FNBP1_RAT
ID FNBP1_RAT Reviewed; 616 AA.
AC Q8R511; Q75UE2; Q75UE3; Q75UE4; Q75UE5; Q75UE6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Formin-binding protein 1;
DE AltName: Full=Formin-binding protein 17;
DE AltName: Full=Rapostlin;
GN Name=Fnbp1; Synonyms=Fbp17;
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 [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH RND2 AND
RP MICROTUBULES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12244061; DOI=10.1074/jbc.m208090200;
RA Fujita H., Katoh H., Ishikawa Y., Mori K., Negishi M.;
RT "Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching.";
RL J. Biol. Chem. 277:45428-45434(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), FUNCTION,
RP INTERACTION WITH CDC42; RND2 AND WASL, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=14732713; DOI=10.1074/jbc.m312763200;
RA Kakimoto T., Katoh H., Negishi M.;
RT "Identification of splicing variants of Rapostlin, a novel RND2 effector
RT that interacts with neural Wiskott-Aldrich syndrome protein and induces
RT neurite branching.";
RL J. Biol. Chem. 279:14104-14110(2004).
RN [3]
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 [4]
RP INTERACTION WITH PDE6G, AND MUTAGENESIS OF TRP-587 AND PRO-601.
RX PubMed=14502124;
RA Morin F., Vannier B., Houdart F., Regnacq M., Berges T., Voisin P.;
RT "A proline-rich domain in the gamma subunit of phosphodiesterase 6 mediates
RT interaction with SH3-containing proteins.";
RL Mol. Vis. 9:449-459(2003).
RN [5]
RP INTERACTION WITH PDE6G.
RX PubMed=16357825;
RA Houdart F., Girard-Nau N., Morin F., Voisin P., Vannier B.;
RT "The regulatory subunit of PDE6 interacts with PACSIN in photoreceptors.";
RL Mol. Vis. 11:1061-1070(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299 AND SER-520, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Required to coordinate membrane tubulation with
CC reorganization of the actin cytoskeleton during the late stage of
CC clathrin-mediated endocytosis. Binds to lipids such as
CC phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and
CC promotes membrane invagination and the formation of tubules. Also
CC enhances actin polymerization via the recruitment of WASL/N-WASP, which
CC in turn activates the Arp2/3 complex. Actin polymerization may promote
CC the fission of membrane tubules to form endocytic vesicles. May be
CC required for the lysosomal retention of FASLG/FASL (By similarity). May
CC act as a link between RND2 signaling and regulation of the actin
CC cytoskeleton. Isoform 1 and isoform 2 promote RND2-induced neurite
CC branching in neuronal cells. {ECO:0000250, ECO:0000269|PubMed:12244061,
CC ECO:0000269|PubMed:14732713}.
CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form
CC filamentous structures. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1,
CC DIAPH2, DNM1, DNM2, DNM3, FASLG/FASL, and SNX2. May interact with TNKS
CC (By similarity). Interacts specifically with GTP-bound RND2 and CDC42.
CC Interacts with PDE6G, WASL/N-WASP and microtubules. {ECO:0000250,
CC ECO:0000269|PubMed:12244061, ECO:0000269|PubMed:14502124,
CC ECO:0000269|PubMed:14732713, ECO:0000269|PubMed:16357825}.
CC -!- INTERACTION:
CC Q8R511; P18545: PDE6G; Xeno; NbExp=2; IntAct=EBI-1111424, EBI-2622029;
CC Q8R511; P52198: RND2; Xeno; NbExp=2; IntAct=EBI-1111424, EBI-1111436;
CC Q8R511; O00401: WASL; Xeno; NbExp=2; IntAct=EBI-1111424, EBI-957615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm. Cytoplasmic
CC vesicle {ECO:0000250}. Lysosome {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane,
CC clathrin-coated pit {ECO:0000250}. Note=Enriched in cortical regions
CC coincident with F-actin. Also localizes to endocytic vesicles and
CC lysosomes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q8R511-1; Sequence=Displayed;
CC Name=2; Synonyms=L;
CC IsoId=Q8R511-2; Sequence=VSP_021708;
CC Name=3; Synonyms=Ld;
CC IsoId=Q8R511-3; Sequence=VSP_021707, VSP_021708;
CC Name=4; Synonyms=M;
CC IsoId=Q8R511-4; Sequence=VSP_021706, VSP_021708;
CC Name=5; Synonyms=Md;
CC IsoId=Q8R511-5; Sequence=VSP_021706, VSP_021707, VSP_021708;
CC Name=6; Synonyms=S;
CC IsoId=Q8R511-6; Sequence=VSP_021705, VSP_021708;
CC Name=7; Synonyms=Sd;
CC IsoId=Q8R511-7; Sequence=VSP_021704, VSP_021708;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and lung. Expressed at
CC lower levels in colon, heart, kidney, liver, small intestine, spleen,
CC testis and thymus. Isoform 1 and isoform 2 are the major isoforms in
CC brain while isoform 5 and isoform 6 are the major isoforms in lung,
CC spleen, testis and thymus. {ECO:0000269|PubMed:12244061,
CC ECO:0000269|PubMed:14732713}.
CC -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its
CC concave surface. The end-to-end polymerization of dimers of these
CC domains provides a curved surface that fits best membranes with around
CC 600 A diameter, and may drive tubulation (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform in brain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FNBP1 family. {ECO:0000305}.
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DR EMBL; AB073208; BAB90845.1; -; mRNA.
DR EMBL; AB126168; BAD13422.1; -; mRNA.
DR EMBL; AB126169; BAD13423.1; -; mRNA.
DR EMBL; AB126170; BAD13424.1; -; mRNA.
DR EMBL; AB126171; BAD13425.1; -; mRNA.
DR EMBL; AB126172; BAD13426.1; -; mRNA.
DR EMBL; AABR03024172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03024739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_620269.1; NM_138914.1. [Q8R511-2]
DR AlphaFoldDB; Q8R511; -.
DR SMR; Q8R511; -.
DR BioGRID; 251405; 4.
DR IntAct; Q8R511; 3.
DR MINT; Q8R511; -.
DR STRING; 10116.ENSRNOP00000049838; -.
DR iPTMnet; Q8R511; -.
DR PhosphoSitePlus; Q8R511; -.
DR jPOST; Q8R511; -.
DR PaxDb; Q8R511; -.
DR PRIDE; Q8R511; -.
DR Ensembl; ENSRNOT00000119171; ENSRNOP00000077955; ENSRNOG00000008258. [Q8R511-1]
DR GeneID; 192348; -.
DR KEGG; rno:192348; -.
DR UCSC; RGD:621350; rat. [Q8R511-1]
DR CTD; 23048; -.
DR RGD; 621350; Fnbp1.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000183047; -.
DR InParanoid; Q8R511; -.
DR OrthoDB; 348563at2759; -.
DR PhylomeDB; Q8R511; -.
DR TreeFam; TF351162; -.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR PRO; PR:Q8R511; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IDA:RGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07676; F-BAR_FBP17; 1.
DR CDD; cd12071; SH3_FBP17; 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; IPR028532; FNBP1/FBP17.
DR InterPro; IPR037449; FNBP1_F-BAR.
DR InterPro; IPR035492; FNBP1_SH3.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735:SF13; PTHR15735:SF13; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Coated pit; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Developmental protein;
KW Differentiation; Endocytosis; Lipid-binding; Lysosome; Membrane;
KW Neurogenesis; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..616
FT /note="Formin-binding protein 1"
FT /id="PRO_0000261432"
FT DOMAIN 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 403..480
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 549..610
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..334
FT /note="Interaction with microtubules"
FT REGION 1..79
FT /note="Required for self-association and induction of
FT membrane tubulation"
FT /evidence="ECO:0000250"
FT REGION 251..616
FT /note="Required for self-association and induction of
FT membrane tubulation"
FT /evidence="ECO:0000250"
FT REGION 280..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..551
FT /note="Interaction with RND2"
FT REGION 494..616
FT /note="Interaction with PDE6G"
FT REGION 494..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..616
FT /note="Required for interaction with TNKS"
FT /evidence="ECO:0000250"
FT REGION 534..616
FT /note="Interaction with DNM1 and DNM3"
FT /evidence="ECO:0000250"
FT REGION 549..616
FT /note="Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2"
FT /evidence="ECO:0000250"
FT REGION 552..609
FT /note="Interaction with FASLG"
FT /evidence="ECO:0000250"
FT REGION 552..608
FT /note="Interaction with DNM2 and WASL"
FT /evidence="ECO:0000250"
FT COILED 67..259
FT /evidence="ECO:0000250"
FT COILED 398..490
FT /evidence="ECO:0000250"
FT COMPBIAS 291..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 166
FT /note="Mediates end-to-end attachment of dimers"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96RU3"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96RU3"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RU3"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RU3"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TY0"
FT MOD_RES 499
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80TY0"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 329..394
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14732713"
FT /id="VSP_021704"
FT VAR_SEQ 329..389
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14732713"
FT /id="VSP_021705"
FT VAR_SEQ 329..357
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14732713"
FT /id="VSP_021706"
FT VAR_SEQ 390..394
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14732713"
FT /id="VSP_021707"
FT VAR_SEQ 616
FT /note="S -> AKTYI (in isoform 2, isoform 3, isoform 4,
FT isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:12244061,
FT ECO:0000303|PubMed:14732713"
FT /id="VSP_021708"
FT MUTAGEN 587
FT /note="W->A: Abrogates interaction with PDE6G."
FT /evidence="ECO:0000269|PubMed:14502124"
FT MUTAGEN 601
FT /note="P->L: Abrogates interaction with PDE6G."
FT /evidence="ECO:0000269|PubMed:14502124"
SQ SEQUENCE 616 AA; 71293 MW; 3F62F30C7AEC674E CRC64;
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK
EEEEYKYTAC KAFLSTLNEL NDYAGQHEVI SENMTSQITV DLVRYVQELK QERKSNFHDG
RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQMRQ
QMAEDSKADY SLILQRFNQE QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ
VIPIIGKCLD GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL
SSSKEGKPEL KFGGKSRGKL WPFIKKNKLM TLLTSPHQPP PPPPASASPS AVPNGPQSPK
QQKEPLSHRF NEFMTSKPKI HCFRSLKRGL SLKLGVTPED FSNFPPEQRR KKLQQKVDDL
NKEIQKETDQ RDAITKMKDV YLKNPQMGDP ASLDHKLAEV TQNIEKLRLE AHKFEAWLAE
VEGRLPARSE QARRQSGLYD GQTHQTVTNC AQDRESPDGS YTEEQSQESE HKVLATDFDD
EFDDEEPLPA IGTCKALYTF EGQNEGTISV VEGETLSVIE EDKGDGWTRI RRNEDEEGYV
PTSYVEVYLD KNAKGS
