ID AP3S2_HUMAN Reviewed; 193 AA. AC P59780; B2R677; B4DGQ3; O09077; O09149; Q53H83; Q99589; DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2003, sequence version 1. DT 24-JAN-2024, entry version 156. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=9118953; DOI=10.1093/emboj/16.5.917; RA Dell'Angelica E.C., Ohno H., Ooi C.E., Rabinovich E., Roche K.W., RA Bonifacino J.S.; RT "AP-3: an adaptor-like protein complex with ubiquitous expression."; RL EMBO J. 16:917-928(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, and Skin; 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). 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 -!- 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). Interacts with CC AGAP1. AP-3 associates with the BLOC-1 complex (By similarity). CC {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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P59780-1; Sequence=Displayed; CC Name=C15orf38-AP3S2; CC IsoId=Q7Z6K5-2; Sequence=External; CC Name=3; CC IsoId=P59780-2; Sequence=VSP_053673, VSP_053674; CC -!- TISSUE SPECIFICITY: Present in all adult tissues examined. CC {ECO:0000269|PubMed:9118953}. 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; X99459; CAA67824.1; -; mRNA. DR EMBL; AK294712; BAG57864.1; -; mRNA. DR EMBL; AK312467; BAG35374.1; -; mRNA. DR EMBL; AK222698; BAD96418.1; -; mRNA. DR EMBL; AC018988; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027176; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471101; EAX02074.1; -; Genomic_DNA. DR EMBL; BC002785; AAH02785.1; -; mRNA. DR EMBL; BC010020; AAH10020.1; -; mRNA. DR CCDS; CCDS10357.1; -. [P59780-1] DR RefSeq; NP_005820.1; NM_005829.4. [P59780-1] DR AlphaFoldDB; P59780; -. DR SMR; P59780; -. DR BioGRID; 115533; 25. DR ComplexPortal; CPX-5052; Ubiquitous AP-3 Adaptor complex, sigma3b variant. DR ComplexPortal; CPX-5053; Neuronal AP-3 Adaptor complex, sigma3b variant. DR CORUM; P59780; -. DR IntAct; P59780; 6. DR STRING; 9606.ENSP00000338777; -. DR iPTMnet; P59780; -. DR PhosphoSitePlus; P59780; -. DR BioMuta; AP3S2; -. DR DMDM; 33112220; -. DR EPD; P59780; -. DR jPOST; P59780; -. DR MassIVE; P59780; -. DR MaxQB; P59780; -. DR PaxDb; 9606-ENSP00000338777; -. DR PeptideAtlas; P59780; -. DR Pumba; P59780; -. DR Antibodypedia; 34959; 103 antibodies from 25 providers. DR DNASU; 10239; -. DR Ensembl; ENST00000336418.9; ENSP00000338777.4; ENSG00000157823.17. [P59780-1] DR Ensembl; ENST00000423566.6; ENSP00000394170.2; ENSG00000157823.17. [P59780-2] DR Ensembl; ENST00000560251.1; ENSP00000453288.1; ENSG00000157823.17. [P59780-2] DR GeneID; 10239; -. DR KEGG; hsa:10239; -. DR MANE-Select; ENST00000336418.9; ENSP00000338777.4; NM_005829.5; NP_005820.1. DR UCSC; uc002boq.5; human. [P59780-1] DR AGR; HGNC:571; -. DR CTD; 10239; -. DR DisGeNET; 10239; -. DR GeneCards; AP3S2; -. DR HGNC; HGNC:571; AP3S2. DR HPA; ENSG00000157823; Low tissue specificity. DR MIM; 602416; gene. DR neXtProt; NX_P59780; -. DR OpenTargets; ENSG00000157823; -. DR PharmGKB; PA24863; -. DR VEuPathDB; HostDB:ENSG00000157823; -. DR eggNOG; KOG0936; Eukaryota. DR GeneTree; ENSGT00970000193421; -. DR InParanoid; P59780; -. DR OrthoDB; 2908594at2759; -. DR PhylomeDB; P59780; -. DR TreeFam; TF300189; -. DR PathwayCommons; P59780; -. DR SignaLink; P59780; -. DR SIGNOR; P59780; -. DR BioGRID-ORCS; 10239; 20 hits in 1154 CRISPR screens. DR GeneWiki; AP3S2; -. DR GenomeRNAi; 10239; -. DR Pharos; P59780; Tdark. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; P59780; Protein. DR Bgee; ENSG00000157823; Expressed in rectum and 195 other cell types or tissues. DR ExpressionAtlas; P59780; baseline and differential. DR GO; GO:0030123; C:AP-3 adaptor complex; IDA:FlyBase. 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:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB. DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS: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; IEA:InterPro. 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:SF10; AP-3 COMPLEX SUBUNIT SIGMA-2; 1. DR Pfam; PF01217; Clat_adaptor_s; 1. DR SUPFAM; SSF64356; SNARE-like; 1. DR PROSITE; PS00989; CLAT_ADAPTOR_S; 1. DR Genevisible; P59780; HS. PE 2: Evidence at transcript level; KW Alternative splicing; Cytoplasmic vesicle; Golgi apparatus; Membrane; KW Protein transport; Reference proteome; Transport. FT CHAIN 1..193 FT /note="AP-3 complex subunit sigma-2" FT /id="PRO_0000193817" FT VAR_SEQ 92..124 FT /note="VFVETLDKCFENVCELDLIFHMDKVHYILQEVV -> LKKRERKKSQCNTLQ FT TGTLALWEQGPDIRTRRL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053673" FT VAR_SEQ 125..193 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053674" FT CONFLICT 84 FT /note="L -> I (in Ref. 2; BAG35374)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="G -> W (in Ref. 3; BAD96418)" 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 //