AP3B_YEAST
ID AP3B_YEAST Reviewed; 809 AA.
AC P46682; D6VV40;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=AP-3 complex subunit beta;
DE AltName: Full=Adaptor-related protein complex 3 subunit beta;
DE AltName: Full=Beta-3-adaptin;
DE AltName: Full=Clathrin assembly protein complex 3 beta large chain;
DE AltName: Full=Clathrin assembly protein large beta chain;
GN Name=APL6; Synonyms=YKS5; OrderedLocusNames=YGR261C; ORFNames=G9331;
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].
RA Robinson L.C., Engle H.M., Panek H.R.;
RT "Suppressors of loss of yeast casein kinase 1 function define the four
RT subunits of a novel putative adaptin complex.";
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9090059;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<287::aid-yea75>3.0.co;2-5;
RA Clemente M.L., Sartori G., Cardazzo B., Carignani G.;
RT "Analysis of an 11.6 kb region from the right arm of chromosome VII of
RT Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals the
RT presence of three new genes.";
RL Yeast 13:287-290(1997).
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION OF THE AP-3 COMPLEX, AND FUNCTION OF THE AP-3 COMPLEX.
RX PubMed=9335339; DOI=10.1016/s0092-8674(01)80013-1;
RA Cowles C.R., Odorizzi G., Payne G.S., Emr S.D.;
RT "The AP-3 adaptor complex is essential for cargo-selective transport to the
RT yeast vacuole.";
RL Cell 91:109-118(1997).
RN [6]
RP IDENTIFICATION OF THE AP-3 COMPLEX, AND FUNCTION OF THE AP-3 COMPLEX.
RX PubMed=9250663; DOI=10.1093/emboj/16.14.4194;
RA Panek H.R., Stepp J.D., Engle H.M., Marks K.M., Tan P.K., Lemmon S.K.,
RA Robinson L.C.;
RT "Suppressors of YCK-encoded yeast casein kinase 1 deficiency define the
RT four subunits of a novel clathrin AP-like complex.";
RL EMBO J. 16:4194-4204(1997).
RN [7]
RP SUBCELLULAR LOCATION, AND FUNCTION OF THE AP-3 COMPLEX.
RX PubMed=10559961; DOI=10.1038/14037;
RA Rehling P., Darsow T., Katzmann D.J., Emr S.D.;
RT "Formation of AP-3 transport intermediates requires Vps41 function.";
RL Nat. Cell Biol. 1:346-353(1999).
RN [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-726, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-693; SER-698; SER-724 AND
RP SER-726, AND IDENTIFICATION BY 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 [13]
RP PYROPHOSPHORYLATION.
RX PubMed=17873058; DOI=10.1073/pnas.0707338104;
RA Bhandari R., Saiardi A., Ahmadibeni Y., Snowman A.M., Resnick A.C.,
RA Kristiansen T.Z., Molina H., Pandey A., Werner J.K. Jr., Juluri K.R.,
RA Xu Y., Prestwich G.D., Parang K., Snyder S.H.;
RT "Protein pyrophosphorylation by inositol pyrophosphates is a
RT posttranslational event.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15305-15310(2007).
CC -!- FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is
CC not clathrin-associated. The complex is associated with the Golgi
CC region as well as more peripheral structures. It facilitates the
CC budding of vesicles from the Golgi membrane and may be directly
CC involved in trafficking to the vacuole. Required for the transport via
CC the ALP pathway, which directs the transport of the cargo proteins PHO8
CC and VAM3 to the vacuole. {ECO:0000269|PubMed:10559961,
CC ECO:0000269|PubMed:9250663, ECO:0000269|PubMed:9335339}.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC of 2 large adaptins (APL5 and APL6), a medium adaptin (APM3) and a
CC small adaptin (APS3).
CC -!- INTERACTION:
CC P46682; Q08951: APL5; NbExp=5; IntAct=EBI-2213, EBI-29702;
CC P46682; P38153: APM3; NbExp=5; IntAct=EBI-2213, EBI-2710;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:10559961,
CC ECO:0000269|PubMed:14562095}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000269|PubMed:10559961}; Peripheral membrane
CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Component
CC of the coat surrounding the cytoplasmic face of coated vesicles located
CC at the Golgi complex. {ECO:0000269|PubMed:10559961}.
CC -!- PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) (PubMed:17873058). Serine pyrophosphorylation is achieved by
CC Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate
CC from a inositol pyrophosphate to a pre-phosphorylated serine residue
CC (PubMed:17873058). {ECO:0000269|PubMed:17873058}.
CC -!- MISCELLANEOUS: Present with 3570 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; U35411; AAC13877.1; -; Genomic_DNA.
DR EMBL; Y07777; CAA69083.1; -; Genomic_DNA.
DR EMBL; Z73046; CAA97290.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08351.1; -; Genomic_DNA.
DR PIR; S64594; S64594.
DR RefSeq; NP_011777.3; NM_001181390.3.
DR PDB; 7P3X; EM; 9.10 A; B=1-809.
DR PDB; 7P3Y; EM; 10.10 A; B=1-809.
DR PDB; 7P3Z; EM; 10.50 A; B=1-809.
DR PDBsum; 7P3X; -.
DR PDBsum; 7P3Y; -.
DR PDBsum; 7P3Z; -.
DR AlphaFoldDB; P46682; -.
DR SMR; P46682; -.
DR BioGRID; 33512; 245.
DR ComplexPortal; CPX-535; Adapter complex AP-3.
DR DIP; DIP-2684N; -.
DR IntAct; P46682; 16.
DR MINT; P46682; -.
DR STRING; 4932.YGR261C; -.
DR iPTMnet; P46682; -.
DR MaxQB; P46682; -.
DR PaxDb; P46682; -.
DR PRIDE; P46682; -.
DR EnsemblFungi; YGR261C_mRNA; YGR261C; YGR261C.
DR GeneID; 853177; -.
DR KEGG; sce:YGR261C; -.
DR SGD; S000003493; APL6.
DR VEuPathDB; FungiDB:YGR261C; -.
DR eggNOG; KOG1060; Eukaryota.
DR GeneTree; ENSGT00940000169094; -.
DR HOGENOM; CLU_006320_3_2_1; -.
DR InParanoid; P46682; -.
DR OMA; IGRCAQS; -.
DR BioCyc; YEAST:G3O-30930-MON; -.
DR PRO; PR:P46682; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P46682; protein.
DR GO; GO:0030123; C:AP-3 adaptor complex; IMP:SGD.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR026740; AP3_beta.
DR InterPro; IPR026739; AP_beta.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR PANTHER; PTHR11134:SF1; PTHR11134:SF1; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..809
FT /note="AP-3 complex subunit beta"
FT /id="PRO_0000193757"
FT REPEAT 37..76
FT /note="HEAT 1"
FT REPEAT 112..151
FT /note="HEAT 2"
FT REPEAT 153..186
FT /note="HEAT 3"
FT REPEAT 187..224
FT /note="HEAT 4"
FT REPEAT 524..561
FT /note="HEAT 5"
FT REGION 708..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..790
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 27..35
FT /note="TSKLGESSY -> PLSWVNPP (in Ref. 1; AAC13877)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="S -> T (in Ref. 1; AAC13877)"
FT /evidence="ECO:0000305"
FT CONFLICT 798..802
FT /note="Missing (in Ref. 1; AAC13877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 809 AA; 91607 MW; 475DA3A4F6E68E97 CRC64;
MVDSIHRIAS ALDTAKVITR EAAAVATSKL GESSYTYYSQ NINPQQLVTL LNSRNSREVR
DAMKRIISIM ASDDDSIDVQ LYFADVVKNI TTNDTKVKRL IHLYLLRFAE NDPNLTLLSI
NSLQKSLSDS NSELRCFALS ALSDMKMSSL APIILHTVKK LVTDPSAMVR GEVALAIIKL
YRAGKNDYHE ELLDILKELM ADTDPKVISC AVLAYKECYA DHLELLHGHF RRYCRIIKQL
DSWSQSYLIE LLIKYCKQYL PKPTVVDKSS EGSPRSCPLP DKYNEIEYPS YEVVNDPDLD
LFLQSLNCLI YSSNPTVILS CCNALYQLAS PLQMKNTKFI EALVRTVTMT ENQGNKEMLL
QAIHFLSILD QTLFLPYTKK FYVFPKDPIV ASIWKIQILS TLINESNVKE IFKELKYYVA
SAHFPENVVI MAVKSLSRCG QLSTSWESHV MKWLIDHMES HNLSASVLDA YVNVIRMLVQ
KNPTKHLRII FKLADLLTVQ TSLADNARAG IVWLFGEIAS IEFKICPDVL RRLIQNFSNE
GPETRCQILV LSAKLLSYDI DNFKQAQVTG SEENNQNPPY YDFSGSRISQ MYNAVLYLAK
YDDEFDIRDR ARMISSLFDS GKYEIVSLLL QAPKPTARSD DFIVSARLET HTPEIKEFFR
MLPWNTEITE VGETGNDIRE GAELKDYNKY KKSFSSQSFI TNNSARSFTS SSNAKLTGIN
DGDSNSISGK GNVNTFTSQN GKKYRLQSLD EFFSDIPERK SKPRKIIKVV EESSDEDEDE
SEESSDDDEY SDSSLGTSSS GTSSSHLEL
