MYO19_MOUSE
ID MYO19_MOUSE Reviewed; 963 AA.
AC Q5SV80; Q8BH54; Q9D2Z3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Unconventional myosin-XIX {ECO:0000303|PubMed:24825904};
DE AltName: Full=Myosin head domain-containing protein 1 {ECO:0000312|MGI:MGI:1913446};
GN Name=Myo19 {ECO:0000303|PubMed:24825904, ECO:0000312|MGI:MGI:1913446};
GN Synonyms=Myohd1 {ECO:0000312|MGI:MGI:1913446};
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 MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 517-963 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cecum, Head, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 222-963 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP FUNCTION, AND INTERACTION WITH MYL9 AND MYL12B.
RX PubMed=24825904; DOI=10.1074/jbc.m114.569087;
RA Lu Z., Ma X.N., Zhang H.M., Ji H.H., Ding H., Zhang J., Luo D., Sun Y.,
RA Li X.D.;
RT "Mouse myosin-19 is a plus-end-directed, high-duty ratio molecular motor.";
RL J. Biol. Chem. 289:18535-18548(2014).
CC -!- FUNCTION: Actin-based motor molecule with ATPase activity that
CC localizes to the mitochondrion outer membrane (PubMed:24825904). Motor
CC protein that moves towards the plus-end of actin filaments
CC (PubMed:24825904). Required for mitochondrial inheritance during
CC mitosis (By similarity). May be involved in mitochondrial transport or
CC positioning (By similarity). {ECO:0000250|UniProtKB:Q96H55,
CC ECO:0000269|PubMed:24825904}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains:
CC interacts with myosin light chains MYL9 and MYL12B.
CC {ECO:0000269|PubMed:24825904}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q96H55}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96H55}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q96H55}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SV80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SV80-2; Sequence=VSP_033407, VSP_033408;
CC -!- DOMAIN: The MyMOMA (MYO19-specific mitochondrial outer membrane-
CC association) region mediates association with the mitochondrion outer
CC membrane via electrostatic interaction. {ECO:0000250|UniProtKB:Q96H55}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AK018609; BAB31305.1; -; mRNA.
DR EMBL; AK053033; BAC35243.1; -; mRNA.
DR EMBL; AK053237; BAC35317.1; -; mRNA.
DR EMBL; AL645623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007156; AAH07156.1; -; mRNA.
DR CCDS; CCDS48871.1; -. [Q5SV80-1]
DR RefSeq; NP_079690.2; NM_025414.3. [Q5SV80-1]
DR RefSeq; XP_011247475.1; XM_011249173.2. [Q5SV80-1]
DR AlphaFoldDB; Q5SV80; -.
DR SMR; Q5SV80; -.
DR BioGRID; 211288; 1.
DR STRING; 10090.ENSMUSP00000091502; -.
DR iPTMnet; Q5SV80; -.
DR PhosphoSitePlus; Q5SV80; -.
DR EPD; Q5SV80; -.
DR MaxQB; Q5SV80; -.
DR PaxDb; Q5SV80; -.
DR PeptideAtlas; Q5SV80; -.
DR PRIDE; Q5SV80; -.
DR ProteomicsDB; 286124; -. [Q5SV80-1]
DR ProteomicsDB; 286125; -. [Q5SV80-2]
DR Antibodypedia; 73086; 151 antibodies from 24 providers.
DR DNASU; 66196; -.
DR Ensembl; ENSMUST00000020837; ENSMUSP00000020837; ENSMUSG00000020527. [Q5SV80-2]
DR Ensembl; ENSMUST00000093969; ENSMUSP00000091502; ENSMUSG00000020527. [Q5SV80-1]
DR GeneID; 66196; -.
DR KEGG; mmu:66196; -.
DR UCSC; uc007kra.2; mouse. [Q5SV80-2]
DR UCSC; uc007krb.2; mouse. [Q5SV80-1]
DR CTD; 80179; -.
DR MGI; MGI:1913446; Myo19.
DR VEuPathDB; HostDB:ENSMUSG00000020527; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000157382; -.
DR HOGENOM; CLU_000192_7_4_1; -.
DR InParanoid; Q5SV80; -.
DR OMA; CQLMDDA; -.
DR OrthoDB; 311886at2759; -.
DR PhylomeDB; Q5SV80; -.
DR TreeFam; TF328771; -.
DR Reactome; R-MMU-9013419; RHOT2 GTPase cycle.
DR Reactome; R-MMU-9013425; RHOT1 GTPase cycle.
DR BioGRID-ORCS; 66196; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Myo19; mouse.
DR PRO; PR:Q5SV80; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SV80; protein.
DR Bgee; ENSMUSG00000020527; Expressed in vomeronasal organ and 153 other tissues.
DR Genevisible; Q5SV80; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0032027; F:myosin light chain binding; IPI:MGI.
DR GO; GO:0060002; F:plus-end directed microfilament motor activity; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0034642; P:mitochondrion migration along actin filament; ISO:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0090140; P:regulation of mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd14880; MYSc_Myo19; 1.
DR Gene3D; 3.40.850.10; -; 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; IPR036035; MYSc_Myo19.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Motor protein;
KW Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..963
FT /note="Unconventional myosin-XIX"
FT /id="PRO_0000332970"
FT DOMAIN 35..758
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 762..782
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 783..812
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 602..624
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 829..963
FT /note="MyMOMA region"
FT /evidence="ECO:0000250|UniProtKB:Q96H55"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT VAR_SEQ 184..206
FT /note="NACTLRNSNSSRFGKFIQLQLNR -> KLSVLALPSGAISSATRPPLPRC
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033407"
FT VAR_SEQ 207..963
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033408"
FT CONFLICT 371
FT /note="Missing (in Ref. 3; AAH07156)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="G -> C (in Ref. 1; BAB31305)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="V -> L (in Ref. 1; BAB31305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 963 AA; 108075 MW; E3DC1F9B13CDF3A5 CRC64;
MLQQVNGHSL GSDAEGRASL KGDLREFLGG EIPLHQLDDL TKVNPVTLET VLRCLQARYT
EDIFYTNAGC TLVALNPFKH VPQLYAPELM QEYHAAPQPQ KLKPHIFTVG EQTYRNVKSL
IEPVNQSIVV SGESGAGKTW TSRCLMKFYA VVAASPTSCE NHKIAERIEQ RILNSNPVME
AFGNACTLRN SNSSRFGKFI QLQLNRAQQM TGAAVQTYLL EKTRVACQAS SERNFHIFYQ
ICKGATKDER LQWHLPEGTA FSWLPNPESS LEEDCFEVTR EAMLHLGIDT PTQNNIFKVL
AGLLHLGNVH FVDSEDEALP CQVMDDTKVS VRTSALLLQL PEKMLLESMQ IRTIKAGKQQ
QVFQKPCSRA ECDTRRDCLA KLIYARLFDW LVSVINSSIC ADSKSWTAFI GLLDVYGFES
FPNNSLEQLC INYANEKLQQ HFVAHYLRAQ QEEYEVEGLE WSFVNYQDNQ TCLDLLEGSP
ISICSLINEE CRLNRPSSAA QLQTRIESTL AGRPCLGHNK LSREPSFVVV HFAGPVRYHT
AGLVEKNKDP VPPELTELLQ QSQDPLLTML FPANPEEKTQ EELSGQSRAP ALTVVSKFKA
SLEQLLQVLH NTTPHYIRCI KPNSQSQPQT FLQEEVLNQL EACGLVETIH ISAAGFPIRV
SHQNFIERYK LLRRLGPRMS SGLGGLEPAE GSSEQPLCAK EATLQPLLQD ILHALPALIQ
TAATPSDPAK NTQIPLYCGR TKIFMTDSML ELLECGRAQM LEQCARCIQC GWRRHRLQKQ
EKQRRAAVLI QAAFRSWLTR KHIRRLHIAA TVIKHAWHKW RIRMACLASK ELDGMEEKPM
PQAPGTLRSS MSPAHTRFLG AIIHLWPLGL VLANSADGVR GFQRKLVAHA CLRLPSDRPS
NKVQTPQQDQ AGITSIRALP QGSIKFHCRK SPLQYADICP DPSASCVTGF NQILLESHRP
VQV
