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P28676

- GRAN_HUMAN

UniProt

P28676 - GRAN_HUMAN

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Protein
Grancalcin
Gene
GCA, GCL
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 72811 Publication
Calcium bindingi132 – 1431221 Publication
Add
BLAST
Calcium bindingi161 – 172123 Reviewed prediction
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. membrane fusion Source: ProtInc
  2. proteolysis Source: RefGenome
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: 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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProt
  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 – 217217Grancalcin
PRO_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

ArrayExpressiP28676.
BgeeiP28676.
CleanExiHS_GCA.
GenevestigatoriP28676.

Organism-specific databases

HPAiHPA035033.
HPA035034.

Interactioni

Subunit structurei

Homodimer. Interacts with SRI and LCP1.4 Publications

Protein-protein interaction databases

BioGridi117333. 8 interactions.
IntActiP28676. 4 interactions.
MINTiMINT-267888.
STRINGi9606.ENSP00000394842.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP28676.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 4 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG298587.
HOGENOMiHOG000231982.
HOVERGENiHBG004492.
InParanoidiP28676.
OMAiSAGDPMW.
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

MAYPGYGGGF GNFSIQVPGM QMGQPVPETG PAILLDGYSG PAYSDTYSSA    50
GDSVYTYFSA VAGQDGEVDA EELQRCLTQS GINGTYSPFS LETCRIMIAM 100
LDRDHTGKMG FNAFKELWAA LNAWKENFMT VDQDGSGTVE HHELRQAIGL 150
MGYRLSPQTL TTIVKRYSKN GRIFFDDYVA CCVKLRALTD FFRKRDHLQQ 200
GSANFIYDDF LQGTMAI 217
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.

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661R → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2218.1.
PIRi A42578.
RefSeqi NP_036330.1. NM_012198.3.
UniGenei Hs.377894.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F4O X-ray 2.50 A/B 53-217 [» ]
1F4Q X-ray 1.90 A/B 53-217 [» ]
1K94 X-ray 1.70 A/B 53-217 [» ]
1K95 X-ray 1.90 A 53-217 [» ]
ProteinModelPortali P28676.
SMRi P28676. Positions 53-217.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117333. 8 interactions.
IntActi P28676. 4 interactions.
MINTi MINT-267888.
STRINGi 9606.ENSP00000394842.

PTM databases

PhosphoSitei P28676.

Polymorphism databases

DMDMi 1170014.

Proteomic databases

MaxQBi P28676.
PaxDbi P28676.
PeptideAtlasi P28676.
PRIDEi P28676.

Protocols and materials databases

DNASUi 25801.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000437150 ; ENSP00000394842 ; ENSG00000115271 .
GeneIDi 25801.
KEGGi hsa:25801.
UCSCi uc002ucg.3. human.

Organism-specific databases

CTDi 25801.
GeneCardsi GC02P163164.
HGNCi HGNC:15990. GCA.
HPAi HPA035033.
HPA035034.
MIMi 607030. gene.
neXtProti NX_P28676.
PharmGKBi PA28602.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG298587.
HOGENOMi HOG000231982.
HOVERGENi HBG004492.
InParanoidi P28676.
OMAi SAGDPMW.
PhylomeDBi P28676.
TreeFami TF314682.

Miscellaneous databases

ChiTaRSi GCA. human.
EvolutionaryTracei P28676.
GeneWikii GCA_(gene).
GenomeRNAii 25801.
NextBioi 47003.
PROi P28676.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28676.
Bgeei P28676.
CleanExi HS_GCA.
Genevestigatori P28676.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF13405. EF-hand_6. 1 hit.
[Graphical view ]
SMARTi SM00054. EFh. 2 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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.
    , 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. 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. 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. 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: July 9, 2014
This is version 135 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

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