ID Q9I8D1; PN Unconventional myosin-VI; GN MYO6; OS 9031; SL Nucleus Position: SL-0198; SL Comments: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11447109}; Peripheral membrane protein {ECO:0000269|PubMed:11447109}. Golgi apparatus {ECO:0000269|PubMed:11447109, ECO:0000269|PubMed:15837803}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, ruffle membrane {ECO:0000269|PubMed:11447109}. Cell projection, microvillus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29122}. Note=Also present in endocyctic vesicles (By similarity). Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage (By similarity). Recruited into membrane ruffles from cell surface by EGF- stimulation (By similarity). Colocalizes with DAB2 in clathrin-coated pits/vesicles (By similarity). Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (PubMed:15837803). {ECO:0000250|UniProtKB:Q9UM54, ECO:0000269|PubMed:15837803}. [Isoform 1]: Cytoplasmic vesicle, clathrin-coated vesicle membrane. DR UNIPROT: Q9I8D1; DR Pfam: PF16521; DR Pfam: PF00063; DR PROSITE: PS50096; DR PROSITE: PS51456; DR PROSITE: PS51844; DE Function: Myosins are actin-based motor molecules with ATPase activity (By similarity). Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (By similarity). Has slow rate of actin-activated ADP release due to weak ATP binding (By similarity). Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway (By similarity). Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (By similarity). Together with TOM1, mediates delivery of endocytic cargo to autophagosomes thereby promoting autophagosome maturation and driving fusion with lysosomes (By similarity). Links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (By similarity). May act as a regulator of F-actin dynamics (By similarity). May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity). May play a role in the extension and network organization of neurites (By similarity). Modulates RNA polymerase II- dependent transcription (By similarity). {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q64331, ECO:0000250|UniProtKB:Q9UM54}. DE Reference Proteome: Yes; DE Interaction: P98082; IntAct: EBI-6307290; Score: 0.37 DE Interaction: P97318; IntAct: EBI-6307483; Score: 0.40 DE Interaction: P98078; IntAct: EBI-6307422; Score: 0.40 DE Interaction: O88797; IntAct: EBI-6307558; Score: 0.27 GO GO:0015629; GO GO:0005884; GO GO:0005938; GO GO:0005905; GO GO:0030136; GO GO:0030665; GO GO:0005737; GO GO:0031410; GO GO:0005829; GO GO:0030139; GO GO:0031941; GO GO:0030175; GO GO:0005794; GO GO:0005902; GO GO:0016459; GO GO:0031965; GO GO:0005654; GO GO:0005634; GO GO:0048471; GO GO:0005886; GO GO:0016591; GO GO:0001726; GO GO:0032587; GO GO:0003779; GO GO:0051015; GO GO:0043531; GO GO:0005524; GO GO:0005516; GO GO:0003774; GO GO:0000146; GO GO:0060002; GO GO:0007015; GO GO:0030048; GO GO:0030330; GO GO:0006897; GO GO:0042491; GO GO:0042472; GO GO:0006886; GO GO:0045944; GO GO:0051046; GO GO:0007605; GO GO:0030050; TP Membrane Topology: Peripheral; Source: UniProt - Experimental Evidence {ECO:0000269|PubMed:11447109}; SQ MEDGKPVWAPHPTDGFQMGMIVDIGTDYLTIEPLNQKGKTFQAAINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVR SQ YSKDRIYTYVANILIAVNPYFDIPKFYSSDAIKKYQGRSLGTLPPHVFAIADKAYRDMKVLKMSQSIIVSGESGAGKTEN SQ TKFVLRYLTESYGTGQDIDDRIVEANPLLEAFGNAKTIRNNNSSRFGKFVEIHFNEKNSVVGGFVSHYLLEKSRICVQGK SQ EERNYHIFYRLCAGAPEDIREKLYLSSPDSFRYLNRGCTRYFATKETDKQILQNRKSPEYLKAGSLKDPLLDDHGDFNRM SQ CTAMKKIGLDDAEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCTLKAQSQPALECCAALLGLDEEDLRVSLTTRVMLTTAG SQ GAKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSFFIGVLDIAGFEYFEHNSFEQFCINYCNEKL SQ QQFFNERILKEEQELYQKEGLGVNEVRYVDNQDCIDLIEAKLIGVLDILDEENRLPQPSDQHFTSVVHQKHKDHFRLSIP SQ RKSKLAVHRNVRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESKDKFVRQLFESNTNNNKDPKQKAGKLSF SQ ISVGNKFKTQLNLLLEKLHSTGSSFIRCIFPNLKMTSHHFEGGQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKK SQ YLPEKLARLDPRLFCKALFKALGLNEIDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNHWLICSRWKKVQWCS SQ LSVIKLKNKIKYRASACIKIQKTIRMWLCKRKHKPRIDGLIKVRTLKKRLDKFNEVVSALKEGKAETSKQIKELEYSIDA SQ SMTKIKTTMMTREQIMKEYDALVRSSEQLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEEEKRRRKEEEERRLKSEI SQ EAKRKQEEEERKKREEEEKRIQAEIEAQLAREREEETQHQAILEQERRDRELAMRIAQTGAELSTEETKLDVGLCRANGT SQ KLQMTAEQMAKEMSEMLSRGPAVQATKAAAGAKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNK SQ KRNAETEQRAPKSVTDYAQQNPTAQLPMRQQEIEINRQQRYFRIPFIRPMDQYKDPQNKKKGWWYAHFDGPWIARQMELH SQ PDKAPILLVAGKDDMDMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQNAIESRQARPTYATAMLQNLLK //