ID H2MGN1_ORYLA Unreviewed; 442 AA.
AC H2MGN1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=AP-2 complex subunit mu {ECO:0000256|PIRNR:PIRNR005992};
GN Name=ap2m1 {ECO:0000313|Ensembl:ENSORLP00000017769.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000017769.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000017769.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000017769.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000017769.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000017769.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|PIRNR:PIRNR005992}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR005992}.
CC Membrane, coated pit {ECO:0000256|PIRNR:PIRNR005992}; Peripheral
CC membrane protein {ECO:0000256|PIRNR:PIRNR005992}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR005992}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000256|ARBA:ARBA00005324, ECO:0000256|PIRNR:PIRNR005992}.
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DR AlphaFoldDB; H2MGN1; -.
DR STRING; 8090.ENSORLP00000017769; -.
DR Ensembl; ENSORLT00000017770.2; ENSORLP00000017769.2; ENSORLG00000014164.2.
DR eggNOG; KOG0938; Eukaryota.
DR GeneTree; ENSGT00940000159223; -.
DR HOGENOM; CLU_026996_5_2_1; -.
DR InParanoid; H2MGN1; -.
DR TreeFam; TF300722; -.
DR Proteomes; UP000001038; Chromosome 17.
DR Bgee; ENSORLG00000014164; Expressed in brain and 15 other cell types or tissues.
DR GO; GO:0030122; C:AP-2 adaptor complex; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR CDD; cd09251; AP-2_Mu2_Cterm; 1.
DR CDD; cd14836; AP2_Mu_N; 1.
DR Gene3D; 3.30.450.60; -; 1.
DR Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR043532; AP2_Mu_N.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR043512; Mu2_C.
DR PANTHER; PTHR10529; AP COMPLEX SUBUNIT MU; 1.
DR PANTHER; PTHR10529:SF371; AP-2 COMPLEX SUBUNIT MU-A; 1.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR005992};
KW Coated pit {ECO:0000256|ARBA:ARBA00023176, ECO:0000256|PIRNR:PIRNR005992};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583, ECO:0000256|PIRNR:PIRNR005992};
KW Lipid-binding {ECO:0000256|PIRSR:PIRSR005992-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005992};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR005992};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005992}.
FT DOMAIN 170..441
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT BINDING 348
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR005992-1"
FT BINDING 350
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR005992-1"
FT BINDING 352
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR005992-1"
FT BINDING 361
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR005992-1"
FT BINDING 363
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR005992-1"
SQ SEQUENCE 442 AA; 50140 MW; FF012A9951863E72 CRC64;
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMT AYFGKISEEN IKNNFVLIYE LLDEILDFGY
PQNSETGALK TFITQQGIKG QFQTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIDKQGKGGA TDDAAKSDLG
GGSGKQSIAI DDCTFHQCVR LSKFDSERSI SFIPPDGEYE LMRYRTTKDI ILPFRVIPLV
REVGRTKLEV KVVIKSNFKP SLLAQKIEVR IPTPLNTSGV QVICMKGKAK YKASENAIVW
KIKRMAGMKE SQISAEIELL PTNDKKKWAR PPISMNFEVP FAPSGLKVRY LKVFESKLNY
SDHDVIKWVR YIGRSGIYET RC
//
