AP3S2_MOUSE
ID AP3S2_MOUSE Reviewed; 193 AA.
AC Q8BSZ2; O09077; O09149; Q3UDG7; Q8CAY1; Q99589;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=AP-3 complex subunit sigma-2;
DE AltName: Full=AP-3 complex subunit sigma-3B;
DE AltName: Full=Adaptor-related protein complex 3 subunit sigma-2;
DE AltName: Full=Sigma-3B-adaptin;
DE Short=Sigma3B-adaptin;
DE AltName: Full=Sigma-adaptin 3b;
GN Name=Ap3s2;
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 TISSUE=Brain;
RX PubMed=9151686; DOI=10.1083/jcb.137.4.835;
RA Simpson F., Peden A.A., Christopoulou L., Robinson M.S.;
RT "Characterization of the adaptor-related protein complex, AP-3.";
RL J. Cell Biol. 137:835-845(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Placenta, and Thymus;
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 INTERACTION WITH AGAP1.
RX PubMed=12967569; DOI=10.1016/s1534-5807(03)00234-x;
RA Nie Z., Boehm M., Boja E.S., Vass W.C., Bonifacino J.S., Fales H.M.,
RA Randazzo P.A.;
RT "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP
RT AGAP1.";
RL Dev. Cell 5:513-521(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, and Spleen;
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: 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 lysosomes. 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: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. Interacts with AGAP1.
CC {ECO:0000250, ECO:0000269|PubMed:12967569}.
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 -!- TISSUE SPECIFICITY: Present in all adult tissues examined.
CC -!- SIMILARITY: Belongs to the adaptor complexes small 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; U91933; AAD03780.1; -; mRNA.
DR EMBL; AK028372; BAC25912.1; -; mRNA.
DR EMBL; AK037336; BAC29788.1; -; mRNA.
DR EMBL; AK150085; BAE29294.1; -; mRNA.
DR CCDS; CCDS21389.1; -.
DR RefSeq; NP_033812.3; NM_009682.3.
DR AlphaFoldDB; Q8BSZ2; -.
DR SMR; Q8BSZ2; -.
DR ComplexPortal; CPX-5146; Ubiquitous AP-3 Adaptor complex, sigma3b variant.
DR ComplexPortal; CPX-5148; Neuronal AP-3 Adaptor complex, sigma3b variant.
DR CORUM; Q8BSZ2; -.
DR IntAct; Q8BSZ2; 1.
DR MINT; Q8BSZ2; -.
DR STRING; 10090.ENSMUSP00000075082; -.
DR iPTMnet; Q8BSZ2; -.
DR PhosphoSitePlus; Q8BSZ2; -.
DR EPD; Q8BSZ2; -.
DR MaxQB; Q8BSZ2; -.
DR PaxDb; Q8BSZ2; -.
DR PRIDE; Q8BSZ2; -.
DR ProteomicsDB; 281896; -.
DR Antibodypedia; 34959; 93 antibodies from 23 providers.
DR DNASU; 11778; -.
DR Ensembl; ENSMUST00000075657; ENSMUSP00000075082; ENSMUSG00000063801.
DR GeneID; 11778; -.
DR KEGG; mmu:11778; -.
DR UCSC; uc009hzf.2; mouse.
DR CTD; 10239; -.
DR MGI; MGI:1337060; Ap3s2.
DR VEuPathDB; HostDB:ENSMUSG00000063801; -.
DR eggNOG; KOG0936; Eukaryota.
DR GeneTree; ENSGT00970000193421; -.
DR HOGENOM; CLU_061221_2_2_1; -.
DR InParanoid; Q8BSZ2; -.
DR OMA; DLIFNWQ; -.
DR OrthoDB; 1458249at2759; -.
DR PhylomeDB; Q8BSZ2; -.
DR TreeFam; TF300189; -.
DR BioGRID-ORCS; 11778; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ap3s2; mouse.
DR PRO; PR:Q8BSZ2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BSZ2; protein.
DR Bgee; ENSMUSG00000063801; Expressed in cortical plate and 260 other tissues.
DR ExpressionAtlas; Q8BSZ2; baseline and differential.
DR Genevisible; Q8BSZ2; MM.
DR GO; GO:0030123; C:AP-3 adaptor complex; ISO:MGI.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:0006896; P:Golgi to vacuole transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:0046907; P:intracellular transport; IC:ComplexPortal.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0060155; P:platelet dense granule organization; 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 CDD; cd14834; AP3_sigma; 1.
DR InterPro; IPR016635; AP_complex_ssu.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR027155; APS3.
DR InterPro; IPR000804; Clathrin_sm-chain_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR PANTHER; PTHR11753; PTHR11753; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..193
FT /note="AP-3 complex subunit sigma-2"
FT /id="PRO_0000193818"
FT CONFLICT 131
FT /note="E -> A (in Ref. 2; BAC29788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 22017 MW; D219EF4A989316EA CRC64;
MIQAILVFNN HGKPRLVRFY QRFPEEIQQQ IVRETFHLVL KRDDNICNFL EGGSLIGGSD
YKLIYRHYAT LYFVFCVDSS ESELGILDLI QVFVETLDKC FENVCELDLI FHMDKVHYIL
QEVVMGGMVL ETNMNEIVAQ IEAQNRLEKS EGGLSAAPAR AVSAVKNINL PEIPRNINIG
DLNIKVPNLS QFV
