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Protein

Adenylyl cyclase-associated protein

Gene

SRV2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • actin binding Source: SGD
  • adenylate cyclase binding Source: SGD
  • identical protein binding Source: IntAct

GO - Biological processi

  • actin filament organization Source: SGD
  • actin filament severing Source: SGD
  • cell morphogenesis Source: InterPro
  • Ras protein signal transduction Source: SGD
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33157-MONOMER.
ReactomeiREACT_350743. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylyl cyclase-associated protein
Short name:
CAP
Gene namesi
Name:SRV2
Synonyms:CAP1
Ordered Locus Names:YNL138W
ORF Names:N1210, N1838
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL138w.
EuPathDBiFungiDB:YNL138W.
SGDiS000005082. SRV2.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 526526Adenylyl cyclase-associated proteinPRO_0000205706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei454 – 4541Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP17555.
PaxDbiP17555.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-4024,EBI-4024
ABP1P158919EBI-4024,EBI-2036
ACT1P600105EBI-4024,EBI-2169
RPL3P141263EBI-4024,EBI-15364
TEF2P029943EBI-4024,EBI-6314

Protein-protein interaction databases

BioGridi35688. 71 interactions.
DIPiDIP-77N.
IntActiP17555. 37 interactions.
MINTiMINT-582270.

Structurei

Secondary structure

1
526
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi371 – 3755Combined sources
Beta strandi378 – 3825Combined sources
Beta strandi391 – 3944Combined sources
Beta strandi400 – 41516Combined sources
Beta strandi417 – 43317Combined sources
Beta strandi435 – 4373Combined sources
Beta strandi439 – 45315Combined sources
Beta strandi456 – 4627Combined sources
Beta strandi464 – 4696Combined sources
Turni473 – 4764Combined sources
Beta strandi478 – 4836Combined sources
Beta strandi485 – 4928Combined sources
Helixi495 – 4973Combined sources
Beta strandi500 – 5034Combined sources
Beta strandi508 – 5136Combined sources
Beta strandi516 – 5216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K4ZX-ray2.30A/B369-526[»]
1KQ5X-ray3.00A/B369-526[»]
ProteinModelPortaliP17555.
SMRiP17555. Positions 78-252, 369-524.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17555.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini369 – 504136C-CAP/cofactor C-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 168168Adenyl cyclase-bindingAdd
BLAST
Regioni354 – 3618Interaction with SH3 domain of ABP1
Regioni370 – 526157Dimerization and actin-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi169 – 369201SH3-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi262 – 30039Ala/Pro/Ser-richAdd
BLAST
Compositional biasi277 – 2826Poly-Pro

Sequence similaritiesi

Belongs to the CAP family.Curated
Contains 1 C-CAP/cofactor C-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG254262.
GeneTreeiENSGT00390000017955.
HOGENOMiHOG000206192.
InParanoidiP17555.
KOiK17261.
OMAiIVNCNSV.
OrthoDBiEOG7H79BV.

Family and domain databases

Gene3Di2.160.20.70. 1 hit.
InterProiIPR001837. Adenylate_cyclase-assoc_CAP.
IPR013912. Adenylate_cyclase-assoc_CAP_C.
IPR013992. Adenylate_cyclase-assoc_CAP_N.
IPR017901. C-CAP_CF_C-like.
IPR016098. CAP/MinC_C.
IPR028417. CAP_CS_C.
IPR018106. CAP_CS_N.
IPR028419. CAP_fungal_type.
IPR006599. CARP_motif.
[Graphical view]
PANTHERiPTHR10652. PTHR10652. 1 hit.
PTHR10652:SF0. PTHR10652:SF0. 1 hit.
PfamiPF08603. CAP_C. 1 hit.
PF01213. CAP_N. 1 hit.
[Graphical view]
SMARTiSM00673. CARP. 2 hits.
[Graphical view]
SUPFAMiSSF101278. SSF101278. 2 hits.
SSF69340. SSF69340. 1 hit.
PROSITEiPS51329. C_CAP_COFACTOR_C. 1 hit.
PS01088. CAP_1. 1 hit.
PS01089. CAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17555-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDSKYTMQG YNLVKLLKRL EEATARLEDV TIYQEGYIQN KLEASKNNKP
60 70 80 90 100
SDSGADANTT NEPSAENAPE VEQDPKCITA FQSYIGENID PLVELSGKID
110 120 130 140 150
TVVLDALQLL KGGFQSQLTF LRAAVRSRKP DYSSQTFADS LRPINENIIK
160 170 180 190 200
LGQLKESNRQ SKYFAYLSAL SEGAPLFSWV AVDTPVSMVT DFKDAAQFWT
210 220 230 240 250
NRILKEYRES DPNAVEWVKK FLASFDNLKA YIKEYHTTGV SWKKDGMDFA
260 270 280 290 300
DAMAQSTKNT GATSSPSPAS ATAAPAPPPP PPAPPASVFE ISNDTPATSS
310 320 330 340 350
DANKGGIGAV FAELNQGENI TKGLKKVDKS QQTHKNPELR QSSTVSSTGS
360 370 380 390 400
KSGPPPRPKK PSTLKTKRPP RKELVGNKWF IENYENETES LVIDANKDES
410 420 430 440 450
IFIGKCSQVL VQIKGKVNAI SLSETESCSV VLDSSISGMD VIKSNKFGIQ
460 470 480 490 500
VNHSLPQISI DKSDGGNIYL SKESLNTEIY TSCSTAINVN LPIGEDDDYV
510 520
EFPIPEQMKH SFADGKFKSA VFEHAG
Length:526
Mass (Da):57,521
Last modified:August 1, 1990 - v1
Checksum:i0EB4D41205E2D464
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58284 mRNA. Translation: AAA63569.1.
M32663 Genomic DNA. Translation: AAA35094.1.
Z46843 Genomic DNA. Translation: CAA86887.1.
Z71414 Genomic DNA. Translation: CAA96020.1.
BK006947 Genomic DNA. Translation: DAA10410.1.
PIRiA34896.
RefSeqiNP_014261.1. NM_001182976.1.

Genome annotation databases

EnsemblFungiiYNL138W; YNL138W; YNL138W.
GeneIDi855584.
KEGGisce:YNL138W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58284 mRNA. Translation: AAA63569.1.
M32663 Genomic DNA. Translation: AAA35094.1.
Z46843 Genomic DNA. Translation: CAA86887.1.
Z71414 Genomic DNA. Translation: CAA96020.1.
BK006947 Genomic DNA. Translation: DAA10410.1.
PIRiA34896.
RefSeqiNP_014261.1. NM_001182976.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K4ZX-ray2.30A/B369-526[»]
1KQ5X-ray3.00A/B369-526[»]
ProteinModelPortaliP17555.
SMRiP17555. Positions 78-252, 369-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35688. 71 interactions.
DIPiDIP-77N.
IntActiP17555. 37 interactions.
MINTiMINT-582270.

Proteomic databases

MaxQBiP17555.
PaxDbiP17555.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL138W; YNL138W; YNL138W.
GeneIDi855584.
KEGGisce:YNL138W.

Organism-specific databases

CYGDiYNL138w.
EuPathDBiFungiDB:YNL138W.
SGDiS000005082. SRV2.

Phylogenomic databases

eggNOGiNOG254262.
GeneTreeiENSGT00390000017955.
HOGENOMiHOG000206192.
InParanoidiP17555.
KOiK17261.
OMAiIVNCNSV.
OrthoDBiEOG7H79BV.

Enzyme and pathway databases

BioCyciYEAST:G3O-33157-MONOMER.
ReactomeiREACT_350743. Platelet degranulation.

Miscellaneous databases

EvolutionaryTraceiP17555.
NextBioi979715.
PROiP17555.

Family and domain databases

Gene3Di2.160.20.70. 1 hit.
InterProiIPR001837. Adenylate_cyclase-assoc_CAP.
IPR013912. Adenylate_cyclase-assoc_CAP_C.
IPR013992. Adenylate_cyclase-assoc_CAP_N.
IPR017901. C-CAP_CF_C-like.
IPR016098. CAP/MinC_C.
IPR028417. CAP_CS_C.
IPR018106. CAP_CS_N.
IPR028419. CAP_fungal_type.
IPR006599. CARP_motif.
[Graphical view]
PANTHERiPTHR10652. PTHR10652. 1 hit.
PTHR10652:SF0. PTHR10652:SF0. 1 hit.
PfamiPF08603. CAP_C. 1 hit.
PF01213. CAP_N. 1 hit.
[Graphical view]
SMARTiSM00673. CARP. 2 hits.
[Graphical view]
SUPFAMiSSF101278. SSF101278. 2 hits.
SSF69340. SSF69340. 1 hit.
PROSITEiPS51329. C_CAP_COFACTOR_C. 1 hit.
PS01088. CAP_1. 1 hit.
PS01089. CAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of CAP, the S. cerevisiae gene encoding the 70 kd adenylyl cyclase-associated protein."
    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.
    Cell 61:319-327(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "SRV2, a gene required for RAS activation of adenylate cyclase in yeast."
    Fedor-Chaiken M., Deschenes R.J., Broach J.R.
    Cell 61:329-340(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "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."
    Mallet L., Bussereau F., Jacquet M.
    Yeast 11:1195-1209(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    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.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization."
    Freeman N.L., Lila T., Mintzer K.A., Chen Z., Pahk A.J., Ren R., Drubin D.G., Field J.
    Mol. Cell. Biol. 16:548-556(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ABP1, SUBCELLULAR LOCATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 368-526.

Entry informationi

Entry nameiCAP_YEAST
AccessioniPrimary (citable) accession number: P17555
Secondary accession number(s): D6W144
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 22, 2015
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8760 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.