(data stored in ACNUC22857 zone)

HOGENOM: SCHPO_2_PE248

ID   SCHPO_2_PE248                        STANDARD;      PRT;   683 AA.
AC   SCHPO_2_PE248; O43079;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=AP-1 complex subunit beta-1;AltName: Full=Beta(1)-adaptin;
DE   Short=Beta-1-adaptin;AltName: Full=Clathrin assembly protein complex 1
DE   beta-1 large chain;AltName: Full=Clathrin assembly protein large beta-1
DE   chain; (SCHPO_2.PE248).
GN   Name=apl2; ORFNames=SPBC947.02;
OS   SCHIZOSACCHAROMYCES POMBE.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SCHPO_2.PE248.
CC       Schizosaccharomyces pombe chromosome II EF1 full sequence 1..4539804
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:AP1B1_SCHPO
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. The AP-1 complex interacts directly with clathrin
CC       (By similarity).
CC   -!- SUBUNIT: Assembly protein complex 1 (AP-1) is a heterotetramer
CC       composed of two large adaptins (gamma-type subunit apl4 and beta-
CC       type subunit apl2), a medium adaptin (mu-type subunit apm1) and a
CC       small adaptin (sigma-type subunit aps1). AP-1 interacts with
CC       clathrin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Membrane,
CC       coated pit; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Note=Component of the coat surrounding the
CC       cytoplasmic face of coated vesicles in the plasma membrane (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC   -!- GENE_FAMILY: HOG000163270 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Schizosaccharomyces_pombe;SPBC947.02;SPBC947.02-1;SPBC947.02-1.
DR   UniProtKB/Swiss-Prot; O43079; -.
DR   EMBL; CU329671; CAA17030.1; -; Genomic_DNA.
DR   PIR; T40780; T40780.
DR   RefSeq; NP_595274.1; NM_001021181.1.
DR   ProteinModelPortal; O43079; -.
DR   STRING; O43079; -.
DR   EnsemblFungi; SPBC947.02-1; SPBC947.02-1; SPBC947.02.
DR   GeneID; 2541255; -.
DR   GenomeReviews; CU329671_GR; apl2.
DR   KEGG; spo:SPBC947.02; -.
DR   NMPDR; fig|4896.1.peg.1140; -.
DR   GeneDB_Spombe; SPBC947.02; -.
DR   eggNOG; fuNOG06950; -.
DR   GeneTree; EFGT00050000000022; -.
DR   OMA; EDGEMDK; -.
DR   OrthoDB; EOG49GPQW; -.
DR   PhylomeDB; O43079; -.
DR   ArrayExpress; O43079; -.
DR   GO; GO:0030121; C:AP-1 adaptor complex; IDA:GeneDB_Spombe.
DR   GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IDA:GeneDB_Spombe.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0016197; P:endosome transport; IMP:GeneDB_Spombe.
DR   GO; GO:0070317; P:negative regulation of G0 to G1 transition; IMP:GeneDB_Spombe.
DR   InterPro; IPR016342; AP_complex_bsu.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   PIRSF; PIRSF002291; AP_complex_beta; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   HOGENOMDNA; SCHPO_2.PE248; -.
KW   SPBC947.02cccc7236820036002503210000011;
KW   O43079;
KW   Cell membrane; Coated pit; Complete proteome; Membrane;
KW   Phosphoprotein; Reference proteome.
SQ   SEQUENCE   683 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVPKLFQSSR FKAFKKSETS ELQKGLVSQY AYERIDAVKR TIAAMTVGKD VSSLFPDVLK
     NLATRDITLK KLVYLYLINY AKTHPDLCIL AVNTFVKDSE EYNPTLRALA IRTMGCIRVN
     KIIGYLADPL RKALKDEHPY VRKAAAVCVV KMYDLDREYC ASNGFIEQLQ ALVSDPNPVV
     VANAVRSLAE IHDQDPEKGY FNVVYTMTDR LMVALSECNE WGRITILNSL ARFRTSDIKE
     AEYVCERVVP QFQHANSGVV LSAVKVIMVH IPLFSSDFTD FLYKKMAPPL LTLLSTDSEI
     QYVALRNINL ILQKRPSIFD VKTRVFFCKY NDPLYIKMEK LKIITMLACD ENINETISEL
     RAYVSEVELE FVKQTIKCLG DVALKVPSVI NDCISIFLEI YELNISYMVQ EVTVVMETVL
     RKYPQKIDLL LPYLSRVIEE LGDPRARSSM AWILGEFSHV IPTSSKLLSE MISTMADEDL
     QIQLALLTAV VKLSLMNGKG NDEELVQKVL NYAINQSSNQ DLRDRAFAYQ RLLTPENVRK
     AQKIVCCEKP SVSYNNNLPE ALLDALLCEI TTLASVYHKL PESFIGQGKF GADAIQRRAV
     EELNIEEANV HEAIEKGANV ENLLDLDFTD PGATSASDSP ITSAQPQSGS NSAMDLFMAF
     EAPSTNNAEP VKARSATDDL LGL
//

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