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Database: UniProt
Entry: P62744
LinkDB: P62744
Original site: P62744 
ID   AP2S1_RAT               Reviewed;         142 AA.
AC   P62744; P70626; P97626; Q00380;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   12-AUG-2020, entry version 123.
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; Synonyms=Ap17, Claps2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=2040623;
RA   Kirchhausen T., Davis A.C., Frucht S., O'Brine Greco B., Payne G.S.,
RA   Tubb B.;
RT   "AP17 and AP19, the mammalian small chains of the clathrin-associated
RT   protein complexes show homology to Yap17p, their putative homolog in
RT   yeast.";
RL   J. Biol. Chem. 266:11153-11157(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar Kyoto;
RX   PubMed=10559001; DOI=10.1161/01.atv.19.11.2600;
RA   Adams L.D., Lemire J.M., Schwartz S.M.;
RT   "A systematic analysis of 40 random genes in cultured vascular smooth
RT   muscle subtypes reveals a heterogeneity of gene expression and identifies
RT   the tight junction gene zonula occludens 2 as a marker of epithelioid 'pup'
RT   smooth muscle cells and a participant in carotid neointimal formation.";
RL   Arterioscler. Thromb. Vasc. Biol. 19:2600-2608(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX   PubMed=14745134; DOI=10.1247/csf.28.419;
RA   Nakatsu F., Ohno H.;
RT   "Adaptor protein complexes as the key regulators of protein sorting in the
RT   post-Golgi network.";
RL   Cell Struct. Funct. 28:419-429(2003).
RN   [5]
RP   FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX   PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA   Owen D.J., Collins B.M., Evans P.R.;
RT   "Adaptors for clathrin coats: structure and function.";
RL   Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
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, ECO:0000269|PubMed:14745134,
CC       ECO:0000269|PubMed:15473838}.
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. Membrane, coated pit; Peripheral
CC       membrane protein; Cytoplasmic side. Note=AP-2 appears to be excluded
CC       from internalizing CCVs and to disengage from sites of endocytosis
CC       seconds before internalization of the nascent CCV. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC       {ECO:0000305}.
DR   EMBL; M37194; AAA40742.1; -; mRNA.
DR   EMBL; U75917; AAB46980.1; -; mRNA.
DR   EMBL; BC088138; AAH88138.1; -; mRNA.
DR   PIR; B40535; B40535.
DR   RefSeq; NP_075241.2; NM_022952.2.
DR   PDB; 4NEE; X-ray; 2.88 A; D/F/I/L=1-142.
DR   PDB; 6OWO; EM; 3.20 A; S=1-142.
DR   PDB; 6OWT; EM; 3.80 A; S=1-142.
DR   PDB; 6OXL; EM; 3.50 A; S=1-142.
DR   PDBsum; 4NEE; -.
DR   PDBsum; 6OWO; -.
DR   PDBsum; 6OWT; -.
DR   PDBsum; 6OXL; -.
DR   SMR; P62744; -.
DR   BioGRID; 249239; 1.
DR   IntAct; P62744; 4.
DR   MINT; P62744; -.
DR   STRING; 10116.ENSRNOP00000021310; -.
DR   BindingDB; P62744; -.
DR   ChEMBL; CHEMBL1697667; -.
DR   DrugCentral; P62744; -.
DR   iPTMnet; P62744; -.
DR   PhosphoSitePlus; P62744; -.
DR   jPOST; P62744; -.
DR   PaxDb; P62744; -.
DR   PRIDE; P62744; -.
DR   Ensembl; ENSRNOT00000021310; ENSRNOP00000021310; ENSRNOG00000015865.
DR   GeneID; 65046; -.
DR   KEGG; rno:65046; -.
DR   UCSC; RGD:620188; rat.
DR   CTD; 1175; -.
DR   RGD; 620188; Ap2s1.
DR   eggNOG; KOG0935; Eukaryota.
DR   GeneTree; ENSGT00970000193421; -.
DR   HOGENOM; CLU_061221_3_1_1; -.
DR   InParanoid; P62744; -.
DR   KO; K11827; -.
DR   OMA; SFFDNVC; -.
DR   OrthoDB; 1307450at2759; -.
DR   PhylomeDB; P62744; -.
DR   TreeFam; TF300139; -.
DR   Reactome; R-RNO-177504; Retrograde neurotrophin signalling.
DR   Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR   Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
DR   Reactome; R-RNO-437239; Recycling pathway of L1.
DR   Reactome; R-RNO-5099900; WNT5A-dependent internalization of FZD4.
DR   Reactome; R-RNO-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR   Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-RNO-8964038; LDL clearance.
DR   PRO; PR:P62744; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000015865; Expressed in brain and 22 other tissues.
DR   Genevisible; P62744; RN.
DR   GO; GO:0030122; C:AP-2 adaptor complex; IDA:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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   IDEAL; IID50215; -.
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   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Coated pit; Endocytosis; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..142
FT                   /note="AP-2 complex subunit sigma"
FT                   /id="PRO_0000193807"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53680"
FT   CONFLICT        83
FT                   /note="A -> G (in Ref. 2; AAB46980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109..110
FT                   /note="KV -> RF (in Ref. 2; AAB46980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="M -> I (in Ref. 2; AAB46980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="T -> R (in Ref. 2; AAB46980)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..9
FT                   /evidence="ECO:0000244|PDB:4NEE"
FT   STRAND          14..21
FT                   /evidence="ECO:0000244|PDB:4NEE"
FT   HELIX           25..41
FT                   /evidence="ECO:0000244|PDB:4NEE"
FT   STRAND          44..46
FT                   /evidence="ECO:0000244|PDB:4NEE"
FT   STRAND          48..51
FT                   /evidence="ECO:0000244|PDB:4NEE"
FT   STRAND          53..62
FT                   /evidence="ECO:0000244|PDB:4NEE"
FT   STRAND          65..72
FT                   /evidence="ECO:0000244|PDB:4NEE"
FT   HELIX           77..95
FT                   /evidence="ECO:0000244|PDB:4NEE"
FT   HELIX           100..105
FT                   /evidence="ECO:0000244|PDB:4NEE"
FT   HELIX           107..117
FT                   /evidence="ECO:0000244|PDB:4NEE"
FT   HELIX           128..140
FT                   /evidence="ECO:0000244|PDB:4NEE"
SQ   SEQUENCE   142 AA;  17018 MW;  CA3FD868C65AEDF6 CRC64;
     MIRFILIQNR AGKTRLAKWY MQFDDDEKQK LIEEVHAVVT VRDAKHTNFV EFRNFKIIYR
     RYAGLYFCIC VDVNDNNLAY LEAIHNFVEV LNEYFHNVCE LDLVFNFYKV YTVVDEMFLA
     GEIRETSQTK VLKQLLMLQS LE
//
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