BIN1_RAT
ID BIN1_RAT Reviewed; 588 AA.
AC O08839;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Myc box-dependent-interacting protein 1;
DE AltName: Full=Amphiphysin II;
DE AltName: Full=Amphiphysin-like protein;
DE AltName: Full=Bridging integrator 1;
GN Name=Bin1; Synonyms=Amph2, Amphl;
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], SUBUNIT, AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex, and Kidney;
RX PubMed=9348539; DOI=10.1091/mbc.8.10.2003;
RA Wigge P., Koehler K., Vallis Y., Doyle C., Owen D., Hunt S.P.,
RA McMahon H.T.;
RT "Amphiphysin heterodimers: potential role in clathrin-mediated
RT endocytosis.";
RL Mol. Biol. Cell 8:2003-2015(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AMPH2-1).
RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
RX PubMed=9280305; DOI=10.1016/s0014-5793(97)00928-9;
RA McMahon H.T., Wigge P., Smith C.;
RT "Clathrin interacts specifically with amphiphysin and is displaced by
RT dynamin.";
RL FEBS Lett. 413:319-322(1997).
RN [3]
RP PROTEIN SEQUENCE OF 155-164; 190-202; 510-537 AND 577-586, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH AMPH; DNM1 AND SYNJ1.
RX PubMed=9341169; DOI=10.1074/jbc.272.43.27239;
RA Micheva K.D., Kay B.K., McPherson P.S.;
RT "Synaptojanin forms two separate complexes in the nerve terminal.
RT Interactions with endophilin and amphiphysin.";
RL J. Biol. Chem. 272:27239-27245(1997).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain, and Skeletal muscle;
RX PubMed=9182667; DOI=10.1083/jcb.137.6.1355;
RA Butler M.H., David C., Ochoa G.-C., Freyberg Z., Daniell L., Grabs D.,
RA Cremona O., De Camilli P.;
RT "Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs family, is
RT concentrated in the cortical cytomatrix of axon initial segments and nodes
RT of Ranvier in brain and around T tubules in skeletal muscle.";
RL J. Cell Biol. 137:1355-1367(1997).
RN [6]
RP INTERACTION WITH AP2A2.
RX PubMed=10380931; DOI=10.1016/s0092-8674(00)80791-6;
RA Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R., Evans P.R.,
RA McMahon H.T.;
RT "A structural explanation for the binding of multiple ligands by the alpha-
RT adaptin appendage domain.";
RL Cell 97:805-815(1999).
RN [7]
RP INTERACTION WITH AP2A2.
RX PubMed=10430869; DOI=10.1073/pnas.96.16.8907;
RA Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.;
RT "Crystal structure of the alpha appendage of AP-2 reveals a recruitment
RT platform for clathrin-coat assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999).
RN [8]
RP INTERACTION WITH AP2B1.
RX PubMed=16516836; DOI=10.1016/j.devcel.2006.01.016;
RA Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M.,
RA Roth R., Heuser J.E., Owen D.J., Traub L.M.;
RT "Molecular switches involving the AP-2 beta2 appendage regulate endocytic
RT cargo selection and clathrin coat assembly.";
RL Dev. Cell 10:329-342(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-304; THR-308 AND
RP SER-324, AND 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).
RN [10]
RP FUNCTION.
RX PubMed=27760323; DOI=10.1016/j.celrep.2016.09.063;
RA Calafate S., Flavin W., Verstreken P., Moechars D.;
RT "Loss of Bin1 promotes the propagation of Tau pathology.";
RL Cell Rep. 17:931-940(2016).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 506-588, FUNCTION, AND INTERACTION
RP WITH DNM1.
RX PubMed=9736607; DOI=10.1093/emboj/17.18.5273;
RA Owen D.J., Wigge P., Vallis Y., Moore J.D.A., Evans P.R., McMahon H.T.;
RT "Crystal structure of the amphiphysin-2 SH3 domain and its role in the
RT prevention of dynamin ring formation.";
RL EMBO J. 17:5273-5285(1998).
CC -!- FUNCTION: Is a key player in the control of plasma membrane curvature,
CC and membrane shaping and remodeling. Required in muscle cells for the
CC formation of T-tubules, tubular invaginations of the plasma membrane
CC that function in depolarization-contraction coupling. Required in
CC muscle cells for the formation of T-tubules, tubular invaginations of
CC the plasma membrane that function in depolarization-contraction
CC coupling (By similarity). Is a negative regulator of endocytosis
CC (PubMed:9736607, PubMed:27760323). Is also involved in the regulation
CC of intracellular vesicles sorting, modulation of BACE1 trafficking and
CC the control of amyloid-beta production (By similarity). In neuronal
CC circuits, endocytosis regulation may influence the internalization of
CC PHF-tau aggregates (PubMed:27760323). May be involved in the regulation
CC of MYC activity and the control cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:O00499, ECO:0000250|UniProtKB:O08539,
CC ECO:0000269|PubMed:27760323, ECO:0000269|PubMed:9736607}.
CC -!- SUBUNIT: Heterodimer with AMPH (PubMed:9348539, PubMed:9341169). Binds
CC SH3GLB1 (By similarity). Interacts (via SH3 domain) with DNM1
CC (PubMed:9736607, PubMed:9341169). Interacts with SYNJ1
CC (PubMed:9341169). Interacts (via SH3 domain) with DNM2 (By similarity).
CC Interacts with CLTC (By similarity). Interacts with AP2A2
CC (PubMed:10430869, PubMed:10380931). Interacts with AP2B1
CC (PubMed:16516836). Interacts with MYC (via N-terminal transactivation
CC domain); the interaction requires the integrity of the conserved MYC
CC box regions 1 and 2 (By similarity). Interacts with BIN2 (By
CC similarity). Interacts with SNX4 (By similarity). Interacts (via BAR
CC domain) with BACE1 (By similarity). Binds (via BAR domain) F-actin (By
CC similarity). {ECO:0000250|UniProtKB:O00499,
CC ECO:0000250|UniProtKB:O08539, ECO:0000269|PubMed:10380931,
CC ECO:0000269|PubMed:10430869, ECO:0000269|PubMed:16516836,
CC ECO:0000269|PubMed:9341169, ECO:0000269|PubMed:9348539,
CC ECO:0000269|PubMed:9736607}.
CC -!- INTERACTION:
CC O08839; O08838: Amph; NbExp=2; IntAct=EBI-80095, EBI-80080;
CC O08839; P21575: Dnm1; NbExp=2; IntAct=EBI-80095, EBI-80070;
CC O08839; Q9CR95: Necap1; Xeno; NbExp=9; IntAct=EBI-80095, EBI-7592476;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O08539}. Cytoplasm
CC {ECO:0000250|UniProtKB:O08539}. Endosome
CC {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T-tubule
CC {ECO:0000269|PubMed:9182667}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=AMPH2-1;
CC IsoId=O08839-1; Sequence=Displayed;
CC Name=AMPH2-2;
CC IsoId=O08839-2; Sequence=VSP_000260;
CC Name=AMPH2-3;
CC IsoId=O08839-3; Sequence=VSP_000258;
CC Name=AMPH2-4;
CC IsoId=O08839-4; Sequence=VSP_000256, VSP_000257;
CC Name=AMPH2-5;
CC IsoId=O08839-5; Sequence=VSP_000259;
CC Name=AMPH2-6;
CC IsoId=O08839-6; Sequence=VSP_000256, VSP_000259;
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and muscle. Isoform
CC AMPH2-1 is expressed only in the brain where it is concentrated in axon
CC initial segments and nodes of Ranvier. Isoform AMPH2-2 is widely
CC expressed. {ECO:0000269|PubMed:9182667}.
CC -!- PTM: Phosphorylated by protein kinase C.
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DR EMBL; Y13380; CAA73807.1; -; mRNA.
DR RefSeq; NP_446411.1; NM_053959.1. [O08839-1]
DR PDB; 1BB9; X-ray; 2.20 A; A=495-588.
DR PDBsum; 1BB9; -.
DR AlphaFoldDB; O08839; -.
DR BMRB; O08839; -.
DR SMR; O08839; -.
DR BioGRID; 250629; 16.
DR CORUM; O08839; -.
DR DIP; DIP-30979N; -.
DR ELM; O08839; -.
DR IntAct; O08839; 12.
DR MINT; O08839; -.
DR STRING; 10116.ENSRNOP00000017573; -.
DR iPTMnet; O08839; -.
DR PhosphoSitePlus; O08839; -.
DR SwissPalm; O08839; -.
DR jPOST; O08839; -.
DR PaxDb; O08839; -.
DR PRIDE; O08839; -.
DR Ensembl; ENSRNOT00000017573; ENSRNOP00000017573; ENSRNOG00000012852. [O08839-1]
DR GeneID; 117028; -.
DR KEGG; rno:117028; -.
DR UCSC; RGD:621786; rat. [O08839-1]
DR CTD; 274; -.
DR RGD; 621786; Bin1.
DR eggNOG; KOG3771; Eukaryota.
DR GeneTree; ENSGT00950000182882; -.
DR InParanoid; O08839; -.
DR OrthoDB; 1366218at2759; -.
DR PhylomeDB; O08839; -.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; O08839; -.
DR PRO; PR:O08839; -.
DR Proteomes; UP000002494; Chromosome 18.
DR GO; GO:0030424; C:axon; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0043194; C:axon initial segment; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0044300; C:cerebellar mossy fiber; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0031674; C:I band; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0060987; C:lipid tube; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005874; C:microtubule; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0033268; C:node of Ranvier; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0043196; C:varicosity; IDA:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0030018; C:Z disc; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0051020; F:GTPase binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:RGD.
DR GO; GO:0048156; F:tau protein binding; ISO:RGD.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:RGD.
DR GO; GO:0060988; P:lipid tube assembly; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0042692; P:muscle cell differentiation; ISO:RGD.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:RGD.
DR GO; GO:1902960; P:negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISO:RGD.
DR GO; GO:1904878; P:negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:RGD.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1903946; P:negative regulation of ventricular cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0051647; P:nucleus localization; ISO:RGD.
DR GO; GO:0006997; P:nucleus organization; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:RGD.
DR GO; GO:0010564; P:regulation of cell cycle process; ISO:RGD.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0033292; P:T-tubule organization; ISO:RGD.
DR CDD; cd12139; SH3_Bin1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR003005; Amphiphysin.
DR InterPro; IPR035471; Amphiphysin-2_SH3.
DR InterPro; IPR003023; Amphiphysin_2.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR46514:SF4; PTHR46514:SF4; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR01251; AMPHIPHYSIN.
DR PRINTS; PR01253; AMPHIPHYSIN2.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Coiled coil; Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Endocytosis; Endosome; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00499"
FT CHAIN 2..588
FT /note="Myc box-dependent-interacting protein 1"
FT /id="PRO_0000192953"
FT DOMAIN 29..276
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 515..588
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 2..122
FT /note="Interaction with BIN2"
FT /evidence="ECO:0000250"
FT REGION 279..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..422
FT /note="Clathrin-binding"
FT /evidence="ECO:0000250"
FT REGION 448..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..42
FT /evidence="ECO:0000255"
FT COILED 193..274
FT /evidence="ECO:0000255"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O00499"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00499"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00499"
FT VAR_SEQ 173..205
FT /note="Missing (in isoform AMPH2-4 and isoform AMPH2-6)"
FT /evidence="ECO:0000305"
FT /id="VSP_000256"
FT VAR_SEQ 253..588
FT /note="Missing (in isoform AMPH2-4)"
FT /evidence="ECO:0000305"
FT /id="VSP_000257"
FT VAR_SEQ 335..588
FT /note="Missing (in isoform AMPH2-3)"
FT /evidence="ECO:0000305"
FT /id="VSP_000258"
FT VAR_SEQ 335..482
FT /note="Missing (in isoform AMPH2-5 and isoform AMPH2-6)"
FT /evidence="ECO:0000305"
FT /id="VSP_000259"
FT VAR_SEQ 423..460
FT /note="Missing (in isoform AMPH2-2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000260"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:1BB9"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:1BB9"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:1BB9"
FT STRAND 557..562
FT /evidence="ECO:0007829|PDB:1BB9"
FT HELIX 563..567
FT /evidence="ECO:0007829|PDB:1BB9"
FT HELIX 572..575
FT /evidence="ECO:0007829|PDB:1BB9"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:1BB9"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:1BB9"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:1BB9"
SQ SEQUENCE 588 AA; 64533 MW; 164AC90E09547F1A CRC64;
MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR
LQKDLRTYLA SVKAMHEASK KLSECLQEVY EPEWPGRDEA NKIAENNDLL WMDYHQKLVD
QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK
AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN
TFQSIAGLEE NFHKEMSKLN QNLNDVLVSL EKQHGSNTFT VKAQPSDSAP EKGNKSPSPP
PDGSPAATPE IRVNHEPEPA SGASPGATIP KSPSQLRKGP PVPPPPKHTP SKEMKQEQIL
SLFDDAFVPE ISVTTPSQFE APGPFSEQAS LLDLDFEPLP PVASPVKAPT PSGQSIPWDL
WEPTESQAGV LPSGEPSSAE GSFAVAWPSQ TAEPGPAQPA EASEVVGGTQ EPGETAASEA
TSSSLPAVVV ETFSATVNGA VEGSTTTGRL DLPPGFMFKV QAQHDYTATD TDELQLKAGD
VVLVIPFQNP EEQDEGWLMG VKESDWNQHK ELEKCRGVFP ENFTERVQ
