ID   AP3B2_MOUSE             Reviewed;        1082 AA.
AC   Q9JME5; B2RTK2; Q3UYP8; Q6QR53; Q8R1E5;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=AP-3 complex subunit beta-2;
DE   AltName: Full=Adaptor protein complex AP-3 subunit beta-2;
DE   AltName: Full=Adaptor-related protein complex 3 subunit beta-2;
DE   AltName: Full=Beta-3B-adaptin;
DE   AltName: Full=Clathrin assembly protein complex 3 beta-2 large chain;
GN   Name=Ap3b2;
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].
RC   STRAIN=C57BL/6J;
RA   Seong E., Burmeister M.;
RT   "Ap3b2, a neuron specific subunit of adaptor protein complex 3 (AP-3).";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-738.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 608-1082.
RC   TISSUE=Brain;
RX   PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA   Inoue S., Sano H., Ohta M.;
RT   "Growth suppression of Escherichia coli by induction of expression of
RT   mammalian genes with transmembrane or ATPase domains.";
RL   Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-282, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, and Pancreas;
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   [7]
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: Subunit of non-clathrin- and clathrin-associated adaptor
CC       protein complex 3 (AP-3) that plays a role in protein sorting in the
CC       late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes
CC       mediate both the recruitment of clathrin to membranes and the
CC       recognition of sorting signals within the cytosolic tails of
CC       transmembrane cargo molecules. AP-3 appears to be involved in the
CC       sorting of a subset of transmembrane proteins targeted to lysosomes and
CC       lysosome-related organelles. In concert with the BLOC-1 complex, AP-3
CC       is required to target cargos into vesicles assembled at cell bodies for
CC       delivery into neurites and nerve terminals.
CC       {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: Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC       Note=Component of the coat surrounding the cytoplasmic face of coated
CC       vesicles located at the Golgi complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AY528675; AAS18679.1; -; mRNA.
DR   EMBL; BC139378; AAI39379.1; -; mRNA.
DR   EMBL; BC139379; AAI39380.1; -; mRNA.
DR   EMBL; AK134504; BAE22164.1; -; mRNA.
DR   EMBL; AB030202; BAA92765.1; -; mRNA.
DR   CCDS; CCDS21403.1; -.
DR   RefSeq; NP_067467.2; NM_021492.3.
DR   AlphaFoldDB; Q9JME5; -.
DR   SMR; Q9JME5; -.
DR   BioGRID; 198133; 11.
DR   ComplexPortal; CPX-5147; Neuronal AP-3 Adaptor complex, sigma3a variant.
DR   ComplexPortal; CPX-5148; Neuronal AP-3 Adaptor complex, sigma3b variant.
DR   IntAct; Q9JME5; 3.
DR   MINT; Q9JME5; -.
DR   STRING; 10090.ENSMUSP00000080739; -.
DR   iPTMnet; Q9JME5; -.
DR   PhosphoSitePlus; Q9JME5; -.
DR   SwissPalm; Q9JME5; -.
DR   jPOST; Q9JME5; -.
DR   MaxQB; Q9JME5; -.
DR   PaxDb; Q9JME5; -.
DR   PeptideAtlas; Q9JME5; -.
DR   PRIDE; Q9JME5; -.
DR   ProteomicsDB; 281895; -.
DR   Antibodypedia; 28110; 141 antibodies from 27 providers.
DR   DNASU; 11775; -.
DR   Ensembl; ENSMUST00000082090; ENSMUSP00000080739; ENSMUSG00000062444.
DR   GeneID; 11775; -.
DR   KEGG; mmu:11775; -.
DR   UCSC; uc009iby.1; mouse.
DR   CTD; 8120; -.
DR   MGI; MGI:1100869; Ap3b2.
DR   VEuPathDB; HostDB:ENSMUSG00000062444; -.
DR   eggNOG; KOG1060; Eukaryota.
DR   GeneTree; ENSGT00940000156817; -.
DR   HOGENOM; CLU_006320_3_1_1; -.
DR   InParanoid; Q9JME5; -.
DR   OMA; IGRCAQS; -.
DR   OrthoDB; 323029at2759; -.
DR   PhylomeDB; Q9JME5; -.
DR   TreeFam; TF314605; -.
DR   BioGRID-ORCS; 11775; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Ap3b2; mouse.
DR   PRO; PR:Q9JME5; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9JME5; protein.
DR   Bgee; ENSMUSG00000062444; Expressed in dentate gyrus of hippocampal formation granule cell and 147 other tissues.
DR   ExpressionAtlas; Q9JME5; baseline and differential.
DR   Genevisible; Q9JME5; MM.
DR   GO; GO:0030123; C:AP-3 adaptor complex; IC:ComplexPortal.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
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:0006886; P:intracellular protein transport; TAS:MGI.
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   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR026740; AP3_beta.
DR   InterPro; IPR029390; AP3B_C.
DR   InterPro; IPR026739; AP_beta.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR   PANTHER; PTHR11134; PTHR11134; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF14796; AP3B1_C; 1.
DR   PIRSF; PIRSF037096; AP3_complex_beta; 1.
DR   SMART; SM01355; AP3B1_C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF49348; SSF49348; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1082
FT                   /note="AP-3 complex subunit beta-2"
FT                   /id="PRO_0000193749"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..680
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..735
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..762
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         272
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        734
FT                   /note="E -> D (in Ref. 4; BAA92765)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1082 AA;  119193 MW;  A2FEB20E83E16A52 CRC64;
     MSAAPAYSED KGGSAGPGEP EYGHDPASGG IFSSDYKRHD DLKEMLDTNK DSLKLEAMKR
     IVAMIARGKN ASDLFPAVVK NVACKNIEVK KLVYVYLVRY AEEQQDLALL SISTFQRGLK
     DPNQLIRASA LRVLSSIRVP IIVPIMMLAI KEAASDMSPY VRKTAAHAIP KLYSLDSDQK
     DQLIEVIEKL LADKTTLVAG SVVMAFEEVC PERIDLIHKN YRKLCNLLID VEEWGQVVII
     SMLTRYARTQ FLSPTQNESL LEENPEKAFY GSEEDEAKGP GSEEAATAAL PARKPYVMDP
     DHRLLLRNTK PLLQSRSAAV VMAVAQLYFH LAPKAEVGVI AKALVRLLRS HSEVQYVVLQ
     NVATMSIKRR GMFEPYLKSF YIRSTDPTQI KILKLEVLTN LANETNIPTV LREFQTYIRS
     MDKDFVAATI QAIGRCATNI GRVRDTCLNG LVQLLSNRDE LVVAESVVVI KKLLQMQPAQ
     HGEIIKHLAK LTDNIQVPMA RASILWLIGE YCEHVPKIAP DVLRKMAKSF TAEEDIVKLQ
     VINLAAKLYL TNSKQTKLLT QYVLSLAKYD QNYDIRDRAR FTRQLIVPSE QGGALSRHAK
     KLFLAPKPAP ILESSFKDRD HFQLGSLSHL LNAKATGYQE LPDWPEEAPD PSVRNVEVPE
     WTKCSNREKR KEKEKPFYSD SEGESGPTES ADSEPESESE SESKSSSGSG SGESSSESDN
     EEEDEEKGGG SESEQSEEED EKKKKTKKKK ASEGHREGSS SEEGSDSSSS SESEVTSESE
     EEQVEPASWR KKTPPGSKSA PVAKEISLLD LEDFTPPSVQ PVSPPMVVST SLAADLEGLT
     LTDSSLVPSL LSPVSSIGRQ ELLHRVAGEG LSVDYAFSRQ PFSGDPHMVS LHIYFSNNSE
     TPIKGLHVGT PKLPAGISIQ EFPEIESLAP GESTTTVMGI NFCDSTQAAN FQLCTQTRQF
     YVSIQPPVGE LMAPVFMSEN EFKKEQGKLT GMNEITEKLT LPDTCRSDHM VVQKVTATAN
     LGRVPCGTSD EYRFAGRTLT SGSLVLLTLD ARAAGAAQLT VNSEKMVIGT MLVKDVIQAL
     TQ