AP2M1_XENLA
ID AP2M1_XENLA Reviewed; 435 AA.
AC Q801Q8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=AP-2 complex subunit mu;
DE AltName: Full=AP-2 mu chain;
DE AltName: Full=Clathrin assembly protein complex 2 mu medium chain;
DE AltName: Full=Clathrin coat assembly protein AP50;
DE AltName: Full=Clathrin coat-associated protein AP50;
DE AltName: Full=Mu2-adaptin;
DE AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
GN Name=ap2m1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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. AP50 is a subunit of the
CC plasma membrane adaptor. The complex binds polyphosphoinositide-
CC containing lipids. {ECO:0000250|UniProtKB:P84092,
CC ECO:0000250|UniProtKB:Q96CW1}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit and beta-type subunit), a
CC medium adaptin (mu-type subunit) and a small adaptin (sigma-type
CC subunit). {ECO:0000250|UniProtKB:Q96CW1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96CW1}.
CC Membrane, coated pit {ECO:0000250|UniProtKB:Q96CW1}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q96CW1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96CW1}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; BC047969; AAH47969.1; -; mRNA.
DR EMBL; BC072057; AAH72057.1; -; mRNA.
DR RefSeq; NP_001080803.1; NM_001087334.1.
DR RefSeq; NP_001085100.1; NM_001091631.1.
DR RefSeq; XP_018117167.1; XM_018261678.1.
DR AlphaFoldDB; Q801Q8; -.
DR SMR; Q801Q8; -.
DR BioGRID; 101537; 1.
DR BioGRID; 98739; 2.
DR IntAct; Q801Q8; 1.
DR MaxQB; Q801Q8; -.
DR DNASU; 380497; -.
DR DNASU; 432171; -.
DR GeneID; 380497; -.
DR GeneID; 432171; -.
DR KEGG; xla:380497; -.
DR KEGG; xla:432171; -.
DR CTD; 380497; -.
DR CTD; 432171; -.
DR Xenbase; XB-GENE-6253608; ap2m1.L.
DR Xenbase; XB-GENE-17345513; ap2m1.S.
DR OrthoDB; 725236at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 380497; Expressed in brain and 19 other tissues.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd09251; AP-2_Mu2_Cterm; 1.
DR CDD; cd14836; AP2_Mu_N; 1.
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 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; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Coated pit; Endocytosis; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..435
FT /note="AP-2 complex subunit mu"
FT /id="PRO_0000318896"
FT DOMAIN 170..434
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT BINDING 341
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:0000250|UniProtKB:P84092"
FT BINDING 345
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:0000250|UniProtKB:P84092"
FT BINDING 354
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:0000250|UniProtKB:P84092"
SQ SEQUENCE 435 AA; 49685 MW; 7AAEB2C3807B911F CRC64;
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMT AYFGKISEEN IKNNFVLIYE LLDEILDFGY
PQNSETGALK TFITQQGIKS QHQTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIEKQGKGTA DETGKTGKQS
IAIDDCTFHQ CVRLSKFDSE RSISFIPPDG EYELMRYRTT KDIILPFRVI PLVREVGRTK
LEVKVVIKSN FKPSLLAQKI EVRIPTPLNT SGVQVICMKG KAKYKASENA IVWKIKRMAG
MKESQISAEI ELLPTNDKKK WARPPISMNF EVPFAPSGLK VRYLKVFEPK LNYSDHDVIK
WVRYIGRSGI YETRC
