AP180_MOUSE
ID AP180_MOUSE Reviewed; 901 AA.
AC Q61548; Q61547; Q8K0D4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Clathrin coat assembly protein AP180;
DE AltName: Full=91 kDa synaptosomal-associated protein;
DE AltName: Full=Clathrin coat-associated protein AP180;
DE AltName: Full=Phosphoprotein F1-20;
GN Name=Snap91;
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 [MRNA] (ISOFORMS LONG AND SHORT).
RX PubMed=1607933; DOI=10.1523/jneurosci.12-06-02144.1992;
RA Zhou S., Sousa R., Tannery N.H., Lafer E.M.;
RT "Characterization of a novel synapse-specific protein. II. cDNA cloning and
RT sequence analysis of the F1-20 protein.";
RL J. Neurosci. 12:2144-2155(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=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 [3]
RP IDENTIFICATION BY 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313 AND THR-317, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Heart;
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).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-859, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Adaptins are components of the adaptor complexes which link
CC clathrin to receptors in coated vesicles. Clathrin-associated protein
CC complexes are believed to interact with the cytoplasmic tails of
CC membrane proteins, leading to their selection and concentration.
CC Binding of AP180 to clathrin triskelia induces their assembly into 60-
CC 70 nm coats.
CC -!- SUBUNIT: Binds AP2A2. Interacts with AP2B1; clathrin competes with
CC SNAP91 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit; Peripheral
CC membrane protein; Cytoplasmic side. Note=Component of the coat
CC surrounding the cytoplasmic face of coated vesicles in the plasma
CC membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Long;
CC IsoId=Q61548-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q61548-2; Sequence=VSP_000172;
CC Name=3;
CC IsoId=Q61548-3; Sequence=VSP_000172, VSP_022635;
CC -!- TISSUE SPECIFICITY: Brain. Associated with the synapses.
CC -!- DEVELOPMENTAL STAGE: Developmentally regulated in a pattern coincident
CC with active synaptogenesis and synaptic maturation.
CC -!- DOMAIN: Possesses a three domain structure: the N-terminal 300 residues
CC harbor a clathrin binding site, an acidic middle domain 450 residues,
CC interrupted by an Ala-rich segment, and the C-terminal domain (166
CC residues).
CC -!- PTM: Thr-310 can be modified by the addition of N-acetylglucosamine
CC which can be further phosphorylated. There is no evidence for direct
CC Thr-310 phosphorylation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family. {ECO:0000305}.
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DR EMBL; M83985; AAA37587.1; -; mRNA.
DR EMBL; M83985; AAA37586.1; -; mRNA.
DR EMBL; BC031773; AAH31773.1; -; mRNA.
DR PIR; A44825; A44825.
DR RefSeq; NP_001264911.1; NM_001277982.1. [Q61548-3]
DR RefSeq; NP_001264915.1; NM_001277986.1. [Q61548-2]
DR RefSeq; NP_038697.1; NM_013669.2. [Q61548-1]
DR RefSeq; XP_006510957.1; XM_006510894.3.
DR RefSeq; XP_006510963.1; XM_006510900.2. [Q61548-3]
DR AlphaFoldDB; Q61548; -.
DR BMRB; Q61548; -.
DR SMR; Q61548; -.
DR BioGRID; 203364; 22.
DR ELM; Q61548; -.
DR IntAct; Q61548; 6.
DR MINT; Q61548; -.
DR STRING; 10090.ENSMUSP00000096096; -.
DR GlyGen; Q61548; 1 site.
DR iPTMnet; Q61548; -.
DR PhosphoSitePlus; Q61548; -.
DR SwissPalm; Q61548; -.
DR CPTAC; non-CPTAC-3444; -.
DR jPOST; Q61548; -.
DR MaxQB; Q61548; -.
DR PaxDb; Q61548; -.
DR PeptideAtlas; Q61548; -.
DR PRIDE; Q61548; -.
DR ProteomicsDB; 296050; -. [Q61548-1]
DR ProteomicsDB; 296051; -. [Q61548-2]
DR ProteomicsDB; 296052; -. [Q61548-3]
DR DNASU; 20616; -.
DR GeneID; 20616; -.
DR KEGG; mmu:20616; -.
DR UCSC; uc029xff.2; mouse. [Q61548-3]
DR UCSC; uc033jlv.1; mouse. [Q61548-2]
DR UCSC; uc033jlw.1; mouse. [Q61548-1]
DR CTD; 9892; -.
DR MGI; MGI:109132; Snap91.
DR eggNOG; KOG0251; Eukaryota.
DR InParanoid; Q61548; -.
DR OrthoDB; 1592722at2759; -.
DR PhylomeDB; Q61548; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 20616; 3 hits in 68 CRISPR screens.
DR ChiTaRS; Snap91; mouse.
DR PRO; PR:Q61548; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61548; protein.
DR GO; GO:0030122; C:AP-2 adaptor complex; IC:BHF-UCL.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; IDA:SynGO.
DR GO; GO:0098894; C:extrinsic component of presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0098833; C:presynaptic endocytic zone; IDA:SynGO.
DR GO; GO:0098830; C:presynaptic endosome; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:BHF-UCL.
DR GO; GO:0035615; F:clathrin adaptor activity; ISO:MGI.
DR GO; GO:0032050; F:clathrin heavy chain binding; IPI:BHF-UCL.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:BHF-UCL.
DR GO; GO:0048268; P:clathrin coat assembly; IDA:BHF-UCL.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISO:MGI.
DR GO; GO:1900275; P:negative regulation of phospholipase C activity; ISO:MGI.
DR GO; GO:1904006; P:negative regulation of phospholipase D activity; ISO:MGI.
DR GO; GO:0048666; P:neuron development; ISO:MGI.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:BHF-UCL.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:MGI.
DR GO; GO:1905445; P:positive regulation of clathrin coat assembly; ISO:MGI.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; ISO:MGI.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; ISO:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:MGI.
DR GO; GO:0051223; P:regulation of protein transport; ISO:MGI.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:2000331; P:regulation of terminal button organization; ISO:MGI.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IMP:SynGO.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR DisProt; DP01073; -.
DR Gene3D; 1.20.58.150; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; ANTH_dom_sf.
DR InterPro; IPR030428; AP180.
DR InterPro; IPR045192; AP180-like.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR PANTHER; PTHR22951; PTHR22951; 1.
DR PANTHER; PTHR22951:SF4; PTHR22951:SF4; 1.
DR Pfam; PF07651; ANTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coated pit; Glycoprotein; Membrane;
KW Methylation; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..901
FT /note="Clathrin coat assembly protein AP180"
FT /id="PRO_0000193865"
FT DOMAIN 14..145
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 285..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 859
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 859
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CARBOHYD 310
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 715..719
FT /note="Missing (in isoform Short and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1607933"
FT /id="VSP_000172"
FT VAR_SEQ 809..836
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022635"
SQ SEQUENCE 901 AA; 91851 MW; 24A98FBACE8DB8B1 CRC64;
MSGQTLTDRI AAAQYSVTGS AVARAVCKAT THEVMGPKKK HLDYLIQATN ETNVNIPQMA
DTLFERATNS SWVVVFKALV TTHHLMVHGN ERFIQYLASR NTLFNLSNFL DKSGSHGYDM
STFIRRYSRY LNEKAFSYRQ MAFDFARVKK GADGVMRTMV PEKLLKSMPI LQGQIDALLE
FDVHPNELTN GVINAAFMLL FKDLIKLFAC YNDGVINLLE KFFEMKKGQC KDALEIYKRF
LTRMTRVSEF LKVAEQVGID KGDIPDLTQA PSSLMETLEQ HLNTLEGKKP GNNEGSGAPS
PLSKSSPATT VTSPNSTPAK TIDTSPPVDI FATASAAAPV SSAKPSSDLL DLQPDFSGAA
AGAAAPVVPP SGGATAWGDL LGEDSLAALS SVPCEAPISD PFAPEPSPPT TTTEPASASA
STTTAVTAVT TEVDLFGDAF AASPGEAPAA SEGATAPATP APVAAALDAC SGNDPFAPSE
GSAEAAPELD LFAMKPPETS APVVTPTAST APPVPATAPS PAPTAVAATA ATTTAAAAAT
TTATTSAAAA TTAAAPPALD IFGDLFDSAP EVAAAPKPDA APSIDLFGTD AFSSPPRGAS
PVPESSLTAD LLSVDAFAAP SPASTASPAK AESSGVIDLF GDAFGSGASE TQPAPQAVSS
SSASADLLAG FGGSFMAPST TPVTPAQNNL LQPSFEAAFG TTPSTSSSSS FDPSVFDGLG
DLLMPTMAPS GQPAPVSMVP PSPAMAASKG LGSDLDSSLA SLVGNLGISG TTSKKGDLQW
NAGEKKLTGG ANWQPKVTPA TWSAGVPPQG TVPPTSSVPP GAGAPSVGQP GAGFGMPPSG
TGMTMMSQQP VMFAQPMMRP PFGAAAVPGT QLSPSPTPAT QSPKKPPAKD PLADLNIKDF
L
