ID   FMNL2_HUMAN             Reviewed;        1086 AA.
AC   Q96PY5; B2RZH5; Q14CC9; Q4ZG52; Q8N3E0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 3.
DT   24-JAN-2024, entry version 165.
DE   RecName: Full=Formin-like protein 2 {ECO:0000305};
DE   AltName: Full=Formin homology 2 domain-containing protein 2;
GN   Name=FMNL2 {ECO:0000312|HGNC:HGNC:18267}; Synonyms=FHOD2, KIAA1902;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA   Nagase T., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XXI. The
RT   complete sequences of 60 new cDNA clones from brain which code for large
RT   proteins.";
RL   DNA Res. 8:179-187(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-1086 (ISOFORM 2).
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   IDENTIFICATION (ISOFORMS 1 AND 2).
RX   PubMed=12684686;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of human FMNL1, FMNL2 and FMNL3 genes
RT   in silico.";
RL   Int. J. Oncol. 22:1161-1168(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   MYRISTOYLATION AT GLY-2.
RX   PubMed=20213681; DOI=10.1002/pmic.200900783;
RA   Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA   Tsunasawa S., Utsumi T.;
RT   "Strategy for comprehensive identification of human N-myristoylated
RT   proteins using an insect cell-free protein synthesis system.";
RL   Proteomics 10:1780-1793(2010).
RN   [8]
RP   FUNCTION.
RX   PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA   Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA   Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT   "Identification and characterization of a set of conserved and new
RT   regulators of cytoskeletal organisation, cell morphology and migration.";
RL   BMC Biol. 9:54-54(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC       cytoskeletal organization. Required in the cortical actin filament
CC       dynamics. {ECO:0000269|PubMed:21834987}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96PY5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96PY5-3; Sequence=VSP_025887;
CC   -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC       interaction with the GBD/FH3 domain. This autoinhibition is released
CC       upon competitive binding of an activated GTPase. The release of DAD
CC       allows the FH2 domain to then nucleate and elongate nonbranched actin
CC       filaments (By similarity). {ECO:0000250|UniProtKB:Q9VUC6}.
CC   -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI13879.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC       Sequence=AAI14439.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC       Sequence=AAX88959.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAB67795.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB067489; BAB67795.1; ALT_INIT; mRNA.
DR   EMBL; AC012066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC012443; AAX88959.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC093794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC113878; AAI13879.1; ALT_SEQ; mRNA.
DR   EMBL; BC114438; AAI14439.1; ALT_SEQ; mRNA.
DR   EMBL; BC167159; AAI67159.1; -; mRNA.
DR   EMBL; AL834396; CAD39058.1; -; mRNA.
DR   CCDS; CCDS46429.1; -. [Q96PY5-3]
DR   RefSeq; NP_443137.2; NM_052905.3. [Q96PY5-3]
DR   PDB; 4YC7; X-ray; 2.50 A; B=1-379.
DR   PDBsum; 4YC7; -.
DR   AlphaFoldDB; Q96PY5; -.
DR   SMR; Q96PY5; -.
DR   BioGRID; 125355; 67.
DR   ELM; Q96PY5; -.
DR   IntAct; Q96PY5; 18.
DR   MINT; Q96PY5; -.
DR   STRING; 9606.ENSP00000288670; -.
DR   GlyGen; Q96PY5; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q96PY5; -.
DR   PhosphoSitePlus; Q96PY5; -.
DR   BioMuta; FMNL2; -.
DR   DMDM; 238054383; -.
DR   EPD; Q96PY5; -.
DR   jPOST; Q96PY5; -.
DR   MassIVE; Q96PY5; -.
DR   MaxQB; Q96PY5; -.
DR   PaxDb; 9606-ENSP00000288670; -.
DR   PeptideAtlas; Q96PY5; -.
DR   ProteomicsDB; 77786; -. [Q96PY5-1]
DR   ProteomicsDB; 77787; -. [Q96PY5-3]
DR   Pumba; Q96PY5; -.
DR   Antibodypedia; 10309; 127 antibodies from 25 providers.
DR   DNASU; 114793; -.
DR   Ensembl; ENST00000288670.14; ENSP00000288670.9; ENSG00000157827.20. [Q96PY5-3]
DR   GeneID; 114793; -.
DR   KEGG; hsa:114793; -.
DR   MANE-Select; ENST00000288670.14; ENSP00000288670.9; NM_052905.4; NP_443137.2. [Q96PY5-3]
DR   UCSC; uc002tye.3; human. [Q96PY5-1]
DR   AGR; HGNC:18267; -.
DR   CTD; 114793; -.
DR   DisGeNET; 114793; -.
DR   GeneCards; FMNL2; -.
DR   HGNC; HGNC:18267; FMNL2.
DR   HPA; ENSG00000157827; Tissue enriched (brain).
DR   MIM; 616285; gene.
DR   neXtProt; NX_Q96PY5; -.
DR   OpenTargets; ENSG00000157827; -.
DR   PharmGKB; PA28144; -.
DR   VEuPathDB; HostDB:ENSG00000157827; -.
DR   eggNOG; KOG1923; Eukaryota.
DR   GeneTree; ENSGT00940000155515; -.
DR   HOGENOM; CLU_003597_0_0_1; -.
DR   InParanoid; Q96PY5; -.
DR   OMA; MMPGFSP; -.
DR   OrthoDB; 471257at2759; -.
DR   PhylomeDB; Q96PY5; -.
DR   TreeFam; TF325155; -.
DR   PathwayCommons; Q96PY5; -.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   SignaLink; Q96PY5; -.
DR   SIGNOR; Q96PY5; -.
DR   BioGRID-ORCS; 114793; 27 hits in 1150 CRISPR screens.
DR   ChiTaRS; FMNL2; human.
DR   GeneWiki; FMNL2; -.
DR   GenomeRNAi; 114793; -.
DR   Pharos; Q96PY5; Tbio.
DR   PRO; PR:Q96PY5; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q96PY5; Protein.
DR   Bgee; ENSG00000157827; Expressed in inferior vagus X ganglion and 188 other cell types or tissues.
DR   ExpressionAtlas; Q96PY5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   DisProt; DP02609; -.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; DAD_dom.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR043592; FMNL_animal.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   PANTHER; PTHR45857; FORMIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR45857:SF5; FORMIN-LIKE PROTEIN 2; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 2.
DR   Pfam; PF02181; FH2; 1.
DR   PRINTS; PR00049; WILMSTUMOUR.
DR   SMART; SM01139; Drf_FH3; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
DR   Genevisible; Q96PY5; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Lipoprotein; Myristate;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..1086
FT                   /note="Formin-like protein 2"
FT                   /id="PRO_0000289093"
FT   DOMAIN          23..469
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT   DOMAIN          616..1007
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   DOMAIN          1040..1079
FT                   /note="DAD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT   REGION          513..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..538
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..597
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:20213681"
FT   VAR_SEQ         1057..1086
FT                   /note="VLKTVPFTARTAKRGSRFFCEPVLTEEYHY -> DLRNQPYRRADAVRRSVR
FT                   RRFDDQNLRSVNGAEITM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11572484,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT                   /id="VSP_025887"
FT   VARIANT         352
FT                   /note="Y -> C (in dbSNP:rs34119671)"
FT                   /id="VAR_032570"
FT   VARIANT         504
FT                   /note="M -> T (in dbSNP:rs11897929)"
FT                   /id="VAR_032571"
FT   CONFLICT        570
FT                   /note="P -> PP (in Ref. 1; BAB67795, 3; AAI67159 and 4;
FT                   CAD39058)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        579
FT                   /note="A -> S (in Ref. 1; BAB67795 and 3; AAI67159)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        964
FT                   /note="T -> R (in Ref. 4; CAD39058)"
FT                   /evidence="ECO:0000305"
FT   TURN            36..39
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           46..53
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           57..69
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           76..87
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           93..99
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           103..116
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           119..126
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   TURN            128..130
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           132..145
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           206..216
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           220..232
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           235..243
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           247..253
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           254..256
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           260..275
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           279..294
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           301..309
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           314..329
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           334..346
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           349..356
FT                   /evidence="ECO:0007829|PDB:4YC7"
FT   HELIX           362..374
FT                   /evidence="ECO:0007829|PDB:4YC7"
SQ   SEQUENCE   1086 AA;  123321 MW;  951ED0A26232F640 CRC64;
     MGNAGSMDSQ QTDFRAHNVP LKLPMPEPGE LEERFAIVLN AMNLPPDKAR LLRQYDNEKK
     WELICDQERF QVKNPPHTYI QKLKGYLDPA VTRKKFRRRV QESTQVLREL EISLRTNHIG
     WVREFLNEEN KGLDVLVEYL SFAQYAVTFD FESVESTVES SVDKSKPWSR SIEDLHRGSN
     LPSPVGNSVS RSGRHSALRY NTLPSRRTLK NSRLVSKKDD VHVCIMCLRA IMNYQYGFNM
     VMSHPHAVNE IALSLNNKNP RTKALVLELL AAVCLVRGGH EIILSAFDNF KEVCGEKQRF
     EKLMEHFRNE DNNIDFMVAS MQFINIVVHS VEDMNFRVHL QYEFTKLGLD EYLDKLKHTE
     SDKLQVQIQA YLDNVFDVGA LLEDAETKNA ALERVEELEE NISHLSEKLQ DTENEAMSKI
     VELEKQLMQR NKELDVVREI YKDANTQVHT LRKMVKEKEE AIQRQSTLEK KIHELEKQGT
     IKIQKKGDGD IAILPVVASG TLSMGSEVVA GNSVGPTMGA ASSGPLPPPP PPLPPSSDTP
     ETVQNGPVTP PMPPPPPPPP PPPPPPPPPP PPPLPGPAAE TVPAPPLAPP LPSAPPLPGT
     SSPTVVFNSG LAAVKIKKPI KTKFRMPVFN WVALKPNQIN GTVFNEIDDE RILEDLNVDE
     FEEIFKTKAQ GPAIDLSSSK QKIPQKGSNK VTLLEANRAK NLAITLRKAG KTADEICKAI
     HVFDLKTLPV DFVECLMRFL PTENEVKVLR LYERERKPLE NLSDEDRFMM QFSKIERLMQ
     KMTIMAFIGN FAESIQMLTP QLHAIIAASV SIKSSQKLKK ILEIILALGN YMNSSKRGAV
     YGFKLQSLDL LLDTKSTDRK QTLLHYISNV VKEKYHQVSL FYNELHYVEK AAAVSLENVL
     LDVKELQRGM DLTKREYTMH DHNTLLKEFI LNNEGKLKKL QDDAKIAQDA FDDVVKYFGE
     NPKTTPPSVF FPVFVRFVKA YKQAEEENEL RKKQEQALME KLLEQEALME QQDPKSPSHK
     SKRQQQELIA ELRRRQVKDN RHVYEGKDGA IEDIITVLKT VPFTARTAKR GSRFFCEPVL
     TEEYHY
//