ID A0A2I0LQ22_COLLI Unreviewed; 469 AA.
AC A0A2I0LQ22;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN ORFNames=A306_00011637 {ECO:0000313|EMBL:PKK19524.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK19524.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK19524.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK19524.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- FUNCTION: Directly regulates filament dynamics and has been implicated
CC in a number of complex developmental and morphological processes,
CC including mRNA localization and the establishment of cell polarity.
CC {ECO:0000256|ARBA:ARBA00003250}.
CC -!- SUBUNIT: Homodimer. Binds actin monomers.
CC {ECO:0000256|ARBA:ARBA00026058}.
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}.
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:PKK19524.1}.
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DR EMBL; AKCR02000145; PKK19524.1; -; Genomic_DNA.
DR RefSeq; XP_005512871.1; XM_005512814.1.
DR AlphaFoldDB; A0A2I0LQ22; -.
DR STRING; 8932.A0A2I0LQ22; -.
DR GeneID; 102084247; -.
DR KEGG; clv:102084247; -.
DR CTD; 10487; -.
DR InParanoid; A0A2I0LQ22; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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:SF1; ADENYLYL CYCLASE-ASSOCIATED PROTEIN 1; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 310..447
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 204..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..237
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 50803 MW; D9B3FC5858CFC013 CRC64;
MERLVGRLEK AVERLEMMCQ GPGMCGNDSS KGVAQYVQAF DALLAGPVAE YMKISKEVGG
DVQKHAEMVH GGLMSERALL VMASQHQQPA ENALSSLLKP ISEQIQMVQD FREKNRGSKM
FNHLSAVSES IPALGWVAMA PKPGPYVKEM TDAAMFYTNR ILKEYKDVDK KQVDWVKAYL
SIWTELQAYI KEYHTTGLTW SKTGPVATEG AKSPSAPPAG AAPPPPGPPP PPAPAPSSSS
TDDTASRSAL FAQINRGEGI TSGLRHVSDD MKTHKNPALK NQGGPVRSGP KPFTAPKPAC
NANPSQKTSP KAPALLELEG KKWRVENQEN ATNLVISDTE LKQVAYVFKC TNSTLQIKGK
INSITLDNCK KLGLVFDDVV GIVEIINSRD VKVQVMGKVP TISINKTDGC HVYLSKDSLD
CEIVSAKSSE MNVLIPAEGG DFTEFPVPEQ FKTVWNGQKL VTTVTEIAG
//
