ID   AP3M_SCHPO              Reviewed;         425 AA.
AC   O94669;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=AP-3 complex subunit mu;
DE   AltName: Full=Adaptor-related protein complex 3 subunit mu;
GN   Name=apm3; ORFNames=SPBC651.11c;
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is
CC       not clathrin-associated. The complex is associated with the Golgi
CC       region as well as more peripheral structures. It facilitates the
CC       budding of vesicles from the Golgi membrane and may be directly
CC       involved in trafficking to the vacuole (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:16823372}. Membrane
CC       {ECO:0000269|PubMed:16823372}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:16823372}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:P38153}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:P38153}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P38153}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P38153}. Note=Localizes at the cell tip and the
CC       barrier septum (PubMed:16823372). Component of the coat surrounding the
CC       cytoplasmic face of coated vesicles located at the Golgi complex (By
CC       similarity). {ECO:0000250|UniProtKB:P38153,
CC       ECO:0000269|PubMed:16823372}.
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; CU329671; CAB37607.1; -; Genomic_DNA.
DR   PIR; T40610; T40610.
DR   RefSeq; NP_595509.1; NM_001021419.2.
DR   AlphaFoldDB; O94669; -.
DR   SMR; O94669; -.
DR   BioGRID; 277634; 46.
DR   STRING; 4896.SPBC651.11c.1; -.
DR   MaxQB; O94669; -.
DR   PaxDb; O94669; -.
DR   EnsemblFungi; SPBC651.11c.1; SPBC651.11c.1:pep; SPBC651.11c.
DR   GeneID; 2541119; -.
DR   KEGG; spo:SPBC651.11c; -.
DR   PomBase; SPBC651.11c; apm3.
DR   VEuPathDB; FungiDB:SPBC651.11c; -.
DR   eggNOG; KOG2740; Eukaryota.
DR   HOGENOM; CLU_026996_6_2_1; -.
DR   InParanoid; O94669; -.
DR   OMA; WDIGRID; -.
DR   PhylomeDB; O94669; -.
DR   PRO; PR:O94669; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030123; C:AP-3 adaptor complex; ISO:PomBase.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0051286; C:cell tip; HDA:PomBase.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0006896; P:Golgi to vacuole transport; ISO:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   InterPro; IPR036168; AP2_Mu_C_sf.
DR   InterPro; IPR001392; Clathrin_mu.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   InterPro; IPR028565; MHD.
DR   Pfam; PF00928; Adap_comp_sub; 1.
DR   PIRSF; PIRSF005992; Clathrin_mu; 1.
DR   PRINTS; PR00314; CLATHRINADPT.
DR   SUPFAM; SSF49447; SSF49447; 1.
DR   SUPFAM; SSF64356; SSF64356; 1.
DR   PROSITE; PS51072; MHD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Golgi apparatus; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..425
FT                   /note="AP-3 complex subunit mu"
FT                   /id="PRO_0000316199"
FT   DOMAIN          175..423
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ   SEQUENCE   425 AA;  48422 MW;  7320E1B47B458854 CRC64;
     MSTIEAIYLV DTNGALLLQL ESRGRTSPIT LEHIKNELFR YKLRNEEPPF ILHNKNFLIF
     QELEEDVRLC IPTTCDTEPL YIHDIMRRIV DVVKTFFGGF NASKVEKNVC VIVQLLAEMI
     DYGYATCMEP NALQDIVPLP SFMNKFMAVT GLQTNTPTLA RDTVPWRTAK AKYATNEFFI
     HVLERVSAVY QPNGKLAFGT VKSDMECKCQ ISGMPLLLLS LRPGTKLGNV RFHQSVNLKR
     WKQHPDQIEF IPPDGKFTLA SFQTDFATQK SLPVVVEAKN KLDGRFEVRI RNTGKKSVEN
     LKILITIPQA LKSVTVTEGN YIFRASKYTH MEEGILEWSV KKLAWTSPAL VLTGFLAPLK
     KDANSTEESS SYSKLEHLDL QYKLQGSTLH NFKVESLKML NHPDKKSYKG VKHTIIAQNV
     SFRFR