FCHO1_MOUSE
ID FCHO1_MOUSE Reviewed; 873 AA.
AC Q8K285; D3Z3Q5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=F-BAR domain only protein 1 {ECO:0000305};
GN Name=Fcho1 {ECO:0000312|MGI:MGI:1921265};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY, AND OLIGOMERIZATION.
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 [5]
RP INTERACTION WITH AP2A2 AND AP2B1.
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).
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 May regulate Bmp signaling by regulating clathrin-mediated endocytosis
CC of Bmp receptors. Involved in the regulation of T-cell poliferation and
CC activation. Affects TCR clustering upon receptor triggering and
CC modulates its internalisation, playing a role in TCR-dependent T-cell
CC activation. {ECO:0000250|UniProtKB:O14526}.
CC -!- SUBUNIT: May oligomerize and form homotetramer (PubMed:21762413).
CC Interacts with AP2A2 and AP2B1; 2 subunits of the adaptor protein
CC complex AP-2 (PubMed:22484487). Interacts with DAB2. Interacts with
CC clathrin (CLTC or CLTCL1). Interacts with EPS15, EPS15R and ITSN1.
CC Interacts with AGFG1 and CALM. May interact with ACVR1; linking this
CC receptor to clathrin-mediated endocytosis (By similarity).
CC {ECO:0000250|UniProtKB:O14526, ECO:0000269|PubMed:21762413,
CC ECO:0000269|PubMed:22484487}.
CC -!- INTERACTION:
CC Q8K285; Q9CR95: Necap1; NbExp=2; IntAct=EBI-16078916, EBI-7592476;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:O14526}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O14526}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O14526}. Note=Associated with forming but not
CC mature clathrin-coated vesicles. The recruitment to coated-pits precede
CC the one of clathrin and the adaptor protein complex AP-2. According to
CC it may also dynamically associate with Golgi/TGN membranes.
CC {ECO:0000250|UniProtKB:O14526}.
CC -!- TISSUE SPECIFICITY: Mainly detected in brain and spleen.
CC {ECO:0000269|PubMed:21762413}.
CC -!- SIMILARITY: Belongs to the FCHO family. {ECO:0000305}.
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DR EMBL; AC162033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032207; AAH32207.1; -; mRNA.
DR CCDS; CCDS52588.1; -.
DR RefSeq; NP_082991.3; NM_028715.3.
DR RefSeq; XP_006509828.1; XM_006509765.2.
DR RefSeq; XP_006509829.1; XM_006509766.3.
DR RefSeq; XP_006509830.1; XM_006509767.3.
DR AlphaFoldDB; Q8K285; -.
DR SMR; Q8K285; -.
DR BioGRID; 216425; 3.
DR DIP; DIP-60611N; -.
DR IntAct; Q8K285; 1.
DR STRING; 10090.ENSMUSP00000117606; -.
DR iPTMnet; Q8K285; -.
DR PhosphoSitePlus; Q8K285; -.
DR EPD; Q8K285; -.
DR jPOST; Q8K285; -.
DR MaxQB; Q8K285; -.
DR PaxDb; Q8K285; -.
DR PRIDE; Q8K285; -.
DR ProteomicsDB; 271733; -.
DR Antibodypedia; 27790; 116 antibodies from 21 providers.
DR DNASU; 74015; -.
DR Ensembl; ENSMUST00000093444; ENSMUSP00000091151; ENSMUSG00000070000.
DR Ensembl; ENSMUST00000146100; ENSMUSP00000117606; ENSMUSG00000070000.
DR GeneID; 74015; -.
DR KEGG; mmu:74015; -.
DR UCSC; uc033jge.1; mouse.
DR CTD; 23149; -.
DR MGI; MGI:1921265; Fcho1.
DR VEuPathDB; HostDB:ENSMUSG00000070000; -.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000160489; -.
DR HOGENOM; CLU_007107_0_0_1; -.
DR InParanoid; Q8K285; -.
DR OMA; FAASECK; -.
DR OrthoDB; 638761at2759; -.
DR PhylomeDB; Q8K285; -.
DR TreeFam; TF328986; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 74015; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q8K285; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K285; protein.
DR Bgee; ENSMUSG00000070000; Expressed in embryonic brain and 149 other tissues.
DR ExpressionAtlas; Q8K285; baseline and differential.
DR Genevisible; Q8K285; MM.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; ISO:MGI.
DR GO; GO:0048268; P:clathrin coat assembly; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR CDD; cd07674; F-BAR_FCHO1; 1.
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; IPR030121; FCHo1.
DR InterPro; IPR042735; FCHo1_F-BAR.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR PANTHER; PTHR23065:SF6; PTHR23065:SF6; 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 Coated pit; Coiled coil; Endocytosis; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..873
FT /note="F-BAR domain only protein 1"
FT /id="PRO_0000271760"
FT DOMAIN 1..248
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 609..872
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 1..275
FT /note="Mediates membrane-binding"
FT /evidence="ECO:0000250"
FT REGION 153..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..439
FT /note="Mediates interaction with the adaptor protein
FT complex AP-2"
FT /evidence="ECO:0000250"
FT REGION 302..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..873
FT /note="Mediates interaction with AGFG1, CALM, DAB2, EPS15,
FT EPS15R, ITSN1 and clathrin"
FT /evidence="ECO:0000250"
FT REGION 813..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 155..178
FT /evidence="ECO:0000255"
FT COMPBIAS 324..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14526"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14526"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14526"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14526"
FT CONFLICT 609
FT /note="A -> T (in Ref. 2; AAH32207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 873 AA; 95122 MW; E0D2549EF2A5C020 CRC64;
MSYFGEHFWG DKNHGFEVLY HCVKQGPVAT KELADFIRER ANIEETYSKA MAKLSKLASN
GTPMGTFAPL WEVFRVSSDK LALCHLELTR KLHDLLKDVL RYGEEQLKTH KKCKEEVLGT
VDAVQMLSGV GQLLPKSREN YLSRCMDLER LRRENTSQKE MDKAETKSKK AADSLRRSVD
KYNSARADFE IKMLDSALRF QAMEEAHLQH MKALLGSYAH SVEDTHVQIG QVHEEFKQNV
ENVTVDMLLR KFAESKGTGR EKPGPLDFDA YSSAALQEAM KRLRGAKAFR LPGLSRREPR
ASVDFLESDS GVPPEVDDEG FTVRPDISQN NGAEPPRFSS SDSDFDDEEP RKFYVHIKPA
PTRAVACSSE AAAAQLRATA GSLILPPGPG GTMKRHSSRD TSGKPQRPRS APRTGSCAEK
PLASEEPLSK SLFGPPLESA FDHDDFTGSS SLGFTSSPSP FSSSSPENVE DSGLDSPSHA
APGPSPESWV PRPGTPQSPP TCRAQHPEPR GLMPRAPSPG PWGPEGGADS LTPADPTREG
LAATLRRPRS RKVSCPLTRS NGDLCRSLSP SPLGSSAPTI PPDRPSFSTQ MGHGISRGPS
PVVLGSQDAL PVATAFTEYV HAYFRGHSPS CLARVTGELT MTFPAGIVRV FSGTPPPPVL
SFRLVNTAPV EHFQPNADLI FSDPSQSDPE TKDFWLNMAA LTEALQHQAE QNPTASYYNL
VLLRYQFSRP GPESVPLQMS AHWQCGPTLT RVSVEYSYRA GATAVSTPLT NVQILLPVGE
PVTSVRLQPA ATWNTEEKRF TWKLPDVCEA GGSGHLSASW QPQSGPSTPS PVAAQFTSEG
ATLSGLDLEL LGGGYRMSLV KRRFATGMYL VSC
