ID A0A556TP97_BAGYA Unreviewed; 469 AA.
AC A0A556TP97;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Adenylyl cyclase-associated protein 2 {ECO:0000313|EMBL:TSK31345.1};
GN ORFNames=Baya_3455 {ECO:0000313|EMBL:TSK31345.1};
OS Bagarius yarrelli (Goonch) (Bagrus yarrelli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Sisoridae; Sisorinae; Bagarius.
OX NCBI_TaxID=175774 {ECO:0000313|EMBL:TSK31345.1, ECO:0000313|Proteomes:UP000319801};
RN [1] {ECO:0000313|EMBL:TSK31345.1, ECO:0000313|Proteomes:UP000319801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JWS20170419001 {ECO:0000313|EMBL:TSK31345.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TSK31345.1};
RX PubMed=31274158;
RA Jiang W., Lv Y., Cheng L., Yang K., Chao B., Wang X., Li Y., Pan X.,
RA You X., Zhang Y., Yang J., Li J., Zhang X., Liu S., Sun C., Yang J.,
RA Shi Q.;
RT "Whole-Genome Sequencing of the Giant Devil Catfish, Bagarius yarrelli.";
RL Genome Biol. Evol. 11:2071-2077(2019).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659}.
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:TSK31345.1}.
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DR EMBL; VCAZ01000009; TSK31345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A556TP97; -.
DR Proteomes; UP000319801; Unassembled WGS sequence.
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; 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; IPR028417; CAP_CS_C.
DR InterPro; IPR018106; CAP_CS_N.
DR InterPro; IPR036222; CAP_N_sf.
DR InterPro; IPR006599; CARP_motif.
DR PANTHER; PTHR10652; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR10652:SF2; ADENYLYL CYCLASE-ASSOCIATED PROTEIN 2; 1.
DR Pfam; PF08603; CAP_C; 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; PS01088; CAP_1; 1.
DR PROSITE; PS01089; CAP_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000319801}.
FT DOMAIN 306..447
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 222..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 51918 MW; A0146AB2F8B95645 CRC64;
MEALVERLEQ AVLRLEAVSA KIHGCSGILS NGEINGYHGE SQCMDAFDHL LRGALSEYMR
NSLTIGGEVA KHAEMVHNAL QVQKAFLKLT TTHQEPAQPE LADLLRPISE QIEQIQNFRE
KNRGSHLFNH LSAVSESIPA LGWVAVNQKP GPYVKEMNDA AIFYTNRVLK DYKDTDPCHV
EWVRSYLSIW TEMQVFIKHH HTTGLVWSKT GPVASSSMLI ATPTTPCPPP PPPPPPAFTD
ECPKPDHSAA QHSALFAQLN QGAAITKGLK HVSDEQKTHK NPALRSQGGT SQASPTKANS
SSLSRPTTAK KSSPVLELEG KKWRVEHQEQ VHDLVIEETE LKQVVYVFSC NNCTLQIKGK
VNSIIVDNCK KLGLVFENVV GIFEIINSKD IRLQVLGKVP TISINKTEGC HVYLSKESLN
CEIVSATSSE MNILLPQDDD DYREFPVPEQ FKTVWDGSKL VTEPTEIAG
//
