MYO3/YKL129C Protein Information

Standard Name	Myo3p 1
Systematic Name	Ykl129cp
ORF Classification	Verified
Description	One of two type I myosins; localizes to actin cortical patches; deletion of MYO3 has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization; MYO3 has a paralog, MYO5, that arose from the whole genome duplication (2, 3, 4, 5)
Name Description	MYOsin 1

Experimental Data
Molecules/cell	155 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	1,272
Molecular Weight (Da)	142,451
Isoelectric Point (pI)	9.89

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Myo3p (InterPro)
Physical Interactions	There are 91 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0001F7BD57 \| P36006 MIPS: YKL129C NCBI: 1171092 \| 330443650 \| 347595818 \| 486219 \| 61679819 \| 71041741 \| 71041742 \| 71041743 \| 71041744 \| 914198 \| 99031901 \| NP_012793.2 \| NM_001179695.2 GenBank/EMBL/DDBJ: DAA09032.2 \| S76960 \| Z28129

Amino Acid Sequence (or in FASTA format)
1 MAVIKKGARR KDVKEPKKRS AKIKKATFDA NKKKEVGISD LTLLSKISDE 51 SINENLKKRF KNGIIYTYIG HVLISVNPFR DLGIYTNAVL ESYKGKNRLE 101 VPPHVFAIAE SMYYNLKSYN ENQCVIISGE SGAGKTEAAK RIMQYIAAAS 151 NSHSESIGKI KDMVLATNPL LESFGCAKTL RNNNSSRHGK YLEIKFNSQF 201 EPCAGNITNY LLEKQRVVGQ IKNERNFHIF YQFTKGASDT YKQMFGVQMP 251 EQYIYTAAAG CTTADTIDDV KDYEGTLEAM RTIGLVQEEQ DQIFRMLAAI 301 LWIGNISFIE NEEGNAQVGD TSVTDFVAYL LQVDASLLVK CLVERIMQTS 351 HGMKRGSVYH VPLNPVQATA VRDALAKAIY NNLFDWIVDR VNVSLQAFPG 401 ADKSIGILDI YGFEIFEHNS FEQICINYVN EKLQQIFIQL TLKAEQETYE 451 REKIKWTPIK YFDNKVVCDL IEAKNPPGIL AAMNDSIATA HADSNAADQA 501 FAQRLNLFNS NPYFELRANK FVIKHYAGDV TYDINGITDK NKDQLQKDLI 551 ELIGTTTNTF LSTIFPDDVD KDSKRRPPTA GDKIIKSANE LVETLSKAEP 601 SYIRTIKPNQ TKSPNDYDDH QVLHQVKYLG LQENVRIRRA GFAYRQTFEK 651 FVERFYLLSP DCSYAGDYTW DGDTLEAVKL ILRDAMIPEK EFQLGVTSVF 701 IKTPESLFAL EDMRDKYWYN MAARIQRAWR RFLQRRIDAA IKIQRTIREK 751 KGGNKYVKLR DYGTKLLAGK KERRSMSLLG YRAFMGDYLS CNESKTKGSY 801 IRRQVGIKDK VVFSIKGECL HSKFGRSAQR LKKVFILTKK TFYIIGQTRE 851 QNAMKYTQDY KIDVGKIKQV SLTNLQDDWM GVILVNSTQS DPLINTPFKT 901 ELMTRLKKLN EKIMIKVGPT IEYHKQPNKL HTVRSKISDS APKYGDIYKS 951 STIYVRRGHP ANSKSNKKPK NPGGLSGKPI KSKKSKHKST HKHTHSHRSH 1001 RDAAKKQPLP SQKPVNPLSL AATAAQAAYN PKPDKTVPIK SSAIPAAKVS 1051 SKHSSKPSSK EKVAVKKASS SHKSSSAKQN QVSMPPSKGV EKNKEPLKET 1101 TATATANIPI PPPPPPMGQP KDPKFEAAYD FPGSGSSSEL PLKKGDIVFI 1151 SRDEPSGWSL AKLLDGSKEG WVPTAYMTPY KDTRNTVPVA ATGAVNDVTN 1201 QKSSQIDNTI SSAQEGVQFG SATVGPTSDN QSNPVGTFSD GLASALAARA 1251 NKMRAESADD DDNDDGDDDD DW*

Amino Acid Sequence (or in FASTA format)

       1  MAVIKKGARR KDVKEPKKRS AKIKKATFDA NKKKEVGISD LTLLSKISDE
      51  SINENLKKRF KNGIIYTYIG HVLISVNPFR DLGIYTNAVL ESYKGKNRLE
     101  VPPHVFAIAE SMYYNLKSYN ENQCVIISGE SGAGKTEAAK RIMQYIAAAS
     151  NSHSESIGKI KDMVLATNPL LESFGCAKTL RNNNSSRHGK YLEIKFNSQF
     201  EPCAGNITNY LLEKQRVVGQ IKNERNFHIF YQFTKGASDT YKQMFGVQMP
     251  EQYIYTAAAG CTTADTIDDV KDYEGTLEAM RTIGLVQEEQ DQIFRMLAAI
     301  LWIGNISFIE NEEGNAQVGD TSVTDFVAYL LQVDASLLVK CLVERIMQTS
     351  HGMKRGSVYH VPLNPVQATA VRDALAKAIY NNLFDWIVDR VNVSLQAFPG
     401  ADKSIGILDI YGFEIFEHNS FEQICINYVN EKLQQIFIQL TLKAEQETYE
     451  REKIKWTPIK YFDNKVVCDL IEAKNPPGIL AAMNDSIATA HADSNAADQA
     501  FAQRLNLFNS NPYFELRANK FVIKHYAGDV TYDINGITDK NKDQLQKDLI
     551  ELIGTTTNTF LSTIFPDDVD KDSKRRPPTA GDKIIKSANE LVETLSKAEP
     601  SYIRTIKPNQ TKSPNDYDDH QVLHQVKYLG LQENVRIRRA GFAYRQTFEK
     651  FVERFYLLSP DCSYAGDYTW DGDTLEAVKL ILRDAMIPEK EFQLGVTSVF
     701  IKTPESLFAL EDMRDKYWYN MAARIQRAWR RFLQRRIDAA IKIQRTIREK
     751  KGGNKYVKLR DYGTKLLAGK KERRSMSLLG YRAFMGDYLS CNESKTKGSY
     801  IRRQVGIKDK VVFSIKGECL HSKFGRSAQR LKKVFILTKK TFYIIGQTRE
     851  QNAMKYTQDY KIDVGKIKQV SLTNLQDDWM GVILVNSTQS DPLINTPFKT
     901  ELMTRLKKLN EKIMIKVGPT IEYHKQPNKL HTVRSKISDS APKYGDIYKS
     951  STIYVRRGHP ANSKSNKKPK NPGGLSGKPI KSKKSKHKST HKHTHSHRSH
    1001  RDAAKKQPLP SQKPVNPLSL AATAAQAAYN PKPDKTVPIK SSAIPAAKVS
    1051  SKHSSKPSSK EKVAVKKASS SHKSSSAKQN QVSMPPSKGV EKNKEPLKET
    1101  TATATANIPI PPPPPPMGQP KDPKFEAAYD FPGSGSSSEL PLKKGDIVFI
    1151  SRDEPSGWSL AKLLDGSKEG WVPTAYMTPY KDTRNTVPVA ATGAVNDVTN
    1201  QKSSQIDNTI SSAQEGVQFG SATVGPTSDN QSNPVGTFSD GLASALAARA
    1251  NKMRAESADD DDNDDGDDDD DW*

external links for Myo3p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
YGOB	BioPIXIE	MIPS	YeastRC Public Image Repository
YOGY	CYC2008 (complexes)	Pfam domains
	Complexome	YeastRC Structure Prediction (Seattle)
	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for Myo3p

1)	Goodson HV and Spudich JA (1995) Identification and molecular characterization of a yeast myosin I. Cell Motil Cytoskeleton 30(1):73-84
2)	Geli MI and Riezman H (1996) Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272(5261):533-5
3)	Anderson BL, et al. (1998) The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J Cell Biol 141(6):1357-70
4)	Tanaka K and Matsui Y (2001) Functions of unconventional myosins in the yeast Saccharomyces cerevisiae. Cell Struct Funct 26(6):671-5
5)	Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
6)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41