ID   AP2S1_PONAB             Reviewed;         142 AA.
AC   Q5R940;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=AP-2 complex subunit sigma;
DE   AltName: Full=Adaptor protein complex AP-2 subunit sigma;
DE   AltName: Full=Adaptor-related protein complex 2 subunit sigma;
DE   AltName: Full=Clathrin assembly protein 2 sigma small chain;
DE   AltName: Full=Clathrin coat assembly protein AP17;
DE   AltName: Full=Clathrin coat-associated protein AP17;
DE   AltName: Full=Plasma membrane adaptor AP-2 17 kDa protein;
DE   AltName: Full=Sigma-adaptin 3b;
DE   AltName: Full=Sigma2-adaptin;
GN   Name=AP2S1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor
CC       protein complexes function in protein Transport via Transport vesicles
CC       in different membrane traffic pathways. Adaptor protein complexes are
CC       vesicle coat components and appear to be involved in cargo selection
CC       and vesicle formation. AP-2 is involved in clathrin-dependent
CC       endocytosis in which cargo proteins are incorporated into vesicles
CC       surrounded by clathrin (clathrin-coated vesicles, CCVs) which are
CC       destined for fusion with the early endosome. The clathrin lattice
CC       serves as a mechanical scaffold but is itself unable to bind directly
CC       to membrane components. Clathrin-associated adaptor protein (AP)
CC       complexes which can bind directly to both the clathrin lattice and to
CC       the lipid and protein components of membranes are considered to be the
CC       major clathrin adaptors contributing the CCV formation. AP-2 also
CC       serves as a cargo receptor to selectively sort the membrane proteins
CC       involved in receptor-mediated endocytosis. AP-2 seems to play a role in
CC       the recycling of synaptic vesicle membranes from the presynaptic
CC       surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-
CC       [LI] endocytosis signal motifs within the cytosolic tails of
CC       transmembrane cargo molecules. AP-2 may also play a role in maintaining
CC       normal post-endocytic trafficking through the ARF6-regulated, non-
CC       clathrin pathway. The AP-2 alpha and AP-2 sigma subunits are thought to
CC       contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. May also
CC       play a role in extracellular calcium homeostasis (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 AP2A1 or AP2A2 and beta-type
CC       subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small
CC       adaptin (sigma-type subunit AP2S1). {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=AP-2 appears to be excluded from internalizing
CC       CCVs and to disengage from sites of endocytosis seconds before
CC       internalization of the nascent CCV. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CR859555; CAH91720.1; -; mRNA.
DR   RefSeq; NP_001125999.1; NM_001132527.1.
DR   AlphaFoldDB; Q5R940; -.
DR   SMR; Q5R940; -.
DR   STRING; 9601.ENSPPYP00000011367; -.
DR   GeneID; 100172940; -.
DR   KEGG; pon:100172940; -.
DR   CTD; 1175; -.
DR   eggNOG; KOG0935; Eukaryota.
DR   HOGENOM; CLU_061221_3_1_1; -.
DR   InParanoid; Q5R940; -.
DR   OMA; IYLSHIH; -.
DR   TreeFam; TF300139; -.
DR   Proteomes; UP000001595; Chromosome 19.
DR   GO; GO:0030122; C:AP-2 adaptor complex; IEA:InterPro.
DR   GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell membrane; Coated pit; Endocytosis; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..142
FT                   /note="AP-2 complex subunit sigma"
FT                   /id="PRO_0000193806"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53680"
SQ   SEQUENCE   142 AA;  17018 MW;  CA3FD868C65AEDF6 CRC64;
     MIRFILIQNR AGKTRLAKWY MQFDDDEKQK LIEEVHAVVT VRDAKHTNFV EFRNFKIIYR
     RYAGLYFCIC VDVNDNNLAY LEAIHNFVEV LNEYFHNVCE LDLVFNFYKV YTVVDEMFLA
     GEIRETSQTK VLKQLLMLQS LE