(data stored in SCRATCH zone)

SWISSPROT: Q4W9N5_ASPFU

ID   Q4W9N5_ASPFU            Unreviewed;       939 AA.
AC   Q4W9N5;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 97.
DE   RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN   ORFNames=AFUA_4G04310 {ECO:0000313|EMBL:EAL84578.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL84578.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL84578.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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: Cytoplasm {ECO:0000256|SAAS:SAAS00556307}.
CC       Membrane, coated pit {ECO:0000256|PIRNR:PIRNR037091}.
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:EAL84578.1}.
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DR   EMBL; AAHF01000016; EAL84578.1; -; Genomic_DNA.
DR   RefSeq; XP_746616.1; XM_741523.1.
DR   STRING; 746128.CADAFUBP00009592; -.
DR   EnsemblFungi; EAL84578; EAL84578; AFUA_4G04310.
DR   GeneID; 3504000; -.
DR   KEGG; afm:AFUA_4G04310; -.
DR   EuPathDB; FungiDB:Afu4g04310; -.
DR   HOGENOM; HOG000170596; -.
DR   InParanoid; Q4W9N5; -.
DR   KO; K11824; -.
DR   OMA; HNELFNC; -.
DR   OrthoDB; 751651at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
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; 1.25.10.10; -; 1.
DR   Gene3D; 3.30.310.10; -; 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   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; SSF48371; 1.
DR   SUPFAM; SSF49348; SSF49348; 1.
DR   SUPFAM; SSF55711; SSF55711; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4W9N5.
DR   SWISS-2DPAGE; Q4W9N5.
KW   Coated pit {ECO:0000256|PIRNR:PIRNR037091};
KW   Endocytosis {ECO:0000256|PIRNR:PIRNR037091};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037091, ECO:0000256|SAAS:SAAS00468874};
KW   Protein transport {ECO:0000256|PIRNR:PIRNR037091,
KW   ECO:0000256|SAAS:SAAS00299732};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transport {ECO:0000256|PIRNR:PIRNR037091, ECO:0000256|SAAS:SAAS00468876}.
FT   DOMAIN          694..805
FT                   /note="Alpha_adaptinC2"
FT                   /evidence="ECO:0000259|SMART:SM00809"
FT   BINDING         37
FT                   /note="Phosphatidylinositol lipid headgroup"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT   BINDING         46
FT                   /note="Phosphatidylinositol lipid headgroup"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT   BINDING         50
FT                   /note="Phosphatidylinositol lipid headgroup"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT   BINDING         51
FT                   /note="Phosphatidylinositol lipid headgroup"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT   BINDING         54
FT                   /note="Phosphatidylinositol lipid headgroup"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
SQ   SEQUENCE   939 AA;  105542 MW;  8BD15D194B2F37DD CRC64;
     MSSMRGLVQF IADLRNARAR ELEEKRVNKE LANIRQKFKA GNLNGYQKKK YVCKLLYVYI
     QGYDVDFGHL EAVNLISSNK YSEKQIGYLA VTLFLHEQHE LLHLVVNSIR KDLLDNNELF
     NCLALHAVAN VGGREMGEAL STDVHRLLIS PTSKAFVKKK AALTLLRLYR KYPGIVQNEW
     AERMISLMDD PDMGVTLSVT SLIMALAQDR PEEYKGSYIK AAQRLKRIVV DNEIAPDYLY
     YRVPCPWIQV KLLRLLQYYP PSQDSHVREI IRASLQQIMT TAMDTPKNVQ QNNAQNAILF
     EAINLLIHLD TEHNLMMQIS SRLGKYIQSR ETNVRYLGLE AMTHFAARAE TLDPIKKHQN
     IILGSLRDRD ISVRRKGLDL IYSMCDTTNA APIVNELLRY LQTADYAIRE EMVLKVAILT
     EKYATDAQWY IDITLKLLSL AGDHVNDEVW QRVIQIVTNN EELQAYAAHT LLGYLKTDCH
     ESLVKIGCYV LGEFGHLIAD NEGSSPIEQF LALQGKMITS NDNTRAMILS SFIKFVNLFP
     EIKPQLLHIF RLYSHSPDTE LQQRAFEYLT LATLPTDDLL RTVCDEMPPF SERTSILLSR
     LHQKTAGTTE KKTWVVGGKD ANADKKEVLL AQNTGLKRTF TTIVNGTKTG ANGSAATSNA
     SGDLAGLDLS APPAPPPNMA SAAHLTPDWE PGYNRLYFAD EGVLFEDAQI QVGLRSEYRG
     HMGVVKIYIS NKSSFAIGSL TTTLDNPAAP NLKIDSKSLP EPSVPAAGQT QQTLLVEAHG
     PFSDAPTIRI SYLAGALQAY TLQLPVLMHR YMEPSTLSAE EFFKRWRQIG GPPLEAQHTF
     GVTAKAKNVS ETFTRRLVEG FHWRILENVD PNPNNIVGCA VYQSHGGKTG CLLRLEPNYE
     RKMFRVTIRA TQEAVPQALA KQMEQKLAQG APDEMFGSR
//

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