ID A0A1E3P1H1_WICAA Unreviewed; 451 AA.
AC A0A1E3P1H1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|ARBA:ARBA00072052};
DE Flags: Fragment;
GN ORFNames=WICANDRAFT_31743 {ECO:0000313|EMBL:ODQ59178.1};
OS Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL
OS Y-366-8) (Yeast) (Hansenula anomala).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Phaffomycetales; Wickerhamomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=683960 {ECO:0000313|EMBL:ODQ59178.1, ECO:0000313|Proteomes:UP000094112};
RN [1] {ECO:0000313|EMBL:ODQ59178.1, ECO:0000313|Proteomes:UP000094112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8
RC {ECO:0000313|Proteomes:UP000094112};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- FUNCTION: The N-terminal domain binds to adenylyl cyclase, thereby
CC enabling adenylyl cyclase to be activated by upstream regulatory
CC signals, such as Ras. The C-terminal domain is required for normal
CC cellular morphology and growth control.
CC {ECO:0000256|ARBA:ARBA00054756}.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659}.
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DR EMBL; KV454211; ODQ59178.1; -; Genomic_DNA.
DR RefSeq; XP_019038385.1; XM_019181875.1.
DR AlphaFoldDB; A0A1E3P1H1; -.
DR STRING; 683960.A0A1E3P1H1; -.
DR GeneID; 30199121; -.
DR OrthoDB; 77251at2759; -.
DR Proteomes; UP000094112; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR GO; GO:0000935; C:division septum; IEA:EnsemblFungi.
DR GO; GO:0035838; C:growing cell tip; IEA:EnsemblFungi.
DR GO; GO:0003779; F:actin binding; IEA:EnsemblFungi.
DR GO; GO:0008179; F:adenylate cyclase binding; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:EnsemblFungi.
DR GO; GO:0051014; P:actin filament severing; IEA:EnsemblFungi.
DR GO; GO:0010619; P:adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0019933; P:cAMP-mediated signaling; IEA:TreeGrafter.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:EnsemblFungi.
DR GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IEA:EnsemblFungi.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:EnsemblFungi.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:EnsemblFungi.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:EnsemblFungi.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:EnsemblFungi.
DR FunFam; 1.25.40.330:FF:000001; Adenylyl cyclase-associated protein; 1.
DR Gene3D; 2.160.20.70; -; 1.
DR Gene3D; 1.25.40.330; Adenylate cyclase-associated CAP, N-terminal domain; 1.
DR InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR036223; CAP_C_sf.
DR InterPro; IPR053950; CAP_N.
DR InterPro; IPR036222; CAP_N_sf.
DR InterPro; IPR006599; CARP_motif.
DR PANTHER; PTHR10652; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR10652:SF0; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR Pfam; PF08603; CAP_C; 1.
DR Pfam; PF21938; CAP_N; 1.
DR SMART; SM00673; CARP; 2.
DR SUPFAM; SSF69340; C-terminal domain of adenylylcyclase associated protein; 1.
DR SUPFAM; SSF101278; N-terminal domain of adenylylcyclase associated protein, CAP; 1.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000094112}.
FT DOMAIN 292..429
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 170..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..197
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..277
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ODQ59178.1"
SQ SEQUENCE 451 AA; 48678 MW; 6C704E7DAAE67223 CRC64;
TIPASVKGFS DFLELYIDPF VSLSNETNPL VGQQATNFAK AFQFQAKLIK AATKSKKPDF
SNPNIVALLK PLQDDVAQIN QFKDDNRSSE VFSHLNAIAE GTGVLSWFLT ETPVSFIPDI
KDSATFWTNK VLKQFKELDQ SHVEWVKQFL GIFDGLKLYV KQYHTEGLSW NSSGDNDISS
SVQSEKSVPV PSAAPSAGGP PPPPPPPPAD IFADDGAKGS SNAVPPPSGG LDAVFSELNK
GEGITKGLKK VEKSQMTHKN PELRKTGSTS STSSRKSPPA KPKKPSSLSL KPKPEPVVEL
RDSKWIIKNV EGDHGIVING EIDQSIFIAD SKDATIQVKG KVNAVSISST TKVGLVVESL
ISGIDVINSK KFGIQVLDKV PQISVDKSDE GQIYLSRSSL ETEVYTSSTT ALNINVPDDA
NDDFKEISVP EQFKHTFTSG KISSTIVEHA G
//
