AP3S2_HUMAN
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 03-AUG-2022, entry version 149.
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}.
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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; 22.
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; P59780; -.
DR PeptideAtlas; P59780; -.
DR PRIDE; P59780; -.
DR Antibodypedia; 34959; 93 antibodies from 23 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 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 PhylomeDB; P59780; -.
DR TreeFam; TF300189; -.
DR PathwayCommons; P59780; -.
DR SignaLink; P59780; -.
DR SIGNOR; P59780; -.
DR BioGRID-ORCS; 10239; 19 hits in 1077 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 193 other tissues.
DR ExpressionAtlas; P59780; baseline and differential.
DR Genevisible; P59780; HS.
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; IC: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; IC: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; 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 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
