ID A0A2I3T6B6_PANTR Unreviewed; 1273 AA.
AC A0A2I3T6B6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Unconventional myosin-VI {ECO:0000256|ARBA:ARBA00015382};
DE AltName: Full=Unconventional myosin-6 {ECO:0000256|ARBA:ARBA00030027};
GN Name=MYO6 {ECO:0000313|Ensembl:ENSPTRP00000084747.1,
GN ECO:0000313|VGNC:VGNC:11129};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000084747.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000084747.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000084747.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, filopodium
CC {ECO:0000256|ARBA:ARBA00004486}. Cell projection, microvillus
CC {ECO:0000256|ARBA:ARBA00004105}. Cell projection, ruffle membrane
CC {ECO:0000256|ARBA:ARBA00004632}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000256|ARBA:ARBA00004132}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000256|ARBA:ARBA00004150}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00004150}. Membrane, clathrin-coated pit
CC {ECO:0000256|ARBA:ARBA00004600}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; AACZ04027198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04027199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04027200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04027201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04027202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3T6B6; -.
DR Ensembl; ENSPTRT00000091464.1; ENSPTRP00000084747.1; ENSPTRG00000023525.6.
DR VGNC; VGNC:11129; MYO6.
DR GeneTree; ENSGT00940000156078; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000023525; Expressed in adult mammalian kidney and 21 other cell types or tissues.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR CDD; cd21759; CBD_MYO6-like; 1.
DR CDD; cd22294; MYO6_MIU_linker; 1.
DR CDD; cd01382; MYSc_Myo6; 1.
DR CDD; cd21958; MyUb_Myo6; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 6.10.220.10; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR049016; MYO6_lever.
DR InterPro; IPR032412; Myosin-VI_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR036114; MYSc_Myo6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF745; UNCONVENTIONAL MYOSIN-VI; 1.
DR Pfam; PF21521; MYO6_lever; 1.
DR Pfam; PF16521; Myosin-VI_CBD; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hearing {ECO:0000256|ARBA:ARBA00022740};
KW Membrane {ECO:0000256|ARBA:ARBA00023176};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT DOMAIN 2..53
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 57..771
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 651..673
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 934..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1273 AA; 147445 MW; BD520A70FE8683AF CRC64;
MEDGKPVWAP HPTDGFQMGN IVDIGPDSLT IEPLNQKGKT FLALINQVFP AEEDSKKDVE
DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY FDIPKIYSSE AIKSYQGKSL
GTRPPHVFAI ADKAFRDMKV LKMSQSIIVS GESGAGKTEN TKFVLRYLTE SYGTGQDIDD
RIVEANPLLE AFGNAKTVRN NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK
EERNYHIFYR LCAGASEDIR EKLHLSSPDN FRYLNRGCTR YFANKETDKQ ILQNRKSPEY
LKAGSMKDPL LDDHGDFIRM CTAMKKIGLD DEEKLDLFRV VAGVLHLGNI DFEEAGSTSG
GCNLKNKSTQ SLEYCAELLG LDQDDLRVSL TTRVMLTTAG GTKGTVIKVP LKVEQANNAR
DALAKTVYSH LFDHVVNRVN QCFPFETSSY FIGVLDIAGF EYFEHNSFEQ FCINYCNEKL
QQFFNERILK EEQELYQKEG LGVNEVHYVD NQDCIDLIEA KLVGILDILD EENRLPQPSD
QHFTSAVHQK HKDHFRLTIP RKSKLAVHRN IRDDEGFIIR HFAGAVCYET TQFVEKNNDA
LHMSLESLIC ESRDKFIREL FESSTNNNKD TKQKAGKLSF ISVGNKFKTQ LNLLLDKLRS
TGASFIRCIK PNLKMTSHHF EGAQILSQLQ CSGMVSVLDL MQGGYPSRAS FHELYNMYKK
YMPDKLARLD PRLFCKALFK ALGLNENDYK FGLTKVFFRP GKFAEFDQIM KSDPDHLAEL
VKRVNHWLTC SRWKKVQWCS LSVIKLKNKI KYRAEACIKM QKTIRMWLCK RRHKPRIDGL
VKVGTLKKRL DKFNEVVSVL KDGKPEMNKQ IKDLEISIDA LMAKIKSTMM TQEQIQKEYD
ALVKSSEELL SALQKKKQQE EEAERLRRIQ EEMEKERKRR EEDEKRRRKE EEERRMKLEM
EAKRKQEEEE RKKREDDEKR IQAEVEAQLA RQREEESQQQ AVLEQERRDR ELALRIAQSE
AELISDEAQA DLALRRYWGP WVGEQMAKEM SEFLSRGPAV QATKAAAGTK KYDLSKWKYA
ELRDTINTSC DIELLAACRE EFHRRLKVYH AWKSKNKKRN TETEQRAPKS VTDYAQQNPA
AQIPARQQEI EMNRQQRFFR IPFIRPADQY KDPQSKKKGW WYAHFDGPWI ARQMELHPDK
PPILLVAGKD DMEMCELNLE ETGLTRKRGA EILPRQFEEI WERCGGIQYL QNAIESRQAR
PTYATAMLQS LLK
//
