Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00782
Entry Name
UniProt Accession
Theoretical PI
6.23
Molecular Weight
117212.83
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Formin-like protein 3
Protein Synonyms/Alias
Formin homology 2 domain-containing protein 3; WW domain-binding protein 3; WBP-3;
Gene Name
FMNL3
Gene Synonyms/Alias
FHOD3; KIAA2014; WBP3;
Created Date
29-MAY-2007
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNLESAEG
[1][2]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Suzuki T, Moriya K, Nagatoshi K, Ota Y, Ezure T, Ando E, Tsunasawa S, UtsumiT. Strategy for comprehensive identification of human N-myristoylated proteinsusing an insect cell-free protein synthesis system. Proteomics. 2010May;10(9):1780-93. doi: 10.1002/pmic.200900783.[PMID:20213681]
[2] Moriya K, Yamamoto T, Takamitsu E, Matsunaga Y, Kimoto M, Fukushige D, Kimoto C, Suzuki T, Utsumi T. Protein N-myristoylation is required for cellularmorphological changes induced by two formin family proteins, FMNL2 and FMNL3.Biosci Biotechnol Biochem. 2012;76(6):1201-9. Epub 2012 Jun 7.[PMID:22790947]
Functional Description
Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration.
Sequence Annotation
Domain: 26 472 GBD/FH3.
Domain: 561 951 FH2.
Domain: 986 1018 DAD.
Modified residue: 174 174 Phosphoserine.
Protein Length
1028 AA.
Protein Sequence
(Canonical)
MGNLESAEGV PGEPPSVPLL LPPGKMPMPE PCELEERFAL VLSSMNLPPD KARLLRQYDN  60
EKKWDLICDQ ERFQVKNPPH TYIQKLQSFL DPSVTRKKFR RRVQESTKVL RELEISLRTN  120
HIGWVREFLN DENKGLDVLV DYLSFAQCSV MFDFEGLESG DDGAFDKLRS WSRSIEDLQP  180
PSALSAPFTN SLARSARQSV LRYSTLPGRR ALKNSRLVSQ KDDVHVCILC LRAIMNYQYG  240
FNLVMSHPHA VNEIALSLNN KNPRTKALVL ELLAAVCLVR GGHEIILAAF DNFKEVCKEL  300
HRFEKLMEYF RNEDSNIDFM VACMQFINIV VHSVEDMNFR VHLQYEFTKL GLEEFLQKSR  360
HTESEKLQVQ IQAYLDNVFD VGGLLEDAET KNVALEKVEE LEEHVSHLTE KLLDLENENM  420
MRVAELEKQL LQREKELESI KETYENTSHQ VHTLRRLIKE KEEAFQRRCH LEPNVRGLES  480
VDSEALARVG PAELSEGMPP SDLDLLAPAP PPEEVLPLPP PPAPPLPPPP PPLPDKCPPA  540
PPLPGAAPSV VLTVGLSAIR IKKPIKTKFR LPVFNWTALK PNQISGTVFS ELDDEKILED  600
LDLDKFEELF KTKAQGPALD LICSKNKTAQ KAASKVTLLE ANRAKNLAIT LRKAGRSAEE  660
ICRAIHTFDL QTLPVDFVEC LMRFLPTEAE VKLLRQYERE RQPLEELAAE DRFMLLFSKV  720
ERLTQRMAGM AFLGNFQDNL QMLTPQLNAI IAASASVKSS QKLKQMLEII LALGNYMNSS  780
KRGAVYGFKL QSLDLLLDTK STDRKMTLLH FIALTVKEKY PDLANFWHEL HFVEKAAAVS  840
LENVLLDVKE LGRGMELIRR ECSIHDNSVL RNFLSTNEGK LDKLQRDAKT AEEAYNAVVR  900
YFGESPKTTP PSVFFPVFVR FIRSYKEAEQ ENEARKKQEE VMREKQLAQE AKKLDAKTPS  960
QRNKWQQQEL IAELRRRQAK EHRPVYEGKD GTIEDIITVL KSVPFTARTA KRGSRFFCDA  1020
AHHDESNC                                                           1028
FASTA
(Canonical)
>LipidDB-9606-00782|Q8IVF7
MGNLESAEGVPGEPPSVPLLLPPGKMPMPEPCELEERFALVLSSMNLPPDKARLLRQYDN
EKKWDLICDQERFQVKNPPHTYIQKLQSFLDPSVTRKKFRRRVQESTKVLRELEISLRTN
HIGWVREFLNDENKGLDVLVDYLSFAQCSVMFDFEGLESGDDGAFDKLRSWSRSIEDLQP
PSALSAPFTNSLARSARQSVLRYSTLPGRRALKNSRLVSQKDDVHVCILCLRAIMNYQYG
FNLVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHEIILAAFDNFKEVCKEL
HRFEKLMEYFRNEDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKSR
HTESEKLQVQIQAYLDNVFDVGGLLEDAETKNVALEKVEELEEHVSHLTEKLLDLENENM
MRVAELEKQLLQREKELESIKETYENTSHQVHTLRRLIKEKEEAFQRRCHLEPNVRGLES
VDSEALARVGPAELSEGMPPSDLDLLAPAPPPEEVLPLPPPPAPPLPPPPPPLPDKCPPA
PPLPGAAPSVVLTVGLSAIRIKKPIKTKFRLPVFNWTALKPNQISGTVFSELDDEKILED
LDLDKFEELFKTKAQGPALDLICSKNKTAQKAASKVTLLEANRAKNLAITLRKAGRSAEE
ICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERQPLEELAAEDRFMLLFSKV
ERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNSS
KRGAVYGFKLQSLDLLLDTKSTDRKMTLLHFIALTVKEKYPDLANFWHELHFVEKAAAVS
LENVLLDVKELGRGMELIRRECSIHDNSVLRNFLSTNEGKLDKLQRDAKTAEEAYNAVVR
YFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEVMREKQLAQEAKKLDAKTPS
QRNKWQQQELIAELRRRQAKEHRPVYEGKDGTIEDIITVLKSVPFTARTAKRGSRFFCDA
AHHDESNC
Gene Ontology
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0032794; F:GTPase activating protein binding; ISS:UniProtKB
GO:0030036; P:actin cytoskeleton organization; IEA:InterPro
GO:0016477; P:cell migration; IMP:UniProtKB
GO:0007010; P:cytoskeleton organization; IMP:UniProtKB
GO:0008360; P:regulation of cell shape; IMP:UniProtKB
Interpro
InterPro; IPR016024; ARM-type_fold
InterPro; IPR015425; FH2_Formin
InterPro; IPR010472; FH3_dom
InterPro; IPR027655; Fmnl3
InterPro; IPR010473; GTPase-bd
InterPro; IPR014768; GTPase-bd/formin_homology_3
Pfam
Pfam; PF06367; Drf_FH3;
Pfam; PF06371; Drf_GBD;
Pfam; PF02181; FH2;
SMART
SMART; SM00498; FH2;
PROSITE
PROSITE; PS51444; FH2;
PROSITE; PS51232; GBD_FH3;
PRINTS