Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00790
Entry Name
UniProt Accession
Theoretical PI
5.56
Molecular Weight
121853.57
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Formin-like protein 1
Protein Synonyms/Alias
CLL-associated antigen KW-13; Leukocyte formin;
Gene Name
FMNL1
Gene Synonyms/Alias
C17orf1; C17orf1B; FMNL;
Created Date
16-APR-2002
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNAAGSAE
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Han Y, Eppinger E, Schuster IG, Weigand LU, Liang X, Kremmer E, Peschel C,Krackhardt AM. Formin-like 1 (FMNL1) is regulated by N-terminal myristoylationand induces polarized membrane blebbing. J Biol Chem. 2009 Nov27;284(48):33409-17. doi: 10.1074/jbc.M109.060699. Epub 2009 Oct 8.[PMID:19815554]
Functional Description
May play a role in the control of cell motility and survival of macrophages (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape.
Sequence Annotation
Domain: 27 468 GBD/FH3.
Domain: 632 1023 FH2.
Domain: 1059 1090 DAD.
Modified residue: 7 7 Phosphoserine.
Modified residue: 184 184 Phosphoserine.
Modified residue: 624 624 Phosphoserine.
Protein Length
1100 AA.
Protein Sequence
(Canonical)
MGNAAGSAEQ PAGPAAPPPK QPAPPKQPMP AAGELEERFN RALNCMNLPP DKVQLLSQYD  60
NEKKWELICD QERFQVKNPP AAYIQKLKSY VDTGGVSRKV AADWMSNLGF KRRVQESTQV  120
LRELETSLRT NHIGWVQEFL NEENRGLDVL LEYLAFAQCS VTYDMESTDN GASNSEKNKP  180
LEQSVEDLSK GPPSSVPKSR HLTIKLTPAH SRKALRNSRI VSQKDDVHVC IMCLRAIMNY  240
QSGFSLVMNH PACVNEIALS LNNKNPRTKA LVLELLAAVC LVRGGHDIIL AAFDNFKEVC  300
GEQHRFEKLM EYFRNEDSNI DFMVACMQFI NIVVHSVENM NFRVFLQYEF THLGLDLYLE  360
RLRLTESDKL QVQIQAYLDN IFDVGALLED TETKNAVLEH MEELQEQVAL LTERLRDAEN  420
ESMAKIAELE KQLSQARKEL ETLRERFSES TAMGPSRRPP EPEKAPPAAP TRPSALELKV  480
EELEEKGLIR ILRGPGDAVS IEILPVAVAT PSGGDAPTPG VPTGSPSPDL APAAEPAPGA  540
APPPPPPLPG LPSPQEAPPS APPQAPPLPG SPEPPPAPPL PGDLPPPPPP PPPPPGTDGP  600
VPPPPPPPPP PPGGPPDALG RRDSELGPGV KAKKPIQTKF RMPLLNWVAL KPSQITGTVF  660
TELNDEKVLQ ELDMSDFEEQ FKTKSQGPSL DLSALKSKAA QKAPSKATLI EANRAKNLAI  720
TLRKGNLGAE RICQAIEAYD LQALGLDFLE LLMRFLPTEY ERSLITRFER EQRPMEELSE  780
EDRFMLCFSR IPRLPERMTT LTFLGNFPDT AQLLMPQLNA IIAASMSIKS SDKLRQILEI  840
VLAFGNYMNS SKRGAAYGFR LQSLDALLEM KSTDRKQTLL HYLVKVIAEK YPQLTGFHSD  900
LHFLDKAGSV SLDSVLADVR SLQRGLELTQ REFVRQDDCM VLKEFLRANS PTMDKLLADS  960
KTAQEAFESV VEYFGENPKT TSPGLFFSLF SRFIKAYKKA EQEVEQWKKE AAAQEAGADT  1020
PGKGEPPAPK SPPKARRPQM DLISELKRRQ QKEPLIYESD RDGAIEDIIT VIKTVPFTAR  1080
TGKRTSRLLC EASLGEEMPL                                              1100
FASTA
(Canonical)
>LipidDB-9606-00790|O95466
MGNAAGSAEQPAGPAAPPPKQPAPPKQPMPAAGELEERFNRALNCMNLPPDKVQLLSQYD
NEKKWELICDQERFQVKNPPAAYIQKLKSYVDTGGVSRKVAADWMSNLGFKRRVQESTQV
LRELETSLRTNHIGWVQEFLNEENRGLDVLLEYLAFAQCSVTYDMESTDNGASNSEKNKP
LEQSVEDLSKGPPSSVPKSRHLTIKLTPAHSRKALRNSRIVSQKDDVHVCIMCLRAIMNY
QSGFSLVMNHPACVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHDIILAAFDNFKEVC
GEQHRFEKLMEYFRNEDSNIDFMVACMQFINIVVHSVENMNFRVFLQYEFTHLGLDLYLE
RLRLTESDKLQVQIQAYLDNIFDVGALLEDTETKNAVLEHMEELQEQVALLTERLRDAEN
ESMAKIAELEKQLSQARKELETLRERFSESTAMGPSRRPPEPEKAPPAAPTRPSALELKV
EELEEKGLIRILRGPGDAVSIEILPVAVATPSGGDAPTPGVPTGSPSPDLAPAAEPAPGA
APPPPPPLPGLPSPQEAPPSAPPQAPPLPGSPEPPPAPPLPGDLPPPPPPPPPPPGTDGP
VPPPPPPPPPPPGGPPDALGRRDSELGPGVKAKKPIQTKFRMPLLNWVALKPSQITGTVF
TELNDEKVLQELDMSDFEEQFKTKSQGPSLDLSALKSKAAQKAPSKATLIEANRAKNLAI
TLRKGNLGAERICQAIEAYDLQALGLDFLELLMRFLPTEYERSLITRFEREQRPMEELSE
EDRFMLCFSRIPRLPERMTTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEI
VLAFGNYMNSSKRGAAYGFRLQSLDALLEMKSTDRKQTLLHYLVKVIAEKYPQLTGFHSD
LHFLDKAGSVSLDSVLADVRSLQRGLELTQREFVRQDDCMVLKEFLRANSPTMDKLLADS
KTAQEAFESVVEYFGENPKTTSPGLFFSLFSRFIKAYKKAEQEVEQWKKEAAAQEAGADT
PGKGEPPAPKSPPKARRPQMDLISELKRRQQKEPLIYESDRDGAIEDIITVIKTVPFTAR
TGKRTSRLLCEASLGEEMPL
Gene Ontology
GO:0042995; C:cell projection; IEA:UniProtKB-KW
GO:0005829; C:cytosol; ISS:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0016020; C:membrane; IDA:UniProtKB
GO:0045335; C:phagocytic vesicle; ISS:UniProtKB
GO:0005886; C:plasma membrane; ISS:UniProtKB
GO:0051015; F:actin filament binding; ISS:UniProtKB
GO:0032794; F:GTPase activating protein binding; IDA:UniProtKB
GO:0048365; F:Rac GTPase binding; ISS:UniProtKB
GO:0051014; P:actin filament severing; ISS:UniProtKB
GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB
GO:0008360; P:regulation of cell shape; IMP:UniProtKB
GO:0006929; P:substrate-dependent cell migration; IEA:Ensembl
Interpro
InterPro; IPR016024; ARM-type_fold
InterPro; IPR014767; Diaphanous_autoregulatory
InterPro; IPR015425; FH2_Formin
InterPro; IPR010472; FH3_dom
InterPro; IPR027657; FMNL1
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; PS51231; DAD;
PROSITE; PS51444; FH2;
PROSITE; PS51232; GBD_FH3;
PRINTS