MYO5A_CHICK
ID MYO5A_CHICK Reviewed; 1829 AA.
AC Q02440;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Unconventional myosin-Va;
DE AltName: Full=Dilute myosin heavy chain, non-muscle;
DE AltName: Full=Myosin heavy chain p190;
DE AltName: Full=Myosin-V;
GN Name=MYO5A;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1383040; DOI=10.1016/0014-5793(92)81123-4;
RA Sanders G., Lichte B., Meyer H.E., Kilimann M.W.;
RT "cDNA encoding the chicken ortholog of the mouse dilute gene product.
RT Sequence comparison reveals a myosin I subfamily with conserved C-terminal
RT domains.";
RL FEBS Lett. 311:295-298(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1154-1163.
RC TISSUE=Brain;
RX PubMed=1469047; DOI=10.1083/jcb.119.6.1541;
RA Espreafico E.M., Cheney R.E., Matteoli M., Nascimento A.A.,
RA de Camilli P.V., Larson R.E., Mooseker M.S.;
RT "Primary structure and cellular localization of chicken brain myosin-V
RT (p190), an unconventional myosin with calmodulin light chains.";
RL J. Cell Biol. 119:1541-1557(1992).
CC -!- FUNCTION: Processive actin-based motor that can move in large steps
CC approximating the 36-nm pseudo-repeat of the actin filament. Involved
CC in melanosome transport. Also mediates the transport of vesicles to the
CC plasma membrane. May also be required for some polarization process
CC involved in dendrite formation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: May be a homodimer, which associates with multiple calmodulin
CC or myosin light chains. {ECO:0000250}.
CC -!- INTERACTION:
CC Q02440; P14649: MYL6B; Xeno; NbExp=2; IntAct=EBI-1040586, EBI-358570;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Neuronal and non-neuronal cells of the brain.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; X67251; CAA47673.1; -; mRNA.
DR EMBL; Z11718; CAA77782.1; -; mRNA.
DR PIR; S19188; S19188.
DR RefSeq; NP_990631.1; NM_205300.1.
DR PDB; 1OE9; X-ray; 2.05 A; A=1-792.
DR PDB; 1W7I; X-ray; 3.00 A; A=1-792.
DR PDB; 1W7J; X-ray; 2.00 A; A=1-792.
DR PDB; 1W8J; X-ray; 2.70 A; A/B/C/D=1-766.
DR PDB; 2DFS; EM; 24.00 A; A/M=1-1080.
DR PDB; 7PLT; EM; 3.30 A; A=1-792.
DR PDB; 7PLU; EM; 3.20 A; A/D=1-792.
DR PDB; 7PLV; EM; 3.50 A; A=1-792.
DR PDB; 7PLW; EM; 3.50 A; A=1-792.
DR PDB; 7PLX; EM; 3.60 A; A=1-792.
DR PDB; 7PLY; EM; 3.20 A; A=1-792.
DR PDB; 7PLZ; EM; 3.20 A; A/D=1-792.
DR PDB; 7PM0; EM; 3.60 A; A=1-792.
DR PDB; 7PM1; EM; 3.50 A; A=1-792.
DR PDB; 7PM2; EM; 3.60 A; A=1-792.
DR PDB; 7PM5; EM; 3.10 A; A=1-792.
DR PDB; 7PM6; EM; 3.00 A; A/D=1-792.
DR PDB; 7PM7; EM; 3.50 A; A=1-792.
DR PDB; 7PM8; EM; 3.50 A; A=1-792.
DR PDB; 7PM9; EM; 3.70 A; A=1-792.
DR PDB; 7PMA; EM; 3.60 A; A=1-792.
DR PDB; 7PMB; EM; 3.60 A; A=1-792.
DR PDB; 7PMC; EM; 3.70 A; A=1-792.
DR PDB; 7PMD; EM; 2.90 A; A=1-792.
DR PDB; 7PME; EM; 2.90 A; A/D=1-792.
DR PDB; 7PMF; EM; 3.40 A; A=1-792.
DR PDB; 7PMG; EM; 3.30 A; A=1-792.
DR PDB; 7PMH; EM; 3.40 A; A=1-792.
DR PDB; 7PMI; EM; 3.30 A; A=1-792.
DR PDB; 7PMJ; EM; 3.40 A; A=1-792.
DR PDB; 7PML; EM; 3.30 A; A=1-792.
DR PDBsum; 1OE9; -.
DR PDBsum; 1W7I; -.
DR PDBsum; 1W7J; -.
DR PDBsum; 1W8J; -.
DR PDBsum; 2DFS; -.
DR PDBsum; 7PLT; -.
DR PDBsum; 7PLU; -.
DR PDBsum; 7PLV; -.
DR PDBsum; 7PLW; -.
DR PDBsum; 7PLX; -.
DR PDBsum; 7PLY; -.
DR PDBsum; 7PLZ; -.
DR PDBsum; 7PM0; -.
DR PDBsum; 7PM1; -.
DR PDBsum; 7PM2; -.
DR PDBsum; 7PM5; -.
DR PDBsum; 7PM6; -.
DR PDBsum; 7PM7; -.
DR PDBsum; 7PM8; -.
DR PDBsum; 7PM9; -.
DR PDBsum; 7PMA; -.
DR PDBsum; 7PMB; -.
DR PDBsum; 7PMC; -.
DR PDBsum; 7PMD; -.
DR PDBsum; 7PME; -.
DR PDBsum; 7PMF; -.
DR PDBsum; 7PMG; -.
DR PDBsum; 7PMH; -.
DR PDBsum; 7PMI; -.
DR PDBsum; 7PMJ; -.
DR PDBsum; 7PML; -.
DR AlphaFoldDB; Q02440; -.
DR SMR; Q02440; -.
DR IntAct; Q02440; 1.
DR STRING; 9031.ENSGALP00000038276; -.
DR BindingDB; Q02440; -.
DR ChEMBL; CHEMBL1781866; -.
DR PaxDb; Q02440; -.
DR PRIDE; Q02440; -.
DR GeneID; 396237; -.
DR KEGG; gga:396237; -.
DR CTD; 4644; -.
DR VEuPathDB; HostDB:geneid_396237; -.
DR eggNOG; KOG0160; Eukaryota.
DR InParanoid; Q02440; -.
DR OrthoDB; 311886at2759; -.
DR PhylomeDB; Q02440; -.
DR EvolutionaryTrace; Q02440; -.
DR PRO; PR:Q02440; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; NAS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0060001; F:minus-end directed microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR CDD; cd15478; Myo5a_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR037988; Myo5a_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 6.
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; SSF52540; 3.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
KW Direct protein sequencing; Golgi apparatus; Membrane; Motor protein;
KW Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1829
FT /note="Unconventional myosin-Va"
FT /id="PRO_0000123459"
FT DOMAIN 8..60
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 69..764
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 767..789
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 790..814
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 815..837
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 838..862
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 863..887
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 888..915
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1508..1784
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 599..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..666
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 1106..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 916..1239
FT /evidence="ECO:0000255"
FT COILED 1315..1419
FT /evidence="ECO:0000255"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 1734
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CONFLICT 1142
FT /note="E -> EQ (in Ref. 2; CAA77782)"
FT /evidence="ECO:0000305"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:7PMJ"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:1W7J"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:1W7J"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7PLY"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:7PMD"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:7PLU"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1OE9"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1OE9"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:7PM8"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:1W7J"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:1W7J"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 319..336
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 368..375
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 393..423
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:1OE9"
FT HELIX 449..479
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 493..500
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:7PMH"
FT HELIX 505..513
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:1W7I"
FT HELIX 520..531
FT /evidence="ECO:0007829|PDB:1W7J"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:7PMD"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 564..569
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 574..581
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:7PMG"
FT HELIX 588..591
FT /evidence="ECO:0007829|PDB:1W7J"
FT TURN 629..633
FT /evidence="ECO:0007829|PDB:1W8J"
FT HELIX 636..652
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 654..662
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 675..684
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 687..696
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 704..711
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 712..714
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 724..735
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 739..741
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:1W7J"
FT STRAND 746..751
FT /evidence="ECO:0007829|PDB:1W7J"
FT HELIX 755..791
FT /evidence="ECO:0007829|PDB:1W7J"
SQ SEQUENCE 1829 AA; 212383 MW; 0538B278DFC09F6E CRC64;
MAASELYTKY ARVWIPDPEE VWKSAELLKD YKPGDKVLQL RLEEGKDLEY CLDPKTKELP
PLRNPDILVG ENDLTALSYL HEPAVLHNLK VRFIDSKLIY TYCGIVLVAI NPYEQLPIYG
EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM ARDERNQSII VSGESGAGKT VSAKYAMRYF
ATVSGSASEA NVEEKVLASN PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR
TYLLEKSRVV FQAEEERNYH IFYQLCASAA LPEFKTLRLG NANYFHYTKQ GGSPVIDGID
DAKEMVNTRQ ACTLLGISDS YQMGIFRILA GILHLGNVEF ASRDSDSCAI PPKHDPLTIF
CDLMGVDYEE MAHWLCHRKL ATATETYIKP ISKLHAINAR DALAKHIYAN LFNWIVDHVN
KALHSTVKQH SFIGVLDIYG FETFEINSFE QFCINYANEK LQQQFNMHVF KLEQEEYMKE
QIPWTLIDFY DNQPCINLIE AKMGVLDLLD EECKMPKGSD DTWAQKLYNT HLNKCALFEK
PRLSNKAFII KHFADKVEYQ CEGFLEKNKD TVYEEQIKVL KSSKKFKLLP ELFQDEEKAI
SPTSATPSGR VPLSRTPVKP AKARPGQTSK EHKKTVGHQF RNSLHLLMET LNATTPHYVR
CIKPNDFKFP FTFDEKRAVQ QLRACGVLET IRISAAGFPS RWTYQEFFSR YRVLMKQKDV
LSDRKQTCKN VLEKLILDKD KYQFGKTKIF FRAGQVAYLE KIRADKLRAA CIRIQKTIRG
WLMRKKYMRM RRAAITIQRY VRGHQARCYA TFLRRTRAAI IIQKFQRMYV VRKRYQCMRD
ATIALQALLR GYLVRNKYQM MLREHKSIII QKHVRGWLAR VHYHRTLKAI VYLQCCYRRM
MAKRELKKLK IEARSVERYK KLHIGLENKI MQLQRKIDEQ NKEYKSLLEK MNNLEITYST
ETEKLRSDVE RLRMSEEEAK NATNRVLSLQ EEIAKLRKEL HQTQTEKKTI EEWADKYKHE
TEQLVSELKE QNTLLKTEKE ELNRRIHDQA KEITETMEKK LVEETKQLEL DLNDERLRYQ
NLLNEFSRLE ERYDDLKDEM NLMVSIPKPG HKRTDSTHSS NESEYTFSSE ITEAEDLPLR
MEEPSEKKAP LDMSLFLKLQ KRVTELEQEK QSLQDELDRK EEQALRAKAK EEERPPIRGA
ELEYESLKRQ ELESENKKLK NELNELQKAL TETRAPEVTA PGAPAYRVLL DQLTSVSEEL
EVRKEEVLIL RSQLVSQKEA IQPKEDKNTM TDSTILLEDV QKMKDKGEIA QAYIGLKETN
RLLESQLQSQ KKSHENELES LRGEIQSLKE ENNRQQQLLA QNLQLPPEAR IEASLQHEIT
RLTNENLDLM EQLEKQDKTV RKLKKQLKVF AKKIGELEVG QMENISPGQI IDEPIRPVNI
PRKEKDFQGM LEYKKEDEQK LVKNLILELK PRGVAVNLIP GLPAYILFMC VRHADYLNDD
QKVRSLLTST INGIKKVLKK RGDDFETVSF WLSNTCRFLH CLKQYSGEEG FMKHNTPRQN
EHCLTNFDLA EYRQVLSDLA IQIYQQLVRV LENILQPMIV SGMLEHETIQ GVSGVKPTGL
RKRTSSIADE GTYTLDSIIR QLNSFHSVMC QHGMDPELIK QVVKQMFYII GAVTLNNLLL
RKDMCSWSKG MQIRYNVSQL EEWLRDKNLM NSGAKETLEP LIQAAQLLQV KKKTDEDAEA
ICSMCNALTT AQIVKVLNLY TPVNEFEERV LVSFIRTIQL RLRDRKDSPQ LLMDAKHIFP
VTFPFNPSSL ALETIQIPAS LGLGFISRV
