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Q6ZPF4

- FMNL3_MOUSE

UniProt

Q6ZPF4 - FMNL3_MOUSE

Protein

Formin-like protein 3

Gene

Fmnl3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 2 (29 May 2007)
      Previous versions | rss
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    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
    2. protein binding Source: MGI

    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

    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

    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

    PaxDbiQ6ZPF4.
    PRIDEiQ6ZPF4.

    PTM databases

    PhosphoSiteiQ6ZPF4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6ZPF4.
    BgeeiQ6ZPF4.
    CleanExiMM_FMNL3.
    GenevestigatoriQ6ZPF4.

    Interactioni

    Subunit structurei

    Interacts with SRGAP2 (via SH3 domain).1 Publication

    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 – 5844
    Turni600 – 6023
    Helixi603 – 6097
    Helixi641 – 65414
    Helixi658 – 6669
    Helixi675 – 6839
    Helixi688 – 69912
    Turni704 – 7063
    Helixi709 – 71911
    Helixi723 – 75836
    Helixi761 – 77818
    Beta strandi780 – 7823
    Helixi790 – 7945
    Beta strandi795 – 8006
    Beta strandi804 – 8074
    Helixi808 – 81912
    Helixi821 – 8244
    Helixi833 – 8375
    Helixi841 – 86323
    Turni868 – 8703
    Helixi871 – 90131
    Turni906 – 9083
    Helixi911 – 93727

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00710000106395.
    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

    MGNLESTDGG PGEPPSVPLL LPPGKTPMPE PCELEERFAL VLSSMNLPPD     50
    KARLLRQYDN EKKWDLICDQ ERFQVKNPPH TYIQKLQSFL DPNVTRKKFR 100
    RRVQESTKVL RELEISLRTN HIGWVREFLN DENKGLDVLV DYLSFAQCSV 150
    MFDFEGLESG DDGAFDKLRS WSRSIEDLQP PNALSAPFTN SLARSARQSV 200
    LRYSTLPGRR ALKNSRLVSQ KDDVHVCILC LRAIMNYQYG FNLVMSHPHA 250
    VNEIALSLNN KNPRTKALVL ELLAAVCLVR GGHEIILAAF DNFKEVCKEL 300
    HRFEKLMEYF RNEDSNIDFM VACMQFINIV VHSVEDMNFR VHLQYEFTKL 350
    GLEEFLQKSR HTESEKLQVQ IQAYLDNVFD VGGLLEDAET KNVALEKVEE 400
    LEEHVSHLTE KLLDLENENM MRVAELEKQL LQREKELESI KETYENTSNQ 450
    VHTLRRLIKE KEEAFQRRCH LEPSARGLES MGGEALARVG PTELTEGIPP 500
    SDLDLLAPAP PTEETLPLPP PPAPPLPPPP PPLPDKCPPA PPLPGAAPSV 550
    VLTVGLSAIR IKKPIKTKFR LPVFNWTALK PNQINGTVFS ELDDEKILED 600
    LDLDRFEELF KTKAQGPALD LICSKNKTAQ KAASKVTLLE ANRAKNLAIT 650
    LRKAGRSAEE ICRAIHTFDL QTLPVDFVEC LMRFLPTEAE VKLLRQYERE 700
    RQPLEELAAE DRFMLLFSKV ERLTQRMAGM AFLGNFQDNL QMLTPQLNAI 750
    IAASASVKSS QKLKQMLEII LALGNYMNSS KRGAVYGFKL QSLDLLLDTK 800
    STDRKMTLLH FIALTVKEKY PELANFWQEL HFVEKAAAVS LENVLLDVKE 850
    LGRGMELIRR ECSIHDNSVL RNFLSTNEGK LDKLQRDAKT AEEAYNAVVR 900
    YFGESPKTTP PSVFFPVFVR FIRSYKEAEQ ENEARKKQEE VMREKQLAQE 950
    AKKLDAKTPS QRNKWQQQEL IAELRRRQAK EHRPVYEGKD GTIEDIITVL 1000
    KSVPFTARTA KRGSRFFCDA AHHDESNC 1028
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    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 ENSGT00710000106395.
    HOGENOMi HOG000231209.
    HOVERGENi HBG053118.
    InParanoidi Q6ZPF4.
    OMAi RCHLEPN.
    OrthoDBi EOG7F7W8J.
    PhylomeDBi Q6ZPF4.
    TreeFami TF325155.

    Miscellaneous databases

    ChiTaRSi FMNL3. mouse.
    NextBioi 302737.
    PROi Q6ZPF4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6ZPF4.
    Bgeei Q6ZPF4.
    CleanExi MM_FMNL3.
    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

    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: October 1, 2014
    This is version 81 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