ID   AP2S_SCHPO              Reviewed;         143 AA.
AC   Q9Y7L6;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=AP-2 complex subunit sigma;
DE   AltName: Full=Adaptin small chain;
DE   AltName: Full=Clathrin assembly protein 2 sigma small chain;
DE   AltName: Full=Sigma2-adaptin;
GN   Name=aps2; ORFNames=SPBC685.04c;
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).
CC   -!- FUNCTION: Component of the adaptor complexes which link 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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC       of two large adaptins (alpha-type subunit apl3 and beta-type subunit
CC       apl1), a medium chain (mu-type subunit apm4) and a small adaptin
CC       (sigma-type subunit aps2). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=Component of the coat surrounding the
CC       cytoplasmic face of the plasma membrane coated vesicles. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAB39361.1; -; Genomic_DNA.
DR   PIR; T40635; T40635.
DR   RefSeq; NP_596138.1; NM_001022056.2.
DR   AlphaFoldDB; Q9Y7L6; -.
DR   SMR; Q9Y7L6; -.
DR   BioGRID; 277601; 11.
DR   STRING; 4896.SPBC685.04c.1; -.
DR   MaxQB; Q9Y7L6; -.
DR   PaxDb; Q9Y7L6; -.
DR   PRIDE; Q9Y7L6; -.
DR   EnsemblFungi; SPBC685.04c.1; SPBC685.04c.1:pep; SPBC685.04c.
DR   GeneID; 2541086; -.
DR   KEGG; spo:SPBC685.04c; -.
DR   PomBase; SPBC685.04c; aps2.
DR   VEuPathDB; FungiDB:SPBC685.04c; -.
DR   eggNOG; KOG0935; Eukaryota.
DR   HOGENOM; CLU_061221_3_1_1; -.
DR   InParanoid; Q9Y7L6; -.
DR   OMA; IYLSHIH; -.
DR   PhylomeDB; Q9Y7L6; -.
DR   Reactome; R-SPO-437239; Recycling pathway of L1.
DR   Reactome; R-SPO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-SPO-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-SPO-8964038; LDL clearance.
DR   PRO; PR:Q9Y7L6; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030122; C:AP-2 adaptor complex; ISO:PomBase.
DR   GO; GO:0005938; C:cell cortex; IC:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IC:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd14833; AP2_sigma; 1.
DR   InterPro; IPR016635; AP_complex_ssu.
DR   InterPro; IPR022775; AP_mu_sigma_su.
DR   InterPro; IPR027156; APS2.
DR   InterPro; IPR000804; Clathrin_sm-chain_CS.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   PANTHER; PTHR11753; PTHR11753; 1.
DR   PANTHER; PTHR11753:SF6; PTHR11753:SF6; 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   3: Inferred from homology;
KW   Cell membrane; Coated pit; Endocytosis; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..143
FT                   /note="AP-2 complex subunit sigma"
FT                   /id="PRO_0000193813"
SQ   SEQUENCE   143 AA;  16939 MW;  87E1A6945A741121 CRC64;
     MIQFILIQNR HGKNRLSKYY VPFDDDEKVR LKARIHQLIS QRNQKFQANF LEWENSKLVY
     RRYAGLYFCF CVDSTDNDLA ILEMIHFFVE ILDSFFGNVC ELDLIFNFYK VSAILDEIIL
     GGEIGESNKK SVLERIEALE KLE