ID   AP3S_YEAST              Reviewed;         194 AA.
AC   P47064; D6VWF8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=AP-3 complex subunit sigma;
DE   AltName: Full=AP-3 complex sigma3A subunit;
DE   AltName: Full=Adaptor-related protein complex 3 subunit sigma;
DE   AltName: Full=Clathrin-associated/assembly/adaptor protein, small 3;
DE   AltName: Full=Sigma-adaptin 3A;
DE   AltName: Full=Sigma3-adaptin;
GN   Name=APS3; Synonyms=YKS7; OrderedLocusNames=YJL024C; ORFNames=J1274;
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], IDENTIFICATION IN THE AP-3 COMPLEX, AND
RP   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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   IDENTIFICATION IN 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   [5]
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   [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).
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). {ECO:0000269|PubMed:9250663,
CC       ECO:0000269|PubMed:9335339}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:14562095}.
CC       Cytoplasmic vesicle membrane {ECO:0000269|PubMed:10559961}; Peripheral
CC       membrane protein {ECO:0000305|PubMed:10559961}; Cytoplasmic side
CC       {ECO:0000305|PubMed:10559961}. Note=Component of the coat surrounding
CC       the cytoplasmic face of coated vesicles located at the Golgi complex.
CC       {ECO:0000269|PubMed:10559961, ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 1240 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC       {ECO:0000305}.
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DR   EMBL; U31448; AAA92051.1; -; Genomic_DNA.
DR   EMBL; Z49299; CAA89315.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08774.1; -; Genomic_DNA.
DR   PIR; S56796; S56796.
DR   RefSeq; NP_012510.3; NM_001181458.3.
DR   PDB; 7P3X; EM; 9.10 A; S=1-194.
DR   PDB; 7P3Y; EM; 10.10 A; S=1-194.
DR   PDB; 7P3Z; EM; 10.50 A; S=1-194.
DR   PDBsum; 7P3X; -.
DR   PDBsum; 7P3Y; -.
DR   PDBsum; 7P3Z; -.
DR   AlphaFoldDB; P47064; -.
DR   EMDB; EMD-13187; -.
DR   EMDB; EMD-13188; -.
DR   EMDB; EMD-13189; -.
DR   SMR; P47064; -.
DR   BioGRID; 33735; 154.
DR   ComplexPortal; CPX-535; Adapter complex AP-3.
DR   DIP; DIP-3978N; -.
DR   IntAct; P47064; 4.
DR   MINT; P47064; -.
DR   STRING; 4932.YJL024C; -.
DR   iPTMnet; P47064; -.
DR   MaxQB; P47064; -.
DR   PaxDb; 4932-YJL024C; -.
DR   PeptideAtlas; P47064; -.
DR   EnsemblFungi; YJL024C_mRNA; YJL024C; YJL024C.
DR   GeneID; 853429; -.
DR   KEGG; sce:YJL024C; -.
DR   AGR; SGD:S000003561; -.
DR   SGD; S000003561; APS3.
DR   VEuPathDB; FungiDB:YJL024C; -.
DR   eggNOG; KOG0936; Eukaryota.
DR   GeneTree; ENSGT00970000193421; -.
DR   HOGENOM; CLU_061221_2_2_1; -.
DR   InParanoid; P47064; -.
DR   OMA; DLIFNWQ; -.
DR   OrthoDB; 3059064at2759; -.
DR   BioCyc; YEAST:G3O-31494-MONOMER; -.
DR   BioGRID-ORCS; 853429; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P47064; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47064; Protein.
DR   GO; GO:0030123; C:AP-3 adaptor complex; IMP:SGD.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; NAS: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; 3.30.450.60; -; 1.
DR   InterPro; IPR016635; AP_complex_ssu.
DR   InterPro; IPR022775; AP_mu_sigma_su.
DR   InterPro; IPR000804; Clathrin_sm-chain_CS.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   PANTHER; PTHR11753; ADAPTOR COMPLEXES SMALL SUBUNIT FAMILY; 1.
DR   PANTHER; PTHR11753:SF2; ADAPTOR PROTEIN COMPLEX AP-3 SMALL CHAIN SIGMA3; 1.
DR   Pfam; PF01217; Clat_adaptor_s; 1.
DR   PIRSF; PIRSF015588; AP_complex_sigma; 1.
DR   SUPFAM; SSF64356; SNARE-like; 1.
DR   PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..194
FT                   /note="AP-3 complex subunit sigma"
FT                   /id="PRO_0000193822"
SQ   SEQUENCE   194 AA;  21938 MW;  688D81AEA77B7555 CRC64;
     MIHAVLIFNK KCQPRLVKFY TPVDLPKQKL LLEQVYELIS QRNSDFQSSF LVTPPSLLLS
     NENNNDEVNN EDIQIIYKNY ATLYFTFIVD DQESELAILD LIQTFVESLD RCFTEVNELD
     LIFNWQTLES VLEEIVQGGM VIETNVNRIV ASVDELNKAA ESTDSKIGRL TSTGFGSALQ
     AFAQGGFAQW ATGQ
//