ID   MYO19_XENLA             Reviewed;         971 AA.
AC   Q569U0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Unconventional myosin-XIX {ECO:0000250|UniProtKB:Q96H55};
GN   Name=myo19 {ECO:0000250|UniProtKB:Q96H55};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actin-based motor molecule with ATPase activity that
CC       localizes to the mitochondrion outer membrane. Motor protein that moves
CC       towards the plus-end of actin filaments. Required for mitochondrial
CC       inheritance during mitosis. May be involved in mitochondrial transport
CC       or positioning. {ECO:0000250|UniProtKB:Q5SV80,
CC       ECO:0000250|UniProtKB:Q96H55}.
CC   -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC       {ECO:0000250|UniProtKB:Q5SV80}.
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   -!- 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; BC092309; AAH92309.1; -; mRNA.
DR   RefSeq; NP_001089346.1; NM_001095877.1.
DR   AlphaFoldDB; Q569U0; -.
DR   SMR; Q569U0; -.
DR   DNASU; 734396; -.
DR   GeneID; 734396; -.
DR   KEGG; xla:734396; -.
DR   CTD; 734396; -.
DR   Xenbase; XB-GENE-999902; myo19.S.
DR   OrthoDB; 311886at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 734396; Expressed in egg cell and 19 other tissues.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:0090140; P:regulation of mitochondrial fission; ISS:UniProtKB.
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; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 3.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Motor protein; Myosin;
KW   Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..971
FT                   /note="Unconventional myosin-XIX"
FT                   /id="PRO_0000332971"
FT   DOMAIN          48..755
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          758..787
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          780..809
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..633
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   REGION          826..971
FT                   /note="MyMOMA region"
FT                   /evidence="ECO:0000250|UniProtKB:Q96H55"
FT   BINDING         145..152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   971 AA;  110621 MW;  056BF2778FE78BC4 CRC64;
     MSRPLSKNTE REPKQINGHQ NNLSNHKHLS KSLEQEMKAF LIDEKELHLY DDLTKVNPVT
     TATVLKCLQA RYSAGVFYTN AGCTVVAVNP FQPVYKLYSS EVMKDYHSTS NPQGCKPHIF
     TVAEQAYRNV QSQIQPVNQS IIVSGESGAG KTWTSRCLMK FYATVSASRC YITNEMVERI
     EGRVLDSNPV MEAFGNACTL RNNNSSRFGK YIQLQLNRAQ QITGASIQTY LLEKTRVAHQ
     APLERNFHIF YQMFKGASRL EREEWNLPEK ANFSWLPNYE NNLEEDDFEV TKKAMLHLGI
     DQPTQNNIFK ILSGLLHLGN IKFSDSVDES QPCEPLNYTQ EFASIAANLL KIPVSHLLER
     LSIRTITAGK QQVFKKPCRK SECDTRRDCL AKTIYARLFE WLVTVINENI CAESCRWNNF
     IGLLDVYGFE SFPENNLEQL CINYANEKLQ QHFVSHYLKS QQDEYAAEGL EWSFISYQDN
     QSCVDLLEGS PISIFSLLNE ECRLNRSLDA GQLQSRLENA LSHNKCIGRD KFSKKPNFIV
     SHYAGKVQYQ IEDMAEKNKD PVPPELIQLL QESDDHLLQK LFPVDNNKLV YGATNNRAVG
     VTVVSKFKGS LESLMQILHS TTPHYIRCIK PNVDCQALVF RQEEVLMQLE ACGIVETINI
     SAAGFPIRIS FENFVERYSV IAPRQSHMKT CFPLKKKQGS IEKTDQLSSK LHTILQAVLP
     KQCKDSTLSN SLVHCGTTKV FLTHLMVELL EERRLIAISS KAMCIQCCWR SYRQRKLAKQ
     SKAATTIQAA VKGWLTKKYI KRMHSAATVI KRIWKKWKEK MEALAAAELD DSTEDVESTL
     FSSMLASPVK SLESSKTNLP DKIMTQSAIL RFGTLGLVLY GAPAIRKYIV ETDELKRNQN
     ILMCLNMLHR NNRYKVTVNR EEPGITSIRA RPQGSIRFHY KRSPLHFANI CPGKINCGIT
     GFNEILLEKT V