ID   CAP_HYDVD               Reviewed;         481 AA.
AC   P40122;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Adenylyl cyclase-associated protein;
DE            Short=CAP;
GN   Name=CAP;
OS   Hydra viridissima (Green hydra) (Chlorohydra viridissima).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Aplanulata; Hydridae; Hydra.
OX   NCBI_TaxID=6082;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7811635; DOI=10.1016/0925-4773(94)90084-1;
RA   Fenger U., Hofmann M., Galliot B., Schaller H.C.;
RT   "The role of the cAMP pathway in mediating the effect of head activator on
RT   nerve-cell determination and differentiation in hydra.";
RL   Mech. Dev. 47:115-125(1994).
CC   -!- FUNCTION: May have a regulatory bifunctional role.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X79567; CAA56104.1; -; mRNA.
DR   PIR; S47091; S47091.
DR   AlphaFoldDB; P40122; -.
DR   SMR; P40122; -.
DR   PRIDE; P40122; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   Gene3D; 1.25.40.330; -; 1.
DR   Gene3D; 2.160.20.70; -; 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; IPR028417; CAP_CS_C.
DR   InterPro; IPR018106; CAP_CS_N.
DR   InterPro; IPR036222; CAP_N_sf.
DR   InterPro; IPR006599; CARP_motif.
DR   PANTHER; PTHR10652; PTHR10652; 1.
DR   Pfam; PF08603; CAP_C; 1.
DR   SMART; SM00673; CARP; 2.
DR   SUPFAM; SSF101278; SSF101278; 1.
DR   SUPFAM; SSF69340; SSF69340; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR   PROSITE; PS01088; CAP_1; 1.
DR   PROSITE; PS01089; CAP_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane.
FT   CHAIN           1..481
FT                   /note="Adenylyl cyclase-associated protein"
FT                   /id="PRO_0000205703"
FT   DOMAIN          319..457
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT   REGION          216..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..240
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  53144 MW;  253617B7915C37A5 CRC64;
     MEQLVSRLEA VTNRLEAVAS RGGGSTIKAA VDDDPAWFDD FKVFNAKFLS GFVNDTIALG
     GELEQMGKFV NEAFHCHLVL MEVAARHNRP SQTDLEGLLK PLSEAISKVQ DFREKNRSSK
     QFNHLSAISE GLPFLGWVGV APKPVLYIQQ MEESAQFYTN KLLKEFRESD PKQANWATSF
     IQLLKGFAAY VKDHHQAGLM WNKEKSAATP AALAVSAHKP PVPPPPSGFA PPPPPPIQAP
     TVTHAVTGSH SSEDSRSQLF AQLSKGSEVT AGLKKVTDDM KTHKNPELRN QPPLKSSALD
     PRPYTPPNLK KFSAPVSKPA KKPALFQLQN KKWVIENQDG NTNLEISECN DKQTVYMYKC
     HASKVHINGK VNSIILDSCE KCVIEFTDVI STFEFTNCKA CKVQIDGFAP TISIEKTDGA
     QVFINPKCLE SQIVTAKSSE MNICVMKPDG DLTEYPLPEQ FKTVWNPATS KFITTTMDLN
     L