ID   AP3M2_MOUSE             Reviewed;         418 AA.
AC   Q8R2R9; Q3UYJ3; Q923G7;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=AP-3 complex subunit mu-2;
DE   AltName: Full=Adaptor-related protein complex 3 subunit mu-2;
DE   AltName: Full=Clathrin assembly protein assembly protein complex 3 mu-2 medium chain;
DE   AltName: Full=Clathrin coat assembly protein AP47 homolog 2;
DE   AltName: Full=Clathrin coat-associated protein AP47 homolog 2;
DE   AltName: Full=Golgi adaptor AP-1 47 kDa protein homolog 2;
DE   AltName: Full=HA1 47 kDa subunit homolog 2;
DE   AltName: Full=Mu3B-adaptin;
DE            Short=m3B;
DE   AltName: Full=P47B;
GN   Name=Ap3m2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nakatsu F., Nakamura N., Shioda N., Saito T., Ohno H.;
RT   "Molecular cloning of the mouse m3B, a subunit of the neuron-specific AP-3B
RT   complex.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpus striatum, Medulla oblongata, Pituitary, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   FUNCTION, AND ASSOCIATION WITH THE BLOC-1 COMPLEX.
RX   PubMed=21998198; DOI=10.1091/mbc.e11-07-0592;
RA   Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B.,
RA   Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
RT   "The schizophrenia susceptibility factor dysbindin and its associated
RT   complex sort cargoes from cell bodies to the synapse.";
RL   Mol. Biol. Cell 22:4854-4867(2011).
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. Ap47 is a subunit of the
CC       plasma membrane adaptor (By similarity). In concert with the BLOC-1
CC       complex, AP-3 is required to target cargos into vesicles assembled at
CC       cell bodies for delivery into neurites and nerve terminals.
CC       {ECO:0000250, ECO:0000269|PubMed:21998198}.
CC   -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC       of two large adaptins (delta-type subunit AP3D1 and beta-type subunit
CC       AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and
CC       a small adaptin (sigma-type subunit APS1 or AP3S2) (By similarity). AP-
CC       3 associates with the BLOC-1 complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane
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 located at the Golgi complex.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AY039763; AAK73278.1; -; mRNA.
DR   EMBL; AK077365; BAC36770.1; -; mRNA.
DR   EMBL; AK081220; BAC38169.1; -; mRNA.
DR   EMBL; AK082988; BAC38723.1; -; mRNA.
DR   EMBL; AK134634; BAE22219.1; -; mRNA.
DR   EMBL; BC027301; AAH27301.1; -; mRNA.
DR   EMBL; BC030484; AAH30484.1; -; mRNA.
DR   CCDS; CCDS22184.1; -.
DR   RefSeq; NP_001116292.1; NM_001122820.1.
DR   RefSeq; NP_083781.2; NM_029505.3.
DR   AlphaFoldDB; Q8R2R9; -.
DR   SMR; Q8R2R9; -.
DR   BioGRID; 211117; 6.
DR   ComplexPortal; CPX-5147; Neuronal AP-3 Adaptor complex, sigma3a variant.
DR   ComplexPortal; CPX-5148; Neuronal AP-3 Adaptor complex, sigma3b variant.
DR   CORUM; Q8R2R9; -.
DR   IntAct; Q8R2R9; 1.
DR   MINT; Q8R2R9; -.
DR   STRING; 10090.ENSMUSP00000128446; -.
DR   iPTMnet; Q8R2R9; -.
DR   PhosphoSitePlus; Q8R2R9; -.
DR   SwissPalm; Q8R2R9; -.
DR   EPD; Q8R2R9; -.
DR   jPOST; Q8R2R9; -.
DR   MaxQB; Q8R2R9; -.
DR   PaxDb; Q8R2R9; -.
DR   PeptideAtlas; Q8R2R9; -.
DR   PRIDE; Q8R2R9; -.
DR   ProteomicsDB; 296211; -.
DR   Antibodypedia; 24004; 85 antibodies from 20 providers.
DR   DNASU; 64933; -.
DR   Ensembl; ENSMUST00000163739; ENSMUSP00000128446; ENSMUSG00000031539.
DR   Ensembl; ENSMUST00000210656; ENSMUSP00000147967; ENSMUSG00000031539.
DR   GeneID; 64933; -.
DR   KEGG; mmu:64933; -.
DR   UCSC; uc009ldy.2; mouse.
DR   CTD; 10947; -.
DR   MGI; MGI:1929214; Ap3m2.
DR   VEuPathDB; HostDB:ENSMUSG00000031539; -.
DR   eggNOG; KOG2740; Eukaryota.
DR   GeneTree; ENSGT00940000157991; -.
DR   HOGENOM; CLU_026996_6_2_1; -.
DR   InParanoid; Q8R2R9; -.
DR   OMA; TEPNTID; -.
DR   OrthoDB; 928391at2759; -.
DR   PhylomeDB; Q8R2R9; -.
DR   TreeFam; TF315187; -.
DR   BioGRID-ORCS; 64933; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Ap3m2; mouse.
DR   PRO; PR:Q8R2R9; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8R2R9; protein.
DR   Bgee; ENSMUSG00000031539; Expressed in glossopharyngeal ganglion and 220 other tissues.
DR   Genevisible; Q8R2R9; MM.
DR   GO; GO:0030123; C:AP-3 adaptor complex; IC:ComplexPortal.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
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:0005769; C:early endosome; IC:ComplexPortal.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR   GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:UniProtKB.
DR   GO; GO:0035654; P:clathrin-coated vesicle cargo loading, AP-3-mediated; IC:ComplexPortal.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0046907; P:intracellular transport; IC:ComplexPortal.
DR   GO; GO:0016183; P:synaptic vesicle coating; IC:ComplexPortal.
DR   GO; GO:0036465; P:synaptic vesicle recycling; IC:ComplexPortal.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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   Cytoplasmic vesicle; Golgi apparatus; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..418
FT                   /note="AP-3 complex subunit mu-2"
FT                   /id="PRO_0000193785"
FT   DOMAIN          176..417
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT   CONFLICT        346..348
FT                   /note="INP -> LNQ (in Ref. 1; AAK73278)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   418 AA;  46916 MW;  BE72859A36889C9C CRC64;
     MIHSLFLINS SGDIFLEKHW KSVVSRSVCD YFFEAQERAT EAENVPPVIP TPHHYLLSVY
     RHKIFFVAVI QTEVPPLFVI EFLHRVVDTF QDYFGVCSEP VIKDNVVVVY EVLEEMLDNG
     FPLATESNIL KELIKPPTIL RTVVNTITGS TNVGDQLPTG QLSVVPWRRT GVKYTNNEAY
     FDVVEEIDAI IDKSGSTVTA EIQGVIDACV KLTGMPDLTL SFMNPRLLDD VSFHPCVRFK
     RWESERILSF IPPDGNFRLL AYHVSAQNLV AIPVYVKHSI SFRDSSSLGR FEITVGPKQT
     MGKTIEGVIV TSQMPKGVLN MSLTPSQGTH TFDPVTKMLS WDVGKINPQK LPSLKGTMGL
     QVGASKPDEN PTINLQFKIQ QLAISGLKVN RLDMYGEKYK PFKGIKYMTK AGKFQVRT