ACAP1_ARATH
ID ACAP1_ARATH Reviewed; 476 AA.
AC O65902;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Cyclase-associated protein 1;
DE Short=AtCAP1;
DE AltName: Full=Adenylyl cyclase-associated protein;
GN Name=CAP1; OrderedLocusNames=At4g34490; ORFNames=T4L20.70;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=11826305; DOI=10.1105/tpc.010301;
RA Barrero R.A., Umeda M., Yamamura S., Uchimiya H.;
RT "Arabidopsis CAP regulates the actin cytoskeleton necessary for plant cell
RT elongation and division.";
RL Plant Cell 14:149-163(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17635992; DOI=10.1242/jcs.007302;
RA Deeks M.J., Rodrigues C., Dimmock S., Ketelaar T., Maciver S.K., Malho R.,
RA Hussey P.J.;
RT "Arabidopsis CAP1 - a key regulator of actin organisation and
RT development.";
RL J. Cell Sci. 120:2609-2618(2007).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17538023; DOI=10.1091/mbc.e06-11-1041;
RA Chaudhry F., Guerin C., von Witsch M., Blanchoin L., Staiger C.J.;
RT "Identification of Arabidopsis cyclase-associated protein 1 as the first
RT nucleotide exchange factor for plant actin.";
RL Mol. Biol. Cell 18:3002-3014(2007).
CC -!- FUNCTION: Actin monomer binding protein that accelerates the exchange
CC of ADP for ATP. Regulates the pool of unpolymerized ATP-actin. Key
CC intermediate between actin-depolymerizing factor (ADF)-mediated
CC disassembly and the profilin-based nucleation and elongation machinery.
CC {ECO:0000269|PubMed:11826305, ECO:0000269|PubMed:17538023,
CC ECO:0000269|PubMed:17635992}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves, stems,
CC flowers, pollen and shoots. Not detected in siliques.
CC {ECO:0000269|PubMed:11826305, ECO:0000269|PubMed:17538023}.
CC -!- DOMAIN: The C-terminal domain (318-476) binds to actin.
CC {ECO:0000269|PubMed:11826305}.
CC -!- DISRUPTION PHENOTYPE: Stunted growth and reduced pollen germination and
CC growth. {ECO:0000269|PubMed:17635992}.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR EMBL; AB014759; BAA28621.1; -; mRNA.
DR EMBL; AL023094; CAA18828.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80166.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86385.1; -; Genomic_DNA.
DR EMBL; BT029161; ABJ17096.1; -; mRNA.
DR PIR; T05269; T05269.
DR RefSeq; NP_195175.1; NM_119614.6.
DR AlphaFoldDB; O65902; -.
DR SMR; O65902; -.
DR STRING; 3702.AT4G34490.1; -.
DR iPTMnet; O65902; -.
DR MetOSite; O65902; -.
DR PaxDb; O65902; -.
DR PRIDE; O65902; -.
DR ProteomicsDB; 244636; -.
DR DNASU; 829600; -.
DR EnsemblPlants; AT4G34490.1; AT4G34490.1; AT4G34490.
DR GeneID; 829600; -.
DR Gramene; AT4G34490.1; AT4G34490.1; AT4G34490.
DR KEGG; ath:AT4G34490; -.
DR Araport; AT4G34490; -.
DR TAIR; locus:2139539; AT4G34490.
DR eggNOG; KOG2675; Eukaryota.
DR HOGENOM; CLU_015780_1_0_1; -.
DR InParanoid; O65902; -.
DR OMA; LDGNKWI; -.
DR PhylomeDB; O65902; -.
DR PRO; PR:O65902; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65902; baseline and differential.
DR Genevisible; O65902; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:TAIR.
DR GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:TAIR.
DR GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0045761; P:regulation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
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; IPR036223; CAP_C_sf.
DR InterPro; IPR018106; CAP_CS_N.
DR InterPro; IPR036222; CAP_N_sf.
DR InterPro; IPR006599; CARP_motif.
DR PANTHER; PTHR10652; PTHR10652; 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.
PE 2: Evidence at transcript level;
KW Actin-binding; Reference proteome.
FT CHAIN 1..476
FT /note="Cyclase-associated protein 1"
FT /id="PRO_0000424560"
FT DOMAIN 316..453
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 224..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..246
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 50970 MW; 8A31948D7F7557A9 CRC64;
MEEDLIKRLE AAVTRLEGIS SNGGGVVSLS RGGDFSSAAG IDIASSDPSI LAYEDLISQC
VGRALTAAEK IGGPVLDVTK IVAEAFASQK ELLVRIKQTQ KPDLAGLAGF LKPLNDVTMK
ANAMTEGKRS DFFNHLKAAC DSLSALAWIA FTGKDCGMSM PIAHVEESWQ MAEFYNNKVL
VEYRNKDADH VEWAKALKEL YLPGLREYVK SHYPLGPVWN ASGKPASAPA KGPPGAPAPP
PAPLFSAESS KPSSSSNQKQ GMSAVFQQLS SGAVTSGLRK VTDDMKTKNR ADRSGAVSAV
EKETRTSKPA FSKTGPPKME LQMGRKWAVE NQIGKKDLVI SECDSKQSVY IYGCKDSVLQ
IQGKVNNITI DKCTKVGVVF TDVVAAFEIV NCNNVEVQCQ GSAPTVSVDN TTGCQLYLNK
DSLETAITTA KSSEINVMVP GATPDGDWVE HALPQQYNHV FTEGKFETTP VSHSGA
