ID   APYA_EMENI              Reviewed;         368 AA.
AC   Q6SCL4; C8VI38; Q5B865;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=HECT-type ubiquitin ligase-interacting protein apyA;
DE   AltName: Full=Arrestin and PY motif-containing protein A;
GN   Name=apyA; ORFNames=AN3265;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH HULA.
RX   PubMed=15255903; DOI=10.1111/j.1365-2958.2004.04172.x;
RA   Boase N.A., Kelly J.M.;
RT   "A role for creD, a carbon catabolite repression gene from Aspergillus
RT   nidulans, in ubiquitination.";
RL   Mol. Microbiol. 53:929-940(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: May be involved in signaling by recognizing appropriately
CC       phosphorylated substrates via its arrestin domains and then recruit a
CC       HECT-type ubiquitin ligase such as hulA, leading to ubiquitination of
CC       the substrate, providing a link between ubiquitination and
CC       phosphorylation in protein regulation and stability.
CC       {ECO:0000269|PubMed:15255903}.
CC   -!- SUBUNIT: Interacts with hulA. {ECO:0000269|PubMed:15255903}.
CC   -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR   EMBL; AY460113; AAS16263.1; -; mRNA.
DR   EMBL; AACD01000054; EAA63166.1; -; Genomic_DNA.
DR   EMBL; BN001306; CBF83070.1; -; Genomic_DNA.
DR   RefSeq; XP_660869.1; XM_655777.1.
DR   AlphaFoldDB; Q6SCL4; -.
DR   SMR; Q6SCL4; -.
DR   STRING; 162425.CADANIAP00009794; -.
DR   PRIDE; Q6SCL4; -.
DR   EnsemblFungi; CBF83070; CBF83070; ANIA_03265.
DR   EnsemblFungi; EAA63166; EAA63166; AN3265.2.
DR   GeneID; 2874246; -.
DR   KEGG; ani:AN3265.2; -.
DR   eggNOG; KOG3780; Eukaryota.
DR   HOGENOM; CLU_018982_0_1_1; -.
DR   InParanoid; Q6SCL4; -.
DR   OMA; LKFTMSL; -.
DR   OrthoDB; 430902at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; IGI:UniProtKB.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
DR   GO; GO:0070086; P:ubiquitin-dependent endocytosis; IBA:GO_Central.
DR   Gene3D; 2.60.40.640; -; 1.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR011021; Arrestin-like_N.
DR   InterPro; IPR011022; Arrestin_C-like.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   Pfam; PF00339; Arrestin_N; 1.
DR   SMART; SM01017; Arrestin_C; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..368
FT                   /note="HECT-type ubiquitin ligase-interacting protein apyA"
FT                   /id="PRO_0000395694"
SQ   SEQUENCE   368 AA;  41840 MW;  CCAD1B2A0AA6831E CRC64;
     MALHRLKGHG ANVGNRVGIQ LDKDFVLFQG SEQEALAVYL SGILSLRLKE TTTIKYIRLH
     LRGVRRVSSD TQSSLPARTG RKRFCSENEF YSRTWNFFDG YREAPMTVPA GEYKYPFDVV
     MEGSLPASVE GMKEASISYL FTVEIGRRHG RDITFDKPLR VIRVPDLEPC SHDFALDEVW
     ANKIAYRIGI QNRTVALGTR IDVDYVFAPL LRDMKIAFIE SQLLEVRDLS VEPNDGGSAH
     AARTETIVCS DRYTLGEEYS SKALESYQFS RTLQLPQALG HCVQDTEDMG VRVSHKLKIH
     VRMHNPDGHE SELRLAIPVL IYLSPYYRVW EDSFCGETIP LPETLNPSDE CPPAYGMHEL
     DQLYMPQD