AP1S1_YEAST
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 03-AUG-2022, entry version 169.
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; 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;
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=5; IntAct=EBI-2612, EBI-2206;
CC P35181; Q12028: APL4; NbExp=4; IntAct=EBI-2612, EBI-33025;
CC P35181; Q00776: APM1; NbExp=4; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 173.
DR ComplexPortal; CPX-532; Adaptor complex AP-1.
DR ComplexPortal; CPX-533; Adaptor complex AP-1R.
DR DIP; DIP-4806N; -.
DR IntAct; P35181; 9.
DR MINT; P35181; -.
DR STRING; 4932.YLR170C; -.
DR iPTMnet; P35181; -.
DR MaxQB; P35181; -.
DR PaxDb; P35181; -.
DR PRIDE; P35181; -.
DR EnsemblFungi; YLR170C_mRNA; YLR170C; YLR170C.
DR GeneID; 850868; -.
DR KEGG; sce:YLR170C; -.
DR SGD; S000004160; APS1.
DR VEuPathDB; FungiDB:YLR170C; -.
DR eggNOG; KOG0934; Eukaryota.
DR GeneTree; ENSGT00970000193372; -.
DR HOGENOM; CLU_061221_0_0_1; -.
DR InParanoid; P35181; -.
DR OMA; KAYHILD; -.
DR BioCyc; YEAST:G3O-32299-MON; -.
DR Reactome; R-SCE-432720; Lysosome Vesicle Biogenesis.
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:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035615; F:clathrin 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 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; PTHR11753; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF015588; AP_complex_sigma; 1.
DR SUPFAM; SSF64356; SSF64356; 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