FCHO2_HUMAN
ID FCHO2_HUMAN Reviewed; 810 AA.
AC Q0JRZ9; A8K6W7; B2RNQ9; B4DHK0; E9PG79; Q0JTJ3; Q96CF5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=F-BAR domain only protein 2;
GN Name=FCHO2;
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] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Urinary bladder;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-403, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488 AND SER-511, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385; SER-387; SER-394;
RP SER-403; SER-488 AND SER-533, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP FUNCTION IN CLATHRIN-COATED PITS NUCLEATION, AND INTERACTION WITH EPS15;
RP EPS15R; ITSN1 AND ITSN2.
RX PubMed=20448150; DOI=10.1126/science.1188462;
RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R.,
RA McMahon H.T.;
RT "FCHo proteins are nucleators of clathrin-mediated endocytosis.";
RL Science 328:1281-1284(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS, INTERACTION WITH EPS15 AND
RP AP2A1, AND SUBCELLULAR LOCATION.
RX PubMed=21762413; DOI=10.1111/j.1365-2443.2011.01536.x;
RA Uezu A., Umeda K., Tsujita K., Suetsugu S., Takenawa T., Nakanishi H.;
RT "Characterization of the EFC/F-BAR domain protein, FCHO2.";
RL Genes Cells 16:868-878(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND IDENTIFICATION BY
RP 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 [13]
RP FUNCTION IN DAB2-MEDIATED ENDOCYTOSIS, INTERACTION WITH DAB2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22323290; DOI=10.1091/mbc.e11-09-0812;
RA Mulkearns E.E., Cooper J.A.;
RT "FCH domain only-2 organizes clathrin-coated structures and interacts with
RT Disabled-2 for low-density lipoprotein receptor endocytosis.";
RL Mol. Biol. Cell 23:1330-1342(2012).
RN [14]
RP LIPID-BINDING, AND INTERACTION WITH DAB2; EPS15; EPS15R AND ITSN1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-394; SER-403;
RP SER-488; SER-496 AND SER-508, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-297, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-274, FUNCTION, SUBUNIT,
RP DISULFIDE BOND, AND MUTAGENESIS OF PHE-10.
RX PubMed=17540576; DOI=10.1016/j.str.2007.05.002;
RA Henne W.M., Kent H.M., Ford M.G., Hegde B.G., Daumke O., Butler P.J.,
RA Mittal R., Langen R., Evans P.R., McMahon H.T.;
RT "Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane
RT recruitment module that effects membrane curvature.";
RL Structure 15:839-852(2007).
CC -!- FUNCTION: Functions in an early step of clathrin-mediated endocytosis.
CC Has both a membrane binding/bending activity and the ability to recruit
CC proteins essential to the formation of functional clathrin-coated pits.
CC Has a lipid-binding activity with a preference for membranes enriched
CC in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like
CC the plasma membrane. Its membrane-bending activity might be important
CC for the subsequent action of clathrin and adaptors in the formation of
CC clathrin-coated vesicles. Involved in adaptor protein complex AP-2-
CC dependent endocytosis of the transferrin receptor, it also functions in
CC the AP-2-independent endocytosis of the LDL receptor.
CC {ECO:0000269|PubMed:17540576, ECO:0000269|PubMed:20448150,
CC ECO:0000269|PubMed:21762413, ECO:0000269|PubMed:22323290}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. May form homotetramer. Interacts
CC with AP2A1. Interacts with EPS15, EPS15R, ITSN1 and ITSN2; recruit
CC those scaffolding proteins which in turn may interact with the adaptor
CC protein complex AP-2 at the plasma membrane. Interacts with DAB2 (via
CC DPF motifs); mediates LDL receptor/LDLR endocytosis.
CC {ECO:0000269|PubMed:17540576, ECO:0000269|PubMed:20448150,
CC ECO:0000269|PubMed:21762413, ECO:0000269|PubMed:22323290,
CC ECO:0000269|PubMed:22484487}.
CC -!- INTERACTION:
CC Q0JRZ9; P42566: EPS15; NbExp=3; IntAct=EBI-2609756, EBI-396684;
CC Q0JRZ9; P98078: Dab2; Xeno; NbExp=4; IntAct=EBI-2609756, EBI-1391846;
CC Q0JRZ9-1; Q0JRZ9-1: FCHO2; NbExp=2; IntAct=EBI-15640469, EBI-15640469;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=Associated with forming but not mature clathrin-
CC coated vesicles. The recruitment to coated-pits precede the one of
CC clathrin and the adaptor protein complex AP-2 (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q0JRZ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0JRZ9-2; Sequence=VSP_021910, VSP_021911;
CC Name=3;
CC IsoId=Q0JRZ9-3; Sequence=VSP_044812;
CC -!- PTM: Ubiquitinated. Mainly undergoes monoubiquitination but also
CC polyubiquitination (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Deforms liposomes into a range of tubule diameters from
CC 20 to 130 nm in vitro.
CC -!- SIMILARITY: Belongs to the FCHO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14311.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK291782; BAF84471.1; -; mRNA.
DR EMBL; AK295141; BAG58162.1; -; mRNA.
DR EMBL; AL831971; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC008972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014311; AAH14311.1; ALT_INIT; mRNA.
DR EMBL; BC137070; AAI37071.1; -; mRNA.
DR CCDS; CCDS47230.1; -. [Q0JRZ9-1]
DR CCDS; CCDS54868.1; -. [Q0JRZ9-3]
DR RefSeq; NP_001139504.1; NM_001146032.1. [Q0JRZ9-3]
DR RefSeq; NP_620137.2; NM_138782.2. [Q0JRZ9-1]
DR PDB; 2V0O; X-ray; 2.30 A; A/B/C=3-274.
DR PDBsum; 2V0O; -.
DR AlphaFoldDB; Q0JRZ9; -.
DR SMR; Q0JRZ9; -.
DR BioGRID; 125437; 76.
DR DIP; DIP-29488N; -.
DR IntAct; Q0JRZ9; 39.
DR MINT; Q0JRZ9; -.
DR STRING; 9606.ENSP00000393776; -.
DR iPTMnet; Q0JRZ9; -.
DR PhosphoSitePlus; Q0JRZ9; -.
DR BioMuta; FCHO2; -.
DR DMDM; 119369487; -.
DR EPD; Q0JRZ9; -.
DR jPOST; Q0JRZ9; -.
DR MassIVE; Q0JRZ9; -.
DR MaxQB; Q0JRZ9; -.
DR PaxDb; Q0JRZ9; -.
DR PeptideAtlas; Q0JRZ9; -.
DR PRIDE; Q0JRZ9; -.
DR ProteomicsDB; 20262; -.
DR ProteomicsDB; 58761; -. [Q0JRZ9-1]
DR ProteomicsDB; 58762; -. [Q0JRZ9-2]
DR Antibodypedia; 48744; 149 antibodies from 23 providers.
DR DNASU; 115548; -.
DR Ensembl; ENST00000430046.7; ENSP00000393776.2; ENSG00000157107.14. [Q0JRZ9-1]
DR Ensembl; ENST00000512348.5; ENSP00000427296.1; ENSG00000157107.14. [Q0JRZ9-3]
DR GeneID; 115548; -.
DR KEGG; hsa:115548; -.
DR MANE-Select; ENST00000430046.7; ENSP00000393776.2; NM_138782.3; NP_620137.2.
DR UCSC; uc003kcl.3; human. [Q0JRZ9-1]
DR CTD; 115548; -.
DR DisGeNET; 115548; -.
DR GeneCards; FCHO2; -.
DR HGNC; HGNC:25180; FCHO2.
DR HPA; ENSG00000157107; Low tissue specificity.
DR MIM; 613438; gene.
DR neXtProt; NX_Q0JRZ9; -.
DR OpenTargets; ENSG00000157107; -.
DR PharmGKB; PA134911830; -.
DR VEuPathDB; HostDB:ENSG00000157107; -.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000157105; -.
DR HOGENOM; CLU_007107_0_0_1; -.
DR InParanoid; Q0JRZ9; -.
DR OMA; IGMADTI; -.
DR OrthoDB; 638761at2759; -.
DR PhylomeDB; Q0JRZ9; -.
DR TreeFam; TF328986; -.
DR PathwayCommons; Q0JRZ9; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q0JRZ9; -.
DR SIGNOR; Q0JRZ9; -.
DR BioGRID-ORCS; 115548; 69 hits in 1093 CRISPR screens.
DR ChiTaRS; FCHO2; human.
DR EvolutionaryTrace; Q0JRZ9; -.
DR GeneWiki; FCHO2; -.
DR GenomeRNAi; 115548; -.
DR Pharos; Q0JRZ9; Tbio.
DR PRO; PR:Q0JRZ9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q0JRZ9; protein.
DR Bgee; ENSG00000157107; Expressed in ileal mucosa and 187 other tissues.
DR ExpressionAtlas; Q0JRZ9; baseline and differential.
DR Genevisible; Q0JRZ9; HS.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0048268; P:clathrin coat assembly; IMP:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:UniProtKB.
DR GO; GO:0010324; P:membrane invagination; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR DisProt; DP02303; -.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR030122; FCHo2.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR PANTHER; PTHR23065:SF8; PTHR23065:SF8; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF10291; muHD; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coated pit; Coiled coil;
KW Disulfide bond; Endocytosis; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..810
FT /note="F-BAR domain only protein 2"
FT /id="PRO_0000266005"
FT DOMAIN 3..250
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 542..809
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 3..274
FT /note="Mediates dimerization and binding to membranes
FT enriched in Pi(4,5)-P2 and induces their tubulation"
FT REGION 301..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..810
FT /note="Mediates interaction with DAB2, EPS15, EPS15R and
FT ITSN1"
FT COILED 87..156
FT /evidence="ECO:0000255"
FT COMPBIAS 433..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQN2"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQN2"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQN2"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT DISULFID 147
FT /note="Interchain (with C-273)"
FT /evidence="ECO:0000269|PubMed:17540576"
FT DISULFID 273
FT /note="Interchain (with C-147)"
FT /evidence="ECO:0000269|PubMed:17540576"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 200..232
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044812"
FT VAR_SEQ 306..373
FT /note="ECPDADSLNIPDVDEEGYSIKPETNQNDTKENHFYSSSDSDSEDEEPKKYRI
FT EIKPMHPNNSHHTMAS -> WSFTVVAQVGMQWRDLGLLHSPPPRFKRFSSYLSLPSSW
FT NYGAHHHIWLIFCIFSRDRVSPYWPGWSRTP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021910"
FT VAR_SEQ 374..810
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021911"
FT VARIANT 371
FT /note="M -> V (in dbSNP:rs185435)"
FT /id="VAR_029636"
FT MUTAGEN 10
FT /note="F->E: Binds preferentially to larger liposomes."
FT /evidence="ECO:0000269|PubMed:17540576"
FT CONFLICT 6
FT /note="F -> L (in Ref. 2; AL831971)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="K -> E (in Ref. 1; BAG58162)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="S -> P (in Ref. 1; BAF84471)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="P -> Q (in Ref. 2; AL831971)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="D -> Y (in Ref. 1; BAG58162)"
FT /evidence="ECO:0000305"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:2V0O"
FT HELIX 17..61
FT /evidence="ECO:0007829|PDB:2V0O"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2V0O"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2V0O"
FT HELIX 73..118
FT /evidence="ECO:0007829|PDB:2V0O"
FT HELIX 120..156
FT /evidence="ECO:0007829|PDB:2V0O"
FT HELIX 160..244
FT /evidence="ECO:0007829|PDB:2V0O"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:2V0O"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2V0O"
SQ SEQUENCE 810 AA; 88924 MW; 0FCFBC5D814B5242 CRC64;
MVMAYFVENF WGEKNSGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS RSMTKLAKSA
SNYSQLGTFA PVWDVFKTST EKLANCHLDL VRKLQELIKE VQKYGEEQVK SHKKTKEEVA
GTLEAVQTIQ SITQALQKSK ENYNAKCVEQ ERLKKEGATQ REIEKAAVKS KKATDTYKLY
VEKYALAKAD FEQKMTETAQ KFQDIEETHL IHIKEIIGSL SNAIKEIHLQ IGQVHEEFIN
NMANTTVESL IQKFAESKGT GKERPGLIEF EECDTASAVE GIKPRKRKTF ALPGIIKKEK
DAESVECPDA DSLNIPDVDE EGYSIKPETN QNDTKENHFY SSSDSDSEDE EPKKYRIEIK
PMHPNNSHHT MASLDELKVS IGNITLSPAI SRHSPVQMNR NLSNEELTKS KPSAPPNEKG
TSDLLAWDPL FGPSLDSSSS SSLTSSSSAR PTTPLSVGTI VPPPRPASRP KLTSGKLSGI
NEIPRPFSPP VTSNTSPPPA APLARAESSS SISSSASLSA ANTPTVGVSR GPSPVSLGNQ
DTLPVAVALT ESVNAYFKGA DPTKCIVKIT GDMTMSFPSG IIKVFTSNPT PAVLCFRVKN
ISRLEQILPN AQLVFSDPSQ CDSNTKDFWM NMQAVTVYLK KLSEQNPAAS YYNVDVLKYQ
VSSNGIQSTP LNLATYWKCS ASTTDLRVDY KYNPEAMVAP SVLSNIQVVV PVDGGVTNMQ
SLPPAIWNAE QMKAFWKLSS ISEKSENGGS GSLRAKFDLS EGPSKPTTLA VQFLSEGSTL
SGVDFELVGT GYRLSLIKKR FATGRYLADC
