AP2M_DICDI
ID AP2M_DICDI Reviewed; 439 AA.
AC P54672; Q54ZW7; Q86AQ0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=AP-2 complex subunit mu;
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=Clathrin-adaptor medium chain Apm2;
DE AltName: Full=Mu2-adaptin;
DE AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
GN Name=apm2; Synonyms=apm1, apmA; ORFNames=DDB_G0277139;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8996086; DOI=10.1016/s0378-1119(96)00444-1;
RA Temesvari L.A., Seastone D.J., Cardelli J.A.;
RT "Cloning and characterization of a Dictyostelium discoideum cDNA encoding a
RT protein related to the medium chain subunit of clathrin-associated adaptor
RT complexes.";
RL Gene 183:47-51(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(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.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type and beta-type subunits), a medium
CC adaptin (mu-type subunit AP50) and a small adaptin (sigma-type subunit
CC AP17).
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.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U44890; AAB41282.1; -; mRNA.
DR EMBL; AAFI02000019; EAL68755.1; -; Genomic_DNA.
DR PIR; JC5719; JC5719.
DR RefSeq; XP_642749.1; XM_637657.1.
DR AlphaFoldDB; P54672; -.
DR SMR; P54672; -.
DR STRING; 44689.DDB0191267; -.
DR PaxDb; P54672; -.
DR PRIDE; P54672; -.
DR EnsemblProtists; EAL68755; EAL68755; DDB_G0277139.
DR GeneID; 8620939; -.
DR KEGG; ddi:DDB_G0277139; -.
DR dictyBase; DDB_G0277139; apm2.
DR eggNOG; KOG0938; Eukaryota.
DR HOGENOM; CLU_026996_5_2_1; -.
DR InParanoid; P54672; -.
DR OMA; VWKIPRI; -.
DR PhylomeDB; P54672; -.
DR Reactome; R-DDI-196025; Formation of annular gap junctions.
DR Reactome; R-DDI-437239; Recycling pathway of L1.
DR Reactome; R-DDI-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DDI-8866427; VLDLR internalisation and degradation.
DR Reactome; R-DDI-8964038; LDL clearance.
DR PRO; PR:P54672; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0030122; C:AP-2 adaptor complex; IDA:dictyBase.
DR GO; GO:0030132; C:clathrin coat of coated pit; IC:dictyBase.
DR GO; GO:0005905; C:clathrin-coated pit; ISS:dictyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IDA:dictyBase.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
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 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; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..439
FT /note="AP-2 complex subunit mu"
FT /id="PRO_0000193792"
FT DOMAIN 172..438
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT CONFLICT 29
FT /note="A -> G (in Ref. 1; AAB41282)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="S -> V (in Ref. 1; AAB41282)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="Q -> H (in Ref. 1; AAB41282)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="A -> R (in Ref. 1; AAB41282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 49785 MW; 49AD576E060E6B31 CRC64;
MISALFLMNG KGEVLISRIY RDDISRGVAN AFRLEVIGSQ ETRSPVKLIG STSFMYIKVG
NIYIVGVSRQ NVNACMVFEV LHQLVDIFKS YFDNLDEDSI RNNFVLVYEL LDEILDFGYP
QNCSTDVLKL YITQGQGKLK SLDKLKQDKI SKITIQATGT TPWRTPDIKY KRNELYIDVV
ESVNLLMSAE GNILRADVSG QVMMKCFLSG MPECKFGMND KVIMDREKST NGGSAARSGA
RRANGIEIDD ITFHQCVRLG KFDSDRTVSF IPPDGEFELM RYRTTEHINL PFKVIPIVRE
MGRTRLECSV TVKSNFSSKM FGANVKVIIP TPKNTAVCKI VVAAGKAKYM PEQDAIIWRI
RRFPGDTEFT LRAEVELMAS VNLDKKAWSR PPISMEFQVT MFTASGFSVR FLKVVEKSNY
TPIKWVRYLT KAGTYQNRI
