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Protein

AP-3 complex subunit sigma-1

Gene

Ap3s1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • anterograde axon cargo transport Source: UniProtKB
  • anterograde synaptic vesicle transport Source: UniProtKB
  • intracellular protein transport Source: MGI
  • vesicle-mediated transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_342454. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-3 complex subunit sigma-1
Alternative name(s):
AP-3 complex subunit sigma-3A
Adaptor-related protein complex 3 subunit sigma-1
Sigma-3A-adaptin
Short name:
Sigma3A-adaptin
Sigma-adaptin 3a
Gene namesi
Name:Ap3s1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1337062. Ap3s1.

Subcellular locationi

GO - Cellular componenti

  • AP-3 adaptor complex Source: MGI
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • membrane Source: CACAO
  • trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193193AP-3 complex subunit sigma-1PRO_0000193816Add
BLAST

Proteomic databases

MaxQBiQ9DCR2.
PaxDbiQ9DCR2.
PRIDEiQ9DCR2.

PTM databases

PhosphoSiteiQ9DCR2.

Expressioni

Gene expression databases

BgeeiQ9DCR2.
ExpressionAtlasiQ9DCR2. baseline and differential.
GenevisibleiQ9DCR2. MM.

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

BioGridi198135. 1 interaction.
IntActiQ9DCR2. 1 interaction.
STRINGi10090.ENSMUSP00000025357.

Structurei

3D structure databases

ProteinModelPortaliQ9DCR2.
SMRiQ9DCR2. Positions 1-148.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5030.
GeneTreeiENSGT00550000074761.
HOGENOMiHOG000185228.
HOVERGENiHBG050517.
InParanoidiQ9DCR2.
KOiK12399.
OMAiLSEMIIG.
OrthoDBiEOG7W41CZ.
PhylomeDBiQ9DCR2.
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]
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DCR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKAILIFNN HGKPRLSKFY QPYSEDTQQQ IIRETFHLVS KRDENVCNFL
60 70 80 90 100
EGGLLIGGSD NKLIYRHYAT LYFVFCVDSS ESELGILDLI QVFVETLDKC
110 120 130 140 150
FENVCELDLI FHVDKVHNIL AEMVMGGMVL ETNMNEIVTQ IDAQNKLEKS
160 170 180 190
EAGLAGAPAR AVSAVKNMNL PEIPRNINIG DISIKVPNLP SFK
Length:193
Mass (Da):21,732
Last modified:July 19, 2003 - v2
Checksum:i1EF17F375881288D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301Q → P in BAB22191 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084575 mRNA. Translation: AAC72819.1.
AK002565 mRNA. Translation: BAB22191.1.
BC012656 mRNA. Translation: AAH12656.1.
CCDSiCCDS29236.1.
RefSeqiNP_033811.1. NM_009681.5.
UniGeneiMm.312536.

Genome annotation databases

EnsembliENSMUST00000025357; ENSMUSP00000025357; ENSMUSG00000024480.
GeneIDi11777.
KEGGimmu:11777.
UCSCiuc008evv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084575 mRNA. Translation: AAC72819.1.
AK002565 mRNA. Translation: BAB22191.1.
BC012656 mRNA. Translation: AAH12656.1.
CCDSiCCDS29236.1.
RefSeqiNP_033811.1. NM_009681.5.
UniGeneiMm.312536.

3D structure databases

ProteinModelPortaliQ9DCR2.
SMRiQ9DCR2. Positions 1-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198135. 1 interaction.
IntActiQ9DCR2. 1 interaction.
STRINGi10090.ENSMUSP00000025357.

PTM databases

PhosphoSiteiQ9DCR2.

Proteomic databases

MaxQBiQ9DCR2.
PaxDbiQ9DCR2.
PRIDEiQ9DCR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025357; ENSMUSP00000025357; ENSMUSG00000024480.
GeneIDi11777.
KEGGimmu:11777.
UCSCiuc008evv.1. mouse.

Organism-specific databases

CTDi1176.
MGIiMGI:1337062. Ap3s1.

Phylogenomic databases

eggNOGiCOG5030.
GeneTreeiENSGT00550000074761.
HOGENOMiHOG000185228.
HOVERGENiHBG050517.
InParanoidiQ9DCR2.
KOiK12399.
OMAiLSEMIIG.
OrthoDBiEOG7W41CZ.
PhylomeDBiQ9DCR2.
TreeFamiTF300189.

Enzyme and pathway databases

ReactomeiREACT_342454. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSiAp3s1. mouse.
NextBioi279575.
PROiQ9DCR2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCR2.
ExpressionAtlasiQ9DCR2. baseline and differential.
GenevisibleiQ9DCR2. MM.

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]
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Interaction of insulin receptor substrate-1 with the sigma3A subunit of the adaptor protein complex-3 in cultured adipocytes."
    VanRenterghem B., Morin M., Czech M.P., Heller-Harrison R.A.
    J. Biol. Chem. 273:29942-29949(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Adipocyte.
  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: Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Salivary gland.
  4. "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.
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. "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 nameiAP3S1_MOUSE
AccessioniPrimary (citable) accession number: Q9DCR2
Secondary accession number(s): O88670
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: July 19, 2003
Last modified: June 24, 2015
This is version 109 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.