AMPH_RAT
ID AMPH_RAT Reviewed; 683 AA.
AC O08838;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Amphiphysin;
GN Name=Amph; Synonyms=Amph1;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
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 PROTEIN SEQUENCE OF 198-207; 242-256 AND 615-633, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP INTERACTION WITH BIN1; 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 [4]
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 [5]
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 [6]
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 [7]
RP INTERACTION WITH AP2B1.
RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
RA Mills I.G., Benmerah A., McMahon H.T.;
RT "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-
RT coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
CC -!- FUNCTION: May participate in mechanisms of regulated exocytosis in
CC synapses and certain endocrine cell types. May control the properties
CC of the membrane associated cytoskeleton (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with BIN1 (PubMed:9341169). Binds SH3GLB1 (By
CC similarity). Interacts with REPS1 and SGIP1 (By similarity). Binds
CC AP2A2 (PubMed:10380931, PubMed:10430869). Interacts with AP2B1
CC (PubMed:16516836, PubMed:16903783). Interacts with DNM1 AND SYNJ1
CC (PubMed:9341169). {ECO:0000250|UniProtKB:P49418,
CC ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:10430869,
CC ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:16903783,
CC ECO:0000269|PubMed:9341169}.
CC -!- INTERACTION:
CC O08838; O08839: Bin1; NbExp=2; IntAct=EBI-80080, EBI-80095;
CC O08838; P21575: Dnm1; NbExp=3; IntAct=EBI-80080, EBI-80070;
CC O08838; P39052: Dnm2; NbExp=2; IntAct=EBI-80080, EBI-349613;
CC O08838; Q9CR95: Necap1; Xeno; NbExp=8; IntAct=EBI-80080, EBI-7592476;
CC O08838; O43295: SRGAP3; Xeno; NbExp=3; IntAct=EBI-80080, EBI-368166;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y13381; CAA73808.1; -; mRNA.
DR RefSeq; NP_071553.1; NM_022217.1.
DR PDB; 2VJ0; X-ray; 1.60 A; Q=324-330.
DR PDB; 5M5T; X-ray; 1.70 A; E/F/G/H/I/J=349-356.
DR PDBsum; 2VJ0; -.
DR PDBsum; 5M5T; -.
DR AlphaFoldDB; O08838; -.
DR SMR; O08838; -.
DR BioGRID; 248889; 22.
DR CORUM; O08838; -.
DR DIP; DIP-30977N; -.
DR ELM; O08838; -.
DR IntAct; O08838; 9.
DR MINT; O08838; -.
DR STRING; 10116.ENSRNOP00000017102; -.
DR iPTMnet; O08838; -.
DR PhosphoSitePlus; O08838; -.
DR jPOST; O08838; -.
DR PaxDb; O08838; -.
DR PRIDE; O08838; -.
DR GeneID; 60668; -.
DR KEGG; rno:60668; -.
DR UCSC; RGD:620274; rat.
DR CTD; 273; -.
DR RGD; 620274; Amph.
DR eggNOG; KOG3771; Eukaryota.
DR InParanoid; O08838; -.
DR OrthoDB; 1366218at2759; -.
DR PhylomeDB; O08838; -.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; O08838; -.
DR PRO; PR:O08838; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0031256; C:leading edge membrane; ISO:RGD.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0098833; C:presynaptic endocytic zone; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
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:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
DR CDD; cd12140; SH3_Amphiphysin_I; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR003005; Amphiphysin.
DR InterPro; IPR003017; Amphiphysin_1.
DR InterPro; IPR035470; Amphiphysin_I_SH3.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR46514:SF2; PTHR46514:SF2; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR01251; AMPHIPHYSIN.
DR PRINTS; PR01252; AMPHIPHYSIN1.
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; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome;
KW SH3 domain; Synapse.
FT CHAIN 1..683
FT /note="Amphiphysin"
FT /id="PRO_0000192949"
FT DOMAIN 24..240
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 610..683
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 244..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 10..83
FT /evidence="ECO:0000255"
FT COILED 144..191
FT /evidence="ECO:0000255"
FT COMPBIAS 287..309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 280
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
SQ SEQUENCE 683 AA; 74878 MW; 7FEA4A9E5A1F6631 CRC64;
MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL
RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT
LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF
EEFNVDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD
KAFSIQGAPS DSGPLRIAKT PSPPEEASPL PSPTASPNHT LAPASPAPVR PRSPSQTRKG
PPVPPLPKVT PTKELQQENI INFFEDNFVP EINVTTPSQN EVLEVKKEET LLDLDFDPFK
PDVTPAGSAA ATHSPMSQTL PWDLWTTSTD LVQPASGGSF NDFTQPQDTS LFTMQTDQNM
AETEQALPTE PQAEEPPTTA AAPTAGLDLG LEMEEPKEEA AIPPGTDAGE TVGTEGSTGE
EAEAEKAALP AGEGESPEGA KIDVESTELA SSESPQAAEL EAGAPQEKVI PSVVIEPASN
HEGEEHQETT TGTETREATE DVAPQGPAGE KQELATEPTP LDSQAATPAP AGAVDASLSA
GDAAQELPPG FLYKVETLHD FEAANSDELT LQRGDVVLVV PSDSEADQDA GWLVGVKESD
WLQYRDLATY KGLFPENFTR HLE
