ADCA_DICDI
ID ADCA_DICDI Reviewed; 580 AA.
AC Q54CH1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Arrestin domain-containing protein A;
GN Name=adcA; ORFNames=DDB_G0292924;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; AAFI02000197; EAL61011.1; -; Genomic_DNA.
DR RefSeq; XP_629445.1; XM_629443.1.
DR AlphaFoldDB; Q54CH1; -.
DR SMR; Q54CH1; -.
DR IntAct; Q54CH1; 9.
DR STRING; 44689.DDB0233899; -.
DR PaxDb; Q54CH1; -.
DR EnsemblProtists; EAL61011; EAL61011; DDB_G0292924.
DR GeneID; 8628964; -.
DR KEGG; ddi:DDB_G0292924; -.
DR dictyBase; DDB_G0292924; adcA.
DR eggNOG; KOG1729; Eukaryota.
DR HOGENOM; CLU_470470_0_0_1; -.
DR InParanoid; Q54CH1; -.
DR OMA; KNAYFPG; -.
DR PhylomeDB; Q54CH1; -.
DR Reactome; R-DDI-844456; The NLRP3 inflammasome.
DR PRO; PR:Q54CH1; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044354; C:macropinosome; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006972; P:hyperosmotic response; IDA:dictyBase.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IDA:dictyBase.
DR GO; GO:0006979; P:response to oxidative stress; IDA:dictyBase.
DR Gene3D; 2.60.40.640; -; 2.
DR Gene3D; 3.30.40.10; -; 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 InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM01017; Arrestin_C; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..580
FT /note="Arrestin domain-containing protein A"
FT /id="PRO_0000363154"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 468..528
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 31..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 523
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 580 AA; 64537 MW; 45E7E9AECB9431F8 CRC64;
MNYQVTVSGD PELAQESVDF VSSGFGNMSM NVNTTSSHHH HHSNSGNAEV SFNGGFGMPN
MTMEVKETHS GHHHHHSNGG NAEISINSGF GMPSMTMSVT DSNSGHHHHH HKESASVNLS
LGGIVGAVVG AVTGGVMIDG RNRIWVQLNQ SSYVGGDIIS GTIEMDCIVP FFAKGVIVKV
KGFERLWLQE LRTETEGEGS NKRTVYKTID HKENKEFFKS TIVVYPQAGT VNCGHYSFPF
SYQLPSDLPG TFCHDGKDAM GAYSAKILYK CKATVDVAHK HDLKSTTKLI INEKCGELVQ
PSFAENKKSF MLTKGKLHVK TWLNKNAYFP GETLVAKMKA NNTSIKPTRK ISLVVHHTMQ
LKTRLYHRCI TNAIYKQQYD GFQPCFYGKR YLPFSIPVDL KPSSSLGKHI TSSYLLELEC
DIPMAIDLSV TLPLTLFAPQ FLYSTVPSQP PGTPLPPDVS YRHPWEGDEH ATACRKCNKG
FSLFARKHHC RHCMKIFCDK CTSTKTTITK LAYPKPVRVC EECYPIATQG GNKYQSAKLM
AAQYQASLNA YYAQYASLYP QIYPDQQQQQ QQPSAPPQQY
