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Protein

Guanylyl cyclase-activating protein 2

Gene

GUCA1B

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Stimulates guanylyl cyclase 1 (GC1) and GC2 when free calcium ions concentration is low, and GC1 and GC2 when free calcium ions concentration is elevated. This Ca2+-sensitive regulation of GC is a key event in recovery of the dark state of rod photoreceptors following light exposure.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi69 – 80121Add
BLAST
Calcium bindingi105 – 116122Add
BLAST
Calcium bindingi158 – 169123Add
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylyl cyclase-activating protein 2
Short name:
GCAP 2
Alternative name(s):
Guanylate cyclase activator 1B
Retinal guanylyl cyclase activator protein p24
Gene namesi
Name:GUCA1B
Synonyms:GCAP-2, GCAP2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi104 – 1041Y → C: Partial loss of activity but no loss of calcium sensitivity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCurated
Chaini2 – 204203Guanylyl cyclase-activating protein 2PRO_0000073807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineCurated

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PaxDbiP51177.
PRIDEiP51177.

PTM databases

iPTMnetiP51177.

Expressioni

Tissue specificityi

Retina. Appears to be more abundant in rods.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000035936.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 125Combined sources
Beta strandi13 – 153Combined sources
Helixi18 – 3215Combined sources
Beta strandi33 – 353Combined sources
Helixi42 – 509Combined sources
Beta strandi53 – 553Combined sources
Helixi58 – 6811Combined sources
Beta strandi71 – 766Combined sources
Helixi78 – 8811Combined sources
Helixi95 – 10410Combined sources
Helixi114 – 13017Combined sources
Helixi146 – 15712Combined sources
Helixi167 – 1748Combined sources
Turni175 – 1795Combined sources
Helixi180 – 1856Combined sources
Beta strandi186 – 1883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JBANMR-A1-204[»]
ProteinModelPortaliP51177.
SMRiP51177. Positions 2-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51177.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 5436EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini56 – 9136EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini92 – 12736EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini145 – 18036EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0044. Eukaryota.
COG5126. LUCA.
HOGENOMiHOG000233019.
HOVERGENiHBG108179.
InParanoidiP51177.
KOiK08328.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR015756. GCAP-2.
IPR028846. Recoverin.
[Graphical view]
PANTHERiPTHR23055. PTHR23055. 1 hit.
PTHR23055:SF11. PTHR23055:SF11. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51177-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQQFSWEEA EENGAVGAAD AAQLQEWYKK FLEECPSGTL FMHEFKRFFK
60 70 80 90 100
VPDNEEATQY VEAMFRAFDT NGDNTIDFLE YVAALNLVLR GTLEHKLKWT
110 120 130 140 150
FKIYDKDRNG CIDRQELLDI VESIYKLKKA CSVEVEAEQQ GKLLTPEEVV
160 170 180 190 200
DRIFLLVDEN GDGQLSLNEF VEGARRDKWV MKMLQMDLNP SSWISQQRRK

SAMF
Length:204
Mass (Da):23,728
Last modified:January 23, 2007 - v2
Checksum:iBA375D54960E5F75
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32856 mRNA. Translation: AAC48478.1.
L43001 mRNA. Translation: AAA83214.1.
PIRiA57604.
RefSeqiNP_777211.1. NM_174786.1.
UniGeneiBt.520.

Genome annotation databases

GeneIDi286851.
KEGGibta:286851.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32856 mRNA. Translation: AAC48478.1.
L43001 mRNA. Translation: AAA83214.1.
PIRiA57604.
RefSeqiNP_777211.1. NM_174786.1.
UniGeneiBt.520.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JBANMR-A1-204[»]
ProteinModelPortaliP51177.
SMRiP51177. Positions 2-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000035936.

PTM databases

iPTMnetiP51177.

Proteomic databases

PaxDbiP51177.
PRIDEiP51177.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi286851.
KEGGibta:286851.

Organism-specific databases

CTDi2979.

Phylogenomic databases

eggNOGiKOG0044. Eukaryota.
COG5126. LUCA.
HOGENOMiHOG000233019.
HOVERGENiHBG108179.
InParanoidiP51177.
KOiK08328.

Miscellaneous databases

EvolutionaryTraceiP51177.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR015756. GCAP-2.
IPR028846. Recoverin.
[Graphical view]
PANTHERiPTHR23055. PTHR23055. 1 hit.
PTHR23055:SF11. PTHR23055:SF11. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing, and expression of a 24-kDa Ca(2+)-binding protein activating photoreceptor guanylyl cyclase."
    Dizhoor A.M., Olshevskaya E.V., Henzel W.J., Wong S.C., Stults J.T., Ankoudinova I., Hurley J.B.
    J. Biol. Chem. 270:25200-25206(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Retina.
  2. "Guanylyl cyclase activating protein. A calcium-sensitive regulator of phototransduction."
    Gorczyca W.A., Polans A.S., Surgucheva I.G., Subbaraya I., Baehr W., Palczewski K.
    J. Biol. Chem. 270:22029-22036(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-81.
    Tissue: Retina.
  3. "Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases."
    Ames J.B., Dizhoor A.M., Ikura M., Palczewski K., Stryer L.
    J. Biol. Chem. 274:19329-19337(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, CALCIUM-BINDING.
  4. "Constitutive activation of photoreceptor guanylate cyclase by Y99C mutant of GCAP-1. Possible role in causing human autosomal dominant cone degeneration."
    Dizhoor A.M., Boikov S.G., Olshevskaya E.V.
    J. Biol. Chem. 273:17311-17314(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-104.

Entry informationi

Entry nameiGUC1B_BOVIN
AccessioniPrimary (citable) accession number: P51177
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds three calcium ions.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.