FCHO2_RAT
ID FCHO2_RAT Reviewed; 809 AA.
AC D3ZYR1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=F-BAR domain only protein 2;
GN Name=Fcho2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP TISSUE SPECIFICITY.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-387; SER-394;
RP SER-487; SER-495 AND SER-532, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(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 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 (By similarity).
CC {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC {ECO:0000269|PubMed:21762413}.
CC -!- PTM: Ubiquitinated. Mainly undergoes monoubiquitination but also
CC polyubiquitination (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FCHO family. {ECO:0000305}.
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DR EMBL; AABR03015854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03014744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03015771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03013202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D3ZYR1; -.
DR SMR; D3ZYR1; -.
DR STRING; 10116.ENSRNOP00000020692; -.
DR iPTMnet; D3ZYR1; -.
DR jPOST; D3ZYR1; -.
DR PaxDb; D3ZYR1; -.
DR PeptideAtlas; D3ZYR1; -.
DR PRIDE; D3ZYR1; -.
DR Ensembl; ENSRNOT00000100868; ENSRNOP00000082647; ENSRNOG00000015334.
DR RGD; 1565396; Fcho2.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000157105; -.
DR HOGENOM; CLU_007107_0_0_1; -.
DR InParanoid; D3ZYR1; -.
DR OMA; IGMADTI; -.
DR PhylomeDB; D3ZYR1; -.
DR TreeFam; TF328986; -.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:D3ZYR1; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000015334; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; D3ZYR1; RN.
DR GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS: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; IGI:SynGO.
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 Coated pit; Coiled coil; Disulfide bond; Endocytosis; Isopeptide bond;
KW Membrane; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..809
FT /note="F-BAR domain only protein 2"
FT /id="PRO_0000417674"
FT DOMAIN 3..250
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 541..808
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 /evidence="ECO:0000250"
FT REGION 301..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..809
FT /note="Mediates interaction with DAB2, EPS15, EPS15R and
FT ITSN1"
FT /evidence="ECO:0000250"
FT COILED 87..156
FT /evidence="ECO:0000255"
FT COMPBIAS 390..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQN2"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQN2"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQN2"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT DISULFID 147
FT /note="Interchain (with C-273)"
FT /evidence="ECO:0000250"
FT DISULFID 273
FT /note="Interchain (with C-147)"
FT /evidence="ECO:0000250"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
SQ SEQUENCE 809 AA; 88712 MW; 9827B74D30A3C4DC CRC64;
MVMAHFVENF WGEKNNGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS RSMTKLAKSA
SNYSQLGTFA PVWDVFKTST EKLANCHLDL VRKLQELIKE VQKYGEEQVK SHKKTKEEVA
GTLEAVQAIQ NITQALQKSK ENYNAKCVEQ ERLKKEGATP REIEKAAVKS KKATDTYKLY
VEKYALTKAD FEQKMTETAQ KFQDIEETHL IHIKEIIGSL SNAIKEIHLQ IGQVHEEFIN
NMANTTIESL IQKFAESKGT GKERPGLIEF EECDPASAVE GIKPRKRKTF ALPGIIKKEK
DAESVECPDA DSLNIPDVDE EGFSIKPEAN QNDTKENHFY SSSDSDSEDE EPKRYRIEIK
PVHPNNVHHT MASLDELKVS IGNITLSPAV SRHSPVQMNR NSSNEELTKS KPSSLPTEKG
TNDLLAWDPL FGSSLESSSA PLTSSSSARP TTPLSLGTIV PPPRPASRPK LTSGKLSGIN
EIPRPFSPPI TSNTSPPPTA PLARAESSSS ISSSASLSAA NTPTVGVSRG PSPVSLGNQD
TLPVAIALTE SVNAYFKGAD PTKCIVKITG DVTISFPSGI IKVFTSNPSP AVLCFRVKNI
SRLEQILPNS QLVFSDPSQC DSNTKDFWMN MQAVTVYLKK LSEQNPAASY YNVDVLKYQV
SSNGIQSTPL NLATYWKCSA STTDLRVDYK YNPEAMVAPS VLSNIQVVVP VDGGVTNMQS
LPPAIWNAEQ MKAFWKLSGI SEKSDSGGSG SLRAKFDLSE GPSKPATLAV QFLSEGNTLS
GVDIELVGTG YRLSLVKKRF ATGRYLADC
