MYO19_HUMAN
ID MYO19_HUMAN Reviewed; 970 AA.
AC Q96H55; Q59GS4; Q9H5X2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Unconventional myosin-XIX {ECO:0000303|PubMed:19932026};
DE AltName: Full=Myosin head domain-containing protein 1 {ECO:0000312|HGNC:HGNC:26234};
GN Name=MYO19 {ECO:0000303|PubMed:19932026, ECO:0000312|HGNC:HGNC:26234};
GN Synonyms=MYOHD1 {ECO:0000312|HGNC:HGNC:26234};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-176.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Placenta;
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, TARGETING REGION, AND SUBCELLULAR LOCATION.
RX PubMed=19932026; DOI=10.1016/j.cub.2009.10.026;
RA Quintero O.A., DiVito M.M., Adikes R.C., Kortan M.B., Case L.B., Lier A.J.,
RA Panaretos N.S., Slater S.Q., Rengarajan M., Feliu M., Cheney R.E.;
RT "Human Myo19 is a novel myosin that associates with mitochondria.";
RL Curr. Biol. 19:2008-2013(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-135.
RX PubMed=23568824; DOI=10.1002/cm.21110;
RA Adikes R.C., Unrath W.C., Yengo C.M., Quintero O.A.;
RT "Biochemical and bioinformatic analysis of the myosin-XIX motor domain.";
RL Cytoskeleton 70:281-295(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25447992; DOI=10.1016/j.cub.2014.09.045;
RA Rohn J.L., Patel J.V., Neumann B., Bulkescher J., Mchedlishvili N.,
RA McMullan R.C., Quintero O.A., Ellenberg J., Baum B.;
RT "Myo19 ensures symmetric partitioning of mitochondria and coupling of
RT mitochondrial segregation to cell division.";
RL Curr. Biol. 24:2598-2605(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ARG-855; 882-ARG-LYS-883;
RP ARG-915; LYS-923 AND 927-ARG-LYS-928.
RX PubMed=27126804; DOI=10.1002/cm.21305;
RA Hawthorne J.L., Mehta P.R., Singh P.P., Wong N.Q., Quintero O.A.;
RT "Positively charged residues within the MYO19 MyMOMA domain are essential
RT for proper localization of MYO19 to the mitochondrial outer membrane.";
RL Cytoskeleton 73:286-299(2016).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=26659663; DOI=10.1242/jcs.175349;
RA Shneyer B.I., Usaj M., Henn A.;
RT "Myo19 is an outer mitochondrial membrane motor and effector of starvation-
RT induced filopodia.";
RL J. Cell Sci. 129:543-556(2016).
CC -!- FUNCTION: Actin-based motor molecule with ATPase activity that
CC localizes to the mitochondrion outer membrane (PubMed:19932026,
CC PubMed:23568824, PubMed:25447992). Motor protein that moves towards the
CC plus-end of actin filaments (By similarity). Required for mitochondrial
CC inheritance during mitosis (PubMed:25447992). May be involved in
CC mitochondrial transport or positioning (PubMed:23568824).
CC {ECO:0000250|UniProtKB:Q5SV80, ECO:0000269|PubMed:19932026,
CC ECO:0000269|PubMed:25447992, ECO:0000305|PubMed:23568824}.
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:0000250|UniProtKB:Q5SV80}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:19932026, ECO:0000269|PubMed:23568824,
CC ECO:0000269|PubMed:25447992, ECO:0000269|PubMed:26659663,
CC ECO:0000269|PubMed:27126804}; Peripheral membrane protein
CC {ECO:0000269|PubMed:27126804}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19932026}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96H55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96H55-2; Sequence=VSP_033402, VSP_033403;
CC Name=3;
CC IsoId=Q96H55-3; Sequence=VSP_033405, VSP_033406;
CC Name=4;
CC IsoId=Q96H55-4; Sequence=VSP_033404;
CC -!- TISSUE SPECIFICITY: Widely expressed in multiple tissues and cell
CC lines. {ECO:0000269|PubMed:19932026}.
CC -!- DOMAIN: The MyMOMA (MYO19-specific mitochondrial outer membrane-
CC association) region mediates association with the mitochondrion outer
CC membrane via electrostatic interaction. {ECO:0000269|PubMed:19932026,
CC ECO:0000269|PubMed:27126804}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92272.1; Type=Erroneous initiation; Evidence={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; AK026518; BAB15495.1; -; mRNA.
DR EMBL; AB209035; BAD92272.1; ALT_INIT; mRNA.
DR EMBL; AC126327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471199; EAW57557.1; -; Genomic_DNA.
DR EMBL; BC008900; AAH08900.1; -; mRNA.
DR CCDS; CCDS45654.1; -. [Q96H55-4]
DR CCDS; CCDS54112.1; -. [Q96H55-1]
DR CCDS; CCDS59283.1; -. [Q96H55-2]
DR RefSeq; NP_001028752.1; NM_001033580.2. [Q96H55-2]
DR RefSeq; NP_001157207.1; NM_001163735.1. [Q96H55-1]
DR RefSeq; NP_079385.2; NM_025109.5. [Q96H55-4]
DR AlphaFoldDB; Q96H55; -.
DR SMR; Q96H55; -.
DR BioGRID; 123161; 285.
DR IntAct; Q96H55; 188.
DR MINT; Q96H55; -.
DR STRING; 9606.ENSP00000479518; -.
DR iPTMnet; Q96H55; -.
DR PhosphoSitePlus; Q96H55; -.
DR BioMuta; MYO19; -.
DR DMDM; 189083208; -.
DR EPD; Q96H55; -.
DR jPOST; Q96H55; -.
DR MassIVE; Q96H55; -.
DR MaxQB; Q96H55; -.
DR PaxDb; Q96H55; -.
DR PeptideAtlas; Q96H55; -.
DR PRIDE; Q96H55; -.
DR ProteomicsDB; 76702; -. [Q96H55-1]
DR ProteomicsDB; 76703; -. [Q96H55-2]
DR ProteomicsDB; 76704; -. [Q96H55-3]
DR ProteomicsDB; 76705; -. [Q96H55-4]
DR Antibodypedia; 73086; 151 antibodies from 24 providers.
DR DNASU; 80179; -.
DR Ensembl; ENST00000610930.4; ENSP00000478437.1; ENSG00000278259.5. [Q96H55-4]
DR Ensembl; ENST00000610992.4; ENSP00000480125.1; ENSG00000278259.5. [Q96H55-3]
DR Ensembl; ENST00000613929.2; ENSP00000478355.1; ENSG00000278372.4. [Q96H55-4]
DR Ensembl; ENST00000614623.5; ENSP00000479518.1; ENSG00000278259.5. [Q96H55-1]
DR Ensembl; ENST00000618519.4; ENSP00000480242.1; ENSG00000278372.4. [Q96H55-1]
DR Ensembl; ENST00000621344.4; ENSP00000477559.1; ENSG00000278259.5. [Q96H55-2]
DR Ensembl; ENST00000633264.1; ENSP00000487617.1; ENSG00000278372.4. [Q96H55-3]
DR Ensembl; ENST00000633938.1; ENSP00000488204.1; ENSG00000278372.4. [Q96H55-2]
DR GeneID; 80179; -.
DR KEGG; hsa:80179; -.
DR MANE-Select; ENST00000614623.5; ENSP00000479518.1; NM_001163735.2; NP_001157207.1.
DR UCSC; uc032fdu.2; human. [Q96H55-1]
DR CTD; 80179; -.
DR DisGeNET; 80179; -.
DR GeneCards; MYO19; -.
DR HGNC; HGNC:26234; MYO19.
DR HPA; ENSG00000278259; Low tissue specificity.
DR MIM; 617379; gene.
DR neXtProt; NX_Q96H55; -.
DR OpenTargets; ENSG00000278259; -.
DR PharmGKB; PA162396512; -.
DR VEuPathDB; HostDB:ENSG00000278259; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000157382; -.
DR HOGENOM; CLU_000192_7_4_1; -.
DR InParanoid; Q96H55; -.
DR OMA; CQLMDDA; -.
DR OrthoDB; 311886at2759; -.
DR PhylomeDB; Q96H55; -.
DR TreeFam; TF328771; -.
DR PathwayCommons; Q96H55; -.
DR Reactome; R-HSA-9013419; RHOT2 GTPase cycle.
DR Reactome; R-HSA-9013425; RHOT1 GTPase cycle.
DR SignaLink; Q96H55; -.
DR BioGRID-ORCS; 80179; 14 hits in 1070 CRISPR screens.
DR ChiTaRS; MYO19; human.
DR GenomeRNAi; 80179; -.
DR Pharos; Q96H55; Tbio.
DR PRO; PR:Q96H55; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96H55; protein.
DR Bgee; ENSG00000278259; Expressed in skin of leg and 171 other tissues.
DR ExpressionAtlas; Q96H55; baseline and differential.
DR Genevisible; Q96H55; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IDA: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:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0032027; F:myosin light chain binding; IEA:Ensembl.
DR GO; GO:0060002; F:plus-end directed microfilament motor activity; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0034642; P:mitochondrion migration along actin filament; IDA:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0090140; P:regulation of mitochondrial fission; IMP: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; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
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; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..970
FT /note="Unconventional myosin-XIX"
FT /id="PRO_0000332969"
FT DOMAIN 35..758
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 759..779
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 824..970
FT /note="MyMOMA region"
FT /evidence="ECO:0000269|PubMed:19932026,
FT ECO:0000269|PubMed:27126804"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 300..317
FT /note="LAGLLHLGNIQFAASEDE -> RRKATPLKFGRDDGQPFA (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033402"
FT VAR_SEQ 318..970
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033403"
FT VAR_SEQ 439..638
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033404"
FT VAR_SEQ 636
FT /note="V -> A (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_033405"
FT VAR_SEQ 637..970
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_033406"
FT VARIANT 176
FT /note="N -> S (in dbSNP:rs2306595)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_043018"
FT VARIANT 203
FT /note="Q -> H (in dbSNP:rs9890918)"
FT /id="VAR_043019"
FT VARIANT 475
FT /note="L -> I (in dbSNP:rs7217346)"
FT /id="VAR_043020"
FT MUTAGEN 135
FT /note="G->R: Rigor-like phenotype due to disruption of ATP-
FT binding. Does not affect localization to mitochondrion."
FT /evidence="ECO:0000269|PubMed:23568824"
FT MUTAGEN 855
FT /note="R->A: Does not affect localization to mitochondrion
FT outer membrane."
FT /evidence="ECO:0000269|PubMed:27126804"
FT MUTAGEN 882..883
FT /note="RK->AA: Abolishes localization to mitochondrion
FT outer membrane."
FT /evidence="ECO:0000269|PubMed:27126804"
FT MUTAGEN 915
FT /note="R->A: Does not affect localization to mitochondrion
FT outer membrane."
FT /evidence="ECO:0000269|PubMed:27126804"
FT MUTAGEN 923
FT /note="K->A: Does not affect localization to mitochondrion
FT outer membrane."
FT /evidence="ECO:0000269|PubMed:27126804"
FT MUTAGEN 927..928
FT /note="RK->AA: Does not affect localization to
FT mitochondrion outer membrane."
FT /evidence="ECO:0000269|PubMed:27126804"
SQ SEQUENCE 970 AA; 109135 MW; 3AB15AD901BE7407 CRC64;
MLQQVNGHNP GSDGQAREYL REDLQEFLGG EVLLYKLDDL TRVNPVTLET VLRCLQARYM
ADTFYTNAGC TLVALNPFKP VPQLYSPELM REYHAAPQPQ KLKPHVFTVG EQTYRNVKSL
IEPVNQSIVV SGESGAGKTW TSRCLMKFYA VVATSPASWE SHKIAERIEQ RILNSNPVME
AFGNACTLRN NNSSRFGKFI QLQLNRAQQM TGAAVQTYLL EKTRVACQAS SERNFHIFYQ
ICKGASEDER LQWHLPEGAA FSWLPNPERS LEEDCFEVTR EAMLHLGIDT PTQNNIFKVL
AGLLHLGNIQ FAASEDEAQP CQPMDDAKYS VRTAASLLGL PEDVLLEMVQ IRTIRAGRQQ
QVFRKPCARA ECDTRRDCLA KLIYARLFDW LVSVINSSIC ADTDSWTTFI GLLDVYGFES
FPDNSLEQLC INYANEKLQQ HFVAHYLRAQ QEEYAVEGLE WSFINYQDNQ PCLDLIEGSP
ISICSLINEE CRLNRPSSAA QLQTRIETAL AGSPCLGHNK LSREPSFIVV HYAGPVRYHT
AGLVEKNKDP IPPELTRLLQ QSQDPLLMGL FPTNPKEKTQ EEPPGQSRAP VLTVVSKFKA
SLEQLLQVLH STTPHYIRCI KPNSQGQAQT FLQEEVLSQL EACGLVETIH ISAAGFPIRV
SHRNFVERYK LLRRLHPCTS SGPDSPYPAK GLPEWCPHSE EATLEPLIQD ILHTLPVLTQ
AAAITGDSAE AMPAPMHCGR TKVFMTDSML ELLECGRARV LEQCARCIQG GWRRHRHREQ
ERQWRAVMLI QAAIRSWLTR KHIQRLHAAA TVIKRAWQKW RIRMACLAAK ELDGVEEKHF
SQAPCSLSTS PLQTRLLEAI IRLWPLGLVL ANTAMGVGSF QRKLVVWACL QLPRGSPSSY
TVQTAQDQAG VTSIRALPQG SIKFHCRKSP LRYADICPEP SPYSITGFNQ ILLERHRLIH
VTSSAFTGLG
