ID A0A665U0E0_ECHNA Unreviewed; 429 AA.
AC A0A665U0E0;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Cyclase associated actin cytoskeleton regulatory protein 2 {ECO:0000313|Ensembl:ENSENLP00000012639.1};
OS Echeneis naucrates (Live sharksucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Echeneidae; Echeneis.
OX NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000012639.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000012639.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR AlphaFoldDB; A0A665U0E0; -.
DR Ensembl; ENSENLT00000013155.1; ENSENLP00000012639.1; ENSENLG00000005193.1.
DR Proteomes; UP000472264; 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; 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: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; PS01089; CAP_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000472264}.
FT DOMAIN 274..407
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 172..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 47854 MW; 7F2A94E7EADEA2C0 CRC64;
MVSSVEEDYL LTKFINDSNT IYCLQDSNFN FPSPLPHSFV LRYLFFLSCS AVTNPTLQDL
LKPISDHIQE IQSFRERNRG SNLFNHLSAV SESIPALGWV TVCQKPGPYV KEMNDAATFY
TNRVLKDYKE TDRRHVEWVH SYLSIWTEMQ SFIKQHHTTG LVWSKNGPIA PASLFETSDS
SAPCPPPPPP PPGPPPVFTD SDSQPQAGGA AAQHSALFAQ LNQGMDITKG LKHVSDKQKT
HKNPSLRSQS AEIKTKTKSS GTASSSKATI QQRPPLLELE GKKWRVENFE EKHDLLIEET
ELKQVVYVFS CNNSTVQIKG KINSIIIDNC KKLGLVFENV VGIVEIINSK AIQLQVLGKV
PTISINKTEG CQVYLSKDSL SCDIVSAKSS EMNILIPEED DYREFPVPEQ FKTVWDGSKL
VTEPTEIAG
//