AP1S1_MOUSE
ID AP1S1_MOUSE Reviewed; 158 AA.
AC P61967; P82267; Q00382; Q9BTN4; Q9UDW9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=AP-1 complex subunit sigma-1A;
DE AltName: Full=Adaptor protein complex AP-1 subunit sigma-1A;
DE AltName: Full=Adaptor-related protein complex 1 subunit sigma-1A;
DE AltName: Full=Clathrin assembly protein complex 1 sigma-1A small chain;
DE AltName: Full=Clathrin coat assembly protein AP19;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin sigma-1A subunit;
DE AltName: Full=HA1 19 kDa subunit;
DE AltName: Full=Sigma 1a subunit of AP-1 clathrin;
DE AltName: Full=Sigma-adaptin 1A;
DE AltName: Full=Sigma1A-adaptin;
GN Name=Ap1s1; Synonyms=Ap19;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2040623; DOI=10.1016/s0021-9258(18)99141-6;
RA Kirchhausen T., Davis A.C., Frucht S., O'Brine Greco B., Payne G.S.,
RA Tubb B.;
RT "AP17 and AP19, the mammalian small chains of the clathrin-associated
RT protein complexes show homology to Yap17p, their putative homolog in
RT yeast.";
RL J. Biol. Chem. 266:11153-11157(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the late-Golgi/trans-Golgi network
CC (TGN) and/or endosomes. The AP complexes mediate both the recruitment
CC of clathrin to membranes and the recognition of sorting signals within
CC the cytosolic tails of transmembrane cargo molecules.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit
CC AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small
CC adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-
CC coated pit. Note=Component of the coat surrounding the cytoplasmic face
CC of coated vesicles located at the Golgi complex.
CC -!- TISSUE SPECIFICITY: Detected in brain and embryonic stem cells.
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC {ECO:0000305}.
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DR EMBL; M62418; AAA37243.1; -; mRNA.
DR EMBL; AK002225; BAB21947.1; -; mRNA.
DR EMBL; BC052692; AAH52692.1; -; mRNA.
DR CCDS; CCDS39330.1; -.
DR PIR; A40535; A40535.
DR RefSeq; NP_031483.1; NM_007457.2.
DR PDB; 1W63; X-ray; 4.00 A; Q/S/T/U/W/X=1-158.
DR PDBsum; 1W63; -.
DR AlphaFoldDB; P61967; -.
DR SMR; P61967; -.
DR BioGRID; 198127; 6.
DR ComplexPortal; CPX-5141; Ubiquitous AP-1 Adaptor complex, sigma1a variant.
DR ComplexPortal; CPX-5144; Endothelial AP-1 Adaptor complex, sigma1a variant.
DR CORUM; P61967; -.
DR IntAct; P61967; 4.
DR STRING; 10090.ENSMUSP00000106709; -.
DR iPTMnet; P61967; -.
DR PhosphoSitePlus; P61967; -.
DR EPD; P61967; -.
DR jPOST; P61967; -.
DR MaxQB; P61967; -.
DR PaxDb; P61967; -.
DR PeptideAtlas; P61967; -.
DR PRIDE; P61967; -.
DR ProteomicsDB; 296325; -.
DR Antibodypedia; 30972; 134 antibodies from 20 providers.
DR DNASU; 11769; -.
DR Ensembl; ENSMUST00000111080; ENSMUSP00000106709; ENSMUSG00000004849.
DR GeneID; 11769; -.
DR KEGG; mmu:11769; -.
DR UCSC; uc009abm.1; mouse.
DR CTD; 1174; -.
DR MGI; MGI:1098244; Ap1s1.
DR VEuPathDB; HostDB:ENSMUSG00000004849; -.
DR eggNOG; KOG0934; Eukaryota.
DR GeneTree; ENSGT00970000193372; -.
DR InParanoid; P61967; -.
DR OMA; MIHFFIL; -.
DR OrthoDB; 1307450at2759; -.
DR PhylomeDB; P61967; -.
DR TreeFam; TF312921; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 11769; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Ap1s1; mouse.
DR EvolutionaryTrace; P61967; -.
DR PRO; PR:P61967; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P61967; protein.
DR Bgee; ENSMUSG00000004849; Expressed in dentate gyrus of hippocampal formation granule cell and 255 other tissues.
DR ExpressionAtlas; P61967; baseline and differential.
DR Genevisible; P61967; MM.
DR GO; GO:0030121; C:AP-1 adaptor complex; NAS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0043195; C:terminal bouton; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; NAS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IC:ComplexPortal.
DR GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR GO; GO:0110010; P:basolateral protein secretion; IC:ComplexPortal.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0060155; P:platelet dense granule organization; IC:ComplexPortal.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd14831; AP1_sigma; 1.
DR InterPro; IPR044733; AP1_sigma.
DR InterPro; IPR016635; AP_complex_ssu.
DR InterPro; IPR022775; AP_mu_sigma_su.
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 PIRSF; PIRSF015588; AP_complex_sigma; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coated pit; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..158
FT /note="AP-1 complex subunit sigma-1A"
FT /id="PRO_0000193798"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 158 AA; 18733 MW; E461937790406D8B CRC64;
MMRFMLLFSR QGKLRLQKWY LATSDKERKK MVRELMQVVL ARKPKMCSFL EWRDLKVVYK
RYASLYFCCA IEGQDNELIT LELIHRYVEL LDKYFGSVCE LDIIFNFEKA YFILDEFLMG
GDVQDTSKKS VLKAIEQADL LQEEDESPRS VLEEMGLA
