ID A0A0E0FPQ7_ORYNI Unreviewed; 868 AA.
AC A0A0E0FPQ7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Beta-adaptin-like protein {ECO:0000256|PIRNR:PIRNR002291};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA01G26360.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA01G26360.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G26360.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA01G26360.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G26360.1};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex that
CC plays a role in protein sorting in the late-Golgi/trans-Golgi network
CC (TGN) and/or endosomes. The AP complexes mediate both the recruitment
CC of clathrin to membranes and the recognition of sorting signals within
CC the cytosolic tails of transmembrane cargo molecules.
CC {ECO:0000256|PIRNR:PIRNR002291}.
CC -!- SUBUNIT: Adaptor protein complexes are heterotetramers composed of two
CC large adaptins (beta-type subunit and alpha-type or delta-type or
CC epsilon-type or gamma-type subunit), a medium adaptin (mu-type subunit)
CC and a small adaptin (sigma-type subunit).
CC {ECO:0000256|PIRNR:PIRNR002291}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000256|ARBA:ARBA00006613, ECO:0000256|PIRNR:PIRNR002291}.
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DR AlphaFoldDB; A0A0E0FPQ7; -.
DR STRING; 4536.A0A0E0FPQ7; -.
DR EnsemblPlants; ONIVA01G26360.1; ONIVA01G26360.1; ONIVA01G26360.
DR Gramene; ONIVA01G26360.1; ONIVA01G26360.1; ONIVA01G26360.
DR eggNOG; KOG1061; Eukaryota.
DR HOGENOM; CLU_006320_4_5_1; -.
DR OMA; ANCMHAL; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0030131; C:clathrin adaptor complex; 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 Gene3D; 3.30.310.10; TATA-Binding Protein; 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; IPR015151; B-adaptin_app_sub_C.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR11134; ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER; 1.
DR PANTHER; PTHR11134:SF4; AP-4 COMPLEX SUBUNIT BETA-1; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF09066; B2-adapt-app_C; 1.
DR PIRSF; PIRSF002291; AP_complex_beta; 2.
DR SMART; SM01020; B2-adapt-app_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002291};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR002291};
KW Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR002291}.
FT DOMAIN 746..863
FT /note="Beta-adaptin appendage C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01020"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 95356 MW; 1626256824BB107E CRC64;
MAPTAPTAAK SASPSQPSGK SEVADLKQQL RQLAGSRAPD ADDQRRDVFK RVISCMTAGI
DVSAAFGEMV LCSATSDVVL KKMCYLYVGV HARNHPDLAL LTINFLQRDC HDQDPTIRGL
ALRSLCSLRV PNLVEYLVSP LATGLKDPSA YVRMIAAVGA AKLYHISATA CLDADLPAAL
KALMLSDPDA QVFGLLVCWP TAGSLFKSVI GGQVVANCMH ALQEIWTLEA AKSEEAAREI
ETLYSKPVVF YLLNRIKEFS EWAQCLVLEL VSNFLPSDNN EIFDIMNLLE DRLQHANGAV
VLATIKVFLH LTMSMTDVHQ QVYERIKAPL LTLVGAGSPE QSYSVLCHLH LLVMRAPMLF
SSDYKSFYCQ FSDPSYVKKL KLEMLTAIAN ESNTYEIVTE LCEYAGNVDV PIARESIRAV
GKIALQQYDV NAIVDRLLQF LEMDKEYVTA ETLVLVKDLL RKYPQWSHDC IAVVGNISSK
NIQEPKGKAA LIWMLGEYSQ DMHDAPYILE SLVENWEEEH SPEVRLHLLT AVMKCFFKRP
PETQMALGAT LTAGLSDTHQ DVHDRALFYY RLLQYDPAVA ERVVNPPKQA VSVFADTQSS
EIKDRIFDEF NSLSVVYQKP SYMFTDKEHR GPFEYSEDLT NLAVGAETTE NTISAQRYQE
SDNDLLLSTS DKEDNATATS NGSSASTYNA PSDLSGPSLL SSQIPSETSL INPGAPTYSS
QSNFSLDDLL GLGVPQASAP PPAPALTLNS KPVLDPGTFQ KKWGQLALSL SQECSLSPQG
AALLMNPQSL IRHMQNNYIQ CIASGGQPPN YKFFFYAQKD GATAFFLVEC IVNTASAKAQ
IKVKADDGTA AEAFSTLFQS ALSKFGLS
//
