ID   AAGAB_RAT               Reviewed;         315 AA.
AC   Q9R0Z7;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Alpha- and gamma-adaptin-binding protein p34;
GN   Name=Aagab; Synonyms=P34;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, IDENTIFICATION IN AP-1 AND
RP   AP-2 COMPLEXES, AND SUBUNIT.
RC   TISSUE=Brain;
RX   PubMed=10477754; DOI=10.1083/jcb.146.5.993;
RA   Page L.J., Sowerby P.J., Lui W.W.Y., Robinson M.S.;
RT   "Gamma-synergin: an EH domain-containing protein that interacts with gamma-
RT   adaptin.";
RL   J. Cell Biol. 146:993-1004(1999).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-311, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: May be involved in endocytic recycling of growth factor
CC       receptors such as EGFR. {ECO:0000250}.
CC   -!- SUBUNIT: Associated with AP-1 and AP-2 complexes.
CC       {ECO:0000269|PubMed:10477754}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10477754}.
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DR   EMBL; AF178669; AAD51852.1; -; mRNA.
DR   RefSeq; NP_599225.1; NM_134398.2.
DR   AlphaFoldDB; Q9R0Z7; -.
DR   SMR; Q9R0Z7; -.
DR   BioGRID; 251245; 2.
DR   MINT; Q9R0Z7; -.
DR   STRING; 10116.ENSRNOP00000011385; -.
DR   iPTMnet; Q9R0Z7; -.
DR   PhosphoSitePlus; Q9R0Z7; -.
DR   jPOST; Q9R0Z7; -.
DR   PaxDb; Q9R0Z7; -.
DR   PeptideAtlas; Q9R0Z7; -.
DR   Ensembl; ENSRNOT00000011385; ENSRNOP00000011385; ENSRNOG00000008424.
DR   GeneID; 171435; -.
DR   KEGG; rno:171435; -.
DR   UCSC; RGD:621601; rat.
DR   CTD; 79719; -.
DR   RGD; 621601; Aagab.
DR   eggNOG; KOG4273; Eukaryota.
DR   GeneTree; ENSGT00390000007218; -.
DR   HOGENOM; CLU_056826_0_0_1; -.
DR   InParanoid; Q9R0Z7; -.
DR   OMA; VTAFWKA; -.
DR   OrthoDB; 1618204at2759; -.
DR   PhylomeDB; Q9R0Z7; -.
DR   PRO; PR:Q9R0Z7; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000008424; Expressed in frontal cortex and 18 other tissues.
DR   Genevisible; Q9R0Z7; RN.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019341; Alpha/Gamma-adaptin-bd_p34.
DR   PANTHER; PTHR14659; PTHR14659; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..315
FT                   /note="Alpha- and gamma-adaptin-binding protein p34"
FT                   /id="PRO_0000058137"
FT   REGION          201..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         311
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   315 AA;  34363 MW;  7330E91679945A9D CRC64;
     MAAGVPCALV TSCSATFTGD RLVQHILGTE DAVVEATSSD AVRFYPWTID NKYYSAEVNL
     CVVPSKCRVT AEIAEAVQAF VVYFDSTQKS GLDSVSSWLP LAETWLPEVM ILVCDRVCED
     GINRQQAQEW CIKHGFELVE LCPEELPEED DDFPESTGVK RIVQALNANV WSNVVMKNDR
     SQGFSLLNSL AGASRSVGSA ESCQCEQEPS PTAERTESLP GHRSGACGPA GAQVDSIVDP
     MLDLDIQELA SLTTGGGDLE NFERLFSKLK EMKDKAATLP HEQRKLHAEK VAKAFWMAIG
     GDRDEIEGLS SDDEH