AP2MA_DANRE
ID AP2MA_DANRE Reviewed; 436 AA.
AC Q6NWK2; Q802V9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=AP-2 complex subunit mu-A;
DE AltName: Full=AP-2 mu-A chain;
DE AltName: Full=Clathrin assembly protein complex 2 mu-A medium chain;
DE AltName: Full=Clathrin coat assembly protein AP50-A;
DE AltName: Full=Clathrin coat-associated protein AP50-A;
DE AltName: Full=Mu2-adaptin-A;
DE AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein A;
GN Name=ap2m1a; ORFNames=si:ch211-252f13.2, zgc:85653;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) 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; BX470264; CAP09331.1; -; Genomic_DNA.
DR EMBL; BC047180; AAH47180.1; -; mRNA.
DR EMBL; BC067560; AAH67560.1; -; mRNA.
DR RefSeq; NP_997742.1; NM_212577.2.
DR AlphaFoldDB; Q6NWK2; -.
DR SMR; Q6NWK2; -.
DR STRING; 7955.ENSDARP00000046586; -.
DR PaxDb; Q6NWK2; -.
DR Ensembl; ENSDART00000046587; ENSDARP00000046586; ENSDARG00000002790.
DR GeneID; 321051; -.
DR KEGG; dre:321051; -.
DR CTD; 321051; -.
DR ZFIN; ZDB-GENE-030131-9784; ap2m1a.
DR eggNOG; KOG0938; Eukaryota.
DR GeneTree; ENSGT00940000159223; -.
DR HOGENOM; CLU_026996_5_2_1; -.
DR InParanoid; Q6NWK2; -.
DR PhylomeDB; Q6NWK2; -.
DR TreeFam; TF300722; -.
DR Reactome; R-DRE-177504; Retrograde neurotrophin signalling.
DR Reactome; R-DRE-190873; Gap junction degradation.
DR Reactome; R-DRE-196025; Formation of annular gap junctions.
DR Reactome; R-DRE-2132295; MHC class II antigen presentation.
DR Reactome; R-DRE-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-DRE-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-DRE-437239; Recycling pathway of L1.
DR Reactome; R-DRE-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-DRE-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-DRE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DRE-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DRE-8866427; VLDLR internalisation and degradation.
DR Reactome; R-DRE-8964038; LDL clearance.
DR PRO; PR:Q6NWK2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000002790; Expressed in presomitic mesoderm and 38 other tissues.
DR ExpressionAtlas; Q6NWK2; baseline and differential.
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-A"
FT /id="PRO_0000318895"
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"
FT CONFLICT 117
FT /note="D -> Y (in Ref. 1; AAH47180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 49660 MW; CAFA6942F73F4B4D CRC64;
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMT AYFGKISEEN IKNNFVLIYE LLDEILDFGY
PQNSETGALK TFITQQGIKG QHQTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIDKQGKGGT TDDAGKSGKQ
SIAIDDCTFH QCVRLSKFDS ERSISFIPPD GEYELMRYRT TKDIILPFRV IPLVREVGRT
KLEVKVVIKS NFKPSLLAQK IEVRIPTPLN TSGVQVICMK GKAKYKASEN AIVWKIKRMA
GMKESQISAE IELLPTNDKK KWARPPISMN FEVPFAPSGL KVRYLKVFES KLNYSDHDVI
KWVRYIGRSG IYETRC
