AP3B1_CANLF
ID AP3B1_CANLF Reviewed; 1091 AA.
AC Q7YRF1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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; Synonyms=ADTB3A;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RA Benson K.F., Li F.-Q., Person R.E., Albani D., Duan Z., Wechsler J.,
RA Meade-White K., Williams K., Acland G.M., Niemeyer G., Lothrop C.D.,
RA Horwitz M.;
RL Submitted (JAN-2003) 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}.
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; AY221640; AAP45786.1; -; mRNA.
DR RefSeq; NP_001002974.1; NM_001002974.2.
DR AlphaFoldDB; Q7YRF1; -.
DR SMR; Q7YRF1; -.
DR STRING; 9615.ENSCAFP00000056696; -.
DR PaxDb; Q7YRF1; -.
DR PRIDE; Q7YRF1; -.
DR GeneID; 403459; -.
DR KEGG; cfa:403459; -.
DR CTD; 8546; -.
DR eggNOG; KOG1060; Eukaryota.
DR InParanoid; Q7YRF1; -.
DR OrthoDB; 323029at2759; -.
DR Proteomes; UP000002254; Unplaced.
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:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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..1091
FT /note="AP-3 complex subunit beta-1"
FT /id="PRO_0000193745"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..714
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..807
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 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00203"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00203"
SQ SEQUENCE 1091 AA; 121191 MW; 53212E479694B4C6 CRC64;
MSGNSFAYSE QAGGGEATEL GQEATSTVSP SGAFGLFSSD LKKNEDLKQM LESNKDSAKL
DAMKRIVGMI AKGKNASELF PAVVKNVASK NIEIKKLVYV YLVRYAEEQQ DLALLSISTF
QRALKDPNQL IRASALRVLS SIRVPIIVPI MMLAIKEASA DLSPYVRKNA AHAIQKLYSL
DPEQKEMLIE VIEKLLKDKS TLVAGSVVMA FEEVCPDRID LIHKNYRKLC NLLVDVEEWG
QVVIIHMLTR YARTQFVSPW KEDDGLEDNE KNFYESDDEQ KEKTDQKKKP YAMDPDHRLL
IRNTKPLLQS RNAAVVMAVA QLYWHISPKS EVGIISKSLV RLLRSNREVQ YIVLQNIATM
SIQRKGMLEP YLKSFYVRST DPTMIKILKL EILTNLANEA NISTLLREFQ TYVKSQDKQF
AAATIQTIGR CATSISEVTD TCLSGLVCLL SNRDEIVVAE SVVVIKKLLQ MQPAQHGEII
KHMAKLLDSI TVPVARASIL WLIGENCERV PKIAPDVLRK MAKSFTNEDD LVKLQILNLG
AKLYLTNSKQ TKLLTQYILN LGKYDQNYDI RDRTRFIRQL IVPNEKSGAL SKYAKKIFLA
QKPAPLLESP FKDRDHFQLG TLSHTLNTKA IGYLELSNWP EVAPDPSVRN VEVIELQAKE
WTPAGKAKKE NPARKFYSDS EEEEDSSDSS SDSESESGSA SGEQDEEGDS SEDSSEDSSS
EHRSDSESVS EVGDKRTAKR NSKSKGKSDS EDEEKENEKS KTSDSSSTDS SSVEESSSDS
ESESESESES ESKKVTMEKE KKTKEDRNLT KDVSLLDLDD FNPVSTPVVL PTPALSPSLI
ADLEGLNLST SSSVISVNTP VFVPVKTHVL LHRMSGRGLA AHYFFPRQPC IFGDKMVSIQ
ITLNNTTDRK IENIHIEGKK LPMGMQMHVF NPIESLEPEG SITVSMGIDF CDSTQTASFQ
LCTKDDCFNV NIQPPVGELL LPVAMSEKDF KKEQGMLTGM NETSTVIIAA PQNFTPSVIL
QKVVNIANVG VVPSGQDNIY RFAAKTVHSG SLMLVTVELK EGSTAQLIIN TERTVIGSVL
LRELKPVLSQ G
