ID   MYO1A_MOUSE             Reviewed;        1043 AA.
AC   O88329; B2RW65;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 174.
DE   RecName: Full=Unconventional myosin-Ia;
DE   AltName: Full=Brush border myosin I;
DE            Short=BBM-I;
DE            Short=BBMI;
DE   AltName: Full=Myosin I heavy chain;
DE            Short=MIHC;
GN   Name=Myo1a; Synonyms=Bbmi, Myhl;
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-909.
RX   PubMed=9933937;
RX   DOI=10.1002/(sici)1097-010x(19990215)283:3<242::aid-jez3>3.3.co;2-6;
RA   Skowron J.F., Mooseker M.S.;
RT   "Cloning and characterization of mouse brush border myosin-I in adult and
RT   embryonic intestine.";
RL   J. Exp. Zool. 283:242-257(1999).
CC   -!- FUNCTION: Involved in directing the movement of organelles along actin
CC       filaments. {ECO:0000305}.
CC   -!- PTM: Phosphorylated by ALPK1. {ECO:0000250|UniProtKB:Q9UBC5}.
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}.
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DR   EMBL; AC160970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC147605; AAI47606.1; -; mRNA.
DR   EMBL; BC147612; AAI47613.1; -; mRNA.
DR   EMBL; AF009960; AAC28397.1; -; mRNA.
DR   CCDS; CCDS36083.1; -.
DR   RefSeq; NP_001074688.1; NM_001081219.2.
DR   RefSeq; XP_006513922.1; XM_006513859.3.
DR   RefSeq; XP_006513923.1; XM_006513860.3.
DR   AlphaFoldDB; O88329; -.
DR   SMR; O88329; -.
DR   BioGRID; 240656; 1.
DR   IntAct; O88329; 1.
DR   STRING; 10090.ENSMUSP00000078540; -.
DR   GlyGen; O88329; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O88329; -.
DR   PhosphoSitePlus; O88329; -.
DR   jPOST; O88329; -.
DR   MaxQB; O88329; -.
DR   PaxDb; 10090-ENSMUSP00000078540; -.
DR   PeptideAtlas; O88329; -.
DR   ProteomicsDB; 293604; -.
DR   Antibodypedia; 28435; 116 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000079590.7; ENSMUSP00000078540.6; ENSMUSG00000025401.10.
DR   GeneID; 432516; -.
DR   KEGG; mmu:432516; -.
DR   UCSC; uc007hkh.2; mouse.
DR   AGR; MGI:107732; -.
DR   CTD; 4640; -.
DR   MGI; MGI:107732; Myo1a.
DR   VEuPathDB; HostDB:ENSMUSG00000025401; -.
DR   eggNOG; KOG0164; Eukaryota.
DR   GeneTree; ENSGT00940000160660; -.
DR   HOGENOM; CLU_000192_7_7_1; -.
DR   InParanoid; O88329; -.
DR   OMA; IKPNEYQ; -.
DR   OrthoDB; 1094820at2759; -.
DR   PhylomeDB; O88329; -.
DR   TreeFam; TF312960; -.
DR   BioGRID-ORCS; 432516; 4 hits in 81 CRISPR screens.
DR   PRO; PR:O88329; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; O88329; Protein.
DR   Bgee; ENSMUSG00000025401; Expressed in small intestine Peyer's patch and 63 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR   GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031941; C:filamentous actin; ISS:UniProtKB.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0005902; C:microvillus; IDA:MGI.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
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:0030030; P:cell projection organization; IMP:MGI.
DR   GO; GO:0030033; P:microvillus assembly; IMP:MGI.
DR   GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   GO; GO:0051648; P:vesicle localization; ISS:UniProtKB.
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; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 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:SF291; UNCONVENTIONAL MYOSIN-IA; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF06017; Myosin_TH1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 3.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 2.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51757; TH1; 1.
DR   Genevisible; O88329; MM.
PE   2: Evidence at transcript level;
KW   Actin-binding; ATP-binding; Calmodulin-binding; Motor protein; Myosin;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1043
FT                   /note="Unconventional myosin-Ia"
FT                   /id="PRO_0000123439"
FT   DOMAIN          8..694
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          697..719
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          720..742
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          743..772
FT                   /note="IQ 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          858..1042
FT                   /note="TH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT   REGION          571..593
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255"
FT   BINDING         101..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        397
FT                   /note="I -> L (in Ref. 3; AAC28397)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1043 AA;  118695 MW;  D66000A9E6FFF17E CRC64;
     MPLLEGPVGV EDLILLEPLD EESLIKNLQL RYENKEIYTY IGNVVISMNP YEQLPIYGPE
     FIAKYRDYTF YELKPHIYAL ANVAYQSLKD RDRDQCILIT GESGAGKTEA SKLVMSYVAA
     VCGKGEQVNS VKEQLLQSNP VLEAFGNAKT IRNNNSSRFG KYMDIEFDFK GSPLGGVITN
     YLLEKSRVVK QLKGERNFHI FYQLLAGADA QLLKALKLEE DTSVYGYLNG EVSKVNGMDD
     ASNFRAVQHA MSVIGFSEEE IRQVLEVTAL VLKLGNVKLT DEFQANGIPA SGICDGKGIQ
     EIGEMMGLNS TELERALCSR TMETGKEKVV TVLNVTQAQY ARDALAKNIY SRLFDWIVKR
     INESIKVGTG EKKKVMGVLD IYGFEILEDN SFEQFVINYC NERLQQVFIE LTLKEEQEEY
     KREGIPWTKV EYFDNGIICN LIEHSQRGIL AMLDEECLRP GVVSDSTFLA KLNQLFSKHS
     HYESKVSQNA QRQYDRTMGL SCFRISHYAG KVTYNVTGFI DKNNDLLFRD LSQTMWKAQH
     PLLKSLFPEG NPKEASLKRP PTAGTQFKNS VAVLMKNLYS KNPNYIRCIK PNDQQQKGRF
     TSEMVMVQAR YLGLLENVRV RRAGYAFRQG YKPFLERYRL LSRSTWPRWN GDDREGVEKV
     LGSLTLSSEE LAYGKTKIFI RSPKTLFYLE EQRRLRLQQL ATLIQKVYRG WRCRTHYQQM
     RKSQILISAW FRGNKQKKHY GKIRSSVLLI QAFVRGWRAR KNYRKYFRSG AALTLANFIY
     QSMAQKFLLN LKKNLPSTKV LDNTWPAAPY RCFNTANQEL QRLFYQWKCK KFRDQLSPKQ
     VQTLREKLCA SELFKGKKAS YPQSVPIPFR GDYIGLQGNP KLQRLKGREE GPVLVADTVK
     KVNRGNGKTS ARILLLTKGH VILTDAKKSQ AQIVIGLEDV AGVSVSSLQD GLFSLHLSEM
     SSAVSKGDIL LVSDHVVELL TKMYQAVLDA TQRQLSVTVT EKFSVRFKEG SVAVKVIQGP
     EGGGNRKLIC KKKGSNAMEV TVR
//