AP180_RAT
ID AP180_RAT Reviewed; 915 AA.
AC Q05140;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Clathrin coat assembly protein AP180;
DE AltName: Full=91 kDa synaptosomal-associated protein;
DE AltName: Full=Clathrin coat-associated protein AP180;
GN Name=Snap91;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=8440257; DOI=10.1002/j.1460-2075.1993.tb05700.x;
RA Morris S.A., Schroeder S., Plessmann U., Weber K., Ungewickell E.;
RT "Clathrin assembly protein AP180: primary structure, domain organization
RT and identification of a clathrin binding site.";
RL EMBO J. 12:667-675(1993).
RN [2]
RP PROTEIN SEQUENCE OF 25-39 AND 247-252 (ISOFORMS 1/2), AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PROTEIN SEQUENCE OF 305-320 (ISOFORMS 1/2), PROTEIN SEQUENCE OF 598-649
RP (ISOFORM 2), GLYCOSYLATION AT THR-310, PHOSPHORYLATION AT SER-306; SER-313;
RP SER-600; SER-640 AND SER-646, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21500857; DOI=10.1021/pr1011153;
RA Graham M.E., Thaysen-Andersen M., Bache N., Craft G.E., Larsen M.R.,
RA Packer N.H., Robinson P.J.;
RT "A novel post-translational modification in nerve terminals: O-linked N-
RT acetylglucosamine phosphorylation.";
RL J. Proteome Res. 10:2725-2733(2011).
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=10944104; DOI=10.1093/emboj/19.16.4216;
RA Owen D.J., Vallis Y., Pearse B.M.F., McMahon H.T., Evans P.R.;
RT "The structure and function of the beta 2-adaptin appendage domain.";
RL EMBO J. 19:4216-4227(2000).
RN [7]
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 [8]
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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-300; SER-313;
RP SER-594 AND SER-775, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 AND
RP SER-627 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Adaptins are components of the adapter 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. {ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:10430869,
CC ECO:0000269|PubMed:10944104, ECO:0000269|PubMed:16516836,
CC ECO:0000269|PubMed:16903783}.
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=2;
CC Name=1;
CC IsoId=Q05140-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05140-2; Sequence=VSP_000173;
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. The form with phosphorylated O-
CC linked N-acetylglucosamine is predominant in brain synaptosomes. There
CC is no evidence for direct Thr-310 phosphorylation (PubMed:21500857).
CC {ECO:0000269|PubMed:21500857}.
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family. {ECO:0000305}.
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DR EMBL; X68877; CAA48748.1; -; mRNA.
DR EMBL; X68878; CAA48749.1; -; mRNA.
DR PIR; S36326; S36326.
DR PIR; S36327; S36327.
DR RefSeq; NP_113916.1; NM_031728.1. [Q05140-1]
DR AlphaFoldDB; Q05140; -.
DR BMRB; Q05140; -.
DR SMR; Q05140; -.
DR BioGRID; 249290; 10.
DR CORUM; Q05140; -.
DR ELM; Q05140; -.
DR IntAct; Q05140; 6.
DR MINT; Q05140; -.
DR STRING; 10116.ENSRNOP00000030821; -.
DR GlyGen; Q05140; 1 site.
DR iPTMnet; Q05140; -.
DR PhosphoSitePlus; Q05140; -.
DR SwissPalm; Q05140; -.
DR jPOST; Q05140; -.
DR PaxDb; Q05140; -.
DR PRIDE; Q05140; -.
DR GeneID; 65178; -.
DR KEGG; rno:65178; -.
DR UCSC; RGD:69276; rat. [Q05140-1]
DR CTD; 9892; -.
DR RGD; 69276; Snap91.
DR eggNOG; KOG0251; Eukaryota.
DR InParanoid; Q05140; -.
DR OrthoDB; 1592722at2759; -.
DR PhylomeDB; Q05140; -.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q05140; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; ISO:RGD.
DR GO; GO:0098894; C:extrinsic component of presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:RGD.
DR GO; GO:0098833; C:presynaptic endocytic zone; ISO:RGD.
DR GO; GO:0098830; C:presynaptic endosome; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; IDA:BHF-UCL.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISO:RGD.
DR GO; GO:0035615; F:clathrin adaptor activity; IMP:CAFA.
DR GO; GO:0032050; F:clathrin heavy chain binding; IPI:CAFA.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:RGD.
DR GO; GO:0043274; F:phospholipase binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0042169; F:SH2 domain binding; IPI:RGD.
DR GO; GO:0000149; F:SNARE binding; IPI:RGD.
DR GO; GO:0007409; P:axonogenesis; IMP:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0048268; P:clathrin coat assembly; ISO:RGD.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:BHF-UCL.
DR GO; GO:0051899; P:membrane depolarization; IEP:RGD.
DR GO; GO:1900275; P:negative regulation of phospholipase C activity; IDA:RGD.
DR GO; GO:1904006; P:negative regulation of phospholipase D activity; IDA:RGD.
DR GO; GO:0048666; P:neuron development; IMP:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:RGD.
DR GO; GO:1905445; P:positive regulation of clathrin coat assembly; IMP:CAFA.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IMP:RGD.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; ISO:RGD.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:BHF-UCL.
DR GO; GO:0051223; P:regulation of protein transport; IMP:BHF-UCL.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:2000331; P:regulation of terminal button organization; IMP:RGD.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR DisProt; DP00225; -.
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; Direct protein sequencing;
KW Glycoprotein; Membrane; Methylation; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..915
FT /note="Clathrin coat assembly protein AP180"
FT /id="PRO_0000193866"
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 391..425
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 720..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..915
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 COMPBIAS 720..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21500857"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21500857,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61548"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21500857"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21500857"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21500857"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 873
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q61548"
FT MOD_RES 873
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q61548"
FT CARBOHYD 310
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:21500857"
FT VAR_SEQ 614..632
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8440257"
FT /id="VSP_000173"
FT MOD_RES Q05140-2:600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q05140-2:627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 915 AA; 93519 MW; 32EC1B38EC5DF8C0 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 LKVADEVGID KGDIPDLTQA PSSLMETLEQ HLNTLEGKKP GNNEGSGAPS
PLSKSSPATT VTSPNSTPAK TIDTSPPVDI FATASAAAPV SSAKPSSDLL DLQPDFSGAR
AGAAAPVPPP TGGATAWGDL LGEDSLAALS SVPSEAPISD PFAPEPSPPT TTTEPASASA
SATTAVTAAT TEVDLFGDAF AASPGEAPAA SEGATAPATP APVAAALDAC SGNDPFAPSE
GSAEAAPELD LFAMKPPETS APVVTPTAST APPVPATAPS PAPTAVAATA ATTTAAAAAT
TTATTSAAAA TTAAAPPALD IFGDLFDSAP EVAAASKPDV APSIDLFGTD AFSSPPRGAS
PVPESSLTAD LLSGSGFHCA EDDRHVPLFF TAVDAFAAPS PASTASPAKA ESSGVIDLFG
DAFGSSASET QPAPQAVSSS SASADLLAGF GGSFMAPSTT PVTPAQNNLL QPNFEAAFGT
TPSTSSSSSF DPSGDLLMPT MAPSGQPAPV SMVPPSPAMS ASKGLGSDLD SSLASLVGNL
GISGTTSKKG DLQWNAGEKK LTGGANWQPK VTPATWSAGV PPQGTVPPTS SVPPGAGAPS
VGQPGAGYGM PPAGTGMTMM PQQPVMFAQP MMRPPFGAAA VPGTQLSPSP TPATQSPKKP
PAKDPLADLN IKDFL
