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P28676 (GRAN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Grancalcin
Gene names
Name:GCA
Synonyms:GCL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homodimer. Interacts with SRI and LCP1. Ref.7 Ref.8 Ref.9 Ref.12

Subcellular location

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. Ref.1 Ref.7

Tissue specificity

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

Miscellaneous

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

Sequence similarities

Contains 4 EF-hand domains.

Sequence caution

The sequence BAD93005.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Grancalcin
PRO_0000073721

Regions

Domain48 – 8336EF-hand 1
Domain89 – 12234EF-hand 2
Domain119 – 15436EF-hand 3
Domain155 – 18026EF-hand 4
Calcium binding65 – 7281 Ref.7
Calcium binding132 – 143122 Ref.7
Calcium binding161 – 172123 Potential

Natural variations

Natural variant801S → A. Ref.3
Corresponds to variant rs17783344 [ dbSNP | Ensembl ].
VAR_048657

Experimental info

Sequence conflict1661R → D AA sequence Ref.7

Secondary structure

........................... 217
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28676 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 88CA4DDF835AFFE4

FASTA21724,010
        10         20         30         40         50         60 
MAYPGYGGGF GNFSIQVPGM QMGQPVPETG PAILLDGYSG PAYSDTYSSA GDSVYTYFSA 

        70         80         90        100        110        120 
VAGQDGEVDA EELQRCLTQS GINGTYSPFS LETCRIMIAM LDRDHTGKMG FNAFKELWAA 

       130        140        150        160        170        180 
LNAWKENFMT VDQDGSGTVE HHELRQAIGL MGYRLSPQTL TTIVKRYSKN GRIFFDDYVA 

       190        200        210 
CCVKLRALTD FFRKRDHLQQ GSANFIYDDF LQGTMAI 

« Hide

References

« Hide 'large scale' references
[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(1992) [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. expand/collapse author list , 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(2004) [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 (MAR-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. expand/collapse author list , 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(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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(2004) [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(1992) [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(2001) [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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRI.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-217.
[12]"Structure of Ca(2+)-loaded human grancalcin."
Jia J., Borregaard N., Lollike K., Cygler M.
Acta Crystallogr. D 57:1843-1849(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 53-217 IN COMPLEX WITH CALCIUM, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA42578.
RefSeqNP_036330.1. NM_012198.3.
UniGeneHs.377894.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F4OX-ray2.50A/B53-217[»]
1F4QX-ray1.90A/B53-217[»]
1K94X-ray1.70A/B53-217[»]
1K95X-ray1.90A53-217[»]
ProteinModelPortalP28676.
SMRP28676. Positions 53-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117333. 8 interactions.
IntActP28676. 4 interactions.
MINTMINT-267888.
STRING9606.ENSP00000394842.

PTM databases

PhosphoSiteP28676.

Polymorphism databases

DMDM1170014.

Proteomic databases

PaxDbP28676.
PeptideAtlasP28676.
PRIDEP28676.

Protocols and materials databases

DNASU25801.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000437150; ENSP00000394842; ENSG00000115271.
GeneID25801.
KEGGhsa:25801.
UCSCuc002ucg.3. human.

Organism-specific databases

CTD25801.
GeneCardsGC02P163164.
HGNCHGNC:15990. GCA.
HPAHPA035033.
HPA035034.
MIM607030. gene.
neXtProtNX_P28676.
PharmGKBPA28602.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298587.
HOGENOMHOG000231982.
HOVERGENHBG004492.
InParanoidP28676.
OMASAGDPMW.
PhylomeDBP28676.
TreeFamTF314682.

Gene expression databases

ArrayExpressP28676.
BgeeP28676.
CleanExHS_GCA.
GenevestigatorP28676.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGCA. human.
EvolutionaryTraceP28676.
GeneWikiGCA_(gene).
GenomeRNAi25801.
NextBio47003.
PROP28676.
SOURCESearch...

Entry information

Entry nameGRAN_HUMAN
AccessionPrimary (citable) accession number: P28676
Secondary accession number(s): B2R5X3, Q53TB5, Q59EP3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM