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P28676

- GRAN_HUMAN

UniProt

P28676 - GRAN_HUMAN

Protein

Grancalcin

Gene

GCA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    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: RefGenome
    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: RefGenome

    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.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. plasma membrane Source: HPA

    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

    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

    1
    217
    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.
    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.
    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.

    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:
    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

    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: October 1, 2014
    This is version 136 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