CALU_HUMAN
ID CALU_HUMAN Reviewed; 315 AA.
AC O43852; B3KPG9; D6QS48; D6QS49; D6QS50; D6QS51; D6QS52; D6QS53; D6QS54;
AC D6QS55; D6QS56; D6QS57; D6QS58; D6QS59; F5H1Q9; F5H879; O60456; Q6FHB9;
AC Q96RL3; Q9NR43;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 206.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 to
RT 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; 13;
RP 14 AND 15), AND VARIANT GLN-4.
RA Wang Q., Chen L., Shen B.R., Feng H., Zheng P.L., Teng J.L., Chen J.G.;
RT "Calumenin isoforms and their intracellular and extracellular 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., 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., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT 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 the
RT medium.";
RL Exp. Cell Res. 248:473-481(1999).
RN [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA 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].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT 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
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-131.
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 multiple
RT 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., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND THR-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; TYR-47; THR-254; SER-261
RP AND SER-277, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP PHOSPHORYLATION AT SER-69.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in regulation of vitamin K-dependent carboxylation
CC of multiple N-terminal glutamate residues. Seems to inhibit gamma-
CC carboxylase GGCX. Binds 7 calcium ions with a low affinity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GGCX. {ECO:0000250}.
CC -!- INTERACTION:
CC O43852; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-1171069, EBI-10173939;
CC O43852-1; P13569: CFTR; NbExp=2; IntAct=EBI-5280679, EBI-349854;
CC O43852-3; P05067: APP; NbExp=3; IntAct=EBI-11536607, EBI-77613;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10222138}. Golgi apparatus
CC {ECO:0000269|PubMed:10222138}. Secreted {ECO:0000305}. Melanosome
CC {ECO:0000269|PubMed:12643545}. Sarcoplasmic reticulum lumen
CC {ECO:0000305}. Note=Identified by mass spectrometry in melanosome
CC fractions from stage I to stage IV. {ECO:0000269|PubMed:12643545}.
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 levels in
CC heart, placenta and skeletal muscle, at lower levels in lung, kidney
CC and pancreas and at very low levels in brain and liver.
CC -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}.
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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 CCDS; CCDS47703.1; -. [O43852-2]
DR CCDS; CCDS56506.1; -. [O43852-3]
DR CCDS; CCDS56507.1; -. [O43852-4]
DR CCDS; CCDS56508.1; -. [O43852-10]
DR CCDS; CCDS5805.1; -. [O43852-1]
DR RefSeq; NP_001124146.1; NM_001130674.2. [O43852-2]
DR RefSeq; NP_001186600.1; NM_001199671.1. [O43852-3]
DR RefSeq; NP_001186601.1; NM_001199672.1. [O43852-4]
DR RefSeq; NP_001186602.1; NM_001199673.1. [O43852-10]
DR RefSeq; NP_001210.1; NM_001219.4. [O43852-1]
DR RefSeq; XP_016868148.1; XM_017012659.1. [O43852-15]
DR AlphaFoldDB; O43852; -.
DR SASBDB; O43852; -.
DR BioGRID; 107263; 307.
DR IntAct; O43852; 97.
DR MINT; O43852; -.
DR STRING; 9606.ENSP00000438248; -.
DR GlyConnect; 1062; 43 N-Linked glycans (1 site).
DR GlyGen; O43852; 3 sites, 45 N-linked glycans (1 site), 2 O-linked glycans (2 sites).
DR iPTMnet; O43852; -.
DR MetOSite; O43852; -.
DR PhosphoSitePlus; O43852; -.
DR SwissPalm; O43852; -.
DR BioMuta; CALU; -.
DR DOSAC-COBS-2DPAGE; O43852; -.
DR EPD; O43852; -.
DR jPOST; O43852; -.
DR MassIVE; O43852; -.
DR MaxQB; O43852; -.
DR PaxDb; O43852; -.
DR PeptideAtlas; O43852; -.
DR PRIDE; O43852; -.
DR ProteomicsDB; 25733; -.
DR ProteomicsDB; 27707; -.
DR ProteomicsDB; 49203; -. [O43852-1]
DR ProteomicsDB; 49204; -. [O43852-2]
DR ProteomicsDB; 49205; -. [O43852-3]
DR ProteomicsDB; 49206; -. [O43852-4]
DR TopDownProteomics; O43852-1; -. [O43852-1]
DR TopDownProteomics; O43852-2; -. [O43852-2]
DR TopDownProteomics; O43852-3; -. [O43852-3]
DR TopDownProteomics; O43852-4; -. [O43852-4]
DR TopDownProteomics; O43852-5; -. [O43852-5]
DR TopDownProteomics; O43852-6; -. [O43852-6]
DR TopDownProteomics; O43852-8; -. [O43852-8]
DR TopDownProteomics; O43852-9; -. [O43852-9]
DR Antibodypedia; 1219; 276 antibodies from 33 providers.
DR DNASU; 813; -.
DR Ensembl; ENST00000249364.9; ENSP00000249364.4; ENSG00000128595.17. [O43852-1]
DR Ensembl; ENST00000449187.6; ENSP00000408838.2; ENSG00000128595.17. [O43852-2]
DR Ensembl; ENST00000479257.5; ENSP00000420381.1; ENSG00000128595.17. [O43852-3]
DR Ensembl; ENST00000535011.6; ENSP00000442110.1; ENSG00000128595.17. [O43852-10]
DR Ensembl; ENST00000542996.6; ENSP00000438248.1; ENSG00000128595.17. [O43852-4]
DR GeneID; 813; -.
DR KEGG; hsa:813; -.
DR MANE-Select; ENST00000249364.9; ENSP00000249364.4; NM_001219.5; NP_001210.1.
DR UCSC; uc003vnr.4; human. [O43852-1]
DR CTD; 813; -.
DR DisGeNET; 813; -.
DR GeneCards; CALU; -.
DR HGNC; HGNC:1458; CALU.
DR HPA; ENSG00000128595; Low tissue specificity.
DR MIM; 603420; gene.
DR neXtProt; NX_O43852; -.
DR OpenTargets; ENSG00000128595; -.
DR PharmGKB; PA26047; -.
DR VEuPathDB; HostDB:ENSG00000128595; -.
DR eggNOG; KOG4223; Eukaryota.
DR GeneTree; ENSGT01010000222360; -.
DR HOGENOM; CLU_044718_0_1_1; -.
DR InParanoid; O43852; -.
DR OrthoDB; 909079at2759; -.
DR PhylomeDB; O43852; -.
DR TreeFam; TF314849; -.
DR PathwayCommons; O43852; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; O43852; -.
DR SIGNOR; O43852; -.
DR BioGRID-ORCS; 813; 12 hits in 1079 CRISPR screens.
DR ChiTaRS; CALU; human.
DR GeneWiki; CALU_(gene); -.
DR GenomeRNAi; 813; -.
DR Pharos; O43852; Tbio.
DR PRO; PR:O43852; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O43852; protein.
DR Bgee; ENSG00000128595; Expressed in stromal cell of endometrium and 216 other tissues.
DR ExpressionAtlas; O43852; baseline and differential.
DR Genevisible; O43852; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
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:SF76; PTHR10827:SF76; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 6.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Sarcoplasmic reticulum; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 20..315
FT /note="Calumenin"
FT /id="PRO_0000004153"
FT DOMAIN 68..103
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 104..139
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 151..186
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 188..223
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 229..264
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 265..300
FT /note="EF-hand 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 312..315
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000305"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000305"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000305"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000305"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000305"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 47
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 69
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35887"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform 15)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045939"
FT VAR_SEQ 1
FT /note="M -> MKETDLIIM (in isoform 3, isoform 4 and isoform
FT 14)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_043570"
FT VAR_SEQ 75..315
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045940"
FT VAR_SEQ 75..137
FT /note="KIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGHDLNEDGLVSW
FT EEYKNATYGYV -> MIVDKIDADKDGFVTEGELKSWIKHAQKKYIYDNVENQWQEFDM
FT NQDGLISWDEYRNVTYGTY (in isoform 2, isoform 4, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|Ref.10, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.4"
FT /id="VSP_007317"
FT VAR_SEQ 94..254
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045941"
FT VAR_SEQ 139
FT /note="D -> E (in isoform 13 and isoform 14)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045942"
FT VAR_SEQ 140..315
FT /note="Missing (in isoform 13 and isoform 14)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045943"
FT VAR_SEQ 154..161
FT /note="VRDERRFK -> GILMSRNG (in isoform 7)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045944"
FT VAR_SEQ 162..315
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045945"
FT VAR_SEQ 164..249
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045946"
FT VAR_SEQ 165..170
FT /note="KDGDLI -> RARAVC (in isoform 11)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045947"
FT VAR_SEQ 171..315
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045948"
FT VAR_SEQ 172..285
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045949"
FT VAR_SEQ 216..315
FT /note="DMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAE
FT AEARHLVYESDQNKDGKLTKEEIVDKYDLFVGSQATDFGEALVRHDEF -> WQAYQGG
FT DR (in isoform 10)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045950"
FT VAR_SEQ 226..275
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045951"
FT VARIANT 4
FT /note="R -> Q (in dbSNP:rs2290228)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_022051"
FT CONFLICT 48
FT /note="D -> G (in Ref. 4; ADG45013)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="K -> R (in Ref. 4; ADG45007)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="V -> A (in Ref. 4; ADG45010)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="D -> G (in Ref. 4; ADG45007)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="L -> H (in Ref. 4; ADG45011)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="F -> S (in Ref. 4; ADG45012)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="M -> V (in Ref. 4; ADG45015)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="F -> L (in Ref. 1; AAB97725)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="T -> S (in Ref. 4; ADG45015)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="E -> V (in Ref. 6; CAG46634)"
FT /evidence="ECO:0000305"
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
