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 27-MAR-2024, entry version 215. 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; PRO_0000449619 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-1171069, EBI-25475847; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR AlphaFoldDB; O43852; -. DR SASBDB; O43852; -. DR SMR; O43852; -. DR BioGRID; 107263; 344. DR IntAct; O43852; 105. DR MINT; O43852; -. DR STRING; 9606.ENSP00000438248; -. DR GlyConnect; 1062; 43 N-Linked glycans (1 site). DR GlyCosmos; O43852; 2 sites, 43 glycans. DR GlyGen; O43852; 9 sites, 45 N-linked glycans (1 site), 3 O-linked glycans (8 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; 9606-ENSP00000438248; -. DR PeptideAtlas; 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 Pumba; O43852; -. 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; 311 antibodies from 33 providers. DR DNASU; 813; -. DR Ensembl; ENST00000249364.9; ENSP00000249364.4; ENSG00000128595.17. [O43852-1] DR Ensembl; ENST00000449187.7; 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; ENST00000542996.7; 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 AGR; HGNC:1458; -. 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; 4490703at2759; -. 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; 13 hits in 1159 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 218 other cell types or tissues. DR ExpressionAtlas; O43852; baseline and differential. 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 CDD; cd16228; EFh_CREC_Calumenin; 1. DR Gene3D; 1.10.238.10; EF-hand; 2. 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; CALUMENIN; 1. DR PANTHER; PTHR10827; RETICULOCALBIN; 1. DR Pfam; PF13202; EF-hand_5; 3. DR SMART; SM00054; EFh; 4. DR SUPFAM; SSF47473; EF-hand; 2. DR PROSITE; PS00018; EF_HAND_1; 4. DR PROSITE; PS50222; EF_HAND_2; 6. DR Genevisible; O43852; HS. 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 //