ID   AP1M1_SCHPO             Reviewed;         426 AA.
AC   Q9HFE5;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=AP-1 complex subunit mu-1;
DE   AltName: Full=Clathrin assembly protein complex 1 mu-1 medium chain;
DE   AltName: Full=Mu-adaptin;
GN   Name=apm1; ORFNames=SPBP16F5.07;
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   INTERACTION WITH SAD1.
RX   PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA   Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT   "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT   membrane-bound components of the spindle pole body in fission yeast.";
RL   Mol. Genet. Genomics 270:449-461(2004).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC       of two large adaptins (gamma-type subunit apl4 and beta-type subunit
CC       apl2), a medium adaptin (mu-type subunit apm1) and a small adaptin
CC       (sigma-type subunit aps1). AP-1 interacts with clathrin (By
CC       similarity). Interacts with sad1. {ECO:0000250,
CC       ECO:0000269|PubMed:14655046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Membrane, clathrin-coated pit
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAC08546.1; -; Genomic_DNA.
DR   RefSeq; NP_595781.1; NM_001021681.2.
DR   AlphaFoldDB; Q9HFE5; -.
DR   SMR; Q9HFE5; -.
DR   BioGRID; 277818; 37.
DR   IntAct; Q9HFE5; 1.
DR   STRING; 4896.SPBP16F5.07.1; -.
DR   iPTMnet; Q9HFE5; -.
DR   MaxQB; Q9HFE5; -.
DR   PaxDb; Q9HFE5; -.
DR   EnsemblFungi; SPBP16F5.07.1; SPBP16F5.07.1:pep; SPBP16F5.07.
DR   GeneID; 2541306; -.
DR   KEGG; spo:SPBP16F5.07; -.
DR   PomBase; SPBP16F5.07; apm1.
DR   VEuPathDB; FungiDB:SPBP16F5.07; -.
DR   eggNOG; KOG0937; Eukaryota.
DR   HOGENOM; CLU_026996_0_0_1; -.
DR   InParanoid; Q9HFE5; -.
DR   OMA; CRAKAQI; -.
DR   PhylomeDB; Q9HFE5; -.
DR   Reactome; R-SPO-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q9HFE5; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030121; C:AP-1 adaptor complex; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0051286; C:cell tip; HDA:PomBase.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005768; C:endosome; IDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; IDA: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:0099638; P:endosome to plasma membrane protein transport; IDA:PomBase.
DR   GO; GO:0006895; P:Golgi to endosome transport; IMP:PomBase.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:PomBase.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:PomBase.
DR   GO; GO:0016192; P:vesicle-mediated transport; IMP:PomBase.
DR   InterPro; IPR036168; AP2_Mu_C_sf.
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   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   Coated pit; Cytoplasmic vesicle; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..426
FT                   /note="AP-1 complex subunit mu-1"
FT                   /id="PRO_0000193777"
FT   DOMAIN          167..425
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ   SEQUENCE   426 AA;  48956 MW;  911FEB137C63AED3 CRC64;
     MASAIFVLNL KGKVIISRDY RADIPMSVVE KFLPLKSEVE EEQGFSTPCL THEGINYIYI
     HHNDVYLLAL SKMNSDAMEM LVFLRKMADV FIDYFKELQE ESIRDNFVLV YELLDEIMDF
     GFPQTTETKI LQEYITQTSN TVKKHAPPPI AMTNAISWRS EGIHYRKNEV FLDVIESVNL
     IAAADGTVIQ SEILGKVRLK CYLSGMPELR LGLNDKVLFE AAGRTIKGNT VEMEDVKFHQ
     CVRLARFEND RTISFIPPDG EFDLMSYRMS SNVRPLIWVE CESIVHSGSR IEFMVKAKAQ
     FKKRCIANNV QIIIPVPEDA DSPRFQTSNG HVQYAPEQAA MVWNIKKFAG GKEFFMRAEM
     GLPSVKNEDI QVQKKRPVQL KFAIPYFTTS GIQVRYLKIT EPKLNYHAMP WVRYVTQNGT
     EYSIRQ