., Lu Q., Nie S., Feng W., Wan J.,
RA Yengo C.M., Liu W., Zhang M.;
RT "Myosin III-mediated cross-linking and stimulation of actin bundling
RT activity of Espin.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Probable actin-based motor with a protein kinase activity (By
CC similarity). Required for normal cochlear hair bundle development and
CC hearing. Plays an important role in the early steps of cochlear hair
CC bundle morphogenesis. Influences the number and lengths of stereocilia
CC to be produced and limits the growth of microvilli within the forming
CC auditory hair bundles thereby contributing to the architecture of the
CC hair bundle, including its staircase pattern (PubMed:26754646).
CC Involved in the elongation of actin in stereocilia tips by transporting
CC the actin regulatory factor ESPN to the plus ends of actin filaments
CC (PubMed:22264607). {ECO:0000250|UniProtKB:Q8WXR4,
CC ECO:0000269|PubMed:22264607, ECO:0000269|PubMed:26754646}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts (via C-terminus) with ESPN (PubMed:26785147,
CC PubMed:26926603). Interacts (via C-terminus) with ESPNL
CC (PubMed:26926603). {ECO:0000269|PubMed:26785147,
CC ECO:0000269|PubMed:26926603}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection, stereocilium {ECO:0000269|PubMed:26754646}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Myosin IIIB1;
CC IsoId=Q1EG27-1; Sequence=Displayed;
CC Name=2; Synonyms=Myosin IIIB2;
CC IsoId=Q1EG27-2; Sequence=VSP_036028, VSP_023112;
CC -!- TISSUE SPECIFICITY: Expressed in the cochlear hair cells (at protein
CC level) (PubMed:26754646). Expressed in utricle hair bundles (at protein
CC level) (PubMed:26926603). {ECO:0000269|PubMed:26754646,
CC ECO:0000269|PubMed:26926603}.
CC -!- DISRUPTION PHENOTYPE: MYO3B single knockout mice do not exhibit early
CC hearing impairment whereas mice with a double knockout of MYO3A and
CC MYO3B are profoundly deaf at 1 month of age. Cochlear hair bundles have
CC abnormally long stereocilia and show dynamic shape defects during
CC development. {ECO:0000269|PubMed:26754646}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase
CC superfamily. STE Ser/Thr protein kinase family. {ECO:0000305}.
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DR EMBL; AY830392; AAX59998.2; -; mRNA.
DR EMBL; AY830393; AAX59999.2; -; mRNA.
DR EMBL; AL845263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_796350.2; NM_177376.4.
DR RefSeq; XP_017174528.1; XM_017319039.1. [Q1EG27-1]
DR PDB; 5ET0; X-ray; 2.30 A; B/D=1252-1305.
DR PDB; 5ET1; X-ray; 1.65 A; C/D=1216-1251.
DR PDBsum; 5ET0; -.
DR PDBsum; 5ET1; -.
DR AlphaFoldDB; Q1EG27; -.
DR SMR; Q1EG27; -.
DR BioGRID; 236763; 2.
DR STRING; 10090.ENSMUSP00000055362; -.
DR iPTMnet; Q1EG27; -.
DR PhosphoSitePlus; Q1EG27; -.
DR PaxDb; Q1EG27; -.
DR PRIDE; Q1EG27; -.
DR ProteomicsDB; 287586; -. [Q1EG27-1]
DR ProteomicsDB; 287587; -. [Q1EG27-2]
DR Antibodypedia; 33828; 165 antibodies from 27 providers.
DR DNASU; 329421; -.
DR Ensembl; ENSMUST00000112243; ENSMUSP00000107862; ENSMUSG00000042064. [Q1EG27-1]
DR GeneID; 329421; -.
DR KEGG; mmu:329421; -.
DR CTD; 140469; -.
DR MGI; MGI:2448580; Myo3b.
DR VEuPathDB; HostDB:ENSMUSG00000042064; -.
DR eggNOG; KOG0587; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000159309; -.
DR HOGENOM; CLU_000192_10_2_1; -.
DR InParanoid; Q1EG27; -.
DR OrthoDB; 36742at2759; -.
DR PhylomeDB; Q1EG27; -.
DR BioGRID-ORCS; 329421; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Myo3b; mouse.
DR PRO; PR:Q1EG27; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q1EG27; protein.
DR Bgee; ENSMUSG00000042064; Expressed in otolith organ and 30 other tissues.
DR ExpressionAtlas; Q1EG27; baseline and differential.
DR Genevisible; Q1EG27; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032433; C:filopodium tip; IPI:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0032426; C:stereocilium tip; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0090103; P:cochlea morphogenesis; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IPI:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0030832; P:regulation of actin filament length; IMP:MGI.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd01379; MYSc_Myo3; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036083; MYSc_Myo3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; ATP-binding;
KW Cell projection; Cytoplasm; Cytoskeleton; Hearing; Kinase; Motor protein;
KW Myosin; Nucleotide-binding; Reference proteome; Repeat;
KW Sensory transduction; Serine/threonine-protein kinase; Transferase; Vision.
FT CHAIN 1..1305
FT /note="Myosin-IIIb"
FT /id="PRO_0000277830"
FT DOMAIN 15..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 331..1046
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1048..1077
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1075..1104
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 927..949
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1093..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 898
FT /note="K -> KKSPHSVPSYVLNTSPPK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036028"
FT VAR_SEQ 1149..1209
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023112"
FT CONFLICT 505
FT /note="E -> K (in Ref. 1; AAX59998/AAX59999)"
FT /evidence="ECO:0000305"
FT HELIX 1223..1225
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 1234..1241
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 1273..1275
FT /evidence="ECO:0007829|PDB:5ET0"
SQ SEQUENCE 1305 AA; 148099 MW; 9B8752F2704C7C80 CRC64;
MMLGLESLPD PMETWEIIET IGKGTYGKVY KVANKRDGSL AAVKVLDPVS DMDEEIEAEY
NILQFLPSHP NVVKFYGMFY KADRCVGGQL WLVLELCNGG SVTELVKGLL RCGKRLDEAV
ISYILYGALL GLQHLHCHRI IHRDVKGNNI LLTTEGGVKL VDFGVSAQLT STRLRRNTSV
GTPFWMAPEV IACEQQYDSS YDARCDVWSL GITAIELGDG DPPLFEMHPV KMLFKIPRNP
PPTLLHPDSW CEEFNHFISQ CLIKDFEKRP SVTHLLDHPF IKGTQGKVLC LQKQLAKVLQ
DQKHRNPVAK TRHERMHTGR PHRVEDAGKC CLEDDLVNLE VLDEDTIIYW LQKRYADALI
YTYVGDILIA LNPFQNLSIY SPQFSRLYHG VKRSSNPPHI FASADNAYQC LVTFSKDQCI
VISGESGSGK TESAHLIVQH LTFLGKADNQ TLRQKILQVN SLVEAFGNAR TAINDNSSRF
GKYLEMMFTP TGAVMGARIS EYLLEKSRVI QQAAGEKNFH IFYYIYAGLY HQKKLAEFRL
PEEKPPRYIA GETERVMQDI TSKESYRTQF EAIQHCFKII GFADKEVHSV YRILAGILNI
GSIEFAAISS QHQTDKSEVP NPEALENAAC VLCISSEELQ EALTSHCVVT RGETIVRANT
VDRAEDVRDA MSKALYGRLF SWIVNRINTL LQPDKNICSA EDRMNVGILD IFGFEDFQRN
SFEQLCINIA NEQIQYYFNQ HVFALEQMEY KNEGVDAVLV QYEDNRPLLD MFLQKPLGLL
ALLDEESRFP QGTDQTLVDK FEDNLRCKFF WRPKGVELCF GIQHYAGPVL YDASGVLEKN
RDTLPADVVV VLRTSENKLL QQLFSIPLTK TGNLAQTRAK ITASSRSLPP HFSAGRAKVD
TLEVIRHPEE TTNMKRQTMA SYFRYSLMDL LSKMVVGQPH FIRCIKPNDD RKALQFSQDR
VLAQLRSTGI LETVSIRRQG YSHRIFFEEF VKRYYYLAFR AHQTPPANKE SCVAILEKSR
LDHWVLGKTK VFLKYYHVEQ LNLLLREVMG RVVMLQAYTK GWLGARRYKR AKEKREKGAI
TIQSAWRGYD ARRKLKQRSR RRSESEAHIH TVLQTTPDQK YCPDSGGESN RGHEETSRNC
PAEADTDGHP QAQSPPTGCD VTSGHADTAA GYTVAELSVA GTDVSPSLVY HTASAHQRLS
PCEDSLKPGS EEGLSQKQRA PRRRCQQPKM LSSPEDTMYY NQLNGTLEYQ GSQRKPRKLG
QIKVLDGEDQ YYKCLSPGAC APEETHSVHP FFFSSSPRED PFAQH
