MYO6_BOVIN
ID MYO6_BOVIN Reviewed; 1295 AA.
AC E1BPK6;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 4.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Unconventional myosin-VI {ECO:0000305};
DE AltName: Full=Unconventional myosin-6 {ECO:0000305};
GN Name=MYO6 {ECO:0000250|UniProtKB:Q9UM54};
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] {ECO:0000312|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136};
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:0000305}
RP INTERACTION WITH CABP5, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=22039235; DOI=10.1167/iovs.11-8246;
RA Sokal I., Haeseleer F.;
RT "Insight into the role of Ca2+-binding protein 5 in vesicle exocytosis.";
RL Invest. Ophthalmol. Vis. Sci. 52:9131-9141(2011).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements (By
CC similarity). Myosin 6 is a reverse-direction motor protein that moves
CC towards the minus-end of actin filaments (By similarity). Has slow rate
CC of actin-activated ADP release due to weak ATP binding. Functions in a
CC variety of intracellular processes such as vesicular membrane
CC trafficking and cell migration (By similarity). Required for the
CC structural integrity of the Golgi apparatus via the p53-dependent pro-
CC survival pathway. Appears to be involved in a very early step of
CC clathrin-mediated endocytosis in polarized epithelial cells (By
CC similarity). May act as a regulator of F-actin dynamics (By
CC similarity). As part of the DISP complex, may regulate the association
CC of septins with actin and thereby regulate the actin cytoskeleton (By
CC similarity). May play a role in transporting DAB2 from the plasma
CC membrane to specific cellular targets (By similarity). May play a role
CC in the extension and network organization of neurites (By similarity).
CC Required for structural integrity of inner ear hair cells (By
CC similarity). Modulates RNA polymerase II-dependent transcription (By
CC similarity). {ECO:0000250|UniProtKB:Q29122,
CC ECO:0000250|UniProtKB:Q64331, ECO:0000250|UniProtKB:Q9UM54}.
CC -!- SUBUNIT: Homodimer; dimerization seems to implicate the unfolding of
CC the three-helix bundle region creating an additional calmodulin binding
CC site, and cargo binding (By similarity). Able to function as a monomer
CC under specific conditions in vitro (By similarity). Forms a complex
CC with CFTR and DAB2 in the apical membrane of epithelial cells (By
CC similarity). Component of the DISP/DOCK7-induced septin displacement
CC complex, at least composed of DOCK7, LRCH3 and MYO6 (By similarity).
CC Binding to calmodulin through a unique insert, not found in other
CC myosins, located in the neck region between the motor domain and the IQ
CC domain appears to contribute to the directionality reversal (By
CC similarity). This interaction occurs only if the C-terminal lobe of
CC calmodulin is occupied by calcium (By similarity). Interaction with F-
CC actin/ACTN1 occurs only at the apical brush border domain of the
CC proximal tubule cells (By similarity). Interacts with DAB2 (By
CC similarity). In vitro, the C-terminal globular tail binds a C-terminal
CC region of DAB2 (By similarity). Interacts with CFTR (By similarity).
CC Interacts with OPTN (By similarity). Interacts with CABP5
CC (PubMed:22039235). {ECO:0000250|UniProtKB:Q29122,
CC ECO:0000250|UniProtKB:Q64331, ECO:0000250|UniProtKB:Q9I8D1,
CC ECO:0000250|UniProtKB:Q9UM54, ECO:0000269|PubMed:22039235}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9UM54}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UM54}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9UM54}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane,
CC clathrin-coated pit {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UM54}. Cell
CC projection, filopodium {ECO:0000250|UniProtKB:Q9UM54}. Cell projection,
CC ruffle membrane {ECO:0000250|UniProtKB:Q29122}. Cell projection,
CC microvillus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q29122}. Note=Also present in endocytic vesicles
CC (By similarity). Translocates from membrane ruffles, endocytic vesicles
CC and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus
CC through induction by p53 and p53-induced DNA damage. Recruited into
CC membrane ruffles from cell surface by EGF-stimulation. Colocalizes with
CC DAB2 in clathrin-coated pits/vesicles (By similarity). Colocalizes with
CC OPTN at the Golgi complex and in vesicular structures close to the
CC plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q29122,
CC ECO:0000250|UniProtKB:Q9I8D1, ECO:0000250|UniProtKB:Q9UM54}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level).
CC {ECO:0000269|PubMed:22039235}.
CC -!- DOMAIN: Divided into three regions: a N-terminal motor (head) domain,
CC followed by a neck domain consisting of a calmodulin-binding linker
CC domain and a single IQ motif, and a C-terminal tail region with a
CC three-helix bundle region, a SAH domain and a unique globular domain
CC required for interaction with other proteins such as cargo-binding.
CC {ECO:0000250|UniProtKB:Q29122}.
CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high
CC content of charged residues which are predicted to stabilize the alpha-
CC helical structure by ionic bonds. Its contribution to the mechanism
CC confering the myosin movement on actin filaments is debated.
CC {ECO:0000250|UniProtKB:Q9UM54}.
CC -!- PTM: Phosphorylation in the motor domain, induced by EGF, results in
CC translocation of MYO6 from the cell surface to membrane ruffles and
CC affects F-actin dynamics. Phosphorylated in vitro by p21-activated
CC kinase (PAK). {ECO:0000250|UniProtKB:Q29122}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000255}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-6 (MYH6). {ECO:0000305}.
CC -!- CAUTION: Originally predicted to contain a coiled coil domain but
CC generally accepted to contain a stable SAH domain instead.
CC {ECO:0000305}.
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DR EMBL; DAAA02025285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02025286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005210731.1; XM_005210674.3.
DR RefSeq; XP_005210732.1; XM_005210675.3.
DR RefSeq; XP_015328260.1; XM_015472774.1.
DR AlphaFoldDB; E1BPK6; -.
DR SMR; E1BPK6; -.
DR STRING; 9913.ENSBTAP00000022276; -.
DR PaxDb; E1BPK6; -.
DR PRIDE; E1BPK6; -.
DR GeneID; 535127; -.
DR CTD; 4646; -.
DR eggNOG; KOG0163; Eukaryota.
DR HOGENOM; CLU_000192_7_2_1; -.
DR InParanoid; E1BPK6; -.
DR OrthoDB; 122881at2759; -.
DR TreeFam; TF351449; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IBA:GO_Central.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IBA:GO_Central.
DR GO; GO:0042472; P:inner ear morphogenesis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01382; MYSc_Myo6; 1.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR032412; Myosin-VI_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR036114; MYSc_Myo6.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF16521; Myosin-VI_CBD; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Cell membrane;
KW Cell projection; Coated pit; Cytoplasm; Cytoplasmic vesicle; Endocytosis;
KW Golgi apparatus; Hearing; Membrane; Motor protein; Myosin;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1295
FT /note="Unconventional myosin-VI"
FT /id="PRO_0000446902"
FT DOMAIN 2..53
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 57..771
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 813..842
FT /note="IQ"
FT /evidence="ECO:0000250|UniProtKB:Q29122"
FT REGION 273..317
FT /note="Responsible for slow ATPase activity"
FT /evidence="ECO:0000250|UniProtKB:Q29122"
FT REGION 651..673
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 782..810
FT /note="Required for binding calmodulin"
FT /evidence="ECO:0000250|UniProtKB:Q29122"
FT REGION 835..916
FT /note="Three-helix bundle"
FT /evidence="ECO:0000250|UniProtKB:Q29122"
FT REGION 917..984
FT /note="SAH"
FT /evidence="ECO:0000250|UniProtKB:Q9UM54"
FT REGION 934..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1119
FT /note="Interaction with OPTN"
FT /evidence="ECO:0000250|UniProtKB:Q9I8D1"
FT BINDING 151..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UM54"
FT MOD_RES 405
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UM54"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64331"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64331"
SQ SEQUENCE 1295 AA; 149616 MW; F0FC8CF7A47C903C CRC64;
MEDGRPVWAP HPTEGFQMGN IVDIGPDSLT IEPLGQKGKT FLALINQVFP AEEDSKKDVE
DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY FDIPKIYSSD SIKSYQGKSL
GTMPPHVFAI ADKAFRDMKV LKMSQSIIVS GESGAGKTEN TKFVLRYLTE SYGSGQDIDD
RIVEANPLLE AFGNAKTVRN NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK
EERNYHIFYR LCAGASEDIR ERLHLSSPDN FRYLNRGCTR YFANKETDKQ ILQNRKTPEH
LKAGSLKDPL LDDHGDFVRM CTAMKKIGLD DEEKLDLFRV VAGVLHLGNI DFEEAGSTSG
GCNLKNKSTQ SLEYCAELLG LDQDDLRVSL TTRVMLTTAG GTKGTVIKVP LKVEQANNAR
DALAKTVYSH LFDHVVNRVN QCFPFETSSY FIGVLDIAGF EYFEHNSFEQ FCINYCNEKL
QQFFNERILK EEQELYQKEG LGVNEVHYVD NQDCIDLIEA KLMGILDILD EENRLPQPSD
QHFTSAVHQK HKDHFRLSIP RKSKLAVHRN IRDDEGFIVR HFAGAVCYET TQFVEKNNDA
LHMSLESLIC ESRDKFIREL FESSTNNNKD TKQKAGKLSF ISVGNKFKTQ LNLLLDKLRS
TGASFIRCIK PNLKMTSHDF EGAQILSQLQ CSGMVSVLDL MQGGFPSRAS FHELYNMYKK
YMPDKLARLD PRLFCKALFK ALGLNEVDYK FGLTKVFFRP GKFAEFDQIM KSDPDHLAQL
VKRVNHWLIC SRWKKVQWCS LSVIKLKNKI KYRAEACIKM QKTIRMWLCK RRHKPRIDGL
VKVGTLKKRL DKFNEVVSAL KDGKAEMNKQ VKDLEISIDA LMAKIKSTMM TREQIQKEYD
ALVKSSEVLL SALQKKKQQE EEAERLRRIQ EEMEKERKRR EEDEQRRRKE EEERRMKLEM
EAKRKQEEEE RKKREDDEKR IQAEVEAQLA RQREEESQQQ AVLEQERRDR ELALRIARSE
AELIIDEAQA DPAALRSLDF HPVTSKINGT RRTMTPEQMA KEMSEILSRG PAVQATKAAA
GTKKHDLSKW KYAELRDTIN TSCDIELLAA CREEFHRRLK VYHAWKSKNK KRNTETEQRA
PKSVTDYDFA PFLNNSPQQN PAAQLPARQQ EIEMNRQQRF FRIPFIRPAD QYKDPQNKKK
GWWYAHFDGP WIARQMELHP DKPPILLVAG KDDMEMCELN LEETGLTRKR GAEILPRQFE
EIWERCGGIQ YLQSAIESRQ ARPTYATAML QNLLK
