AP4S1_MOUSE
ID AP4S1_MOUSE Reviewed; 144 AA.
AC Q9WVL1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=AP-4 complex subunit sigma-1 {ECO:0000305};
DE AltName: Full=AP-4 adaptor complex subunit sigma-1;
DE AltName: Full=Adaptor-related protein complex 4 subunit sigma-1;
DE AltName: Full=Sigma-1 subunit of AP-4;
DE AltName: Full=Sigma-4-adaptin;
DE Short=Sigma4-adaptin;
GN Name=Ap4s1 {ECO:0000312|MGI:MGI:1337065};
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=Placenta;
RX PubMed=10066790; DOI=10.1074/jbc.274.11.7278;
RA Dell'Angelica E.C., Mullins C., Bonifacino J.S.;
RT "AP-4, a novel protein complex related to clathrin adaptors.";
RL J. Biol. Chem. 274:7278-7285(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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=FVB/N-3; TISSUE=Mammary gland;
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: Component of the adaptor protein complex 4 (AP-4). Adaptor
CC protein complexes are vesicle coat components involved both in vesicle
CC formation and cargo selection. They control the vesicular transport of
CC proteins in different trafficking pathways. AP-4 forms a non clathrin-
CC associated coat on vesicles departing the trans-Golgi network (TGN) and
CC may be involved in the targeting of proteins from the trans-Golgi
CC network (TGN) to the endosomal-lysosomal system. It is also involved in
CC protein sorting to the basolateral membrane in epithelial cells and the
CC proper asymmetric localization of somatodendritic proteins in neurons.
CC AP-4 is involved in the recognition and binding of tyrosine-based
CC sorting signals found in the cytoplasmic part of cargos, but may also
CC recognize other types of sorting signal.
CC {ECO:0000250|UniProtKB:Q9Y587}.
CC -!- SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer composed
CC of two large adaptins (epsilon-type subunit AP4E1 and beta-type subunit
CC AP4B1), a medium adaptin (mu-type subunit AP4M1) and a small adaptin
CC (sigma-type AP4S1). {ECO:0000250|UniProtKB:Q9Y587}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9Y587}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Y587}.
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC {ECO:0000305}.
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DR EMBL; AF092093; AAD20447.1; -; mRNA.
DR EMBL; AK005283; BAB23931.1; -; mRNA.
DR EMBL; BC053339; AAH53339.1; -; mRNA.
DR CCDS; CCDS36441.1; -.
DR RefSeq; NP_068356.1; NM_021710.4.
DR RefSeq; XP_017170429.1; XM_017314940.1.
DR RefSeq; XP_017170430.1; XM_017314941.1.
DR AlphaFoldDB; Q9WVL1; -.
DR SMR; Q9WVL1; -.
DR BioGRID; 198138; 1.
DR ComplexPortal; CPX-5154; AP-4 Adaptor complex.
DR STRING; 10090.ENSMUSP00000021338; -.
DR PhosphoSitePlus; Q9WVL1; -.
DR EPD; Q9WVL1; -.
DR MaxQB; Q9WVL1; -.
DR PaxDb; Q9WVL1; -.
DR PeptideAtlas; Q9WVL1; -.
DR PRIDE; Q9WVL1; -.
DR ProteomicsDB; 281788; -.
DR Antibodypedia; 51162; 31 antibodies from 11 providers.
DR DNASU; 11782; -.
DR Ensembl; ENSMUST00000021338; ENSMUSP00000021338; ENSMUSG00000020955.
DR GeneID; 11782; -.
DR KEGG; mmu:11782; -.
DR UCSC; uc007nmv.2; mouse.
DR CTD; 11154; -.
DR MGI; MGI:1337065; Ap4s1.
DR VEuPathDB; HostDB:ENSMUSG00000020955; -.
DR eggNOG; KOG0934; Eukaryota.
DR GeneTree; ENSGT00970000193421; -.
DR HOGENOM; CLU_061221_4_0_1; -.
DR InParanoid; Q9WVL1; -.
DR OMA; KDQCSFI; -.
DR OrthoDB; 1307450at2759; -.
DR PhylomeDB; Q9WVL1; -.
DR TreeFam; TF331913; -.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR BioGRID-ORCS; 11782; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ap4s1; mouse.
DR PRO; PR:Q9WVL1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9WVL1; protein.
DR Bgee; ENSMUSG00000020955; Expressed in intercostal muscle and 256 other tissues.
DR ExpressionAtlas; Q9WVL1; baseline and differential.
DR Genevisible; Q9WVL1; MM.
DR GO; GO:0030124; C:AP-4 adaptor complex; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR016635; AP_complex_ssu.
DR InterPro; IPR022775; AP_mu_sigma_su.
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.
PE 2: Evidence at transcript level;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..144
FT /note="AP-4 complex subunit sigma-1"
FT /id="PRO_0000193821"
SQ SEQUENCE 144 AA; 16818 MW; 8EC280834976B430 CRC64;
MIKFFLMVNK QGQTRLSKYY EHVDINKRAL LETEVSKSCL SRSSEQCSFI EYKDFKLIYR
QYAALFVVVG VNDTENEMAI YEFIHNFVEV LDGYFSRVSE LDIMFNLDKV HIILDEMVLN
GCIVETNRAR ILAPLLILDK LSES