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Adenylyl cyclase-associated protein (CAP)

 CAP_YEAST               Reviewed;         526 AA.
P17555; D6W144;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
25-OCT-2017, entry version 167.
RecName: Full=Adenylyl cyclase-associated protein;
Short=CAP;
Name=SRV2; Synonyms=CAP1; OrderedLocusNames=YNL138W;
ORFNames=N1210, N1838;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2184942; DOI=10.1016/0092-8674(90)90812-S;
Field J., Vojtek A., Ballester R., Bolger G., Colicelli J.,
Ferguson K., Gerst J., Kataoka T., Michaeli T., Powers S., Riggs M.,
Rodgers L., Wieland I., Wheland B., Wigler M.;
"Cloning and characterization of CAP, the S. cerevisiae gene encoding
the 70 kd adenylyl cyclase-associated protein.";
Cell 61:319-327(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=2158860; DOI=10.1016/0092-8674(90)90813-T;
Fedor-Chaiken M., Deschenes R.J., Broach J.R.;
"SRV2, a gene required for RAS activation of adenylate cyclase in
yeast.";
Cell 61:329-340(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8619318; DOI=10.1002/yea.320111210;
Mallet L., Bussereau F., Jacquet M.;
"A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
deaminase gene and 14 new open reading frames.";
Yeast 11:1195-1209(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
INTERACTION WITH ABP1, AND SUBCELLULAR LOCATION.
PubMed=8552082; DOI=10.1128/MCB.16.2.548;
Freeman N.L., Lila T., Mintzer K.A., Chen Z., Pahk A.J., Ren R.,
Drubin D.G., Field J.;
"A conserved proline-rich region of the Saccharomyces cerevisiae
cyclase-associated protein binds SH3 domains and modulates
cytoskeletal localization.";
Mol. Cell. Biol. 16:548-556(1996).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 368-526.
PubMed=15311924; DOI=10.1021/bi049071r;
Dodatko T., Fedorov A.A., Grynberg M., Patskovsky Y., Rozwarski D.A.,
Jaroszewski L., Aronoff-Spencer E., Kondraskina E., Irving T.,
Godzik A., Almo S.C.;
"Crystal structure of the actin binding domain of the cyclase-
associated protein.";
Biochemistry 43:10628-10641(2004).
-!- FUNCTION: The N-terminal domain binds to adenylyl cyclase, thereby
enabling adenylyl cyclase to be activated by upstream regulatory
signals, such as Ras. The C-terminal domain is required for normal
cellular morphology and growth control.
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-4024, EBI-4024;
P15891:ABP1; NbExp=9; IntAct=EBI-4024, EBI-2036;
P60010:ACT1; NbExp=7; IntAct=EBI-4024, EBI-2169;
P08678:CYR1; NbExp=5; IntAct=EBI-4024, EBI-5364;
P14126:RPL3; NbExp=3; IntAct=EBI-4024, EBI-15364;
P02994:TEF2; NbExp=3; IntAct=EBI-4024, EBI-6314;
P53250:TWF1; NbExp=3; IntAct=EBI-4024, EBI-19663;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
{ECO:0000269|PubMed:8552082}. Note=Cortical actin patches.
-!- MISCELLANEOUS: Present with 8760 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M58284; AAA63569.1; -; mRNA.
EMBL; M32663; AAA35094.1; -; Genomic_DNA.
EMBL; Z46843; CAA86887.1; -; Genomic_DNA.
EMBL; Z71414; CAA96020.1; -; Genomic_DNA.
EMBL; BK006947; DAA10410.1; -; Genomic_DNA.
PIR; A34896; A34896.
RefSeq; NP_014261.1; NM_001182976.1.
PDB; 1K4Z; X-ray; 2.30 A; A/B=369-526.
PDB; 1KQ5; X-ray; 3.00 A; A/B=369-526.
PDBsum; 1K4Z; -.
PDBsum; 1KQ5; -.
ProteinModelPortal; P17555; -.
SMR; P17555; -.
BioGrid; 35688; 622.
DIP; DIP-77N; -.
IntAct; P17555; 44.
MINT; MINT-582270; -.
STRING; 4932.YNL138W; -.
iPTMnet; P17555; -.
MaxQB; P17555; -.
PRIDE; P17555; -.
EnsemblFungi; YNL138W; YNL138W; YNL138W.
GeneID; 855584; -.
KEGG; sce:YNL138W; -.
EuPathDB; FungiDB:YNL138W; -.
SGD; S000005082; SRV2.
GeneTree; ENSGT00390000017955; -.
HOGENOM; HOG000206192; -.
InParanoid; P17555; -.
KO; K17261; -.
OMA; HCGYGDS; -.
OrthoDB; EOG092C2MM2; -.
BioCyc; YEAST:G3O-33157-MONOMER; -.
Reactome; R-SCE-6798695; Neutrophil degranulation.
EvolutionaryTrace; P17555; -.
PRO; PR:P17555; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0030479; C:actin cortical patch; IDA:SGD.
GO; GO:0003779; F:actin binding; IDA:SGD.
GO; GO:0008179; F:adenylate cyclase binding; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030042; P:actin filament depolymerization; IDA:SGD.
GO; GO:0007015; P:actin filament organization; IDA:SGD.
GO; GO:0051014; P:actin filament severing; IDA:SGD.
GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
GO; GO:0030836; P:positive regulation of actin filament depolymerization; IDA:SGD.
GO; GO:0007265; P:Ras protein signal transduction; IMP:SGD.
GO; GO:0045761; P:regulation of adenylate cyclase activity; IBA:GO_Central.
InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
InterPro; IPR017901; C-CAP_CF_C-like.
InterPro; IPR036223; CAP_C_sf.
InterPro; IPR028417; CAP_CS_C.
InterPro; IPR018106; CAP_CS_N.
InterPro; IPR028419; CAP_fungal_type.
InterPro; IPR036222; CAP_N_sf.
InterPro; IPR006599; CARP_motif.
PANTHER; PTHR10652; PTHR10652; 1.
PANTHER; PTHR10652:SF0; PTHR10652:SF0; 1.
Pfam; PF08603; CAP_C; 1.
Pfam; PF01213; CAP_N; 1.
SMART; SM00673; CARP; 2.
SUPFAM; SSF101278; SSF101278; 2.
SUPFAM; SSF69340; SSF69340; 1.
PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PROSITE; PS01088; CAP_1; 1.
PROSITE; PS01089; CAP_2; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Complete proteome; Cytoplasm;
Cytoskeleton; Phosphoprotein; Reference proteome.
CHAIN 1 526 Adenylyl cyclase-associated protein.
/FTId=PRO_0000205706.
DOMAIN 369 504 C-CAP/cofactor C-like.
{ECO:0000255|PROSITE-ProRule:PRU00659}.
REGION 1 168 Adenyl cyclase-binding.
REGION 354 361 Interaction with SH3 domain of ABP1.
REGION 370 526 Dimerization and actin-binding.
MOTIF 169 369 SH3-binding.
COMPBIAS 262 300 Ala/Pro/Ser-rich.
COMPBIAS 277 282 Poly-Pro.
MOD_RES 454 454 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
STRAND 371 375 {ECO:0000244|PDB:1K4Z}.
STRAND 378 382 {ECO:0000244|PDB:1K4Z}.
STRAND 391 394 {ECO:0000244|PDB:1K4Z}.
STRAND 400 415 {ECO:0000244|PDB:1K4Z}.
STRAND 417 433 {ECO:0000244|PDB:1K4Z}.
STRAND 435 437 {ECO:0000244|PDB:1K4Z}.
STRAND 439 453 {ECO:0000244|PDB:1K4Z}.
STRAND 456 462 {ECO:0000244|PDB:1K4Z}.
STRAND 464 469 {ECO:0000244|PDB:1K4Z}.
TURN 473 476 {ECO:0000244|PDB:1K4Z}.
STRAND 478 483 {ECO:0000244|PDB:1K4Z}.
STRAND 485 492 {ECO:0000244|PDB:1K4Z}.
HELIX 495 497 {ECO:0000244|PDB:1K4Z}.
STRAND 500 503 {ECO:0000244|PDB:1K4Z}.
STRAND 508 513 {ECO:0000244|PDB:1K4Z}.
STRAND 516 521 {ECO:0000244|PDB:1K4Z}.
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


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