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Database: UniProt
Entry: A0A135LAJ9_PENPA
LinkDB: A0A135LAJ9_PENPA
Original site: A0A135LAJ9_PENPA 
ID   A0A135LAJ9_PENPA        Unreviewed;       744 AA.
AC   A0A135LAJ9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=AP complex subunit beta {ECO:0000256|PIRNR:PIRNR002291};
GN   ORFNames=PGRI_048640 {ECO:0000313|EMBL:KXG46008.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG46008.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG46008.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG46008.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
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:PIRNR002291}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000256|ARBA:ARBA00006613, ECO:0000256|PIRNR:PIRNR002291}.
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:KXG46008.1}.
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DR   EMBL; LHQR01000069; KXG46008.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LAJ9; -.
DR   STRING; 5078.A0A135LAJ9; -.
DR   OMA; NPPEVQW; -.
DR   OrthoDB; 648032at2759; -.
DR   Proteomes; UP000070168; Unassembled WGS sequence.
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; Leucine-rich Repeat Variant; 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; ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER; 1.
DR   PANTHER; PTHR11134:SF3; AP COMPLEX SUBUNIT BETA; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   PIRSF; PIRSF002291; AP_complex_beta; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|PIRNR:PIRNR002291};
KW   Protein transport {ECO:0000256|PIRNR:PIRNR002291};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW   Transport {ECO:0000256|PIRNR:PIRNR002291}.
FT   DOMAIN          15..533
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   REGION          638..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   744 AA;  81330 MW;  C617F4B1B5C9D280 CRC64;
     MAMNKIRGAF AVPRKGETFE LRAGLVSQYA YERKESIQKT IMAMTLGKDV SALFPDVLKN
     IATADLEQKK LVYLYLMNYA KSHPDLCILA VNTFVQDSED PNPLIRALAI RTMGCIRVEK
     MVDYMEEPLR KTLRDESPYV RKTAAICVAK LFDLNPTMAL ENGFLETLQE MIGDPNPMVV
     ANSVTALQEI QHTAPETQAL QINSNSLRKM LMALNECTEW GRVTILSTLA EYKTADVKES
     EHICERVAPQ FQHVNSGVVL AAVKAVFLHM KNVNPELSKT YLKKMAPPLV TLVSSAPEVQ
     YVALRNIDLL LQKEPEILNK ELRVFFCKYN DPQYVKFQKL EIMVRIANDR NVDQLLAELK
     EYALEVDMDF VRRAVKAIGQ VAIKIESASE RCVNTLLDLI NTKVNYVVQE AIVVIKDIFR
     KYPGYEGIIP TLCQCIDELD EPNARAALIW IVGEYAEKIS NAGDILGGFV DGFNEEFSST
     QLQILTAVVK LFLKRPEKAQ GLVQRVLQAA TSENDNPDVR DRAYIYWRLL SNTSDSNATK
     NIVLSDKPPI VTTIHSLPTT LLDQLLSELS TLSSVYHKPP EQFVGHGRFG ADAVMRAAIE
     EQIQNARENP LAAAAAAAAG GTTAPAQAQN NVENLLDIDF DGGAPASAQS QPSSGMSGLE
     GLAGTPVRVA SPAAGTPTGQ ASNNLDDLLG VFGDSGAAQP SSGANSGGGA DLMNGFSGLD
     LSGNAGPSQN NQSKKSNEDI LSLF
//
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