ID A0A4P1RPI3_LUPAN Unreviewed; 1002 AA.
AC A0A4P1RPI3;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN ORFNames=TanjilG_04333 {ECO:0000313|EMBL:OIW15798.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW15798.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIW15798.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIW15798.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
CC -!- FUNCTION: Subunit 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.
CC {ECO:0000256|PIRNR:PIRNR037091}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type and beta-type subunits), a medium
CC adaptin (mu-type subunit) and a small adaptin (sigma-type subunit).
CC {ECO:0000256|PIRNR:PIRNR037091}.
CC -!- SUBCELLULAR LOCATION: Membrane, coated pit
CC {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004277}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000256|PIRNR:PIRNR037091}.
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DR EMBL; CM007363; OIW15798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P1RPI3; -.
DR STRING; 3871.A0A4P1RPI3; -.
DR Proteomes; UP000188354; Chromosome LG03.
DR GO; GO:0030122; C:AP-2 adaptor complex; IEA:InterPro.
DR GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.1230; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.310.10; TATA-Binding Protein; 1.
DR InterPro; IPR017104; AP2_complex_asu.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR22780; ADAPTIN, ALPHA/GAMMA/EPSILON; 1.
DR PANTHER; PTHR22780:SF4; AP-2 COMPLEX SUBUNIT ALPHA; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02296; Alpha_adaptin_C; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037091; AP2_complex_alpha; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
DR SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1.
PE 3: Inferred from homology;
KW Coated pit {ECO:0000256|ARBA:ARBA00023176, ECO:0000256|PIRNR:PIRNR037091};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583, ECO:0000256|PIRNR:PIRNR037091};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037091};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR037091};
KW Reference proteome {ECO:0000313|Proteomes:UP000188354};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 750..859
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT REGION 638..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7..8
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT BINDING 49
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT BINDING 53..57
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
SQ SEQUENCE 1002 AA; 112084 MW; F22762D841660228 CRC64;
MAMSGMRGLS VFISDIRNCQ NKEQERLRVD KELGNIRTRF KNEKALTPYE KKKYVWKMLY
IYMLGYDVDF GHMEAVSLIS APKYPEKQVG YIVTSSLLHE NHDFLRLAIN TVRNDIIGRN
ETFQCLALTM VGNIGGREFA ESLAPDVQKL LISSSCRPLV RKKAALCLLR LYRKNPDVVN
VDGWADRMAQ LLDERDLGVL TSSMSLLVAL VSNHHEAYWS CLPKCVKILE RLARNQDIPP
EYTYYGIPSP WLQVKTMRAL QYFPTIEDPN TRRSLFEVLQ RILMGTDVVK NVNKNNASHA
VLFESLALVM HLDAEKEMMS QCAALLGKFI AVREPNIRYL GLENMTRMLM VTDVQDIIKR
HQAQIITSLK DPDISIRRRA LDLLYGMCDI SNAKDIVEEL LQYLSTAEFA MREELSLKAA
ILAEKFAPDL SWYVDVILQL IDKAGDFVSD DIWFRVVQFV TNNEDLQPYA AAKAREYLDK
PAIHETMVKV SAYILGEFGH LLARRPGCSP KEIFNIIHEK LPTVSTSTIS ILLSTYAKIL
MHTQPPDPEL QNQIWAIFKK YESSIEVEIQ QRAVEYFTLC RKGADLMDIL AEMPKFPERQ
SALIRKAEDT EVDTAEQSAI KLRAQQQSQA SNALAVTDQS YGNGTPTVSH LSPVKLPSTS
SKVDNSLADQ RLYQENGTLN KEDSVPPSED LLSDLLGPLA IEGPPSSSVH PQRSTTSGLE
DTVVDATALV PAGEQANAVQ PIGNTAERFH ALCVKDSGVL YEDPYIQIGI KAEWRAHHGH
LVLFLGNKNT SPLVSVQAII LPPTHLKMEL SLVPETIPPR AQVQCPLEVI NLRPSRDVAV
VDFSYKFGND MVNVKLRLPA ILNKFLQPIP VSAEEFFPQW RSLTGPPLKL QEVVRGVKPL
PVLEMANLFN SFHLTVSPGL DPNPNNLVAS TTFFSESTRA MLCLVILILI CRLKEFIKEQ
LIVIPTVTHA PTQAPPGPPP LAQPASNPAA LTDPGAMLAA LL
//
