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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: -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.

Miscellaneous

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

GO - Molecular functioni

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

GO - Biological processi

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

Keywordsi

Molecular functionActin-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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP17555
PRIDEiP17555

PTM databases

iPTMnetiP17555

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi35688, 623 interactors
DIPiDIP-77N
IntActiP17555, 44 interactors
MINTiP17555
STRINGi4932.YNL138W

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

Phylogenomic databases

GeneTreeiENSGT00390000017955
HOGENOMiHOG000206192
InParanoidiP17555
KOiK17261
OMAiHCGYGDS
OrthoDBiEOG092C2MM2

Family and domain databases

Gene3Di1.25.40.330, 1 hit
2.160.20.70, 1 hit
InterProiView protein in InterPro
IPR001837 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
IPR036223 CAP_C_sf
IPR028417 CAP_CS_C
IPR018106 CAP_CS_N
IPR028419 CAP_fungal_type
IPR036222 CAP_N_sf
IPR006599 CARP_motif
PANTHERiPTHR10652 PTHR10652, 1 hit
PTHR10652:SF0 PTHR10652:SF0, 1 hit
PfamiView protein in Pfam
PF08603 CAP_C, 1 hit
PF01213 CAP_N, 1 hit
SMARTiView protein in SMART
SM00673 CARP, 2 hits
SUPFAMiSSF101278 SSF101278, 2 hits
SSF69340 SSF69340, 1 hit
PROSITEiView protein in PROSITE
PS51329 C_CAP_COFACTOR_C, 1 hit
PS01088 CAP_1, 1 hit
PS01089 CAP_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCAP_YEAST
AccessioniPrimary (citable) accession number: P17555
Secondary accession number(s): D6W144
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 23, 2018
This is version 173 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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