AP2B1_BOVIN
ID AP2B1_BOVIN Reviewed; 937 AA.
AC P63009; P21851;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=AP-2 complex subunit beta;
DE AltName: Full=AP105B;
DE AltName: Full=Adaptor protein complex AP-2 subunit beta;
DE AltName: Full=Adaptor-related protein complex 2 subunit beta;
DE AltName: Full=Beta-2-adaptin;
DE AltName: Full=Beta-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 beta large chain;
DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin beta subunit;
GN Name=AP2B1; Synonyms=CLAPB1;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-268, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lymphocyte;
RX PubMed=1969413; DOI=10.1016/s0021-9258(19)34045-1;
RA Ponnambalam S., Robinson M.S., Jackson A.P., Peiperl L., Parham P.;
RT "Conservation and diversity in families of coated vesicle adaptins.";
RL J. Biol. Chem. 265:4814-4820(1990).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor
CC protein complexes function in protein transport via transport vesicles
CC in different membrane traffic pathways. Adaptor protein complexes are
CC vesicle coat components and appear to be involved in cargo selection
CC and vesicle formation. AP-2 is involved in clathrin-dependent
CC endocytosis in which cargo proteins are incorporated into vesicles
CC surrounded by clathrin (clathrin-coated vesicles, CCVs) which are
CC destined for fusion with the early endosome. The clathrin lattice
CC serves as a mechanical scaffold but is itself unable to bind directly
CC to membrane components. Clathrin-associated adaptor protein (AP)
CC complexes which can bind directly to both the clathrin lattice and to
CC the lipid and protein components of membranes are considered to be the
CC major clathrin adaptors contributing the CCV formation. AP-2 also
CC serves as a cargo receptor to selectively sort the membrane proteins
CC involved in receptor-mediated endocytosis. AP-2 seems to play a role in
CC the recycling of synaptic vesicle membranes from the presynaptic
CC surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-
CC [LI] endocytosis signal motifs within the cytosolic tails of
CC transmembrane cargo molecules. AP-2 may also play a role in maintaining
CC normal post-endocytic trafficking through the ARF6-regulated, non-
CC clathrin pathway. During long-term potentiation in hippocampal neurons,
CC AP-2 is responsible for the endocytosis of ADAM10 (By similarity). The
CC AP-2 beta subunit acts via its C-terminal appendage domain as a
CC scaffolding platform for endocytic accessory proteins; at least some
CC clathrin-associated sorting proteins (CLASPs) are recognized by their
CC [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to
CC clathrin heavy chain, promoting clathrin lattice assembly; clathrin
CC displaces at least some CLASPs from AP2B1 which probably then can be
CC positioned for further coat assembly (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P63010}.
CC -!- SUBUNIT: adapter protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type
CC subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small
CC adaptin (sigma-type subunit AP2S1) (By similarity). Interacts with EPN1
CC (By similarity). Interacts with EPS15; clathrin competes with EPS15 (By
CC similarity). Interacts with SNAP91; clathrin competes with SNAP91 (By
CC similarity). Interacts with CLTC; clathrin competes with EPS15, SNAP91
CC and PIP5K1C (By similarity). Interacts with LDLRAP1 (By similarity).
CC Interacts with AMPH and BIN1 (By similarity). Interacts with ARF6 (GDP-
CC bound) (By similarity). Interacts (dephosphorylated at Tyr-737) with
CC ARRB1; phosphorylation of AP2B1 at Tyr-737 disrupts the interaction (By
CC similarity). Interacts with SLC2A8 (By similarity). Interacts with
CC SCYL1 and SCYL2 (By similarity). Interacts with TGFBR1 and TGFBR2 (By
CC similarity). Interacts with PIP5K1C; clathrin competes with PIP5K1C (By
CC similarity). Interacts with DENND1B (By similarity). Interacts with
CC FCHO1 (By similarity). Interacts with RFTN1 (By similarity). Interacts
CC with KIAA1107 (By similarity). Together with AP2A1 or AP2A2 and AP2M1,
CC it interacts with ADAM10; this interaction facilitates ADAM10
CC endocytosis from the plasma membrane during long-term potentiation in
CC hippocampal neurons (By similarity). {ECO:0000250|UniProtKB:P62944,
CC ECO:0000250|UniProtKB:P63010, ECO:0000250|UniProtKB:Q9DBG3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=AP-2 appears to be excluded from internalizing
CC CCVs and to disengage from sites of endocytosis seconds before
CC internalization of the nascent CCV. {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Phosphorylation at Tyr-737 by SRC occurs at the plasma membrane in
CC clathrin-coated vesicles (CCVs). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; M34177; AAA30405.1; -; mRNA.
DR PIR; B35553; B35553.
DR AlphaFoldDB; P63009; -.
DR SMR; P63009; -.
DR DIP; DIP-44826N; -.
DR ELM; P63009; -.
DR IntAct; P63009; 2.
DR MINT; P63009; -.
DR PeptideAtlas; P63009; -.
DR PRIDE; P63009; -.
DR Ensembl; ENSBTAT00000084860; ENSBTAP00000065136; ENSBTAG00000020316.
DR VEuPathDB; HostDB:ENSBTAG00000020316; -.
DR VGNC; VGNC:55033; AP2B1.
DR GeneTree; ENSGT00940000155206; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000020316; Expressed in spermatid and 105 other tissues.
DR ExpressionAtlas; P63009; baseline and differential.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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 Gene3D; 2.60.40.1150; -; 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; IPR000225; Armadillo.
DR InterPro; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF09066; B2-adapt-app_C; 1.
DR PIRSF; PIRSF002291; AP_complex_beta; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SMART; SM00185; ARM; 2.
DR SMART; SM01020; B2-adapt-app_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Coated pit; Direct protein sequencing;
KW Endocytosis; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63010"
FT CHAIN 2..937
FT /note="AP-2 complex subunit beta"
FT /id="PRO_0000193741"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P63010"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63010"
FT MOD_RES 265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63010"
FT MOD_RES 737
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P63010"
FT MOD_RES 928
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62944"
SQ SEQUENCE 937 AA; 104567 MW; 1BE161EF3B8C07A3 CRC64;
MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL FPDVVNCMQT
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP LIRALAVRTM GCIRVDKITE
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQMVEDQG FLDSLRDLIA DSNPMVVANA
VAALSEISES HPNSNLLDLN PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI
CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKESDYYNML LKKLAPPLVT LLSGEPEVQY
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIRDIFRK
YPNKYESIIA TLCENLDSLD EPDARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV
QLTLLTAIVK LFLKKPSETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV
VLSEKPLISE ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST
DAGDSPVGTT TATNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM GAVDLLGGGL
DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI GMAPGGYVAP KAVWLPAVKA
KGLEISGTFT HRQGHIYMEM NFTNKALQHM TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ
SIDVSLPLNT LGPVMKMEPL NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT
WKDIPNENEL QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN
