ID   AP1S1_SCHPO             Reviewed;         162 AA.
AC   Q9P7N2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-SEP-2026, entry version 124.
DE   RecName: Full=AP-1 complex subunit sigma-1;
DE   AltName: Full=Sigma1-adaptin;
DE   AltName: Full=Valproic acid-sensitive protein 2;
GN   Name=vas2; Synonyms=aps1; ORFNames=SPAP27G11.06c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   DISRUPTION PHENOTYPE, IDENTIFICATION IN THE AP-1 COMPLEX, SUBCELLULAR
RP   LOCATION, AND FUNCTION.
RX   PubMed=19624755; DOI=10.1111/j.1365-2443.2009.01327.x;
RA   Ma Y., Takeuchi M., Sugiura R., Sio S.O., Kuno T.;
RT   "Deletion mutants of AP-1 adaptin subunits display distinct phenotypes in
RT   fission yeast.";
RL   Genes Cells 14:1015-1028(2009).
CC   -!- FUNCTION: Component of the AP-1 complex which links clathrin to
CC       receptors in coated vesicles. Clathrin-associated protein complexes are
CC       believed to interact with the cytoplasmic tails of membrane proteins,
CC       leading to their selection and concentration.
CC       {ECO:0000269|PubMed:19624755}.
CC   -!- SUBUNIT: Adaptor 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). AP-1 interacts with clathrin (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle membrane {ECO:0000269|PubMed:19624755, ECO:0000305}. Endosome
CC       {ECO:0000269|PubMed:19624755}. Golgi apparatus
CC       {ECO:0000269|PubMed:19624755}.
CC   -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to valproic acid.
CC       {ECO:0000269|PubMed:19624755}.
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; CU329670; CAB76027.1; -; Genomic_DNA.
DR   RefSeq; NP_593410.1; NM_001018843.3.
DR   AlphaFoldDB; Q9P7N2; -.
DR   SMR; Q9P7N2; -.
DR   BioGRID; 279330; 3.
DR   ComplexPortal; CPX-26625; Adaptor complex AP-1.
DR   FunCoup; Q9P7N2; 442.
DR   STRING; 284812.Q9P7N2; -.
DR   PaxDb; 284812-Q9P7N2; -.
DR   GeneID; 2542885; -.
DR   KEGG; spo:2542885; -.
DR   PomBase; SPAP27G11.06c; vas2.
DR   VEuPathDB; FungiDB:SPAP27G11.06c; -.
DR   eggNOG; KOG0934; Eukaryota.
DR   HOGENOM; CLU_061221_1_3_1; -.
DR   InParanoid; Q9P7N2; -.
DR   OMA; KAYHILD; -.
DR   PhylomeDB; Q9P7N2; -.
DR   Reactome; R-SPO-432720; Lysosome Vesicle Biogenesis.
DR   PRO; PR:Q9P7N2; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0030121; C:AP-1 adaptor complex; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005768; C:endosome; IDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0030276; F:clathrin binding; ISO:PomBase.
DR   GO; GO:0035615; F:clathrin-cargo adaptor activity; IEA:InterPro.
DR   GO; GO:0099638; P:endosome to plasma membrane protein transport; IDA:PomBase.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:PomBase.
DR   GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; NAS: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; 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.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoplasmic vesicle; Endosome; Golgi apparatus; Membrane;
KW   Nucleus; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..162
FT                   /note="AP-1 complex subunit sigma-1"
FT                   /id="PRO_0000316201"
SQ   SEQUENCE   162 AA;  18647 MW;  9616603E7EF51C7D CRC64;
     MSIKFFLLVS RQGKVRLAKW FNTLSIKERA KIIRDVSSLV ITRKPKMCNF VEYKGEKIVY
     RRYASLFFVC GIEQDDNELI ILEVIHKFVE CLDKYFGNVC ELDLIFNFEK AYYVMEELLL
     AGELQESSKT NVLSAVLAGD AESEADAQQD SLQKLVGSVK KR
//