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Q8BSZ2

- AP3S2_MOUSE

UniProt

Q8BSZ2 - AP3S2_MOUSE

Protein

AP-3 complex subunit sigma-2

Gene

Ap3s2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.1 Publication

    GO - Molecular functioni

    1. protein transporter activity Source: InterPro

    GO - Biological processi

    1. anterograde axon cargo transport Source: UniProtKB
    2. anterograde synaptic vesicle transport Source: UniProtKB
    3. intracellular protein transport Source: MGI
    4. vesicle-mediated transport Source: MGI

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AP-3 complex subunit sigma-2
    Alternative name(s):
    AP-3 complex subunit sigma-3B
    Adaptor-related protein complex 3 subunit sigma-2
    Sigma-3B-adaptin
    Short name:
    Sigma3B-adaptin
    Sigma-adaptin 3b
    Gene namesi
    Name:Ap3s2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1337060. Ap3s2.

    Subcellular locationi

    Golgi apparatus. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.By similarity

    GO - Cellular componenti

    1. AP-3 adaptor complex Source: Ensembl
    2. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    3. trans-Golgi network Source: MGI

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 193193AP-3 complex subunit sigma-2PRO_0000193818Add
    BLAST

    Proteomic databases

    MaxQBiQ8BSZ2.
    PaxDbiQ8BSZ2.
    PRIDEiQ8BSZ2.

    PTM databases

    PhosphoSiteiQ8BSZ2.

    Expressioni

    Tissue specificityi

    Present in all adult tissues examined.

    Gene expression databases

    ArrayExpressiQ8BSZ2.
    BgeeiQ8BSZ2.
    GenevestigatoriQ8BSZ2.

    Interactioni

    Subunit structurei

    Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2) By similarity. AP-3 associates with the BLOC-1 complex. Interacts with AGAP1.By similarity1 Publication

    Protein-protein interaction databases

    IntActiQ8BSZ2. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BSZ2.
    SMRiQ8BSZ2. Positions 1-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5030.
    GeneTreeiENSGT00550000074761.
    HOVERGENiHBG050517.
    InParanoidiQ8BSZ2.
    KOiK12399.
    OMAiNRMEKSE.
    OrthoDBiEOG7W41CZ.
    PhylomeDBiQ8BSZ2.
    TreeFamiTF300189.

    Family and domain databases

    InterProiIPR016635. AP_complex_ssu.
    IPR022775. AP_mu_sigma_su.
    IPR000804. Clathrin_sm-chain_CS.
    IPR011012. Longin-like_dom.
    [Graphical view]
    PANTHERiPTHR11753. PTHR11753. 1 hit.
    PfamiPF01217. Clat_adaptor_s. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015588. AP_complex_sigma. 1 hit.
    SUPFAMiSSF64356. SSF64356. 1 hit.
    PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BSZ2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIQAILVFNN HGKPRLVRFY QRFPEEIQQQ IVRETFHLVL KRDDNICNFL    50
    EGGSLIGGSD YKLIYRHYAT LYFVFCVDSS ESELGILDLI QVFVETLDKC 100
    FENVCELDLI FHMDKVHYIL QEVVMGGMVL ETNMNEIVAQ IEAQNRLEKS 150
    EGGLSAAPAR AVSAVKNINL PEIPRNINIG DLNIKVPNLS QFV 193
    Length:193
    Mass (Da):22,017
    Last modified:March 1, 2003 - v1
    Checksum:iD219EF4A989316EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311E → A in BAC29788. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U91933 mRNA. Translation: AAD03780.1.
    AK028372 mRNA. Translation: BAC25912.1.
    AK037336 mRNA. Translation: BAC29788.1.
    AK150085 mRNA. Translation: BAE29294.1.
    CCDSiCCDS21389.1.
    RefSeqiNP_033812.3. NM_009682.3.
    UniGeneiMm.220173.

    Genome annotation databases

    EnsembliENSMUST00000075657; ENSMUSP00000075082; ENSMUSG00000063801.
    GeneIDi11778.
    KEGGimmu:11778.
    UCSCiuc009hzf.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U91933 mRNA. Translation: AAD03780.1 .
    AK028372 mRNA. Translation: BAC25912.1 .
    AK037336 mRNA. Translation: BAC29788.1 .
    AK150085 mRNA. Translation: BAE29294.1 .
    CCDSi CCDS21389.1.
    RefSeqi NP_033812.3. NM_009682.3.
    UniGenei Mm.220173.

    3D structure databases

    ProteinModelPortali Q8BSZ2.
    SMRi Q8BSZ2. Positions 1-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BSZ2. 1 interaction.

    PTM databases

    PhosphoSitei Q8BSZ2.

    Proteomic databases

    MaxQBi Q8BSZ2.
    PaxDbi Q8BSZ2.
    PRIDEi Q8BSZ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000075657 ; ENSMUSP00000075082 ; ENSMUSG00000063801 .
    GeneIDi 11778.
    KEGGi mmu:11778.
    UCSCi uc009hzf.2. mouse.

    Organism-specific databases

    CTDi 10239.
    MGIi MGI:1337060. Ap3s2.

    Phylogenomic databases

    eggNOGi COG5030.
    GeneTreei ENSGT00550000074761.
    HOVERGENi HBG050517.
    InParanoidi Q8BSZ2.
    KOi K12399.
    OMAi NRMEKSE.
    OrthoDBi EOG7W41CZ.
    PhylomeDBi Q8BSZ2.
    TreeFami TF300189.

    Miscellaneous databases

    ChiTaRSi AP3S2. mouse.
    NextBioi 279579.
    PROi Q8BSZ2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BSZ2.
    Bgeei Q8BSZ2.
    Genevestigatori Q8BSZ2.

    Family and domain databases

    InterProi IPR016635. AP_complex_ssu.
    IPR022775. AP_mu_sigma_su.
    IPR000804. Clathrin_sm-chain_CS.
    IPR011012. Longin-like_dom.
    [Graphical view ]
    PANTHERi PTHR11753. PTHR11753. 1 hit.
    Pfami PF01217. Clat_adaptor_s. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015588. AP_complex_sigma. 1 hit.
    SUPFAMi SSF64356. SSF64356. 1 hit.
    PROSITEi PS00989. CLAT_ADAPTOR_S. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the adaptor-related protein complex, AP-3."
      Simpson F., Peden A.A., Christopoulou L., Robinson M.S.
      J. Cell Biol. 137:835-845(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow, Placenta and Thymus.
    3. "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1."
      Nie Z., Boehm M., Boja E.S., Vass W.C., Bonifacino J.S., Fales H.M., Randazzo P.A.
      Dev. Cell 5:513-521(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGAP1.
    4. "The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse."
      Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.
      Mol. Biol. Cell 22:4854-4867(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH THE BLOC-1 COMPLEX.

    Entry informationi

    Entry nameiAP3S2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BSZ2
    Secondary accession number(s): O09077
    , O09149, Q3UDG7, Q8CAY1, Q99589
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3