ID CALU_HUMAN Reviewed; 315 AA. AC O43852; B3KPG9; D6QS48; D6QS49; D6QS50; D6QS51; D6QS52; D6QS53; AC 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 13-FEB-2019, entry version 186. 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]. 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]. 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 IDENTIFICATION RP BY 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 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 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 RT the 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 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 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., 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). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; TYR-47; THR-254; RP SER-261 AND SER-277, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE 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 RP BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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 RT 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., RA Ayoub D., 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 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). {ECO:0000250}. CC -!- SUBUNIT: Interacts with GGCX. {ECO:0000250}. CC -!- INTERACTION: CC Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-1171069, EBI-10173939; 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 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. {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. [O43852-15] DR UniGene; Hs.743262; -. DR UniGene; Hs.7753; -. DR ProteinModelPortal; O43852; -. DR SMR; O43852; -. DR BioGrid; 107263; 145. DR IntAct; O43852; 64. DR MINT; O43852; -. DR STRING; 9606.ENSP00000420381; -. DR GlyConnect; 1062; -. DR iPTMnet; O43852; -. DR PhosphoSitePlus; O43852; -. DR SwissPalm; O43852; -. DR BioMuta; CALU; -. DR DOSAC-COBS-2DPAGE; O43852; -. DR EPD; O43852; -. DR jPOST; O43852; -. DR PaxDb; O43852; -. DR PeptideAtlas; O43852; -. DR PRIDE; O43852; -. DR ProteomicsDB; 49203; -. 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 DNASU; 813; -. DR Ensembl; ENST00000249364; ENSP00000249364; ENSG00000128595. [O43852-1] DR Ensembl; ENST00000449187; ENSP00000408838; ENSG00000128595. [O43852-2] DR Ensembl; ENST00000479257; ENSP00000420381; ENSG00000128595. [O43852-3] DR Ensembl; ENST00000535011; ENSP00000442110; ENSG00000128595. [O43852-10] DR Ensembl; ENST00000542996; ENSP00000438248; ENSG00000128595. [O43852-4] DR GeneID; 813; -. DR KEGG; hsa:813; -. DR UCSC; uc003vnr.4; human. [O43852-1] DR CTD; 813; -. DR DisGeNET; 813; -. DR EuPathDB; HostDB:ENSG00000128595.16; -. DR GeneCards; CALU; -. DR HGNC; HGNC:1458; CALU. DR HPA; HPA006018; -. DR MIM; 603420; gene. DR neXtProt; NX_O43852; -. DR OpenTargets; ENSG00000128595; -. DR PharmGKB; PA26047; -. DR eggNOG; KOG4223; Eukaryota. DR eggNOG; ENOG410XRVE; LUCA. DR GeneTree; ENSGT00940000155072; -. DR HOGENOM; HOG000230934; -. DR HOVERGEN; HBG002834; -. DR InParanoid; O43852; -. DR OMA; EVKTWII; -. DR OrthoDB; 909079at2759; -. DR PhylomeDB; O43852; -. DR TreeFam; TF314849; -. 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 ChiTaRS; CALU; human. DR GeneWiki; CALU_(gene); -. DR GenomeRNAi; 813; -. DR PRO; PR:O43852; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000128595; Expressed in 237 organ(s), highest expression level in smooth muscle tissue. 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; IEA:UniProtKB-SubCell. 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: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 GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. 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:SF70; PTHR10827:SF70; 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; Complete proteome; KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; KW Golgi apparatus; Membrane; Metal-binding; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; Sarcoplasmic reticulum; KW Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:12665801}. FT CHAIN 20 315 Calumenin. FT /FTId=PRO_0000004153. FT DOMAIN 68 103 EF-hand 1. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 104 139 EF-hand 2. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 151 186 EF-hand 3. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 188 223 EF-hand 4. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 229 264 EF-hand 5. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 265 300 EF-hand 6. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 81 92 1. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 117 128 2. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 164 175 3; possibly ancestral. FT {ECO:0000255|PROSITE-ProRule:PRU00448}. FT CA_BIND 201 212 4. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 242 253 5. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 278 289 6. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT MOTIF 312 315 Prevents secretion from ER. FT {ECO:0000250}. FT MOD_RES 44 44 Phosphoserine. FT {ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 47 47 Phosphotyrosine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 65 65 Phosphothreonine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 69 69 Phosphoserine; by FAM20C. FT {ECO:0000269|PubMed:26091039}. FT MOD_RES 165 165 N6-acetyllysine. FT {ECO:0000250|UniProtKB:O35887}. FT MOD_RES 254 254 Phosphothreonine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 261 261 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 277 277 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT CARBOHYD 131 131 N-linked (GlcNAc...) (complex) FT asparagine. {ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218}. FT VAR_SEQ 1 151 Missing (in isoform 15). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045939. FT VAR_SEQ 1 1 M -> MKETDLIIM (in isoform 3, isoform 4 FT and isoform 14). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|Ref.4}. FT /FTId=VSP_043570. FT VAR_SEQ 75 315 Missing (in isoform 12). FT {ECO:0000303|Ref.4}. 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). {ECO:0000303|Ref.10, FT ECO:0000303|Ref.3, ECO:0000303|Ref.4}. FT /FTId=VSP_007317. FT VAR_SEQ 94 254 Missing (in isoform 9). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045941. FT VAR_SEQ 139 139 D -> E (in isoform 13 and isoform 14). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045942. FT VAR_SEQ 140 315 Missing (in isoform 13 and isoform 14). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045943. FT VAR_SEQ 154 161 VRDERRFK -> GILMSRNG (in isoform 7). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045944. FT VAR_SEQ 162 315 Missing (in isoform 7). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045945. FT VAR_SEQ 164 249 Missing (in isoform 5). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045946. FT VAR_SEQ 165 170 KDGDLI -> RARAVC (in isoform 11). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045947. FT VAR_SEQ 171 315 Missing (in isoform 11). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045948. FT VAR_SEQ 172 285 Missing (in isoform 8). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045949. FT VAR_SEQ 216 315 DMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKD FT WILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLF FT VGSQATDFGEALVRHDEF -> WQAYQGGDR (in FT isoform 10). {ECO:0000303|Ref.4}. FT /FTId=VSP_045950. FT VAR_SEQ 226 275 Missing (in isoform 6). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045951. FT VARIANT 4 4 R -> Q (in dbSNP:rs2290228). FT {ECO:0000269|Ref.4}. FT /FTId=VAR_022051. FT CONFLICT 48 48 D -> G (in Ref. 4; ADG45013). FT {ECO:0000305}. FT CONFLICT 84 84 K -> R (in Ref. 4; ADG45007). FT {ECO:0000305}. FT CONFLICT 90 90 V -> A (in Ref. 4; ADG45010). FT {ECO:0000305}. FT CONFLICT 117 117 D -> G (in Ref. 4; ADG45007). FT {ECO:0000305}. FT CONFLICT 118 118 L -> H (in Ref. 4; ADG45011). FT {ECO:0000305}. FT CONFLICT 147 147 F -> S (in Ref. 4; ADG45012). FT {ECO:0000305}. FT CONFLICT 188 188 M -> V (in Ref. 4; ADG45015). FT {ECO:0000305}. FT CONFLICT 207 207 F -> L (in Ref. 1; AAB97725). FT {ECO:0000305}. FT CONFLICT 232 232 T -> S (in Ref. 4; ADG45015). FT {ECO:0000305}. FT CONFLICT 267 267 E -> V (in Ref. 6; CAG46634). FT {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 //