ID W5N7A7_LEPOC Unreviewed; 1866 AA.
AC W5N7A7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=cAMP regulated phosphoprotein 19 {ECO:0000313|Ensembl:ENSLOCP00000016516.1};
GN Name=MYO5A {ECO:0000313|Ensembl:ENSLOCP00000016516.1};
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:ENSLOCP00000016516.1, 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:ENSLOCP00000016516.1}
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|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; AHAT01026108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000016516; -.
DR Ensembl; ENSLOCT00000016546.1; ENSLOCP00000016516.1; ENSLOCG00000013374.1.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG4076; Eukaryota.
DR GeneTree; ENSGT00940000155347; -.
DR HOGENOM; CLU_000192_9_1_1; -.
DR InParanoid; W5N7A7; -.
DR OMA; GKSKHFE; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000013374; 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:0016459; C:myosin complex; IEA:UniProtKB-KW.
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:0048731; P:system development; IEA:UniProt.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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 InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF273; UNCONVENTIONAL MYOSIN-VA; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 5.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 5.
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}; Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT DOMAIN 60..112
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 121..812
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1545..1821
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..714
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1154..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 947..1154
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1361..1450
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1866 AA; 216422 MW; 78600826AAFF2A3C CRC64;
MSGETEETKT IEEATTEEQR EMEDKVISPE KAEEAKLKER YPHLGSKPGG SDFLRKRLQK
GYARVWIPDA EDVWKSAELL KDYKQGDTVL HLQLEDGTEI EHKLDPKTRN LPHLRNPDIL
VGENDLTALS YLHEPAVLHN LKVRFIDSKL IYTYCGIVLV AINPYETLPI YGTDIINAYS
GQNMGDMDPH IFAVAEEAYK QMARDERNQS IIVSGESGAG KTVSAKYAMR YFATVSGSAS
EANVEEKVLA SNPIMEAIGN AKTTRNDNSS RFGKYIEIGF DKRYRIIGAN MRTYLLEKSR
VVFQADEERN YHIFYQLCAS ARLPEFKALK LGSANDFHCT NQGRSPVIDG VDDAKEMVTT
RQAFTLLGIN ESYQMGIFQV LAAILHLGNV AIKDRDSDSS IILPNNVHLT IFCELMGVTY
QDMSHWLCHK KLMTAAETYI KPIPKLQAIN ARDALAKHIY AKLFSWIVDH VNQALHSTVK
QHSFIGVLDI YGFETFEINS FEQFCINYAN EKLQQQFNMH VFKLEQEEYM KEQIPWTLID
FYDNQPCINL IEARLGVLDL LDEECRMPKG TDDTWAQKLY NTHLNKCALF QKPRLSNRAF
IIQHFADKVE YQCEGFLEKN KDTVNEEQIH VLKASKFELL VELFQEEEKV TSPTGAPPGG
RTRLSIKPDK TRHSQSSKEH KKTVGLQFRN SLQLLMDTLN ATTPHYVRCI KPNDHKYPFT
FDPRRAVQQL RACGVLETIR ISAAGFPSRW TYQEFFSRYR VLMKQKDVLS DKKLTCKNVL
EKLIKDQDKY QFGKTKIFFR AGQVAYLEKL RADKLRAACI RIQKTIRCWL MRKKYLRMRS
AAITIQTHIR GYQARCLAKF LRRTRAAIII QKFQRMYVER KRYKRLQASA LIIQCILRAY
MARQKYQAML REHKAIIIQK MVRGWLARQW FKRSLEAIVY LQCCVRRMKA KRELKKLKIE
ARSVEHYKKL NIGMENKIMQ LQRRIDEQHK ENKNMHERLS SLESSYASES EKLRNEVARL
RVTEEEARNN ANRITTLLEE LARLTKELEE TRKEKKTIEE WAEKYRDEME QMVSDLKERN
TLLKSEKDDL NRLIQEQAQQ MKEKMEKALM EETKQLESDL NEERSRYQNL LSEHLRLEER
YDDLKEEMNL AVNVPKPGHK RTDSTHSSNE SEYTYNSEFA ESEEISRGGE DVTKAPWDMS
LFLKLQKRVT ELEQEKQSLQ GELDRKEEQA QRARTRARGA ELEYESLKRQ ELESENKKLK
HDLNEMRKSM SEKTGPGSAV PGSPVYKVLL DQLNSSNEEL EVRKEEVLIL RSQLVSQKEA
MQHKETMTEA MSYIEDVQKM KDAGEITQAY IGLKETNRLL ESQLQTQRKA HENEVEVLRG
ELQGVKEENN RQQQLLAQNL QLPPEARIEA SLQHEITRLT NENLDLMEQL EKQDKTVRKL
KKQLKVFAKK IGELEGGQME NVSPGQTVDE PIRPVNIPRK EKDFQGMLEY KKDDETKLVK
NLILELKPRG VAVNLIPGLP AYILFMCLRH ADYINDDQKV RTLLTSTING IKKILKKRGD
DFETVSFWLS NTCRFLHCLK QYSGEESFMK HNTPRQNDHC LTNFDLAEYR QVLSDLAIQI
YQQLIKCMEN ILHPMIVSGM LEHETIQGVS GVKPTGLRKR TSSIADEGTY TLDSILRQLN
SFHSTMCQHG MDPELIKQVV KQMFYIIGAV TLNNLLLRKD MCSWSKGMQI RYNVSQLEEW
LRDKNLMMSG AKETLEPLIQ AAQLLQVKKK TDEDAEAICS MCNALSTAQI VKVLNLYTPV
NEFEERVSIT FIRTIQTRLR DRKESPQLLM DTKTIYPVTF PFNPSSLALE TIQLPSSLNL
GFLTRV
//