ID   PHAF1_RAT               Reviewed;         422 AA.
AC   O08654;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Phagosome assembly factor 1;
GN   Name=Phaf1;
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].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=9480860; DOI=10.1006/bbrc.1998.8142;
RA   Ide N., Hirao K., Hata Y., Takeuchi M., Irie M., Yao I., Deguchi M.,
RA   Toyoda A., Nishioka H., Mizoguchi A., Takai Y.;
RT   "Molecular cloning and characterization of rat lin-10.";
RL   Biochem. Biophys. Res. Commun. 243:634-638(1998).
CC   -!- FUNCTION: Plays a regulatory role in autophagic activity. In complex
CC       with BCAS3, associates with the autophagosome formation site during
CC       both non-selective and selective autophagy.
CC       {ECO:0000250|UniProtKB:Q9BSU1}.
CC   -!- SUBUNIT: Interacts with BCAS3; the interaction is requrired for the
CC       association with the phagophore. {ECO:0000250|UniProtKB:Q9BSU1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BSU1}.
CC       Preautophagosomal structure {ECO:0000250|UniProtKB:Q9BSU1}. Note=The
CC       BCAS3:PHAF1 complex is recruited to the preautophagosomal structures
CC       adjacent to the damaged mitochondria upon mitophagy in a PRKN-PINK1
CC       dependent manner. {ECO:0000250|UniProtKB:Q9BSU1}.
CC   -!- SIMILARITY: Belongs to the PHAF1 family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a lin-10 homolog.
CC       {ECO:0000305|PubMed:9480860}.
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DR   EMBL; U92010; AAB51383.1; -; mRNA.
DR   PIR; JE0239; JE0239.
DR   RefSeq; NP_620609.1; NM_139040.1.
DR   AlphaFoldDB; O08654; -.
DR   STRING; 10116.ENSRNOP00000020003; -.
DR   iPTMnet; O08654; -.
DR   PhosphoSitePlus; O08654; -.
DR   PaxDb; O08654; -.
DR   PRIDE; O08654; -.
DR   GeneID; 207123; -.
DR   KEGG; rno:207123; -.
DR   UCSC; RGD:621098; rat.
DR   CTD; 80262; -.
DR   RGD; 621098; RGD621098.
DR   eggNOG; KOG2819; Eukaryota.
DR   InParanoid; O08654; -.
DR   OrthoDB; 709631at2759; -.
DR   PhylomeDB; O08654; -.
DR   PRO; PR:O08654; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0000407; C:phagophore assembly site; ISS:UniProtKB.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR   GO; GO:0035254; F:glutamate receptor binding; IDA:RGD.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:RGD.
DR   InterPro; IPR005373; PHAF1.
DR   InterPro; IPR039156; PHAF1/BROMI.
DR   PANTHER; PTHR13465; PTHR13465; 1.
DR   PANTHER; PTHR13465:SF2; PTHR13465:SF2; 1.
DR   Pfam; PF03676; UPF0183; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..422
FT                   /note="Phagosome assembly factor 1"
FT                   /id="PRO_0000221085"
SQ   SEQUENCE   422 AA;  47463 MW;  D5E185189FF2E320 CRC64;
     MLDLEVVPER SLGNEQWEFT LGMPLAQAVA ILQKHCRIIK NVQVLYSEQS PLSHDLILNL
     TQDGIKLLFD AFNQRLKVIE VYDLTKVKLK YCGVHFNSQA IAPTIEQIDQ SFGATHPGVY
     NSAEQLFHLN FRGLSFSFQL DSWTEAPKYE PNFAHGLASL QIPHGATVKR MYIYSGNSLQ
     DTKAPMMPLS CFLGNVYAES VDVIRDGTGP SGLRLRLLAA GCGPGVLADA KMRVFERAVY
     FGDSCQDVLS MLGSPHKVFY KSEDKMKIHS PSPHKQVPSK CNDYFFNYFT LGVDILFDAN
     THKVKKFVLH TNYPGHYNFN IYHRCEFKIP LAIKKENAGG QTEICTTYSK WDSIQELLGH
     PVEKPVVLHR SSSPNNTNPF GSTFCFGLQR MIFEVMQNNH IASVTLYGPP RPGAHLRTAE
     LP