AP2S1_BOVIN
ID AP2S1_BOVIN Reviewed; 142 AA.
AC Q17QC5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Sigma2-adaptin;
GN Name=AP2S1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) 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; BC118437; AAI18438.1; -; mRNA.
DR RefSeq; NP_001069546.1; NM_001076078.2.
DR AlphaFoldDB; Q17QC5; -.
DR SMR; Q17QC5; -.
DR STRING; 9913.ENSBTAP00000013989; -.
DR PaxDb; Q17QC5; -.
DR PRIDE; Q17QC5; -.
DR Ensembl; ENSBTAT00000013989; ENSBTAP00000013989; ENSBTAG00000010584.
DR GeneID; 536553; -.
DR KEGG; bta:536553; -.
DR CTD; 1175; -.
DR VEuPathDB; HostDB:ENSBTAG00000010584; -.
DR VGNC; VGNC:25986; AP2S1.
DR eggNOG; KOG0935; Eukaryota.
DR GeneTree; ENSGT00970000193421; -.
DR HOGENOM; CLU_061221_3_1_1; -.
DR InParanoid; Q17QC5; -.
DR OMA; IYLSHIH; -.
DR OrthoDB; 1307450at2759; -.
DR TreeFam; TF300139; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000010584; Expressed in floor plate of diencephalon and 101 other tissues.
DR ExpressionAtlas; Q17QC5; baseline.
DR GO; GO:0030122; C:AP-2 adaptor complex; IEA:InterPro.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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 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 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_0000283805"
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
