(data stored in ACNUC22857 zone)

SWISSPROT: A2R7T2_ASPNC

ID   A2R7T2_ASPNC            Unreviewed;       709 AA.
AC   A2R7T2;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=AP complex subunit beta {ECO:0000256|PIRNR:PIRNR002291};
GN   ORFNames=An16g04650 {ECO:0000313|EMBL:CAK42893.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK42893.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G.,
RA   Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K.,
RA   Andersen M.R., Bendtsen J.D., Benen J.A., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G., Debets A.J., Dekker P., van Dijck P.W., van Dijk A.,
RA   Dijkhuizen L., Driessen A.J., d'Enfert C., Geysens S., Goosen C.,
RA   Groot G.S., de Groot P.W., Guillemette T., Henrissat B., Herweijer M.,
RA   van den Hombergh J.P., van den Hondel C.A., van der Heijden R.T.,
RA   van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P.,
RA   van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J., Meulenberg R.,
RA   Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M.,
RA   Pal K., van Peij N.N., Ram A.F., Rinas U., Roubos J.A., Sagt C.M.,
RA   Schmoll M., Sun J., Ussery D., Varga J., Vervecken W.,
RA   van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory
RT   Aspergillus niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Adaptins are components of the adaptor complexes which
CC       link clathrin to receptors in coated vesicles. Clathrin-associated
CC       protein complexes are believed to interact with the cytoplasmic
CC       tails of membrane proteins, leading to their selection and
CC       concentration. {ECO:0000256|PIRNR:PIRNR002291}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000256|PIRNR:PIRNR002291}.
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DR   EMBL; AM270369; CAK42893.1; -; Genomic_DNA.
DR   PaxDb; A2R7T2; -.
DR   EnsemblFungi; CAK42893; CAK42893; An16g04650.
DR   HOGENOM; HOG000163270; -.
DR   Proteomes; UP000006706; Chromosome 5R.
DR   GO; GO:0030117; C:membrane coat; IEA:InterPro.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR026739; AP_beta.
DR   InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   PANTHER; PTHR11134; PTHR11134; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   PIRSF; PIRSF002291; AP_complex_beta; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2R7T2.
DR   SWISS-2DPAGE; A2R7T2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006706};
KW   Membrane {ECO:0000256|PIRNR:PIRNR002291,
KW   ECO:0000256|SAAS:SAAS00468874};
KW   Protein transport {ECO:0000256|PIRNR:PIRNR002291,
KW   ECO:0000256|SAAS:SAAS00299732};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW   Transport {ECO:0000256|PIRNR:PIRNR002291,
KW   ECO:0000256|SAAS:SAAS00468876}.
FT   DOMAIN       19    537       Adaptin_N. {ECO:0000259|Pfam:PF01602}.
SQ   SEQUENCE   709 AA;  78791 MW;  227E1F3A4FE530E2 CRC64;
     MSSSGGDAKL FARGKVAELR QELNSGGKKD KNHSAKKIAL KKIVANMTMS NNDMVALFPD
     VIGCMNLPSL EIKKMCFLFL VNYSRAKPEV ALKALPFLID DMEDSNPLVR ALALRTISYI
     HVREFVEATV QPVKRLMSDM DPYVRKTAAF CVAKLYEHDK KMVEASDLID RLNSMLKDEN
     PTVVSSVLAS LVDIWGRSES ISLTIDYTSA SKLVSILPDC SEWGQSYILE ALMSYVPQDS
     AESLLLAERI APRLSHSNSA VVLTSIRVIL YLMNYIADER HVTSLAKKLS PPLVTLLSKP
     PEVQYLALRN AILILQKRPE VLRNDIRCFF CNYNDPIYVK VTKLELIFML TTKENISVVL
     AELREYATEI DVHFVRKAVR AIGKLAIKIE SAAKQCIDTL LELVNAKIPY IVQEATVVIR
     NIFRKYPNQY ENIIGNVIQN IDELDEPEAK AAIIWIIGQY ADRIENSDGL LQDYLATFHD
     ETVEVQLALL TATVKFFIQR PTKGQQLVPQ VLKWCTEETD DPDLRDRGYM YWRLLSTDPK
     TAKQIVMGEK PPISAESEKL DSRTLEELCL NVGTLATVYL KPVQQVFRSA RTRRLQYSPA
     LQKPKEEPGN AVWQFPAPSQ SSSPTAAMAA SASAPADMNA AVNAADSYFN SVGTQQMAAL
     DLGGREDGGV GGGGAPQTQY VVTQNQQQVY QPQLAGGAAT GNYALLGHE
//

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