MYO1F_MOUSE
ID MYO1F_MOUSE Reviewed; 1099 AA.
AC P70248;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Unconventional myosin-If;
GN Name=Myo1f;
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], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Cochlea;
RX PubMed=9119401; DOI=10.1006/geno.1996.4526;
RA Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
RA Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G., Weil D.,
RA Pujol R., Petit C.;
RT "Cloning of the genes encoding two murine and human cochlear unconventional
RT type I myosins.";
RL Genomics 40:332-341(1997).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails are presumed to bind to membranous compartments, which
CC would be moved relative to actin filaments (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, spleen, eye, brain,
CC lung, small intestine, testis and cochlea. Barely detectable in heart.
CC {ECO:0000269|PubMed:9119401}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-1 (MYH1). {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X97650; CAA66251.1; -; mRNA.
DR PIR; A59300; A59300.
DR AlphaFoldDB; P70248; -.
DR SMR; P70248; -.
DR IntAct; P70248; 2.
DR MINT; P70248; -.
DR STRING; 10090.ENSMUSP00000084887; -.
DR iPTMnet; P70248; -.
DR PhosphoSitePlus; P70248; -.
DR EPD; P70248; -.
DR jPOST; P70248; -.
DR MaxQB; P70248; -.
DR PeptideAtlas; P70248; -.
DR PRIDE; P70248; -.
DR ProteomicsDB; 293605; -.
DR MGI; MGI:107711; Myo1f.
DR eggNOG; KOG0162; Eukaryota.
DR InParanoid; P70248; -.
DR PhylomeDB; P70248; -.
DR ChiTaRS; Myo1f; mouse.
DR PRO; PR:P70248; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70248; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031941; C:filamentous actin; IDA:MGI.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IMP:MGI.
DR GO; GO:0043312; P:neutrophil degranulation; IMP:MGI.
DR GO; GO:0002446; P:neutrophil mediated immunity; IMP:MGI.
DR GO; GO:1990266; P:neutrophil migration; IMP:MGI.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; IMP:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11827; SH3_MyoIe_If_like; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR035507; Ie/If_SH3.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..1099
FT /note="Unconventional myosin-If"
FT /id="PRO_0000123453"
FT DOMAIN 17..690
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 693..722
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 728..917
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1042..1099
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 579..589
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 916..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00160"
SQ SEQUENCE 1099 AA; 125947 MW; 7D11592310C0C8F0 CRC64;
MGSKERFHWQ SHNVKQSGVD DMVLLSQITE DAIVRNLHKR FMDDYIFTYI GSVLISVNPF
KQMPYFTDRE IDLYQGAVQY EEPPHIYALT DNMYRNMLID CENQCVIISG ESGAGKTVAA
KYIMGYISKV SGGGDKVQHV KDIILQSNPL LEAFGNAKTV RNNNSSRFGK YFEIQFSRGG
EPDGGKISNF LLEKSRVVMQ NENERNFHIY YQLLEGASQE QQQNLGIMSQ DYYYYLNQSD
TYKVEGTDDR SDFSETLSAM QVMGFRQACQ QLVLQLVAGI LHLGNISFCE EGNYARVESV
DSLAFPAYLL GIDSGRLQEK LTSRKMDSKW GGRSESIDVT LNVEQAAYTR DALAKGLYAR
LFDFLVEAIN RAMQKPQEEY SIGVLDIYGF EIFQKNGFEQ FCINFVNEKL QQIFIELTLK
AEQEEYVQEG IRWTPIEYFN NKIVCDLIEN KLSPPGIMSV LDDVCATMHA TGGGADQTLL
QKLQAAVGTH EHFNSWSAGF VIHHYAGKVS YDVSGFCERN RDVLFSDLIE LMQSSDQDFL
RMLFPEKLNI DKKGRPSTAG SKIKKQANDL VSTLKKCTPH YIRCIKPNET KRPRDWEESR
VKHQVEYLGL RENIRVRRAG FAYRRQFSKF LQRYAILTPE TWPRWRGDER QGVQHLLRAV
NMEPDQYQMG STKVFVKNPE SLFLLEEMRE RKFDGFARTI QKAWRRHVAV RKYEEMREEA
SNILLNKKER RRNSINRNFV GNYLGLEERP ELRQFLAKRE RVDFADSVTK YDRRFKPIKR
DLILTPKCVY VIGTEKVKRG PEKGLVREVL KKKLDIQALR GVSLSTRQDD FFILQEEAAD
TFLESIFKTE FVSLLCKRFE EAARRPLPLT FQDILQFRVK KKGWGGGGTR NVTFSAGQVN
LAVLKAGGKT LTISLGDGLP KNSKPTRKGL AQGKPRRSAQ APTRAVPWAS QGLNRNGATL
FPRGEGPYTL EIYIWPQEFP EASTAIHLQP QDASRRPRAR PPSEHSTEFL NVPDQGVAGM
QRKRSIGQRP VPASRPKPQP RTHGPRCRAL YQYIGQDVDE LSFNVNEVIE ILIEDSSGWW
KGRLHGQEGL FPGNYVEKI
