ID   AP1S1_YEAST             Reviewed;         156 AA.
AC   P35181; D6VYH5;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 183.
DE   RecName: Full=AP-1 complex subunit sigma-1;
DE   AltName: Full=Clathrin assembly protein complex 1 sigma-1 small chain;
DE   AltName: Full=Clathrin coat assembly protein AP19;
DE   AltName: Full=Clathrin coat-associated protein AP19;
DE   AltName: Full=Golgi adaptor AP-1 19 kDa adaptin;
DE   AltName: Full=HA1 19 kDa subunit;
DE   AltName: Full=Sigma1-adaptin;
GN   Name=APS1; Synonyms=YAP19; OrderedLocusNames=YLR170C;
GN   ORFNames=L9470.16;
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=SP1;
RX   PubMed=8373805; DOI=10.1016/0167-4781(93)90198-m;
RA   Nakai M., Takada T., Endo T.;
RT   "Cloning of the YAP19 gene encoding a putative yeast homolog of AP19, the
RT   mammalian small chain of the clathrin-assembly proteins.";
RL   Biochim. Biophys. Acta 1174:282-284(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GPY 297;
RX   PubMed=8157009; DOI=10.1002/j.1460-2075.1994.tb06435.x;
RA   Phan H.L., Finlay J.A., Chu D.S., Tan P.K., Kirchhausen T., Payne G.S.;
RT   "The Saccharomyces cerevisiae APS1 gene encodes a homolog of the small
RT   subunit of the mammalian clathrin AP-1 complex: evidence for functional
RT   interaction with clathrin at the Golgi complex.";
RL   EMBO J. 13:1706-1717(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871; DOI=10.1038/387s087;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH CLATHRIN.
RX   PubMed=10564262; DOI=10.1091/mbc.10.11.3643;
RA   Yeung B.G., Phan H.L., Payne G.S.;
RT   "Adaptor complex-independent clathrin function in yeast.";
RL   Mol. Biol. Cell 10:3643-3659(1999).
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   FUNCTION, AND SUBUNIT.
RX   PubMed=26658609; DOI=10.1091/mbc.e15-09-0621;
RA   Whitfield S.T., Burston H.E., Bean B.D., Raghuram N., Maldonado-Baez L.,
RA   Davey M., Wendland B., Conibear E.;
RT   "The alternate AP-1 adaptor subunit Apm2 interacts with the Mil1 regulatory
RT   protein and confers differential cargo sorting.";
RL   Mol. Biol. Cell 27:588-598(2016).
CC   -!- FUNCTION: Component of the adapter complexes which link clathrin to
CC       receptors in coated vesicles (PubMed:10564262). Clathrin-associated
CC       protein complexes are believed to interact with the cytoplasmic tails
CC       of membrane proteins, leading to their selection and concentration
CC       (PubMed:10564262). AP19 is probably a subunit of the Golgi membrane
CC       adapter (PubMed:10564262). Component of the AP-1-related (AP-1R)
CC       complex, an adapter protein complex that mediates sorting of cargo
CC       SNARE SNC1 (PubMed:26658609). In contrast to the APM1-containing AP-1
CC       complex, AP-1R is incapable of sorting CHS3 (PubMed:26658609).
CC       {ECO:0000269|PubMed:10564262, ECO:0000269|PubMed:26658609}.
CC   -!- SUBUNIT: Adapter protein complex 1 (AP-1) is a heterotetramer composed
CC       of two large adaptins (gamma-type subunit APL4 and beta-type subunit
CC       APL2), a medium adaptin (mu-type subunit APM1) and a small adaptin
CC       (sigma-type subunit APS1) (PubMed:10564262). AP-1 interacts with
CC       clathrin (PubMed:10564262). Also a component of the AP-1R complex
CC       composed of at least APM2, APL4 and APS1 (PubMed:26658609).
CC       {ECO:0000269|PubMed:10564262, ECO:0000269|PubMed:26658609}.
CC   -!- INTERACTION:
CC       P35181; P36000: APL2; NbExp=6; IntAct=EBI-2612, EBI-2206;
CC       P35181; Q12028: APL4; NbExp=5; IntAct=EBI-2612, EBI-33025;
CC       P35181; Q00776: APM1; NbExp=5; IntAct=EBI-2612, EBI-2624;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9P7N2}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9P7N2}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle membrane {ECO:0000250|UniProtKB:Q9P7N2}. Endosome
CC       {ECO:0000250|UniProtKB:Q9P7N2}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q9P7N2}.
CC   -!- MISCELLANEOUS: Present with 6370 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; X70279; CAA49765.1; -; Genomic_DNA.
DR   EMBL; Z30314; CAA82959.2; -; Genomic_DNA.
DR   EMBL; U17246; AAB67468.1; -; Genomic_DNA.
DR   EMBL; AY692851; AAT92870.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09491.1; -; Genomic_DNA.
DR   PIR; S37757; S37757.
DR   RefSeq; NP_013271.1; NM_001182057.1.
DR   AlphaFoldDB; P35181; -.
DR   SMR; P35181; -.
DR   BioGRID; 31442; 179.
DR   ComplexPortal; CPX-532; Adaptor complex AP-1.
DR   ComplexPortal; CPX-533; Adaptor complex AP-1R.
DR   DIP; DIP-4806N; -.
DR   FunCoup; P35181; 505.
DR   IntAct; P35181; 9.
DR   MINT; P35181; -.
DR   STRING; 4932.YLR170C; -.
DR   iPTMnet; P35181; -.
DR   PaxDb; 4932-YLR170C; -.
DR   PeptideAtlas; P35181; -.
DR   EnsemblFungi; YLR170C_mRNA; YLR170C; YLR170C.
DR   GeneID; 850868; -.
DR   KEGG; sce:YLR170C; -.
DR   AGR; SGD:S000004160; -.
DR   SGD; S000004160; APS1.
DR   VEuPathDB; FungiDB:YLR170C; -.
DR   eggNOG; KOG0934; Eukaryota.
DR   HOGENOM; CLU_061221_0_0_1; -.
DR   InParanoid; P35181; -.
DR   OMA; KAYHILD; -.
DR   OrthoDB; 371463at2759; -.
DR   BioCyc; YEAST:G3O-32299-MONOMER; -.
DR   Reactome; R-SCE-432720; Lysosome Vesicle Biogenesis.
DR   BioGRID-ORCS; 850868; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P35181; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P35181; protein.
DR   GO; GO:0030121; C:AP-1 adaptor complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035615; F:clathrin-cargo adaptor activity; IEA:InterPro.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; IMP:ComplexPortal.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd14831; AP1_sigma; 1.
DR   FunFam; 3.30.450.60:FF:000007; AP complex subunit sigma; 1.
DR   Gene3D; 3.30.450.60; -; 1.
DR   InterPro; IPR044733; AP1_sigma.
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   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   Cytoplasm; Cytoplasmic vesicle; Endosome; Golgi apparatus; Membrane;
KW   Nucleus; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..156
FT                   /note="AP-1 complex subunit sigma-1"
FT                   /id="PRO_0000193803"
SQ   SEQUENCE   156 AA;  18152 MW;  1A584883F1DF815D CRC64;
     MTQLKYLLLV SRQGKIRLKK WYTAMSAGEK AKIVKDLTPT ILARKPKMCN IIEYNDHKVV
     YKRYASLYFI VGMTPDVDNE LLTLEIIHRF VETMDTYFGN VCELDIIFNF SKVYDILNEM
     IMCDGSIAES SRKEVLHHVT VMDTMESNDN LERVLS
//