AP3M1_HUMAN
ID AP3M1_HUMAN Reviewed; 418 AA.
AC Q9Y2T2; Q5JQ12; Q9H5L2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=AP-3 complex subunit mu-1;
DE AltName: Full=AP-3 adaptor complex mu3A subunit;
DE AltName: Full=Adaptor-related protein complex 3 subunit mu-1;
DE AltName: Full=Mu-adaptin 3A;
DE AltName: Full=Mu3A-adaptin;
GN Name=AP3M1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood, and Skin fibroblast;
RX PubMed=10024875; DOI=10.1016/s1097-2765(00)80170-7;
RA Dell'Angelica E.C., Shotelersuk V., Aguilar R.C., Gahl W.A.,
RA Bonifacino J.S.;
RT "Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due
RT to mutations in the beta 3A subunit of the AP-3 adaptor.";
RL Mol. Cell 3:11-21(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Prostate;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP INTERACTION WITH HRSV MATRIX PROTEIN (MICROBIAL INFECTION).
RX PubMed=29028839; DOI=10.1371/journal.pone.0184629;
RA Ward C., Maselko M., Lupfer C., Prescott M., Pastey M.K.;
RT "Interaction of the Human Respiratory Syncytial Virus matrix protein with
RT cellular adaptor protein complex 3 plays a critical role in trafficking.";
RL PLoS ONE 12:E0184629-E0184629(2017).
CC -!- FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is
CC not clathrin-associated. The complex is associated with the Golgi
CC region as well as more peripheral structures. It facilitates the
CC budding of vesicles from the Golgi membrane and may be directly
CC involved in trafficking to lysosomes. In concert with the BLOC-1
CC complex, AP-3 is required to target cargos into vesicles assembled at
CC cell bodies for delivery into neurites and nerve terminals.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC of two large adaptins (delta-type subunit AP3D1 and beta-type subunit
CC AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and
CC a small adaptin (sigma-type subunit APS1 or AP3S2). Interacts with
CC AGAP1. AP-3 associates with the BLOC-1 complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human respiratory virus
CC (HRSV) matrix protein; this interaction plays an essential role in
CC trafficking the matrix protein in host cells.
CC {ECO:0000269|PubMed:29028839}.
CC -!- INTERACTION:
CC Q9Y2T2; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-2371151, EBI-741181;
CC Q9Y2T2; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-2371151, EBI-11522760;
CC Q9Y2T2; A0A087WVE9: ARNT2; NbExp=3; IntAct=EBI-2371151, EBI-12808086;
CC Q9Y2T2; Q14194: CRMP1; NbExp=6; IntAct=EBI-2371151, EBI-473101;
CC Q9Y2T2; Q92997: DVL3; NbExp=3; IntAct=EBI-2371151, EBI-739789;
CC Q9Y2T2; Q96NE9-2: FRMD6; NbExp=3; IntAct=EBI-2371151, EBI-13213391;
CC Q9Y2T2; P42858: HTT; NbExp=3; IntAct=EBI-2371151, EBI-466029;
CC Q9Y2T2; Q9UBH0: IL36RN; NbExp=3; IntAct=EBI-2371151, EBI-465156;
CC Q9Y2T2; Q9UHP6: RSPH14; NbExp=11; IntAct=EBI-2371151, EBI-748350;
CC Q9Y2T2; Q9P2F8-2: SIPA1L2; NbExp=6; IntAct=EBI-2371151, EBI-10326741;
CC Q9Y2T2; Q9UP95: SLC12A4; NbExp=3; IntAct=EBI-2371151, EBI-7244836;
CC Q9Y2T2; Q8N0X2-4: SPAG16; NbExp=3; IntAct=EBI-2371151, EBI-11946259;
CC Q9Y2T2; P36406: TRIM23; NbExp=3; IntAct=EBI-2371151, EBI-740098;
CC Q9Y2T2; Q9C026: TRIM9; NbExp=3; IntAct=EBI-2371151, EBI-720828;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Component of the coat surrounding the
CC cytoplasmic face of coated vesicles located at the Golgi complex.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF092092; AAD20446.1; -; mRNA.
DR EMBL; AK026983; BAB15614.1; -; mRNA.
DR EMBL; AL731576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026232; AAH26232.1; -; mRNA.
DR EMBL; BC067127; AAH67127.1; -; mRNA.
DR CCDS; CCDS7342.1; -.
DR RefSeq; NP_001307192.1; NM_001320263.1.
DR RefSeq; NP_001307193.1; NM_001320264.1.
DR RefSeq; NP_036227.1; NM_012095.5.
DR RefSeq; NP_996895.1; NM_207012.3.
DR AlphaFoldDB; Q9Y2T2; -.
DR SMR; Q9Y2T2; -.
DR BioGRID; 117938; 163.
DR ComplexPortal; CPX-5051; Ubiquitous AP-3 Adaptor complex, sigma3a variant.
DR ComplexPortal; CPX-5052; Ubiquitous AP-3 Adaptor complex, sigma3b variant.
DR CORUM; Q9Y2T2; -.
DR IntAct; Q9Y2T2; 63.
DR MINT; Q9Y2T2; -.
DR STRING; 9606.ENSP00000347408; -.
DR iPTMnet; Q9Y2T2; -.
DR PhosphoSitePlus; Q9Y2T2; -.
DR SwissPalm; Q9Y2T2; -.
DR BioMuta; AP3M1; -.
DR DMDM; 13123952; -.
DR EPD; Q9Y2T2; -.
DR jPOST; Q9Y2T2; -.
DR MassIVE; Q9Y2T2; -.
DR MaxQB; Q9Y2T2; -.
DR PaxDb; Q9Y2T2; -.
DR PeptideAtlas; Q9Y2T2; -.
DR PRIDE; Q9Y2T2; -.
DR ProteomicsDB; 85889; -.
DR Antibodypedia; 45437; 133 antibodies from 28 providers.
DR DNASU; 26985; -.
DR Ensembl; ENST00000355264.9; ENSP00000347408.4; ENSG00000185009.13.
DR Ensembl; ENST00000372745.1; ENSP00000361831.1; ENSG00000185009.13.
DR GeneID; 26985; -.
DR KEGG; hsa:26985; -.
DR MANE-Select; ENST00000355264.9; ENSP00000347408.4; NM_012095.6; NP_036227.1.
DR UCSC; uc001jwg.4; human.
DR CTD; 26985; -.
DR DisGeNET; 26985; -.
DR GeneCards; AP3M1; -.
DR HGNC; HGNC:569; AP3M1.
DR HPA; ENSG00000185009; Low tissue specificity.
DR MIM; 610366; gene.
DR neXtProt; NX_Q9Y2T2; -.
DR OpenTargets; ENSG00000185009; -.
DR PharmGKB; PA24860; -.
DR VEuPathDB; HostDB:ENSG00000185009; -.
DR eggNOG; KOG2740; Eukaryota.
DR GeneTree; ENSGT00940000158184; -.
DR HOGENOM; CLU_026996_6_2_1; -.
DR InParanoid; Q9Y2T2; -.
DR OMA; SCGTIRY; -.
DR OrthoDB; 928391at2759; -.
DR PhylomeDB; Q9Y2T2; -.
DR TreeFam; TF315187; -.
DR PathwayCommons; Q9Y2T2; -.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR SignaLink; Q9Y2T2; -.
DR SIGNOR; Q9Y2T2; -.
DR BioGRID-ORCS; 26985; 20 hits in 1079 CRISPR screens.
DR ChiTaRS; AP3M1; human.
DR GeneWiki; AP3M1; -.
DR GenomeRNAi; 26985; -.
DR Pharos; Q9Y2T2; Tbio.
DR PRO; PR:Q9Y2T2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9Y2T2; protein.
DR Bgee; ENSG00000185009; Expressed in pancreatic ductal cell and 180 other tissues.
DR ExpressionAtlas; Q9Y2T2; baseline and differential.
DR Genevisible; Q9Y2T2; HS.
DR GO; GO:0030123; C:AP-3 adaptor complex; IC:ComplexPortal.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; TAS:ProtInc.
DR GO; GO:0031267; F:small GTPase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0035654; P:clathrin-coated vesicle cargo loading, AP-3-mediated; IC:ComplexPortal.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; IC:ComplexPortal.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0060155; P:platelet dense granule organization; IC:ComplexPortal.
DR GO; GO:0006622; P:protein targeting to lysosome; TAS:ProtInc.
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 Cytoplasmic vesicle; Golgi apparatus; Host-virus interaction; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..418
FT /note="AP-3 complex subunit mu-1"
FT /id="PRO_0000193781"
FT DOMAIN 176..417
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT CONFLICT 160
FT /note="G -> V (in Ref. 2; BAB15614)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="N -> D (in Ref. 2; BAB15614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46939 MW; 533E189C320C4C48 CRC64;
MIHSLFLINC SGDIFLEKHW KSVVSQSVCD YFFEAQEKAA DVENVPPVIS TPHHYLISIY
RDKLFFVSVI QTEVPPLFVI EFLHRVADTF QDYFGECSEA AIKDNVVIVY ELLEEMLDNG
FPLATESNIL KELIKPPTIL RSVVNSITGS SNVGDTLPTG QLSNIPWRRA GVKYTNNEAY
FDVVEEIDAI IDKSGSTVFA EIQGVIDACI KLSGMPDLSL SFMNPRLLDD VSFHPCIRFK
RWESERVLSF IPPDGNFRLI SYRVSSQNLV AIPVYVKHSI SFKENSSCGR FDITIGPKQN
MGKTIEGITV TVHMPKVVLN MNLTPTQGSY TFDPVTKVLT WDVGKITPQK LPSLKGLVNL
QSGAPKPEEN PSLNIQFKIQ QLAISGLKVN RLDMYGEKYK PFKGVKYVTK AGKFQVRT
