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Database: UniProt
Entry: A0A2T7PFF1_POMCA
LinkDB: A0A2T7PFF1_POMCA
Original site: A0A2T7PFF1_POMCA 
ID   A0A2T7PFF1_POMCA        Unreviewed;       654 AA.
AC   A0A2T7PFF1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN   ORFNames=C0Q70_07562 {ECO:0000313|EMBL:PVD32134.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD32134.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD32134.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD32134.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD32134.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC       ECO:0000256|RuleBase:RU000647}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PVD32134.1}.
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DR   EMBL; PZQS01000004; PVD32134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7PFF1; -.
DR   STRING; 400727.A0A2T7PFF1; -.
DR   EnsemblMetazoa; XM_025234084.1; XP_025089869.1; LOC112561529.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg4.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
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; IPR013992; Adenylate_cyclase-assoc_CAP_N.
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; 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; PF01213; 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.
DR   PROSITE; PS01089; CAP_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT   DOMAIN          497..634
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..426
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  69744 MW;  D28A55F057A8117B CRC64;
     MLCCASCRQT SSPSPDRSPT KDANATKKDN GFSDVAIATQ PFSSPSVTQP AQQHLAKADA
     SQSLNLPESK IPISDPLARP VLNPESIGAT HKSASVPSTT ISLNTNLTTP PGPATHVSIT
     PTSMASQVSV KEEALLKEIN KLSETVEKAA AGSGSTGREV ASVYASQLKA LTSQVRKEAG
     SMSESALNIA VSRLEAVAAR LESLTLQGGR GGGTAESDEV AQSIIAYDEF LKGAVAKFIQ
     NSSAIGGDVQ TQAKQVERAF QAQRQFLVAA SKSKQPPQNV LMQLIDPVAK QLTAIQEFRE
     HNRRSEFFNH LSAVSESIAA LGWITVSPAP GPYVKEMTDA GTFYTNRVLK DYKDKDPKHV
     EWARSWISAL TELQAYIKQF HTTGVTWNPK GGNATAAPPA PAAGGVPPPP PPGGPPPPPP
     PPPADLGQKG SSGDDSRAAL FADLNKGSSV TEGLRKVTDD MKTHKNPALR QGPAPFKAAH
     KPSVAAKPAV AAKTKAPERP PLIELQNKKW VVEFHEGNKN IILDQTELKQ VVYIYKCINC
     VVQVKGKVNS ITLDSCKKTA LVFEDVVSSV EFVNCQSMQA QVLGKVPTIS IDKTDGCMVY
     LSNQSLDAEI VTAKSSEMNV LIPAGDGDFK EFALPEQFKT KWNGKEMVTV QTDI
//
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