AP2B1_RAT
ID AP2B1_RAT Reviewed; 937 AA.
AC P62944; P21851;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 163.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=2495531; DOI=10.1073/pnas.86.8.2612;
RA Kirchhausen T., Nathanson K.L., Matsui W., Vaisberg A., Chow E.P.,
RA Burne C., Keen J.H., Davis A.E.;
RT "Structural and functional division into two domains of the large (100- to
RT 115-kDa) chains of the clathrin-associated protein complex AP-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2612-2616(1989).
RN [3]
RP INTERACTION WITH CLATHRIN.
RX PubMed=7559550; DOI=10.1074/jbc.270.40.23768;
RA Goodman O.B. Jr., Keen J.H.;
RT "The alpha chain of the AP-2 adaptor is a clathrin binding subunit.";
RL J. Biol. Chem. 270:23768-23773(1995).
RN [4]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14745134; DOI=10.1247/csf.28.419;
RA Nakatsu F., Ohno H.;
RT "Adaptor protein complexes as the key regulators of protein sorting in the
RT post-Golgi network.";
RL Cell Struct. Funct. 28:419-429(2003).
RN [5]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA Owen D.J., Collins B.M., Evans P.R.;
RT "Adaptors for clathrin coats: structure and function.";
RL Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN [6]
RP INTERACTION WITH PIP5K1C, AND MUTAGENESIS OF GLN-756; GLN-804; ALA-806;
RP LYS-808 AND TYR-815.
RX PubMed=19287005; DOI=10.1074/jbc.m901017200;
RA Thieman J.R., Mishra S.K., Ling K., Doray B., Anderson R.A., Traub L.M.;
RT "Clathrin regulates the association of PIPKIgamma661 with the AP-2 adaptor
RT beta2 appendage.";
RL J. Biol. Chem. 284:13924-13939(2009).
RN [7]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-928, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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, ECO:0000269|PubMed:14745134,
CC ECO:0000269|PubMed:15473838}.
CC -!- SUBUNIT: Adaptor 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 (PubMed:7559550). 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
CC (PubMed:19287005). Interacts with DENND1B (By similarity). Interacts
CC with FCHO1 (PubMed:22484487). Interacts with RFTN1 (By similarity).
CC Interacts with KIAA1107 (By similarity). Together with AP2A1 or AP2A2
CC and AP2M1, it interacts with ADAM10; this interaction facilitates
CC ADAM10 endocytosis from the plasma membrane during long-term
CC potentiation in hippocampal neurons (By similarity).
CC {ECO:0000250|UniProtKB:P63010, ECO:0000250|UniProtKB:Q9DBG3,
CC ECO:0000269|PubMed:19287005, ECO:0000269|PubMed:22484487,
CC ECO:0000269|PubMed:7559550}.
CC -!- INTERACTION:
CC P62944-2; Q3MUI1: Numb; NbExp=2; IntAct=EBI-7008032, EBI-7007865;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62944-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62944-2; Sequence=VSP_011492;
CC -!- MISCELLANEOUS: [Isoform 2]: Brain specific. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; M34176; AAA40797.1; -; mRNA.
DR EMBL; M77246; AAA40808.1; -; mRNA.
DR PIR; C35553; C35553.
DR RefSeq; NP_542150.1; NM_080583.1. [P62944-2]
DR RefSeq; XP_008766157.1; XM_008767935.2. [P62944-2]
DR RefSeq; XP_008766158.1; XM_008767936.2. [P62944-2]
DR RefSeq; XP_008766159.1; XM_008767937.2. [P62944-2]
DR RefSeq; XP_008766160.1; XM_008767938.1. [P62944-2]
DR RefSeq; XP_008766161.1; XM_008767939.2. [P62944-1]
DR RefSeq; XP_017452462.1; XM_017596973.1. [P62944-2]
DR PDB; 3H1Z; X-ray; 1.83 A; A=701-937.
DR PDB; 3HS9; X-ray; 2.15 A; A=701-937.
DR PDB; 6OWT; EM; 3.80 A; B=1-591.
DR PDBsum; 3H1Z; -.
DR PDBsum; 3HS9; -.
DR PDBsum; 6OWT; -.
DR AlphaFoldDB; P62944; -.
DR SMR; P62944; -.
DR BioGRID; 250830; 29.
DR CORUM; P62944; -.
DR DIP; DIP-40944N; -.
DR IntAct; P62944; 7.
DR MINT; P62944; -.
DR STRING; 10116.ENSRNOP00000068516; -.
DR iPTMnet; P62944; -.
DR PhosphoSitePlus; P62944; -.
DR SwissPalm; P62944; -.
DR jPOST; P62944; -.
DR PaxDb; P62944; -.
DR PRIDE; P62944; -.
DR Ensembl; ENSRNOT00000088198; ENSRNOP00000070905; ENSRNOG00000061543. [P62944-2]
DR GeneID; 140670; -.
DR KEGG; rno:140670; -.
DR CTD; 163; -.
DR RGD; 71048; Ap2b1.
DR VEuPathDB; HostDB:ENSRNOG00000061543; -.
DR eggNOG; KOG1061; Eukaryota.
DR GeneTree; ENSGT00940000155206; -.
DR HOGENOM; CLU_006320_1_1_1; -.
DR InParanoid; P62944; -.
DR OMA; ASIYHKS; -.
DR TreeFam; TF300318; -.
DR Reactome; R-RNO-177504; Retrograde neurotrophin signalling.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-RNO-437239; Recycling pathway of L1.
DR Reactome; R-RNO-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-RNO-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-8866427; VLDLR internalisation and degradation.
DR Reactome; R-RNO-8964038; LDL clearance.
DR EvolutionaryTrace; P62944; -.
DR PRO; PR:P62944; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000061543; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; P62944; baseline and differential.
DR Genevisible; P62944; RN.
DR GO; GO:0030122; C:AP-2 adaptor complex; ISO:RGD.
DR GO; GO:0030119; C:AP-type membrane coat adaptor complex; TAS:ProtInc.
DR GO; GO:0030131; C:clathrin adaptor complex; ISO:RGD.
DR GO; GO:0030118; C:clathrin coat; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0030276; F:clathrin binding; IDA:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0003279; P:cardiac septum development; ISO:RGD.
DR GO; GO:0048268; P:clathrin coat assembly; IDA:BHF-UCL.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:RGD.
DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR GO; GO:0099590; P:neurotransmitter receptor internalization; ISO:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; IMP:RGD.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:0003281; P:ventricular septum development; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR DisProt; DP02887; -.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.1150; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR IDEAL; IID50159; -.
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 3D-structure; Acetylation; Alternative splicing; Cell membrane; Coated pit;
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_0000193744"
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:0007744|PubMed:22673903"
FT VAR_SEQ 663
FT /note="L -> LLGSDLGGGIGGSPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2495531"
FT /id="VSP_011492"
FT MUTAGEN 756
FT /note="Q->A: Abolishes interaction with PIP5K1C."
FT /evidence="ECO:0000269|PubMed:19287005"
FT MUTAGEN 804
FT /note="Q->A: Abolishes interaction with PIP5K1C."
FT /evidence="ECO:0000269|PubMed:19287005"
FT MUTAGEN 806
FT /note="A->F: Abolishes interaction with PIP5K1C."
FT /evidence="ECO:0000269|PubMed:19287005"
FT MUTAGEN 808
FT /note="K->E: Abolishes interaction with PIP5K1C."
FT /evidence="ECO:0000269|PubMed:19287005"
FT MUTAGEN 815
FT /note="Y->A: Abolishes interaction with PIP5K1C."
FT /evidence="ECO:0000269|PubMed:19287005"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:3H1Z"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:3H1Z"
FT TURN 720..722
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 723..732
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 735..744
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 746..748
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 754..757
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 765..768
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 781..790
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 802..808
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 813..819
FT /evidence="ECO:0007829|PDB:3H1Z"
FT HELIX 822..825
FT /evidence="ECO:0007829|PDB:3H1Z"
FT HELIX 834..843
FT /evidence="ECO:0007829|PDB:3H1Z"
FT HELIX 846..848
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 850..854
FT /evidence="ECO:0007829|PDB:3H1Z"
FT HELIX 861..870
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 874..881
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 884..893
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 898..905
FT /evidence="ECO:0007829|PDB:3H1Z"
FT STRAND 912..917
FT /evidence="ECO:0007829|PDB:3H1Z"
FT HELIX 921..923
FT /evidence="ECO:0007829|PDB:3H1Z"
FT HELIX 924..935
FT /evidence="ECO:0007829|PDB:3H1Z"
SQ SEQUENCE 937 AA; 104553 MW; B472EE5B2AE176DF 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 PKDSDYYNML 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
