AP2M_SCHPO
ID AP2M_SCHPO Reviewed; 446 AA.
AC Q09718;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=AP-2 complex subunit mu;
DE AltName: Full=Clathrin assembly protein complex 2 mu medium chain;
DE AltName: Full=Clathrin coat-associated protein AP50;
DE AltName: Full=Mu2-adaptin;
DE AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
DE AltName: Full=Probable clathrin coat assembly protein AP50;
GN Name=apm4; ORFNames=SPAC31A2.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-151; SER-152 AND
RP THR-157, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 (Potential). {ECO:0000305}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit apl3 and beta-type subunit
CC apl1), a medium chain (mu-type subunit apm4) and a small adaptin
CC (sigma-type subunit aps2). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Component of the coat surrounding the
CC cytoplasmic face of coated vesicles in the plasma membrane.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA90467.1; -; Genomic_DNA.
DR PIR; S59646; S59646.
DR RefSeq; NP_592921.1; NM_001018322.2.
DR AlphaFoldDB; Q09718; -.
DR SMR; Q09718; -.
DR BioGRID; 278027; 41.
DR STRING; 4896.SPAC31A2.09c.1; -.
DR iPTMnet; Q09718; -.
DR MaxQB; Q09718; -.
DR PaxDb; Q09718; -.
DR PRIDE; Q09718; -.
DR EnsemblFungi; SPAC31A2.09c.1; SPAC31A2.09c.1:pep; SPAC31A2.09c.
DR GeneID; 2541527; -.
DR KEGG; spo:SPAC31A2.09c; -.
DR PomBase; SPAC31A2.09c; apm4.
DR VEuPathDB; FungiDB:SPAC31A2.09c; -.
DR eggNOG; KOG0938; Eukaryota.
DR HOGENOM; CLU_026996_5_2_1; -.
DR InParanoid; Q09718; -.
DR OMA; VWKIPRI; -.
DR PhylomeDB; Q09718; -.
DR Reactome; R-SPO-196025; Formation of annular gap junctions.
DR Reactome; R-SPO-437239; Recycling pathway of L1.
DR Reactome; R-SPO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SPO-8866427; VLDLR internalisation and degradation.
DR Reactome; R-SPO-8964038; LDL clearance.
DR PRO; PR:Q09718; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030122; C:AP-2 adaptor complex; ISO:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; ISO:PomBase.
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 1: Evidence at protein level;
KW Cell membrane; Coated pit; Endocytosis; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..446
FT /note="AP-2 complex subunit mu"
FT /id="PRO_0000193779"
FT DOMAIN 177..445
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 446 AA; 50821 MW; 95AA8F8A8CFFA680 CRC64;
MISGLFIFNL KGDTLICKTF RHDLKKSVTE IFRVAILTNT DYRHPIVSIG SSTYIYTKHE
DLYVVAITKG NPNVMIVLEF LESLIQDLTH YFGKLNENTV KDNVSFIFEL LDEMIDYGII
QTTEPDALAR SVSITAVKKK GNALSLKRSH SSQLAHTTSS EIPGSVPWRR AGIKYRKNSI
YIDIVERMNL LISSTGNVLR SDVSGVVKMR AMLSGMPECQ FGLNDKLDFK LKQSESKSKS
NNSRNPSSVN GGFVILEDCQ FHQCVRLPEF ENEHRITFIP PDGEVELMSY RSHENINIPF
RIVPIVEQLS KQKIIYRISI RADYPHKLSS SLNFRIPVPT NVVKANPRVN RGKAGYEPSE
NIINWKIPRF LGETELIFYA EVELSNTTNQ QIWAKPPISL DFNILMFTSS GLHVQYLRVS
EPSNSKYKSI KWVRYSTRAG TCEIRI
