(data stored in ACNUC22857 zone)

SWISSPROT: Q6BKZ5_DEBHA

ID   Q6BKZ5_DEBHA            Unreviewed;       740 AA.
AC   Q6BKZ5;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   07-JUN-2017, entry version 83.
DE   RecName: Full=AP complex subunit beta {ECO:0000256|PIRNR:PIRNR002291};
GN   OrderedLocusNames=DEHA2F17622g {ECO:0000313|EMBL:CAG89509.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89509.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89509.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR382138; CAG89509.2; -; Genomic_DNA.
DR   RefSeq; XP_461126.2; XM_461126.1.
DR   ProteinModelPortal; Q6BKZ5; -.
DR   EnsemblFungi; CAG89509; CAG89509; DEHA2F17622g.
DR   GeneID; 2903677; -.
DR   KEGG; dha:DEHA2F17622g; -.
DR   HOGENOM; HOG000163270; -.
DR   InParanoid; Q6BKZ5; -.
DR   OMA; ARASMVW; -.
DR   OrthoDB; EOG092C18N0; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0030121; C:AP-1 adaptor complex; IEA:EnsemblFungi.
DR   GO; GO:0030276; F:clathrin binding; IEA:EnsemblFungi.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IEA:EnsemblFungi.
DR   GO; GO:0006886; P:intracellular protein 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; Q6BKZ5.
DR   SWISS-2DPAGE; Q6BKZ5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Membrane {ECO:0000256|PIRNR:PIRNR002291,
KW   ECO:0000256|SAAS:SAAS00101884};
KW   Protein transport {ECO:0000256|PIRNR:PIRNR002291,
KW   ECO:0000256|SAAS:SAAS00468902};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transport {ECO:0000256|PIRNR:PIRNR002291,
KW   ECO:0000256|SAAS:SAAS00299740}.
FT   DOMAIN       16    544       Adaptin_N. {ECO:0000259|Pfam:PF01602}.
SQ   SEQUENCE   740 AA;  83042 MW;  08CD8FD7892982B5 CRC64;
     MSLEKKIRNF LQGPRKGETF ELKNGLVSQY RGERKDAIQR VIQAMTVGKD VSALFPDVLK
     NIATYDLEQK KLVYLYLMNY AKTHPELCIL AVNTFVQDTE DPNPLIRALA IRTMGCIRVA
     KMVDYMEIPL SRTLKDDNPY VRKTAAICVA KLFDLNSEMC IEFGFLSELS KLIKDPNPMV
     VANALNALFE IKDMNTNPDL EIIEVNKGMV SNLLMCLNEC TEWGRITILT TLNDYKAETS
     NEANHIIERI IPQLQHVNPS VVLSSIKAII NQLDSISVTA QRSSILKKLS APLVSLVSSS
     IPEAQYVGLK NIRIILEKYP QILSKELRVF FIKYSDPLYL KLEKLEIMVR LANDSNSTLL
     LGELKEYAME FESSLVAKAI RSIGTVAIKL TGCVIKSVNL ICSLIDQRGG DLIINESIIV
     LTNILRRYPG KNDLITLIVP IISNHTSELS KNEALSGYIW LLGEYPKYFS QLKQNLSDLI
     DGFLDYESLL QLNILTTIVK INLSIENQTY SNYLQKVLEM ATKDCENADV RDKAYIYWRL
     LSSSSKESQK KIVLSKLPPI KTTIASFNPV VLEALVKELS TLASVYHKPS FTFIDPNLYS
     PLSSDQVTTR RSKSSNKDEN IEDLTNLAKQ EIINNSKNEN LLDFDDDEVK PDNSSSNGSA
     SLLDELNDLF SAPSMPSQAQ PTQPVQSSTN DILDLFKTSA PQSSQQNQNL TQGIDNLNID
     NTSSSSSNQN KLNNDLLDLF
//

If you have problems or comments...

PBIL Back to PBIL home page