Full text data of GCA
GCA
(GCL)
[Confidence: low (only semi-automatic identification from reviews)]
Grancalcin
Grancalcin
UniProt
P28676
ID GRAN_HUMAN Reviewed; 217 AA.
AC P28676; B2R5X3; Q53TB5; Q59EP3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 2.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=Grancalcin;
GN Name=GCA; Synonyms=GCL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Neutrophil;
RX PubMed=1737748;
RA Boyhan A., Casimir C.M., French J.K., Teahan C.G., Segal A.W.;
RT "Molecular cloning and characterization of grancalcin, a novel EF-hand
RT calcium-binding protein abundant in neutrophils and monocytes.";
RL J. Biol. Chem. 267:2928-2933(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-80.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 15-27; 109-125 AND 146-175, SUBUNIT,
RP CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
RC TISSUE=Neutrophil;
RX PubMed=1530588;
RA Teahan C.G., Totty N.F., Segal A.W.;
RT "Isolation and characterization of grancalcin, a novel 28 kDa EF-hand
RT calcium-binding protein from human neutrophils.";
RL Biochem. J. 286:549-554(1992).
RN [8]
RP INTERACTION WITH LCP1.
RX PubMed=11279160; DOI=10.1074/jbc.M100965200;
RA Lollike K., Johnsen A.H., Durussel I., Borregaard N., Cox J.A.;
RT "Biochemical characterization of the penta-EF-hand protein grancalcin
RT and identification of L-plastin as a binding partner.";
RL J. Biol. Chem. 276:17762-17769(2001).
RN [9]
RP INTERACTION WITH SRI.
RX PubMed=12804766; DOI=10.1016/S0014-5793(03)00518-0;
RA Hansen C., Tarabykina S., la Cour J.M., Lollike K., Berchtold M.W.;
RT "The PEF family proteins sorcin and grancalcin interact in vivo and in
RT vitro.";
RL FEBS Lett. 545:151-154(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-217.
RX PubMed=10903868; DOI=10.1006/jmbi.2000.3925;
RA Jia J., Han Q., Borregaard N., Lollike K., Cygler M.;
RT "Crystal structure of human grancalcin, a member of the penta-EF-hand
RT protein family.";
RL J. Mol. Biol. 300:1271-1281(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 53-217 IN COMPLEX WITH
RP CALCIUM, AND SUBUNIT.
RX PubMed=11717497; DOI=10.1107/S0907444901016511;
RA Jia J., Borregaard N., Lollike K., Cygler M.;
RT "Structure of Ca(2+)-loaded human grancalcin.";
RL Acta Crystallogr. D 57:1843-1849(2001).
CC -!- FUNCTION: Calcium-binding protein that may play a role in the
CC adhesion of neutrophils to fibronectin. May play a role in the
CC formation of focal adhesions.
CC -!- SUBUNIT: Homodimer. Interacts with SRI and LCP1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic granule membrane;
CC Peripheral membrane protein; Cytoplasmic side. Note=Primarily
CC cytosolic in the absence of calcium or magnesium ions. Relocates
CC to granules and other membranes in response to elevated calcium
CC and magnesium levels.
CC -!- TISSUE SPECIFICITY: Detected in neutrophils and macrophages (at
CC protein level). Highly expressed in bone marrow.
CC -!- MISCELLANEOUS: This protein has been shown to bind calcium with
CC high affinity.
CC -!- SIMILARITY: Contains 4 EF-hand domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93005.1; Type=Erroneous initiation;
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DR EMBL; M81637; AAA58498.1; -; mRNA.
DR EMBL; AK312349; BAG35270.1; -; mRNA.
DR EMBL; AB209768; BAD93005.1; ALT_INIT; mRNA.
DR EMBL; AC010876; AAX93138.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11350.1; -; Genomic_DNA.
DR EMBL; BC005214; AAH05214.1; -; mRNA.
DR PIR; A42578; A42578.
DR RefSeq; NP_036330.1; NM_012198.3.
DR UniGene; Hs.377894; -.
DR PDB; 1F4O; X-ray; 2.50 A; A/B=53-217.
DR PDB; 1F4Q; X-ray; 1.90 A; A/B=53-217.
DR PDB; 1K94; X-ray; 1.70 A; A/B=53-217.
DR PDB; 1K95; X-ray; 1.90 A; A=53-217.
DR PDBsum; 1F4O; -.
DR PDBsum; 1F4Q; -.
DR PDBsum; 1K94; -.
DR PDBsum; 1K95; -.
DR ProteinModelPortal; P28676; -.
DR SMR; P28676; 53-217.
DR IntAct; P28676; 4.
DR MINT; MINT-267888; -.
DR STRING; 9606.ENSP00000394842; -.
DR PhosphoSite; P28676; -.
DR DMDM; 1170014; -.
DR PaxDb; P28676; -.
DR PeptideAtlas; P28676; -.
DR PRIDE; P28676; -.
DR DNASU; 25801; -.
DR Ensembl; ENST00000437150; ENSP00000394842; ENSG00000115271.
DR GeneID; 25801; -.
DR KEGG; hsa:25801; -.
DR UCSC; uc002ucg.3; human.
DR CTD; 25801; -.
DR GeneCards; GC02P163164; -.
DR HGNC; HGNC:15990; GCA.
DR HPA; HPA035033; -.
DR HPA; HPA035034; -.
DR MIM; 607030; gene.
DR neXtProt; NX_P28676; -.
DR PharmGKB; PA28602; -.
DR eggNOG; NOG298587; -.
DR HOGENOM; HOG000231982; -.
DR HOVERGEN; HBG004492; -.
DR InParanoid; P28676; -.
DR OMA; SAGDPMW; -.
DR PhylomeDB; P28676; -.
DR ChiTaRS; GCA; human.
DR EvolutionaryTrace; P28676; -.
DR GeneWiki; GCA_(gene); -.
DR GenomeRNAi; 25801; -.
DR NextBio; 47003; -.
DR PRO; PR:P28676; -.
DR ArrayExpress; P28676; -.
DR Bgee; P28676; -.
DR CleanEx; HS_GCA; -.
DR Genevestigator; P28676; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13405; EF-hand_6; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 217 Grancalcin.
FT /FTId=PRO_0000073721.
FT DOMAIN 48 83 EF-hand 1.
FT DOMAIN 89 122 EF-hand 2.
FT DOMAIN 119 154 EF-hand 3.
FT DOMAIN 155 180 EF-hand 4.
FT CA_BIND 65 72 1.
FT CA_BIND 132 143 2.
FT CA_BIND 161 172 3 (Potential).
FT VARIANT 80 80 S -> A (in dbSNP:rs17783344).
FT /FTId=VAR_048657.
FT CONFLICT 166 166 R -> D (in Ref. 7; AA sequence).
FT HELIX 54 62
FT HELIX 63 65
FT HELIX 70 80
FT TURN 81 85
FT HELIX 91 101
FT STRAND 106 109
FT HELIX 111 131
FT HELIX 133 135
FT STRAND 138 140
FT HELIX 141 150
FT HELIX 157 167
FT STRAND 169 171
FT STRAND 172 174
FT HELIX 175 193
FT STRAND 201 206
FT HELIX 207 215
SQ SEQUENCE 217 AA; 24010 MW; 88CA4DDF835AFFE4 CRC64;
MAYPGYGGGF GNFSIQVPGM QMGQPVPETG PAILLDGYSG PAYSDTYSSA GDSVYTYFSA
VAGQDGEVDA EELQRCLTQS GINGTYSPFS LETCRIMIAM LDRDHTGKMG FNAFKELWAA
LNAWKENFMT VDQDGSGTVE HHELRQAIGL MGYRLSPQTL TTIVKRYSKN GRIFFDDYVA
CCVKLRALTD FFRKRDHLQQ GSANFIYDDF LQGTMAI
//
ID GRAN_HUMAN Reviewed; 217 AA.
AC P28676; B2R5X3; Q53TB5; Q59EP3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1995, sequence version 2.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=Grancalcin;
GN Name=GCA; Synonyms=GCL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Neutrophil;
RX PubMed=1737748;
RA Boyhan A., Casimir C.M., French J.K., Teahan C.G., Segal A.W.;
RT "Molecular cloning and characterization of grancalcin, a novel EF-hand
RT calcium-binding protein abundant in neutrophils and monocytes.";
RL J. Biol. Chem. 267:2928-2933(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-80.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 15-27; 109-125 AND 146-175, SUBUNIT,
RP CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
RC TISSUE=Neutrophil;
RX PubMed=1530588;
RA Teahan C.G., Totty N.F., Segal A.W.;
RT "Isolation and characterization of grancalcin, a novel 28 kDa EF-hand
RT calcium-binding protein from human neutrophils.";
RL Biochem. J. 286:549-554(1992).
RN [8]
RP INTERACTION WITH LCP1.
RX PubMed=11279160; DOI=10.1074/jbc.M100965200;
RA Lollike K., Johnsen A.H., Durussel I., Borregaard N., Cox J.A.;
RT "Biochemical characterization of the penta-EF-hand protein grancalcin
RT and identification of L-plastin as a binding partner.";
RL J. Biol. Chem. 276:17762-17769(2001).
RN [9]
RP INTERACTION WITH SRI.
RX PubMed=12804766; DOI=10.1016/S0014-5793(03)00518-0;
RA Hansen C., Tarabykina S., la Cour J.M., Lollike K., Berchtold M.W.;
RT "The PEF family proteins sorcin and grancalcin interact in vivo and in
RT vitro.";
RL FEBS Lett. 545:151-154(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-217.
RX PubMed=10903868; DOI=10.1006/jmbi.2000.3925;
RA Jia J., Han Q., Borregaard N., Lollike K., Cygler M.;
RT "Crystal structure of human grancalcin, a member of the penta-EF-hand
RT protein family.";
RL J. Mol. Biol. 300:1271-1281(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 53-217 IN COMPLEX WITH
RP CALCIUM, AND SUBUNIT.
RX PubMed=11717497; DOI=10.1107/S0907444901016511;
RA Jia J., Borregaard N., Lollike K., Cygler M.;
RT "Structure of Ca(2+)-loaded human grancalcin.";
RL Acta Crystallogr. D 57:1843-1849(2001).
CC -!- FUNCTION: Calcium-binding protein that may play a role in the
CC adhesion of neutrophils to fibronectin. May play a role in the
CC formation of focal adhesions.
CC -!- SUBUNIT: Homodimer. Interacts with SRI and LCP1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic granule membrane;
CC Peripheral membrane protein; Cytoplasmic side. Note=Primarily
CC cytosolic in the absence of calcium or magnesium ions. Relocates
CC to granules and other membranes in response to elevated calcium
CC and magnesium levels.
CC -!- TISSUE SPECIFICITY: Detected in neutrophils and macrophages (at
CC protein level). Highly expressed in bone marrow.
CC -!- MISCELLANEOUS: This protein has been shown to bind calcium with
CC high affinity.
CC -!- SIMILARITY: Contains 4 EF-hand domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93005.1; Type=Erroneous initiation;
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DR EMBL; M81637; AAA58498.1; -; mRNA.
DR EMBL; AK312349; BAG35270.1; -; mRNA.
DR EMBL; AB209768; BAD93005.1; ALT_INIT; mRNA.
DR EMBL; AC010876; AAX93138.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11350.1; -; Genomic_DNA.
DR EMBL; BC005214; AAH05214.1; -; mRNA.
DR PIR; A42578; A42578.
DR RefSeq; NP_036330.1; NM_012198.3.
DR UniGene; Hs.377894; -.
DR PDB; 1F4O; X-ray; 2.50 A; A/B=53-217.
DR PDB; 1F4Q; X-ray; 1.90 A; A/B=53-217.
DR PDB; 1K94; X-ray; 1.70 A; A/B=53-217.
DR PDB; 1K95; X-ray; 1.90 A; A=53-217.
DR PDBsum; 1F4O; -.
DR PDBsum; 1F4Q; -.
DR PDBsum; 1K94; -.
DR PDBsum; 1K95; -.
DR ProteinModelPortal; P28676; -.
DR SMR; P28676; 53-217.
DR IntAct; P28676; 4.
DR MINT; MINT-267888; -.
DR STRING; 9606.ENSP00000394842; -.
DR PhosphoSite; P28676; -.
DR DMDM; 1170014; -.
DR PaxDb; P28676; -.
DR PeptideAtlas; P28676; -.
DR PRIDE; P28676; -.
DR DNASU; 25801; -.
DR Ensembl; ENST00000437150; ENSP00000394842; ENSG00000115271.
DR GeneID; 25801; -.
DR KEGG; hsa:25801; -.
DR UCSC; uc002ucg.3; human.
DR CTD; 25801; -.
DR GeneCards; GC02P163164; -.
DR HGNC; HGNC:15990; GCA.
DR HPA; HPA035033; -.
DR HPA; HPA035034; -.
DR MIM; 607030; gene.
DR neXtProt; NX_P28676; -.
DR PharmGKB; PA28602; -.
DR eggNOG; NOG298587; -.
DR HOGENOM; HOG000231982; -.
DR HOVERGEN; HBG004492; -.
DR InParanoid; P28676; -.
DR OMA; SAGDPMW; -.
DR PhylomeDB; P28676; -.
DR ChiTaRS; GCA; human.
DR EvolutionaryTrace; P28676; -.
DR GeneWiki; GCA_(gene); -.
DR GenomeRNAi; 25801; -.
DR NextBio; 47003; -.
DR PRO; PR:P28676; -.
DR ArrayExpress; P28676; -.
DR Bgee; P28676; -.
DR CleanEx; HS_GCA; -.
DR Genevestigator; P28676; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13405; EF-hand_6; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 217 Grancalcin.
FT /FTId=PRO_0000073721.
FT DOMAIN 48 83 EF-hand 1.
FT DOMAIN 89 122 EF-hand 2.
FT DOMAIN 119 154 EF-hand 3.
FT DOMAIN 155 180 EF-hand 4.
FT CA_BIND 65 72 1.
FT CA_BIND 132 143 2.
FT CA_BIND 161 172 3 (Potential).
FT VARIANT 80 80 S -> A (in dbSNP:rs17783344).
FT /FTId=VAR_048657.
FT CONFLICT 166 166 R -> D (in Ref. 7; AA sequence).
FT HELIX 54 62
FT HELIX 63 65
FT HELIX 70 80
FT TURN 81 85
FT HELIX 91 101
FT STRAND 106 109
FT HELIX 111 131
FT HELIX 133 135
FT STRAND 138 140
FT HELIX 141 150
FT HELIX 157 167
FT STRAND 169 171
FT STRAND 172 174
FT HELIX 175 193
FT STRAND 201 206
FT HELIX 207 215
SQ SEQUENCE 217 AA; 24010 MW; 88CA4DDF835AFFE4 CRC64;
MAYPGYGGGF GNFSIQVPGM QMGQPVPETG PAILLDGYSG PAYSDTYSSA GDSVYTYFSA
VAGQDGEVDA EELQRCLTQS GINGTYSPFS LETCRIMIAM LDRDHTGKMG FNAFKELWAA
LNAWKENFMT VDQDGSGTVE HHELRQAIGL MGYRLSPQTL TTIVKRYSKN GRIFFDDYVA
CCVKLRALTD FFRKRDHLQQ GSANFIYDDF LQGTMAI
//
MIM
607030
*RECORD*
*FIELD* NO
607030
*FIELD* TI
*607030 GRANCALCIN; GCA
*FIELD* TX
CLONING
By probing with antibody to the purified protein, Boyhan et al. (1992)
read morecloned GCA, which they called grancalcin, from a promyocytic cell line
expression library. The deduced 217-amino acid protein has a calculated
molecular mass of 24 kD. The sequence contains an EF-hand
calcium-binding region, a potential phosphorylation site, and 2
potential N-glycosylation sites. GCA shares 58% identity over 192 amino
acids with sorcin (182520), and about 30% identity over the
calcium-binding domains of calpains (see 114220). Northern blot analysis
revealed abundant expression of a 1.65-kb transcript in bone marrow and
weaker expression in neutrophils, myeloid leukemic cells, and 2
Epstein-Barr virus-transformed B-cell lines. By Western blot analysis, a
28-kD protein was observed in B and T cells at low concentrations, and
at higher levels in neutrophils and macrophages. Subcellular
fractionation showed localization to be dependent upon Ca(2+) and
Mg(2+). In the absence of divalent cation, grancalcin localized to the
cytosolic fraction; with Mg(2+) alone, it partitioned with the granule
fraction; and in the presence of Mg(2+) and Ca(2+), it associated with
both the granule and membrane fractions.
Teahan et al. (1992) purified grancalcin from leukopheresis samples of
patients with chronic granulocytic leukemia. The purified protein
migrated as a 28-kD protein by SDS-PAGE and formed homodimers of 55 kD
upon gel filtration that was independent of reducing agents. No
biochemical evidence was found for phosphorylation or glycosylation.
Calcium binding was suggested by the difference in migration on SDS/PAGE
between calcium-loaded and calcium-depleted preparations, and was
confirmed by the binding of Ca(2+) to slot blots of the native protein.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the GCA
gene to chromosome 2 (TMAP stSG15301).
*FIELD* RF
1. Boyhan, A.; Casimir, C. M.; French, J. K.; Teahan, C. G.; Segal,
A. W.: Molecular cloning and characterization of grancalcin, a novel
EF-hand calcium-binding protein abundant in neutrophils and monocytes. J.
Biol. Chem. 267: 2928-2933, 1992.
2. Teahan, C. G.; Totty, N. F.; Segal, A. W.: Isolation and characterization
of grancalcin, a novel 28 kDa EF-hand calcium-binding protein from
human neutrophils. Biochem. J. 286: 549-554, 1992.
*FIELD* CD
Patricia A. Hartz: 6/11/2002
*FIELD* ED
carol: 06/13/2002
*RECORD*
*FIELD* NO
607030
*FIELD* TI
*607030 GRANCALCIN; GCA
*FIELD* TX
CLONING
By probing with antibody to the purified protein, Boyhan et al. (1992)
read morecloned GCA, which they called grancalcin, from a promyocytic cell line
expression library. The deduced 217-amino acid protein has a calculated
molecular mass of 24 kD. The sequence contains an EF-hand
calcium-binding region, a potential phosphorylation site, and 2
potential N-glycosylation sites. GCA shares 58% identity over 192 amino
acids with sorcin (182520), and about 30% identity over the
calcium-binding domains of calpains (see 114220). Northern blot analysis
revealed abundant expression of a 1.65-kb transcript in bone marrow and
weaker expression in neutrophils, myeloid leukemic cells, and 2
Epstein-Barr virus-transformed B-cell lines. By Western blot analysis, a
28-kD protein was observed in B and T cells at low concentrations, and
at higher levels in neutrophils and macrophages. Subcellular
fractionation showed localization to be dependent upon Ca(2+) and
Mg(2+). In the absence of divalent cation, grancalcin localized to the
cytosolic fraction; with Mg(2+) alone, it partitioned with the granule
fraction; and in the presence of Mg(2+) and Ca(2+), it associated with
both the granule and membrane fractions.
Teahan et al. (1992) purified grancalcin from leukopheresis samples of
patients with chronic granulocytic leukemia. The purified protein
migrated as a 28-kD protein by SDS-PAGE and formed homodimers of 55 kD
upon gel filtration that was independent of reducing agents. No
biochemical evidence was found for phosphorylation or glycosylation.
Calcium binding was suggested by the difference in migration on SDS/PAGE
between calcium-loaded and calcium-depleted preparations, and was
confirmed by the binding of Ca(2+) to slot blots of the native protein.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the GCA
gene to chromosome 2 (TMAP stSG15301).
*FIELD* RF
1. Boyhan, A.; Casimir, C. M.; French, J. K.; Teahan, C. G.; Segal,
A. W.: Molecular cloning and characterization of grancalcin, a novel
EF-hand calcium-binding protein abundant in neutrophils and monocytes. J.
Biol. Chem. 267: 2928-2933, 1992.
2. Teahan, C. G.; Totty, N. F.; Segal, A. W.: Isolation and characterization
of grancalcin, a novel 28 kDa EF-hand calcium-binding protein from
human neutrophils. Biochem. J. 286: 549-554, 1992.
*FIELD* CD
Patricia A. Hartz: 6/11/2002
*FIELD* ED
carol: 06/13/2002