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

Grancalcin

Gene

GCA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-binding protein that may play a role in the adhesion of neutrophils to fibronectin. May play a role in the formation of focal adhesions.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi65 – 7218
Calcium bindingi132 – 1432Add BLAST12
Calcium bindingi161 – 1723PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • calcium-dependent cysteine-type endopeptidase activity Source: GO_Central
  • calcium ion binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • membrane fusion Source: ProtInc
  • proteolysis Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000115271-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Grancalcin
Gene namesi
Name:GCA
Synonyms:GCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:15990. GCA.

Subcellular locationi

  • Cytoplasm 2 Publications
  • Cytoplasmic granule membrane 1 Publication1 Publication; Peripheral membrane protein; Cytoplasmic side

  • Note: Primarily cytosolic in the absence of calcium or magnesium ions. Relocates to granules and other membranes in response to elevated calcium and magnesium levels.1 Publication

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi25801.
OpenTargetsiENSG00000115271.
PharmGKBiPA28602.

Polymorphism and mutation databases

BioMutaiGCA.
DMDMi1170014.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000737211 – 217GrancalcinAdd BLAST217

Proteomic databases

EPDiP28676.
MaxQBiP28676.
PaxDbiP28676.
PeptideAtlasiP28676.
PRIDEiP28676.

PTM databases

iPTMnetiP28676.
PhosphoSitePlusiP28676.

Expressioni

Tissue specificityi

Detected in neutrophils and macrophages (at protein level). Highly expressed in bone marrow.1 Publication

Gene expression databases

BgeeiENSG00000115271.
CleanExiHS_GCA.
ExpressionAtlasiP28676. baseline and differential.
GenevisibleiP28676. HS.

Organism-specific databases

HPAiHPA035033.
HPA035034.

Interactioni

Subunit structurei

Homodimer. Interacts with SRI and LCP1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAGEA8P433615EBI-947242,EBI-10182930

GO - Molecular functioni

  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi117333. 20 interactors.
DIPiDIP-41437N.
IntActiP28676. 8 interactors.
MINTiMINT-267888.
STRINGi9606.ENSP00000394842.

Structurei

Secondary structure

1217
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi54 – 62Combined sources9
Helixi63 – 65Combined sources3
Helixi70 – 80Combined sources11
Turni81 – 85Combined sources5
Helixi91 – 101Combined sources11
Beta strandi106 – 109Combined sources4
Helixi111 – 131Combined sources21
Beta strandi134 – 136Combined sources3
Beta strandi138 – 140Combined sources3
Helixi141 – 150Combined sources10
Helixi157 – 167Combined sources11
Beta strandi169 – 171Combined sources3
Beta strandi172 – 174Combined sources3
Helixi175 – 193Combined sources19
Beta strandi201 – 206Combined sources6
Helixi207 – 215Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F4OX-ray2.50A/B53-217[»]
1F4QX-ray1.90A/B53-217[»]
1K94X-ray1.70A/B53-217[»]
1K95X-ray1.90A53-217[»]
ProteinModelPortaliP28676.
SMRiP28676.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini48 – 83EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini89 – 122EF-hand 2PROSITE-ProRule annotationAdd BLAST34
Domaini119 – 154EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini155 – 180EF-hand 4PROSITE-ProRule annotationAdd BLAST26

Sequence similaritiesi

Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0037. Eukaryota.
ENOG410YKQK. LUCA.
GeneTreeiENSGT00620000087734.
HOGENOMiHOG000231982.
HOVERGENiHBG004492.
InParanoidiP28676.
OMAiSAGDPMW.
OrthoDBiEOG091G0ISY.
PhylomeDBiP28676.
TreeFamiTF314682.

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.
[Graphical view]
PfamiPF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28676-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYPGYGGGF GNFSIQVPGM QMGQPVPETG PAILLDGYSG PAYSDTYSSA
60 70 80 90 100
GDSVYTYFSA VAGQDGEVDA EELQRCLTQS GINGTYSPFS LETCRIMIAM
110 120 130 140 150
LDRDHTGKMG FNAFKELWAA LNAWKENFMT VDQDGSGTVE HHELRQAIGL
160 170 180 190 200
MGYRLSPQTL TTIVKRYSKN GRIFFDDYVA CCVKLRALTD FFRKRDHLQQ
210
GSANFIYDDF LQGTMAI
Length:217
Mass (Da):24,010
Last modified:November 1, 1995 - v2
Checksum:i88CA4DDF835AFFE4
GO

Sequence cautioni

The sequence BAD93005 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti166R → D AA sequence (PubMed:1530588).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04865780S → A.1 PublicationCorresponds to variant rs17783344dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81637 mRNA. Translation: AAA58498.1.
AK312349 mRNA. Translation: BAG35270.1.
AB209768 mRNA. Translation: BAD93005.1. Different initiation.
AC010876 Genomic DNA. Translation: AAX93138.1.
CH471058 Genomic DNA. Translation: EAX11350.1.
BC005214 mRNA. Translation: AAH05214.1.
CCDSiCCDS2218.1.
PIRiA42578.
RefSeqiNP_036330.1. NM_012198.4.
UniGeneiHs.377894.

Genome annotation databases

EnsembliENST00000437150; ENSP00000394842; ENSG00000115271.
GeneIDi25801.
KEGGihsa:25801.
UCSCiuc002ucg.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81637 mRNA. Translation: AAA58498.1.
AK312349 mRNA. Translation: BAG35270.1.
AB209768 mRNA. Translation: BAD93005.1. Different initiation.
AC010876 Genomic DNA. Translation: AAX93138.1.
CH471058 Genomic DNA. Translation: EAX11350.1.
BC005214 mRNA. Translation: AAH05214.1.
CCDSiCCDS2218.1.
PIRiA42578.
RefSeqiNP_036330.1. NM_012198.4.
UniGeneiHs.377894.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F4OX-ray2.50A/B53-217[»]
1F4QX-ray1.90A/B53-217[»]
1K94X-ray1.70A/B53-217[»]
1K95X-ray1.90A53-217[»]
ProteinModelPortaliP28676.
SMRiP28676.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117333. 20 interactors.
DIPiDIP-41437N.
IntActiP28676. 8 interactors.
MINTiMINT-267888.
STRINGi9606.ENSP00000394842.

PTM databases

iPTMnetiP28676.
PhosphoSitePlusiP28676.

Polymorphism and mutation databases

BioMutaiGCA.
DMDMi1170014.

Proteomic databases

EPDiP28676.
MaxQBiP28676.
PaxDbiP28676.
PeptideAtlasiP28676.
PRIDEiP28676.

Protocols and materials databases

DNASUi25801.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000437150; ENSP00000394842; ENSG00000115271.
GeneIDi25801.
KEGGihsa:25801.
UCSCiuc002ucg.4. human.

Organism-specific databases

CTDi25801.
DisGeNETi25801.
GeneCardsiGCA.
HGNCiHGNC:15990. GCA.
HPAiHPA035033.
HPA035034.
MIMi607030. gene.
neXtProtiNX_P28676.
OpenTargetsiENSG00000115271.
PharmGKBiPA28602.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0037. Eukaryota.
ENOG410YKQK. LUCA.
GeneTreeiENSGT00620000087734.
HOGENOMiHOG000231982.
HOVERGENiHBG004492.
InParanoidiP28676.
OMAiSAGDPMW.
OrthoDBiEOG091G0ISY.
PhylomeDBiP28676.
TreeFamiTF314682.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000115271-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiGCA. human.
EvolutionaryTraceiP28676.
GeneWikiiGCA_(gene).
GenomeRNAii25801.
PROiP28676.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000115271.
CleanExiHS_GCA.
ExpressionAtlasiP28676. baseline and differential.
GenevisibleiP28676. HS.

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.
[Graphical view]
PfamiPF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGRAN_HUMAN
AccessioniPrimary (citable) accession number: P28676
Secondary accession number(s): B2R5X3, Q53TB5, Q59EP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

This protein has been shown to bind calcium with high affinity.

Keywords - Technical termi

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

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.