ID A0A3Q1IJB1_ANATE Unreviewed; 480 AA.
AC A0A3Q1IJB1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000020375.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000020375.2}
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 AlphaFoldDB; A0A3Q1IJB1; -.
DR STRING; 64144.ENSATEP00000020375; -.
DR Ensembl; ENSATET00000020728.2; ENSATEP00000020375.2; ENSATEG00000014209.2.
DR GeneTree; ENSGT00390000017955; -.
DR InParanoid; A0A3Q1IJB1; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000265040; 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; 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; PS01089; CAP_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000265040}.
FT DOMAIN 312..446
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 214..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 53337 MW; 7F5DCB2B1E44E6B7 CRC64;
MEDLMQRLER AVTRMEQMSI TMQASSGMAN GDCVNGINGG KSCLEAFDVL LGGPVSDYLN
HSQAIGSEVE KHAEMVNHAL QTQRAFLKLA ATHQEPTELH DLLKPISDHI HEIQNFRERN
RGSSFFNHLS AVSESIPALG WIAVTQRPGP YVKEMNDAAT FYTNRVLKDY KETDRRHVDW
VRSYLSIWTE MQSFIKQHHT TGLAWSKSGP IAPSSLFDPP AAPSAPCPPP PPGPPPVFTD
DDPLPQTGSA GAQHSALFAQ LNQGMDITKG LKRVSDDQKT HKNPNLRTHG TPTKNKAPGA
VSSQKAAVQK RPPLLELEGK KWRVEYFEQK HDLIIEETEL KQVVYVFSCN NSTLQIKGKI
NSIIVDNCKK LGLVFENVVG IVEIINSKAI QLQVLGAVPT ISINKTEGCQ VYLSKDSLNC
DIVSAKSSEM NIMVPEGDDD YREFPVPEQF KTVWDGSKLV TEPTEIGRLR PPGKKQWKKD
//
