CAP1_BOVIN
ID CAP1_BOVIN Reviewed; 472 AA.
AC Q3SYV4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Adenylyl cyclase-associated protein 1;
DE Short=CAP 1;
GN Name=CAP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC -!- SUBUNIT: Homodimer. Binds actin monomers (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR EMBL; BC103366; AAI03367.1; -; mRNA.
DR RefSeq; NP_001030182.1; NM_001035010.2.
DR RefSeq; XP_005204711.1; XM_005204654.3.
DR RefSeq; XP_005204712.1; XM_005204655.3.
DR AlphaFoldDB; Q3SYV4; -.
DR SMR; Q3SYV4; -.
DR STRING; 9913.ENSBTAP00000017775; -.
DR PaxDb; Q3SYV4; -.
DR PeptideAtlas; Q3SYV4; -.
DR PRIDE; Q3SYV4; -.
DR GeneID; 504519; -.
DR KEGG; bta:504519; -.
DR CTD; 10487; -.
DR eggNOG; KOG2675; Eukaryota.
DR HOGENOM; CLU_015780_1_1_1; -.
DR InParanoid; Q3SYV4; -.
DR OrthoDB; 1098760at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0045761; P:regulation of adenylate cyclase activity; IBA:GO_Central.
DR Gene3D; 1.25.40.330; -; 1.
DR Gene3D; 2.160.20.70; -; 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; IPR028415; CAP1.
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; PTHR10652; 1.
DR PANTHER; PTHR10652:SF1; PTHR10652:SF1; 1.
DR Pfam; PF08603; CAP_C; 1.
DR Pfam; PF01213; CAP_N; 1.
DR SMART; SM00673; CARP; 2.
DR SUPFAM; SSF101278; SSF101278; 1.
DR SUPFAM; SSF69340; SSF69340; 1.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR PROSITE; PS01088; CAP_1; 1.
DR PROSITE; PS01089; CAP_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Cell membrane; Isopeptide bond; Membrane;
KW Methylation; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT CHAIN 2..472
FT /note="Adenylyl cyclase-associated protein 1"
FT /id="PRO_0000271433"
FT DOMAIN 307..450
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 216..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 31
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P40124"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 287
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT CROSSLNK 345
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
SQ SEQUENCE 472 AA; 51273 MW; 8D164F8B19927E67 CRC64;
MADMRNLVER LERVVGRLEA VSHASDTHCG YGDSAAKAGT TPYVQAFDSL LAGPVAEYLK
ISKEIGGDVQ KHAEMVHTGL KLERALLVTA SQCQQPAGNK LSDLLAPISE QIQEVVTFRE
KNRGSKLFNH LSAVSESIQA LGWVAMAPKP GPYVKEMNDA AMFYTNRVLK EYKDVDKKHV
DWVKAYLSIW TELQAYIKEF HTTGLAWSRT GPVAKELSGL PSGPSAGSGP PPPPPGPPPP
PVPTSSGSDD SASRSALFAQ INQGESITHA LKHVSDDMKT HKNPALKAQS GLIRSGPKPF
SASKPDPPKP VAKKEPALLE LEGKKWRVEN QENVSNLMIE DTELKQVAYI FKCVNSTLQI
KGKINSITVD NCKKLGLVFD DVVGIVEIIN SKDVKVQVMG KVPTISINKT DGCHVYLSKN
SLDCEIVSAK SSEMNVLIPT EGGDFNEFPV PEQFKTLWNG QKLVTTVTEI AG
