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Protein

Unconventional myosin-Va

Gene

MYO5A

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi163 – 170ATPBy similarity8

GO - Molecular functioni

  • actin filament binding Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: UniProtKB
  • microfilament motor activity Source: UniProtKB
  • microtubule binding Source: InterPro
  • microtubule motor activity Source: InterPro
  • minus-end directed microfilament motor activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionActin-binding, Calmodulin-binding, Motor protein, Myosin
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-Va
Alternative name(s):
Dilute myosin heavy chain, non-muscle
Myosin heavy chain p190
Myosin-V
Gene namesi
Name:MYO5A
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1781866

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001234591 – 1829Unconventional myosin-VaAdd BLAST1829

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1734PhosphothreonineSequence analysis1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ02440
PRIDEiQ02440

Expressioni

Tissue specificityi

Neuronal and non-neuronal cells of the brain.

Interactioni

Subunit structurei

May be a homodimer, which associates with multiple calmodulin or myosin light chains.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MYL6BP146492EBI-1040586,EBI-358570From Homo sapiens.

GO - Molecular functioni

  • actin filament binding Source: InterPro
  • calmodulin binding Source: UniProtKB
  • microtubule binding Source: InterPro

Protein-protein interaction databases

IntActiQ02440, 1 interactor
STRINGi9031.ENSGALP00000007352

Chemistry databases

BindingDBiQ02440

Structurei

Secondary structure

11829
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Beta strandi12 – 17Combined sources6
Turni18 – 20Combined sources3
Beta strandi21 – 29Combined sources9
Beta strandi36 – 41Combined sources6
Beta strandi43 – 51Combined sources9
Turni54 – 57Combined sources4
Helixi66 – 68Combined sources3
Beta strandi72 – 74Combined sources3
Helixi82 – 96Combined sources15
Beta strandi100 – 103Combined sources4
Beta strandi106 – 110Combined sources5
Beta strandi117 – 120Combined sources4
Helixi121 – 127Combined sources7
Helixi132 – 134Combined sources3
Helixi139 – 153Combined sources15
Beta strandi157 – 162Combined sources6
Helixi169 – 183Combined sources15
Beta strandi187 – 190Combined sources4
Helixi192 – 207Combined sources16
Beta strandi208 – 211Combined sources4
Beta strandi214 – 218Combined sources5
Beta strandi220 – 228Combined sources9
Beta strandi234 – 242Combined sources9
Helixi246 – 249Combined sources4
Helixi260 – 267Combined sources8
Turni268 – 270Combined sources3
Helixi272 – 277Combined sources6
Turni282 – 284Combined sources3
Helixi286 – 289Combined sources4
Helixi301 – 314Combined sources14
Helixi319 – 336Combined sources18
Beta strandi341 – 344Combined sources4
Beta strandi347 – 349Combined sources3
Helixi355 – 364Combined sources10
Helixi368 – 375Combined sources8
Beta strandi376 – 381Combined sources6
Beta strandi386 – 390Combined sources5
Helixi393 – 423Combined sources31
Beta strandi430 – 437Combined sources8
Beta strandi445 – 447Combined sources3
Helixi449 – 479Combined sources31
Helixi484 – 486Combined sources3
Helixi493 – 500Combined sources8
Helixi505 – 513Combined sources9
Beta strandi515 – 517Combined sources3
Helixi520 – 531Combined sources12
Turni532 – 534Combined sources3
Beta strandi545 – 551Combined sources7
Beta strandi556 – 560Combined sources5
Helixi564 – 569Combined sources6
Helixi574 – 581Combined sources8
Helixi588 – 591Combined sources4
Turni629 – 633Combined sources5
Helixi636 – 652Combined sources17
Beta strandi654 – 662Combined sources9
Helixi675 – 684Combined sources10
Helixi687 – 696Combined sources10
Beta strandi700 – 703Combined sources4
Helixi704 – 711Combined sources8
Helixi712 – 714Combined sources3
Helixi717 – 719Combined sources3
Helixi724 – 735Combined sources12
Helixi739 – 741Combined sources3
Beta strandi742 – 744Combined sources3
Beta strandi746 – 751Combined sources6
Helixi755 – 791Combined sources37

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OE9X-ray2.05A1-792[»]
1W7IX-ray3.00A1-792[»]
1W7JX-ray2.00A1-792[»]
1W8JX-ray2.70A/B/C/D1-766[»]
2DFSelectron microscopy24.00A/M1-1080[»]
ProteinModelPortaliQ02440
SMRiQ02440
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02440

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 60Myosin N-terminal SH3-likePROSITE-ProRule annotationAdd BLAST53
Domaini69 – 764Myosin motorPROSITE-ProRule annotationAdd BLAST696
Domaini767 – 789IQ 1PROSITE-ProRule annotationAdd BLAST23
Domaini790 – 814IQ 2PROSITE-ProRule annotationAdd BLAST25
Domaini815 – 837IQ 3PROSITE-ProRule annotationAdd BLAST23
Domaini838 – 862IQ 4PROSITE-ProRule annotationAdd BLAST25
Domaini863 – 887IQ 5PROSITE-ProRule annotationAdd BLAST25
Domaini888 – 915IQ 6PROSITE-ProRule annotationAdd BLAST28
Domaini1508 – 1784DilutePROSITE-ProRule annotationAdd BLAST277

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni644 – 666Actin-bindingSequence analysisAdd BLAST23

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili916 – 1239Sequence analysisAdd BLAST324
Coiled coili1315 – 1419Sequence analysisAdd BLAST105

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0160 Eukaryota
KOG0161 Eukaryota
COG5022 LUCA
HOGENOMiHOG000171839
HOVERGENiHBG052556
InParanoidiQ02440
KOiK10357
PhylomeDBiQ02440

Family and domain databases

CDDicd15478 Myo5a_CBD, 1 hit
cd01380 MYSc_Myo5, 1 hit
Gene3Di2.30.30.360, 1 hit
3.40.850.10, 3 hits
InterProiView protein in InterPro
IPR002710 Dilute_dom
IPR000048 IQ_motif_EF-hand-BS
IPR036961 Kinesin_motor_dom_sf
IPR037988 Myo5a_CBD
IPR001609 Myosin_head_motor_dom
IPR008989 Myosin_S1_N
IPR036103 MYSc_Myo5
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF01843 DIL, 1 hit
PF00612 IQ, 6 hits
PF00063 Myosin_head, 1 hit
PRINTSiPR00193 MYOSINHEAVY
SMARTiView protein in SMART
SM01132 DIL, 1 hit
SM00015 IQ, 6 hits
SM00242 MYSc, 1 hit
SUPFAMiSSF52540 SSF52540, 3 hits
PROSITEiView protein in PROSITE
PS51126 DILUTE, 1 hit
PS50096 IQ, 6 hits
PS51456 MYOSIN_MOTOR, 1 hit
PS51844 SH3_LIKE, 1 hit

Sequencei

Sequence statusi: Complete.

Q02440-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASELYTKY ARVWIPDPEE VWKSAELLKD YKPGDKVLQL RLEEGKDLEY
60 70 80 90 100
CLDPKTKELP PLRNPDILVG ENDLTALSYL HEPAVLHNLK VRFIDSKLIY
110 120 130 140 150
TYCGIVLVAI NPYEQLPIYG EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM
160 170 180 190 200
ARDERNQSII VSGESGAGKT VSAKYAMRYF ATVSGSASEA NVEEKVLASN
210 220 230 240 250
PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR TYLLEKSRVV
260 270 280 290 300
FQAEEERNYH IFYQLCASAA LPEFKTLRLG NANYFHYTKQ GGSPVIDGID
310 320 330 340 350
DAKEMVNTRQ ACTLLGISDS YQMGIFRILA GILHLGNVEF ASRDSDSCAI
360 370 380 390 400
PPKHDPLTIF CDLMGVDYEE MAHWLCHRKL ATATETYIKP ISKLHAINAR
410 420 430 440 450
DALAKHIYAN LFNWIVDHVN KALHSTVKQH SFIGVLDIYG FETFEINSFE
460 470 480 490 500
QFCINYANEK LQQQFNMHVF KLEQEEYMKE QIPWTLIDFY DNQPCINLIE
510 520 530 540 550
AKMGVLDLLD EECKMPKGSD DTWAQKLYNT HLNKCALFEK PRLSNKAFII
560 570 580 590 600
KHFADKVEYQ CEGFLEKNKD TVYEEQIKVL KSSKKFKLLP ELFQDEEKAI
610 620 630 640 650
SPTSATPSGR VPLSRTPVKP AKARPGQTSK EHKKTVGHQF RNSLHLLMET
660 670 680 690 700
LNATTPHYVR CIKPNDFKFP FTFDEKRAVQ QLRACGVLET IRISAAGFPS
710 720 730 740 750
RWTYQEFFSR YRVLMKQKDV LSDRKQTCKN VLEKLILDKD KYQFGKTKIF
760 770 780 790 800
FRAGQVAYLE KIRADKLRAA CIRIQKTIRG WLMRKKYMRM RRAAITIQRY
810 820 830 840 850
VRGHQARCYA TFLRRTRAAI IIQKFQRMYV VRKRYQCMRD ATIALQALLR
860 870 880 890 900
GYLVRNKYQM MLREHKSIII QKHVRGWLAR VHYHRTLKAI VYLQCCYRRM
910 920 930 940 950
MAKRELKKLK IEARSVERYK KLHIGLENKI MQLQRKIDEQ NKEYKSLLEK
960 970 980 990 1000
MNNLEITYST ETEKLRSDVE RLRMSEEEAK NATNRVLSLQ EEIAKLRKEL
1010 1020 1030 1040 1050
HQTQTEKKTI EEWADKYKHE TEQLVSELKE QNTLLKTEKE ELNRRIHDQA
1060 1070 1080 1090 1100
KEITETMEKK LVEETKQLEL DLNDERLRYQ NLLNEFSRLE ERYDDLKDEM
1110 1120 1130 1140 1150
NLMVSIPKPG HKRTDSTHSS NESEYTFSSE ITEAEDLPLR MEEPSEKKAP
1160 1170 1180 1190 1200
LDMSLFLKLQ KRVTELEQEK QSLQDELDRK EEQALRAKAK EEERPPIRGA
1210 1220 1230 1240 1250
ELEYESLKRQ ELESENKKLK NELNELQKAL TETRAPEVTA PGAPAYRVLL
1260 1270 1280 1290 1300
DQLTSVSEEL EVRKEEVLIL RSQLVSQKEA IQPKEDKNTM TDSTILLEDV
1310 1320 1330 1340 1350
QKMKDKGEIA QAYIGLKETN RLLESQLQSQ KKSHENELES LRGEIQSLKE
1360 1370 1380 1390 1400
ENNRQQQLLA QNLQLPPEAR IEASLQHEIT RLTNENLDLM EQLEKQDKTV
1410 1420 1430 1440 1450
RKLKKQLKVF AKKIGELEVG QMENISPGQI IDEPIRPVNI PRKEKDFQGM
1460 1470 1480 1490 1500
LEYKKEDEQK LVKNLILELK PRGVAVNLIP GLPAYILFMC VRHADYLNDD
1510 1520 1530 1540 1550
QKVRSLLTST INGIKKVLKK RGDDFETVSF WLSNTCRFLH CLKQYSGEEG
1560 1570 1580 1590 1600
FMKHNTPRQN EHCLTNFDLA EYRQVLSDLA IQIYQQLVRV LENILQPMIV
1610 1620 1630 1640 1650
SGMLEHETIQ GVSGVKPTGL RKRTSSIADE GTYTLDSIIR QLNSFHSVMC
1660 1670 1680 1690 1700
QHGMDPELIK QVVKQMFYII GAVTLNNLLL RKDMCSWSKG MQIRYNVSQL
1710 1720 1730 1740 1750
EEWLRDKNLM NSGAKETLEP LIQAAQLLQV KKKTDEDAEA ICSMCNALTT
1760 1770 1780 1790 1800
AQIVKVLNLY TPVNEFEERV LVSFIRTIQL RLRDRKDSPQ LLMDAKHIFP
1810 1820
VTFPFNPSSL ALETIQIPAS LGLGFISRV
Length:1,829
Mass (Da):212,383
Last modified:June 1, 1994 - v1
Checksum:i0538B278DFC09F6E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1142E → EQ in CAA77782 (PubMed:1469047).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67251 mRNA Translation: CAA47673.1
Z11718 mRNA Translation: CAA77782.1
PIRiS19188
RefSeqiNP_990631.1, NM_205300.1
UniGeneiGga.3550

Genome annotation databases

GeneIDi396237
KEGGigga:396237

Similar proteinsi

Entry informationi

Entry nameiMYO5A_CHICK
AccessioniPrimary (citable) accession number: Q02440
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: March 28, 2018
This is version 132 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health