CAP_YEAST
ID CAP_YEAST Reviewed; 526 AA.
AC P17555; D6W144;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Adenylyl cyclase-associated protein;
DE Short=CAP;
GN Name=SRV2; Synonyms=CAP1; OrderedLocusNames=YNL138W; ORFNames=N1210, N1838;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2184942; DOI=10.1016/0092-8674(90)90812-s;
RA Field J., Vojtek A., Ballester R., Bolger G., Colicelli J., Ferguson K.,
RA Gerst J., Kataoka T., Michaeli T., Powers S., Riggs M., Rodgers L.,
RA Wieland I., Wheland B., Wigler M.;
RT "Cloning and characterization of CAP, the S. cerevisiae gene encoding the
RT 70 kd adenylyl cyclase-associated protein.";
RL Cell 61:319-327(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2158860; DOI=10.1016/0092-8674(90)90813-t;
RA Fedor-Chaiken M., Deschenes R.J., Broach J.R.;
RT "SRV2, a gene required for RAS activation of adenylate cyclase in yeast.";
RL Cell 61:329-340(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP INTERACTION WITH ABP1, AND SUBCELLULAR LOCATION.
RX PubMed=8552082; DOI=10.1128/mcb.16.2.548;
RA Freeman N.L., Lila T., Mintzer K.A., Chen Z., Pahk A.J., Ren R.,
RA Drubin D.G., Field J.;
RT "A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-
RT associated protein binds SH3 domains and modulates cytoskeletal
RT localization.";
RL Mol. Cell. Biol. 16:548-556(1996).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 368-526.
RX PubMed=15311924; DOI=10.1021/bi049071r;
RA Dodatko T., Fedorov A.A., Grynberg M., Patskovsky Y., Rozwarski D.A.,
RA Jaroszewski L., Aronoff-Spencer E., Kondraskina E., Irving T., Godzik A.,
RA Almo S.C.;
RT "Crystal structure of the actin binding domain of the cyclase-associated
RT protein.";
RL Biochemistry 43:10628-10641(2004).
CC -!- FUNCTION: The N-terminal domain binds to adenylyl cyclase, thereby
CC enabling adenylyl cyclase to be activated by upstream regulatory
CC signals, such as Ras. The C-terminal domain is required for normal
CC cellular morphology and growth control.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P17555; P15891: ABP1; NbExp=9; IntAct=EBI-4024, EBI-2036;
CC P17555; P60010: ACT1; NbExp=7; IntAct=EBI-4024, EBI-2169;
CC P17555; P08678: CYR1; NbExp=5; IntAct=EBI-4024, EBI-5364;
CC P17555; P14126: RPL3; NbExp=3; IntAct=EBI-4024, EBI-15364;
CC P17555; P17555: SRV2; NbExp=3; IntAct=EBI-4024, EBI-4024;
CC P17555; P02994: TEF2; NbExp=3; IntAct=EBI-4024, EBI-6314;
CC P17555; P53250: TWF1; NbExp=3; IntAct=EBI-4024, EBI-19663;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:8552082}. Note=Cortical actin patches.
CC -!- MISCELLANEOUS: Present with 8760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR EMBL; M58284; AAA63569.1; -; mRNA.
DR EMBL; M32663; AAA35094.1; -; Genomic_DNA.
DR EMBL; Z46843; CAA86887.1; -; Genomic_DNA.
DR EMBL; Z71414; CAA96020.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10410.1; -; Genomic_DNA.
DR PIR; A34896; A34896.
DR RefSeq; NP_014261.1; NM_001182976.1.
DR PDB; 1K4Z; X-ray; 2.30 A; A/B=369-526.
DR PDB; 1KQ5; X-ray; 3.00 A; A/B=369-526.
DR PDBsum; 1K4Z; -.
DR PDBsum; 1KQ5; -.
DR AlphaFoldDB; P17555; -.
DR BMRB; P17555; -.
DR SMR; P17555; -.
DR BioGRID; 35688; 697.
DR ComplexPortal; CPX-695; Adenylyl cyclase complex.
DR DIP; DIP-77N; -.
DR IntAct; P17555; 44.
DR MINT; P17555; -.
DR STRING; 4932.YNL138W; -.
DR iPTMnet; P17555; -.
DR MaxQB; P17555; -.
DR PaxDb; P17555; -.
DR PRIDE; P17555; -.
DR EnsemblFungi; YNL138W_mRNA; YNL138W; YNL138W.
DR GeneID; 855584; -.
DR KEGG; sce:YNL138W; -.
DR SGD; S000005082; SRV2.
DR VEuPathDB; FungiDB:YNL138W; -.
DR eggNOG; KOG2675; Eukaryota.
DR GeneTree; ENSGT00390000017955; -.
DR HOGENOM; CLU_015780_1_0_1; -.
DR InParanoid; P17555; -.
DR OMA; LDGNKWI; -.
DR BioCyc; YEAST:G3O-33157-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; P17555; -.
DR PRO; PR:P17555; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P17555; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0003779; F:actin binding; IDA:SGD.
DR GO; GO:0008179; F:adenylate cyclase binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:SGD.
DR GO; GO:0007015; P:actin filament organization; IDA:SGD.
DR GO; GO:0051014; P:actin filament severing; IDA:SGD.
DR GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IDA:SGD.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:SGD.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:ComplexPortal.
DR GO; GO:0007265; P:Ras protein signal transduction; IMP:SGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:SGD.
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; IPR036223; CAP_C_sf.
DR InterPro; IPR028417; CAP_CS_C.
DR InterPro; IPR018106; CAP_CS_N.
DR InterPro; IPR028419; CAP_fungal_type.
DR InterPro; IPR036222; CAP_N_sf.
DR InterPro; IPR006599; CARP_motif.
DR PANTHER; PTHR10652; PTHR10652; 1.
DR PANTHER; PTHR10652:SF0; PTHR10652:SF0; 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 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..526
FT /note="Adenylyl cyclase-associated protein"
FT /id="PRO_0000205706"
FT DOMAIN 369..504
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 1..168
FT /note="Adenyl cyclase-binding"
FT REGION 43..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..361
FT /note="Interaction with SH3 domain of ABP1"
FT REGION 370..526
FT /note="Dimerization and actin-binding"
FT MOTIF 169..369
FT /note="SH3-binding"
FT COMPBIAS 43..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 400..415
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 417..433
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 439..453
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 464..469
FT /evidence="ECO:0007829|PDB:1K4Z"
FT TURN 473..476
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 485..492
FT /evidence="ECO:0007829|PDB:1K4Z"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:1K4Z"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:1K4Z"
SQ SEQUENCE 526 AA; 57521 MW; 0EB4D41205E2D464 CRC64;
MPDSKYTMQG YNLVKLLKRL EEATARLEDV TIYQEGYIQN KLEASKNNKP SDSGADANTT
NEPSAENAPE VEQDPKCITA FQSYIGENID PLVELSGKID TVVLDALQLL KGGFQSQLTF
LRAAVRSRKP DYSSQTFADS LRPINENIIK LGQLKESNRQ SKYFAYLSAL SEGAPLFSWV
AVDTPVSMVT DFKDAAQFWT NRILKEYRES DPNAVEWVKK FLASFDNLKA YIKEYHTTGV
SWKKDGMDFA DAMAQSTKNT GATSSPSPAS ATAAPAPPPP PPAPPASVFE ISNDTPATSS
DANKGGIGAV FAELNQGENI TKGLKKVDKS QQTHKNPELR QSSTVSSTGS KSGPPPRPKK
PSTLKTKRPP RKELVGNKWF IENYENETES LVIDANKDES IFIGKCSQVL VQIKGKVNAI
SLSETESCSV VLDSSISGMD VIKSNKFGIQ VNHSLPQISI DKSDGGNIYL SKESLNTEIY
TSCSTAINVN LPIGEDDDYV EFPIPEQMKH SFADGKFKSA VFEHAG
