AP1M_DICDI
ID AP1M_DICDI Reviewed; 428 AA.
AC Q54HS9; Q9GPF2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=AP-1 complex subunit mu;
DE AltName: Full=AP-1 adaptor complex mu1 subunit;
DE AltName: Full=Adaptor protein complex AP-1 subunit mu;
DE AltName: Full=Adaptor-related protein complex 1 subunit mu;
DE AltName: Full=Clathrin-adaptor medium chain Apm1;
DE AltName: Full=Mu1-adaptin;
GN Name=apm1; ORFNames=DDB_G0289247;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=AX4;
RX PubMed=11179674; DOI=10.1016/s0378-1119(00)00545-x;
RA de Chassey B., Dubois A., Lefkir Y., Letourneur F.;
RT "Identification of clathrin-adaptor medium chains in Dictyostelium
RT discoideum: differential expression during development.";
RL Gene 262:115-122(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 2-12; 20-32; 61-85; 129-140 AND 213-226, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
RN [4]
RP FUNCTION.
RX PubMed=12802059; DOI=10.1091/mbc.e02-10-0627;
RA Lefkir Y., de Chassey B., Dubois A., Bogdanovic A., Brady R.J.,
RA Destaing O., Bruckert F., O'Halloran T.J., Cosson P., Letourneur F.;
RT "The AP-1 clathrin-adaptor is required for lysosomal enzymes sorting and
RT biogenesis of the contractile vacuole complex in Dictyostelium cells.";
RL Mol. Biol. Cell 14:1835-1851(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14617812; DOI=10.1091/mbc.e03-06-0365;
RA Lefkir Y., Malbouyres M., Gotthardt D., Ozinsky A., Cornillon S.,
RA Bruckert F., Aderem A.A., Soldati T., Cosson P., Letourneur F.;
RT "Involvement of the AP-1 adaptor complex in early steps of phagocytosis and
RT macropinocytosis.";
RL Mol. Biol. Cell 15:861-869(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16782229; DOI=10.1016/j.ejcb.2006.05.008;
RA Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R.;
RT "Identification and isolation of Dictyostelium microtubule-associated
RT protein interactors by tandem affinity purification.";
RL Eur. J. Cell Biol. 85:1079-1090(2006).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the trans-Golgi network (TGN) and
CC endosomes. The AP complexes mediate the recruitment of clathrin to
CC membranes and the recognition of sorting signals within the cytosolic
CC tails of transmembrane cargo molecules. Also involved in early steps of
CC phagocytosis and macropinocytosis. {ECO:0000269|PubMed:12802059,
CC ECO:0000269|PubMed:14617812}.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit and beta-type subunit), a
CC medium adaptin (mu-type subunit) and a small adaptin (sigma-type
CC subunit). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Cytoplasmic
CC vesicle, clathrin-coated vesicle membrane {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Constant expression throughout development.
CC {ECO:0000269|PubMed:11179674}.
CC -!- DISRUPTION PHENOTYPE: Cells are viable but display a severe growth
CC defect and a delayed developmental cycle. In this mutant, phagocytosis
CC drops by 60%, the protein transport between the TGN and lysosomes is
CC probably defective and the contractile vacuole is lost.
CC {ECO:0000269|PubMed:14617812}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; AY007278; AAG11391.1; -; mRNA.
DR EMBL; AAFI02000132; EAL62811.1; -; Genomic_DNA.
DR RefSeq; XP_636252.1; XM_631160.1.
DR AlphaFoldDB; Q54HS9; -.
DR SMR; Q54HS9; -.
DR STRING; 44689.DDB0191102; -.
DR PaxDb; Q54HS9; -.
DR EnsemblProtists; EAL62811; EAL62811; DDB_G0289247.
DR GeneID; 8627033; -.
DR KEGG; ddi:DDB_G0289247; -.
DR dictyBase; DDB_G0289247; apm1.
DR eggNOG; KOG0937; Eukaryota.
DR HOGENOM; CLU_026996_0_0_1; -.
DR InParanoid; Q54HS9; -.
DR OMA; CRAKAQI; -.
DR PhylomeDB; Q54HS9; -.
DR Reactome; R-DDI-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54HS9; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0030121; C:AP-1 adaptor complex; IDA:dictyBase.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IDA:dictyBase.
DR GO; GO:0007032; P:endosome organization; IMP:dictyBase.
DR GO; GO:0006971; P:hypotonic response; IMP:dictyBase.
DR GO; GO:0006886; P:intracellular protein transport; IMP:dictyBase.
DR GO; GO:0007041; P:lysosomal transport; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasmic vesicle; Direct protein sequencing;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..428
FT /note="AP-1 complex subunit mu"
FT /id="PRO_0000327979"
FT DOMAIN 169..426
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT MOD_RES 2
FT /note="N-acetylalanine; partial"
FT /evidence="ECO:0000269|Ref.3"
FT CONFLICT 32
FT /note="K -> R (in Ref. 1; AAG11391)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="T -> I (in Ref. 1; AAG11391)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="I -> L (in Ref. 1; AAG11391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 48565 MW; 01B67F142AC73B89 CRC64;
MAASAIFLMD SKGKVLISRN YRGDVPMSVA SKFISKILEE EDLNLKPIIQ EDGISYIYVK
HNNLFLLATT ERNANAATIL LFLYKMIEVF NEYFKELEEE SIRDNFVVIY ELMDEMMDFG
YPQSTEPKIL QEYITQEGYK LERGARGMVL PAAITGAVSW RKEGIKYNKN EVFLDVVESI
NLLVSANGTV LRSEIVGAVK MKSKLSGMPE LRLGLNDKIL FENSAKTGAP KGKGVELEDV
KFHQCVRLSK FENDRTISFI PPDGEFELMS YRLNTTVKPL IWVECISDTH AHSRVEYMVK
AKSQFKGKSI ANNVEIIVPV PPDADTPKFR CTVGTCKYAP EKDAIIWTIK QFPGGGREFL
MRAHFGLPSI SDEKPATKPP IMVKFEIPYY TVSGIQVRYL KIIEKSGYQA LPWVRYVCLS
GDYQFRTS
