ID A0A1U8I153_GOSHI Unreviewed; 1026 AA.
AC A0A1U8I153;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN Name=LOC107891639 {ECO:0000313|RefSeq:XP_016671970.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016671970.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016671970.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016671970.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_016671970.1; XM_016816481.1.
DR AlphaFoldDB; A0A1U8I153; -.
DR STRING; 3635.A0A1U8I153; -.
DR PaxDb; 3635-A0A1U8I153; -.
DR GeneID; 107891639; -.
DR KEGG; ghi:107891639; -.
DR OMA; ILYEDQY; -.
DR OrthoDB; 25313at2759; -.
DR Proteomes; UP000189702; Chromosome 14.
DR GO; GO:0030122; C:AP-2 adaptor complex; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
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:UP000189702};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 753..862
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT REGION 663..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1011
FT /note="Pro residues"
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 1026 AA; 114434 MW; 4C5FB9AEA1B49376 CRC64;
MAMHGMRGLS VFISDIRNCQ NKEQERQRID KELGNVRNRF KNEKGLSPYE KKKYVWKMLY
IYMLGYDVDF GHMEAVSLIS APKYPEKQVG YIVTSCLLNE NHDFLRLAIN TVRNDIIGRN
ETFQCLALTM VGNIGGREFA ESLAPDVQKL LLSSSCRPLV RKKAALCLLR LYRKNPDVVN
VDGWADRMAQ LLDERDLGVL TSSMSLLVAL VSNNHEAYWS CLPKCVKTLE RLARNQDIPQ
EYTYYGIPSP WLQVKTMRAL QYFPTIEDPY TRRTLFEVLQ RILMGTDVVK NVNKNNASHA
VLFEALALVM HLDAEKEMMS QCVALLGKFI AVREPNIRYL GLENMTRMLM VTDAQEIIKR
HQAQIITSLK DPDISIRRRA LDLLYGMCDV TNAKDIVEEL LQYLSSADFT MREELSLKAA
ILAEKFAPDL SWYVDVILQL IDKAGDFISD DIWFRVVQFV TNNDDLQPYA AAKVKEYLEK
PAVHETMVKV SAYILGEYSH LLARRPGCSP KEIFGILHEK LPTVSTTTIP ILLSAYAKIL
MHTQPPDQEL QSQIWAIFNK YESCIDAEIQ QRAVEYFALC QKGAALMDIL AEMPKFPERK
SSLIKRAEYS EADTAEQSAI KLRAQQQPSN ALVVTDQPPA NGATSPVPVG QLSLAMVPSM
ITTEDHTSTD PASSQQNGSL TKVDPQHPSA DLLGDLLGPL AIEGPPGATV QSEHNAVSRL
EGGPDAVDGS AIVPVEEQRN TVQPIGNIAE RFHALCLKDS GVLYEDPYIQ IGIKAEWRAH
HGRLVLFLGN KNTAPLVSVQ ALMLPPAHLK MELSLVPDTI PPRAQVQCPL EVVNLRPSRD
VAVLDFSYKF GTNMVNVKLR LPAVLNKFLQ PIPVPAEEFF PQWRSLSGPP LKLQEVVRGV
RPMPLPEMAN LLNSFRLMIC PGLDPNPNNL VASTTFYSES THAMLCLIRI ETDPADRTQL
RMTLASGDPT LTFELKEFIK EQLISIPTAP PQSPAPAPAP APPPAAQATP QIPPNDPAAL
LAGLLS
//
