RCN1_HUMAN
ID RCN1_HUMAN Reviewed; 331 AA.
AC Q15293; B7Z1M1; D3DR00;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Reticulocalbin-1;
DE Flags: Precursor;
GN Name=RCN1; Synonyms=RCN;
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).
RX PubMed=8586628; DOI=10.1093/oxfordjournals.jbchem.a124815;
RA Ozawa M.;
RT "Cloning of a human homologue of mouse reticulocalbin reveals conservation
RT of structural domains in the novel endoplasmic reticulum resident Ca(2+)-
RT binding protein with multiple EF-hand motifs.";
RL J. Biochem. 117:1113-1119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-76 AND SER-80, AND
RP IDENTIFICATION 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., 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 [10]
RP PHOSPHORYLATION AT SER-80.
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 [11]
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).
RN [12]
RP GLYCOSYLATION.
RX PubMed=28512129; DOI=10.1074/jbc.m117.794487;
RA Larsen I.S.B., Narimatsu Y., Joshi H.J., Yang Z., Harrison O.J., Brasch J.,
RA Shapiro L., Honig B., Vakhrushev S.Y., Clausen H., Halim A.;
RT "Mammalian O-mannosylation of cadherins and plexins is independent of
RT protein O-mannosyltransferases 1 and 2.";
RL J. Biol. Chem. 292:11586-11598(2017).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-117.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May regulate calcium-dependent activities in the endoplasmic
CC reticulum lumen or post-ER compartment.
CC -!- INTERACTION:
CC Q15293; Q12797-6: ASPH; NbExp=3; IntAct=EBI-948278, EBI-12092171;
CC Q15293; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-948278, EBI-1166928;
CC Q15293; P54253: ATXN1; NbExp=9; IntAct=EBI-948278, EBI-930964;
CC Q15293; P46379-2: BAG6; NbExp=3; IntAct=EBI-948278, EBI-10988864;
CC Q15293; O15182: CETN3; NbExp=5; IntAct=EBI-948278, EBI-712959;
CC Q15293; Q8TEB1: DCAF11; NbExp=5; IntAct=EBI-948278, EBI-2213388;
CC Q15293; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-948278, EBI-12593112;
CC Q15293; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-948278, EBI-743105;
CC Q15293; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-948278, EBI-744099;
CC Q15293; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-948278, EBI-1752811;
CC Q15293; O95257: GADD45G; NbExp=3; IntAct=EBI-948278, EBI-448202;
CC Q15293; O43681: GET3; NbExp=5; IntAct=EBI-948278, EBI-2515857;
CC Q15293; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-948278, EBI-740290;
CC Q15293; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-948278, EBI-14103818;
CC Q15293; P42858: HTT; NbExp=3; IntAct=EBI-948278, EBI-466029;
CC Q15293; O14901: KLF11; NbExp=3; IntAct=EBI-948278, EBI-948266;
CC Q15293; P25800: LMO1; NbExp=3; IntAct=EBI-948278, EBI-8639312;
CC Q15293; P25791-3: LMO2; NbExp=3; IntAct=EBI-948278, EBI-11959475;
CC Q15293; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-948278, EBI-11742507;
CC Q15293; P61968: LMO4; NbExp=3; IntAct=EBI-948278, EBI-2798728;
CC Q15293; O43765: SGTA; NbExp=3; IntAct=EBI-948278, EBI-347996;
CC Q15293; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-948278, EBI-744081;
CC Q15293; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-948278, EBI-5235340;
CC Q15293; P51687: SUOX; NbExp=3; IntAct=EBI-948278, EBI-3921347;
CC Q15293; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-948278, EBI-11741890;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15293-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15293-2; Sequence=VSP_055511;
CC -!- PTM: O-glycosylated. O-mannosylated by POMT1 and POMT2 and elongated by
CC POMGNT1. {ECO:0000269|PubMed:28512129}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites;
CC potential sites II and VI have lost affinity for calcium.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}.
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DR EMBL; D42073; BAA07670.1; -; mRNA.
DR EMBL; AK293652; BAH11557.1; -; mRNA.
DR EMBL; AL035078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL078612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z95332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68227.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68228.1; -; Genomic_DNA.
DR EMBL; BC010120; AAH10120.1; -; mRNA.
DR CCDS; CCDS7876.1; -. [Q15293-1]
DR PIR; JC4173; JC4173.
DR RefSeq; NP_002892.1; NM_002901.2. [Q15293-1]
DR AlphaFoldDB; Q15293; -.
DR BioGRID; 111887; 233.
DR ELM; Q15293; -.
DR IntAct; Q15293; 117.
DR MINT; Q15293; -.
DR STRING; 9606.ENSP00000054950; -.
DR GlyConnect; 1712; 21 N-Linked glycans (1 site).
DR GlyGen; Q15293; 2 sites, 28 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q15293; -.
DR MetOSite; Q15293; -.
DR PhosphoSitePlus; Q15293; -.
DR BioMuta; RCN1; -.
DR DMDM; 2493462; -.
DR CPTAC; CPTAC-266; -.
DR CPTAC; CPTAC-267; -.
DR EPD; Q15293; -.
DR jPOST; Q15293; -.
DR MassIVE; Q15293; -.
DR MaxQB; Q15293; -.
DR PaxDb; Q15293; -.
DR PeptideAtlas; Q15293; -.
DR PRIDE; Q15293; -.
DR ProteomicsDB; 60519; -. [Q15293-1]
DR ProteomicsDB; 6347; -.
DR TopDownProteomics; Q15293-1; -. [Q15293-1]
DR Antibodypedia; 25609; 138 antibodies from 23 providers.
DR DNASU; 5954; -.
DR Ensembl; ENST00000054950.4; ENSP00000054950.4; ENSG00000049449.10. [Q15293-1]
DR GeneID; 5954; -.
DR KEGG; hsa:5954; -.
DR MANE-Select; ENST00000054950.4; ENSP00000054950.4; NM_002901.4; NP_002892.1.
DR UCSC; uc058acp.1; human. [Q15293-1]
DR CTD; 5954; -.
DR DisGeNET; 5954; -.
DR GeneCards; RCN1; -.
DR HGNC; HGNC:9934; RCN1.
DR HPA; ENSG00000049449; Tissue enriched (epididymis).
DR MIM; 602735; gene.
DR neXtProt; NX_Q15293; -.
DR OpenTargets; ENSG00000049449; -.
DR PharmGKB; PA34303; -.
DR VEuPathDB; HostDB:ENSG00000049449; -.
DR eggNOG; KOG4223; Eukaryota.
DR GeneTree; ENSGT01010000222360; -.
DR HOGENOM; CLU_044718_0_1_1; -.
DR InParanoid; Q15293; -.
DR OMA; EIRQWIM; -.
DR PhylomeDB; Q15293; -.
DR TreeFam; TF314849; -.
DR PathwayCommons; Q15293; -.
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; Q15293; -.
DR BioGRID-ORCS; 5954; 34 hits in 1068 CRISPR screens.
DR ChiTaRS; RCN1; human.
DR GeneWiki; RCN1; -.
DR GenomeRNAi; 5954; -.
DR Pharos; Q15293; Tbio.
DR PRO; PR:Q15293; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q15293; protein.
DR Bgee; ENSG00000049449; Expressed in corpus epididymis and 202 other tissues.
DR ExpressionAtlas; Q15293; baseline and differential.
DR Genevisible; Q15293; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 6.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Endoplasmic reticulum; Glycoprotein;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..331
FT /note="Reticulocalbin-1"
FT /id="PRO_0000004145"
FT DOMAIN 79..114
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 115..150
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 166..201
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 203..238
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 244..279
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 280..315
FT /note="EF-hand 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 328..331
FT /note="Prevents secretion from ER"
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 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000305"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000305"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000305"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000305"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000305"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 80
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1..85
FT /note="MARGGRGRRLGLALGLLLALVLAPRVLRAKPTVRKERVVRPDSELGERPPED
FT NQSFQYDHEAFLGKEDSKTFDQLTPDESKERLG -> MTGGEGPLPTAKQATCSPPSSR
FT ERNPRRRGSRPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055511"
FT VARIANT 73
FT /note="D -> Y (in dbSNP:rs1804281)"
FT /id="VAR_011965"
FT VARIANT 117
FT /note="F -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035460"
SQ SEQUENCE 331 AA; 38890 MW; 608AAD536963F789 CRC64;
MARGGRGRRL GLALGLLLAL VLAPRVLRAK PTVRKERVVR PDSELGERPP EDNQSFQYDH
EAFLGKEDSK TFDQLTPDES KERLGKIVDR IDNDGDGFVT TEELKTWIKR VQKRYIFDNV
AKVWKDYDRD KDDKISWEEY KQATYGYYLG NPAEFHDSSD HHTFKKMLPR DERRFKAADL
NGDLTATREE FTAFLHPEEF EHMKEIVVLE TLEDIDKNGD GFVDQDEYIA DMFSHEENGP
EPDWVLSERE QFNEFRDLNK DGKLDKDEIR HWILPQDYDH AQAEARHLVY ESDKNKDEKL
TKEEILENWN MFVGSQATNY GEDLTKNHDE L
