AMPH_MOUSE
ID AMPH_MOUSE Reviewed; 686 AA.
AC Q7TQF7; Q8R1C4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Amphiphysin;
GN Name=Amph; Synonyms=Amph1;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; THR-260; SER-262;
RP SER-268; SER-272; SER-276; THR-280; SER-500 AND SER-629, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Lung;
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).
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 (By similarity). Binds SH3GLB1 (By
CC similarity). Interacts with REPS1 and SGIP1 (By similarity). Binds
CC AP2A2. Interacts with AP2B1. Interacts with DNM1 AND SYNJ1 (By
CC similarity). {ECO:0000250|UniProtKB:O08838}.
CC -!- INTERACTION:
CC Q7TQF7; P39053: Dnm1; NbExp=3; IntAct=EBI-775139, EBI-397785;
CC Q7TQF7; P39054: Dnm2; NbExp=5; IntAct=EBI-775139, EBI-642337;
CC Q7TQF7; Q8BZ98: Dnm3; NbExp=2; IntAct=EBI-775139, EBI-6880033;
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}.
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DR EMBL; BC024817; AAH24817.1; -; mRNA.
DR EMBL; BC054718; AAH54718.1; -; mRNA.
DR CCDS; CCDS26258.1; -.
DR RefSeq; NP_001276475.1; NM_001289546.1.
DR RefSeq; NP_778172.1; NM_175007.2.
DR AlphaFoldDB; Q7TQF7; -.
DR SMR; Q7TQF7; -.
DR BioGRID; 229989; 28.
DR IntAct; Q7TQF7; 8.
DR MINT; Q7TQF7; -.
DR STRING; 10090.ENSMUSP00000003345; -.
DR iPTMnet; Q7TQF7; -.
DR PhosphoSitePlus; Q7TQF7; -.
DR MaxQB; Q7TQF7; -.
DR PaxDb; Q7TQF7; -.
DR PeptideAtlas; Q7TQF7; -.
DR PRIDE; Q7TQF7; -.
DR ProteomicsDB; 296031; -.
DR Antibodypedia; 3258; 494 antibodies from 41 providers.
DR DNASU; 218038; -.
DR Ensembl; ENSMUST00000003345; ENSMUSP00000003345; ENSMUSG00000021314.
DR GeneID; 218038; -.
DR KEGG; mmu:218038; -.
DR UCSC; uc007pom.2; mouse.
DR CTD; 273; -.
DR MGI; MGI:103574; Amph.
DR VEuPathDB; HostDB:ENSMUSG00000021314; -.
DR eggNOG; KOG3771; Eukaryota.
DR GeneTree; ENSGT00950000182882; -.
DR HOGENOM; CLU_017859_4_0_1; -.
DR InParanoid; Q7TQF7; -.
DR OMA; QADQSMI; -.
DR OrthoDB; 1366218at2759; -.
DR PhylomeDB; Q7TQF7; -.
DR TreeFam; TF313542; -.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 218038; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Amph; mouse.
DR PRO; PR:Q7TQF7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q7TQF7; protein.
DR Bgee; ENSMUSG00000021314; Expressed in saccule of membranous labyrinth and 171 other tissues.
DR ExpressionAtlas; Q7TQF7; baseline and differential.
DR Genevisible; Q7TQF7; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0031256; C:leading edge membrane; ISO:MGI.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0098833; C:presynaptic endocytic zone; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
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 Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain; Synapse.
FT CHAIN 1..686
FT /note="Amphiphysin"
FT /id="PRO_0000192948"
FT DOMAIN 24..240
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 613..686
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 244..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..597
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 260..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 686 AA; 75013 MW; D292E24653A442A5 CRC64;
MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL
RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT
LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF
EEFNVDLQEE LPSLWSSRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD
KAFSIQGAPS DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPVR PRSPSQTRKG
PPVPPLPKVT PTKELKQENI INFFEDNFVP EINVTTPSQN EVLEVKKEET LLDLDFDPFK
PDVAPAGSAA ATHSPMSQTL PWDLWTTSTD LVQPASGGSF NDFTQAQDTS LFTMQTDQNM
AETEQALPTE PQAEEPPATA AAPTAGLDLG LEMEEPKEEA VIPPATDTGE TVETAVPTEG
APVEEAEAEK AALPAGEGGS PEGAKIDGES TELAISESPQ PVEPEAGAPQ VIPSVVIEPA
SNHEGEGEHQ ETATGTEPRE AAEDVAAQGS AGEKQEVATE PTPLDSQATL PASAGAVDAS
LSAGDATQEL PPGFLYKVET LHDFEAANSD ELNLQRGDVV LVVPSDSEAD QDAGWLVGVK
ESDWLQYRDL ATYKGLFPEN FTRRLE
