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Q9DCR2 (AP3S1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AP-3 complex subunit sigma-1
Alternative name(s):
AP-3 complex subunit sigma-3A
Adapter-related protein complex 3 subunit sigma-1
Sigma-3A-adaptin
Short name=Sigma3A-adaptin
Sigma-adaptin 3a
Gene names
Name:Ap3s1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the AP-3 complex, an adapter-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. Ref.6

Subunit structure

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. Ref.4

Subcellular location

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

Sequence similarities

Belongs to the adaptor complexes small subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193AP-3 complex subunit sigma-1
PRO_0000193816

Experimental info

Sequence conflict301Q → P in BAB22191. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9DCR2 [UniParc].

Last modified July 19, 2003. Version 2.
Checksum: 1EF17F375881288D

FASTA19321,732
        10         20         30         40         50         60 
MIKAILIFNN HGKPRLSKFY QPYSEDTQQQ IIRETFHLVS KRDENVCNFL EGGLLIGGSD 

        70         80         90        100        110        120 
NKLIYRHYAT LYFVFCVDSS ESELGILDLI QVFVETLDKC FENVCELDLI FHVDKVHNIL 

       130        140        150        160        170        180 
AEMVMGGMVL ETNMNEIVTQ IDAQNKLEKS EAGLAGAPAR AVSAVKNMNL PEIPRNINIG 

       190 
DISIKVPNLP SFK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084575 mRNA. Translation: AAC72819.1.
AK002565 mRNA. Translation: BAB22191.1.
BC012656 mRNA. Translation: AAH12656.1.
CCDSCCDS29236.1.
RefSeqNP_033811.1. NM_009681.4.
UniGeneMm.312536.

3D structure databases

ProteinModelPortalQ9DCR2.
SMRQ9DCR2. Positions 1-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198135. 1 interaction.
STRING10090.ENSMUSP00000025357.

PTM databases

PhosphoSiteQ9DCR2.

Proteomic databases

MaxQBQ9DCR2.
PaxDbQ9DCR2.
PRIDEQ9DCR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025357; ENSMUSP00000025357; ENSMUSG00000024480.
GeneID11777.
KEGGmmu:11777.
UCSCuc008evv.1. mouse.

Organism-specific databases

CTD1176.
MGIMGI:1337062. Ap3s1.

Phylogenomic databases

eggNOGCOG5030.
GeneTreeENSGT00550000074761.
HOGENOMHOG000185228.
HOVERGENHBG050517.
InParanoidQ9DCR2.
KOK12399.
OMALSEMIIG.
OrthoDBEOG7W41CZ.
PhylomeDBQ9DCR2.
TreeFamTF300189.

Gene expression databases

BgeeQ9DCR2.
GenevestigatorQ9DCR2.

Family and domain databases

InterProIPR016635. AP_complex_ssu.
IPR022775. AP_mu_sigma_su.
IPR000804. Clathrin_sm-chain_CS.
IPR011012. Longin-like_dom.
[Graphical view]
PANTHERPTHR11753. PTHR11753. 1 hit.
PfamPF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFPIRSF015588. AP_complex_sigma. 1 hit.
SUPFAMSSF64356. SSF64356. 1 hit.
PROSITEPS00989. CLAT_ADAPTOR_S. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAP3S1. mouse.
NextBio279575.
PROQ9DCR2.
SOURCESearch...

Entry information

Entry nameAP3S1_MOUSE
AccessionPrimary (citable) accession number: Q9DCR2
Secondary accession number(s): O88670
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: July 19, 2003
Last modified: July 9, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot