ID A4HT27_LEIIN Unreviewed; 961 AA.
AC A4HT27; A0A2K4YLP3; A0A381MA74;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN ORFNames=LINJ_07_0060 {ECO:0000313|EMBL:CAM65571.1};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM65571.1, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CAM65571.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM65571.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CAM65571.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM65571.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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|PIRNR:PIRNR037091}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000256|PIRNR:PIRNR037091}.
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DR EMBL; FR796439; CAM65571.1; -; Genomic_DNA.
DR RefSeq; XP_001463218.1; XM_001463181.1.
DR AlphaFoldDB; A4HT27; -.
DR SMR; A4HT27; -.
DR STRING; 5671.A4HT27; -.
DR GeneID; 5066626; -.
DR KEGG; lif:LINJ_07_0060; -.
DR VEuPathDB; TriTrypDB:LINF_070005500; -.
DR eggNOG; KOG1077; Eukaryota.
DR InParanoid; A4HT27; -.
DR OMA; PVLMHRY; -.
DR OrthoDB; 123661at2759; -.
DR Proteomes; UP000008153; Chromosome 7.
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 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 PANTHER; PTHR22780; ADAPTIN, ALPHA/GAMMA/EPSILON; 1.
DR PANTHER; PTHR22780:SF4; AP-2 COMPLEX SUBUNIT ALPHA; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR PIRSF; PIRSF037091; AP2_complex_alpha; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Coated pit {ECO:0000256|PIRNR:PIRNR037091};
KW Endocytosis {ECO:0000256|PIRNR:PIRNR037091};
KW Membrane {ECO:0000256|PIRNR:PIRNR037091};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR037091};
KW Reference proteome {ECO:0000313|Proteomes:UP000008153};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 23..595
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT REGION 648..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4..5
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 37
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 47
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 51..55
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 961 AA; 107546 MW; CE3702F8200AB0D3 CRC64;
MDMRGLAHFI RDIRRATGNK KEEESRVDEE LAKIRAKFIE TSTMTTYDRK KYVCKLMFIS
MLGYPITFGH IEGLKLMSQE SPSAKLIGYL STSVLLNENS DLLTLTTHTV YRDLLSASDL
SRSLALTAVA NTGSRDFVEV MHEGVFSIIM DDSVNQHVHK KALLTLLHIY RKYPEIVDLN
TVIPKAAELL LSKQDGVSMC AVTFLNGCIS KESRHLYRGI PDKLIQVLAR IILEKQTEPG
YVYYGVPAPW LQAKLLRLLQ YFPLPSEADQ RHRIILVLRK VVKATEKVLK DAQAQQKQRG
TQSRVSAMNA VLFEVVSLCI QWDVGSKLIL ECVALISSFL SDKRESNLRY IGLSLLARLS
FVDVPGFDFH MHCRQHQQQI IVGLHDSDAS IRKKALDVLV AMCNRSTADD IIKELISYLP
IAADPNFKTS LVLSIALLSE KYCKDYNVYV DIMLTVVSEA GDLCPPDIVH RVVQVVVNDP
SVQKRAANIV FQELRKKTNV PEVMLRVAAF VLGEFGYQIA LNAESTPMVQ LNLLTQKLSF
TSVVTQSIII STFFKFYTLY DDVAVRERIV KTLQAYTNSP HPELQQRATE FIALVEFARS
ELLEKVFEPM PPFRDDVNTV MDQVKRLQSS VQDIWALKIL ERGVEDVNHT GKRKSKSESA
EKQKVQAKQG ITLHDLSTVS TAAPVQGDST DQAYAELDAL LDVSLSSQDV DRVRSVYEEH
RRRLFELSRA EKGVLFSNES IELQCTKSTY GADTRMTVVV RDKTGKGLVQ VAVEVIRAEA
GLILQSRTKD GTTVAAWGTI AIEFAARSCF AFRSPPSVRV QYAPASGSAR VCTDVLSLPI
LPMTFFTPYQ VDSDANFSRL YETTRRASTF AGWRKEASPS ARVDANALMQ LLELQGYRTK
VTGLGAIVGA AAFAVQPKER VEYVPVVCEI QTSASEMQVF VYTESSVLQH GALDTIKFAL
Q
//
