ID A0A3Q3AB57_KRYMA Unreviewed; 474 AA.
AC A0A3Q3AB57;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000008339.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000008339.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 ECO:0000256|RuleBase:RU000647}.
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DR RefSeq; XP_017275046.1; XM_017419557.1.
DR AlphaFoldDB; A0A3Q3AB57; -.
DR STRING; 37003.ENSKMAP00000008339; -.
DR Ensembl; ENSKMAT00000008466.1; ENSKMAP00000008339.1; ENSKMAG00000006237.1.
DR GeneID; 108237855; -.
DR KEGG; kmr:108237855; -.
DR CTD; 10486; -.
DR GeneTree; ENSGT00390000017955; -.
DR OMA; HEDRNDL; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000264800; Unplaced.
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; 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; 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 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; PS01088; CAP_1; 1.
DR PROSITE; PS01089; CAP_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT DOMAIN 318..452
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 217..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 52187 MW; 9DD2E00DBD1CF41C CRC64;
MEGLMQRLEQ AVTRLEQMAA AAQLSGSMAN GSCVNGIDGG PTQSVEVFDA LLRGPVSDYL
SCSRAIGGEV EKHAEMVNDA LQTQRTFLKM AATHQEPAQM ELQDLLKPIS DHIQEIQNFR
EQNRGSLLFN HLSAVSESIP ALGWVAVSQK PGPYVKEMND AATFYTNRVL KDYKETDRQH
VDWVRSYLSI WTEVQSFIKQ HHTTGLVWSK TGPIAPASLF DSPPAPSAPC PPPPPPPPGP
PPVFIDDDSK PQEGGAAAQH SALFTQLNQG MDITKGLKHV SDEQKTHKNP NLRSQTSPTK
SKEPRPVKSP KAAVQKRPPL LELEGKKWRV EHFEQKHDLL IEETELKQVV YVFSCNNSTL
QVKGKINSII IDNCKKLGLV FENAVGIVEI INSKAIQLQV LGTVPTISVN KTEGCQIYLS
KDALSCDVVS AKSSEMNILI PDGDDDYKEF PVPEQFKTVW DGSKLVTEPT EIAG
//
