GenomeNet

Database: UniProt
Entry: F1MFG9_BOVIN
LinkDB: F1MFG9_BOVIN
Original site: F1MFG9_BOVIN 
ID   F1MFG9_BOVIN            Unreviewed;      1013 AA.
AC   F1MFG9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Myosin IG {ECO:0000313|Ensembl:ENSBTAP00000008366.4};
GN   Name=MYO1G {ECO:0000313|Ensembl:ENSBTAP00000008366.4,
GN   ECO:0000313|VGNC:VGNC:31822};
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:0000313|Ensembl:ENSBTAP00000008366.4, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000008366.4, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000008366.4,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000008366.4}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000008366.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   RefSeq; XP_005192371.1; XM_005192314.3.
DR   RefSeq; XP_005205671.1; XM_005205614.3.
DR   AlphaFoldDB; F1MFG9; -.
DR   SMR; F1MFG9; -.
DR   STRING; 9913.ENSBTAP00000008366; -.
DR   PaxDb; 9913-ENSBTAP00000008366; -.
DR   Ensembl; ENSBTAT00000008366.4; ENSBTAP00000008366.4; ENSBTAG00000006377.4.
DR   GeneID; 516513; -.
DR   KEGG; bta:516513; -.
DR   CTD; 64005; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006377; -.
DR   VGNC; VGNC:31822; MYO1G.
DR   eggNOG; KOG0160; Eukaryota.
DR   eggNOG; KOG0164; Eukaryota.
DR   GeneTree; ENSGT00940000158053; -.
DR   HOGENOM; CLU_000192_7_7_1; -.
DR   InParanoid; F1MFG9; -.
DR   OMA; YMILRKY; -.
DR   OrthoDB; 1094820at2759; -.
DR   TreeFam; TF312960; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000006377; Expressed in blood and 94 other cell types or tissues.
DR   ExpressionAtlas; F1MFG9; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR   GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR   GO; GO:0031256; C:leading edge membrane; IEA:Ensembl.
DR   GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0001891; C:phagocytic cup; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IEA:Ensembl.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0071976; P:cell gliding; IEA:Ensembl.
DR   GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:0006887; P:exocytosis; IEA:Ensembl.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; IEA:Ensembl.
DR   GO; GO:0120117; P:T cell meandering migration; IEA:Ensembl.
DR   GO; GO:0002456; P:T cell mediated immunity; IEA:Ensembl.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR   CDD; cd01378; MYSc_Myo1; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
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   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF381; UNCONVENTIONAL MYOSIN-IG; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF06017; Myosin_TH1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51757; TH1; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT   DOMAIN          9..702
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          819..1012
FT                   /note="TH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51757"
FT   REGION          579..601
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   BINDING         102..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1013 AA;  115907 MW;  742624AC49A0A3BC CRC64;
     MEDDEGPECG KPDFVLLDQV TMEDFMENLK LRFEKGRIYT YIGEVLVSVN PYQELPLYGP
     EAIARYQGRE LYERPPHLYA VANAAYRAMK RRSRDTCIVI SGESGAGKTE ASKHIMQYIA
     AVTNPSQRAE VERVKDVLLK STCVLEAFGN ARTNRNHNSS RFGKYMDINF DFKGDPVGGH
     IHSYLLEKSR VLKQHVGERN FHAFYQVLRG CEDEELQELH LQRNPAVYNF TRQGAGLNVL
     DIDEKSHHQA VTEAMRVIGF SPEEVASVHR ILAAILHLGN IEFVELESNL EQGRLAVTEE
     VLVDHVAELT ATPRELVLRC LLARTVASGG REVIEKGHTA AEASYARDAC AKAVYQRLFE
     WVVDRINHVM EPRDRDPRRD GKDTVIGVLD IYGFEVFPVN SFEQFCINYC NEKLQQLFIQ
     LILKQEQEEY EREGIAWQTV EYFNNATIVD LVERPHRGIL SVLDEACSTA GPITDRIFLQ
     TLDTHHRHHP HYTSRQLCPT DKTMEFGRDF RIKHYAGDVT YSVEGFIDKN RDFLFQDFKR
     LLYNSKDPTL RAMWPDGQQD ITEVTKRPLT AGTLFKNSMV ALVENLASKE PFYVRCIKPN
     EDKVAGKLDE GHCRHQVAYL GLLENVRVRR AGFASRQPYA RFLLRYKMTC EYTWPNHLLG
     SDKAAVGALL EQHGLQGDVA FGHSKLFIRS PRTLVTLEQS RACLIPIIVL LLQKAWRGTL
     ARRRCRRLRA IYTIMRCFRR HKVRAHLTEL QRRFQAARQP PHYGRDLVWP PPPTVLQPFQ
     DICQALFSRW RARQLVKNIP PSDMAQIKAK VAAMAALQEL RQDWGCRRAW ARDYLSSATD
     NPTASGLFAQ RLKTLREKDG FGAVLFSSHV RKVNRFNKSR DRALLLTDRH LYKLEPGRQY
     RVMRAVPLDA VTGLSVTSGR DQLVVLHARG YDDLVVCLHR SQPPLDNRIG ELVGVLAAHC
     QGEGRALEVR VSDCIPLTQR GARRLVSVEP RSEQPEPDFR CSRGAFTLLW PSC
//
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