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Database: UniProt
Entry: A6RDP5_AJECN
LinkDB: A6RDP5_AJECN
Original site: A6RDP5_AJECN 
ID   A6RDP5_AJECN            Unreviewed;       993 AA.
AC   A6RDP5;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN   ORFNames=HCAG_07753 {ECO:0000313|EMBL:EDN11300.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN11300.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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}.
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DR   EMBL; CH476663; EDN11300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6RDP5; -.
DR   STRING; 339724.A6RDP5; -.
DR   VEuPathDB; FungiDB:HCAG_07753; -.
DR   HOGENOM; CLU_003824_1_0_1; -.
DR   OMA; PVLMHRY; -.
DR   OrthoDB; 123661at2759; -.
DR   Proteomes; UP000009297; 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:UP000009297};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT   TRANSMEM        947..972
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          695..806
FT                   /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT                   Ig-like subdomain"
FT                   /evidence="ECO:0000259|SMART:SM00809"
FT   BINDING         5..6
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         46
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         50..54
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   993 AA;  112415 MW;  DE91F8B8DC4ADA23 CRC64;
     MSSMRGLVQF IADLRNARAR ELEEKRINKE LANIRQKFKD ANLNGYQKKK YVCKLLYVYI
     QGYDIDFGHL EAVNLISANK YSEKQIGYLA VTLFLHEGHE LLHLVVNSIR KDLLDYNELN
     NCLALHAVAN VGGREMGEAL GVDVHRLLIS PTSKAFVKKK AALTLLRLYR KHPGIVQPEW
     AERIISLMDD PDMGVALSVL SLVMALVQDN PERYKGSYAK AAQRLKRIVV DNDIAQDYIY
     YKVPCPWVQV KLLRLLQYYP PSDDTHVRHL IRQSIEEVMH SAMDTPKNAQ QNNAQNAVLF
     EAINLLIHLD TEHNLMMKIS LRLGKFIQSR ETNVRYLGLE AMTHFAARAE TLDPIKHHQD
     IILGSLRDRD ISVRRKGLDL LYSMCDTSNA RPIVNELLKY LQTADYSIRE EMVLKIAILT
     EKYATDAQWY IDISLKLLSL AGDHVSDEVW QRVIQIVTNN EELQAYAAQH LLQYVKGDCH
     DSLVKIGGYI LGEFGHLIAD NKGCSPIEQF LALQNKLNFC SDTTRALLLS SFIKFVNLFP
     EIKPQLLRVF RIYSQSPDSE LQQRACEYLT LATLPTDDLL RTVCDEMPPF SERTSVLLSR
     LHQKSAGISD KRTWVVGGKD ANADKQEVLL AQQTGLKRSF TTIVNGTSSG PKATVAKSTV
     SSDLAGLDMS SSSDGPEPNL ASAAHLSADW EIGFNRLYFK DEGVLFEDAQ IQVGLRSEYR
     VHLGVCKLYF TNKSSFPIGS FTTTLDNPSP QSIKIDSKNL PDPDVQAQSQ TQQTICFESK
     GPFTKPPTIR ISYLAGALQA YTLQLPVLMH KYMDESTLSP DDFFKRWRQI GGPPLEAQST
     FAVQGKGRMI TESFTRGIVQ GFRFRILGGV DPNSKNVVGC AVYQMDGGKT GCLLRLEPNY
     EKKMYRITIR ATQDAVPQAL VKLMEERLAQ GVFYVDVHTT ALTNSYLFIR LALIFSLRFP
     FLFPIPLFRF YVFTFRDLMI LQETHHGLLV RSQ
//
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