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GRAN_MOUSE
ID   GRAN_MOUSE              Reviewed;         220 AA.
AC   Q8VC88; Q8BL53; Q8K3Z6;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Grancalcin;
GN   Name=Gca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RX   PubMed=12529388; DOI=10.1128/mcb.23.3.826-830.2003;
RA   Roes J., Choi B.K., Power D., Xu P., Segal A.W.;
RT   "Granulocyte function in grancalcin-deficient mice.";
RL   Mol. Cell. Biol. 23:826-830(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15118320; DOI=10.1271/bbb.68.894;
RA   Liu F., Shinomiya H., Kirikae T., Hirata H., Asano Y.;
RT   "Characterization of murine grancalcin specifically expressed in leukocytes
RT   and its possible role in host defense against bacterial infection.";
RL   Biosci. Biotechnol. Biochem. 68:894-902(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, Corpora quadrigemina, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=16934789; DOI=10.1016/j.cellimm.2006.07.004;
RA   Xu P., Roes J., Segal A.W., Radulovic M.;
RT   "The role of grancalcin in adhesion of neutrophils.";
RL   Cell. Immunol. 240:116-121(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Calcium-binding protein that may play a role in the adhesion
CC       of neutrophils to fibronectin. May play a role in the formation of
CC       focal adhesions. {ECO:0000269|PubMed:16934789}.
CC   -!- SUBUNIT: Homodimer. Interacts with SRI and LCP1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28676}.
CC       Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P28676}; Peripheral
CC       membrane protein {ECO:0000250|UniProtKB:P28676}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P28676}. Note=Primarily cytosolic in the absence
CC       of calcium or magnesium ions. Relocates to granules and other membranes
CC       in response to elevated calcium and magnesium levels.
CC       {ECO:0000250|UniProtKB:P28676}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Not essential for normal
CC       resistance to microbial infections. Grancalcin-deficient neutrophils
CC       exhibit decreased adhesion to fibronectin, and a strongly reduced
CC       number of focal adhesion complexes. {ECO:0000269|PubMed:12529388,
CC       ECO:0000269|PubMed:16934789}.
CC   -!- MISCELLANEOUS: This protein has been shown to bind calcium with high
CC       affinity. {ECO:0000250}.
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DR   EMBL; AF518325; AAM66720.1; -; mRNA.
DR   EMBL; AB088388; BAC07231.1; -; mRNA.
DR   EMBL; AK033740; BAC28458.1; -; mRNA.
DR   EMBL; AK046347; BAC32686.1; -; mRNA.
DR   EMBL; AK049317; BAC33679.1; -; mRNA.
DR   EMBL; AK050540; BAC34315.1; -; mRNA.
DR   EMBL; AK078915; BAC37457.1; -; mRNA.
DR   EMBL; BC021450; AAH21450.1; -; mRNA.
DR   CCDS; CCDS16069.1; -.
DR   RefSeq; NP_663498.1; NM_145523.3.
DR   AlphaFoldDB; Q8VC88; -.
DR   SMR; Q8VC88; -.
DR   STRING; 10090.ENSMUSP00000028257; -.
DR   PhosphoSitePlus; Q8VC88; -.
DR   REPRODUCTION-2DPAGE; IPI00308789; -.
DR   MaxQB; Q8VC88; -.
DR   PaxDb; Q8VC88; -.
DR   PeptideAtlas; Q8VC88; -.
DR   PRIDE; Q8VC88; -.
DR   ProteomicsDB; 271288; -.
DR   Antibodypedia; 33752; 135 antibodies from 26 providers.
DR   DNASU; 227960; -.
DR   Ensembl; ENSMUST00000028257; ENSMUSP00000028257; ENSMUSG00000026893.
DR   GeneID; 227960; -.
DR   KEGG; mmu:227960; -.
DR   UCSC; uc008jvp.1; mouse.
DR   CTD; 25801; -.
DR   MGI; MGI:1918521; Gca.
DR   VEuPathDB; HostDB:ENSMUSG00000026893; -.
DR   eggNOG; KOG0037; Eukaryota.
DR   GeneTree; ENSGT00940000153979; -.
DR   HOGENOM; CLU_051357_4_0_1; -.
DR   InParanoid; Q8VC88; -.
DR   OMA; DSMWTYF; -.
DR   OrthoDB; 1330600at2759; -.
DR   PhylomeDB; Q8VC88; -.
DR   TreeFam; TF314682; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 227960; 1 hit in 73 CRISPR screens.
DR   PRO; PR:Q8VC88; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8VC88; protein.
DR   Bgee; ENSMUSG00000026893; Expressed in granulocyte and 222 other tissues.
DR   Genevisible; Q8VC88; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13833; EF-hand_8; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Membrane; Metal-binding; Reference proteome; Repeat.
FT   CHAIN           1..220
FT                   /note="Grancalcin"
FT                   /id="PRO_0000073722"
FT   DOMAIN          51..86
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          92..127
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          122..157
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          158..193
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000305"
FT   BINDING         105
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         107
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         109
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         111
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         116
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         135
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         137
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         139
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         141
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         146
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CONFLICT        187..188
FT                   /note="KL -> NV (in Ref. 1; AAM66720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="T -> P (in Ref. 3; BAC32686)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   220 AA;  24663 MW;  694DCA7D6ADF8279 CRC64;
     MAYPGYGGAF GNFSGQIPGM QMQMGQPMPG AGPNMFSGGY PGYLGYSDSY SPADDSMWTY
     FTAVAGQDGE VDAEELQRCL TQSGISGTYA PFSLETCRIM IAMLDRDYTG KMGFNEFKEL
     WAALNAWKQN FMTIDQDQSG TVEHHELSQA IALMGYRLSP QTLAAIVRRY SKNGRIFFDD
     YVACCVKLRA LTDFFRRRDH LQQGIVNFMY EDFLQGTMTI
 
 
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