ID W5N887_LEPOC Unreviewed; 1105 AA.
AC W5N887;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Myosin IEa {ECO:0000313|Ensembl:ENSLOCP00000016846.1};
GN Name=MYO1E {ECO:0000313|Ensembl:ENSLOCP00000016846.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016846.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016846.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; AHAT01024868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01024869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01024870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N887; -.
DR STRING; 7918.ENSLOCP00000016846; -.
DR Ensembl; ENSLOCT00000016876.1; ENSLOCP00000016846.1; ENSLOCG00000013657.1.
DR eggNOG; KOG0162; Eukaryota.
DR GeneTree; ENSGT00940000157461; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; W5N887; -.
DR OMA; RFEEKTH; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000013657; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0003094; P:glomerular filtration; IEA:Ensembl.
DR GO; GO:0032835; P:glomerulus development; IEA:Ensembl.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd11827; SH3_MyoIe_If_like; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035507; Ie/If_SH3.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF341; UNCONVENTIONAL MYOSIN-IE; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 19..682
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 720..912
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1048..1105
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 559..581
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 908..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1105 AA; 126417 MW; F76A8CCF4506C1F6 CRC64;
QGSKGHYRYH WQSHNVKQSG VDDMVLLTKI NEDAIVENLK KRYMDDYIFT YIGPVLISVN
PFKQMPYFGD KEVEMYQGAA QYENPPHIYA LADNMYRNMM IDRENQCVII SGESGAGKTV
AAKYIMSYIS RVSGGGSKVQ HVKDIILQSN PLLEAFGNAK TLRNNNSSRF GKYFEIQFSS
GGEPDGGKIS NFLLEKSRVV MRNPGERSFH IFYQLIEGAS GDQRSSLGIT SLDYYNYLNQ
SGSYKVEDIN DKSDFQETMH AMNVIGIRSE EQMQVLQIVA GVLHLGNITF KESGNYAAVE
SEEFLAFPAF LLGIDQSRLK EKLTSRKMDS KWGGKSESID VTLNVEQACY TRDALSKALH
ARVFDYLVES INKAMVKDHQ DYNIGVLDIY GFEIFQKNGF EQFCINFVNE KLQQIFIELT
LKAEQEEYIQ EGIRWTPIDY FNNKIVCDLI ESKIFSPHCV TSIHDKAESQ DKAILGLIRC
PLSVHFILAL CTILNSSRSL ELQQREHFCC KVKHQLIYCI PVPRSASSQV SFCFTAAAPR
SVVIELSFPP PDIHSQKQAN DLVSTLVKCT PHYIRCIKPN ETKKPRDWEE GRVKHQVEYL
GLKENIRVRR AGYAYRRVFR KFLNRYAILT KESWPTWRGD EKQGVLHLLR SVNMDQDQFQ
LGRTKIFIKA PESLFLLEET RERKFDGYAR AIQKAWRKYQ ARKKYVQMRE EASDLLLNRK
ERRRHSINRN FVGDYLGMDD RPELRQFLAK REKIDFADKV TKYDRRFKGV KRDLVLTPRC
VYLIGREKVK QGPDKGQVTE VLKRRVEVEK ILAISLSTMQ DDFLILHEQE YDSLLECIFK
TEFISLLSKR FEEKTHRTLP LKFGTILEMK LKKESWGPWS AGGTRQVQFV QGQGDVAVLN
PTNKMLQVSI GPGLPKNTRP TRKNFSQSRS VSRAPQSYPT RAAPGPPASH QNGVIKSAGN
NVSQRAAPTN HPSHHPTFLP PPVTLHQLKQ RNSRPPQPDL DCLRVPDQGA AGNRQRLPTE
SGRTAHRQTT SRPMPGGGRP KPLPKPKPQV PQCKALYAYD AQDTDELSFN ADDVIEIVKE
DASGWWTGRL RGKQGLFPNN YVSKL
//
