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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)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi65 – 7281
Calcium bindingi132 – 143122Add
BLAST
Calcium bindingi161 – 172123PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium-dependent cysteine-type endopeptidase activity Source: GO_Central
  2. calcium ion binding Source: UniProtKB
  3. protein heterodimerization activity Source: BHF-UCL
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. membrane fusion Source: ProtInc
  2. proteolysis Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Grancalcin
Gene namesi
Name:GCA
Synonyms:GCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:15990. GCA.

Subcellular locationi

Cytoplasm. Cytoplasmic granule membrane; 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.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProtKB
  3. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28602.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217GrancalcinPRO_0000073721Add
BLAST

Proteomic databases

MaxQBiP28676.
PaxDbiP28676.
PeptideAtlasiP28676.
PRIDEiP28676.

PTM databases

PhosphoSiteiP28676.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP28676.
CleanExiHS_GCA.
ExpressionAtlasiP28676. baseline and differential.
GenevestigatoriP28676.

Organism-specific databases

HPAiHPA035033.
HPA035034.

Interactioni

Subunit structurei

Homodimer. Interacts with SRI and LCP1.4 Publications

Protein-protein interaction databases

BioGridi117333. 11 interactions.
IntActiP28676. 4 interactions.
MINTiMINT-267888.
STRINGi9606.ENSP00000394842.

Structurei

Secondary structure

1
217
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi54 – 629Combined sources
Helixi63 – 653Combined sources
Helixi70 – 8011Combined sources
Turni81 – 855Combined sources
Helixi91 – 10111Combined sources
Beta strandi106 – 1094Combined sources
Helixi111 – 13121Combined sources
Helixi133 – 1353Combined sources
Beta strandi138 – 1403Combined sources
Helixi141 – 15010Combined sources
Helixi157 – 16711Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi172 – 1743Combined sources
Helixi175 – 19319Combined sources
Beta strandi201 – 2066Combined sources
Helixi207 – 2159Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F4OX-ray2.50A/B53-217[»]
1F4QX-ray1.90A/B53-217[»]
1K94X-ray1.70A/B53-217[»]
1K95X-ray1.90A53-217[»]
ProteinModelPortaliP28676.
SMRiP28676. Positions 53-217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 8336EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini89 – 12234EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini119 – 15436EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini155 – 18026EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG298587.
GeneTreeiENSGT00620000087734.
HOGENOMiHOG000231982.
HOVERGENiHBG004492.
InParanoidiP28676.
OMAiFMTIDQD.
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]
PfamiPF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
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 BAD93005.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661R → D AA sequence (PubMed:1530588).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti80 – 801S → A.1 Publication
Corresponds to variant rs17783344 [ dbSNP | Ensembl ].
VAR_048657

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_012198.3.
UniGeneiHs.377894.

Genome annotation databases

EnsembliENST00000437150; ENSP00000394842; ENSG00000115271.
GeneIDi25801.
KEGGihsa:25801.
UCSCiuc002ucg.3. human.

Polymorphism databases

DMDMi1170014.

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_012198.3.
UniGeneiHs.377894.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F4OX-ray2.50A/B53-217[»]
1F4QX-ray1.90A/B53-217[»]
1K94X-ray1.70A/B53-217[»]
1K95X-ray1.90A53-217[»]
ProteinModelPortaliP28676.
SMRiP28676. Positions 53-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117333. 11 interactions.
IntActiP28676. 4 interactions.
MINTiMINT-267888.
STRINGi9606.ENSP00000394842.

PTM databases

PhosphoSiteiP28676.

Polymorphism databases

DMDMi1170014.

Proteomic databases

MaxQBiP28676.
PaxDbiP28676.
PeptideAtlasiP28676.
PRIDEiP28676.

Protocols and materials databases

DNASUi25801.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000437150; ENSP00000394842; ENSG00000115271.
GeneIDi25801.
KEGGihsa:25801.
UCSCiuc002ucg.3. human.

Organism-specific databases

CTDi25801.
GeneCardsiGC02P163164.
HGNCiHGNC:15990. GCA.
HPAiHPA035033.
HPA035034.
MIMi607030. gene.
neXtProtiNX_P28676.
PharmGKBiPA28602.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG298587.
GeneTreeiENSGT00620000087734.
HOGENOMiHOG000231982.
HOVERGENiHBG004492.
InParanoidiP28676.
OMAiFMTIDQD.
PhylomeDBiP28676.
TreeFamiTF314682.

Miscellaneous databases

ChiTaRSiGCA. human.
EvolutionaryTraceiP28676.
GeneWikiiGCA_(gene).
GenomeRNAii25801.
NextBioi47003.
PROiP28676.
SOURCEiSearch...

Gene expression databases

BgeeiP28676.
CleanExiHS_GCA.
ExpressionAtlasiP28676. baseline and differential.
GenevestigatoriP28676.

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]
PfamiPF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of grancalcin, a novel EF-hand calcium-binding protein abundant in neutrophils and monocytes."
    Boyhan A., Casimir C.M., French J.K., Teahan C.G., Segal A.W.
    J. Biol. Chem. 267:2928-2933(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Neutrophil.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-80.
    Tissue: Brain.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Urinary bladder.
  7. "Isolation and characterization of grancalcin, a novel 28 kDa EF-hand calcium-binding protein from human neutrophils."
    Teahan C.G., Totty N.F., Segal A.W.
    Biochem. J. 286:549-554(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 15-27; 109-125 AND 146-175, SUBUNIT, CALCIUM-BINDING, SUBCELLULAR LOCATION.
    Tissue: Neutrophil.
  8. "Biochemical characterization of the penta-EF-hand protein grancalcin and identification of L-plastin as a binding partner."
    Lollike K., Johnsen A.H., Durussel I., Borregaard N., Cox J.A.
    J. Biol. Chem. 276:17762-17769(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LCP1.
  9. "The PEF family proteins sorcin and grancalcin interact in vivo and in vitro."
    Hansen C., Tarabykina S., la Cour J.M., Lollike K., Berchtold M.W.
    FEBS Lett. 545:151-154(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRI.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Crystal structure of human grancalcin, a member of the penta-EF-hand protein family."
    Jia J., Han Q., Borregaard N., Lollike K., Cygler M.
    J. Mol. Biol. 300:1271-1281(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-217.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 53-217 IN COMPLEX WITH CALCIUM, SUBUNIT.

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: February 4, 2015
This is version 140 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

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.