ID   AP2MB_DANRE             Reviewed;         436 AA.
AC   Q7ZW98;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=AP-2 complex subunit mu-B;
DE   AltName: Full=AP-2 mu-B chain;
DE   AltName: Full=Clathrin assembly protein complex 2 mu-B medium chain;
DE   AltName: Full=Clathrin coat assembly protein AP50-B;
DE   AltName: Full=Clathrin coat-associated protein AP50-B;
DE   AltName: Full=Mu2-adaptin-B;
DE   AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein B;
GN   Name=ap2m1b; Synonyms=ap2m1; ORFNames=zgc:56643;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) 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 (By similarity). {ECO:0000250}.
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}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit; Peripheral
CC       membrane protein; Cytoplasmic side. Note=Component of the coat
CC       surrounding the cytoplasmic face of coated vesicles in the plasma
CC       membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       {ECO:0000305}.
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DR   EMBL; BC049515; AAH49515.1; -; mRNA.
DR   RefSeq; NP_957320.1; NM_201026.2.
DR   AlphaFoldDB; Q7ZW98; -.
DR   SMR; Q7ZW98; -.
DR   STRING; 7955.ENSDARP00000106819; -.
DR   PaxDb; Q7ZW98; -.
DR   GeneID; 394001; -.
DR   KEGG; dre:394001; -.
DR   CTD; 394001; -.
DR   ZFIN; ZDB-GENE-040426-1103; ap2m1b.
DR   eggNOG; KOG0938; Eukaryota.
DR   InParanoid; Q7ZW98; -.
DR   PhylomeDB; Q7ZW98; -.
DR   PRO; PR:Q7ZW98; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IGI:ZFIN.
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..436
FT                   /note="AP-2 complex subunit mu-B"
FT                   /id="PRO_0000318894"
FT   DOMAIN          170..435
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT   BINDING         342
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         346
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         355
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   436 AA;  49743 MW;  95E17931B3AE8C58 CRC64;
     MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
     SNIWLAAVTK QNVNAAMVFE FLYKMCDVMT AYFGKISEEN IKNNFVLIYE LLDEILDFGY
     PQNSETGALK TFITQQGIKS QHLTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
     VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIDKQGKGGT TDDTGKSGKQ
     SIAIDDCTFH QCVRLSKFDS ERSISFIPPD GEYELMRYRT TKDIILPFRV IPLVREVGRT
     KLEVKVVIKS NFKPSLLAQK IEVRIPTPLN TSGVQVICMK GKAKYKASEN AIVWKIKRMV
     GMKESQISAE IELLPTNDKK KWARPPISMN FEVPFAPSGL KVRYLKVFEP KLNYSDHDVI
     KWVRYIGRSG IYETRC