AP3B1_BOVIN
ID AP3B1_BOVIN Reviewed; 1084 AA.
AC Q32PG1;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=AP-3 complex subunit beta-1;
DE AltName: Full=Adaptor protein complex AP-3 subunit beta-1;
DE AltName: Full=Adaptor-related protein complex 3 subunit beta-1;
DE AltName: Full=Beta-3A-adaptin;
DE AltName: Full=Clathrin assembly protein complex 3 beta-1 large chain;
GN Name=AP3B1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor
CC protein complex 3 (AP-3) that plays a role in protein sorting in the
CC late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes
CC mediate both the recruitment of clathrin to membranes and the
CC recognition of sorting signals within the cytosolic tails of
CC transmembrane cargo molecules. AP-3 appears to be involved in the
CC sorting of a subset of transmembrane proteins targeted to lysosomes and
CC lysosome-related organelles. In concert with the BLOC-1 complex, AP-3
CC is required to target cargos into vesicles assembled at cell bodies for
CC delivery into neurites and nerve terminals.
CC {ECO:0000250|UniProtKB:Q9Z1T1}.
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) (By similarity). AP-
CC 3 associates with the BLOC-1 complex (By similarity). Interacts with
CC KIF3A; interaction is direct; interaction is impaired by
CC pyrophosphorylation of AP3B1 (By similarity).
CC {ECO:0000250|UniProtKB:O00203, ECO:0000250|UniProtKB:Q9Z1T1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:O00203}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O00203}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O00203}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O00203}. Note=Component of the coat surrounding
CC the cytoplasmic face of coated vesicles located at the Golgi complex.
CC {ECO:0000250|UniProtKB:O00203}.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000250|UniProtKB:O00203}.
CC -!- PTM: Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) impairs interaction with KIF3A. Serine pyrophosphorylation is
CC achieved by Mg(2+)-dependent, but enzyme independent transfer of a
CC beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated
CC serine residue. {ECO:0000250|UniProtKB:O00203}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; BC108129; AAI08130.1; -; mRNA.
DR RefSeq; NP_001070002.1; NM_001076534.1.
DR AlphaFoldDB; Q32PG1; -.
DR SMR; Q32PG1; -.
DR BioGRID; 612977; 1.
DR STRING; 9913.ENSBTAP00000006605; -.
DR PaxDb; Q32PG1; -.
DR PRIDE; Q32PG1; -.
DR Ensembl; ENSBTAT00000006605; ENSBTAP00000006605; ENSBTAG00000005016.
DR GeneID; 767602; -.
DR KEGG; bta:767602; -.
DR CTD; 8546; -.
DR VEuPathDB; HostDB:ENSBTAG00000005016; -.
DR VGNC; VGNC:25987; AP3B1.
DR eggNOG; KOG1060; Eukaryota.
DR GeneTree; ENSGT00940000157603; -.
DR HOGENOM; CLU_006320_3_1_1; -.
DR InParanoid; Q32PG1; -.
DR OMA; ASSNEWK; -.
DR OrthoDB; 323029at2759; -.
DR TreeFam; TF314605; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000005016; Expressed in ileum and 105 other tissues.
DR ExpressionAtlas; Q32PG1; baseline and differential.
DR GO; GO:0030123; C:AP-3 adaptor complex; IEA:InterPro.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0030742; F:GTP-dependent protein binding; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IEA:Ensembl.
DR GO; GO:0090152; P:establishment of protein localization to mitochondrial membrane involved in mitochondrial fission; IEA:Ensembl.
DR GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl.
DR GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR GO; GO:0032438; P:melanosome organization; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060155; P:platelet dense granule organization; IEA:Ensembl.
DR GO; GO:0051138; P:positive regulation of NK T cell differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0036211; P:protein modification process; IEA:Ensembl.
DR GO; GO:0006622; P:protein targeting to lysosome; IEA:Ensembl.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:Ensembl.
DR GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR GO; GO:0098773; P:skin epidermis development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0016182; P:synaptic vesicle budding from endosome; IEA:Ensembl.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR026740; AP3_beta.
DR InterPro; IPR029394; AP3B1_Ser.
DR InterPro; IPR029390; AP3B_C.
DR InterPro; IPR026739; AP_beta.
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 PANTHER; PTHR11134; PTHR11134; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF14796; AP3B1_C; 1.
DR Pfam; PF14797; SEEEED; 1.
DR PIRSF; PIRSF037096; AP3_complex_beta; 1.
DR SMART; SM01355; AP3B1_C; 1.
DR SMART; SM01020; B2-adapt-app_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1084
FT /note="AP-3 complex subunit beta-1"
FT /id="PRO_0000283801"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..712
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00203"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00203"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00203"
SQ SEQUENCE 1084 AA; 119968 MW; 4B694C02E3F3C636 CRC64;
MSSNSFAYNE QSGGGEATEL GQEATSTISP SGAFGLFSSD MKKNEDLKQM LESNKDSAKL
DAMKRIVGMI AKGKNASELF PAVVKNVASK NIEIKKLVYV YLVRYAEEQQ DLALLSISTF
QRALKDPNQL IRASALRVLS SIRVPIIVPI MMLAIKEASA DLSPYVRKNA AHAIQKLYSL
DPEQKEMLIE IIEKLLKDKS TLVAGSVVMA FEEVCPDRID LIHKNYRKLC NLLVDVEEWG
QVVIIHMLTR YARTQFVSPW RQGDVLEDNE KDFYDSDEEQ KEKADKRKRP YAMDPDHRLL
IRNTKPLLQS RNAAVVMAVA QLYWHIAPKS EAGIISKSLV RLLRSSREVQ YIVLQNIATM
SIQRKGMFEP YLKSFYVRST DATMIKILKL EILTNLANEA NISTLLREFQ TYVKSQDKQF
AAATIQTIGR CATSITEVSD TCLNGLVCLL SNRDEIVVAE SVVVIKKLLQ MQPMQHGEII
KHMAKLLDSI TVPVARASIL WLIGENCERV PKIAPDVLRK TAKSFTSEDD LVKLQILNLG
AKLYLTNSKQ TKLLTQYILN LGKYDQNYDI RDRTRFIRQL IVPNEKSGAL SKYAKKIFLA
QKPAPLLESP FKDRDHFQLG TLSHTLNTKA TGYLELSNWP EVAPDPSVRN VEVIELAKEW
TPAGKAKKEN PDKKFYSESE EEEDSSESSS DSESESGSES GEDEEDDRSG DSAEDSGESG
SEPEAGKGRA ATRSRARGRG DSKDVDKEKE NSKTSESSSG ESSSIEESSS DSESESESES
ESESRKVTKE KEKKTKQERN PLTKDVSLLD LDDFNLVSTP VALPTPALSP SLIADLEGLN
LSATSSVISV STPVFVPGKT HVLLHRMSGK GLAAHYFFPR QPCIFGDKMV SVQITLNNTT
DQKIENIHVG GKKLPMGMQM HVFNPIESLE PAGSITVSMG IDFCDSTQTA SFQLCTKDDC
FSVNIQPPVG ELLLPVAMSE KDFKKEQGML SGMNETSTTI IAAPQNFASS VILQKIVNVA
NVGVVPSGQD NIHRFAAKTV HSGSLMLVTV ELKEGSTAQL IINTEKTVIG SVLLRELKPV
LSQG
