ID AP2M1_CHICK Reviewed; 433 AA.
AC Q5ZMP6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
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=HA2 50 kDa subunit;
DE AltName: Full=Mu2-adaptin;
DE AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
GN Name=AP2M1; ORFNames=RCJMB04_1h23;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719338; CAG30997.1; -; mRNA.
DR RefSeq; NP_001072962.1; NM_001079494.1.
DR RefSeq; XP_015146933.1; XM_015291447.1.
DR AlphaFoldDB; Q5ZMP6; -.
DR SMR; Q5ZMP6; -.
DR STRING; 9031.ENSGALP00000013724; -.
DR PaxDb; 9031-ENSGALP00000013724; -.
DR Ensembl; ENSGALT00000013739; ENSGALP00000013724; ENSGALG00000008432.
DR Ensembl; ENSGALT00010046066.1; ENSGALP00010027460.1; ENSGALG00010019023.1.
DR Ensembl; ENSGALT00015047249; ENSGALP00015027802; ENSGALG00015019278.
DR GeneID; 770246; -.
DR KEGG; gga:770246; -.
DR CTD; 1173; -.
DR VEuPathDB; HostDB:geneid_770246; -.
DR eggNOG; KOG0938; Eukaryota.
DR GeneTree; ENSGT00940000159223; -.
DR HOGENOM; CLU_026996_5_2_1; -.
DR InParanoid; Q5ZMP6; -.
DR PhylomeDB; Q5ZMP6; -.
DR TreeFam; TF300722; -.
DR Reactome; R-GGA-177504; Retrograde neurotrophin signalling.
DR Reactome; R-GGA-190873; Gap junction degradation.
DR Reactome; R-GGA-196025; Formation of annular gap junctions.
DR Reactome; R-GGA-2132295; MHC class II antigen presentation.
DR Reactome; R-GGA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-GGA-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-GGA-437239; Recycling pathway of L1.
DR Reactome; R-GGA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-GGA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-GGA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-GGA-8866427; VLDLR internalisation and degradation.
DR Reactome; R-GGA-8964038; LDL clearance.
DR PRO; PR:Q5ZMP6; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000008432; Expressed in brain and 13 other cell types or tissues.
DR ExpressionAtlas; Q5ZMP6; 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:0006886; P:intracellular protein transport; IEA:InterPro.
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:SF236; AP-2 COMPLEX SUBUNIT MU; 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 2: Evidence at transcript level;
KW Cell membrane; Coated pit; Endocytosis; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..433
FT /note="AP-2 complex subunit mu"
FT /id="PRO_0000318893"
FT DOMAIN 168..432
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT BINDING 339
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 343
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 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:0000250|UniProtKB:P84092"
SQ SEQUENCE 433 AA; 49389 MW; D546E1BBCE90C796 CRC64;
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMT AYFGKISEEN IKNNFVLIYE LLDEILDFGY
PQNSETGALK TFITQQGIKS QTKEEQSQIT SQVTGQIGWR REGIKYRRNE LFLDVLESVN
LLMSPQGQVL SAHVSGRVVM KSYLSGMPEC KFGMNDKIVI EKQGKGTADE TGKSGKQSIA
IDDCTFHQCV RLSKFDSERS ISFIPPDGEF ELMRYRTTKD IILPFRVIPL VREVGRTKLE
VKVVIKSNFK PSLLAQKIEV RIPTPLNTSG VQVICMKGKA KYKASENAIV WKIKRMAGMK
ESQISAEIEL LPTNDKKKWA RPPISMNFEV PFAPSGLKVR YLKVFEPKLN YSDHDVIKWV
RYIGRSGIYE TRC
//
