AP4M_DICDI
ID AP4M_DICDI Reviewed; 530 AA.
AC Q9GPF0; Q550G8; Q86AZ5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=AP-4 complex subunit mu {ECO:0000305};
DE AltName: Full=AP-4 adaptor complex mu4 subunit;
DE AltName: Full=Adaptor-related protein complex 4 subunit mu;
DE AltName: Full=Clathrin-adaptor medium chain Apm4;
DE AltName: Full=Mu4-adaptin;
GN Name=apm4 {ECO:0000312|dictyBase:DDB_G0276945};
GN ORFNames=DDB_G0276945 {ECO:0000312|dictyBase:DDB_G0276945};
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.
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
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).
CC -!- FUNCTION: Probable component of an adaptor protein complex. 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.
CC {ECO:0000250|UniProtKB:O00189}.
CC -!- SUBUNIT: May be part of the adaptor protein complex 4 (AP-4), a
CC heterotetramer composed of two large adaptins (epsilon-type subunitand
CC beta-type subunit), a medium adaptin (mu-type subunit) and a small
CC adaptin (sigma-type). {ECO:0000250|UniProtKB:O00189}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:O00189}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O00189}. Early endosome
CC {ECO:0000250|UniProtKB:O00189}.
CC -!- DEVELOPMENTAL STAGE: Poorly expressed in vegetative cells. Well
CC detected in migrating slugs and highly induced at the finger stage,
CC reaching a peak level at 16 hours of development, and then decreasing
CC to a very low level at 20 hours. {ECO:0000269|PubMed:11179674}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; AY007280; AAG11393.1; -; mRNA.
DR EMBL; AAFI02000019; EAL68974.1; -; Genomic_DNA.
DR RefSeq; XP_642964.1; XM_637872.1.
DR AlphaFoldDB; Q9GPF0; -.
DR SMR; Q9GPF0; -.
DR STRING; 44689.DDB0219948; -.
DR PaxDb; Q9GPF0; -.
DR EnsemblProtists; EAL68974; EAL68974; DDB_G0276945.
DR GeneID; 8620834; -.
DR KEGG; ddi:DDB_G0276945; -.
DR dictyBase; DDB_G0276945; apm4.
DR eggNOG; KOG0937; Eukaryota.
DR HOGENOM; CLU_026996_5_0_1; -.
DR InParanoid; Q9GPF0; -.
DR OMA; NVCATIP; -.
DR PhylomeDB; Q9GPF0; -.
DR Reactome; R-DDI-432720; Lysosome Vesicle Biogenesis.
DR PRO; PR:Q9GPF0; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0030124; C:AP-4 adaptor complex; ISS:dictyBase.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0090160; P:Golgi to lysosome transport; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS51072; MHD; 1.
PE 2: Evidence at transcript level;
KW Endosome; Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..530
FT /note="AP-4 complex subunit mu"
FT /id="PRO_0000327981"
FT DOMAIN 227..527
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 164..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 58930 MW; 7EBA6BBF23D86FDC CRC64;
MFSQFFILNN KGETIIFKDY RFDISKDSNE IFFKHVQSMK SEITPAFNID GINYLYIKKR
EMYFVFTTRL LVSPSLGFEL LNRASKIIQD YTASLTEEAI RLNFILIYEL LDELMDYGVP
QSTGTETLKA FVFTPPKQIK SKQLESDSII DNFLKATNKI SVPPKQGVKP IHSGSKNSSS
GGSSLSTNTV SKVVNNIVDS ISGAATNLHN STSGGGSGSG VTDADGDNEI YIDLCERLTV
LYSSNGTILR NEITGKIQMK SYLRGNPALS LGLSPEFTFK TIANRDESNE NEIDNNNIGG
VSNLSAPSSN TTSFIVDDCS FHECAGSGFQ PNNTINFKPP QGDFTLLKYR ISNNNYTPFL
VKTNLESTIR NRFDLVVTIR SNFSNKVVPN FIFVSIPVPK STKSLTHSLD YGSQNQKVEY
KQSTQAGNLV FWSIKKLRGG METILRIQIH VDGATSSSSN NNQQQQQPQI DVGSTLRKEI
GPIGLEFSIP QFSCSTLQIK FLKMLGSNIS PIRWIRYITD SKSFVSRINN
