Q6ZPF4 (FMNL3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Formin-like protein 3

Gene names

Name:	Fmnl3
Synonyms:	Kiaa2014

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1028 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration By similarity.
Subunit structure	Interacts with SRGAP2 (via SH3 domain). Ref.4
Subcellular location	Cytoplasm By similarity. Note: Enriched in lamellipodia By similarity.
Domain	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.
Sequence similarities	Belongs to the formin homology family. Contains 1 DAD (diaphanous autoregulatory) domain. Contains 1 FH2 (formin homology 2) domain. Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.
Sequence caution	The sequence BAC98283.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro cell migration Inferred from sequence or structural similarity. Source: UniProtKB cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell shape Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	GTPase activating protein binding Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6ZPF4-1)

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.

Isoform 2 (identifier: Q6ZPF4-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1028

1028

Formin-like protein 3

PRO_0000289096

Regions

Domain

26 – 472

447

GBD/FH3

Domain

561 – 951

391

FH2

Domain

986 – 1018

33

DAD

Compositional bias

499 – 548

50

Pro-rich

Amino acid modifications

Modified residue

174

1

Phosphoserine By similarity

Lipidation

2

1

N-myristoyl glycine By similarity

Natural variations

Alternative sequence

152 – 202

51

Missing in isoform 2.

VSP_025894

Alternative sequence

999 – 1028

30

VLKSV…DESNC → GFNHQRMVVHSQVRSAVPPS GPPRAPGPH in isoform 2.

VSP_025895

Secondary structure

1

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1028

Helix Strand Turn

Details...

Helix

581 – 584

4

Turn

600 – 602

3

Helix

603 – 609

7

Helix

641 – 654

14

Helix

658 – 666

9

Helix

675 – 683

9

Helix

688 – 699

12

Turn

704 – 706

3

Helix

709 – 719

11

Helix

723 – 758

36

Helix

761 – 778

18

Beta strand

780 – 782

3

Helix

790 – 794

5

Beta strand

795 – 800

6

Beta strand

804 – 807

4

Helix

808 – 819

12

Helix

821 – 824

4

Helix

833 – 837

5

Helix

841 – 863

23

Turn

868 – 870

3

Helix

871 – 901

31

Turn

906 – 908

3

Helix

911 – 937

27

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: BBA0436746934A3B	FASTA	1,028	117,169
	10 20 30 40 50 60 MGNLESTDGG PGEPPSVPLL LPPGKTPMPE PCELEERFAL VLSSMNLPPD KARLLRQYDN 70 80 90 100 110 120 EKKWDLICDQ ERFQVKNPPH TYIQKLQSFL DPNVTRKKFR RRVQESTKVL RELEISLRTN 130 140 150 160 170 180 HIGWVREFLN DENKGLDVLV DYLSFAQCSV MFDFEGLESG DDGAFDKLRS WSRSIEDLQP 190 200 210 220 230 240 PNALSAPFTN SLARSARQSV LRYSTLPGRR ALKNSRLVSQ KDDVHVCILC LRAIMNYQYG 250 260 270 280 290 300 FNLVMSHPHA VNEIALSLNN KNPRTKALVL ELLAAVCLVR GGHEIILAAF DNFKEVCKEL 310 320 330 340 350 360 HRFEKLMEYF RNEDSNIDFM VACMQFINIV VHSVEDMNFR VHLQYEFTKL GLEEFLQKSR 370 380 390 400 410 420 HTESEKLQVQ IQAYLDNVFD VGGLLEDAET KNVALEKVEE LEEHVSHLTE KLLDLENENM 430 440 450 460 470 480 MRVAELEKQL LQREKELESI KETYENTSNQ VHTLRRLIKE KEEAFQRRCH LEPSARGLES 490 500 510 520 530 540 MGGEALARVG PTELTEGIPP SDLDLLAPAP PTEETLPLPP PPAPPLPPPP PPLPDKCPPA 550 560 570 580 590 600 PPLPGAAPSV VLTVGLSAIR IKKPIKTKFR LPVFNWTALK PNQINGTVFS ELDDEKILED 610 620 630 640 650 660 LDLDRFEELF KTKAQGPALD LICSKNKTAQ KAASKVTLLE ANRAKNLAIT LRKAGRSAEE 670 680 690 700 710 720 ICRAIHTFDL QTLPVDFVEC LMRFLPTEAE VKLLRQYERE RQPLEELAAE DRFMLLFSKV 730 740 750 760 770 780 ERLTQRMAGM AFLGNFQDNL QMLTPQLNAI IAASASVKSS QKLKQMLEII LALGNYMNSS 790 800 810 820 830 840 KRGAVYGFKL QSLDLLLDTK STDRKMTLLH FIALTVKEKY PELANFWQEL HFVEKAAAVS 850 860 870 880 890 900 LENVLLDVKE LGRGMELIRR ECSIHDNSVL RNFLSTNEGK LDKLQRDAKT AEEAYNAVVR 910 920 930 940 950 960 YFGESPKTTP PSVFFPVFVR FIRSYKEAEQ ENEARKKQEE VMREKQLAQE AKKLDAKTPS 970 980 990 1000 1010 1020 QRNKWQQQEL IAELRRRQAK EHRPVYEGKD GTIEDIITVL KSVPFTARTA KRGSRFFCDA AHHDESNC
	Isoform 2 [UniParc]. Checksum: 702206CD74A93F8B	FASTA	976	111,279
	10 20 30 40 50 60 MGNLESTDGG PGEPPSVPLL LPPGKTPMPE PCELEERFAL VLSSMNLPPD KARLLRQYDN 70 80 90 100 110 120 EKKWDLICDQ ERFQVKNPPH TYIQKLQSFL DPNVTRKKFR RRVQESTKVL RELEISLRTN 130 140 150 160 170 180 HIGWVREFLN DENKGLDVLV DYLSFAQCSV MYSTLPGRRA LKNSRLVSQK DDVHVCILCL 190 200 210 220 230 240 RAIMNYQYGF NLVMSHPHAV NEIALSLNNK NPRTKALVLE LLAAVCLVRG GHEIILAAFD 250 260 270 280 290 300 NFKEVCKELH RFEKLMEYFR NEDSNIDFMV ACMQFINIVV HSVEDMNFRV HLQYEFTKLG 310 320 330 340 350 360 LEEFLQKSRH TESEKLQVQI QAYLDNVFDV GGLLEDAETK NVALEKVEEL EEHVSHLTEK 370 380 390 400 410 420 LLDLENENMM RVAELEKQLL QREKELESIK ETYENTSNQV HTLRRLIKEK EEAFQRRCHL 430 440 450 460 470 480 EPSARGLESM GGEALARVGP TELTEGIPPS DLDLLAPAPP TEETLPLPPP PAPPLPPPPP 490 500 510 520 530 540 PLPDKCPPAP PLPGAAPSVV LTVGLSAIRI KKPIKTKFRL PVFNWTALKP NQINGTVFSE 550 560 570 580 590 600 LDDEKILEDL DLDRFEELFK TKAQGPALDL ICSKNKTAQK AASKVTLLEA NRAKNLAITL 610 620 630 640 650 660 RKAGRSAEEI CRAIHTFDLQ TLPVDFVECL MRFLPTEAEV KLLRQYERER QPLEELAAED 670 680 690 700 710 720 RFMLLFSKVE RLTQRMAGMA FLGNFQDNLQ MLTPQLNAII AASASVKSSQ KLKQMLEIIL 730 740 750 760 770 780 ALGNYMNSSK RGAVYGFKLQ SLDLLLDTKS TDRKMTLLHF IALTVKEKYP ELANFWQELH 790 800 810 820 830 840 FVEKAAAVSL ENVLLDVKEL GRGMELIRRE CSIHDNSVLR NFLSTNEGKL DKLQRDAKTA 850 860 870 880 890 900 EEAYNAVVRY FGESPKTTPP SVFFPVFVRF IRSYKEAEQE NEARKKQEEV MREKQLAQEA 910 920 930 940 950 960 KKLDAKTPSQ RNKWQQQELI AELRRRQAKE HRPVYEGKDG TIEDIITGFN HQRMVVHSQV 970 RSAVPPSGPP RAPGPH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Bi-modal regulation of a formin by srGAP2." Mason F.M., Heimsath E.G., Higgs H.N., Soderling S.H. J. Biol. Chem. 286:6577-6586(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRGAP2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK129473 mRNA. Translation: BAC98283.1. Different initiation.
AK155331 mRNA. Translation: BAE33197.1.
AK170744 mRNA. Translation: BAE41997.1.
BC131961 mRNA. Translation: AAI31962.1.

IPI

IPI00420509.
IPI00652582.

RefSeq

NP_035841.1. NM_011711.1.

UniGene

Mm.29043.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4EAH	X-ray	3.40	A/B/C/E	555-954	[»]

ProteinModelPortal

Q6ZPF4.

SMR

Q6ZPF4. Positions 225-422, 551-973.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q6ZPF4. 3 interactions.

PTM databases

PhosphoSite

Q6ZPF4.

Proteomic databases

PaxDb

Q6ZPF4.

PRIDE

Q6ZPF4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000081224; ENSMUSP00000079984; ENSMUSG00000023008.
ENSMUST00000088233; ENSMUSP00000085566; ENSMUSG00000023008.

GeneID

22379.

KEGG

mmu:22379.

UCSC

uc007xpj.1. mouse.
uc007xpl.1. mouse.

Organism-specific databases

CTD

91010.

MGI

MGI:109569. Fmnl3.

Rouge

Search...

Phylogenomic databases

eggNOG

NOG149898.

GeneTree

ENSGT00700000104080.

HOGENOM

HOG000231209.

HOVERGEN

HBG053118.

InParanoid

Q6ZPF4.

OMA

KMPMPEP.

OrthoDB

EOG4N8R43.

Gene expression databases

ArrayExpress

Q6ZPF4.

Bgee

Q6ZPF4.

CleanEx

MM_FMNL3.

Genevestigator

Q6ZPF4.

Family and domain databases

InterPro

IPR003104. Actin-bd_FH2/DRF_autoreg.
IPR016024. ARM-type_fold.
IPR010472. Drf_FH3.
IPR010473. Drf_GTPase-bd.
IPR015425. FH2_actin-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]

Pfam

PF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 2 hits.
PF02181. FH2. 1 hit.
[Graphical view]

SMART

SM00498. FH2. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.
SSF101447. FH2_actin_bd. 1 hit.

PROSITE

PS51231. DAD. False negative.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FMNL3. mouse.

NextBio

302737.

SOURCE

Search...

Entry information

Entry name

FMNL3_MOUSE

Accession

Primary (citable) accession number: Q6ZPF4
Secondary accession number(s): Q3TCF9, Q3U2E4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 29, 2007
Last modified:	May 1, 2013
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program