ID A0A3Q7RBK9_VULVU Unreviewed; 475 AA.
AC A0A3Q7RBK9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN Name=CAP1 {ECO:0000313|RefSeq:XP_025839487.1,
GN ECO:0000313|RefSeq:XP_025839488.1, ECO:0000313|RefSeq:XP_025839490.1,
GN ECO:0000313|RefSeq:XP_025839491.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025839491.1};
RN [1]
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025839488.1,
RC ECO:0000313|RefSeq:XP_025839490.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025839488.1,
RC ECO:0000313|RefSeq:XP_025839490.1};
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025839487.1, ECO:0000313|RefSeq:XP_025839491.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025839487.1,
RC ECO:0000313|RefSeq:XP_025839491.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025839487.1,
RC ECO:0000313|RefSeq:XP_025839491.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_025839487.1; XM_025983702.1.
DR RefSeq; XP_025839488.1; XM_025983703.1.
DR RefSeq; XP_025839490.1; XM_025983705.1.
DR RefSeq; XP_025839491.1; XM_025983706.1.
DR STRING; 9627.ENSVVUP00000006693; -.
DR Ensembl; ENSVVUT00000008912; ENSVVUP00000006693; ENSVVUG00000005182.
DR KEGG; vvp:112908236; -.
DR OMA; KSQQTHK; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000286640; Unplaced.
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; 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: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; PS01088; CAP_1; 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:UP000286640};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 313..453
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 214..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..318
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 COMPBIAS 298..312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 51438 MW; 8614A3FC9122E69E CRC64;
MADMQKLVER LERAVGRLEA VSHASDMHCG YGDSAPKAGA APYVQAFDSL LAGPVAEYLK
ISKEIGGDVQ KHAEMVHTGL KLERALLVTA SQCQQPAGNK LSDLLAPISE QIQEVITFRE
KNRGSKLFNH LSAVSESIQA LGWVAMAPKP GPYVKEMNDA AMFYTNRVLK EYKDVDKKHV
DWVKAYLSIW TELQAYIKEF HTTGLAWSKT GPVAQELSGL PSGPSAGSGP PPPPPGPPPP
PVPTSSGSDE SASRSALFAQ INQGESITHA LKHVSDDMKT HKNPALKAQS GPVRSGPKPF
SAPKPGVSPS PKPTAKKEPA VLELEGKKWR VENQENVSNL VIDDTELKQV AYIYKCVNTT
LQIKGKINSI TVDNCKKLGL VFDDVVGIVE IINSRDVKVQ VMGKVPTISI NKTDGCHVYL
SKNSLDCEIV SAKSSEMNVL IPTEGGDYNE FPVPEQFKTL WNGQKLVTTV TEIAG
//
