ID   AP3S1_MOUSE             Reviewed;         193 AA.
AC   Q9DCR2; O88670;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=AP-3 complex subunit sigma-1;
DE   AltName: Full=AP-3 complex subunit sigma-3A;
DE   AltName: Full=Adaptor-related protein complex 3 subunit sigma-1;
DE   AltName: Full=Sigma-3A-adaptin;
DE            Short=Sigma3A-adaptin;
DE   AltName: Full=Sigma-adaptin 3a;
GN   Name=Ap3s1;
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=Adipocyte;
RX   PubMed=9792713; DOI=10.1074/jbc.273.45.29942;
RA   VanRenterghem B., Morin M., Czech M.P., Heller-Harrison R.A.;
RT   "Interaction of insulin receptor substrate-1 with the sigma3A subunit of
RT   the adaptor protein complex-3 in cultured adipocytes.";
RL   J. Biol. Chem. 273:29942-29949(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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   TISSUE=Salivary gland;
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   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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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: 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   -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF084575; AAC72819.1; -; mRNA.
DR   EMBL; AK002565; BAB22191.1; -; mRNA.
DR   EMBL; BC012656; AAH12656.1; -; mRNA.
DR   CCDS; CCDS29236.1; -.
DR   RefSeq; NP_033811.1; NM_009681.5.
DR   AlphaFoldDB; Q9DCR2; -.
DR   SMR; Q9DCR2; -.
DR   BioGRID; 198135; 21.
DR   ComplexPortal; CPX-5145; Ubiquitous AP-3 Adaptor complex, sigma3a variant.
DR   ComplexPortal; CPX-5147; Neuronal AP-3 Adaptor complex, sigma3a variant.
DR   IntAct; Q9DCR2; 5.
DR   MINT; Q9DCR2; -.
DR   STRING; 10090.ENSMUSP00000025357; -.
DR   iPTMnet; Q9DCR2; -.
DR   PhosphoSitePlus; Q9DCR2; -.
DR   EPD; Q9DCR2; -.
DR   MaxQB; Q9DCR2; -.
DR   PaxDb; 10090-ENSMUSP00000025357; -.
DR   ProteomicsDB; 296359; -.
DR   Pumba; Q9DCR2; -.
DR   Antibodypedia; 25448; 134 antibodies from 22 providers.
DR   DNASU; 11777; -.
DR   Ensembl; ENSMUST00000025357.9; ENSMUSP00000025357.8; ENSMUSG00000024480.10.
DR   GeneID; 11777; -.
DR   KEGG; mmu:11777; -.
DR   UCSC; uc008evv.2; mouse.
DR   AGR; MGI:1337062; -.
DR   CTD; 1176; -.
DR   MGI; MGI:1337062; Ap3s1.
DR   VEuPathDB; HostDB:ENSMUSG00000024480; -.
DR   eggNOG; KOG0936; Eukaryota.
DR   GeneTree; ENSGT00970000193421; -.
DR   HOGENOM; CLU_061221_2_2_1; -.
DR   InParanoid; Q9DCR2; -.
DR   OMA; VYKTFAT; -.
DR   OrthoDB; 3059064at2759; -.
DR   PhylomeDB; Q9DCR2; -.
DR   TreeFam; TF300189; -.
DR   Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR   BioGRID-ORCS; 11777; 5 hits in 80 CRISPR screens.
DR   ChiTaRS; Ap3s1; mouse.
DR   PRO; PR:Q9DCR2; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q9DCR2; Protein.
DR   Bgee; ENSMUSG00000024480; Expressed in ganglionic eminence and 70 other cell types or tissues.
DR   ExpressionAtlas; Q9DCR2; baseline and differential.
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; NAS:ComplexPortal.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IMP:CACAO.
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; NAS: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; NAS:ComplexPortal.
DR   GO; GO:1903232; P:melanosome assembly; NAS:ComplexPortal.
DR   GO; GO:0060155; P:platelet dense granule organization; NAS:ComplexPortal.
DR   GO; GO:0016183; P:synaptic vesicle coating; NAS:ComplexPortal.
DR   GO; GO:0036465; P:synaptic vesicle recycling; NAS:ComplexPortal.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd14834; AP3_sigma; 1.
DR   Gene3D; 3.30.450.60; -; 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; ADAPTOR COMPLEXES SMALL SUBUNIT FAMILY; 1.
DR   PANTHER; PTHR11753:SF12; AP-3 COMPLEX SUBUNIT SIGMA-1; 1.
DR   Pfam; PF01217; Clat_adaptor_s; 1.
DR   SUPFAM; SSF64356; SNARE-like; 1.
DR   PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
DR   Genevisible; Q9DCR2; MM.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..193
FT                   /note="AP-3 complex subunit sigma-1"
FT                   /id="PRO_0000193816"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92572"
FT   CONFLICT        30
FT                   /note="Q -> P (in Ref. 2; BAB22191)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   193 AA;  21732 MW;  1EF17F375881288D CRC64;
     MIKAILIFNN HGKPRLSKFY QPYSEDTQQQ IIRETFHLVS KRDENVCNFL EGGLLIGGSD
     NKLIYRHYAT LYFVFCVDSS ESELGILDLI QVFVETLDKC FENVCELDLI FHVDKVHNIL
     AEMVMGGMVL ETNMNEIVTQ IDAQNKLEKS EAGLAGAPAR AVSAVKNMNL PEIPRNINIG
     DISIKVPNLP SFK
//