ID A0A196S472_BLAHN Unreviewed; 914 AA.
AC A0A196S472;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN ORFNames=AV274_6389 {ECO:0000313|EMBL:OAO11938.1};
OS Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=478820 {ECO:0000313|EMBL:OAO11938.1, ECO:0000313|Proteomes:UP000078348};
RN [1] {ECO:0000313|EMBL:OAO11938.1, ECO:0000313|Proteomes:UP000078348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50177 / NandII {ECO:0000313|Proteomes:UP000078348};
RA Gentekaki E., Curtis B., Stairs C., Eme L., Herman E., Klimes V.,
RA Arias M.C., Elias M., Hilliou F., Klute M., Malik S.-B., Pightling A.,
RA Rachubinski R., Salas D., Schlacht A., Suga H., Archibald J., Ball S.G.,
RA Clark G., Dacks J., Van Der Giezen M., Tsaousis A., Roger A.;
RT "Nuclear genome of Blastocystis sp. subtype 1 NandII.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adaptins are components of the adaptor complexes which link
CC clathrin to receptors in coated vesicles. Clathrin-associated protein
CC complexes are believed to interact with the cytoplasmic tails of
CC membrane proteins, leading to their selection and concentration.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAO11938.1}.
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DR EMBL; LXWW01000573; OAO11938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A196S472; -.
DR STRING; 478820.A0A196S472; -.
DR OrthoDB; 25313at2759; -.
DR Proteomes; UP000078348; Unassembled WGS sequence.
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:UP000078348};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 677..783
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT REGION 612..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..667
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 103672 MW; 5CB98A8FB69FB470 CRC64;
MALRMRTLKN FINDIKNCQT KEAESTRVMQ ELATIRNSFT SAKLTAADRK KYVWTLVYIY
LLGYEIDFGH MEVITLISSP NFQEKQVGYL AAAVLFKCTD KLFTLIVNSM RNDVINGVEV
NQILALSAVA NLGGRDLAET LLEDILQLVQ KDTTTHLVKQ KCALTLLSLF RSSPDTVGTQ
WIDKVLPMFD IRANIGCALS VSGLLANLIP HIKEEEMIDE IRHISIGVLR TLVLDKVCPE
NYVYYDVPCP WLVVNCLRIL KSCPYPTSKK DVNLLEDALH TILQRNEMTK NRNHDNVTHG
ELFEAVNLII SYGNETDPEL RASVVSYLGR FIMYEEPNIR YLGLDYMSRL AQLSGVSDKI
KKHQDTIMAS LEDPDLAIRK RALHMLFSMC DEENAEEIVK KLLEHLKTPD FLIKEEMALK
TAILAERFPP DNQWYIDVIT DLMLNAGDFV SDDIWHRMVQ IVSQQDDLQE YACHKMFELL
QPTTVHEIMV RAGTYILGEY AELIVEPEIE GNEPVEPEAI LETLQRHYVK VSLNTQTLMM
TAFAKLLVQF EELEDEIREL FEQNLSHIDS EMQQRAVEYN ALADSEIMED VLDQMPPFAE
DRENVLEMKL KAPEEAEEEE EEEDDDDDDD DDDDDDDDDD DDDDDDDDDE EEEEEEEDGE
AEGIDEETEE KLPAWFNKCV TKEKAVLFQD EHLQIGMTKD VQGATARFNL FYTNKSDSTL
KKFSAEVESE ESGLAIEATE CNSTIEAGAK GKQQVTVTCN KPFAESPVLT VSFSCDGTTY
KFPITFPVVG CTFCTPAELD ADTFQQRWSN PKLQEKEAKE TFRAAEDKGI ETLETVLPTL
GFNIVEDVDE SANKVYAAGT FVTSKIAASG KPMTVSVLCL FEWAKAKRAY RLTVRASNET
VATVCEEHLK AQLA
//