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Q6ZPF4

- FMNL3_MOUSE

UniProt

Q6ZPF4 - FMNL3_MOUSE

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Protein

Formin-like protein 3

Gene

Fmnl3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration (By similarity).By similarity

GO - Molecular functioni

  1. GTPase activating protein binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  2. cell migration Source: UniProtKB
  3. cytoskeleton organization Source: UniProtKB
  4. regulation of cell shape Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-like protein 3
Gene namesi
Name:Fmnl3
Synonyms:Kiaa2014
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:109569. Fmnl3.

Subcellular locationi

Cytoplasm By similarity
Note: Enriched in lamellipodia.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 10281027Formin-like protein 3PRO_0000289096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei174 – 1741PhosphoserineBy similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ6ZPF4.
PaxDbiQ6ZPF4.
PRIDEiQ6ZPF4.

PTM databases

PhosphoSiteiQ6ZPF4.

Expressioni

Gene expression databases

BgeeiQ6ZPF4.
CleanExiMM_FMNL3.
ExpressionAtlasiQ6ZPF4. baseline and differential.
GenevestigatoriQ6ZPF4.

Interactioni

Subunit structurei

Interacts with SRGAP2 (via SH3 domain).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SRGAP2O750443EBI-774731,EBI-1051034From a different organism.

Protein-protein interaction databases

BioGridi204547. 1 interaction.
DIPiDIP-32010N.
IntActiQ6ZPF4. 3 interactions.

Structurei

Secondary structure

1
1028
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi581 – 5844Combined sources
Turni600 – 6023Combined sources
Helixi603 – 6097Combined sources
Helixi641 – 65414Combined sources
Helixi658 – 6669Combined sources
Helixi675 – 6839Combined sources
Helixi688 – 69912Combined sources
Turni704 – 7063Combined sources
Helixi709 – 71911Combined sources
Helixi723 – 75836Combined sources
Helixi761 – 77818Combined sources
Beta strandi780 – 7823Combined sources
Helixi790 – 7945Combined sources
Beta strandi795 – 8006Combined sources
Beta strandi804 – 8074Combined sources
Helixi808 – 81912Combined sources
Helixi821 – 8244Combined sources
Helixi833 – 8375Combined sources
Helixi841 – 86323Combined sources
Turni868 – 8703Combined sources
Helixi871 – 90131Combined sources
Turni906 – 9083Combined sources
Helixi911 – 93727Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EAHX-ray3.40A/B/C/E555-954[»]
ProteinModelPortaliQ6ZPF4.
SMRiQ6ZPF4. Positions 225-422, 551-973.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 472447GBD/FH3PROSITE-ProRule annotationAdd
BLAST
Domaini561 – 951391FH2PROSITE-ProRule annotationAdd
BLAST
Domaini986 – 101833DADAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi499 – 54850Pro-richAdd
BLAST

Domaini

The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).By similarity

Sequence similaritiesi

Belongs to the formin homology family.Curated
Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG149898.
GeneTreeiENSGT00760000118986.
HOGENOMiHOG000231209.
HOVERGENiHBG053118.
InParanoidiQ6ZPF4.
OMAiRCHLEPN.
OrthoDBiEOG7F7W8J.
PhylomeDBiQ6ZPF4.
TreeFamiTF325155.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027655. Fmnl3.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]
PANTHERiPTHR23213:SF29. PTHR23213:SF29. 1 hit.
PfamiPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 2 hits.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6ZPF4-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGNLESTDGG PGEPPSVPLL LPPGKTPMPE PCELEERFAL VLSSMNLPPD
60 70 80 90 100
KARLLRQYDN EKKWDLICDQ ERFQVKNPPH TYIQKLQSFL DPNVTRKKFR
110 120 130 140 150
RRVQESTKVL RELEISLRTN HIGWVREFLN DENKGLDVLV DYLSFAQCSV
160 170 180 190 200
MFDFEGLESG DDGAFDKLRS WSRSIEDLQP PNALSAPFTN SLARSARQSV
210 220 230 240 250
LRYSTLPGRR ALKNSRLVSQ KDDVHVCILC LRAIMNYQYG FNLVMSHPHA
260 270 280 290 300
VNEIALSLNN KNPRTKALVL ELLAAVCLVR GGHEIILAAF DNFKEVCKEL
310 320 330 340 350
HRFEKLMEYF RNEDSNIDFM VACMQFINIV VHSVEDMNFR VHLQYEFTKL
360 370 380 390 400
GLEEFLQKSR HTESEKLQVQ IQAYLDNVFD VGGLLEDAET KNVALEKVEE
410 420 430 440 450
LEEHVSHLTE KLLDLENENM MRVAELEKQL LQREKELESI KETYENTSNQ
460 470 480 490 500
VHTLRRLIKE KEEAFQRRCH LEPSARGLES MGGEALARVG PTELTEGIPP
510 520 530 540 550
SDLDLLAPAP PTEETLPLPP PPAPPLPPPP PPLPDKCPPA PPLPGAAPSV
560 570 580 590 600
VLTVGLSAIR IKKPIKTKFR LPVFNWTALK PNQINGTVFS ELDDEKILED
610 620 630 640 650
LDLDRFEELF KTKAQGPALD LICSKNKTAQ KAASKVTLLE ANRAKNLAIT
660 670 680 690 700
LRKAGRSAEE ICRAIHTFDL QTLPVDFVEC LMRFLPTEAE VKLLRQYERE
710 720 730 740 750
RQPLEELAAE DRFMLLFSKV ERLTQRMAGM AFLGNFQDNL QMLTPQLNAI
760 770 780 790 800
IAASASVKSS QKLKQMLEII LALGNYMNSS KRGAVYGFKL QSLDLLLDTK
810 820 830 840 850
STDRKMTLLH FIALTVKEKY PELANFWQEL HFVEKAAAVS LENVLLDVKE
860 870 880 890 900
LGRGMELIRR ECSIHDNSVL RNFLSTNEGK LDKLQRDAKT AEEAYNAVVR
910 920 930 940 950
YFGESPKTTP PSVFFPVFVR FIRSYKEAEQ ENEARKKQEE VMREKQLAQE
960 970 980 990 1000
AKKLDAKTPS QRNKWQQQEL IAELRRRQAK EHRPVYEGKD GTIEDIITVL
1010 1020
KSVPFTARTA KRGSRFFCDA AHHDESNC
Length:1,028
Mass (Da):117,169
Last modified:May 29, 2007 - v2
Checksum:iBBA0436746934A3B
GO
Isoform 2 (identifier: Q6ZPF4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-202: Missing.
     999-1028: VLKSVPFTARTAKRGSRFFCDAAHHDESNC → GFNHQRMVVHSQVRSAVPPSGPPRAPGPH

Show »
Length:976
Mass (Da):111,279
Checksum:i702206CD74A93F8B
GO

Sequence cautioni

The sequence BAC98283.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei152 – 20251Missing in isoform 2. 1 PublicationVSP_025894Add
BLAST
Alternative sequencei999 – 102830VLKSV…DESNC → GFNHQRMVVHSQVRSAVPPS GPPRAPGPH in isoform 2. 1 PublicationVSP_025895Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129473 mRNA. Translation: BAC98283.1. Different initiation.
AK155331 mRNA. Translation: BAE33197.1.
AK170744 mRNA. Translation: BAE41997.1.
BC131961 mRNA. Translation: AAI31962.1.
CCDSiCCDS27819.1. [Q6ZPF4-1]
RefSeqiNP_035841.1. NM_011711.1. [Q6ZPF4-1]
XP_006520908.1. XM_006520845.1. [Q6ZPF4-2]
UniGeneiMm.29043.

Genome annotation databases

EnsembliENSMUST00000081224; ENSMUSP00000079984; ENSMUSG00000023008. [Q6ZPF4-2]
ENSMUST00000088233; ENSMUSP00000085566; ENSMUSG00000023008. [Q6ZPF4-1]
GeneIDi22379.
KEGGimmu:22379.
UCSCiuc007xpj.1. mouse. [Q6ZPF4-1]
uc007xpl.1. mouse. [Q6ZPF4-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129473 mRNA. Translation: BAC98283.1 . Different initiation.
AK155331 mRNA. Translation: BAE33197.1 .
AK170744 mRNA. Translation: BAE41997.1 .
BC131961 mRNA. Translation: AAI31962.1 .
CCDSi CCDS27819.1. [Q6ZPF4-1 ]
RefSeqi NP_035841.1. NM_011711.1. [Q6ZPF4-1 ]
XP_006520908.1. XM_006520845.1. [Q6ZPF4-2 ]
UniGenei Mm.29043.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4EAH X-ray 3.40 A/B/C/E 555-954 [» ]
ProteinModelPortali Q6ZPF4.
SMRi Q6ZPF4. Positions 225-422, 551-973.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204547. 1 interaction.
DIPi DIP-32010N.
IntActi Q6ZPF4. 3 interactions.

PTM databases

PhosphoSitei Q6ZPF4.

Proteomic databases

MaxQBi Q6ZPF4.
PaxDbi Q6ZPF4.
PRIDEi Q6ZPF4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000081224 ; ENSMUSP00000079984 ; ENSMUSG00000023008 . [Q6ZPF4-2 ]
ENSMUST00000088233 ; ENSMUSP00000085566 ; ENSMUSG00000023008 . [Q6ZPF4-1 ]
GeneIDi 22379.
KEGGi mmu:22379.
UCSCi uc007xpj.1. mouse. [Q6ZPF4-1 ]
uc007xpl.1. mouse. [Q6ZPF4-2 ]

Organism-specific databases

CTDi 91010.
MGIi MGI:109569. Fmnl3.
Rougei Search...

Phylogenomic databases

eggNOGi NOG149898.
GeneTreei ENSGT00760000118986.
HOGENOMi HOG000231209.
HOVERGENi HBG053118.
InParanoidi Q6ZPF4.
OMAi RCHLEPN.
OrthoDBi EOG7F7W8J.
PhylomeDBi Q6ZPF4.
TreeFami TF325155.

Miscellaneous databases

NextBioi 302737.
PROi Q6ZPF4.
SOURCEi Search...

Gene expression databases

Bgeei Q6ZPF4.
CleanExi MM_FMNL3.
ExpressionAtlasi Q6ZPF4. baseline and differential.
Genevestigatori Q6ZPF4.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027655. Fmnl3.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view ]
PANTHERi PTHR23213:SF29. PTHR23213:SF29. 1 hit.
Pfami PF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 2 hits.
PF02181. FH2. 1 hit.
[Graphical view ]
SMARTi SM00498. FH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
PROSITEi PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryonic tail.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: NOD.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. Cited for: INTERACTION WITH SRGAP2.

Entry informationi

Entry nameiFMNL3_MOUSE
AccessioniPrimary (citable) accession number: Q6ZPF4
Secondary accession number(s): Q3TCF9, Q3U2E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: November 26, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3