Full text data of FCHO2
FCHO2
[Confidence: low (only semi-automatic identification from reviews)]
FCH domain only protein 2
FCH domain only protein 2
UniProt
Q0JRZ9
ID FCHO2_HUMAN Reviewed; 810 AA.
AC Q0JRZ9; A8K6W7; B2RNQ9; B4DHK0; E9PG79; Q0JTJ3; Q96CF5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 12-DEC-2006, sequence version 2.
DT 22-JAN-2014, entry version 71.
DE RecName: Full=FCH domain only protein 2;
GN Name=FCHO2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA 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
RT project: 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-403, AND
RP MASS SPECTROMETRY.
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
RT phosphorylation 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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP FUNCTION IN CLATHRIN-COATED PITS NUCLEATION, AND INTERACTION WITH
RP EPS15; EPS15R; ITSN1 AND ITSN2.
RX PubMed=20448150; DOI=10.1126/science.1188462;
RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y.,
RA Mittal R., 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome 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
RT with 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 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
RT membrane recruitment module that effects membrane curvature.";
RL Structure 15:839-852(2007).
CC -!- FUNCTION: Functions in an early step of clathrin-mediated
CC endocytosis. Has both a membrane binding/bending activity and the
CC ability to recruit proteins essential to the formation of
CC functional clathrin-coated pits. Has a lipid-binding activity with
CC a preference for membranes enriched in phosphatidylserine and
CC phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane.
CC Its membrane-bending activity might be important for the
CC subsequent action of clathrin and adaptors in the formation of
CC clathrin-coated vesicles. Involved in adaptor protein complex AP-
CC 2-dependent endocytosis of the transferin receptor, it also
CC functions in the AP-2-independent endocytosis of the LDL receptor.
CC -!- SUBUNIT: Homodimer; disulfide-linked. May form homotetramer.
CC Interacts with AP2A1. Interacts with EPS15, EPS15R, ITSN1 and
CC ITSN2; recruit those scaffolding proteins which in turn may
CC interact with the adaptor protein complex AP-2 at the plasma
CC membrane. Interacts with DAB2 (via DPF motifs); mediates LDL
CC receptor/LDLR endocytosis.
CC -!- INTERACTION:
CC P98078:Dab2 (xeno); NbExp=4; IntAct=EBI-2609756, EBI-1391846;
CC P42566:EPS15; NbExp=3; IntAct=EBI-2609756, EBI-396684;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit; Peripheral
CC membrane protein; Cytoplasmic side (By similarity).
CC Note=Associated with forming but not mature clathrin-coated
CC vesicles. The recruitment to coated-pits precede the one of
CC clathrin and the adaptor protein complex AP-2 (By similarity).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q0JRZ9-3; Sequence=VSP_044812;
CC Note=No experimental confirmation available;
CC -!- PTM: Ubiquitinated. Mainly undergoes monoubiquitination but also
CC polyubiquitination (By similarity).
CC -!- MISCELLANEOUS: Deforms liposomes into a range of tubule diameters
CC from 20 to 130 nm in vitro.
CC -!- SIMILARITY: Belongs to the FCHO family.
CC -!- SIMILARITY: Contains 1 FCH domain.
CC -!- SIMILARITY: Contains 1 MHD (mu homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14311.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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 RefSeq; NP_001139504.1; NM_001146032.1.
DR RefSeq; NP_620137.2; NM_138782.2.
DR UniGene; Hs.165762; -.
DR PDB; 2V0O; X-ray; 2.30 A; A/B/C=3-274.
DR PDBsum; 2V0O; -.
DR ProteinModelPortal; Q0JRZ9; -.
DR SMR; Q0JRZ9; 3-274.
DR DIP; DIP-29488N; -.
DR IntAct; Q0JRZ9; 10.
DR STRING; 9606.ENSP00000393776; -.
DR PhosphoSite; Q0JRZ9; -.
DR DMDM; 119369487; -.
DR PaxDb; Q0JRZ9; -.
DR PRIDE; Q0JRZ9; -.
DR DNASU; 115548; -.
DR Ensembl; ENST00000430046; ENSP00000393776; ENSG00000157107.
DR Ensembl; ENST00000512348; ENSP00000427296; ENSG00000157107.
DR GeneID; 115548; -.
DR KEGG; hsa:115548; -.
DR UCSC; uc011csl.2; human.
DR CTD; 115548; -.
DR GeneCards; GC05P072287; -.
DR H-InvDB; HIX0004941; -.
DR HGNC; HGNC:25180; FCHO2.
DR HPA; HPA037686; -.
DR MIM; 613438; gene.
DR neXtProt; NX_Q0JRZ9; -.
DR PharmGKB; PA134911830; -.
DR eggNOG; NOG324072; -.
DR HOGENOM; HOG000231544; -.
DR HOVERGEN; HBG081524; -.
DR InParanoid; Q0JRZ9; -.
DR OMA; FNCEGTT; -.
DR OrthoDB; EOG712TVK; -.
DR ChiTaRS; FCHO2; human.
DR EvolutionaryTrace; Q0JRZ9; -.
DR GeneWiki; FCHO2; -.
DR GenomeRNAi; 115548; -.
DR NextBio; 79607; -.
DR PRO; PR:Q0JRZ9; -.
DR ArrayExpress; Q0JRZ9; -.
DR Bgee; Q0JRZ9; -.
DR CleanEx; HS_FCHO2; -.
DR Genevestigator; Q0JRZ9; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; 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-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0010324; P:membrane invagination; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF10291; muHD; 1.
DR SMART; SM00055; FCH; 1.
DR PROSITE; PS50133; FCH; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coated pit; Coiled coil;
KW Complete proteome; Disulfide bond; Endocytosis; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
FT CHAIN 1 810 FCH domain only protein 2.
FT /FTId=PRO_0000266005.
FT DOMAIN 4 85 FCH.
FT DOMAIN 542 809 MHD.
FT REGION 3 274 Mediates dimerization and binding to
FT membranes enriched in Pi(4,5)-P2 and
FT induces their tubulation.
FT REGION 521 810 Mediates interaction with DAB2, EPS15,
FT EPS15R and ITSN1.
FT COILED 87 156 Potential.
FT COMPBIAS 434 519 Ser-rich.
FT MOD_RES 385 385 Phosphothreonine.
FT MOD_RES 387 387 Phosphoserine.
FT MOD_RES 394 394 Phosphoserine.
FT MOD_RES 403 403 Phosphoserine.
FT MOD_RES 488 488 Phosphoserine.
FT MOD_RES 511 511 Phosphoserine.
FT MOD_RES 533 533 Phosphoserine.
FT DISULFID 147 147 Interchain (with C-273).
FT DISULFID 273 273 Interchain (with C-147).
FT VAR_SEQ 200 232 Missing (in isoform 3).
FT /FTId=VSP_044812.
FT VAR_SEQ 306 373 ECPDADSLNIPDVDEEGYSIKPETNQNDTKENHFYSSSDSD
FT SEDEEPKKYRIEIKPMHPNNSHHTMAS -> WSFTVVAQVG
FT MQWRDLGLLHSPPPRFKRFSSYLSLPSSWNYGAHHHIWLIF
FT CIFSRDRVSPYWPGWSRTP (in isoform 2).
FT /FTId=VSP_021910.
FT VAR_SEQ 374 810 Missing (in isoform 2).
FT /FTId=VSP_021911.
FT VARIANT 371 371 M -> V (in dbSNP:rs185435).
FT /FTId=VAR_029636.
FT MUTAGEN 10 10 F->E: Binds preferentially to larger
FT liposomes.
FT CONFLICT 6 6 F -> L (in Ref. 2; AL831971).
FT CONFLICT 286 286 K -> E (in Ref. 1; BAG58162).
FT CONFLICT 439 439 S -> P (in Ref. 1; BAF84471).
FT CONFLICT 462 462 P -> Q (in Ref. 2; AL831971).
FT CONFLICT 617 617 D -> Y (in Ref. 1; BAG58162).
FT HELIX 5 9
FT HELIX 17 61
FT STRAND 67 69
FT HELIX 70 72
FT HELIX 73 118
FT HELIX 120 156
FT HELIX 160 244
FT HELIX 247 258
FT STRAND 261 263
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
//
ID FCHO2_HUMAN Reviewed; 810 AA.
AC Q0JRZ9; A8K6W7; B2RNQ9; B4DHK0; E9PG79; Q0JTJ3; Q96CF5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 12-DEC-2006, sequence version 2.
DT 22-JAN-2014, entry version 71.
DE RecName: Full=FCH domain only protein 2;
GN Name=FCHO2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA 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
RT project: 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-403, AND
RP MASS SPECTROMETRY.
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
RT phosphorylation 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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP FUNCTION IN CLATHRIN-COATED PITS NUCLEATION, AND INTERACTION WITH
RP EPS15; EPS15R; ITSN1 AND ITSN2.
RX PubMed=20448150; DOI=10.1126/science.1188462;
RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y.,
RA Mittal R., 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome 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
RT with 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 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
RT membrane recruitment module that effects membrane curvature.";
RL Structure 15:839-852(2007).
CC -!- FUNCTION: Functions in an early step of clathrin-mediated
CC endocytosis. Has both a membrane binding/bending activity and the
CC ability to recruit proteins essential to the formation of
CC functional clathrin-coated pits. Has a lipid-binding activity with
CC a preference for membranes enriched in phosphatidylserine and
CC phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane.
CC Its membrane-bending activity might be important for the
CC subsequent action of clathrin and adaptors in the formation of
CC clathrin-coated vesicles. Involved in adaptor protein complex AP-
CC 2-dependent endocytosis of the transferin receptor, it also
CC functions in the AP-2-independent endocytosis of the LDL receptor.
CC -!- SUBUNIT: Homodimer; disulfide-linked. May form homotetramer.
CC Interacts with AP2A1. Interacts with EPS15, EPS15R, ITSN1 and
CC ITSN2; recruit those scaffolding proteins which in turn may
CC interact with the adaptor protein complex AP-2 at the plasma
CC membrane. Interacts with DAB2 (via DPF motifs); mediates LDL
CC receptor/LDLR endocytosis.
CC -!- INTERACTION:
CC P98078:Dab2 (xeno); NbExp=4; IntAct=EBI-2609756, EBI-1391846;
CC P42566:EPS15; NbExp=3; IntAct=EBI-2609756, EBI-396684;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit; Peripheral
CC membrane protein; Cytoplasmic side (By similarity).
CC Note=Associated with forming but not mature clathrin-coated
CC vesicles. The recruitment to coated-pits precede the one of
CC clathrin and the adaptor protein complex AP-2 (By similarity).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q0JRZ9-3; Sequence=VSP_044812;
CC Note=No experimental confirmation available;
CC -!- PTM: Ubiquitinated. Mainly undergoes monoubiquitination but also
CC polyubiquitination (By similarity).
CC -!- MISCELLANEOUS: Deforms liposomes into a range of tubule diameters
CC from 20 to 130 nm in vitro.
CC -!- SIMILARITY: Belongs to the FCHO family.
CC -!- SIMILARITY: Contains 1 FCH domain.
CC -!- SIMILARITY: Contains 1 MHD (mu homology) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14311.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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 RefSeq; NP_001139504.1; NM_001146032.1.
DR RefSeq; NP_620137.2; NM_138782.2.
DR UniGene; Hs.165762; -.
DR PDB; 2V0O; X-ray; 2.30 A; A/B/C=3-274.
DR PDBsum; 2V0O; -.
DR ProteinModelPortal; Q0JRZ9; -.
DR SMR; Q0JRZ9; 3-274.
DR DIP; DIP-29488N; -.
DR IntAct; Q0JRZ9; 10.
DR STRING; 9606.ENSP00000393776; -.
DR PhosphoSite; Q0JRZ9; -.
DR DMDM; 119369487; -.
DR PaxDb; Q0JRZ9; -.
DR PRIDE; Q0JRZ9; -.
DR DNASU; 115548; -.
DR Ensembl; ENST00000430046; ENSP00000393776; ENSG00000157107.
DR Ensembl; ENST00000512348; ENSP00000427296; ENSG00000157107.
DR GeneID; 115548; -.
DR KEGG; hsa:115548; -.
DR UCSC; uc011csl.2; human.
DR CTD; 115548; -.
DR GeneCards; GC05P072287; -.
DR H-InvDB; HIX0004941; -.
DR HGNC; HGNC:25180; FCHO2.
DR HPA; HPA037686; -.
DR MIM; 613438; gene.
DR neXtProt; NX_Q0JRZ9; -.
DR PharmGKB; PA134911830; -.
DR eggNOG; NOG324072; -.
DR HOGENOM; HOG000231544; -.
DR HOVERGEN; HBG081524; -.
DR InParanoid; Q0JRZ9; -.
DR OMA; FNCEGTT; -.
DR OrthoDB; EOG712TVK; -.
DR ChiTaRS; FCHO2; human.
DR EvolutionaryTrace; Q0JRZ9; -.
DR GeneWiki; FCHO2; -.
DR GenomeRNAi; 115548; -.
DR NextBio; 79607; -.
DR PRO; PR:Q0JRZ9; -.
DR ArrayExpress; Q0JRZ9; -.
DR Bgee; Q0JRZ9; -.
DR CleanEx; HS_FCHO2; -.
DR Genevestigator; Q0JRZ9; -.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; 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-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0010324; P:membrane invagination; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF10291; muHD; 1.
DR SMART; SM00055; FCH; 1.
DR PROSITE; PS50133; FCH; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coated pit; Coiled coil;
KW Complete proteome; Disulfide bond; Endocytosis; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
FT CHAIN 1 810 FCH domain only protein 2.
FT /FTId=PRO_0000266005.
FT DOMAIN 4 85 FCH.
FT DOMAIN 542 809 MHD.
FT REGION 3 274 Mediates dimerization and binding to
FT membranes enriched in Pi(4,5)-P2 and
FT induces their tubulation.
FT REGION 521 810 Mediates interaction with DAB2, EPS15,
FT EPS15R and ITSN1.
FT COILED 87 156 Potential.
FT COMPBIAS 434 519 Ser-rich.
FT MOD_RES 385 385 Phosphothreonine.
FT MOD_RES 387 387 Phosphoserine.
FT MOD_RES 394 394 Phosphoserine.
FT MOD_RES 403 403 Phosphoserine.
FT MOD_RES 488 488 Phosphoserine.
FT MOD_RES 511 511 Phosphoserine.
FT MOD_RES 533 533 Phosphoserine.
FT DISULFID 147 147 Interchain (with C-273).
FT DISULFID 273 273 Interchain (with C-147).
FT VAR_SEQ 200 232 Missing (in isoform 3).
FT /FTId=VSP_044812.
FT VAR_SEQ 306 373 ECPDADSLNIPDVDEEGYSIKPETNQNDTKENHFYSSSDSD
FT SEDEEPKKYRIEIKPMHPNNSHHTMAS -> WSFTVVAQVG
FT MQWRDLGLLHSPPPRFKRFSSYLSLPSSWNYGAHHHIWLIF
FT CIFSRDRVSPYWPGWSRTP (in isoform 2).
FT /FTId=VSP_021910.
FT VAR_SEQ 374 810 Missing (in isoform 2).
FT /FTId=VSP_021911.
FT VARIANT 371 371 M -> V (in dbSNP:rs185435).
FT /FTId=VAR_029636.
FT MUTAGEN 10 10 F->E: Binds preferentially to larger
FT liposomes.
FT CONFLICT 6 6 F -> L (in Ref. 2; AL831971).
FT CONFLICT 286 286 K -> E (in Ref. 1; BAG58162).
FT CONFLICT 439 439 S -> P (in Ref. 1; BAF84471).
FT CONFLICT 462 462 P -> Q (in Ref. 2; AL831971).
FT CONFLICT 617 617 D -> Y (in Ref. 1; BAG58162).
FT HELIX 5 9
FT HELIX 17 61
FT STRAND 67 69
FT HELIX 70 72
FT HELIX 73 118
FT HELIX 120 156
FT HELIX 160 244
FT HELIX 247 258
FT STRAND 261 263
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
//
MIM
613438
*RECORD*
*FIELD* NO
613438
*FIELD* TI
*613438 FCH DOMAIN ONLY PROTEIN 2; FCHO2
*FIELD* TX
CLONING
By searching databases for genes encoding a FES (190030)-CIP4 (TRIP10;
read more604504) homology (FCH) domain, Katoh and Katoh (2004) identified FCHO2.
The deduced 810-amino acid protein contains an N-terminal FCH domain and
an evolutionarily conserved C-terminal FCHO homology (FOH) domain. FCHO2
shares 94.6% identity with mouse Fcho2 and 50.4% identity with human
FCHO1 (613437).
GENE FUNCTION
Henne et al. (2010) reported that the membrane-sculpting F-BAR
domain-containing Fer/Cip4 homology domain-only proteins 1 and 2
(FCHO1/2) are required for plasma membrane clathrin-coated vesicle (CCV)
budding and marked sites of CCV formation. Changes in FCHO1/2 expression
levels correlated directly with numbers of CCV budding events, ligand
endocytosis, and synaptic vesicle marker recycling. FCHO1/2 proteins
bound specifically to the plasma membrane and recruited the scaffold
proteins eps15 (600051) and intersectin (602442), which in turn engaged
the adaptor complex AP2 (see 601024). The FCHO F-BAR membrane-bending
activity was required, leading to the proposal that FCHO1/2 sculpt the
initial bud site and recruit the clathrin machinery for CCV formation.
GENE STRUCTURE
Katoh and Katoh (2004) determined that the FCHO2 gene contains at least
26 exons and spans 134.4 kb.
MAPPING
By genomic sequence analysis, Katoh and Katoh (2004) mapped the FCHO2
gene to chromosome 5q13.2.
*FIELD* RF
1. Henne, W. M.; Boucrot, E.; Meinecke, M.; Evergren, E.; Vallis,
Y.; Mittal, R.; McMahon, H. T.: FCHo proteins are nucleators of clathrin-mediated
endocytosis. Science 328: 1281-1284, 2010.
2. Katoh, M.; Katoh, M.: Identification and characterization of human
FCHO2 and mouse Fcho2 genes in silico. Int. J. Molec. Med. 14: 327-331,
2004.
*FIELD* CN
Ada Hamosh - updated: 6/30/2010
*FIELD* CD
Patricia A. Hartz: 6/10/2010
*FIELD* ED
alopez: 07/01/2010
terry: 6/30/2010
mgross: 6/10/2010
*RECORD*
*FIELD* NO
613438
*FIELD* TI
*613438 FCH DOMAIN ONLY PROTEIN 2; FCHO2
*FIELD* TX
CLONING
By searching databases for genes encoding a FES (190030)-CIP4 (TRIP10;
read more604504) homology (FCH) domain, Katoh and Katoh (2004) identified FCHO2.
The deduced 810-amino acid protein contains an N-terminal FCH domain and
an evolutionarily conserved C-terminal FCHO homology (FOH) domain. FCHO2
shares 94.6% identity with mouse Fcho2 and 50.4% identity with human
FCHO1 (613437).
GENE FUNCTION
Henne et al. (2010) reported that the membrane-sculpting F-BAR
domain-containing Fer/Cip4 homology domain-only proteins 1 and 2
(FCHO1/2) are required for plasma membrane clathrin-coated vesicle (CCV)
budding and marked sites of CCV formation. Changes in FCHO1/2 expression
levels correlated directly with numbers of CCV budding events, ligand
endocytosis, and synaptic vesicle marker recycling. FCHO1/2 proteins
bound specifically to the plasma membrane and recruited the scaffold
proteins eps15 (600051) and intersectin (602442), which in turn engaged
the adaptor complex AP2 (see 601024). The FCHO F-BAR membrane-bending
activity was required, leading to the proposal that FCHO1/2 sculpt the
initial bud site and recruit the clathrin machinery for CCV formation.
GENE STRUCTURE
Katoh and Katoh (2004) determined that the FCHO2 gene contains at least
26 exons and spans 134.4 kb.
MAPPING
By genomic sequence analysis, Katoh and Katoh (2004) mapped the FCHO2
gene to chromosome 5q13.2.
*FIELD* RF
1. Henne, W. M.; Boucrot, E.; Meinecke, M.; Evergren, E.; Vallis,
Y.; Mittal, R.; McMahon, H. T.: FCHo proteins are nucleators of clathrin-mediated
endocytosis. Science 328: 1281-1284, 2010.
2. Katoh, M.; Katoh, M.: Identification and characterization of human
FCHO2 and mouse Fcho2 genes in silico. Int. J. Molec. Med. 14: 327-331,
2004.
*FIELD* CN
Ada Hamosh - updated: 6/30/2010
*FIELD* CD
Patricia A. Hartz: 6/10/2010
*FIELD* ED
alopez: 07/01/2010
terry: 6/30/2010
mgross: 6/10/2010