AP18B_YEAST
ID AP18B_YEAST Reviewed; 568 AA.
AC P53309; D6VV22;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Clathrin coat assembly protein AP180B;
GN Name=YAP1802; OrderedLocusNames=YGR241C; ORFNames=G8610;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9090057;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<275::aid-yea73>3.0.co;2-g;
RA Guerreiro P., Azevedo D., Barreiros T., Rodrigues-Pousada C.;
RT "Sequencing of a 9.9 kb segment on the right arm of yeast chromosome VII
RT reveals four open reading frames, including PFK1, the gene coding for
RT succinyl-CoA synthetase (beta-chain) and two ORFs sharing homology with
RT ORFs of the yeast chromosome VIII.";
RL Yeast 13:275-280(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND INTERACTION WITH CHC1; CLC1 AND PAN1.
RX PubMed=9531549; DOI=10.1083/jcb.141.1.71;
RA Wendland B., Emr S.D.;
RT "Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates
RT protein-protein interactions essential for endocytosis.";
RL J. Cell Biol. 141:71-84(1998).
RN [5]
RP FUNCTION.
RX PubMed=14704157; DOI=10.1093/genetics/165.4.1661;
RA Baggett J.J., D'Aquino K.E., Wendland B.;
RT "The Sla2p talin domain plays a role in endocytosis in Saccharomyces
RT cerevisiae.";
RL Genetics 165:1661-1674(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-449, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-282, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Involved in endocytosis and clathrin cage assembly.
CC {ECO:0000269|PubMed:14704157, ECO:0000269|PubMed:9531549}.
CC -!- SUBUNIT: Interacts with PAN1 and the clathrin heavy and light chains
CC CHC1 and CLC1. {ECO:0000269|PubMed:9531549}.
CC -!- SUBCELLULAR LOCATION: Bud {ECO:0000269|PubMed:14562095}. Bud neck
CC {ECO:0000269|PubMed:14562095}. Cell membrane
CC {ECO:0000269|PubMed:14562095}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095}; Cytoplasmic side
CC {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 6800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AP180 family. {ECO:0000305}.
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DR EMBL; Z73026; CAA97270.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08333.1; -; Genomic_DNA.
DR PIR; S64567; S64567.
DR RefSeq; NP_011757.3; NM_001181370.3.
DR AlphaFoldDB; P53309; -.
DR SMR; P53309; -.
DR BioGRID; 33493; 86.
DR DIP; DIP-2751N; -.
DR ELM; P53309; -.
DR IntAct; P53309; 19.
DR MINT; P53309; -.
DR STRING; 4932.YGR241C; -.
DR iPTMnet; P53309; -.
DR MaxQB; P53309; -.
DR PaxDb; P53309; -.
DR PRIDE; P53309; -.
DR EnsemblFungi; YGR241C_mRNA; YGR241C; YGR241C.
DR GeneID; 853157; -.
DR KEGG; sce:YGR241C; -.
DR SGD; S000003473; YAP1802.
DR VEuPathDB; FungiDB:YGR241C; -.
DR eggNOG; KOG0251; Eukaryota.
DR GeneTree; ENSGT00950000183068; -.
DR HOGENOM; CLU_025901_0_0_1; -.
DR InParanoid; P53309; -.
DR OMA; RDSAWTI; -.
DR BioCyc; YEAST:G3O-30918-MON; -.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR PRO; PR:P53309; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53309; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; TAS:SGD.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IPI:SGD.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
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; IPR045192; AP180-like.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR PANTHER; PTHR22951; PTHR22951; 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 Cell membrane; Cytoplasm; Endocytosis; Isopeptide bond; Membrane;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..568
FT /note="Clathrin coat assembly protein AP180B"
FT /id="PRO_0000202856"
FT DOMAIN 1..127
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 262..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 449
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 568 AA; 64328 MW; C5B5FD733739C3CD CRC64;
MSSLYTKLVK GATKIKMAPP KQKYVDPILS GTSSARGLQE ITHALDIRLS DTAWTIVYKA
LIVLHLMIQQ GEKDVTLRHY SHNLDVFQLR KISHTTKWSS NDMRALQRYD EYLKTRCEEY
GRLGMDHLRD NYSSLKLGSK NQLSMDEELD HVESLEIQIN ALIRNKYSVS DLENHLLLYA
FQLLVQDLLG LYNALNEGVI TLLESFFELS IEHAKRTLDL YKDFVDMTEY VVRYLKIGKA
VGLKIPVIKH ITTKLINSLE EHLREETKRQ RGEPSEPQQD RKPSTAISST SSHNNNSNDK
NKSIAQKKLE QIREQKRLLE QQLQNQQLLI SPTVPQDAYN PFGSQQQDLN NDTFSFEPTQ
PQMTAQVPQP TANPFLIPQQ QQQALQLTSA STMPQPSEIQ ITPNLNNQQT GMYASNLQYT
PNFTGSGFGG YTTTENNAIM TGTLDPTKTG SNNPFSLENI AREQQQQNFQ NSPNPFTLQQ
AQTTPILAHS QTGNPFQAQN VVTSPMGTYM TNPVAGQLQY ASTGAQQQPQ MMQGQQTGYV
MVPTAFVPIN QQQQQQQHQQ ENPNLIDI
