Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

GO - Biological processi

  • actin filament organization Source: SGD
  • actin filament severing Source: SGD
  • actin polymerization or depolymerization Source: GO_Central
  • cell morphogenesis Source: GO_Central
  • establishment or maintenance of cell polarity Source: GO_Central
  • Ras protein signal transduction Source: SGD
  • regulation of adenylate cyclase activity Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33157-MONOMER.
ReactomeiR-SCE-6798695. Neutrophil 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
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002057061 – 526Adenylyl cyclase-associated proteinAdd BLAST526

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei454PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP17555.
PRIDEiP17555.

PTM databases

iPTMnetiP17555.

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

GO - Molecular functioni

  • actin binding Source: SGD
  • adenylate cyclase binding Source: SGD

Protein-protein interaction databases

BioGridi35688. 73 interactors.
DIPiDIP-77N.
IntActiP17555. 37 interactors.
MINTiMINT-582270.

Structurei

Secondary structure

1526
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi371 – 375Combined sources5
Beta strandi378 – 382Combined sources5
Beta strandi391 – 394Combined sources4
Beta strandi400 – 415Combined sources16
Beta strandi417 – 433Combined sources17
Beta strandi435 – 437Combined sources3
Beta strandi439 – 453Combined sources15
Beta strandi456 – 462Combined sources7
Beta strandi464 – 469Combined sources6
Turni473 – 476Combined sources4
Beta strandi478 – 483Combined sources6
Beta strandi485 – 492Combined sources8
Helixi495 – 497Combined sources3
Beta strandi500 – 503Combined sources4
Beta strandi508 – 513Combined sources6
Beta strandi516 – 521Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K4ZX-ray2.30A/B369-526[»]
1KQ5X-ray3.00A/B369-526[»]
ProteinModelPortaliP17555.
SMRiP17555.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17555.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini369 – 504C-CAP/cofactor C-likePROSITE-ProRule annotationAdd BLAST136

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 168Adenyl cyclase-bindingAdd BLAST168
Regioni354 – 361Interaction with SH3 domain of ABP18
Regioni370 – 526Dimerization and actin-bindingAdd BLAST157

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi169 – 369SH3-bindingAdd BLAST201

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi262 – 300Ala/Pro/Ser-richAdd BLAST39
Compositional biasi277 – 282Poly-Pro6

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00390000017955.
HOGENOMiHOG000206192.
InParanoidiP17555.
KOiK17261.
OMAiIVNCNSV.
OrthoDBiEOG092C2MM2.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K4ZX-ray2.30A/B369-526[»]
1KQ5X-ray3.00A/B369-526[»]
ProteinModelPortaliP17555.
SMRiP17555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35688. 73 interactors.
DIPiDIP-77N.
IntActiP17555. 37 interactors.
MINTiMINT-582270.

PTM databases

iPTMnetiP17555.

Proteomic databases

MaxQBiP17555.
PRIDEiP17555.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YNL138W.
SGDiS000005082. SRV2.

Phylogenomic databases

GeneTreeiENSGT00390000017955.
HOGENOMiHOG000206192.
InParanoidiP17555.
KOiK17261.
OMAiIVNCNSV.
OrthoDBiEOG092C2MM2.

Enzyme and pathway databases

BioCyciYEAST:G3O-33157-MONOMER.
ReactomeiR-SCE-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP17555.
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...

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: November 30, 2016
This is version 159 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

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 one 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.