AP4B1_MOUSE
ID AP4B1_MOUSE Reviewed; 738 AA.
AC Q9WV76; B0V3P2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=AP-4 complex subunit beta-1 {ECO:0000305};
DE AltName: Full=AP-4 adaptor complex subunit beta;
DE AltName: Full=Adaptor-related protein complex 4 subunit beta-1;
DE AltName: Full=Beta subunit of AP-4;
DE AltName: Full=Beta4-adaptin;
GN Name=Ap4b1 {ECO:0000312|MGI:MGI:1337130};
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].
RX PubMed=10436028; DOI=10.1091/mbc.10.8.2787;
RA Hirst J., Bright N.A., Rous B., Robinson M.S.;
RT "Characterization of a fourth adaptor-related protein complex.";
RL Mol. Biol. Cell 10:2787-2802(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH GRIA2.
RX PubMed=18341993; DOI=10.1016/j.neuron.2008.02.012;
RA Matsuda S., Miura E., Matsuda K., Kakegawa W., Kohda K., Watanabe M.,
RA Yuzaki M.;
RT "Accumulation of AMPA receptors in autophagosomes in neuronal axons lacking
RT adaptor protein AP-4.";
RL Neuron 57:730-745(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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: 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 (By similarity). It is
CC also involved in protein sorting to the basolateral membrane in
CC epithelial cells and the proper asymmetric localization of
CC somatodendritic proteins in neurons (PubMed:18341993). AP-4 is involved
CC in the recognition and binding of tyrosine-based sorting signals found
CC in the cytoplasmic part of cargos, but may also recognize other types
CC of sorting signal (By similarity). {ECO:0000250|UniProtKB:Q9Y6B7,
CC ECO:0000269|PubMed:18341993}.
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). Interacts with TEPSIN; this interaction requires
CC the presence of a functional AP-4 complex (By similarity). Interacts
CC with GRIA2; probably indirect it mediates the somatodendritic
CC localization of GRIA2 in neurons (PubMed:18341993).
CC {ECO:0000250|UniProtKB:Q9Y6B7, ECO:0000269|PubMed:18341993}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9Y6B7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Y6B7}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Ap4b1 are fertile, have no overt
CC anatomical abnormalities and have normal life spans. They only show a
CC significantly poorer rotorod performance than wild-type mice. No
CC significant differences in body weight or grip power is observed
CC compared to wild-type mice. The cerebella has normal foliation and a
CC normal laminated cortical structure. Main neuronal types are present in
CC the cerebella and the gross morphology of the soma and dendrites of
CC Purkinje cells is normal. {ECO:0000269|PubMed:18341993}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large 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; AF155157; AAD43327.1; -; mRNA.
DR EMBL; AC124698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU210953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS17696.1; -.
DR RefSeq; NP_001157024.1; NM_001163552.1.
DR RefSeq; NP_080469.2; NM_026193.2.
DR AlphaFoldDB; Q9WV76; -.
DR SMR; Q9WV76; -.
DR BioGRID; 212225; 1.
DR ComplexPortal; CPX-5154; AP-4 Adaptor complex.
DR IntAct; Q9WV76; 1.
DR MINT; Q9WV76; -.
DR STRING; 10090.ENSMUSP00000044262; -.
DR iPTMnet; Q9WV76; -.
DR PhosphoSitePlus; Q9WV76; -.
DR jPOST; Q9WV76; -.
DR MaxQB; Q9WV76; -.
DR PaxDb; Q9WV76; -.
DR PRIDE; Q9WV76; -.
DR ProteomicsDB; 281787; -.
DR DNASU; 67489; -.
DR Ensembl; ENSMUST00000047285; ENSMUSP00000044262; ENSMUSG00000032952.
DR Ensembl; ENSMUST00000076599; ENSMUSP00000075904; ENSMUSG00000032952.
DR GeneID; 67489; -.
DR KEGG; mmu:67489; -.
DR UCSC; uc008qtq.2; mouse.
DR CTD; 10717; -.
DR MGI; MGI:1337130; Ap4b1.
DR VEuPathDB; HostDB:ENSMUSG00000032952; -.
DR eggNOG; KOG1061; Eukaryota.
DR GeneTree; ENSGT00940000157025; -.
DR InParanoid; Q9WV76; -.
DR OMA; KMCFLYL; -.
DR OrthoDB; 323029at2759; -.
DR PhylomeDB; Q9WV76; -.
DR TreeFam; TF354235; -.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 67489; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ap4b1; mouse.
DR PRO; PR:Q9WV76; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9WV76; protein.
DR Bgee; ENSMUSG00000032952; Expressed in spermatocyte and 62 other tissues.
DR ExpressionAtlas; Q9WV76; baseline and differential.
DR Genevisible; Q9WV76; MM.
DR GO; GO:0030124; C:AP-4 adaptor complex; ISS:UniProtKB.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:0061938; P:protein localization to somatodendritic compartment; IMP:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR InterPro; IPR026739; AP_beta.
DR InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF09066; B2-adapt-app_C; 1.
DR PIRSF; PIRSF002291; AP_complex_beta; 1.
DR SMART; SM01020; B2-adapt-app_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..738
FT /note="AP-4 complex subunit beta-1"
FT /id="PRO_0000193751"
FT REGION 534..600
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6B7"
FT REGION 601..738
FT /note="Ear; mediates interaction with TEPSIN"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6B7"
FT CONFLICT 228
FT /note="R -> L (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="A -> S (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="S -> N (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 462..463
FT /note="DN -> QS (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="V -> F (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="M -> V (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="H -> L (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="E -> Q (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="V -> T (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="L -> S (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="R -> K (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 580..583
FT /note="QVER -> KIEP (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="S -> A (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="E -> EP (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 615..618
FT /note="DTLM -> GALV (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="Y -> C (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="R -> T (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="Q -> H (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="F -> L (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 672..673
FT /note="RA -> KP (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="D -> G (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="A -> T (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="M -> V (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="K -> E (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
FT CONFLICT 718..720
FT /note="SLH -> ALR (in Ref. 1; AAD43327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 738 AA; 82976 MW; 1F05223F89E1A360 CRC64;
MPYLGSEDVV KELKKALCNP HIQADRLRYR NVIQRVIRHM TQGLDMSDVF MEMVKASATV
DIVQKKLVYL YMGTYAPLKP DLALLAINTL CKDCSDPNPM VRGLALRSMC SLRMPGVQEY
IQQPVVNGLR DKASYVRRVA VLGCAKMHNL HGDSEVDGAL VNELYSLLRD QDPIVVVNCL
RSLEEILKQE GGVVINKPIA HHLLNRMSKL DQWGQAEVLN FLLRYQPRSE EELFDILNLL
DSYLKSSSTG VVMGATKLFL ILAKKFPHVQ TDVLVRVKGP LLAACSSESR ELCFAALCHV
RQVLHSLPGH FSSHYKKFFC SYSEPHYIKL QKVEVLCELV NDENVQQVLE ELRGYCTDVA
ADFAQAAIFA IGSIAKTYTD QCVQILTELL GLRQEHITTV VVQTFRDLVW LCPQCTEAVC
QALPGCEENI QDSEGKQALI WLLGVHGEKI PNAPYVLEDF VDNVKSETFP AVKMELLTAL
MRLVLSRPAE CQDMLGRLLH YCIEEEKDMA VRDRGLFYYR LLLVGIDKVK QILCSPKSDP
SLGLLEDQPE RPVNSWASDF NTLAPVYGRA HWATISKCQQ VERHRLELPH NASFATSGHL
ISEENKEGAQ EPDSDTLMLV PNLQLTAEYF EKTWLSLRVS YQQVFPWQGE VQPDTLQMAL
KVVNIQTIAM SRAGAQPWKA YLSAQDDTGG LFLAELLLKP ENSEMQISVK QSKARTESLH
GFVSVLETVI GTVGDIKS
