Full text data of CALU
CALU
[Confidence: low (only semi-automatic identification from reviews)]
Calumenin (Crocalbin; IEF SSP 9302; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Calumenin (Crocalbin; IEF SSP 9302; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43852
ID CALU_HUMAN Reviewed; 315 AA.
AC O43852; B3KPG9; D6QS48; D6QS49; D6QS50; D6QS51; D6QS52; D6QS53;
read moreAC D6QS54; D6QS55; D6QS56; D6QS57; D6QS58; D6QS59; F5H1Q9; F5H879;
AC O60456; Q6FHB9; Q96RL3; Q9NR43;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Calumenin;
DE AltName: Full=Crocalbin;
DE AltName: Full=IEF SSP 9302;
DE Flags: Precursor;
GN Name=CALU;
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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP CALCIUM-BINDING.
RC TISSUE=Keratinocyte;
RX PubMed=9675259; DOI=10.1016/S0167-4838(98)00089-2;
RA Vorum H., Liu X., Madsen P., Rasmussen H.H., Honore B.;
RT "Molecular cloning of a cDNA encoding human calumenin, expression in
RT Escherichia coli and analysis of its Ca2+-binding activity.";
RL Biochim. Biophys. Acta 1386:121-131(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9598325; DOI=10.1006/geno.1998.5245;
RA Yabe D., Taniwaki M., Nakamura T., Kanazawa N., Tashiro K., Honjo T.;
RT "Human calumenin gene (CALU): cDNA isolation and chromosomal mapping
RT to 7q32.";
RL Genomics 49:331-333(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Peterson R.E. Jr., Watson D.K.;
RT "Novel splice variant of human calumenin.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6; 7; 8; 9; 10; 11; 12;
RP 13; 14 AND 15), AND VARIANT GLN-4.
RA Wang Q., Chen L., Shen B.R., Feng H., Zheng P.L., Teng J.L.,
RA Chen J.G.;
RT "Calumenin isoforms and their intracellular and extracellular
RT function.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-315 (ISOFORM 2).
RC TISSUE=Brain;
RA Hseu M.-J., Tzeng M.-C.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PROTEIN SEQUENCE OF 20-27.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=10222138; DOI=10.1006/excr.1999.4431;
RA Vorum H., Hager H., Christensen B.M., Nielsen S., Honore B.;
RT "Human calumenin localizes to the secretory pathway and is secreted to
RT the medium.";
RL Exp. Cell Res. 248:473-481(1999).
RN [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND THR-65, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-131, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP GLYCOSYLATION AT ASN-131.
RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND THR-65, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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).
CC -!- FUNCTION: Involved in regulation of vitamin K-dependent
CC carboxylation of multiple N-terminal glutamate residues. Seems to
CC inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low
CC affinity (By similarity).
CC -!- SUBUNIT: Interacts with GGCX (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Secreted.
CC Melanosome. Sarcoplasmic reticulum lumen (By similarity).
CC Note=Identified by mass spectrometry in melanosome fractions from
CC stage I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=15;
CC Name=1;
CC IsoId=O43852-1; Sequence=Displayed;
CC Name=2; Synonyms=Crocalbin;
CC IsoId=O43852-2; Sequence=VSP_007317;
CC Name=3;
CC IsoId=O43852-3; Sequence=VSP_043570;
CC Name=4;
CC IsoId=O43852-4; Sequence=VSP_043570, VSP_007317;
CC Name=5;
CC IsoId=O43852-5; Sequence=VSP_045946;
CC Name=6;
CC IsoId=O43852-6; Sequence=VSP_045951;
CC Name=7;
CC IsoId=O43852-7; Sequence=VSP_007317, VSP_045944, VSP_045945;
CC Name=8;
CC IsoId=O43852-8; Sequence=VSP_007317, VSP_045949;
CC Name=9;
CC IsoId=O43852-9; Sequence=VSP_045941;
CC Name=10;
CC IsoId=O43852-10; Sequence=VSP_045950;
CC Name=11;
CC IsoId=O43852-11; Sequence=VSP_045947, VSP_045948;
CC Name=12;
CC IsoId=O43852-12; Sequence=VSP_045940;
CC Name=13;
CC IsoId=O43852-13; Sequence=VSP_045942, VSP_045943;
CC Name=14;
CC IsoId=O43852-14; Sequence=VSP_043570, VSP_045942, VSP_045943;
CC Name=15;
CC IsoId=O43852-15; Sequence=VSP_045939;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high
CC levels in heart, placenta and skeletal muscle, at lower levels in
CC lung, kidney and pancreas and at very low levels in brain and
CC liver.
CC -!- SIMILARITY: Belongs to the CREC family.
CC -!- SIMILARITY: Contains 6 EF-hand domains.
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DR EMBL; U67280; AAB97725.1; -; mRNA.
DR EMBL; AF013759; AAC17216.1; -; mRNA.
DR EMBL; AF345637; AAK72908.1; -; mRNA.
DR EMBL; HM002604; ADG45004.1; -; mRNA.
DR EMBL; HM002605; ADG45005.1; -; mRNA.
DR EMBL; HM002606; ADG45006.1; -; mRNA.
DR EMBL; HM002607; ADG45007.1; -; mRNA.
DR EMBL; HM002608; ADG45008.1; -; mRNA.
DR EMBL; HM002609; ADG45009.1; -; mRNA.
DR EMBL; HM002610; ADG45010.1; -; mRNA.
DR EMBL; HM002611; ADG45011.1; -; mRNA.
DR EMBL; HM002612; ADG45012.1; -; mRNA.
DR EMBL; HM002613; ADG45013.1; -; mRNA.
DR EMBL; HM002614; ADG45014.1; -; mRNA.
DR EMBL; HM002615; ADG45015.1; -; mRNA.
DR EMBL; HM002616; ADG45016.1; -; mRNA.
DR EMBL; AK056338; BAG51681.1; -; mRNA.
DR EMBL; CR541835; CAG46634.1; -; mRNA.
DR EMBL; AC024952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471070; EAW83679.1; -; Genomic_DNA.
DR EMBL; BC013383; AAH13383.1; -; mRNA.
DR EMBL; AF257659; AAF76141.1; -; mRNA.
DR RefSeq; NP_001124146.1; NM_001130674.2.
DR RefSeq; NP_001186600.1; NM_001199671.1.
DR RefSeq; NP_001186601.1; NM_001199672.1.
DR RefSeq; NP_001186602.1; NM_001199673.1.
DR RefSeq; NP_001210.1; NM_001219.4.
DR UniGene; Hs.743262; -.
DR UniGene; Hs.7753; -.
DR ProteinModelPortal; O43852; -.
DR SMR; O43852; 69-292.
DR IntAct; O43852; 17.
DR STRING; 9606.ENSP00000249364; -.
DR PhosphoSite; O43852; -.
DR DOSAC-COBS-2DPAGE; O43852; -.
DR PaxDb; O43852; -.
DR PRIDE; O43852; -.
DR DNASU; 813; -.
DR Ensembl; ENST00000249364; ENSP00000249364; ENSG00000128595.
DR Ensembl; ENST00000449187; ENSP00000408838; ENSG00000128595.
DR Ensembl; ENST00000479257; ENSP00000420381; ENSG00000128595.
DR Ensembl; ENST00000535011; ENSP00000442110; ENSG00000128595.
DR Ensembl; ENST00000535623; ENSP00000439139; ENSG00000128595.
DR Ensembl; ENST00000538546; ENSP00000438994; ENSG00000128595.
DR Ensembl; ENST00000542996; ENSP00000438248; ENSG00000128595.
DR GeneID; 813; -.
DR KEGG; hsa:813; -.
DR UCSC; uc003vnq.3; human.
DR CTD; 813; -.
DR GeneCards; GC07P128438; -.
DR HGNC; HGNC:1458; CALU.
DR HPA; HPA006018; -.
DR MIM; 603420; gene.
DR neXtProt; NX_O43852; -.
DR PharmGKB; PA26047; -.
DR eggNOG; NOG271367; -.
DR HOGENOM; HOG000230934; -.
DR HOVERGEN; HBG002834; -.
DR OMA; WIQYTQR; -.
DR OrthoDB; EOG73Z2TD; -.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; CALU; human.
DR GeneWiki; CALU_(gene); -.
DR GenomeRNAi; 813; -.
DR NextBio; 3296; -.
DR PRO; PR:O43852; -.
DR ArrayExpress; O43852; -.
DR Bgee; O43852; -.
DR CleanEx; HS_CALU; -.
DR Genevestigator; O43852; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR Gene3D; 1.10.238.10; -; 2.
DR InterPro; IPR027239; Calumenin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR10827:SF34; PTHR10827:SF34; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat; Sarcoplasmic reticulum; Secreted; Signal.
FT SIGNAL 1 19
FT CHAIN 20 315 Calumenin.
FT /FTId=PRO_0000004153.
FT DOMAIN 68 103 EF-hand 1.
FT DOMAIN 104 139 EF-hand 2.
FT DOMAIN 151 186 EF-hand 3.
FT DOMAIN 188 223 EF-hand 4.
FT DOMAIN 229 264 EF-hand 5.
FT DOMAIN 265 300 EF-hand 6.
FT CA_BIND 81 92 1 (Potential).
FT CA_BIND 117 128 2 (Potential).
FT CA_BIND 164 175 3; possibly ancestral (Potential).
FT CA_BIND 201 212 4 (Potential).
FT CA_BIND 242 253 5 (Potential).
FT CA_BIND 278 289 6 (Potential).
FT MOTIF 312 315 Prevents secretion from ER (By
FT similarity).
FT MOD_RES 44 44 Phosphoserine.
FT MOD_RES 65 65 Phosphothreonine.
FT CARBOHYD 131 131 N-linked (GlcNAc...) (complex).
FT VAR_SEQ 1 151 Missing (in isoform 15).
FT /FTId=VSP_045939.
FT VAR_SEQ 1 1 M -> MKETDLIIM (in isoform 3, isoform 4
FT and isoform 14).
FT /FTId=VSP_043570.
FT VAR_SEQ 75 315 Missing (in isoform 12).
FT /FTId=VSP_045940.
FT VAR_SEQ 75 137 KIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKG
FT HDLNEDGLVSWEEYKNATYGYV -> MIVDKIDADKDGFVT
FT EGELKSWIKHAQKKYIYDNVENQWQEFDMNQDGLISWDEYR
FT NVTYGTY (in isoform 2, isoform 4, isoform
FT 7 and isoform 8).
FT /FTId=VSP_007317.
FT VAR_SEQ 94 254 Missing (in isoform 9).
FT /FTId=VSP_045941.
FT VAR_SEQ 139 139 D -> E (in isoform 13 and isoform 14).
FT /FTId=VSP_045942.
FT VAR_SEQ 140 315 Missing (in isoform 13 and isoform 14).
FT /FTId=VSP_045943.
FT VAR_SEQ 154 161 VRDERRFK -> GILMSRNG (in isoform 7).
FT /FTId=VSP_045944.
FT VAR_SEQ 162 315 Missing (in isoform 7).
FT /FTId=VSP_045945.
FT VAR_SEQ 164 249 Missing (in isoform 5).
FT /FTId=VSP_045946.
FT VAR_SEQ 165 170 KDGDLI -> RARAVC (in isoform 11).
FT /FTId=VSP_045947.
FT VAR_SEQ 171 315 Missing (in isoform 11).
FT /FTId=VSP_045948.
FT VAR_SEQ 172 285 Missing (in isoform 8).
FT /FTId=VSP_045949.
FT VAR_SEQ 216 315 DMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKD
FT WILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLF
FT VGSQATDFGEALVRHDEF -> WQAYQGGDR (in
FT isoform 10).
FT /FTId=VSP_045950.
FT VAR_SEQ 226 275 Missing (in isoform 6).
FT /FTId=VSP_045951.
FT VARIANT 4 4 R -> Q (in dbSNP:rs2290228).
FT /FTId=VAR_022051.
FT CONFLICT 48 48 D -> G (in Ref. 4; ADG45013).
FT CONFLICT 84 84 K -> R (in Ref. 4; ADG45007).
FT CONFLICT 90 90 V -> A (in Ref. 4; ADG45010).
FT CONFLICT 117 117 D -> G (in Ref. 4; ADG45007).
FT CONFLICT 118 118 L -> H (in Ref. 4; ADG45011).
FT CONFLICT 147 147 F -> S (in Ref. 4; ADG45012).
FT CONFLICT 188 188 M -> V (in Ref. 4; ADG45015).
FT CONFLICT 207 207 F -> L (in Ref. 1; AAB97725).
FT CONFLICT 232 232 T -> S (in Ref. 4; ADG45015).
FT CONFLICT 267 267 E -> V (in Ref. 6; CAG46634).
SQ SEQUENCE 315 AA; 37107 MW; 25BAE5A99B527375 CRC64;
MDLRQFLMCL SLCTAFALSK PTEKKDRVHH EPQLSDKVHN DAQSFDYDHD AFLGAEEAKT
FDQLTPEESK ERLGKIVSKI DGDKDGFVTV DELKDWIKFA QKRWIYEDVE RQWKGHDLNE
DGLVSWEEYK NATYGYVLDD PDPDDGFNYK QMMVRDERRF KMADKDGDLI ATKEEFTAFL
HPEEYDYMKD IVVQETMEDI DKNADGFIDL EEYIGDMYSH DGNTDEPEWV KTEREQFVEF
RDKNRDGKMD KEETKDWILP SDYDHAEAEA RHLVYESDQN KDGKLTKEEI VDKYDLFVGS
QATDFGEALV RHDEF
//
ID CALU_HUMAN Reviewed; 315 AA.
AC O43852; B3KPG9; D6QS48; D6QS49; D6QS50; D6QS51; D6QS52; D6QS53;
read moreAC D6QS54; D6QS55; D6QS56; D6QS57; D6QS58; D6QS59; F5H1Q9; F5H879;
AC O60456; Q6FHB9; Q96RL3; Q9NR43;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Calumenin;
DE AltName: Full=Crocalbin;
DE AltName: Full=IEF SSP 9302;
DE Flags: Precursor;
GN Name=CALU;
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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP CALCIUM-BINDING.
RC TISSUE=Keratinocyte;
RX PubMed=9675259; DOI=10.1016/S0167-4838(98)00089-2;
RA Vorum H., Liu X., Madsen P., Rasmussen H.H., Honore B.;
RT "Molecular cloning of a cDNA encoding human calumenin, expression in
RT Escherichia coli and analysis of its Ca2+-binding activity.";
RL Biochim. Biophys. Acta 1386:121-131(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9598325; DOI=10.1006/geno.1998.5245;
RA Yabe D., Taniwaki M., Nakamura T., Kanazawa N., Tashiro K., Honjo T.;
RT "Human calumenin gene (CALU): cDNA isolation and chromosomal mapping
RT to 7q32.";
RL Genomics 49:331-333(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Peterson R.E. Jr., Watson D.K.;
RT "Novel splice variant of human calumenin.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6; 7; 8; 9; 10; 11; 12;
RP 13; 14 AND 15), AND VARIANT GLN-4.
RA Wang Q., Chen L., Shen B.R., Feng H., Zheng P.L., Teng J.L.,
RA Chen J.G.;
RT "Calumenin isoforms and their intracellular and extracellular
RT function.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-315 (ISOFORM 2).
RC TISSUE=Brain;
RA Hseu M.-J., Tzeng M.-C.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PROTEIN SEQUENCE OF 20-27.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=10222138; DOI=10.1006/excr.1999.4431;
RA Vorum H., Hager H., Christensen B.M., Nielsen S., Honore B.;
RT "Human calumenin localizes to the secretory pathway and is secreted to
RT the medium.";
RL Exp. Cell Res. 248:473-481(1999).
RN [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND THR-65, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-131, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP GLYCOSYLATION AT ASN-131.
RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND THR-65, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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).
CC -!- FUNCTION: Involved in regulation of vitamin K-dependent
CC carboxylation of multiple N-terminal glutamate residues. Seems to
CC inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low
CC affinity (By similarity).
CC -!- SUBUNIT: Interacts with GGCX (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Secreted.
CC Melanosome. Sarcoplasmic reticulum lumen (By similarity).
CC Note=Identified by mass spectrometry in melanosome fractions from
CC stage I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=15;
CC Name=1;
CC IsoId=O43852-1; Sequence=Displayed;
CC Name=2; Synonyms=Crocalbin;
CC IsoId=O43852-2; Sequence=VSP_007317;
CC Name=3;
CC IsoId=O43852-3; Sequence=VSP_043570;
CC Name=4;
CC IsoId=O43852-4; Sequence=VSP_043570, VSP_007317;
CC Name=5;
CC IsoId=O43852-5; Sequence=VSP_045946;
CC Name=6;
CC IsoId=O43852-6; Sequence=VSP_045951;
CC Name=7;
CC IsoId=O43852-7; Sequence=VSP_007317, VSP_045944, VSP_045945;
CC Name=8;
CC IsoId=O43852-8; Sequence=VSP_007317, VSP_045949;
CC Name=9;
CC IsoId=O43852-9; Sequence=VSP_045941;
CC Name=10;
CC IsoId=O43852-10; Sequence=VSP_045950;
CC Name=11;
CC IsoId=O43852-11; Sequence=VSP_045947, VSP_045948;
CC Name=12;
CC IsoId=O43852-12; Sequence=VSP_045940;
CC Name=13;
CC IsoId=O43852-13; Sequence=VSP_045942, VSP_045943;
CC Name=14;
CC IsoId=O43852-14; Sequence=VSP_043570, VSP_045942, VSP_045943;
CC Name=15;
CC IsoId=O43852-15; Sequence=VSP_045939;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high
CC levels in heart, placenta and skeletal muscle, at lower levels in
CC lung, kidney and pancreas and at very low levels in brain and
CC liver.
CC -!- SIMILARITY: Belongs to the CREC family.
CC -!- SIMILARITY: Contains 6 EF-hand domains.
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DR EMBL; U67280; AAB97725.1; -; mRNA.
DR EMBL; AF013759; AAC17216.1; -; mRNA.
DR EMBL; AF345637; AAK72908.1; -; mRNA.
DR EMBL; HM002604; ADG45004.1; -; mRNA.
DR EMBL; HM002605; ADG45005.1; -; mRNA.
DR EMBL; HM002606; ADG45006.1; -; mRNA.
DR EMBL; HM002607; ADG45007.1; -; mRNA.
DR EMBL; HM002608; ADG45008.1; -; mRNA.
DR EMBL; HM002609; ADG45009.1; -; mRNA.
DR EMBL; HM002610; ADG45010.1; -; mRNA.
DR EMBL; HM002611; ADG45011.1; -; mRNA.
DR EMBL; HM002612; ADG45012.1; -; mRNA.
DR EMBL; HM002613; ADG45013.1; -; mRNA.
DR EMBL; HM002614; ADG45014.1; -; mRNA.
DR EMBL; HM002615; ADG45015.1; -; mRNA.
DR EMBL; HM002616; ADG45016.1; -; mRNA.
DR EMBL; AK056338; BAG51681.1; -; mRNA.
DR EMBL; CR541835; CAG46634.1; -; mRNA.
DR EMBL; AC024952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471070; EAW83679.1; -; Genomic_DNA.
DR EMBL; BC013383; AAH13383.1; -; mRNA.
DR EMBL; AF257659; AAF76141.1; -; mRNA.
DR RefSeq; NP_001124146.1; NM_001130674.2.
DR RefSeq; NP_001186600.1; NM_001199671.1.
DR RefSeq; NP_001186601.1; NM_001199672.1.
DR RefSeq; NP_001186602.1; NM_001199673.1.
DR RefSeq; NP_001210.1; NM_001219.4.
DR UniGene; Hs.743262; -.
DR UniGene; Hs.7753; -.
DR ProteinModelPortal; O43852; -.
DR SMR; O43852; 69-292.
DR IntAct; O43852; 17.
DR STRING; 9606.ENSP00000249364; -.
DR PhosphoSite; O43852; -.
DR DOSAC-COBS-2DPAGE; O43852; -.
DR PaxDb; O43852; -.
DR PRIDE; O43852; -.
DR DNASU; 813; -.
DR Ensembl; ENST00000249364; ENSP00000249364; ENSG00000128595.
DR Ensembl; ENST00000449187; ENSP00000408838; ENSG00000128595.
DR Ensembl; ENST00000479257; ENSP00000420381; ENSG00000128595.
DR Ensembl; ENST00000535011; ENSP00000442110; ENSG00000128595.
DR Ensembl; ENST00000535623; ENSP00000439139; ENSG00000128595.
DR Ensembl; ENST00000538546; ENSP00000438994; ENSG00000128595.
DR Ensembl; ENST00000542996; ENSP00000438248; ENSG00000128595.
DR GeneID; 813; -.
DR KEGG; hsa:813; -.
DR UCSC; uc003vnq.3; human.
DR CTD; 813; -.
DR GeneCards; GC07P128438; -.
DR HGNC; HGNC:1458; CALU.
DR HPA; HPA006018; -.
DR MIM; 603420; gene.
DR neXtProt; NX_O43852; -.
DR PharmGKB; PA26047; -.
DR eggNOG; NOG271367; -.
DR HOGENOM; HOG000230934; -.
DR HOVERGEN; HBG002834; -.
DR OMA; WIQYTQR; -.
DR OrthoDB; EOG73Z2TD; -.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; CALU; human.
DR GeneWiki; CALU_(gene); -.
DR GenomeRNAi; 813; -.
DR NextBio; 3296; -.
DR PRO; PR:O43852; -.
DR ArrayExpress; O43852; -.
DR Bgee; O43852; -.
DR CleanEx; HS_CALU; -.
DR Genevestigator; O43852; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR Gene3D; 1.10.238.10; -; 2.
DR InterPro; IPR027239; Calumenin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR10827:SF34; PTHR10827:SF34; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat; Sarcoplasmic reticulum; Secreted; Signal.
FT SIGNAL 1 19
FT CHAIN 20 315 Calumenin.
FT /FTId=PRO_0000004153.
FT DOMAIN 68 103 EF-hand 1.
FT DOMAIN 104 139 EF-hand 2.
FT DOMAIN 151 186 EF-hand 3.
FT DOMAIN 188 223 EF-hand 4.
FT DOMAIN 229 264 EF-hand 5.
FT DOMAIN 265 300 EF-hand 6.
FT CA_BIND 81 92 1 (Potential).
FT CA_BIND 117 128 2 (Potential).
FT CA_BIND 164 175 3; possibly ancestral (Potential).
FT CA_BIND 201 212 4 (Potential).
FT CA_BIND 242 253 5 (Potential).
FT CA_BIND 278 289 6 (Potential).
FT MOTIF 312 315 Prevents secretion from ER (By
FT similarity).
FT MOD_RES 44 44 Phosphoserine.
FT MOD_RES 65 65 Phosphothreonine.
FT CARBOHYD 131 131 N-linked (GlcNAc...) (complex).
FT VAR_SEQ 1 151 Missing (in isoform 15).
FT /FTId=VSP_045939.
FT VAR_SEQ 1 1 M -> MKETDLIIM (in isoform 3, isoform 4
FT and isoform 14).
FT /FTId=VSP_043570.
FT VAR_SEQ 75 315 Missing (in isoform 12).
FT /FTId=VSP_045940.
FT VAR_SEQ 75 137 KIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKG
FT HDLNEDGLVSWEEYKNATYGYV -> MIVDKIDADKDGFVT
FT EGELKSWIKHAQKKYIYDNVENQWQEFDMNQDGLISWDEYR
FT NVTYGTY (in isoform 2, isoform 4, isoform
FT 7 and isoform 8).
FT /FTId=VSP_007317.
FT VAR_SEQ 94 254 Missing (in isoform 9).
FT /FTId=VSP_045941.
FT VAR_SEQ 139 139 D -> E (in isoform 13 and isoform 14).
FT /FTId=VSP_045942.
FT VAR_SEQ 140 315 Missing (in isoform 13 and isoform 14).
FT /FTId=VSP_045943.
FT VAR_SEQ 154 161 VRDERRFK -> GILMSRNG (in isoform 7).
FT /FTId=VSP_045944.
FT VAR_SEQ 162 315 Missing (in isoform 7).
FT /FTId=VSP_045945.
FT VAR_SEQ 164 249 Missing (in isoform 5).
FT /FTId=VSP_045946.
FT VAR_SEQ 165 170 KDGDLI -> RARAVC (in isoform 11).
FT /FTId=VSP_045947.
FT VAR_SEQ 171 315 Missing (in isoform 11).
FT /FTId=VSP_045948.
FT VAR_SEQ 172 285 Missing (in isoform 8).
FT /FTId=VSP_045949.
FT VAR_SEQ 216 315 DMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKD
FT WILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLF
FT VGSQATDFGEALVRHDEF -> WQAYQGGDR (in
FT isoform 10).
FT /FTId=VSP_045950.
FT VAR_SEQ 226 275 Missing (in isoform 6).
FT /FTId=VSP_045951.
FT VARIANT 4 4 R -> Q (in dbSNP:rs2290228).
FT /FTId=VAR_022051.
FT CONFLICT 48 48 D -> G (in Ref. 4; ADG45013).
FT CONFLICT 84 84 K -> R (in Ref. 4; ADG45007).
FT CONFLICT 90 90 V -> A (in Ref. 4; ADG45010).
FT CONFLICT 117 117 D -> G (in Ref. 4; ADG45007).
FT CONFLICT 118 118 L -> H (in Ref. 4; ADG45011).
FT CONFLICT 147 147 F -> S (in Ref. 4; ADG45012).
FT CONFLICT 188 188 M -> V (in Ref. 4; ADG45015).
FT CONFLICT 207 207 F -> L (in Ref. 1; AAB97725).
FT CONFLICT 232 232 T -> S (in Ref. 4; ADG45015).
FT CONFLICT 267 267 E -> V (in Ref. 6; CAG46634).
SQ SEQUENCE 315 AA; 37107 MW; 25BAE5A99B527375 CRC64;
MDLRQFLMCL SLCTAFALSK PTEKKDRVHH EPQLSDKVHN DAQSFDYDHD AFLGAEEAKT
FDQLTPEESK ERLGKIVSKI DGDKDGFVTV DELKDWIKFA QKRWIYEDVE RQWKGHDLNE
DGLVSWEEYK NATYGYVLDD PDPDDGFNYK QMMVRDERRF KMADKDGDLI ATKEEFTAFL
HPEEYDYMKD IVVQETMEDI DKNADGFIDL EEYIGDMYSH DGNTDEPEWV KTEREQFVEF
RDKNRDGKMD KEETKDWILP SDYDHAEAEA RHLVYESDQN KDGKLTKEEI VDKYDLFVGS
QATDFGEALV RHDEF
//
MIM
603420
*RECORD*
*FIELD* NO
603420
*FIELD* TI
*603420 CALUMENIN; CALU
*FIELD* TX
CLONING
Many calcium-binding proteins are reported to be localized in the
read moreendoplasmic reticulum (ER) and involved in such ER functions as protein
folding and sorting. Among these are RCN1 (602735), RCN2 (602584), and
calumenin (CALU), which form a novel family of calcium-binding proteins
in the ER and Golgi apparatus. By searching sequence databases with a
mouse Calu cDNA sequence (Yabe et al., 1997), Yabe et al. (1998)
identified a human CALU EST, which they used to clone a full-length CALU
cDNA. The cDNA encodes a deduced 315-amino acid protein containing 6
EF-hand motifs, 1 potential N-glycosylation site, and a C-terminal ER
retention signal. The human and mouse CALU proteins are 98% identical.
Northern blot analysis demonstrated that the 3.4-kb CALU mRNA is
ubiquitously expressed in human tissues. Southern blot analysis using a
human CALU cDNA probe detected bands in a variety of species.
MAPPING
Yabe et al. (1997) mapped the mouse Calu gene to the proximal portion of
chromosome 7. By fluorescence in situ hybridization, Yabe et al. (1998)
localized the human CALU gene to 7q32, which was an unexpected result
due to the homology of synteny between proximal mouse chromosome 7 and
human 19q13.2-q13.3.
*FIELD* RF
1. Yabe, D.; Nakamura, T.; Kanazawa, N.; Tashiro, K.; Honjo, T.:
Calumenin, a Ca(2+)-binding protein retained in the endoplasmic reticulum
with a novel carboxyl-terminal sequence, HDEF. J. Biol. Chem. 272:
18232-18239, 1997.
2. Yabe, D.; Taniwaki, M.; Nakamura, T.; Kanazawa, N.; Tashiro, K.;
Honjo, T.: Human calumenin gene (CALU): cDNA isolation and chromosomal
mapping to 7q32. Genomics 49: 331-333, 1998.
*FIELD* CD
Sheryl A. Jankowski: 1/12/1999
*FIELD* ED
carol: 06/22/2012
psherman: 1/12/1999
*RECORD*
*FIELD* NO
603420
*FIELD* TI
*603420 CALUMENIN; CALU
*FIELD* TX
CLONING
Many calcium-binding proteins are reported to be localized in the
read moreendoplasmic reticulum (ER) and involved in such ER functions as protein
folding and sorting. Among these are RCN1 (602735), RCN2 (602584), and
calumenin (CALU), which form a novel family of calcium-binding proteins
in the ER and Golgi apparatus. By searching sequence databases with a
mouse Calu cDNA sequence (Yabe et al., 1997), Yabe et al. (1998)
identified a human CALU EST, which they used to clone a full-length CALU
cDNA. The cDNA encodes a deduced 315-amino acid protein containing 6
EF-hand motifs, 1 potential N-glycosylation site, and a C-terminal ER
retention signal. The human and mouse CALU proteins are 98% identical.
Northern blot analysis demonstrated that the 3.4-kb CALU mRNA is
ubiquitously expressed in human tissues. Southern blot analysis using a
human CALU cDNA probe detected bands in a variety of species.
MAPPING
Yabe et al. (1997) mapped the mouse Calu gene to the proximal portion of
chromosome 7. By fluorescence in situ hybridization, Yabe et al. (1998)
localized the human CALU gene to 7q32, which was an unexpected result
due to the homology of synteny between proximal mouse chromosome 7 and
human 19q13.2-q13.3.
*FIELD* RF
1. Yabe, D.; Nakamura, T.; Kanazawa, N.; Tashiro, K.; Honjo, T.:
Calumenin, a Ca(2+)-binding protein retained in the endoplasmic reticulum
with a novel carboxyl-terminal sequence, HDEF. J. Biol. Chem. 272:
18232-18239, 1997.
2. Yabe, D.; Taniwaki, M.; Nakamura, T.; Kanazawa, N.; Tashiro, K.;
Honjo, T.: Human calumenin gene (CALU): cDNA isolation and chromosomal
mapping to 7q32. Genomics 49: 331-333, 1998.
*FIELD* CD
Sheryl A. Jankowski: 1/12/1999
*FIELD* ED
carol: 06/22/2012
psherman: 1/12/1999